data_1OC6 # _entry.id 1OC6 # _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 1OC6 PDBE EBI-9307 WWPDB D_1290009307 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 1BVW unspecified 'CELLOBIOHYDROLASE II (CEL6A) FROM HUMICOLA INSOLENS' PDB 1GZ1 unspecified ;MUTANT D416A OF THE CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS IN COMPLEX WITH METHYL-CELLOBIOSYL-4-DEOXY-4-THIO-BETA-D- CELLOBIOSIDE ; PDB 1HGW unspecified 'CEL6A D175A MUTANT' PDB 1HGY unspecified 'CEL6A D221A MUTANT' PDB 1OC5 unspecified '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 1OC6 _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2003-02-06 _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Varrot, A.' 1 'Frandsen, T.P.' 2 'Von Ossowski, I.' 3 'Boyer, V.' 4 'Driguez, H.' 5 'Schulein, M.' 6 'Davies, G.J.' 7 # _citation.id primary _citation.title 'Structural Basis for Ligand Binding and Processivity in Cellobiohydrolase Cel6A from Humicola Insolens' _citation.journal_abbrev Structure _citation.journal_volume 11 _citation.page_first 855 _citation.page_last ? _citation.year 2003 _citation.journal_id_ASTM STRUE6 _citation.country UK _citation.journal_id_ISSN 0969-2126 _citation.journal_id_CSD 2005 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 12842048 _citation.pdbx_database_id_DOI '10.1016/S0969-2126(03)00124-2' # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Varrot, A.' 1 primary 'Frandsen, T.P.' 2 primary 'Von Ossowski, I.' 3 primary 'Boyer, V.' 4 primary 'Driguez, H.' 5 primary 'Schulein, M.' 6 primary 'Davies, G.J.' 7 # _cell.entry_id 1OC6 _cell.length_a 57.504 _cell.length_b 60.148 _cell.length_c 97.207 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 4 _cell.pdbx_unique_axis ? # _symmetry.entry_id 1OC6 _symmetry.space_group_name_H-M 'P 21 21 21' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 19 # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man 'CELLOBIOHYDROLASE II' 40181.723 1 3.2.1.91 YES 'CATALYTIC CORE DOMAIN RESIDUES 87-450' 'N-LINKED N-ACETYLGLUCOSAMINE ON RESIDUE ASN 141' 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 1 ? ? ? ? 3 non-polymer syn 'CALCIUM ION' 40.078 1 ? ? ? ? 4 non-polymer syn GLYCEROL 92.094 7 ? ? ? ? 5 water nat water 18.015 465 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'CELLULASE, CEL6A' # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer no _entity_poly.pdbx_seq_one_letter_code ;APYNGNPFEGVQLWANNYYRSEVHTLAIPQITDPALRAAASAVAEVPSFQWLDRNVTVDTLLVQTLSEIREANQAGANPQ YAAQIVVYDLPDRDCAAAASNGEWAIANNGVNNYKAYINRIREILISFSDVRTILVIEPDSLANMVTNMNVPKCSGAAST YRELTIYALKQLDLPHVAMYMDAGHAGWLGWPANIQPAAELFAKIYEDAGKPRAVRGLATNVANYNAWSVSSPPPYTSPN PNYDEKHYIEAFRPLLEARGFPAQFIVDQGRSGKQPTGQKEWGHWCNAIGTGFGMRPTANTGHQYVDAFVWVKPGGECNG TSDTTAARYDYHCGLEDALKPAPEAGQWFNEYFIQLLRNANPPF ; _entity_poly.pdbx_seq_one_letter_code_can ;APYNGNPFEGVQLWANNYYRSEVHTLAIPQITDPALRAAASAVAEVPSFQWLDRNVTVDTLLVQTLSEIREANQAGANPQ YAAQIVVYDLPDRDCAAAASNGEWAIANNGVNNYKAYINRIREILISFSDVRTILVIEPDSLANMVTNMNVPKCSGAAST YRELTIYALKQLDLPHVAMYMDAGHAGWLGWPANIQPAAELFAKIYEDAGKPRAVRGLATNVANYNAWSVSSPPPYTSPN PNYDEKHYIEAFRPLLEARGFPAQFIVDQGRSGKQPTGQKEWGHWCNAIGTGFGMRPTANTGHQYVDAFVWVKPGGECNG TSDTTAARYDYHCGLEDALKPAPEAGQWFNEYFIQLLRNANPPF ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ALA n 1 2 PRO n 1 3 TYR n 1 4 ASN n 1 5 GLY n 1 6 ASN n 1 7 PRO n 1 8 PHE n 1 9 GLU n 1 10 GLY n 1 11 VAL n 1 12 GLN n 1 13 LEU n 1 14 TRP n 1 15 ALA n 1 16 ASN n 1 17 ASN n 1 18 TYR n 1 19 TYR n 1 20 ARG n 1 21 SER n 1 22 GLU n 1 23 VAL n 1 24 HIS n 1 25 THR n 1 26 LEU n 1 27 ALA n 1 28 ILE n 1 29 PRO n 1 30 GLN n 1 31 ILE n 1 32 THR n 1 33 ASP n 1 34 PRO n 1 35 ALA n 1 36 LEU n 1 37 ARG n 1 38 ALA n 1 39 ALA n 1 40 ALA n 1 41 SER n 1 42 ALA n 1 43 VAL n 1 44 ALA n 1 45 GLU n 1 46 VAL n 1 47 PRO n 1 48 SER n 1 49 PHE n 1 50 GLN n 1 51 TRP n 1 52 LEU n 1 53 ASP n 1 54 ARG n 1 55 ASN n 1 56 VAL n 1 57 THR n 1 58 VAL n 1 59 ASP n 1 60 THR n 1 61 LEU n 1 62 LEU n 1 63 VAL n 1 64 GLN n 1 65 THR n 1 66 LEU n 1 67 SER n 1 68 GLU n 1 69 ILE n 1 70 ARG n 1 71 GLU n 1 72 ALA n 1 73 ASN n 1 74 GLN n 1 75 ALA n 1 76 GLY n 1 77 ALA n 1 78 ASN n 1 79 PRO n 1 80 GLN n 1 81 TYR n 1 82 ALA n 1 83 ALA n 1 84 GLN n 1 85 ILE n 1 86 VAL n 1 87 VAL n 1 88 TYR n 1 89 ASP n 1 90 LEU n 1 91 PRO n 1 92 ASP n 1 93 ARG n 1 94 ASP n 1 95 CYS n 1 96 ALA n 1 97 ALA n 1 98 ALA n 1 99 ALA n 1 100 SER n 1 101 ASN n 1 102 GLY n 1 103 GLU n 1 104 TRP n 1 105 ALA n 1 106 ILE n 1 107 ALA n 1 108 ASN n 1 109 ASN n 1 110 GLY n 1 111 VAL n 1 112 ASN n 1 113 ASN n 1 114 TYR n 1 115 LYS n 1 116 ALA n 1 117 TYR n 1 118 ILE n 1 119 ASN n 1 120 ARG n 1 121 ILE n 1 122 ARG n 1 123 GLU n 1 124 ILE n 1 125 LEU n 1 126 ILE n 1 127 SER n 1 128 PHE n 1 129 SER n 1 130 ASP n 1 131 VAL n 1 132 ARG n 1 133 THR n 1 134 ILE n 1 135 LEU n 1 136 VAL n 1 137 ILE n 1 138 GLU n 1 139 PRO n 1 140 ASP n 1 141 SER n 1 142 LEU n 1 143 ALA n 1 144 ASN n 1 145 MET n 1 146 VAL n 1 147 THR n 1 148 ASN n 1 149 MET n 1 150 ASN n 1 151 VAL n 1 152 PRO n 1 153 LYS n 1 154 CYS n 1 155 SER n 1 156 GLY n 1 157 ALA n 1 158 ALA n 1 159 SER n 1 160 THR n 1 161 TYR n 1 162 ARG n 1 163 GLU n 1 164 LEU n 1 165 THR n 1 166 ILE n 1 167 TYR n 1 168 ALA n 1 169 LEU n 1 170 LYS n 1 171 GLN n 1 172 LEU n 1 173 ASP n 1 174 LEU n 1 175 PRO n 1 176 HIS n 1 177 VAL n 1 178 ALA n 1 179 MET n 1 180 TYR n 1 181 MET n 1 182 ASP n 1 183 ALA n 1 184 GLY n 1 185 HIS n 1 186 ALA n 1 187 GLY n 1 188 TRP n 1 189 LEU n 1 190 GLY n 1 191 TRP n 1 192 PRO n 1 193 ALA n 1 194 ASN n 1 195 ILE n 1 196 GLN n 1 197 PRO n 1 198 ALA n 1 199 ALA n 1 200 GLU n 1 201 LEU n 1 202 PHE n 1 203 ALA n 1 204 LYS n 1 205 ILE n 1 206 TYR n 1 207 GLU n 1 208 ASP n 1 209 ALA n 1 210 GLY n 1 211 LYS n 1 212 PRO n 1 213 ARG n 1 214 ALA n 1 215 VAL n 1 216 ARG n 1 217 GLY n 1 218 LEU n 1 219 ALA n 1 220 THR n 1 221 ASN n 1 222 VAL n 1 223 ALA n 1 224 ASN n 1 225 TYR n 1 226 ASN n 1 227 ALA n 1 228 TRP n 1 229 SER n 1 230 VAL n 1 231 SER n 1 232 SER n 1 233 PRO n 1 234 PRO n 1 235 PRO n 1 236 TYR n 1 237 THR n 1 238 SER n 1 239 PRO n 1 240 ASN n 1 241 PRO n 1 242 ASN n 1 243 TYR n 1 244 ASP n 1 245 GLU n 1 246 LYS n 1 247 HIS n 1 248 TYR n 1 249 ILE n 1 250 GLU n 1 251 ALA n 1 252 PHE n 1 253 ARG n 1 254 PRO n 1 255 LEU n 1 256 LEU n 1 257 GLU n 1 258 ALA n 1 259 ARG n 1 260 GLY n 1 261 PHE n 1 262 PRO n 1 263 ALA n 1 264 GLN n 1 265 PHE n 1 266 ILE n 1 267 VAL n 1 268 ASP n 1 269 GLN n 1 270 GLY n 1 271 ARG n 1 272 SER n 1 273 GLY n 1 274 LYS n 1 275 GLN n 1 276 PRO n 1 277 THR n 1 278 GLY n 1 279 GLN n 1 280 LYS n 1 281 GLU n 1 282 TRP n 1 283 GLY n 1 284 HIS n 1 285 TRP n 1 286 CYS n 1 287 ASN n 1 288 ALA n 1 289 ILE n 1 290 GLY n 1 291 THR n 1 292 GLY n 1 293 PHE n 1 294 GLY n 1 295 MET n 1 296 ARG n 1 297 PRO n 1 298 THR n 1 299 ALA n 1 300 ASN n 1 301 THR n 1 302 GLY n 1 303 HIS n 1 304 GLN n 1 305 TYR n 1 306 VAL n 1 307 ASP n 1 308 ALA n 1 309 PHE n 1 310 VAL n 1 311 TRP n 1 312 VAL n 1 313 LYS n 1 314 PRO n 1 315 GLY n 1 316 GLY n 1 317 GLU n 1 318 CYS n 1 319 ASN n 1 320 GLY n 1 321 THR n 1 322 SER n 1 323 ASP n 1 324 THR n 1 325 THR n 1 326 ALA n 1 327 ALA n 1 328 ARG n 1 329 TYR n 1 330 ASP n 1 331 TYR n 1 332 HIS n 1 333 CYS n 1 334 GLY n 1 335 LEU n 1 336 GLU n 1 337 ASP n 1 338 ALA n 1 339 LEU n 1 340 LYS n 1 341 PRO n 1 342 ALA n 1 343 PRO n 1 344 GLU n 1 345 ALA n 1 346 GLY n 1 347 GLN n 1 348 TRP n 1 349 PHE n 1 350 ASN n 1 351 GLU n 1 352 TYR n 1 353 PHE n 1 354 ILE n 1 355 GLN n 1 356 LEU n 1 357 LEU n 1 358 ARG n 1 359 ASN n 1 360 ALA n 1 361 ASN n 1 362 PRO n 1 363 PRO n 1 364 PHE n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name ? _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene ? _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'HUMICOLA INSOLENS' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 34413 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name ? _entity_src_gen.pdbx_host_org_scientific_name 'ASPERGILLUS ORYZAE' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 5062 _entity_src_gen.host_org_genus ? _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type ? _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name 'UNDER CONTROL OF THE FUNGAL AMYLASE PROMOTER AND AMYLOGLUCOSIDASE TERMINATOR' _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name PDB _struct_ref.db_code 1OC6 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_align_begin ? _struct_ref.pdbx_db_accession 1OC6 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 1OC6 _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 1 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 364 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession 1OC6 _struct_ref_seq.db_align_beg 87 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 450 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 87 _struct_ref_seq.pdbx_auth_seq_align_end 450 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CA non-polymer . 'CALCIUM ION' ? 'Ca 2' 40.078 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 GOL non-polymer . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3' 92.094 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 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 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 1OC6 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 4.05 _exptl_crystal.density_percent_sol 38.8 _exptl_crystal.description ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 7.00 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details ;PROTEIN WAS CONCENTRATED TO 20 MG/ML IN WATER. CRYSTALLISATION IN 200MM CALCIUM ACETATE IN 100MM HEPES BUFFER AT PH 7.0. PRECIPITANT WAS 18% POLYETHYLENE GLYCOL 8000. ; # _diffrn.id 1 _diffrn.ambient_temp 100.0 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector 'IMAGE PLATE' _diffrn_detector.type MARRESEARCH _diffrn_detector.pdbx_collection_date 1999-10-15 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.8445 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'EMBL/DESY, HAMBURG BEAMLINE BW7B' _diffrn_source.pdbx_synchrotron_site 'EMBL/DESY, Hamburg' _diffrn_source.pdbx_synchrotron_beamline BW7B _diffrn_source.pdbx_wavelength 0.8445 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 1OC6 _reflns.observed_criterion_sigma_I 0.000 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 20.000 _reflns.d_resolution_high 1.500 _reflns.number_obs 54127 _reflns.number_all ? _reflns.percent_possible_obs 99.5 _reflns.pdbx_Rmerge_I_obs 0.07000 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 17.2000 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 3.700 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 1.50 _reflns_shell.d_res_low 1.55 _reflns_shell.percent_possible_all 95.0 _reflns_shell.Rmerge_I_obs 0.35800 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 3.400 _reflns_shell.pdbx_redundancy 3.50 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 1OC6 _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 51648 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 20.00 _refine.ls_d_res_high 1.50 _refine.ls_percent_reflns_obs 99.4 _refine.ls_R_factor_obs 0.115 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.113 _refine.ls_R_factor_R_free 0.149 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.000 _refine.ls_number_reflns_R_free 2710 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.978 _refine.correlation_coeff_Fo_to_Fc_free 0.965 _refine.B_iso_mean 8.34 _refine.aniso_B[1][1] -0.42000 _refine.aniso_B[2][2] 0.34000 _refine.aniso_B[3][3] 0.08000 _refine.aniso_B[1][2] 0.00000 _refine.aniso_B[1][3] 0.00000 _refine.aniso_B[2][3] 0.00000 _refine.solvent_model_details 'BABINET MODEL WITH MASK' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.40 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' _refine.pdbx_starting_model 'PDB ENTRY 1OC5' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.071 _refine.pdbx_overall_ESU_R_Free 0.059 _refine.overall_SU_ML 0.034 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 0.913 _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 2839 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 57 _refine_hist.number_atoms_solvent 465 _refine_hist.number_atoms_total 3361 _refine_hist.d_res_high 1.50 _refine_hist.d_res_low 20.00 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.015 0.021 ? 3066 'X-RAY DIFFRACTION' ? r_bond_other_d 0.002 0.020 ? 2668 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.704 1.940 ? 4187 'X-RAY DIFFRACTION' ? r_angle_other_deg 1.357 3.000 ? 6232 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.674 5.000 ? 365 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 40.135 24.452 ? 155 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 11.815 15.000 ? 452 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 19.858 15.000 ? 19 'X-RAY DIFFRACTION' ? r_chiral_restr 0.108 0.200 ? 446 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.009 0.020 ? 3415 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.003 0.020 ? 614 'X-RAY DIFFRACTION' ? r_nbd_refined 0.225 0.200 ? 573 'X-RAY DIFFRACTION' ? r_nbd_other 0.275 0.200 ? 3043 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other 0.082 0.200 ? 1591 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined 0.134 0.200 ? 278 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined 0.137 0.200 ? 5 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined 0.129 0.200 ? 8 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other 0.229 0.200 ? 47 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined 0.127 0.200 ? 40 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it 1.205 1.500 ? 1846 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it 1.759 2.000 ? 2991 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it 2.489 3.000 ? 1220 'X-RAY DIFFRACTION' ? r_scbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_it 3.609 4.500 ? 1196 '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 1.50 _refine_ls_shell.d_res_low 1.54 _refine_ls_shell.number_reflns_R_work 3475 _refine_ls_shell.R_factor_R_work 0.1440 _refine_ls_shell.percent_reflns_obs ? _refine_ls_shell.R_factor_R_free 0.1820 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 175 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 1OC6 _struct.title 'structure native of the D405N mutant of the CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS at 1.5 angstrom resolution' _struct.pdbx_descriptor 'CELLOBIOHYDROLASE II (E.C.3.2.1.91)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 1OC6 _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'HYDROLASE, CELLULOSE DEGRADATION, CELLOBIOHYDROLASE, CELLULASE, GLYCOSIDE HYDROLASE FAMILY 6, PROCESSIVE MECHANISM' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 4 ? E N N 4 ? F N N 4 ? G N N 4 ? H N N 4 ? I N N 4 ? J N N 4 ? K N N 5 ? # _struct_biol.id 1 # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 ASN A 16 ? LEU A 26 ? ASN A 102 LEU A 112 1 ? 11 HELX_P HELX_P2 2 ALA A 27 ? ILE A 31 ? ALA A 113 ILE A 117 5 ? 5 HELX_P HELX_P3 3 ASP A 33 ? ALA A 44 ? ASP A 119 ALA A 130 1 ? 12 HELX_P HELX_P4 4 ARG A 54 ? VAL A 58 ? ARG A 140 VAL A 144 5 ? 5 HELX_P HELX_P5 5 THR A 60 ? ALA A 75 ? THR A 146 ALA A 161 1 ? 16 HELX_P HELX_P6 6 ALA A 105 ? ASN A 108 ? ALA A 191 ASN A 194 5 ? 4 HELX_P HELX_P7 7 ASN A 109 ? PHE A 128 ? ASN A 195 PHE A 214 1 ? 20 HELX_P HELX_P8 8 LEU A 142 ? ASN A 148 ? LEU A 228 ASN A 234 1 ? 7 HELX_P HELX_P9 9 VAL A 151 ? LEU A 172 ? VAL A 237 LEU A 258 1 ? 22 HELX_P HELX_P10 10 TRP A 191 ? ALA A 209 ? TRP A 277 ALA A 295 1 ? 19 HELX_P HELX_P11 11 PRO A 234 ? SER A 238 ? PRO A 320 SER A 324 5 ? 5 HELX_P HELX_P12 12 ASP A 244 ? ARG A 259 ? ASP A 330 ARG A 345 1 ? 16 HELX_P HELX_P13 13 ASP A 330 ? LEU A 335 ? ASP A 416 LEU A 421 5 ? 6 HELX_P HELX_P14 14 PHE A 349 ? ASN A 359 ? PHE A 435 ASN A 445 1 ? 11 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 95 SG ? ? ? 1_555 A CYS 154 SG ? ? A CYS 181 A CYS 240 1_555 ? ? ? ? ? ? ? 2.191 ? disulf2 disulf ? ? A CYS 286 SG ? ? ? 1_555 A CYS 333 SG ? ? A CYS 372 A CYS 419 1_555 ? ? ? ? ? ? ? 2.086 ? covale1 covale ? ? A ASN 55 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 141 A NAG 500 1_555 ? ? ? ? ? ? ? 1.468 ? metalc1 metalc ? ? C CA . CA ? ? ? 1_555 K HOH . O ? ? A CA 501 A HOH 2332 1_555 ? ? ? ? ? ? ? 2.417 ? metalc2 metalc ? ? C CA . CA ? ? ? 1_555 K HOH . O ? ? A CA 501 A HOH 2173 1_555 ? ? ? ? ? ? ? 2.137 ? metalc3 metalc ? ? C CA . CA ? ? ? 1_555 K HOH . O ? ? A CA 501 A HOH 2335 1_555 ? ? ? ? ? ? ? 2.390 ? metalc4 metalc ? ? C CA . CA ? ? ? 1_555 A GLU 281 OE1 ? ? A CA 501 A GLU 367 1_555 ? ? ? ? ? ? ? 2.455 ? metalc5 metalc ? ? C CA . CA ? ? ? 1_555 K HOH . O ? ? A CA 501 A HOH 2154 3_645 ? ? ? ? ? ? ? 2.311 ? metalc6 metalc ? ? C CA . CA ? ? ? 1_555 K HOH . O ? ? A CA 501 A HOH 2293 1_555 ? ? ? ? ? ? ? 2.383 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 ASN 78 A . ? ASN 164 A PRO 79 A ? PRO 165 A 1 -0.09 2 SER 238 A . ? SER 324 A PRO 239 A ? PRO 325 A 1 -2.07 3 GLN 275 A . ? GLN 361 A PRO 276 A ? PRO 362 A 1 -8.32 4 LYS 340 A . ? LYS 426 A PRO 341 A ? PRO 427 A 1 -4.15 5 ASN 361 A . ? ASN 447 A PRO 362 A ? PRO 448 A 1 0.56 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA ? 3 ? AB ? 7 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense AA 1 2 ? parallel AA 2 3 ? parallel AB 1 2 ? parallel AB 2 3 ? parallel AB 3 4 ? parallel AB 4 5 ? parallel AB 5 6 ? parallel AB 6 7 ? parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id AA 1 GLN A 12 ? LEU A 13 ? GLN A 98 LEU A 99 AA 2 TYR A 81 ? VAL A 87 ? TYR A 167 VAL A 173 AA 3 GLN A 50 ? LEU A 52 ? GLN A 136 LEU A 138 AB 1 GLN A 12 ? LEU A 13 ? GLN A 98 LEU A 99 AB 2 TYR A 81 ? VAL A 87 ? TYR A 167 VAL A 173 AB 3 THR A 133 ? ILE A 137 ? THR A 219 ILE A 223 AB 4 VAL A 177 ? ASP A 182 ? VAL A 263 ASP A 268 AB 5 VAL A 215 ? THR A 220 ? VAL A 301 THR A 306 AB 6 GLN A 264 ? ASP A 268 ? GLN A 350 ASP A 354 AB 7 VAL A 306 ? VAL A 310 ? VAL A 392 VAL A 396 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id AA 1 2 O GLN A 12 ? O GLN A 98 N ALA A 82 ? N ALA A 168 AA 2 3 N VAL A 86 ? N VAL A 172 O GLN A 50 ? O GLN A 136 AB 1 2 O GLN A 12 ? O GLN A 98 N ALA A 82 ? N ALA A 168 AB 2 3 N ILE A 85 ? N ILE A 171 O ILE A 134 ? O ILE A 220 AB 3 4 N LEU A 135 ? N LEU A 221 O ALA A 178 ? O ALA A 264 AB 4 5 O MET A 179 ? O MET A 265 N ARG A 216 ? N ARG A 302 AB 5 6 N LEU A 218 ? N LEU A 304 O GLN A 264 ? O GLN A 350 AB 6 7 O PHE A 265 ? O PHE A 351 N ASP A 307 ? N ASP A 393 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 15 'BINDING SITE FOR RESIDUE NAG A 500' AC2 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE CA A 501' AC3 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE GOL A 510' AC4 Software ? ? ? ? 11 'BINDING SITE FOR RESIDUE GOL A 511' AC5 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE GOL A 512' AC6 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE GOL A 514' AC7 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE GOL A 515' AC8 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE GOL A 516' AC9 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE GOL A 517' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 15 ASN A 55 ? ASN A 141 . ? 1_555 ? 2 AC1 15 ASP A 59 ? ASP A 145 . ? 1_555 ? 3 AC1 15 ASN A 113 ? ASN A 199 . ? 1_555 ? 4 AC1 15 GLU A 281 ? GLU A 367 . ? 1_555 ? 5 AC1 15 HIS A 284 ? HIS A 370 . ? 1_555 ? 6 AC1 15 LEU A 335 ? LEU A 421 . ? 1_555 ? 7 AC1 15 HOH K . ? HOH A 2064 . ? 1_555 ? 8 AC1 15 HOH K . ? HOH A 2066 . ? 1_555 ? 9 AC1 15 HOH K . ? HOH A 2153 . ? 1_555 ? 10 AC1 15 HOH K . ? HOH A 2333 . ? 1_555 ? 11 AC1 15 HOH K . ? HOH A 2404 . ? 1_555 ? 12 AC1 15 HOH K . ? HOH A 2445 . ? 1_555 ? 13 AC1 15 HOH K . ? HOH A 2447 . ? 1_555 ? 14 AC1 15 HOH K . ? HOH A 2448 . ? 1_555 ? 15 AC1 15 HOH K . ? HOH A 2449 . ? 1_555 ? 16 AC2 6 GLU A 281 ? GLU A 367 . ? 1_555 ? 17 AC2 6 HOH K . ? HOH A 2154 . ? 1_555 ? 18 AC2 6 HOH K . ? HOH A 2173 . ? 1_555 ? 19 AC2 6 HOH K . ? HOH A 2293 . ? 1_555 ? 20 AC2 6 HOH K . ? HOH A 2332 . ? 1_555 ? 21 AC2 6 HOH K . ? HOH A 2335 . ? 1_555 ? 22 AC3 9 ALA A 227 ? ALA A 313 . ? 1_555 ? 23 AC3 9 TRP A 228 ? TRP A 314 . ? 1_555 ? 24 AC3 9 SER A 229 ? SER A 315 . ? 1_555 ? 25 AC3 9 GLN A 269 ? GLN A 355 . ? 1_555 ? 26 AC3 9 SER A 272 ? SER A 358 . ? 1_555 ? 27 AC3 9 GLY A 273 ? GLY A 359 . ? 1_555 ? 28 AC3 9 ASN A 361 ? ASN A 447 . ? 1_555 ? 29 AC3 9 HOH K . ? HOH A 2450 . ? 1_555 ? 30 AC3 9 HOH K . ? HOH A 2451 . ? 1_555 ? 31 AC4 11 TYR A 18 ? TYR A 104 . ? 1_555 ? 32 AC4 11 GLN A 50 ? GLN A 136 . ? 1_555 ? 33 AC4 11 TRP A 51 ? TRP A 137 . ? 1_555 ? 34 AC4 11 ASP A 53 ? ASP A 139 . ? 1_555 ? 35 AC4 11 ARG A 54 ? ARG A 140 . ? 1_555 ? 36 AC4 11 LEU A 61 ? LEU A 147 . ? 1_555 ? 37 AC4 11 GLU A 317 ? GLU A 403 . ? 1_555 ? 38 AC4 11 HOH K . ? HOH A 2374 . ? 1_555 ? 39 AC4 11 HOH K . ? HOH A 2422 . ? 1_555 ? 40 AC4 11 HOH K . ? HOH A 2452 . ? 1_555 ? 41 AC4 11 HOH K . ? HOH A 2453 . ? 1_555 ? 42 AC5 6 ASN A 148 ? ASN A 234 . ? 1_555 ? 43 AC5 6 TRP A 188 ? TRP A 274 . ? 1_555 ? 44 AC5 6 HOH K . ? HOH A 2454 . ? 1_555 ? 45 AC5 6 HOH K . ? HOH A 2455 . ? 1_555 ? 46 AC5 6 HOH K . ? HOH A 2456 . ? 1_555 ? 47 AC5 6 HOH K . ? HOH A 2457 . ? 1_555 ? 48 AC6 5 TYR A 206 ? TYR A 292 . ? 1_555 ? 49 AC6 5 ARG A 216 ? ARG A 302 . ? 1_555 ? 50 AC6 5 PHE A 261 ? PHE A 347 . ? 1_555 ? 51 AC6 5 PRO A 262 ? PRO A 348 . ? 1_555 ? 52 AC6 5 GLN A 264 ? GLN A 350 . ? 1_555 ? 53 AC7 8 ARG A 54 ? ARG A 140 . ? 1_555 ? 54 AC7 8 THR A 60 ? THR A 146 . ? 1_555 ? 55 AC7 8 ALA A 96 ? ALA A 182 . ? 1_555 ? 56 AC7 8 VAL A 151 ? VAL A 237 . ? 1_555 ? 57 AC7 8 HOH K . ? HOH A 2061 . ? 1_555 ? 58 AC7 8 HOH K . ? HOH A 2403 . ? 1_555 ? 59 AC7 8 HOH K . ? HOH A 2459 . ? 1_555 ? 60 AC7 8 HOH K . ? HOH A 2460 . ? 1_555 ? 61 AC8 5 ASN A 224 ? ASN A 310 . ? 1_555 ? 62 AC8 5 HOH K . ? HOH A 2461 . ? 1_555 ? 63 AC8 5 HOH K . ? HOH A 2463 . ? 1_555 ? 64 AC8 5 HOH K . ? HOH A 2464 . ? 1_555 ? 65 AC8 5 HOH K . ? HOH A 2465 . ? 1_555 ? 66 AC9 6 PHE A 8 ? PHE A 94 . ? 1_555 ? 67 AC9 6 GLU A 9 ? GLU A 95 . ? 1_555 ? 68 AC9 6 GLY A 10 ? GLY A 96 . ? 1_555 ? 69 AC9 6 VAL A 11 ? VAL A 97 . ? 1_555 ? 70 AC9 6 HOH K . ? HOH A 2354 . ? 1_555 ? 71 AC9 6 HOH K . ? HOH A 2356 . ? 1_555 ? # _database_PDB_matrix.entry_id 1OC6 _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 1OC6 _atom_sites.fract_transf_matrix[1][1] 0.017390 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.016626 _atom_sites.fract_transf_matrix[2][3] 0.000000 _atom_sites.fract_transf_matrix[3][1] 0.000000 _atom_sites.fract_transf_matrix[3][2] 0.000000 _atom_sites.fract_transf_matrix[3][3] 0.010287 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C CA N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . ALA A 1 1 ? -1.523 36.170 18.818 1.00 10.47 ? 87 ALA A N 1 ATOM 2 C CA . ALA A 1 1 ? -2.806 35.612 18.337 1.00 12.50 ? 87 ALA A CA 1 ATOM 3 C C . ALA A 1 1 ? -2.683 34.099 18.295 1.00 11.81 ? 87 ALA A C 1 ATOM 4 O O . ALA A 1 1 ? -1.574 33.567 18.083 1.00 11.47 ? 87 ALA A O 1 ATOM 5 C CB . ALA A 1 1 ? -3.120 36.097 16.962 1.00 12.69 ? 87 ALA A CB 1 ATOM 6 N N . PRO A 1 2 ? -3.786 33.400 18.412 1.00 12.86 ? 88 PRO A N 1 ATOM 7 C CA . PRO A 1 2 ? -3.740 31.946 18.360 1.00 12.44 ? 88 PRO A CA 1 ATOM 8 C C . PRO A 1 2 ? -3.631 31.481 16.929 1.00 12.40 ? 88 PRO A C 1 ATOM 9 O O . PRO A 1 2 ? -3.777 32.248 15.965 1.00 12.62 ? 88 PRO A O 1 ATOM 10 C CB . PRO A 1 2 ? -5.094 31.564 18.903 1.00 14.58 ? 88 PRO A CB 1 ATOM 11 C CG . PRO A 1 2 ? -5.954 32.662 18.377 1.00 14.99 ? 88 PRO A CG 1 ATOM 12 C CD . PRO A 1 2 ? -5.174 33.888 18.573 1.00 13.31 ? 88 PRO A CD 1 ATOM 13 N N . TYR A 1 3 ? -3.342 30.209 16.779 1.00 12.53 ? 89 TYR A N 1 ATOM 14 C CA . TYR A 1 3 ? -3.360 29.540 15.483 1.00 11.24 ? 89 TYR A CA 1 ATOM 15 C C . TYR A 1 3 ? -3.893 28.109 15.671 1.00 11.91 ? 89 TYR A C 1 ATOM 16 O O . TYR A 1 3 ? -3.871 27.556 16.774 1.00 12.05 ? 89 TYR A O 1 ATOM 17 C CB . TYR A 1 3 ? -1.965 29.530 14.851 1.00 10.78 ? 89 TYR A CB 1 ATOM 18 C CG . TYR A 1 3 ? -1.009 28.690 15.635 1.00 10.11 ? 89 TYR A CG 1 ATOM 19 C CD1 . TYR A 1 3 ? -0.334 29.214 16.711 1.00 9.87 ? 89 TYR A CD1 1 ATOM 20 C CD2 . TYR A 1 3 ? -0.828 27.347 15.343 1.00 9.87 ? 89 TYR A CD2 1 ATOM 21 C CE1 . TYR A 1 3 ? 0.506 28.425 17.469 1.00 7.80 ? 89 TYR A CE1 1 ATOM 22 C CE2 . TYR A 1 3 ? -0.003 26.558 16.083 1.00 8.15 ? 89 TYR A CE2 1 ATOM 23 C CZ . TYR A 1 3 ? 0.672 27.080 17.147 1.00 7.65 ? 89 TYR A CZ 1 ATOM 24 O OH . TYR A 1 3 ? 1.478 26.272 17.942 1.00 8.81 ? 89 TYR A OH 1 ATOM 25 N N . ASN A 1 4 ? -4.335 27.519 14.572 1.00 14.27 ? 90 ASN A N 1 ATOM 26 C CA . ASN A 1 4 ? -4.739 26.100 14.561 1.00 14.96 ? 90 ASN A CA 1 ATOM 27 C C . ASN A 1 4 ? -3.807 25.318 13.635 1.00 14.10 ? 90 ASN A C 1 ATOM 28 O O . ASN A 1 4 ? -3.395 25.856 12.616 1.00 15.03 ? 90 ASN A O 1 ATOM 29 C CB . ASN A 1 4 ? -6.169 26.014 14.006 1.00 16.62 ? 90 ASN A CB 1 ATOM 30 C CG . ASN A 1 4 ? -7.169 26.662 14.925 1.00 19.58 ? 90 ASN A CG 1 ATOM 31 O OD1 . ASN A 1 4 ? -7.169 26.412 16.158 1.00 22.25 ? 90 ASN A OD1 1 ATOM 32 N ND2 . ASN A 1 4 ? -8.031 27.496 14.354 1.00 24.50 ? 90 ASN A ND2 1 ATOM 33 N N . GLY A 1 5 ? -3.419 24.107 13.985 1.00 12.93 ? 91 GLY A N 1 ATOM 34 C CA . GLY A 1 5 ? -2.718 23.293 13.008 1.00 11.07 ? 91 GLY A CA 1 ATOM 35 C C . GLY A 1 5 ? -1.250 23.663 12.876 1.00 9.19 ? 91 GLY A C 1 ATOM 36 O O . GLY A 1 5 ? -0.595 24.038 13.845 1.00 10.45 ? 91 GLY A O 1 ATOM 37 N N . ASN A 1 6 ? -0.735 23.482 11.668 1.00 8.77 ? 92 ASN A N 1 ATOM 38 C CA . ASN A 1 6 ? 0.680 23.653 11.347 1.00 7.14 ? 92 ASN A CA 1 ATOM 39 C C . ASN A 1 6 ? 1.063 25.133 11.522 1.00 6.72 ? 92 ASN A C 1 ATOM 40 O O . ASN A 1 6 ? 0.547 25.984 10.810 1.00 7.25 ? 92 ASN A O 1 ATOM 41 C CB . ASN A 1 6 ? 0.917 23.206 9.914 1.00 7.20 ? 92 ASN A CB 1 ATOM 42 C CG . ASN A 1 6 ? 2.350 23.281 9.500 1.00 7.72 ? 92 ASN A CG 1 ATOM 43 O OD1 . ASN A 1 6 ? 3.192 23.774 10.252 1.00 7.31 ? 92 ASN A OD1 1 ATOM 44 N ND2 . ASN A 1 6 ? 2.632 22.801 8.284 1.00 8.62 ? 92 ASN A ND2 1 ATOM 45 N N . PRO A 1 7 ? 1.963 25.451 12.453 1.00 7.28 ? 93 PRO A N 1 ATOM 46 C CA . PRO A 1 7 ? 2.314 26.865 12.713 1.00 7.18 ? 93 PRO A CA 1 ATOM 47 C C . PRO A 1 7 ? 3.062 27.488 11.562 1.00 7.20 ? 93 PRO A C 1 ATOM 48 O O . PRO A 1 7 ? 3.179 28.702 11.516 1.00 7.07 ? 93 PRO A O 1 ATOM 49 C CB . PRO A 1 7 ? 3.174 26.793 13.968 1.00 7.15 ? 93 PRO A CB 1 ATOM 50 C CG . PRO A 1 7 ? 3.815 25.450 13.917 1.00 7.57 ? 93 PRO A CG 1 ATOM 51 C CD . PRO A 1 7 ? 2.721 24.554 13.338 1.00 7.86 ? 93 PRO A CD 1 ATOM 52 N N . PHE A 1 8 ? 3.551 26.685 10.603 1.00 7.01 ? 94 PHE A N 1 ATOM 53 C CA . PHE A 1 8 ? 4.261 27.219 9.447 1.00 7.36 ? 94 PHE A CA 1 ATOM 54 C C . PHE A 1 8 ? 3.275 27.630 8.338 1.00 7.51 ? 94 PHE A C 1 ATOM 55 O O . PHE A 1 8 ? 3.688 28.264 7.352 1.00 8.83 ? 94 PHE A O 1 ATOM 56 C CB . PHE A 1 8 ? 5.263 26.211 8.881 1.00 7.53 ? 94 PHE A CB 1 ATOM 57 C CG . PHE A 1 8 ? 6.443 25.968 9.777 1.00 5.88 ? 94 PHE A CG 1 ATOM 58 C CD1 . PHE A 1 8 ? 6.367 25.091 10.833 1.00 6.80 ? 94 PHE A CD1 1 ATOM 59 C CD2 . PHE A 1 8 ? 7.627 26.652 9.561 1.00 6.42 ? 94 PHE A CD2 1 ATOM 60 C CE1 . PHE A 1 8 ? 7.467 24.864 11.642 1.00 6.64 ? 94 PHE A CE1 1 ATOM 61 C CE2 . PHE A 1 8 ? 8.748 26.423 10.349 1.00 6.60 ? 94 PHE A CE2 1 ATOM 62 C CZ . PHE A 1 8 ? 8.660 25.527 11.392 1.00 6.43 ? 94 PHE A CZ 1 ATOM 63 N N . GLU A 1 9 ? 2.006 27.238 8.486 1.00 8.26 ? 95 GLU A N 1 ATOM 64 C CA . GLU A 1 9 ? 0.969 27.620 7.493 1.00 10.15 ? 95 GLU A CA 1 ATOM 65 C C . GLU A 1 9 ? 0.452 29.021 7.772 1.00 10.42 ? 95 GLU A C 1 ATOM 66 O O . GLU A 1 9 ? 0.193 29.384 8.899 1.00 10.74 ? 95 GLU A O 1 ATOM 67 C CB A GLU A 1 9 ? -0.203 26.663 7.597 0.50 11.00 ? 95 GLU A CB 1 ATOM 68 C CB B GLU A 1 9 ? -0.154 26.575 7.386 0.50 10.70 ? 95 GLU A CB 1 ATOM 69 C CG A GLU A 1 9 ? -1.255 26.734 6.509 0.50 14.77 ? 95 GLU A CG 1 ATOM 70 C CG B GLU A 1 9 ? 0.418 25.206 6.976 0.50 13.93 ? 95 GLU A CG 1 ATOM 71 C CD A GLU A 1 9 ? -2.223 25.562 6.591 0.50 19.52 ? 95 GLU A CD 1 ATOM 72 C CD B GLU A 1 9 ? -0.560 24.020 6.820 0.50 17.79 ? 95 GLU A CD 1 ATOM 73 O OE1 A GLU A 1 9 ? -1.967 24.603 7.370 0.50 22.85 ? 95 GLU A OE1 1 ATOM 74 O OE1 B GLU A 1 9 ? -1.786 24.165 6.943 0.50 20.20 ? 95 GLU A OE1 1 ATOM 75 O OE2 A GLU A 1 9 ? -3.246 25.606 5.884 0.50 22.77 ? 95 GLU A OE2 1 ATOM 76 O OE2 B GLU A 1 9 ? -0.061 22.882 6.592 0.50 19.35 ? 95 GLU A OE2 1 ATOM 77 N N . GLY A 1 10 ? 0.263 29.782 6.703 1.00 11.76 ? 96 GLY A N 1 ATOM 78 C CA . GLY A 1 10 ? -0.301 31.102 6.809 1.00 12.95 ? 96 GLY A CA 1 ATOM 79 C C . GLY A 1 10 ? 0.611 32.237 7.184 1.00 12.03 ? 96 GLY A C 1 ATOM 80 O O . GLY A 1 10 ? 0.167 33.368 7.434 1.00 14.46 ? 96 GLY A O 1 ATOM 81 N N . VAL A 1 11 ? 1.903 31.932 7.236 1.00 11.09 ? 97 VAL A N 1 ATOM 82 C CA . VAL A 1 11 ? 2.948 32.909 7.567 1.00 9.82 ? 97 VAL A CA 1 ATOM 83 C C . VAL A 1 11 ? 4.133 32.758 6.636 1.00 9.78 ? 97 VAL A C 1 ATOM 84 O O . VAL A 1 11 ? 4.289 31.726 5.981 1.00 12.23 ? 97 VAL A O 1 ATOM 85 C CB . VAL A 1 11 ? 3.476 32.770 9.014 1.00 9.79 ? 97 VAL A CB 1 ATOM 86 C CG1 . VAL A 1 11 ? 2.387 33.115 10.020 1.00 10.30 ? 97 VAL A CG1 1 ATOM 87 C CG2 . VAL A 1 11 ? 3.950 31.377 9.277 1.00 9.72 ? 97 VAL A CG2 1 ATOM 88 N N . GLN A 1 12 ? 4.956 33.797 6.570 1.00 9.92 ? 98 GLN A N 1 ATOM 89 C CA . GLN A 1 12 ? 6.267 33.799 5.923 1.00 10.60 ? 98 GLN A CA 1 ATOM 90 C C . GLN A 1 12 ? 7.275 33.639 7.052 1.00 9.11 ? 98 GLN A C 1 ATOM 91 O O . GLN A 1 12 ? 7.014 34.042 8.188 1.00 9.06 ? 98 GLN A O 1 ATOM 92 C CB . GLN A 1 12 ? 6.598 35.172 5.270 1.00 12.61 ? 98 GLN A CB 1 ATOM 93 C CG . GLN A 1 12 ? 5.764 35.592 4.176 1.00 16.29 ? 98 GLN A CG 1 ATOM 94 C CD . GLN A 1 12 ? 6.396 36.813 3.495 1.00 18.70 ? 98 GLN A CD 1 ATOM 95 O OE1 . GLN A 1 12 ? 7.487 36.720 2.886 1.00 19.63 ? 98 GLN A OE1 1 ATOM 96 N NE2 . GLN A 1 12 ? 5.755 37.946 3.654 1.00 18.16 ? 98 GLN A NE2 1 ATOM 97 N N . LEU A 1 13 ? 8.414 33.077 6.745 1.00 8.35 ? 99 LEU A N 1 ATOM 98 C CA . LEU A 1 13 ? 9.458 32.932 7.753 1.00 7.52 ? 99 LEU A CA 1 ATOM 99 C C . LEU A 1 13 ? 10.444 34.097 7.659 1.00 6.93 ? 99 LEU A C 1 ATOM 100 O O . LEU A 1 13 ? 11.023 34.384 6.612 1.00 8.66 ? 99 LEU A O 1 ATOM 101 C CB . LEU A 1 13 ? 10.181 31.588 7.604 1.00 7.70 ? 99 LEU A CB 1 ATOM 102 C CG . LEU A 1 13 ? 9.265 30.379 7.802 1.00 8.13 ? 99 LEU A CG 1 ATOM 103 C CD1 . LEU A 1 13 ? 9.964 29.055 7.469 1.00 9.55 ? 99 LEU A CD1 1 ATOM 104 C CD2 . LEU A 1 13 ? 8.666 30.350 9.205 1.00 8.75 ? 99 LEU A CD2 1 ATOM 105 N N . TRP A 1 14 ? 10.697 34.766 8.775 1.00 7.18 ? 100 TRP A N 1 ATOM 106 C CA . TRP A 1 14 ? 11.631 35.897 8.804 1.00 8.19 ? 100 TRP A CA 1 ATOM 107 C C . TRP A 1 14 ? 13.076 35.432 8.709 1.00 7.86 ? 100 TRP A C 1 ATOM 108 O O . TRP A 1 14 ? 13.504 34.564 9.451 1.00 7.46 ? 100 TRP A O 1 ATOM 109 C CB . TRP A 1 14 ? 11.499 36.613 10.139 1.00 8.99 ? 100 TRP A CB 1 ATOM 110 C CG . TRP A 1 14 ? 12.380 37.784 10.409 1.00 7.90 ? 100 TRP A CG 1 ATOM 111 C CD1 . TRP A 1 14 ? 13.376 37.834 11.298 1.00 8.59 ? 100 TRP A CD1 1 ATOM 112 C CD2 . TRP A 1 14 ? 12.265 39.099 9.858 1.00 10.15 ? 100 TRP A CD2 1 ATOM 113 N NE1 . TRP A 1 14 ? 13.955 39.070 11.307 1.00 8.72 ? 100 TRP A NE1 1 ATOM 114 C CE2 . TRP A 1 14 ? 13.273 39.874 10.434 1.00 9.37 ? 100 TRP A CE2 1 ATOM 115 C CE3 . TRP A 1 14 ? 11.414 39.693 8.922 1.00 10.94 ? 100 TRP A CE3 1 ATOM 116 C CZ2 . TRP A 1 14 ? 13.454 41.226 10.134 1.00 11.34 ? 100 TRP A CZ2 1 ATOM 117 C CZ3 . TRP A 1 14 ? 11.584 41.039 8.620 1.00 13.11 ? 100 TRP A CZ3 1 ATOM 118 C CH2 . TRP A 1 14 ? 12.583 41.792 9.239 1.00 11.55 ? 100 TRP A CH2 1 ATOM 119 N N . ALA A 1 15 ? 13.822 36.060 7.822 1.00 7.34 ? 101 ALA A N 1 ATOM 120 C CA . ALA A 1 15 ? 15.273 35.870 7.741 1.00 7.82 ? 101 ALA A CA 1 ATOM 121 C C . ALA A 1 15 ? 15.918 36.938 8.602 1.00 6.90 ? 101 ALA A C 1 ATOM 122 O O . ALA A 1 15 ? 15.720 38.157 8.375 1.00 9.35 ? 101 ALA A O 1 ATOM 123 C CB . ALA A 1 15 ? 15.778 35.943 6.320 1.00 8.19 ? 101 ALA A CB 1 ATOM 124 N N . ASN A 1 16 ? 16.633 36.534 9.636 1.00 7.02 ? 102 ASN A N 1 ATOM 125 C CA . ASN A 1 16 ? 17.047 37.473 10.658 1.00 7.41 ? 102 ASN A CA 1 ATOM 126 C C . ASN A 1 16 ? 18.287 38.254 10.275 1.00 7.76 ? 102 ASN A C 1 ATOM 127 O O . ASN A 1 16 ? 19.087 37.865 9.440 1.00 7.43 ? 102 ASN A O 1 ATOM 128 C CB . ASN A 1 16 ? 17.207 36.752 12.014 1.00 7.74 ? 102 ASN A CB 1 ATOM 129 C CG . ASN A 1 16 ? 18.448 35.812 12.047 1.00 8.47 ? 102 ASN A CG 1 ATOM 130 O OD1 . ASN A 1 16 ? 19.576 36.264 12.144 1.00 8.51 ? 102 ASN A OD1 1 ATOM 131 N ND2 . ASN A 1 16 ? 18.209 34.478 11.961 1.00 7.16 ? 102 ASN A ND2 1 ATOM 132 N N . ASN A 1 17 ? 18.434 39.390 10.922 1.00 7.76 ? 103 ASN A N 1 ATOM 133 C CA . ASN A 1 17 ? 19.537 40.302 10.637 1.00 8.39 ? 103 ASN A CA 1 ATOM 134 C C . ASN A 1 17 ? 20.875 39.928 11.204 1.00 8.12 ? 103 ASN A C 1 ATOM 135 O O . ASN A 1 17 ? 21.884 40.440 10.746 1.00 9.38 ? 103 ASN A O 1 ATOM 136 C CB . ASN A 1 17 ? 19.129 41.738 11.019 1.00 9.41 ? 103 ASN A CB 1 ATOM 137 C CG . ASN A 1 17 ? 18.271 42.369 9.947 1.00 12.15 ? 103 ASN A CG 1 ATOM 138 O OD1 . ASN A 1 17 ? 18.684 42.407 8.774 1.00 16.34 ? 103 ASN A OD1 1 ATOM 139 N ND2 . ASN A 1 17 ? 17.090 42.876 10.307 1.00 14.66 ? 103 ASN A ND2 1 ATOM 140 N N . TYR A 1 18 ? 20.921 38.989 12.148 1.00 8.00 ? 104 TYR A N 1 ATOM 141 C CA . TYR A 1 18 ? 22.175 38.499 12.670 1.00 7.30 ? 104 TYR A CA 1 ATOM 142 C C . TYR A 1 18 ? 22.885 37.706 11.545 1.00 6.61 ? 104 TYR A C 1 ATOM 143 O O . TYR A 1 18 ? 23.996 37.989 11.181 1.00 7.25 ? 104 TYR A O 1 ATOM 144 C CB . TYR A 1 18 ? 21.941 37.631 13.895 1.00 8.11 ? 104 TYR A CB 1 ATOM 145 C CG . TYR A 1 18 ? 23.137 37.068 14.578 1.00 8.47 ? 104 TYR A CG 1 ATOM 146 C CD1 . TYR A 1 18 ? 23.797 35.917 14.105 1.00 9.08 ? 104 TYR A CD1 1 ATOM 147 C CD2 . TYR A 1 18 ? 23.620 37.631 15.731 1.00 8.71 ? 104 TYR A CD2 1 ATOM 148 C CE1 . TYR A 1 18 ? 24.861 35.358 14.790 1.00 8.93 ? 104 TYR A CE1 1 ATOM 149 C CE2 . TYR A 1 18 ? 24.679 37.060 16.400 1.00 10.27 ? 104 TYR A CE2 1 ATOM 150 C CZ . TYR A 1 18 ? 25.306 35.946 15.948 1.00 10.02 ? 104 TYR A CZ 1 ATOM 151 O OH . TYR A 1 18 ? 26.361 35.394 16.671 1.00 13.03 ? 104 TYR A OH 1 ATOM 152 N N . TYR A 1 19 ? 22.198 36.717 10.988 1.00 7.01 ? 105 TYR A N 1 ATOM 153 C CA . TYR A 1 19 ? 22.777 35.916 9.873 1.00 6.39 ? 105 TYR A CA 1 ATOM 154 C C . TYR A 1 19 ? 23.004 36.801 8.661 1.00 6.27 ? 105 TYR A C 1 ATOM 155 O O . TYR A 1 19 ? 24.041 36.723 7.999 1.00 6.52 ? 105 TYR A O 1 ATOM 156 C CB . TYR A 1 19 ? 21.851 34.757 9.522 1.00 6.89 ? 105 TYR A CB 1 ATOM 157 C CG . TYR A 1 19 ? 22.478 33.811 8.536 1.00 5.81 ? 105 TYR A CG 1 ATOM 158 C CD1 . TYR A 1 19 ? 23.415 32.869 8.974 1.00 5.94 ? 105 TYR A CD1 1 ATOM 159 C CD2 . TYR A 1 19 ? 22.170 33.850 7.187 1.00 7.25 ? 105 TYR A CD2 1 ATOM 160 C CE1 . TYR A 1 19 ? 24.023 31.985 8.081 1.00 8.38 ? 105 TYR A CE1 1 ATOM 161 C CE2 . TYR A 1 19 ? 22.774 32.998 6.310 1.00 7.26 ? 105 TYR A CE2 1 ATOM 162 C CZ . TYR A 1 19 ? 23.673 32.058 6.763 1.00 7.35 ? 105 TYR A CZ 1 ATOM 163 O OH . TYR A 1 19 ? 24.266 31.183 5.856 1.00 7.40 ? 105 TYR A OH 1 ATOM 164 N N . ARG A 1 20 ? 22.057 37.691 8.383 1.00 7.20 ? 106 ARG A N 1 ATOM 165 C CA . ARG A 1 20 ? 22.249 38.620 7.245 1.00 7.26 ? 106 ARG A CA 1 ATOM 166 C C . ARG A 1 20 ? 23.519 39.475 7.409 1.00 7.53 ? 106 ARG A C 1 ATOM 167 O O . ARG A 1 20 ? 24.296 39.622 6.475 1.00 8.25 ? 106 ARG A O 1 ATOM 168 C CB . ARG A 1 20 ? 21.016 39.495 7.023 1.00 8.39 ? 106 ARG A CB 1 ATOM 169 C CG . ARG A 1 20 ? 21.083 40.391 5.787 1.00 8.76 ? 106 ARG A CG 1 ATOM 170 C CD . ARG A 1 20 ? 19.832 41.263 5.620 1.00 10.63 ? 106 ARG A CD 1 ATOM 171 N NE . ARG A 1 20 ? 18.668 40.474 5.199 1.00 11.38 ? 106 ARG A NE 1 ATOM 172 C CZ . ARG A 1 20 ? 17.676 40.043 5.981 1.00 14.32 ? 106 ARG A CZ 1 ATOM 173 N NH1 . ARG A 1 20 ? 17.606 40.342 7.270 1.00 15.87 ? 106 ARG A NH1 1 ATOM 174 N NH2 . ARG A 1 20 ? 16.730 39.307 5.472 1.00 16.41 ? 106 ARG A NH2 1 ATOM 175 N N . SER A 1 21 ? 23.750 39.979 8.622 1.00 8.33 ? 107 SER A N 1 ATOM 176 C CA . SER A 1 21 ? 24.946 40.779 8.927 1.00 8.78 ? 107 SER A CA 1 ATOM 177 C C . SER A 1 21 ? 26.201 39.931 8.807 1.00 8.50 ? 107 SER A C 1 ATOM 178 O O . SER A 1 21 ? 27.228 40.378 8.317 1.00 8.73 ? 107 SER A O 1 ATOM 179 C CB A SER A 1 21 ? 24.838 41.448 10.309 0.55 9.52 ? 107 SER A CB 1 ATOM 180 C CB B SER A 1 21 ? 24.861 41.353 10.336 0.45 9.24 ? 107 SER A CB 1 ATOM 181 O OG A SER A 1 21 ? 25.102 40.580 11.390 0.55 11.36 ? 107 SER A OG 1 ATOM 182 O OG B SER A 1 21 ? 23.918 42.409 10.366 0.45 11.83 ? 107 SER A OG 1 ATOM 183 N N . GLU A 1 22 ? 26.139 38.667 9.254 1.00 7.72 ? 108 GLU A N 1 ATOM 184 C CA . GLU A 1 22 ? 27.284 37.783 9.055 1.00 6.63 ? 108 GLU A CA 1 ATOM 185 C C . GLU A 1 22 ? 27.641 37.661 7.575 1.00 6.85 ? 108 GLU A C 1 ATOM 186 O O . GLU A 1 22 ? 28.788 37.799 7.164 1.00 6.89 ? 108 GLU A O 1 ATOM 187 C CB . GLU A 1 22 ? 27.050 36.390 9.651 1.00 6.56 ? 108 GLU A CB 1 ATOM 188 C CG . GLU A 1 22 ? 26.963 36.384 11.165 1.00 7.49 ? 108 GLU A CG 1 ATOM 189 C CD . GLU A 1 22 ? 26.703 34.991 11.734 1.00 7.07 ? 108 GLU A CD 1 ATOM 190 O OE1 . GLU A 1 22 ? 25.660 34.391 11.332 1.00 7.69 ? 108 GLU A OE1 1 ATOM 191 O OE2 . GLU A 1 22 ? 27.541 34.469 12.524 1.00 8.18 ? 108 GLU A OE2 1 ATOM 192 N N . VAL A 1 23 ? 26.636 37.434 6.743 1.00 7.79 ? 109 VAL A N 1 ATOM 193 C CA . VAL A 1 23 ? 26.931 37.249 5.316 1.00 7.67 ? 109 VAL A CA 1 ATOM 194 C C . VAL A 1 23 ? 27.467 38.554 4.684 1.00 8.14 ? 109 VAL A C 1 ATOM 195 O O . VAL A 1 23 ? 28.487 38.527 3.992 1.00 9.04 ? 109 VAL A O 1 ATOM 196 C CB . VAL A 1 23 ? 25.741 36.693 4.508 1.00 7.31 ? 109 VAL A CB 1 ATOM 197 C CG1 . VAL A 1 23 ? 26.057 36.617 3.055 1.00 8.43 ? 109 VAL A CG1 1 ATOM 198 C CG2 . VAL A 1 23 ? 25.349 35.305 5.025 1.00 7.49 ? 109 VAL A CG2 1 ATOM 199 N N . HIS A 1 24 ? 26.788 39.661 4.938 1.00 8.49 ? 110 HIS A N 1 ATOM 200 C CA . HIS A 1 24 ? 27.150 40.920 4.281 1.00 9.07 ? 110 HIS A CA 1 ATOM 201 C C . HIS A 1 24 ? 28.408 41.574 4.848 1.00 10.68 ? 110 HIS A C 1 ATOM 202 O O . HIS A 1 24 ? 29.204 42.167 4.095 1.00 11.71 ? 110 HIS A O 1 ATOM 203 C CB . HIS A 1 24 ? 25.992 41.869 4.318 1.00 9.03 ? 110 HIS A CB 1 ATOM 204 C CG . HIS A 1 24 ? 24.979 41.547 3.281 1.00 9.47 ? 110 HIS A CG 1 ATOM 205 N ND1 . HIS A 1 24 ? 25.085 41.987 1.965 1.00 13.98 ? 110 HIS A ND1 1 ATOM 206 C CD2 . HIS A 1 24 ? 23.897 40.737 3.330 1.00 11.20 ? 110 HIS A CD2 1 ATOM 207 C CE1 . HIS A 1 24 ? 24.063 41.487 1.285 1.00 14.75 ? 110 HIS A CE1 1 ATOM 208 N NE2 . HIS A 1 24 ? 23.322 40.747 2.099 1.00 11.94 ? 110 HIS A NE2 1 ATOM 209 N N . THR A 1 25 ? 28.668 41.423 6.133 1.00 10.83 ? 111 THR A N 1 ATOM 210 C CA . THR A 1 25 ? 29.873 42.064 6.724 1.00 10.59 ? 111 THR A CA 1 ATOM 211 C C . THR A 1 25 ? 31.104 41.189 6.868 1.00 10.73 ? 111 THR A C 1 ATOM 212 O O . THR A 1 25 ? 32.242 41.680 6.942 1.00 11.41 ? 111 THR A O 1 ATOM 213 C CB . THR A 1 25 ? 29.566 42.753 8.068 1.00 12.31 ? 111 THR A CB 1 ATOM 214 O OG1 . THR A 1 25 ? 29.304 41.825 9.111 1.00 13.86 ? 111 THR A OG1 1 ATOM 215 C CG2 . THR A 1 25 ? 28.373 43.619 7.980 1.00 12.43 ? 111 THR A CG2 1 ATOM 216 N N . LEU A 1 26 ? 30.875 39.872 6.985 1.00 9.34 ? 112 LEU A N 1 ATOM 217 C CA . LEU A 1 26 ? 31.964 38.949 7.201 1.00 9.84 ? 112 LEU A CA 1 ATOM 218 C C . LEU A 1 26 ? 32.293 38.103 5.966 1.00 9.94 ? 112 LEU A C 1 ATOM 219 O O . LEU A 1 26 ? 33.458 37.900 5.645 1.00 12.87 ? 112 LEU A O 1 ATOM 220 C CB . LEU A 1 26 ? 31.739 38.027 8.418 1.00 9.42 ? 112 LEU A CB 1 ATOM 221 C CG . LEU A 1 26 ? 31.246 38.742 9.684 1.00 9.22 ? 112 LEU A CG 1 ATOM 222 C CD1 . LEU A 1 26 ? 30.889 37.768 10.769 1.00 9.45 ? 112 LEU A CD1 1 ATOM 223 C CD2 . LEU A 1 26 ? 32.297 39.788 10.173 1.00 11.09 ? 112 LEU A CD2 1 ATOM 224 N N . ALA A 1 27 ? 31.285 37.624 5.266 1.00 8.51 ? 113 ALA A N 1 ATOM 225 C CA . ALA A 1 27 ? 31.492 36.684 4.144 1.00 8.91 ? 113 ALA A CA 1 ATOM 226 C C . ALA A 1 27 ? 31.762 37.394 2.814 1.00 8.73 ? 113 ALA A C 1 ATOM 227 O O . ALA A 1 27 ? 32.816 37.223 2.224 1.00 9.93 ? 113 ALA A O 1 ATOM 228 C CB . ALA A 1 27 ? 30.280 35.794 3.968 1.00 9.70 ? 113 ALA A CB 1 ATOM 229 N N . ILE A 1 28 ? 30.806 38.211 2.392 1.00 9.38 ? 114 ILE A N 1 ATOM 230 C CA . ILE A 1 28 ? 30.870 38.843 1.061 1.00 10.00 ? 114 ILE A CA 1 ATOM 231 C C . ILE A 1 28 ? 32.147 39.686 0.852 1.00 10.62 ? 114 ILE A C 1 ATOM 232 O O . ILE A 1 28 ? 32.755 39.611 -0.221 1.00 10.54 ? 114 ILE A O 1 ATOM 233 C CB . ILE A 1 28 ? 29.563 39.568 0.741 1.00 10.77 ? 114 ILE A CB 1 ATOM 234 C CG1 . ILE A 1 28 ? 28.447 38.555 0.514 1.00 9.79 ? 114 ILE A CG1 1 ATOM 235 C CG2 . ILE A 1 28 ? 29.702 40.489 -0.505 1.00 12.04 ? 114 ILE A CG2 1 ATOM 236 C CD1 . ILE A 1 28 ? 27.069 39.124 0.295 1.00 11.24 ? 114 ILE A CD1 1 ATOM 237 N N . PRO A 1 29 ? 32.602 40.463 1.829 1.00 11.39 ? 115 PRO A N 1 ATOM 238 C CA . PRO A 1 29 ? 33.849 41.216 1.615 1.00 12.83 ? 115 PRO A CA 1 ATOM 239 C C . PRO A 1 29 ? 35.065 40.367 1.320 1.00 14.01 ? 115 PRO A C 1 ATOM 240 O O . PRO A 1 29 ? 36.055 40.891 0.791 1.00 16.66 ? 115 PRO A O 1 ATOM 241 C CB . PRO A 1 29 ? 34.018 41.995 2.922 1.00 12.67 ? 115 PRO A CB 1 ATOM 242 C CG . PRO A 1 29 ? 32.654 42.154 3.428 1.00 12.64 ? 115 PRO A CG 1 ATOM 243 C CD . PRO A 1 29 ? 31.981 40.841 3.102 1.00 10.11 ? 115 PRO A CD 1 ATOM 244 N N . GLN A 1 30 ? 35.018 39.079 1.645 1.00 15.41 ? 116 GLN A N 1 ATOM 245 C CA . GLN A 1 30 ? 36.110 38.144 1.372 1.00 16.20 ? 116 GLN A CA 1 ATOM 246 C C . GLN A 1 30 ? 35.939 37.403 0.042 1.00 16.85 ? 116 GLN A C 1 ATOM 247 O O . GLN A 1 30 ? 36.797 36.611 -0.311 1.00 18.57 ? 116 GLN A O 1 ATOM 248 C CB . GLN A 1 30 ? 36.241 37.097 2.499 1.00 16.85 ? 116 GLN A CB 1 ATOM 249 C CG . GLN A 1 30 ? 36.446 37.678 3.856 1.00 19.97 ? 116 GLN A CG 1 ATOM 250 C CD . GLN A 1 30 ? 36.686 36.610 4.964 1.00 25.01 ? 116 GLN A CD 1 ATOM 251 O OE1 . GLN A 1 30 ? 37.791 36.084 5.087 1.00 30.01 ? 116 GLN A OE1 1 ATOM 252 N NE2 . GLN A 1 30 ? 35.666 36.351 5.808 1.00 28.31 ? 116 GLN A NE2 1 ATOM 253 N N . ILE A 1 31 ? 34.835 37.643 -0.667 1.00 16.17 ? 117 ILE A N 1 ATOM 254 C CA . ILE A 1 31 ? 34.502 36.916 -1.889 1.00 16.87 ? 117 ILE A CA 1 ATOM 255 C C . ILE A 1 31 ? 34.627 37.859 -3.089 1.00 17.97 ? 117 ILE A C 1 ATOM 256 O O . ILE A 1 31 ? 33.977 38.887 -3.155 1.00 18.08 ? 117 ILE A O 1 ATOM 257 C CB . ILE A 1 31 ? 33.095 36.307 -1.801 1.00 16.36 ? 117 ILE A CB 1 ATOM 258 C CG1 . ILE A 1 31 ? 32.992 35.317 -0.615 1.00 15.23 ? 117 ILE A CG1 1 ATOM 259 C CG2 . ILE A 1 31 ? 32.748 35.549 -3.108 1.00 18.59 ? 117 ILE A CG2 1 ATOM 260 C CD1 . ILE A 1 31 ? 31.580 34.904 -0.323 1.00 16.65 ? 117 ILE A CD1 1 ATOM 261 N N . THR A 1 32 ? 35.496 37.513 -4.032 1.00 19.39 ? 118 THR A N 1 ATOM 262 C CA . THR A 1 32 ? 35.671 38.364 -5.231 1.00 20.21 ? 118 THR A CA 1 ATOM 263 C C . THR A 1 32 ? 34.968 37.872 -6.465 1.00 19.88 ? 118 THR A C 1 ATOM 264 O O . THR A 1 32 ? 34.701 38.640 -7.358 1.00 20.55 ? 118 THR A O 1 ATOM 265 C CB . THR A 1 32 ? 37.141 38.553 -5.574 1.00 21.00 ? 118 THR A CB 1 ATOM 266 O OG1 . THR A 1 32 ? 37.793 37.274 -5.628 1.00 22.07 ? 118 THR A OG1 1 ATOM 267 C CG2 . THR A 1 32 ? 37.792 39.368 -4.459 1.00 22.70 ? 118 THR A CG2 1 ATOM 268 N N . ASP A 1 33 ? 34.617 36.598 -6.479 1.00 18.92 ? 119 ASP A N 1 ATOM 269 C CA . ASP A 1 33 ? 33.929 36.049 -7.642 1.00 18.89 ? 119 ASP A CA 1 ATOM 270 C C . ASP A 1 33 ? 32.496 36.585 -7.741 1.00 18.66 ? 119 ASP A C 1 ATOM 271 O O . ASP A 1 33 ? 31.673 36.386 -6.820 1.00 17.42 ? 119 ASP A O 1 ATOM 272 C CB A ASP A 1 33 ? 33.869 34.536 -7.545 0.55 19.36 ? 119 ASP A CB 1 ATOM 273 C CB B ASP A 1 33 ? 33.982 34.531 -7.624 0.45 18.96 ? 119 ASP A CB 1 ATOM 274 C CG A ASP A 1 33 ? 33.251 33.906 -8.769 0.55 20.31 ? 119 ASP A CG 1 ATOM 275 C CG B ASP A 1 33 ? 33.128 33.920 -8.699 0.45 19.08 ? 119 ASP A CG 1 ATOM 276 O OD1 A ASP A 1 33 ? 31.997 33.973 -8.993 0.55 19.64 ? 119 ASP A OD1 1 ATOM 277 O OD1 B ASP A 1 33 ? 33.184 34.409 -9.862 0.45 18.77 ? 119 ASP A OD1 1 ATOM 278 O OD2 A ASP A 1 33 ? 33.984 33.323 -9.587 0.55 21.69 ? 119 ASP A OD2 1 ATOM 279 O OD2 B ASP A 1 33 ? 32.348 32.969 -8.463 0.45 18.02 ? 119 ASP A OD2 1 ATOM 280 N N . PRO A 1 34 ? 32.152 37.272 -8.809 1.00 18.34 ? 120 PRO A N 1 ATOM 281 C CA . PRO A 1 34 ? 30.823 37.871 -8.901 1.00 18.84 ? 120 PRO A CA 1 ATOM 282 C C . PRO A 1 34 ? 29.675 36.865 -8.678 1.00 18.59 ? 120 PRO A C 1 ATOM 283 O O . PRO A 1 34 ? 28.704 37.179 -7.990 1.00 18.13 ? 120 PRO A O 1 ATOM 284 C CB . PRO A 1 34 ? 30.797 38.463 -10.308 1.00 19.62 ? 120 PRO A CB 1 ATOM 285 C CG . PRO A 1 34 ? 32.221 38.782 -10.559 1.00 19.13 ? 120 PRO A CG 1 ATOM 286 C CD . PRO A 1 34 ? 32.997 37.647 -9.968 1.00 18.52 ? 120 PRO A CD 1 ATOM 287 N N . ALA A 1 35 ? 29.767 35.692 -9.275 1.00 18.60 ? 121 ALA A N 1 ATOM 288 C CA . ALA A 1 35 ? 28.669 34.739 -9.148 1.00 18.95 ? 121 ALA A CA 1 ATOM 289 C C . ALA A 1 35 ? 28.531 34.249 -7.705 1.00 17.85 ? 121 ALA A C 1 ATOM 290 O O . ALA A 1 35 ? 27.391 34.161 -7.217 1.00 17.66 ? 121 ALA A O 1 ATOM 291 C CB . ALA A 1 35 ? 28.797 33.612 -10.135 1.00 19.57 ? 121 ALA A CB 1 ATOM 292 N N . LEU A 1 36 ? 29.647 33.957 -7.038 1.00 16.43 ? 122 LEU A N 1 ATOM 293 C CA . LEU A 1 36 ? 29.625 33.548 -5.612 1.00 15.69 ? 122 LEU A CA 1 ATOM 294 C C . LEU A 1 36 ? 29.130 34.706 -4.730 1.00 15.73 ? 122 LEU A C 1 ATOM 295 O O . LEU A 1 36 ? 28.437 34.472 -3.740 1.00 13.82 ? 122 LEU A O 1 ATOM 296 C CB . LEU A 1 36 ? 30.953 32.988 -5.073 1.00 17.31 ? 122 LEU A CB 1 ATOM 297 C CG . LEU A 1 36 ? 31.418 31.571 -5.400 1.00 19.78 ? 122 LEU A CG 1 ATOM 298 C CD1 . LEU A 1 36 ? 32.825 31.375 -4.843 1.00 22.25 ? 122 LEU A CD1 1 ATOM 299 C CD2 . LEU A 1 36 ? 30.437 30.521 -4.829 1.00 22.10 ? 122 LEU A CD2 1 ATOM 300 N N . ARG A 1 37 ? 29.444 35.961 -5.075 1.00 13.76 ? 123 ARG A N 1 ATOM 301 C CA . ARG A 1 37 ? 28.891 37.108 -4.329 1.00 13.76 ? 123 ARG A CA 1 ATOM 302 C C . ARG A 1 37 ? 27.379 37.200 -4.421 1.00 12.88 ? 123 ARG A C 1 ATOM 303 O O . ARG A 1 37 ? 26.689 37.444 -3.415 1.00 12.08 ? 123 ARG A O 1 ATOM 304 C CB . ARG A 1 37 ? 29.516 38.429 -4.788 1.00 14.33 ? 123 ARG A CB 1 ATOM 305 C CG . ARG A 1 37 ? 30.968 38.536 -4.499 1.00 14.57 ? 123 ARG A CG 1 ATOM 306 C CD . ARG A 1 37 ? 31.542 39.860 -5.034 1.00 15.13 ? 123 ARG A CD 1 ATOM 307 N NE . ARG A 1 37 ? 30.841 41.004 -4.462 1.00 14.85 ? 123 ARG A NE 1 ATOM 308 C CZ . ARG A 1 37 ? 31.187 41.649 -3.339 1.00 11.46 ? 123 ARG A CZ 1 ATOM 309 N NH1 . ARG A 1 37 ? 32.217 41.299 -2.586 1.00 15.02 ? 123 ARG A NH1 1 ATOM 310 N NH2 . ARG A 1 37 ? 30.463 42.668 -2.930 1.00 14.12 ? 123 ARG A NH2 1 ATOM 311 N N . ALA A 1 38 ? 26.836 37.013 -5.623 1.00 13.49 ? 124 ALA A N 1 ATOM 312 C CA . ALA A 1 38 ? 25.396 37.080 -5.806 1.00 13.51 ? 124 ALA A CA 1 ATOM 313 C C . ALA A 1 38 ? 24.713 35.889 -5.086 1.00 12.23 ? 124 ALA A C 1 ATOM 314 O O . ALA A 1 38 ? 23.611 36.047 -4.487 1.00 13.10 ? 124 ALA A O 1 ATOM 315 C CB . ALA A 1 38 ? 25.018 37.057 -7.304 1.00 15.21 ? 124 ALA A CB 1 ATOM 316 N N . ALA A 1 39 ? 25.369 34.741 -5.137 1.00 11.82 ? 125 ALA A N 1 ATOM 317 C CA . ALA A 1 39 ? 24.846 33.525 -4.462 1.00 11.05 ? 125 ALA A CA 1 ATOM 318 C C . ALA A 1 39 ? 24.821 33.770 -2.957 1.00 10.37 ? 125 ALA A C 1 ATOM 319 O O . ALA A 1 39 ? 23.871 33.446 -2.285 1.00 10.96 ? 125 ALA A O 1 ATOM 320 C CB . ALA A 1 39 ? 25.684 32.310 -4.750 1.00 12.51 ? 125 ALA A CB 1 ATOM 321 N N . ALA A 1 40 ? 25.879 34.385 -2.435 1.00 9.75 ? 126 ALA A N 1 ATOM 322 C CA . ALA A 1 40 ? 25.970 34.687 -1.019 1.00 9.48 ? 126 ALA A CA 1 ATOM 323 C C . ALA A 1 40 ? 24.870 35.659 -0.581 1.00 8.38 ? 126 ALA A C 1 ATOM 324 O O . ALA A 1 40 ? 24.208 35.493 0.447 1.00 8.76 ? 126 ALA A O 1 ATOM 325 C CB . ALA A 1 40 ? 27.295 35.256 -0.699 1.00 9.01 ? 126 ALA A CB 1 ATOM 326 N N . SER A 1 41 ? 24.674 36.708 -1.382 1.00 9.29 ? 127 SER A N 1 ATOM 327 C CA . SER A 1 41 ? 23.602 37.645 -1.105 1.00 10.03 ? 127 SER A CA 1 ATOM 328 C C . SER A 1 41 ? 22.243 36.952 -1.034 1.00 9.96 ? 127 SER A C 1 ATOM 329 O O . SER A 1 41 ? 21.381 37.300 -0.209 1.00 10.00 ? 127 SER A O 1 ATOM 330 C CB A SER A 1 41 ? 23.646 38.802 -2.105 0.60 10.68 ? 127 SER A CB 1 ATOM 331 C CB B SER A 1 41 ? 23.477 38.706 -2.202 0.40 10.67 ? 127 SER A CB 1 ATOM 332 O OG A SER A 1 41 ? 22.770 39.822 -1.713 0.60 11.48 ? 127 SER A OG 1 ATOM 333 O OG B SER A 1 41 ? 24.491 39.666 -2.113 0.40 11.95 ? 127 SER A OG 1 ATOM 334 N N . ALA A 1 42 ? 22.015 35.979 -1.906 1.00 9.39 ? 128 ALA A N 1 ATOM 335 C CA . ALA A 1 42 ? 20.737 35.253 -1.916 1.00 8.51 ? 128 ALA A CA 1 ATOM 336 C C . ALA A 1 42 ? 20.552 34.393 -0.646 1.00 7.76 ? 128 ALA A C 1 ATOM 337 O O . ALA A 1 42 ? 19.474 34.308 -0.084 1.00 7.98 ? 128 ALA A O 1 ATOM 338 C CB . ALA A 1 42 ? 20.641 34.375 -3.163 1.00 8.41 ? 128 ALA A CB 1 ATOM 339 N N . VAL A 1 43 ? 21.644 33.741 -0.215 1.00 7.63 ? 129 VAL A N 1 ATOM 340 C CA . VAL A 1 43 ? 21.537 32.857 0.954 1.00 8.02 ? 129 VAL A CA 1 ATOM 341 C C . VAL A 1 43 ? 21.278 33.639 2.261 1.00 7.46 ? 129 VAL A C 1 ATOM 342 O O . VAL A 1 43 ? 20.586 33.169 3.148 1.00 7.22 ? 129 VAL A O 1 ATOM 343 C CB A VAL A 1 43 ? 22.655 31.802 1.014 0.60 8.52 ? 129 VAL A CB 1 ATOM 344 C CB B VAL A 1 43 ? 22.770 31.925 1.135 0.40 8.67 ? 129 VAL A CB 1 ATOM 345 C CG1 A VAL A 1 43 ? 23.947 32.400 1.209 0.60 10.37 ? 129 VAL A CG1 1 ATOM 346 C CG1 B VAL A 1 43 ? 23.196 31.326 -0.172 0.40 9.32 ? 129 VAL A CG1 1 ATOM 347 C CG2 A VAL A 1 43 ? 22.300 30.701 2.098 0.60 7.02 ? 129 VAL A CG2 1 ATOM 348 C CG2 B VAL A 1 43 ? 23.905 32.620 1.783 0.40 11.10 ? 129 VAL A CG2 1 ATOM 349 N N . ALA A 1 44 ? 21.703 34.907 2.302 1.00 8.10 ? 130 ALA A N 1 ATOM 350 C CA . ALA A 1 44 ? 21.429 35.779 3.431 1.00 7.93 ? 130 ALA A CA 1 ATOM 351 C C . ALA A 1 44 ? 19.959 36.011 3.656 1.00 8.42 ? 130 ALA A C 1 ATOM 352 O O . ALA A 1 44 ? 19.565 36.423 4.743 1.00 9.19 ? 130 ALA A O 1 ATOM 353 C CB . ALA A 1 44 ? 22.127 37.084 3.222 1.00 8.97 ? 130 ALA A CB 1 ATOM 354 N N . GLU A 1 45 ? 19.173 35.795 2.608 1.00 8.03 ? 131 GLU A N 1 ATOM 355 C CA . GLU A 1 45 ? 17.702 35.949 2.635 1.00 8.15 ? 131 GLU A CA 1 ATOM 356 C C . GLU A 1 45 ? 16.938 34.687 2.962 1.00 6.95 ? 131 GLU A C 1 ATOM 357 O O . GLU A 1 45 ? 15.703 34.720 3.064 1.00 8.24 ? 131 GLU A O 1 ATOM 358 C CB . GLU A 1 45 ? 17.174 36.571 1.337 1.00 8.21 ? 131 GLU A CB 1 ATOM 359 C CG . GLU A 1 45 ? 17.890 37.880 0.981 1.00 9.70 ? 131 GLU A CG 1 ATOM 360 C CD . GLU A 1 45 ? 17.732 38.922 2.068 1.00 11.22 ? 131 GLU A CD 1 ATOM 361 O OE1 . GLU A 1 45 ? 16.608 39.085 2.594 1.00 13.83 ? 131 GLU A OE1 1 ATOM 362 O OE2 . GLU A 1 45 ? 18.731 39.571 2.475 1.00 13.52 ? 131 GLU A OE2 1 ATOM 363 N N . VAL A 1 46 ? 17.666 33.580 3.125 1.00 6.61 ? 132 VAL A N 1 ATOM 364 C CA . VAL A 1 46 ? 17.009 32.324 3.464 1.00 6.67 ? 132 VAL A CA 1 ATOM 365 C C . VAL A 1 46 ? 16.760 32.278 4.969 1.00 6.83 ? 132 VAL A C 1 ATOM 366 O O . VAL A 1 46 ? 17.665 32.488 5.763 1.00 7.70 ? 132 VAL A O 1 ATOM 367 C CB . VAL A 1 46 ? 17.833 31.091 3.002 1.00 7.80 ? 132 VAL A CB 1 ATOM 368 C CG1 . VAL A 1 46 ? 17.107 29.775 3.414 1.00 7.63 ? 132 VAL A CG1 1 ATOM 369 C CG2 . VAL A 1 46 ? 18.017 31.107 1.538 1.00 7.95 ? 132 VAL A CG2 1 ATOM 370 N N . PRO A 1 47 ? 15.531 32.037 5.391 1.00 6.85 ? 133 PRO A N 1 ATOM 371 C CA . PRO A 1 47 ? 15.204 32.147 6.823 1.00 7.13 ? 133 PRO A CA 1 ATOM 372 C C . PRO A 1 47 ? 15.588 30.937 7.656 1.00 7.51 ? 133 PRO A C 1 ATOM 373 O O . PRO A 1 47 ? 14.890 29.931 7.668 1.00 9.93 ? 133 PRO A O 1 ATOM 374 C CB . PRO A 1 47 ? 13.709 32.396 6.814 1.00 7.52 ? 133 PRO A CB 1 ATOM 375 C CG . PRO A 1 47 ? 13.241 31.690 5.595 1.00 7.65 ? 133 PRO A CG 1 ATOM 376 C CD . PRO A 1 47 ? 14.329 31.851 4.565 1.00 6.22 ? 133 PRO A CD 1 ATOM 377 N N . SER A 1 48 ? 16.647 31.124 8.444 1.00 6.08 ? 134 SER A N 1 ATOM 378 C CA . SER A 1 48 ? 17.147 30.084 9.355 1.00 5.19 ? 134 SER A CA 1 ATOM 379 C C . SER A 1 48 ? 16.843 30.446 10.818 1.00 5.45 ? 134 SER A C 1 ATOM 380 O O . SER A 1 48 ? 16.601 31.598 11.151 1.00 5.78 ? 134 SER A O 1 ATOM 381 C CB . SER A 1 48 ? 18.652 29.909 9.195 1.00 6.69 ? 134 SER A CB 1 ATOM 382 O OG . SER A 1 48 ? 19.379 31.151 9.240 1.00 6.21 ? 134 SER A OG 1 ATOM 383 N N . PHE A 1 49 ? 16.848 29.434 11.694 1.00 5.14 ? 135 PHE A N 1 ATOM 384 C CA . PHE A 1 49 ? 16.614 29.657 13.119 1.00 5.12 ? 135 PHE A CA 1 ATOM 385 C C . PHE A 1 49 ? 17.720 30.520 13.756 1.00 4.78 ? 135 PHE A C 1 ATOM 386 O O . PHE A 1 49 ? 18.899 30.438 13.367 1.00 5.10 ? 135 PHE A O 1 ATOM 387 C CB . PHE A 1 49 ? 16.567 28.319 13.867 1.00 4.20 ? 135 PHE A CB 1 ATOM 388 C CG . PHE A 1 49 ? 15.217 27.617 13.845 1.00 4.66 ? 135 PHE A CG 1 ATOM 389 C CD1 . PHE A 1 49 ? 14.678 27.095 12.661 1.00 4.90 ? 135 PHE A CD1 1 ATOM 390 C CD2 . PHE A 1 49 ? 14.475 27.511 15.008 1.00 4.63 ? 135 PHE A CD2 1 ATOM 391 C CE1 . PHE A 1 49 ? 13.446 26.480 12.672 1.00 4.96 ? 135 PHE A CE1 1 ATOM 392 C CE2 . PHE A 1 49 ? 13.232 26.952 15.030 1.00 4.89 ? 135 PHE A CE2 1 ATOM 393 C CZ . PHE A 1 49 ? 12.733 26.398 13.845 1.00 4.50 ? 135 PHE A CZ 1 ATOM 394 N N . GLN A 1 50 ? 17.332 31.303 14.752 1.00 5.73 ? 136 GLN A N 1 ATOM 395 C CA . GLN A 1 50 ? 18.213 32.060 15.590 1.00 6.24 ? 136 GLN A CA 1 ATOM 396 C C . GLN A 1 50 ? 18.325 31.331 16.930 1.00 5.34 ? 136 GLN A C 1 ATOM 397 O O . GLN A 1 50 ? 17.312 30.994 17.528 1.00 6.50 ? 136 GLN A O 1 ATOM 398 C CB . GLN A 1 50 ? 17.648 33.466 15.770 1.00 8.01 ? 136 GLN A CB 1 ATOM 399 C CG . GLN A 1 50 ? 18.451 34.308 16.714 1.00 11.89 ? 136 GLN A CG 1 ATOM 400 C CD . GLN A 1 50 ? 18.313 35.773 16.462 1.00 13.77 ? 136 GLN A CD 1 ATOM 401 O OE1 . GLN A 1 50 ? 19.161 36.388 15.774 1.00 15.58 ? 136 GLN A OE1 1 ATOM 402 N NE2 . GLN A 1 50 ? 17.276 36.341 17.039 1.00 13.03 ? 136 GLN A NE2 1 ATOM 403 N N . TRP A 1 51 ? 19.535 31.137 17.411 1.00 6.14 ? 137 TRP A N 1 ATOM 404 C CA . TRP A 1 51 ? 19.796 30.320 18.584 1.00 5.28 ? 137 TRP A CA 1 ATOM 405 C C . TRP A 1 51 ? 20.037 31.145 19.829 1.00 5.85 ? 137 TRP A C 1 ATOM 406 O O . TRP A 1 51 ? 20.913 32.026 19.864 1.00 6.60 ? 137 TRP A O 1 ATOM 407 C CB . TRP A 1 51 ? 21.026 29.451 18.338 1.00 5.32 ? 137 TRP A CB 1 ATOM 408 C CG . TRP A 1 51 ? 20.842 28.354 17.294 1.00 4.75 ? 137 TRP A CG 1 ATOM 409 C CD1 . TRP A 1 51 ? 20.418 28.486 15.990 1.00 6.14 ? 137 TRP A CD1 1 ATOM 410 C CD2 . TRP A 1 51 ? 21.074 26.954 17.486 1.00 5.01 ? 137 TRP A CD2 1 ATOM 411 N NE1 . TRP A 1 51 ? 20.401 27.265 15.380 1.00 6.32 ? 137 TRP A NE1 1 ATOM 412 C CE2 . TRP A 1 51 ? 20.816 26.305 16.256 1.00 6.09 ? 137 TRP A CE2 1 ATOM 413 C CE3 . TRP A 1 51 ? 21.531 26.189 18.556 1.00 6.72 ? 137 TRP A CE3 1 ATOM 414 C CZ2 . TRP A 1 51 ? 20.943 24.903 16.094 1.00 6.56 ? 137 TRP A CZ2 1 ATOM 415 C CZ3 . TRP A 1 51 ? 21.690 24.841 18.401 1.00 7.12 ? 137 TRP A CZ3 1 ATOM 416 C CH2 . TRP A 1 51 ? 21.392 24.194 17.169 1.00 7.15 ? 137 TRP A CH2 1 ATOM 417 N N . LEU A 1 52 ? 19.295 30.812 20.884 1.00 5.61 ? 138 LEU A N 1 ATOM 418 C CA . LEU A 1 52 ? 19.526 31.404 22.195 1.00 5.69 ? 138 LEU A CA 1 ATOM 419 C C . LEU A 1 52 ? 20.457 30.493 22.987 1.00 5.66 ? 138 LEU A C 1 ATOM 420 O O . LEU A 1 52 ? 20.055 29.849 23.938 1.00 6.17 ? 138 LEU A O 1 ATOM 421 C CB . LEU A 1 52 ? 18.215 31.708 22.950 1.00 5.52 ? 138 LEU A CB 1 ATOM 422 C CG . LEU A 1 52 ? 17.172 32.473 22.159 1.00 5.64 ? 138 LEU A CG 1 ATOM 423 C CD1 . LEU A 1 52 ? 15.945 32.673 23.015 1.00 6.31 ? 138 LEU A CD1 1 ATOM 424 C CD2 . LEU A 1 52 ? 17.731 33.791 21.560 1.00 5.96 ? 138 LEU A CD2 1 ATOM 425 N N . ASP A 1 53 ? 21.697 30.381 22.517 1.00 5.75 ? 139 ASP A N 1 ATOM 426 C CA . ASP A 1 53 ? 22.628 29.398 23.027 1.00 6.49 ? 139 ASP A CA 1 ATOM 427 C C . ASP A 1 53 ? 23.493 29.920 24.172 1.00 6.54 ? 139 ASP A C 1 ATOM 428 O O . ASP A 1 53 ? 24.290 29.197 24.694 1.00 6.88 ? 139 ASP A O 1 ATOM 429 C CB . ASP A 1 53 ? 23.513 28.889 21.898 1.00 6.86 ? 139 ASP A CB 1 ATOM 430 C CG . ASP A 1 53 ? 24.383 29.953 21.310 1.00 11.30 ? 139 ASP A CG 1 ATOM 431 O OD1 . ASP A 1 53 ? 24.057 31.150 21.239 1.00 11.14 ? 139 ASP A OD1 1 ATOM 432 O OD2 . ASP A 1 53 ? 25.504 29.628 20.915 1.00 21.24 ? 139 ASP A OD2 1 ATOM 433 N N . ARG A 1 54 ? 23.292 31.185 24.541 1.00 7.08 ? 140 ARG A N 1 ATOM 434 C CA . ARG A 1 54 ? 23.934 31.857 25.678 1.00 7.58 ? 140 ARG A CA 1 ATOM 435 C C . ARG A 1 54 ? 22.872 32.800 26.236 1.00 6.88 ? 140 ARG A C 1 ATOM 436 O O . ARG A 1 54 ? 22.109 33.409 25.498 1.00 6.60 ? 140 ARG A O 1 ATOM 437 C CB . ARG A 1 54 ? 25.159 32.715 25.267 1.00 9.79 ? 140 ARG A CB 1 ATOM 438 C CG . ARG A 1 54 ? 26.333 31.921 24.719 1.00 16.77 ? 140 ARG A CG 1 ATOM 439 C CD . ARG A 1 54 ? 27.276 32.820 23.960 1.00 21.57 ? 140 ARG A CD 1 ATOM 440 N NE . ARG A 1 54 ? 26.628 33.207 22.702 1.00 25.38 ? 140 ARG A NE 1 ATOM 441 C CZ . ARG A 1 54 ? 26.496 34.446 22.200 1.00 26.36 ? 140 ARG A CZ 1 ATOM 442 N NH1 . ARG A 1 54 ? 27.031 35.526 22.740 1.00 28.97 ? 140 ARG A NH1 1 ATOM 443 N NH2 . ARG A 1 54 ? 25.851 34.598 21.069 1.00 29.41 ? 140 ARG A NH2 1 ATOM 444 N N . ASN A 1 55 ? 22.876 32.971 27.531 1.00 6.27 ? 141 ASN A N 1 ATOM 445 C CA . ASN A 1 55 ? 21.889 33.825 28.228 1.00 5.74 ? 141 ASN A CA 1 ATOM 446 C C . ASN A 1 55 ? 21.825 35.273 27.723 1.00 5.10 ? 141 ASN A C 1 ATOM 447 O O . ASN A 1 55 ? 20.737 35.869 27.633 1.00 5.36 ? 141 ASN A O 1 ATOM 448 C CB . ASN A 1 55 ? 22.118 33.743 29.725 1.00 5.86 ? 141 ASN A CB 1 ATOM 449 C CG . ASN A 1 55 ? 21.059 34.458 30.531 1.00 6.83 ? 141 ASN A CG 1 ATOM 450 O OD1 . ASN A 1 55 ? 19.850 34.222 30.368 1.00 6.80 ? 141 ASN A OD1 1 ATOM 451 N ND2 . ASN A 1 55 ? 21.527 35.370 31.409 1.00 6.01 ? 141 ASN A ND2 1 ATOM 452 N N . VAL A 1 56 ? 22.976 35.840 27.377 1.00 5.28 ? 142 VAL A N 1 ATOM 453 C CA . VAL A 1 56 ? 23.008 37.214 26.871 1.00 5.80 ? 142 VAL A CA 1 ATOM 454 C C . VAL A 1 56 ? 22.214 37.457 25.597 1.00 5.91 ? 142 VAL A C 1 ATOM 455 O O . VAL A 1 56 ? 21.915 38.606 25.295 1.00 7.77 ? 142 VAL A O 1 ATOM 456 C CB . VAL A 1 56 ? 24.441 37.737 26.651 1.00 7.19 ? 142 VAL A CB 1 ATOM 457 C CG1 . VAL A 1 56 ? 25.156 37.925 27.985 1.00 9.15 ? 142 VAL A CG1 1 ATOM 458 C CG2 . VAL A 1 56 ? 25.236 36.839 25.706 1.00 7.88 ? 142 VAL A CG2 1 ATOM 459 N N . THR A 1 57 ? 21.855 36.386 24.860 1.00 5.66 ? 143 THR A N 1 ATOM 460 C CA . THR A 1 57 ? 21.049 36.510 23.630 1.00 6.18 ? 143 THR A CA 1 ATOM 461 C C . THR A 1 57 ? 19.593 36.867 23.908 1.00 6.02 ? 143 THR A C 1 ATOM 462 O O . THR A 1 57 ? 18.910 37.324 23.000 1.00 7.08 ? 143 THR A O 1 ATOM 463 C CB . THR A 1 57 ? 21.067 35.243 22.755 1.00 6.03 ? 143 THR A CB 1 ATOM 464 O OG1 . THR A 1 57 ? 20.493 34.144 23.489 1.00 7.29 ? 143 THR A OG1 1 ATOM 465 C CG2 . THR A 1 57 ? 22.504 34.873 22.389 1.00 7.63 ? 143 THR A CG2 1 ATOM 466 N N . VAL A 1 58 ? 19.120 36.610 25.138 1.00 5.28 ? 144 VAL A N 1 ATOM 467 C CA . VAL A 1 58 ? 17.703 36.767 25.441 1.00 5.79 ? 144 VAL A CA 1 ATOM 468 C C . VAL A 1 58 ? 17.277 38.238 25.385 1.00 6.15 ? 144 VAL A C 1 ATOM 469 O O . VAL A 1 58 ? 16.334 38.602 24.667 1.00 5.94 ? 144 VAL A O 1 ATOM 470 C CB . VAL A 1 58 ? 17.347 36.116 26.784 1.00 5.67 ? 144 VAL A CB 1 ATOM 471 C CG1 . VAL A 1 58 ? 15.913 36.370 27.191 1.00 5.50 ? 144 VAL A CG1 1 ATOM 472 C CG2 . VAL A 1 58 ? 17.610 34.628 26.719 1.00 7.26 ? 144 VAL A CG2 1 ATOM 473 N N . ASP A 1 59 ? 17.983 39.103 26.102 1.00 5.91 ? 145 ASP A N 1 ATOM 474 C CA . ASP A 1 59 ? 17.616 40.508 26.124 1.00 6.71 ? 145 ASP A CA 1 ATOM 475 C C . ASP A 1 59 ? 18.283 41.333 25.002 1.00 6.99 ? 145 ASP A C 1 ATOM 476 O O . ASP A 1 59 ? 18.149 42.576 24.963 1.00 9.79 ? 145 ASP A O 1 ATOM 477 C CB . ASP A 1 59 ? 17.842 41.131 27.508 1.00 5.61 ? 145 ASP A CB 1 ATOM 478 C CG . ASP A 1 59 ? 16.573 41.133 28.354 1.00 8.51 ? 145 ASP A CG 1 ATOM 479 O OD1 . ASP A 1 59 ? 15.590 41.803 27.927 1.00 10.20 ? 145 ASP A OD1 1 ATOM 480 O OD2 . ASP A 1 59 ? 16.500 40.442 29.390 1.00 7.60 ? 145 ASP A OD2 1 ATOM 481 N N . THR A 1 60 ? 19.013 40.677 24.114 1.00 6.76 ? 146 THR A N 1 ATOM 482 C CA . THR A 1 60 ? 19.582 41.293 22.913 1.00 6.82 ? 146 THR A CA 1 ATOM 483 C C . THR A 1 60 ? 18.905 40.749 21.665 1.00 7.00 ? 146 THR A C 1 ATOM 484 O O . THR A 1 60 ? 17.899 41.304 21.215 1.00 7.78 ? 146 THR A O 1 ATOM 485 C CB . THR A 1 60 ? 21.105 41.153 22.887 1.00 7.62 ? 146 THR A CB 1 ATOM 486 O OG1 . THR A 1 60 ? 21.539 39.763 22.936 1.00 7.16 ? 146 THR A OG1 1 ATOM 487 C CG2 . THR A 1 60 ? 21.718 41.889 24.069 1.00 8.45 ? 146 THR A CG2 1 ATOM 488 N N . LEU A 1 61 ? 19.369 39.615 21.180 1.00 7.16 ? 147 LEU A N 1 ATOM 489 C CA . LEU A 1 61 ? 18.914 39.037 19.920 1.00 7.31 ? 147 LEU A CA 1 ATOM 490 C C . LEU A 1 61 ? 17.434 38.744 19.885 1.00 6.50 ? 147 LEU A C 1 ATOM 491 O O . LEU A 1 61 ? 16.728 39.037 18.876 1.00 6.71 ? 147 LEU A O 1 ATOM 492 C CB . LEU A 1 61 ? 19.683 37.727 19.644 1.00 7.86 ? 147 LEU A CB 1 ATOM 493 C CG . LEU A 1 61 ? 21.218 37.856 19.541 1.00 10.32 ? 147 LEU A CG 1 ATOM 494 C CD1 . LEU A 1 61 ? 21.767 36.561 18.970 1.00 11.46 ? 147 LEU A CD1 1 ATOM 495 C CD2 . LEU A 1 61 ? 21.611 39.029 18.692 1.00 12.14 ? 147 LEU A CD2 1 ATOM 496 N N . LEU A 1 62 ? 16.911 38.116 20.940 1.00 5.87 ? 148 LEU A N 1 ATOM 497 C CA . LEU A 1 62 ? 15.487 37.746 20.876 1.00 5.89 ? 148 LEU A CA 1 ATOM 498 C C . LEU A 1 62 ? 14.597 38.983 20.751 1.00 5.67 ? 148 LEU A C 1 ATOM 499 O O . LEU A 1 62 ? 13.725 39.058 19.910 1.00 6.16 ? 148 LEU A O 1 ATOM 500 C CB . LEU A 1 62 ? 15.088 36.893 22.074 1.00 4.80 ? 148 LEU A CB 1 ATOM 501 C CG . LEU A 1 62 ? 13.626 36.446 22.123 1.00 5.07 ? 148 LEU A CG 1 ATOM 502 C CD1 . LEU A 1 62 ? 13.250 35.518 20.988 1.00 5.86 ? 148 LEU A CD1 1 ATOM 503 C CD2 . LEU A 1 62 ? 13.336 35.776 23.474 1.00 6.99 ? 148 LEU A CD2 1 ATOM 504 N N . VAL A 1 63 ? 14.849 39.955 21.581 1.00 5.91 ? 149 VAL A N 1 ATOM 505 C CA . VAL A 1 63 ? 14.070 41.218 21.601 1.00 6.62 ? 149 VAL A CA 1 ATOM 506 C C . VAL A 1 63 ? 14.222 41.936 20.250 1.00 6.55 ? 149 VAL A C 1 ATOM 507 O O . VAL A 1 63 ? 13.266 42.422 19.670 1.00 7.16 ? 149 VAL A O 1 ATOM 508 C CB . VAL A 1 63 ? 14.533 42.117 22.756 1.00 6.94 ? 149 VAL A CB 1 ATOM 509 C CG1 . VAL A 1 63 ? 13.908 43.507 22.691 1.00 8.99 ? 149 VAL A CG1 1 ATOM 510 C CG2 . VAL A 1 63 ? 14.191 41.492 24.093 1.00 7.89 ? 149 VAL A CG2 1 ATOM 511 N N . GLN A 1 64 ? 15.450 41.998 19.758 1.00 6.94 ? 150 GLN A N 1 ATOM 512 C CA . GLN A 1 64 ? 15.723 42.685 18.483 1.00 7.98 ? 150 GLN A CA 1 ATOM 513 C C . GLN A 1 64 ? 14.981 42.014 17.335 1.00 6.90 ? 150 GLN A C 1 ATOM 514 O O . GLN A 1 64 ? 14.296 42.695 16.524 1.00 7.85 ? 150 GLN A O 1 ATOM 515 C CB A GLN A 1 64 ? 17.225 42.646 18.219 0.50 8.72 ? 150 GLN A CB 1 ATOM 516 C CB B GLN A 1 64 ? 17.217 42.784 18.209 0.50 8.65 ? 150 GLN A CB 1 ATOM 517 C CG A GLN A 1 64 ? 17.957 43.627 19.089 0.50 12.11 ? 150 GLN A CG 1 ATOM 518 C CG B GLN A 1 64 ? 17.520 43.644 16.965 0.50 11.41 ? 150 GLN A CG 1 ATOM 519 C CD A GLN A 1 64 ? 19.461 43.405 19.210 0.50 15.75 ? 150 GLN A CD 1 ATOM 520 C CD B GLN A 1 64 ? 17.194 45.155 17.164 0.50 16.30 ? 150 GLN A CD 1 ATOM 521 O OE1 A GLN A 1 64 ? 20.085 44.024 20.079 0.50 20.22 ? 150 GLN A OE1 1 ATOM 522 O OE1 B GLN A 1 64 ? 17.264 45.683 18.287 0.50 20.13 ? 150 GLN A OE1 1 ATOM 523 N NE2 A GLN A 1 64 ? 20.046 42.540 18.367 0.50 16.57 ? 150 GLN A NE2 1 ATOM 524 N NE2 B GLN A 1 64 ? 16.848 45.842 16.078 0.50 16.24 ? 150 GLN A NE2 1 ATOM 525 N N . THR A 1 65 ? 15.082 40.685 17.237 1.00 5.83 ? 151 THR A N 1 ATOM 526 C CA . THR A 1 65 ? 14.423 39.979 16.154 1.00 6.86 ? 151 THR A CA 1 ATOM 527 C C . THR A 1 65 ? 12.898 40.137 16.205 1.00 7.08 ? 151 THR A C 1 ATOM 528 O O . THR A 1 65 ? 12.270 40.445 15.208 1.00 7.27 ? 151 THR A O 1 ATOM 529 C CB . THR A 1 65 ? 14.854 38.527 16.178 1.00 8.28 ? 151 THR A CB 1 ATOM 530 O OG1 . THR A 1 65 ? 16.223 38.491 15.721 1.00 11.16 ? 151 THR A OG1 1 ATOM 531 C CG2 . THR A 1 65 ? 14.005 37.704 15.188 1.00 9.84 ? 151 THR A CG2 1 ATOM 532 N N . LEU A 1 66 ? 12.309 39.942 17.373 1.00 6.36 ? 152 LEU A N 1 ATOM 533 C CA . LEU A 1 66 ? 10.873 40.099 17.529 1.00 6.77 ? 152 LEU A CA 1 ATOM 534 C C . LEU A 1 66 ? 10.458 41.544 17.188 1.00 7.44 ? 152 LEU A C 1 ATOM 535 O O . LEU A 1 66 ? 9.438 41.758 16.566 1.00 7.45 ? 152 LEU A O 1 ATOM 536 C CB . LEU A 1 66 ? 10.424 39.654 18.907 1.00 7.31 ? 152 LEU A CB 1 ATOM 537 C CG . LEU A 1 66 ? 10.648 38.165 19.209 1.00 6.79 ? 152 LEU A CG 1 ATOM 538 C CD1 . LEU A 1 66 ? 10.326 37.847 20.643 1.00 6.92 ? 152 LEU A CD1 1 ATOM 539 C CD2 . LEU A 1 66 ? 9.819 37.269 18.259 1.00 9.14 ? 152 LEU A CD2 1 ATOM 540 N N . SER A 1 67 ? 11.226 42.517 17.653 1.00 7.80 ? 153 SER A N 1 ATOM 541 C CA . SER A 1 67 ? 10.928 43.943 17.358 1.00 8.14 ? 153 SER A CA 1 ATOM 542 C C . SER A 1 67 ? 10.952 44.214 15.857 1.00 8.59 ? 153 SER A C 1 ATOM 543 O O . SER A 1 67 ? 10.083 44.916 15.323 1.00 8.66 ? 153 SER A O 1 ATOM 544 C CB . SER A 1 67 ? 11.949 44.849 18.018 1.00 9.95 ? 153 SER A CB 1 ATOM 545 O OG . SER A 1 67 ? 11.852 44.771 19.424 1.00 14.13 ? 153 SER A OG 1 ATOM 546 N N . GLU A 1 68 ? 11.937 43.649 15.162 1.00 6.91 ? 154 GLU A N 1 ATOM 547 C CA . GLU A 1 68 ? 12.105 43.845 13.734 1.00 8.18 ? 154 GLU A CA 1 ATOM 548 C C . GLU A 1 68 ? 10.957 43.169 13.005 1.00 8.16 ? 154 GLU A C 1 ATOM 549 O O . GLU A 1 68 ? 10.462 43.693 11.996 1.00 9.37 ? 154 GLU A O 1 ATOM 550 C CB . GLU A 1 68 ? 13.467 43.374 13.218 1.00 8.14 ? 154 GLU A CB 1 ATOM 551 C CG . GLU A 1 68 ? 14.567 44.253 13.778 1.00 9.17 ? 154 GLU A CG 1 ATOM 552 C CD . GLU A 1 68 ? 15.989 43.788 13.472 1.00 13.17 ? 154 GLU A CD 1 ATOM 553 O OE1 . GLU A 1 68 ? 16.132 42.681 12.934 1.00 12.59 ? 154 GLU A OE1 1 ATOM 554 O OE2 . GLU A 1 68 ? 16.975 44.547 13.743 1.00 16.76 ? 154 GLU A OE2 1 ATOM 555 N N . ILE A 1 69 ? 10.558 41.976 13.449 1.00 7.24 ? 155 ILE A N 1 ATOM 556 C CA . ILE A 1 69 ? 9.428 41.309 12.793 1.00 7.89 ? 155 ILE A CA 1 ATOM 557 C C . ILE A 1 69 ? 8.128 42.100 13.012 1.00 7.29 ? 155 ILE A C 1 ATOM 558 O O . ILE A 1 69 ? 7.341 42.280 12.078 1.00 8.00 ? 155 ILE A O 1 ATOM 559 C CB . ILE A 1 69 ? 9.251 39.853 13.291 1.00 7.63 ? 155 ILE A CB 1 ATOM 560 C CG1 . ILE A 1 69 ? 10.462 39.012 12.891 1.00 8.70 ? 155 ILE A CG1 1 ATOM 561 C CG2 . ILE A 1 69 ? 7.947 39.261 12.756 1.00 7.91 ? 155 ILE A CG2 1 ATOM 562 C CD1 . ILE A 1 69 ? 10.532 37.676 13.666 1.00 7.97 ? 155 ILE A CD1 1 ATOM 563 N N . ARG A 1 70 ? 7.890 42.581 14.212 1.00 7.79 ? 156 ARG A N 1 ATOM 564 C CA . ARG A 1 70 ? 6.720 43.401 14.457 1.00 8.07 ? 156 ARG A CA 1 ATOM 565 C C . ARG A 1 70 ? 6.718 44.590 13.530 1.00 8.67 ? 156 ARG A C 1 ATOM 566 O O . ARG A 1 70 ? 5.690 44.854 12.929 1.00 9.22 ? 156 ARG A O 1 ATOM 567 C CB . ARG A 1 70 ? 6.710 43.908 15.886 1.00 8.39 ? 156 ARG A CB 1 ATOM 568 C CG . ARG A 1 70 ? 5.604 44.911 16.193 1.00 8.35 ? 156 ARG A CG 1 ATOM 569 C CD . ARG A 1 70 ? 5.637 45.397 17.608 1.00 10.63 ? 156 ARG A CD 1 ATOM 570 N NE . ARG A 1 70 ? 5.061 44.429 18.521 1.00 8.56 ? 156 ARG A NE 1 ATOM 571 C CZ . ARG A 1 70 ? 5.176 44.484 19.831 1.00 10.64 ? 156 ARG A CZ 1 ATOM 572 N NH1 . ARG A 1 70 ? 5.906 45.438 20.413 1.00 12.16 ? 156 ARG A NH1 1 ATOM 573 N NH2 . ARG A 1 70 ? 4.536 43.589 20.561 1.00 9.64 ? 156 ARG A NH2 1 ATOM 574 N N . GLU A 1 71 ? 7.849 45.254 13.404 1.00 7.07 ? 157 GLU A N 1 ATOM 575 C CA . GLU A 1 71 ? 7.947 46.440 12.507 1.00 9.13 ? 157 GLU A CA 1 ATOM 576 C C . GLU A 1 71 ? 7.581 46.032 11.076 1.00 9.70 ? 157 GLU A C 1 ATOM 577 O O . GLU A 1 71 ? 6.799 46.710 10.390 1.00 10.87 ? 157 GLU A O 1 ATOM 578 C CB . GLU A 1 71 ? 9.333 47.057 12.593 1.00 10.59 ? 157 GLU A CB 1 ATOM 579 C CG . GLU A 1 71 ? 9.597 48.181 11.599 1.00 13.05 ? 157 GLU A CG 1 ATOM 580 C CD . GLU A 1 71 ? 11.016 48.670 11.696 1.00 19.66 ? 157 GLU A CD 1 ATOM 581 O OE1 . GLU A 1 71 ? 11.919 47.848 11.506 1.00 20.88 ? 157 GLU A OE1 1 ATOM 582 O OE2 . GLU A 1 71 ? 11.237 49.857 11.983 1.00 25.63 ? 157 GLU A OE2 1 ATOM 583 N N . ALA A 1 72 ? 8.117 44.910 10.593 1.00 10.06 ? 158 ALA A N 1 ATOM 584 C CA . ALA A 1 72 ? 7.850 44.473 9.223 1.00 10.15 ? 158 ALA A CA 1 ATOM 585 C C . ALA A 1 72 ? 6.384 44.131 8.970 1.00 10.29 ? 158 ALA A C 1 ATOM 586 O O . ALA A 1 72 ? 5.799 44.417 7.903 1.00 10.84 ? 158 ALA A O 1 ATOM 587 C CB . ALA A 1 72 ? 8.762 43.292 8.864 1.00 9.77 ? 158 ALA A CB 1 ATOM 588 N N . ASN A 1 73 ? 5.794 43.489 9.966 1.00 9.53 ? 159 ASN A N 1 ATOM 589 C CA . ASN A 1 73 ? 4.391 43.103 9.929 1.00 9.09 ? 159 ASN A CA 1 ATOM 590 C C . ASN A 1 73 ? 3.470 44.330 9.958 1.00 10.83 ? 159 ASN A C 1 ATOM 591 O O . ASN A 1 73 ? 2.494 44.408 9.204 1.00 11.41 ? 159 ASN A O 1 ATOM 592 C CB . ASN A 1 73 ? 4.028 42.120 11.041 1.00 9.06 ? 159 ASN A CB 1 ATOM 593 C CG . ASN A 1 73 ? 4.601 40.727 10.776 1.00 9.99 ? 159 ASN A CG 1 ATOM 594 O OD1 . ASN A 1 73 ? 5.075 40.457 9.687 1.00 10.53 ? 159 ASN A OD1 1 ATOM 595 N ND2 . ASN A 1 73 ? 4.593 39.865 11.803 1.00 10.29 ? 159 ASN A ND2 1 ATOM 596 N N . GLN A 1 74 ? 3.838 45.296 10.766 1.00 10.79 ? 160 GLN A N 1 ATOM 597 C CA . GLN A 1 74 ? 3.034 46.524 10.873 1.00 12.53 ? 160 GLN A CA 1 ATOM 598 C C . GLN A 1 74 ? 3.225 47.370 9.609 1.00 13.27 ? 160 GLN A C 1 ATOM 599 O O . GLN A 1 74 ? 2.356 48.199 9.287 1.00 15.64 ? 160 GLN A O 1 ATOM 600 C CB . GLN A 1 74 ? 3.425 47.316 12.098 1.00 12.14 ? 160 GLN A CB 1 ATOM 601 C CG . GLN A 1 74 ? 2.885 46.665 13.394 1.00 13.49 ? 160 GLN A CG 1 ATOM 602 C CD . GLN A 1 74 ? 3.248 47.394 14.673 1.00 13.06 ? 160 GLN A CD 1 ATOM 603 O OE1 . GLN A 1 74 ? 2.706 47.049 15.749 1.00 16.73 ? 160 GLN A OE1 1 ATOM 604 N NE2 . GLN A 1 74 ? 4.139 48.338 14.606 1.00 13.47 ? 160 GLN A NE2 1 ATOM 605 N N . ALA A 1 75 ? 4.341 47.167 8.912 1.00 13.47 ? 161 ALA A N 1 ATOM 606 C CA . ALA A 1 75 ? 4.633 47.795 7.584 1.00 14.64 ? 161 ALA A CA 1 ATOM 607 C C . ALA A 1 75 ? 4.065 47.020 6.403 1.00 14.79 ? 161 ALA A C 1 ATOM 608 O O . ALA A 1 75 ? 4.405 47.329 5.261 1.00 17.02 ? 161 ALA A O 1 ATOM 609 C CB . ALA A 1 75 ? 6.085 47.985 7.367 1.00 15.13 ? 161 ALA A CB 1 ATOM 610 N N . GLY A 1 76 ? 3.228 46.043 6.673 1.00 15.52 ? 162 GLY A N 1 ATOM 611 C CA . GLY A 1 76 ? 2.377 45.374 5.699 1.00 16.03 ? 162 GLY A CA 1 ATOM 612 C C . GLY A 1 76 ? 2.824 44.056 5.093 1.00 16.07 ? 162 GLY A C 1 ATOM 613 O O . GLY A 1 76 ? 2.312 43.628 4.044 1.00 17.10 ? 162 GLY A O 1 ATOM 614 N N . ALA A 1 77 ? 3.789 43.400 5.728 1.00 15.58 ? 163 ALA A N 1 ATOM 615 C CA . ALA A 1 77 ? 4.212 42.073 5.267 1.00 15.49 ? 163 ALA A CA 1 ATOM 616 C C . ALA A 1 77 ? 3.015 41.171 5.062 1.00 15.94 ? 163 ALA A C 1 ATOM 617 O O . ALA A 1 77 ? 2.138 41.061 5.886 1.00 16.71 ? 163 ALA A O 1 ATOM 618 C CB . ALA A 1 77 ? 5.190 41.431 6.231 1.00 15.41 ? 163 ALA A CB 1 ATOM 619 N N . ASN A 1 78 ? 2.983 40.504 3.913 1.00 17.68 ? 164 ASN A N 1 ATOM 620 C CA . ASN A 1 78 ? 1.838 39.653 3.615 1.00 18.39 ? 164 ASN A CA 1 ATOM 621 C C . ASN A 1 78 ? 2.245 38.427 2.835 1.00 18.26 ? 164 ASN A C 1 ATOM 622 O O . ASN A 1 78 ? 2.739 38.584 1.726 1.00 19.59 ? 164 ASN A O 1 ATOM 623 C CB . ASN A 1 78 ? 0.819 40.453 2.791 1.00 20.14 ? 164 ASN A CB 1 ATOM 624 C CG . ASN A 1 78 ? -0.379 39.645 2.452 1.00 24.61 ? 164 ASN A CG 1 ATOM 625 O OD1 . ASN A 1 78 ? -0.826 38.785 3.234 1.00 26.21 ? 164 ASN A OD1 1 ATOM 626 N ND2 . ASN A 1 78 ? -0.945 39.918 1.287 1.00 30.01 ? 164 ASN A ND2 1 ATOM 627 N N . PRO A 1 79 ? 2.143 37.221 3.403 1.00 17.59 ? 165 PRO A N 1 ATOM 628 C CA . PRO A 1 79 ? 1.658 36.984 4.756 1.00 15.76 ? 165 PRO A CA 1 ATOM 629 C C . PRO A 1 79 ? 2.645 37.524 5.800 1.00 13.39 ? 165 PRO A C 1 ATOM 630 O O . PRO A 1 79 ? 3.779 37.861 5.512 1.00 13.26 ? 165 PRO A O 1 ATOM 631 C CB . PRO A 1 79 ? 1.564 35.435 4.882 1.00 16.48 ? 165 PRO A CB 1 ATOM 632 C CG . PRO A 1 79 ? 2.080 34.846 3.672 1.00 18.90 ? 165 PRO A CG 1 ATOM 633 C CD . PRO A 1 79 ? 2.514 35.971 2.726 1.00 18.11 ? 165 PRO A CD 1 ATOM 634 N N . GLN A 1 80 ? 2.136 37.626 6.999 1.00 12.25 ? 166 GLN A N 1 ATOM 635 C CA . GLN A 1 80 ? 2.936 38.124 8.115 1.00 11.71 ? 166 GLN A CA 1 ATOM 636 C C . GLN A 1 80 ? 4.112 37.185 8.393 1.00 10.04 ? 166 GLN A C 1 ATOM 637 O O . GLN A 1 80 ? 4.021 35.982 8.141 1.00 10.01 ? 166 GLN A O 1 ATOM 638 C CB . GLN A 1 80 ? 2.071 38.279 9.339 1.00 12.53 ? 166 GLN A CB 1 ATOM 639 C CG . GLN A 1 80 ? 0.926 39.298 9.126 1.00 16.85 ? 166 GLN A CG 1 ATOM 640 C CD . GLN A 1 80 ? 0.710 40.135 10.358 1.00 21.05 ? 166 GLN A CD 1 ATOM 641 O OE1 . GLN A 1 80 ? 0.377 39.626 11.473 1.00 26.48 ? 166 GLN A OE1 1 ATOM 642 N NE2 . GLN A 1 80 ? 0.899 41.408 10.198 1.00 25.85 ? 166 GLN A NE2 1 ATOM 643 N N . TYR A 1 81 ? 5.176 37.763 8.945 1.00 8.69 ? 167 TYR A N 1 ATOM 644 C CA . TYR A 1 81 ? 6.372 37.029 9.310 1.00 7.46 ? 167 TYR A CA 1 ATOM 645 C C . TYR A 1 81 ? 6.204 36.345 10.655 1.00 7.44 ? 167 TYR A C 1 ATOM 646 O O . TYR A 1 81 ? 5.614 36.912 11.597 1.00 7.58 ? 167 TYR A O 1 ATOM 647 C CB . TYR A 1 81 ? 7.525 38.002 9.371 1.00 7.98 ? 167 TYR A CB 1 ATOM 648 C CG . TYR A 1 81 ? 8.045 38.372 8.017 1.00 9.96 ? 167 TYR A CG 1 ATOM 649 C CD1 . TYR A 1 81 ? 8.697 37.448 7.249 1.00 9.23 ? 167 TYR A CD1 1 ATOM 650 C CD2 . TYR A 1 81 ? 7.906 39.664 7.538 1.00 11.03 ? 167 TYR A CD2 1 ATOM 651 C CE1 . TYR A 1 81 ? 9.217 37.779 6.011 1.00 12.23 ? 167 TYR A CE1 1 ATOM 652 C CE2 . TYR A 1 81 ? 8.453 40.033 6.312 1.00 12.95 ? 167 TYR A CE2 1 ATOM 653 C CZ . TYR A 1 81 ? 9.079 39.082 5.546 1.00 14.58 ? 167 TYR A CZ 1 ATOM 654 O OH . TYR A 1 81 ? 9.612 39.446 4.299 1.00 19.61 ? 167 TYR A OH 1 ATOM 655 N N . ALA A 1 82 ? 6.828 35.164 10.769 1.00 7.51 ? 168 ALA A N 1 ATOM 656 C CA . ALA A 1 82 ? 6.983 34.422 12.016 1.00 6.69 ? 168 ALA A CA 1 ATOM 657 C C . ALA A 1 82 ? 8.448 34.259 12.371 1.00 6.30 ? 168 ALA A C 1 ATOM 658 O O . ALA A 1 82 ? 9.303 34.205 11.492 1.00 6.21 ? 168 ALA A O 1 ATOM 659 C CB . ALA A 1 82 ? 6.359 33.044 11.899 1.00 7.37 ? 168 ALA A CB 1 ATOM 660 N N . ALA A 1 83 ? 8.704 34.122 13.666 1.00 6.22 ? 169 ALA A N 1 ATOM 661 C CA . ALA A 1 83 ? 10.037 33.897 14.200 1.00 6.22 ? 169 ALA A CA 1 ATOM 662 C C . ALA A 1 83 ? 10.320 32.407 14.401 1.00 5.20 ? 169 ALA A C 1 ATOM 663 O O . ALA A 1 83 ? 9.445 31.621 14.648 1.00 5.45 ? 169 ALA A O 1 ATOM 664 C CB . ALA A 1 83 ? 10.167 34.600 15.520 1.00 6.49 ? 169 ALA A CB 1 ATOM 665 N N . GLN A 1 84 ? 11.610 32.100 14.267 1.00 5.57 ? 170 GLN A N 1 ATOM 666 C CA . GLN A 1 84 ? 12.163 30.733 14.456 1.00 5.08 ? 170 GLN A CA 1 ATOM 667 C C . GLN A 1 84 ? 13.331 30.813 15.419 1.00 5.05 ? 170 GLN A C 1 ATOM 668 O O . GLN A 1 84 ? 14.356 31.434 15.085 1.00 5.28 ? 170 GLN A O 1 ATOM 669 C CB . GLN A 1 84 ? 12.666 30.159 13.116 1.00 5.63 ? 170 GLN A CB 1 ATOM 670 C CG . GLN A 1 84 ? 11.554 29.830 12.086 1.00 6.43 ? 170 GLN A CG 1 ATOM 671 C CD . GLN A 1 84 ? 12.162 29.387 10.779 1.00 8.32 ? 170 GLN A CD 1 ATOM 672 O OE1 . GLN A 1 84 ? 12.093 28.190 10.389 1.00 8.44 ? 170 GLN A OE1 1 ATOM 673 N NE2 . GLN A 1 84 ? 12.759 30.363 10.052 1.00 8.31 ? 170 GLN A NE2 1 ATOM 674 N N . ILE A 1 85 ? 13.150 30.258 16.600 1.00 4.13 ? 171 ILE A N 1 ATOM 675 C CA . ILE A 1 85 ? 14.111 30.378 17.689 1.00 4.33 ? 171 ILE A CA 1 ATOM 676 C C . ILE A 1 85 ? 14.468 29.006 18.268 1.00 4.90 ? 171 ILE A C 1 ATOM 677 O O . ILE A 1 85 ? 13.616 28.147 18.460 1.00 4.77 ? 171 ILE A O 1 ATOM 678 C CB . ILE A 1 85 ? 13.518 31.284 18.810 1.00 5.30 ? 171 ILE A CB 1 ATOM 679 C CG1 . ILE A 1 85 ? 13.112 32.676 18.273 1.00 7.03 ? 171 ILE A CG1 1 ATOM 680 C CG2 . ILE A 1 85 ? 14.433 31.389 20.019 1.00 6.58 ? 171 ILE A CG2 1 ATOM 681 C CD1 . ILE A 1 85 ? 14.279 33.541 17.846 1.00 10.42 ? 171 ILE A CD1 1 ATOM 682 N N . VAL A 1 86 ? 15.727 28.834 18.606 1.00 3.74 ? 172 VAL A N 1 ATOM 683 C CA . VAL A 1 86 ? 16.216 27.650 19.356 1.00 4.19 ? 172 VAL A CA 1 ATOM 684 C C . VAL A 1 86 ? 16.522 27.987 20.807 1.00 5.13 ? 172 VAL A C 1 ATOM 685 O O . VAL A 1 86 ? 17.242 28.948 21.086 1.00 4.74 ? 172 VAL A O 1 ATOM 686 C CB . VAL A 1 86 ? 17.490 27.023 18.714 1.00 4.31 ? 172 VAL A CB 1 ATOM 687 C CG1 . VAL A 1 86 ? 17.831 25.705 19.411 1.00 4.99 ? 172 VAL A CG1 1 ATOM 688 C CG2 . VAL A 1 86 ? 17.317 26.845 17.260 1.00 5.71 ? 172 VAL A CG2 1 ATOM 689 N N . VAL A 1 87 ? 15.971 27.226 21.724 1.00 4.59 ? 173 VAL A N 1 ATOM 690 C CA . VAL A 1 87 ? 16.281 27.301 23.155 1.00 4.43 ? 173 VAL A CA 1 ATOM 691 C C . VAL A 1 87 ? 17.348 26.238 23.418 1.00 4.40 ? 173 VAL A C 1 ATOM 692 O O . VAL A 1 87 ? 17.129 25.041 23.236 1.00 4.65 ? 173 VAL A O 1 ATOM 693 C CB . VAL A 1 87 ? 15.023 27.037 23.971 1.00 4.71 ? 173 VAL A CB 1 ATOM 694 C CG1 . VAL A 1 87 ? 15.298 27.112 25.474 1.00 5.58 ? 173 VAL A CG1 1 ATOM 695 C CG2 . VAL A 1 87 ? 13.916 28.003 23.603 1.00 5.67 ? 173 VAL A CG2 1 ATOM 696 N N . TYR A 1 88 ? 18.519 26.705 23.852 1.00 4.54 ? 174 TYR A N 1 ATOM 697 C CA . TYR A 1 88 ? 19.698 25.834 23.931 1.00 4.45 ? 174 TYR A CA 1 ATOM 698 C C . TYR A 1 88 ? 20.638 26.286 25.062 1.00 5.14 ? 174 TYR A C 1 ATOM 699 O O . TYR A 1 88 ? 21.750 26.752 24.801 1.00 5.94 ? 174 TYR A O 1 ATOM 700 C CB . TYR A 1 88 ? 20.416 25.853 22.574 1.00 4.56 ? 174 TYR A CB 1 ATOM 701 C CG . TYR A 1 88 ? 21.572 24.874 22.486 1.00 4.95 ? 174 TYR A CG 1 ATOM 702 C CD1 . TYR A 1 88 ? 21.450 23.612 23.011 1.00 5.65 ? 174 TYR A CD1 1 ATOM 703 C CD2 . TYR A 1 88 ? 22.734 25.218 21.823 1.00 6.33 ? 174 TYR A CD2 1 ATOM 704 C CE1 . TYR A 1 88 ? 22.477 22.698 22.924 1.00 5.72 ? 174 TYR A CE1 1 ATOM 705 C CE2 . TYR A 1 88 ? 23.769 24.298 21.678 1.00 6.89 ? 174 TYR A CE2 1 ATOM 706 C CZ . TYR A 1 88 ? 23.636 23.031 22.234 1.00 4.97 ? 174 TYR A CZ 1 ATOM 707 O OH . TYR A 1 88 ? 24.710 22.151 22.109 1.00 7.61 ? 174 TYR A OH 1 ATOM 708 N N . ASP A 1 89 ? 20.226 26.111 26.319 1.00 5.18 ? 175 ASP A N 1 ATOM 709 C CA . ASP A 1 89 ? 21.100 26.498 27.424 1.00 4.68 ? 175 ASP A CA 1 ATOM 710 C C . ASP A 1 89 ? 20.883 25.700 28.697 1.00 4.78 ? 175 ASP A C 1 ATOM 711 O O . ASP A 1 89 ? 21.118 26.182 29.792 1.00 5.02 ? 175 ASP A O 1 ATOM 712 C CB . ASP A 1 89 ? 20.941 28.006 27.710 1.00 5.38 ? 175 ASP A CB 1 ATOM 713 C CG . ASP A 1 89 ? 22.182 28.630 28.277 1.00 7.17 ? 175 ASP A CG 1 ATOM 714 O OD1 . ASP A 1 89 ? 23.273 27.982 28.327 1.00 5.43 ? 175 ASP A OD1 1 ATOM 715 O OD2 . ASP A 1 89 ? 22.159 29.838 28.654 1.00 5.94 ? 175 ASP A OD2 1 ATOM 716 N N . LEU A 1 90 ? 20.527 24.422 28.571 1.00 4.92 ? 176 LEU A N 1 ATOM 717 C CA . LEU A 1 90 ? 20.416 23.573 29.760 1.00 5.10 ? 176 LEU A CA 1 ATOM 718 C C . LEU A 1 90 ? 21.731 23.573 30.554 1.00 5.18 ? 176 LEU A C 1 ATOM 719 O O . LEU A 1 90 ? 22.789 23.589 29.965 1.00 5.85 ? 176 LEU A O 1 ATOM 720 C CB . LEU A 1 90 ? 20.080 22.131 29.417 1.00 5.42 ? 176 LEU A CB 1 ATOM 721 C CG . LEU A 1 90 ? 18.579 21.855 29.126 1.00 5.49 ? 176 LEU A CG 1 ATOM 722 C CD1 . LEU A 1 90 ? 18.418 20.503 28.424 1.00 5.73 ? 176 LEU A CD1 1 ATOM 723 C CD2 . LEU A 1 90 ? 17.704 21.912 30.392 1.00 5.14 ? 176 LEU A CD2 1 ATOM 724 N N . PRO A 1 91 ? 21.665 23.495 31.871 1.00 5.15 ? 177 PRO A N 1 ATOM 725 C CA . PRO A 1 91 ? 22.877 23.318 32.673 1.00 4.94 ? 177 PRO A CA 1 ATOM 726 C C . PRO A 1 91 ? 23.416 21.906 32.471 1.00 4.41 ? 177 PRO A C 1 ATOM 727 O O . PRO A 1 91 ? 22.678 20.962 32.227 1.00 5.30 ? 177 PRO A O 1 ATOM 728 C CB . PRO A 1 91 ? 22.385 23.568 34.112 1.00 5.46 ? 177 PRO A CB 1 ATOM 729 C CG . PRO A 1 91 ? 20.967 23.012 34.104 1.00 6.58 ? 177 PRO A CG 1 ATOM 730 C CD . PRO A 1 91 ? 20.442 23.406 32.699 1.00 5.30 ? 177 PRO A CD 1 ATOM 731 N N . ASP A 1 92 ? 24.728 21.748 32.623 1.00 5.03 ? 178 ASP A N 1 ATOM 732 C CA . ASP A 1 92 ? 25.415 20.507 32.270 1.00 5.79 ? 178 ASP A CA 1 ATOM 733 C C . ASP A 1 92 ? 25.014 20.078 30.833 1.00 5.97 ? 178 ASP A C 1 ATOM 734 O O . ASP A 1 92 ? 24.787 18.893 30.542 1.00 5.89 ? 178 ASP A O 1 ATOM 735 C CB . ASP A 1 92 ? 25.126 19.381 33.276 1.00 7.01 ? 178 ASP A CB 1 ATOM 736 C CG . ASP A 1 92 ? 25.955 19.470 34.539 1.00 8.74 ? 178 ASP A CG 1 ATOM 737 O OD1 . ASP A 1 92 ? 26.368 20.569 34.997 1.00 8.31 ? 178 ASP A OD1 1 ATOM 738 O OD2 . ASP A 1 92 ? 26.173 18.408 35.178 1.00 12.36 ? 178 ASP A OD2 1 ATOM 739 N N . ARG A 1 93 ? 24.977 21.075 29.949 1.00 6.05 ? 179 ARG A N 1 ATOM 740 C CA . ARG A 1 93 ? 24.625 20.911 28.527 1.00 5.59 ? 179 ARG A CA 1 ATOM 741 C C . ARG A 1 93 ? 25.512 19.875 27.848 1.00 5.33 ? 179 ARG A C 1 ATOM 742 O O . ARG A 1 93 ? 26.725 19.776 28.170 1.00 6.40 ? 179 ARG A O 1 ATOM 743 C CB . ARG A 1 93 ? 24.711 22.227 27.784 1.00 5.47 ? 179 ARG A CB 1 ATOM 744 C CG . ARG A 1 93 ? 23.661 22.406 26.738 1.00 6.99 ? 179 ARG A CG 1 ATOM 745 C CD . ARG A 1 93 ? 23.700 23.771 26.056 1.00 6.57 ? 179 ARG A CD 1 ATOM 746 N NE . ARG A 1 93 ? 24.896 23.921 25.210 1.00 5.25 ? 179 ARG A NE 1 ATOM 747 C CZ . ARG A 1 93 ? 25.270 25.045 24.626 1.00 6.63 ? 179 ARG A CZ 1 ATOM 748 N NH1 . ARG A 1 93 ? 24.607 26.163 24.804 1.00 6.19 ? 179 ARG A NH1 1 ATOM 749 N NH2 . ARG A 1 93 ? 26.363 25.066 23.882 1.00 9.01 ? 179 ARG A NH2 1 ATOM 750 N N . ASP A 1 94 ? 24.945 19.151 26.918 1.00 5.80 ? 180 ASP A N 1 ATOM 751 C CA . ASP A 1 94 ? 25.716 18.249 26.046 1.00 5.81 ? 180 ASP A CA 1 ATOM 752 C C . ASP A 1 94 ? 26.463 17.232 26.880 1.00 6.58 ? 180 ASP A C 1 ATOM 753 O O . ASP A 1 94 ? 27.657 17.037 26.731 1.00 6.84 ? 180 ASP A O 1 ATOM 754 C CB . ASP A 1 94 ? 26.688 19.021 25.127 1.00 6.88 ? 180 ASP A CB 1 ATOM 755 C CG . ASP A 1 94 ? 26.026 20.196 24.445 1.00 6.71 ? 180 ASP A CG 1 ATOM 756 O OD1 . ASP A 1 94 ? 25.157 19.958 23.549 1.00 7.85 ? 180 ASP A OD1 1 ATOM 757 O OD2 . ASP A 1 94 ? 26.373 21.365 24.778 1.00 8.48 ? 180 ASP A OD2 1 ATOM 758 N N . CYS A 1 95 ? 25.727 16.521 27.715 1.00 6.01 ? 181 CYS A N 1 ATOM 759 C CA . CYS A 1 95 ? 26.339 15.685 28.744 1.00 6.84 ? 181 CYS A CA 1 ATOM 760 C C . CYS A 1 95 ? 27.271 14.596 28.250 1.00 6.46 ? 181 CYS A C 1 ATOM 761 O O . CYS A 1 95 ? 28.152 14.192 28.993 1.00 7.18 ? 181 CYS A O 1 ATOM 762 C CB . CYS A 1 95 ? 25.239 15.050 29.620 1.00 7.94 ? 181 CYS A CB 1 ATOM 763 S SG . CYS A 1 95 ? 24.050 14.018 28.770 1.00 9.29 ? 181 CYS A SG 1 ATOM 764 N N . ALA A 1 96 ? 27.074 14.102 27.033 1.00 5.99 ? 182 ALA A N 1 ATOM 765 C CA . ALA A 1 96 ? 27.903 13.007 26.495 1.00 7.55 ? 182 ALA A CA 1 ATOM 766 C C . ALA A 1 96 ? 29.019 13.477 25.564 1.00 8.13 ? 182 ALA A C 1 ATOM 767 O O . ALA A 1 96 ? 29.779 12.634 25.053 1.00 9.96 ? 182 ALA A O 1 ATOM 768 C CB . ALA A 1 96 ? 27.048 11.949 25.750 1.00 7.34 ? 182 ALA A CB 1 ATOM 769 N N . ALA A 1 97 ? 29.099 14.763 25.314 1.00 8.44 ? 183 ALA A N 1 ATOM 770 C CA . ALA A 1 97 ? 30.072 15.322 24.367 1.00 7.79 ? 183 ALA A CA 1 ATOM 771 C C . ALA A 1 97 ? 31.458 15.301 24.978 1.00 8.51 ? 183 ALA A C 1 ATOM 772 O O . ALA A 1 97 ? 31.645 15.361 26.183 1.00 10.18 ? 183 ALA A O 1 ATOM 773 C CB . ALA A 1 97 ? 29.650 16.760 23.968 1.00 8.16 ? 183 ALA A CB 1 ATOM 774 N N . ALA A 1 98 ? 32.451 15.308 24.102 1.00 8.50 ? 184 ALA A N 1 ATOM 775 C CA . ALA A 1 98 ? 33.840 15.412 24.482 1.00 8.85 ? 184 ALA A CA 1 ATOM 776 C C . ALA A 1 98 ? 34.142 16.729 25.143 1.00 9.11 ? 184 ALA A C 1 ATOM 777 O O . ALA A 1 98 ? 34.983 16.826 26.033 1.00 11.96 ? 184 ALA A O 1 ATOM 778 C CB . ALA A 1 98 ? 34.722 15.234 23.268 1.00 9.23 ? 184 ALA A CB 1 ATOM 779 N N . ALA A 1 99 ? 33.406 17.763 24.723 1.00 9.92 ? 185 ALA A N 1 ATOM 780 C CA . ALA A 1 99 ? 33.529 19.117 25.252 1.00 10.43 ? 185 ALA A CA 1 ATOM 781 C C . ALA A 1 99 ? 32.195 19.784 25.029 1.00 10.83 ? 185 ALA A C 1 ATOM 782 O O . ALA A 1 99 ? 31.437 19.405 24.129 1.00 12.71 ? 185 ALA A O 1 ATOM 783 C CB . ALA A 1 99 ? 34.617 19.876 24.527 1.00 10.60 ? 185 ALA A CB 1 ATOM 784 N N . SER A 1 100 ? 31.884 20.756 25.873 1.00 10.17 ? 186 SER A N 1 ATOM 785 C CA . SER A 1 100 ? 30.663 21.538 25.704 1.00 9.41 ? 186 SER A CA 1 ATOM 786 C C . SER A 1 100 ? 30.949 22.996 25.866 1.00 9.62 ? 186 SER A C 1 ATOM 787 O O . SER A 1 100 ? 31.786 23.364 26.690 1.00 10.70 ? 186 SER A O 1 ATOM 788 C CB . SER A 1 100 ? 29.653 21.144 26.764 1.00 8.69 ? 186 SER A CB 1 ATOM 789 O OG . SER A 1 100 ? 28.469 21.963 26.663 1.00 9.08 ? 186 SER A OG 1 ATOM 790 N N . ASN A 1 101 ? 30.270 23.819 25.054 1.00 9.39 ? 187 ASN A N 1 ATOM 791 C CA . ASN A 1 101 ? 30.292 25.262 25.161 1.00 10.31 ? 187 ASN A CA 1 ATOM 792 C C . ASN A 1 101 ? 29.174 25.798 26.073 1.00 9.64 ? 187 ASN A C 1 ATOM 793 O O . ASN A 1 101 ? 29.036 27.000 26.205 1.00 11.74 ? 187 ASN A O 1 ATOM 794 C CB . ASN A 1 101 ? 30.246 25.877 23.768 1.00 12.50 ? 187 ASN A CB 1 ATOM 795 C CG . ASN A 1 101 ? 31.358 25.323 22.870 1.00 15.79 ? 187 ASN A CG 1 ATOM 796 O OD1 . ASN A 1 101 ? 31.112 24.747 21.800 1.00 19.90 ? 187 ASN A OD1 1 ATOM 797 N ND2 . ASN A 1 101 ? 32.564 25.475 23.334 1.00 19.32 ? 187 ASN A ND2 1 ATOM 798 N N . GLY A 1 102 ? 28.386 24.913 26.697 1.00 8.86 ? 188 GLY A N 1 ATOM 799 C CA . GLY A 1 102 ? 27.344 25.351 27.618 1.00 7.89 ? 188 GLY A CA 1 ATOM 800 C C . GLY A 1 102 ? 27.913 26.137 28.792 1.00 7.04 ? 188 GLY A C 1 ATOM 801 O O . GLY A 1 102 ? 28.887 25.767 29.438 1.00 9.11 ? 188 GLY A O 1 ATOM 802 N N . GLU A 1 103 ? 27.272 27.242 29.122 1.00 6.47 ? 189 GLU A N 1 ATOM 803 C CA . GLU A 1 103 ? 27.806 28.144 30.146 1.00 6.45 ? 189 GLU A CA 1 ATOM 804 C C . GLU A 1 103 ? 27.476 27.797 31.582 1.00 5.96 ? 189 GLU A C 1 ATOM 805 O O . GLU A 1 103 ? 28.179 28.290 32.475 1.00 8.33 ? 189 GLU A O 1 ATOM 806 C CB . GLU A 1 103 ? 27.408 29.586 29.877 1.00 6.63 ? 189 GLU A CB 1 ATOM 807 C CG . GLU A 1 103 ? 25.911 29.829 29.996 1.00 6.06 ? 189 GLU A CG 1 ATOM 808 C CD . GLU A 1 103 ? 25.459 31.163 29.481 1.00 8.63 ? 189 GLU A CD 1 ATOM 809 O OE1 . GLU A 1 103 ? 26.279 32.121 29.327 1.00 12.08 ? 189 GLU A OE1 1 ATOM 810 O OE2 . GLU A 1 103 ? 24.226 31.261 29.209 1.00 7.08 ? 189 GLU A OE2 1 ATOM 811 N N . TRP A 1 104 ? 26.452 26.972 31.823 1.00 6.28 ? 190 TRP A N 1 ATOM 812 C CA . TRP A 1 104 ? 25.960 26.726 33.154 1.00 6.66 ? 190 TRP A CA 1 ATOM 813 C C . TRP A 1 104 ? 26.153 25.298 33.624 1.00 6.72 ? 190 TRP A C 1 ATOM 814 O O . TRP A 1 104 ? 26.084 24.352 32.843 1.00 7.64 ? 190 TRP A O 1 ATOM 815 C CB . TRP A 1 104 ? 24.478 27.088 33.271 1.00 6.68 ? 190 TRP A CB 1 ATOM 816 C CG . TRP A 1 104 ? 24.230 28.562 33.186 1.00 6.74 ? 190 TRP A CG 1 ATOM 817 C CD1 . TRP A 1 104 ? 25.066 29.555 33.601 1.00 7.36 ? 190 TRP A CD1 1 ATOM 818 C CD2 . TRP A 1 104 ? 23.049 29.207 32.720 1.00 6.49 ? 190 TRP A CD2 1 ATOM 819 N NE1 . TRP A 1 104 ? 24.503 30.785 33.360 1.00 6.64 ? 190 TRP A NE1 1 ATOM 820 C CE2 . TRP A 1 104 ? 23.251 30.585 32.830 1.00 6.47 ? 190 TRP A CE2 1 ATOM 821 C CE3 . TRP A 1 104 ? 21.852 28.751 32.167 1.00 5.80 ? 190 TRP A CE3 1 ATOM 822 C CZ2 . TRP A 1 104 ? 22.319 31.492 32.426 1.00 5.93 ? 190 TRP A CZ2 1 ATOM 823 C CZ3 . TRP A 1 104 ? 20.907 29.640 31.786 1.00 7.59 ? 190 TRP A CZ3 1 ATOM 824 C CH2 . TRP A 1 104 ? 21.141 31.017 31.921 1.00 6.84 ? 190 TRP A CH2 1 ATOM 825 N N . ALA A 1 105 ? 26.390 25.161 34.933 1.00 7.88 ? 191 ALA A N 1 ATOM 826 C CA . ALA A 1 105 ? 26.592 23.877 35.587 1.00 7.20 ? 191 ALA A CA 1 ATOM 827 C C . ALA A 1 105 ? 25.552 23.638 36.634 1.00 7.26 ? 191 ALA A C 1 ATOM 828 O O . ALA A 1 105 ? 25.257 24.527 37.419 1.00 7.82 ? 191 ALA A O 1 ATOM 829 C CB . ALA A 1 105 ? 27.958 23.829 36.260 1.00 9.13 ? 191 ALA A CB 1 ATOM 830 N N . ILE A 1 106 ? 25.046 22.405 36.725 1.00 6.70 ? 192 ILE A N 1 ATOM 831 C CA . ILE A 1 106 ? 24.105 22.033 37.798 1.00 8.08 ? 192 ILE A CA 1 ATOM 832 C C . ILE A 1 106 ? 24.728 22.353 39.166 1.00 9.43 ? 192 ILE A C 1 ATOM 833 O O . ILE A 1 106 ? 24.062 22.905 40.026 1.00 10.09 ? 192 ILE A O 1 ATOM 834 C CB . ILE A 1 106 ? 23.690 20.550 37.691 1.00 8.55 ? 192 ILE A CB 1 ATOM 835 C CG1 . ILE A 1 106 ? 22.910 20.349 36.373 1.00 8.50 ? 192 ILE A CG1 1 ATOM 836 C CG2 . ILE A 1 106 ? 22.838 20.122 38.884 1.00 10.28 ? 192 ILE A CG2 1 ATOM 837 C CD1 . ILE A 1 106 ? 22.551 18.895 36.046 1.00 8.84 ? 192 ILE A CD1 1 ATOM 838 N N . ALA A 1 107 ? 26.026 22.081 39.324 1.00 10.76 ? 193 ALA A N 1 ATOM 839 C CA . ALA A 1 107 ? 26.717 22.345 40.617 1.00 12.57 ? 193 ALA A CA 1 ATOM 840 C C . ALA A 1 107 ? 26.875 23.835 40.967 1.00 12.78 ? 193 ALA A C 1 ATOM 841 O O . ALA A 1 107 ? 27.221 24.163 42.098 1.00 13.53 ? 193 ALA A O 1 ATOM 842 C CB . ALA A 1 107 ? 28.088 21.727 40.614 1.00 13.59 ? 193 ALA A CB 1 ATOM 843 N N . ASN A 1 108 ? 26.680 24.735 40.000 1.00 12.59 ? 194 ASN A N 1 ATOM 844 C CA . ASN A 1 108 ? 26.901 26.188 40.181 1.00 11.85 ? 194 ASN A CA 1 ATOM 845 C C . ASN A 1 108 ? 25.598 26.963 39.867 1.00 10.15 ? 194 ASN A C 1 ATOM 846 O O . ASN A 1 108 ? 25.545 27.853 39.028 1.00 10.21 ? 194 ASN A O 1 ATOM 847 C CB A ASN A 1 108 ? 28.060 26.715 39.268 0.65 13.45 ? 194 ASN A CB 1 ATOM 848 C CB B ASN A 1 108 ? 28.062 26.732 39.356 0.35 12.70 ? 194 ASN A CB 1 ATOM 849 C CG A ASN A 1 108 ? 29.436 26.019 39.508 0.65 15.06 ? 194 ASN A CG 1 ATOM 850 C CG B ASN A 1 108 ? 28.607 28.032 39.933 0.35 13.78 ? 194 ASN A CG 1 ATOM 851 O OD1 A ASN A 1 108 ? 30.083 25.522 38.567 0.65 17.83 ? 194 ASN A OD1 1 ATOM 852 O OD1 B ASN A 1 108 ? 28.534 28.261 41.145 0.35 16.99 ? 194 ASN A OD1 1 ATOM 853 N ND2 A ASN A 1 108 ? 29.873 25.997 40.742 0.65 18.10 ? 194 ASN A ND2 1 ATOM 854 N ND2 B ASN A 1 108 ? 29.141 28.887 39.075 0.35 15.03 ? 194 ASN A ND2 1 ATOM 855 N N . ASN A 1 109 ? 24.524 26.561 40.533 1.00 9.21 ? 195 ASN A N 1 ATOM 856 C CA . ASN A 1 109 ? 23.232 27.249 40.447 1.00 8.90 ? 195 ASN A CA 1 ATOM 857 C C . ASN A 1 109 ? 22.554 27.163 39.066 1.00 7.92 ? 195 ASN A C 1 ATOM 858 O O . ASN A 1 109 ? 21.690 27.945 38.717 1.00 7.37 ? 195 ASN A O 1 ATOM 859 C CB . ASN A 1 109 ? 23.333 28.715 40.856 1.00 9.03 ? 195 ASN A CB 1 ATOM 860 C CG . ASN A 1 109 ? 22.051 29.226 41.486 1.00 11.77 ? 195 ASN A CG 1 ATOM 861 O OD1 . ASN A 1 109 ? 21.280 28.448 42.058 1.00 12.98 ? 195 ASN A OD1 1 ATOM 862 N ND2 . ASN A 1 109 ? 21.824 30.541 41.407 1.00 14.37 ? 195 ASN A ND2 1 ATOM 863 N N . GLY A 1 110 ? 22.908 26.146 38.300 1.00 7.45 ? 196 GLY A N 1 ATOM 864 C CA . GLY A 1 110 ? 22.438 26.044 36.919 1.00 6.42 ? 196 GLY A CA 1 ATOM 865 C C . GLY A 1 110 ? 20.946 25.843 36.776 1.00 6.68 ? 196 GLY A C 1 ATOM 866 O O . GLY A 1 110 ? 20.340 26.320 35.820 1.00 6.81 ? 196 GLY A O 1 ATOM 867 N N . VAL A 1 111 ? 20.344 25.075 37.686 1.00 6.62 ? 197 VAL A N 1 ATOM 868 C CA . VAL A 1 111 ? 18.882 24.882 37.676 1.00 7.38 ? 197 VAL A CA 1 ATOM 869 C C . VAL A 1 111 ? 18.155 26.215 37.819 1.00 6.51 ? 197 VAL A C 1 ATOM 870 O O . VAL A 1 111 ? 17.291 26.563 37.020 1.00 6.62 ? 197 VAL A O 1 ATOM 871 C CB . VAL A 1 111 ? 18.420 23.854 38.708 1.00 8.59 ? 197 VAL A CB 1 ATOM 872 C CG1 . VAL A 1 111 ? 16.887 23.917 38.850 1.00 11.07 ? 197 VAL A CG1 1 ATOM 873 C CG2 . VAL A 1 111 ? 18.902 22.462 38.304 1.00 9.21 ? 197 VAL A CG2 1 ATOM 874 N N . ASN A 1 112 ? 18.496 26.983 38.835 1.00 7.32 ? 198 ASN A N 1 ATOM 875 C CA . ASN A 1 112 ? 17.884 28.299 39.009 1.00 7.50 ? 198 ASN A CA 1 ATOM 876 C C . ASN A 1 112 ? 18.185 29.230 37.840 1.00 6.22 ? 198 ASN A C 1 ATOM 877 O O . ASN A 1 112 ? 17.341 29.992 37.370 1.00 6.43 ? 198 ASN A O 1 ATOM 878 C CB . ASN A 1 112 ? 18.308 28.945 40.344 1.00 9.14 ? 198 ASN A CB 1 ATOM 879 C CG . ASN A 1 112 ? 17.662 28.286 41.524 1.00 12.47 ? 198 ASN A CG 1 ATOM 880 O OD1 . ASN A 1 112 ? 16.557 27.713 41.409 1.00 16.79 ? 198 ASN A OD1 1 ATOM 881 N ND2 . ASN A 1 112 ? 18.349 28.331 42.669 1.00 16.93 ? 198 ASN A ND2 1 ATOM 882 N N . ASN A 1 113 ? 19.411 29.165 37.345 1.00 5.72 ? 199 ASN A N 1 ATOM 883 C CA . ASN A 1 113 ? 19.767 29.976 36.187 1.00 5.98 ? 199 ASN A CA 1 ATOM 884 C C . ASN A 1 113 ? 18.854 29.685 34.975 1.00 5.55 ? 199 ASN A C 1 ATOM 885 O O . ASN A 1 113 ? 18.374 30.616 34.292 1.00 5.66 ? 199 ASN A O 1 ATOM 886 C CB . ASN A 1 113 ? 21.214 29.770 35.771 1.00 5.87 ? 199 ASN A CB 1 ATOM 887 C CG . ASN A 1 113 ? 22.219 30.316 36.777 1.00 7.54 ? 199 ASN A CG 1 ATOM 888 O OD1 . ASN A 1 113 ? 21.854 31.032 37.711 1.00 8.93 ? 199 ASN A OD1 1 ATOM 889 N ND2 . ASN A 1 113 ? 23.502 30.006 36.554 1.00 8.82 ? 199 ASN A ND2 1 ATOM 890 N N . TYR A 1 114 ? 18.620 28.395 34.739 1.00 4.86 ? 200 TYR A N 1 ATOM 891 C CA . TYR A 1 114 ? 17.814 27.973 33.599 1.00 4.93 ? 200 TYR A CA 1 ATOM 892 C C . TYR A 1 114 ? 16.353 28.379 33.758 1.00 5.23 ? 200 TYR A C 1 ATOM 893 O O . TYR A 1 114 ? 15.703 28.841 32.804 1.00 4.63 ? 200 TYR A O 1 ATOM 894 C CB . TYR A 1 114 ? 17.905 26.471 33.394 1.00 5.32 ? 200 TYR A CB 1 ATOM 895 C CG . TYR A 1 114 ? 17.346 26.045 32.053 1.00 4.40 ? 200 TYR A CG 1 ATOM 896 C CD1 . TYR A 1 114 ? 18.042 26.217 30.872 1.00 4.48 ? 200 TYR A CD1 1 ATOM 897 C CD2 . TYR A 1 114 ? 16.073 25.527 31.982 1.00 6.60 ? 200 TYR A CD2 1 ATOM 898 C CE1 . TYR A 1 114 ? 17.487 25.838 29.640 1.00 5.42 ? 200 TYR A CE1 1 ATOM 899 C CE2 . TYR A 1 114 ? 15.541 25.127 30.793 1.00 5.61 ? 200 TYR A CE2 1 ATOM 900 C CZ . TYR A 1 114 ? 16.245 25.294 29.610 1.00 5.30 ? 200 TYR A CZ 1 ATOM 901 O OH . TYR A 1 114 ? 15.712 24.886 28.403 1.00 6.39 ? 200 TYR A OH 1 ATOM 902 N N . LYS A 1 115 ? 15.834 28.190 34.977 1.00 5.37 ? 201 LYS A N 1 ATOM 903 C CA . LYS A 1 115 ? 14.429 28.534 35.193 1.00 5.96 ? 201 LYS A CA 1 ATOM 904 C C . LYS A 1 115 ? 14.230 30.027 34.942 1.00 5.25 ? 201 LYS A C 1 ATOM 905 O O . LYS A 1 115 ? 13.243 30.430 34.335 1.00 5.83 ? 201 LYS A O 1 ATOM 906 C CB A LYS A 1 115 ? 13.924 28.153 36.580 0.55 7.01 ? 201 LYS A CB 1 ATOM 907 C CB B LYS A 1 115 ? 13.942 28.106 36.581 0.45 7.05 ? 201 LYS A CB 1 ATOM 908 C CG A LYS A 1 115 ? 13.806 26.661 36.757 0.55 7.83 ? 201 LYS A CG 1 ATOM 909 C CG B LYS A 1 115 ? 13.889 26.585 36.730 0.45 8.25 ? 201 LYS A CG 1 ATOM 910 C CD A LYS A 1 115 ? 13.125 26.330 38.048 0.55 10.43 ? 201 LYS A CD 1 ATOM 911 C CD B LYS A 1 115 ? 13.521 26.156 38.134 0.45 11.34 ? 201 LYS A CD 1 ATOM 912 C CE A LYS A 1 115 ? 13.037 24.831 38.248 0.55 12.61 ? 201 LYS A CE 1 ATOM 913 C CE B LYS A 1 115 ? 12.059 26.468 38.425 0.45 13.39 ? 201 LYS A CE 1 ATOM 914 N NZ A LYS A 1 115 ? 12.427 24.589 39.582 0.55 15.48 ? 201 LYS A NZ 1 ATOM 915 N NZ B LYS A 1 115 ? 11.668 26.068 39.817 0.45 16.53 ? 201 LYS A NZ 1 ATOM 916 N N . ALA A 1 116 ? 15.184 30.839 35.387 1.00 4.95 ? 202 ALA A N 1 ATOM 917 C CA . ALA A 1 116 ? 15.095 32.294 35.185 1.00 4.91 ? 202 ALA A CA 1 ATOM 918 C C . ALA A 1 116 ? 15.158 32.645 33.701 1.00 5.03 ? 202 ALA A C 1 ATOM 919 O O . ALA A 1 116 ? 14.475 33.540 33.234 1.00 6.04 ? 202 ALA A O 1 ATOM 920 C CB . ALA A 1 116 ? 16.173 33.037 35.982 1.00 6.05 ? 202 ALA A CB 1 ATOM 921 N N . TYR A 1 117 ? 16.049 31.978 32.972 1.00 4.88 ? 203 TYR A N 1 ATOM 922 C CA . TYR A 1 117 ? 16.160 32.143 31.515 1.00 4.81 ? 203 TYR A CA 1 ATOM 923 C C . TYR A 1 117 ? 14.832 31.834 30.826 1.00 5.19 ? 203 TYR A C 1 ATOM 924 O O . TYR A 1 117 ? 14.357 32.610 30.000 1.00 5.55 ? 203 TYR A O 1 ATOM 925 C CB . TYR A 1 117 ? 17.333 31.251 31.082 1.00 4.69 ? 203 TYR A CB 1 ATOM 926 C CG . TYR A 1 117 ? 17.483 30.795 29.639 1.00 5.41 ? 203 TYR A CG 1 ATOM 927 C CD1 . TYR A 1 117 ? 18.227 31.527 28.739 1.00 4.58 ? 203 TYR A CD1 1 ATOM 928 C CD2 . TYR A 1 117 ? 16.991 29.553 29.235 1.00 5.61 ? 203 TYR A CD2 1 ATOM 929 C CE1 . TYR A 1 117 ? 18.458 31.058 27.454 1.00 5.88 ? 203 TYR A CE1 1 ATOM 930 C CE2 . TYR A 1 117 ? 17.177 29.111 27.961 1.00 4.82 ? 203 TYR A CE2 1 ATOM 931 C CZ . TYR A 1 117 ? 17.906 29.847 27.062 1.00 4.40 ? 203 TYR A CZ 1 ATOM 932 O OH . TYR A 1 117 ? 18.109 29.369 25.753 1.00 4.98 ? 203 TYR A OH 1 ATOM 933 N N . ILE A 1 118 ? 14.237 30.687 31.156 1.00 4.47 ? 204 ILE A N 1 ATOM 934 C CA . ILE A 1 118 ? 12.924 30.346 30.581 1.00 5.25 ? 204 ILE A CA 1 ATOM 935 C C . ILE A 1 118 ? 11.887 31.395 30.970 1.00 5.33 ? 204 ILE A C 1 ATOM 936 O O . ILE A 1 118 ? 11.097 31.791 30.144 1.00 4.59 ? 204 ILE A O 1 ATOM 937 C CB . ILE A 1 118 ? 12.464 28.935 31.046 1.00 5.27 ? 204 ILE A CB 1 ATOM 938 C CG1 . ILE A 1 118 ? 13.350 27.824 30.497 1.00 5.35 ? 204 ILE A CG1 1 ATOM 939 C CG2 . ILE A 1 118 ? 11.001 28.694 30.698 1.00 6.48 ? 204 ILE A CG2 1 ATOM 940 C CD1 . ILE A 1 118 ? 13.471 27.770 28.973 1.00 5.76 ? 204 ILE A CD1 1 ATOM 941 N N . ASN A 1 119 ? 11.894 31.828 32.230 1.00 5.28 ? 205 ASN A N 1 ATOM 942 C CA . ASN A 1 119 ? 10.927 32.823 32.704 1.00 5.53 ? 205 ASN A CA 1 ATOM 943 C C . ASN A 1 119 ? 11.084 34.138 31.923 1.00 5.73 ? 205 ASN A C 1 ATOM 944 O O . ASN A 1 119 ? 10.091 34.798 31.597 1.00 5.36 ? 205 ASN A O 1 ATOM 945 C CB . ASN A 1 119 ? 11.103 33.118 34.192 1.00 6.90 ? 205 ASN A CB 1 ATOM 946 C CG . ASN A 1 119 ? 10.724 31.972 35.124 1.00 8.60 ? 205 ASN A CG 1 ATOM 947 O OD1 . ASN A 1 119 ? 10.063 31.028 34.746 1.00 9.93 ? 205 ASN A OD1 1 ATOM 948 N ND2 . ASN A 1 119 ? 11.174 32.075 36.402 1.00 12.23 ? 205 ASN A ND2 1 ATOM 949 N N . ARG A 1 120 ? 12.323 34.564 31.676 1.00 5.17 ? 206 ARG A N 1 ATOM 950 C CA . ARG A 1 120 ? 12.554 35.813 30.952 1.00 5.95 ? 206 ARG A CA 1 ATOM 951 C C . ARG A 1 120 ? 12.106 35.659 29.486 1.00 5.25 ? 206 ARG A C 1 ATOM 952 O O . ARG A 1 120 ? 11.500 36.557 28.899 1.00 5.03 ? 206 ARG A O 1 ATOM 953 C CB . ARG A 1 120 ? 14.017 36.262 31.046 1.00 4.97 ? 206 ARG A CB 1 ATOM 954 C CG . ARG A 1 120 ? 14.253 37.597 30.379 1.00 5.42 ? 206 ARG A CG 1 ATOM 955 C CD . ARG A 1 120 ? 13.523 38.760 31.019 1.00 6.58 ? 206 ARG A CD 1 ATOM 956 N NE . ARG A 1 120 ? 13.729 39.949 30.185 1.00 6.79 ? 206 ARG A NE 1 ATOM 957 C CZ . ARG A 1 120 ? 12.806 40.831 29.881 1.00 7.97 ? 206 ARG A CZ 1 ATOM 958 N NH1 . ARG A 1 120 ? 11.591 40.718 30.398 1.00 9.86 ? 206 ARG A NH1 1 ATOM 959 N NH2 . ARG A 1 120 ? 13.075 41.843 29.084 1.00 10.72 ? 206 ARG A NH2 1 ATOM 960 N N . ILE A 1 121 ? 12.405 34.517 28.872 1.00 5.38 ? 207 ILE A N 1 ATOM 961 C CA . ILE A 1 121 ? 11.913 34.228 27.498 1.00 5.56 ? 207 ILE A CA 1 ATOM 962 C C . ILE A 1 121 ? 10.397 34.329 27.482 1.00 4.91 ? 207 ILE A C 1 ATOM 963 O O . ILE A 1 121 ? 9.840 34.936 26.586 1.00 5.05 ? 207 ILE A O 1 ATOM 964 C CB . ILE A 1 121 ? 12.425 32.855 26.979 1.00 4.90 ? 207 ILE A CB 1 ATOM 965 C CG1 . ILE A 1 121 ? 13.926 32.927 26.802 1.00 4.60 ? 207 ILE A CG1 1 ATOM 966 C CG2 . ILE A 1 121 ? 11.710 32.454 25.681 1.00 5.29 ? 207 ILE A CG2 1 ATOM 967 C CD1 . ILE A 1 121 ? 14.613 31.591 26.626 1.00 4.58 ? 207 ILE A CD1 1 ATOM 968 N N . ARG A 1 122 ? 9.728 33.735 28.463 1.00 4.91 ? 208 ARG A N 1 ATOM 969 C CA . ARG A 1 122 ? 8.271 33.782 28.527 1.00 4.70 ? 208 ARG A CA 1 ATOM 970 C C . ARG A 1 122 ? 7.762 35.231 28.545 1.00 4.63 ? 208 ARG A C 1 ATOM 971 O O . ARG A 1 122 ? 6.834 35.576 27.835 1.00 5.29 ? 208 ARG A O 1 ATOM 972 C CB . ARG A 1 122 ? 7.740 33.002 29.726 1.00 5.64 ? 208 ARG A CB 1 ATOM 973 C CG . ARG A 1 122 ? 6.254 33.095 29.945 1.00 6.49 ? 208 ARG A CG 1 ATOM 974 C CD . ARG A 1 122 ? 5.787 32.466 31.200 1.00 7.39 ? 208 ARG A CD 1 ATOM 975 N NE . ARG A 1 122 ? 4.363 32.791 31.447 1.00 12.53 ? 208 ARG A NE 1 ATOM 976 C CZ . ARG A 1 122 ? 3.329 32.032 31.144 1.00 12.15 ? 208 ARG A CZ 1 ATOM 977 N NH1 . ARG A 1 122 ? 3.504 30.854 30.592 1.00 12.14 ? 208 ARG A NH1 1 ATOM 978 N NH2 . ARG A 1 122 ? 2.085 32.442 31.365 1.00 15.23 ? 208 ARG A NH2 1 ATOM 979 N N . GLU A 1 123 ? 8.405 36.082 29.361 1.00 5.14 ? 209 GLU A N 1 ATOM 980 C CA . GLU A 1 123 ? 7.994 37.491 29.444 1.00 5.55 ? 209 GLU A CA 1 ATOM 981 C C . GLU A 1 123 ? 8.120 38.161 28.076 1.00 5.67 ? 209 GLU A C 1 ATOM 982 O O . GLU A 1 123 ? 7.245 38.957 27.659 1.00 6.35 ? 209 GLU A O 1 ATOM 983 C CB . GLU A 1 123 ? 8.832 38.281 30.473 1.00 5.53 ? 209 GLU A CB 1 ATOM 984 C CG . GLU A 1 123 ? 8.552 37.887 31.889 1.00 7.63 ? 209 GLU A CG 1 ATOM 985 C CD . GLU A 1 123 ? 9.476 38.557 32.898 1.00 12.74 ? 209 GLU A CD 1 ATOM 986 O OE1 . GLU A 1 123 ? 10.526 39.105 32.540 1.00 12.05 ? 209 GLU A OE1 1 ATOM 987 O OE2 . GLU A 1 123 ? 9.129 38.533 34.110 1.00 16.42 ? 209 GLU A OE2 1 ATOM 988 N N . ILE A 1 124 ? 9.220 37.904 27.399 1.00 4.93 ? 210 ILE A N 1 ATOM 989 C CA . ILE A 1 124 ? 9.434 38.528 26.083 1.00 5.00 ? 210 ILE A CA 1 ATOM 990 C C . ILE A 1 124 ? 8.455 38.002 25.035 1.00 4.76 ? 210 ILE A C 1 ATOM 991 O O . ILE A 1 124 ? 7.899 38.780 24.249 1.00 5.56 ? 210 ILE A O 1 ATOM 992 C CB . ILE A 1 124 ? 10.898 38.383 25.652 1.00 5.45 ? 210 ILE A CB 1 ATOM 993 C CG1 . ILE A 1 124 ? 11.794 39.215 26.602 1.00 5.68 ? 210 ILE A CG1 1 ATOM 994 C CG2 . ILE A 1 124 ? 11.122 38.745 24.191 1.00 5.83 ? 210 ILE A CG2 1 ATOM 995 C CD1 . ILE A 1 124 ? 13.242 38.743 26.600 1.00 5.78 ? 210 ILE A CD1 1 ATOM 996 N N . LEU A 1 125 ? 8.253 36.694 24.994 1.00 4.32 ? 211 LEU A N 1 ATOM 997 C CA . LEU A 1 125 ? 7.268 36.152 24.058 1.00 4.72 ? 211 LEU A CA 1 ATOM 998 C C . LEU A 1 125 ? 5.869 36.717 24.307 1.00 5.73 ? 211 LEU A C 1 ATOM 999 O O . LEU A 1 125 ? 5.163 37.041 23.365 1.00 6.60 ? 211 LEU A O 1 ATOM 1000 C CB . LEU A 1 125 ? 7.258 34.633 24.079 1.00 4.97 ? 211 LEU A CB 1 ATOM 1001 C CG . LEU A 1 125 ? 8.570 33.880 23.751 1.00 5.18 ? 211 LEU A CG 1 ATOM 1002 C CD1 . LEU A 1 125 ? 8.346 32.388 23.862 1.00 7.75 ? 211 LEU A CD1 1 ATOM 1003 C CD2 . LEU A 1 125 ? 9.072 34.298 22.389 1.00 8.21 ? 211 LEU A CD2 1 ATOM 1004 N N . ILE A 1 126 ? 5.461 36.862 25.567 1.00 5.09 ? 212 ILE A N 1 ATOM 1005 C CA . ILE A 1 126 ? 4.189 37.527 25.895 1.00 6.12 ? 212 ILE A CA 1 ATOM 1006 C C . ILE A 1 126 ? 4.121 38.949 25.355 1.00 5.73 ? 212 ILE A C 1 ATOM 1007 O O . ILE A 1 126 ? 3.149 39.328 24.684 1.00 5.94 ? 212 ILE A O 1 ATOM 1008 C CB . ILE A 1 126 ? 3.927 37.458 27.433 1.00 6.29 ? 212 ILE A CB 1 ATOM 1009 C CG1 . ILE A 1 126 ? 3.456 36.064 27.799 1.00 7.07 ? 212 ILE A CG1 1 ATOM 1010 C CG2 . ILE A 1 126 ? 2.985 38.581 27.891 1.00 7.35 ? 212 ILE A CG2 1 ATOM 1011 C CD1 . ILE A 1 126 ? 3.482 35.811 29.285 1.00 7.67 ? 212 ILE A CD1 1 ATOM 1012 N N . SER A 1 127 ? 5.189 39.714 25.553 1.00 5.49 ? 213 SER A N 1 ATOM 1013 C CA . SER A 1 127 ? 5.272 41.063 25.004 1.00 6.14 ? 213 SER A CA 1 ATOM 1014 C C . SER A 1 127 ? 5.057 41.108 23.512 1.00 5.97 ? 213 SER A C 1 ATOM 1015 O O . SER A 1 127 ? 4.345 41.974 22.974 1.00 6.82 ? 213 SER A O 1 ATOM 1016 C CB A SER A 1 127 ? 6.622 41.693 25.364 0.60 7.10 ? 213 SER A CB 1 ATOM 1017 C CB B SER A 1 127 ? 6.629 41.708 25.301 0.40 6.73 ? 213 SER A CB 1 ATOM 1018 O OG A SER A 1 127 ? 6.608 43.052 25.020 0.60 9.83 ? 213 SER A OG 1 ATOM 1019 O OG B SER A 1 127 ? 6.699 42.066 26.658 0.40 8.45 ? 213 SER A OG 1 ATOM 1020 N N . PHE A 1 128 ? 5.627 40.115 22.852 1.00 5.78 ? 214 PHE A N 1 ATOM 1021 C CA . PHE A 1 128 ? 5.533 39.935 21.395 1.00 5.21 ? 214 PHE A CA 1 ATOM 1022 C C . PHE A 1 128 ? 4.567 38.838 20.935 1.00 5.22 ? 214 PHE A C 1 ATOM 1023 O O . PHE A 1 128 ? 4.803 38.146 19.951 1.00 6.58 ? 214 PHE A O 1 ATOM 1024 C CB . PHE A 1 128 ? 6.928 39.756 20.754 1.00 6.59 ? 214 PHE A CB 1 ATOM 1025 C CG . PHE A 1 128 ? 7.783 40.957 20.877 1.00 6.35 ? 214 PHE A CG 1 ATOM 1026 C CD1 . PHE A 1 128 ? 7.635 41.965 19.923 1.00 7.65 ? 214 PHE A CD1 1 ATOM 1027 C CD2 . PHE A 1 128 ? 8.692 41.125 21.907 1.00 6.72 ? 214 PHE A CD2 1 ATOM 1028 C CE1 . PHE A 1 128 ? 8.405 43.106 20.003 1.00 8.34 ? 214 PHE A CE1 1 ATOM 1029 C CE2 . PHE A 1 128 ? 9.480 42.267 21.990 1.00 8.60 ? 214 PHE A CE2 1 ATOM 1030 C CZ . PHE A 1 128 ? 9.343 43.240 21.014 1.00 9.34 ? 214 PHE A CZ 1 ATOM 1031 N N . SER A 1 129 ? 3.415 38.768 21.610 1.00 5.65 ? 215 SER A N 1 ATOM 1032 C CA . SER A 1 129 ? 2.336 37.816 21.264 1.00 5.22 ? 215 SER A CA 1 ATOM 1033 C C . SER A 1 129 ? 1.844 37.945 19.847 1.00 5.91 ? 215 SER A C 1 ATOM 1034 O O . SER A 1 129 ? 1.296 37.002 19.306 1.00 7.12 ? 215 SER A O 1 ATOM 1035 C CB . SER A 1 129 ? 1.177 37.868 22.269 1.00 5.84 ? 215 SER A CB 1 ATOM 1036 O OG . SER A 1 129 ? 0.556 39.166 22.196 1.00 6.20 ? 215 SER A OG 1 ATOM 1037 N N . ASP A 1 130 ? 1.999 39.137 19.264 1.00 6.57 ? 216 ASP A N 1 ATOM 1038 C CA . ASP A 1 130 ? 1.601 39.407 17.890 1.00 6.62 ? 216 ASP A CA 1 ATOM 1039 C C . ASP A 1 130 ? 2.503 38.761 16.843 1.00 6.80 ? 216 ASP A C 1 ATOM 1040 O O . ASP A 1 130 ? 2.180 38.753 15.669 1.00 9.83 ? 216 ASP A O 1 ATOM 1041 C CB . ASP A 1 130 ? 1.504 40.941 17.636 1.00 6.65 ? 216 ASP A CB 1 ATOM 1042 C CG . ASP A 1 130 ? 2.678 41.720 18.122 1.00 9.93 ? 216 ASP A CG 1 ATOM 1043 O OD1 . ASP A 1 130 ? 3.296 41.451 19.185 1.00 9.91 ? 216 ASP A OD1 1 ATOM 1044 O OD2 . ASP A 1 130 ? 3.023 42.705 17.467 1.00 13.76 ? 216 ASP A OD2 1 ATOM 1045 N N . VAL A 1 131 ? 3.617 38.202 17.281 1.00 5.65 ? 217 VAL A N 1 ATOM 1046 C CA . VAL A 1 131 ? 4.587 37.571 16.375 1.00 5.99 ? 217 VAL A CA 1 ATOM 1047 C C . VAL A 1 131 ? 4.582 36.066 16.634 1.00 5.23 ? 217 VAL A C 1 ATOM 1048 O O . VAL A 1 131 ? 5.116 35.600 17.647 1.00 5.63 ? 217 VAL A O 1 ATOM 1049 C CB . VAL A 1 131 ? 6.004 38.097 16.558 1.00 6.25 ? 217 VAL A CB 1 ATOM 1050 C CG1 . VAL A 1 131 ? 6.997 37.343 15.620 1.00 7.76 ? 217 VAL A CG1 1 ATOM 1051 C CG2 . VAL A 1 131 ? 6.083 39.615 16.293 1.00 6.96 ? 217 VAL A CG2 1 ATOM 1052 N N . ARG A 1 132 ? 3.976 35.315 15.732 1.00 6.42 ? 218 ARG A N 1 ATOM 1053 C CA . ARG A 1 132 ? 3.954 33.858 15.858 1.00 5.74 ? 218 ARG A CA 1 ATOM 1054 C C . ARG A 1 132 ? 5.406 33.373 15.964 1.00 5.53 ? 218 ARG A C 1 ATOM 1055 O O . ARG A 1 132 ? 6.252 33.795 15.199 1.00 6.20 ? 218 ARG A O 1 ATOM 1056 C CB . ARG A 1 132 ? 3.266 33.170 14.703 1.00 6.97 ? 218 ARG A CB 1 ATOM 1057 C CG . ARG A 1 132 ? 2.980 31.722 15.016 1.00 8.70 ? 218 ARG A CG 1 ATOM 1058 C CD . ARG A 1 132 ? 2.321 30.980 13.876 1.00 8.07 ? 218 ARG A CD 1 ATOM 1059 N NE . ARG A 1 132 ? 1.017 31.566 13.524 1.00 9.83 ? 218 ARG A NE 1 ATOM 1060 C CZ . ARG A 1 132 ? 0.340 31.201 12.454 1.00 10.59 ? 218 ARG A CZ 1 ATOM 1061 N NH1 . ARG A 1 132 ? 0.816 30.282 11.661 1.00 9.02 ? 218 ARG A NH1 1 ATOM 1062 N NH2 . ARG A 1 132 ? -0.828 31.751 12.172 1.00 13.14 ? 218 ARG A NH2 1 ATOM 1063 N N . THR A 1 133 ? 5.658 32.523 16.958 1.00 5.54 ? 219 THR A N 1 ATOM 1064 C CA . THR A 1 133 ? 7.015 32.113 17.309 1.00 4.78 ? 219 THR A CA 1 ATOM 1065 C C . THR A 1 133 ? 7.142 30.593 17.430 1.00 4.67 ? 219 THR A C 1 ATOM 1066 O O . THR A 1 133 ? 6.436 29.953 18.206 1.00 5.51 ? 219 THR A O 1 ATOM 1067 C CB . THR A 1 133 ? 7.423 32.780 18.597 1.00 5.02 ? 219 THR A CB 1 ATOM 1068 O OG1 . THR A 1 133 ? 7.406 34.220 18.415 1.00 5.50 ? 219 THR A OG1 1 ATOM 1069 C CG2 . THR A 1 133 ? 8.856 32.384 18.968 1.00 5.85 ? 219 THR A CG2 1 ATOM 1070 N N . ILE A 1 134 ? 8.049 30.047 16.612 1.00 4.57 ? 220 ILE A N 1 ATOM 1071 C CA . ILE A 1 134 ? 8.294 28.631 16.493 1.00 5.55 ? 220 ILE A CA 1 ATOM 1072 C C . ILE A 1 134 ? 9.609 28.324 17.179 1.00 4.86 ? 220 ILE A C 1 ATOM 1073 O O . ILE A 1 134 ? 10.645 28.898 16.833 1.00 5.77 ? 220 ILE A O 1 ATOM 1074 C CB . ILE A 1 134 ? 8.280 28.174 14.990 1.00 5.95 ? 220 ILE A CB 1 ATOM 1075 C CG1 . ILE A 1 134 ? 6.896 28.473 14.391 1.00 9.07 ? 220 ILE A CG1 1 ATOM 1076 C CG2 . ILE A 1 134 ? 8.646 26.690 14.902 1.00 7.53 ? 220 ILE A CG2 1 ATOM 1077 C CD1 . ILE A 1 134 ? 6.850 28.502 12.903 1.00 8.80 ? 220 ILE A CD1 1 ATOM 1078 N N . LEU A 1 135 ? 9.573 27.381 18.127 1.00 4.19 ? 221 LEU A N 1 ATOM 1079 C CA . LEU A 1 135 ? 10.725 27.037 18.953 1.00 4.73 ? 221 LEU A CA 1 ATOM 1080 C C . LEU A 1 135 ? 11.176 25.610 18.746 1.00 4.65 ? 221 LEU A C 1 ATOM 1081 O O . LEU A 1 135 ? 10.338 24.729 18.689 1.00 4.49 ? 221 LEU A O 1 ATOM 1082 C CB . LEU A 1 135 ? 10.400 27.192 20.456 1.00 4.70 ? 221 LEU A CB 1 ATOM 1083 C CG . LEU A 1 135 ? 9.851 28.512 20.915 1.00 5.76 ? 221 LEU A CG 1 ATOM 1084 C CD1 . LEU A 1 135 ? 9.573 28.479 22.412 1.00 6.29 ? 221 LEU A CD1 1 ATOM 1085 C CD2 . LEU A 1 135 ? 10.822 29.636 20.585 1.00 6.60 ? 221 LEU A CD2 1 ATOM 1086 N N . VAL A 1 136 ? 12.482 25.406 18.646 1.00 5.14 ? 222 VAL A N 1 ATOM 1087 C CA . VAL A 1 136 ? 13.130 24.124 18.821 1.00 4.71 ? 222 VAL A CA 1 ATOM 1088 C C . VAL A 1 136 ? 13.673 24.106 20.267 1.00 4.33 ? 222 VAL A C 1 ATOM 1089 O O . VAL A 1 136 ? 14.422 25.000 20.647 1.00 4.96 ? 222 VAL A O 1 ATOM 1090 C CB . VAL A 1 136 ? 14.274 23.883 17.828 1.00 4.72 ? 222 VAL A CB 1 ATOM 1091 C CG1 . VAL A 1 136 ? 15.105 22.673 18.255 1.00 6.05 ? 222 VAL A CG1 1 ATOM 1092 C CG2 . VAL A 1 136 ? 13.708 23.696 16.442 1.00 5.40 ? 222 VAL A CG2 1 ATOM 1093 N N . ILE A 1 137 ? 13.253 23.110 21.056 1.00 3.73 ? 223 ILE A N 1 ATOM 1094 C CA . ILE A 1 137 ? 13.691 22.982 22.451 1.00 3.78 ? 223 ILE A CA 1 ATOM 1095 C C . ILE A 1 137 ? 14.881 22.038 22.578 1.00 4.69 ? 223 ILE A C 1 ATOM 1096 O O . ILE A 1 137 ? 14.780 20.814 22.359 1.00 4.12 ? 223 ILE A O 1 ATOM 1097 C CB . ILE A 1 137 ? 12.515 22.510 23.342 1.00 4.29 ? 223 ILE A CB 1 ATOM 1098 C CG1 . ILE A 1 137 ? 11.305 23.431 23.179 1.00 4.59 ? 223 ILE A CG1 1 ATOM 1099 C CG2 . ILE A 1 137 ? 12.942 22.370 24.802 1.00 5.71 ? 223 ILE A CG2 1 ATOM 1100 C CD1 . ILE A 1 137 ? 11.521 24.879 23.542 1.00 5.12 ? 223 ILE A CD1 1 ATOM 1101 N N . GLU A 1 138 ? 16.018 22.637 22.959 1.00 4.09 ? 224 GLU A N 1 ATOM 1102 C CA . GLU A 1 138 ? 17.224 21.944 23.482 1.00 4.45 ? 224 GLU A CA 1 ATOM 1103 C C . GLU A 1 138 ? 17.775 20.767 22.648 1.00 3.50 ? 224 GLU A C 1 ATOM 1104 O O . GLU A 1 138 ? 17.686 19.573 23.018 1.00 4.46 ? 224 GLU A O 1 ATOM 1105 C CB . GLU A 1 138 ? 16.985 21.533 24.935 1.00 5.09 ? 224 GLU A CB 1 ATOM 1106 C CG . GLU A 1 138 ? 16.724 22.706 25.895 1.00 4.97 ? 224 GLU A CG 1 ATOM 1107 C CD . GLU A 1 138 ? 17.935 23.611 26.143 1.00 4.95 ? 224 GLU A CD 1 ATOM 1108 O OE1 . GLU A 1 138 ? 19.103 23.170 25.890 1.00 5.32 ? 224 GLU A OE1 1 ATOM 1109 O OE2 . GLU A 1 138 ? 17.732 24.769 26.617 1.00 4.83 ? 224 GLU A OE2 1 ATOM 1110 N N . PRO A 1 139 ? 18.430 21.107 21.539 1.00 4.03 ? 225 PRO A N 1 ATOM 1111 C CA . PRO A 1 139 ? 19.205 20.110 20.809 1.00 4.60 ? 225 PRO A CA 1 ATOM 1112 C C . PRO A 1 139 ? 20.159 19.345 21.729 1.00 4.52 ? 225 PRO A C 1 ATOM 1113 O O . PRO A 1 139 ? 20.677 19.894 22.695 1.00 5.19 ? 225 PRO A O 1 ATOM 1114 C CB . PRO A 1 139 ? 19.966 20.937 19.772 1.00 6.20 ? 225 PRO A CB 1 ATOM 1115 C CG . PRO A 1 139 ? 19.076 22.115 19.546 1.00 5.54 ? 225 PRO A CG 1 ATOM 1116 C CD . PRO A 1 139 ? 18.534 22.426 20.928 1.00 4.36 ? 225 PRO A CD 1 ATOM 1117 N N . ASP A 1 140 ? 20.411 18.076 21.405 1.00 5.32 ? 226 ASP A N 1 ATOM 1118 C CA . ASP A 1 140 ? 21.421 17.280 22.132 1.00 5.57 ? 226 ASP A CA 1 ATOM 1119 C C . ASP A 1 140 ? 21.156 17.222 23.615 1.00 5.48 ? 226 ASP A C 1 ATOM 1120 O O . ASP A 1 140 ? 22.103 17.280 24.430 1.00 6.18 ? 226 ASP A O 1 ATOM 1121 C CB . ASP A 1 140 ? 22.821 17.866 21.895 1.00 6.63 ? 226 ASP A CB 1 ATOM 1122 C CG . ASP A 1 140 ? 23.971 17.007 22.390 1.00 8.56 ? 226 ASP A CG 1 ATOM 1123 O OD1 . ASP A 1 140 ? 23.834 15.776 22.293 1.00 9.99 ? 226 ASP A OD1 1 ATOM 1124 O OD2 . ASP A 1 140 ? 25.077 17.523 22.819 1.00 9.80 ? 226 ASP A OD2 1 ATOM 1125 N N . SER A 1 141 ? 19.861 17.089 23.975 1.00 5.19 ? 227 SER A N 1 ATOM 1126 C CA . SER A 1 141 ? 19.456 16.923 25.374 1.00 5.20 ? 227 SER A CA 1 ATOM 1127 C C . SER A 1 141 ? 18.900 15.545 25.682 1.00 4.85 ? 227 SER A C 1 ATOM 1128 O O . SER A 1 141 ? 19.641 14.623 25.998 1.00 5.36 ? 227 SER A O 1 ATOM 1129 C CB . SER A 1 141 ? 18.578 18.080 25.911 1.00 5.17 ? 227 SER A CB 1 ATOM 1130 O OG . SER A 1 141 ? 17.355 18.143 25.211 1.00 5.43 ? 227 SER A OG 1 ATOM 1131 N N . LEU A 1 142 ? 17.601 15.395 25.604 1.00 4.82 ? 228 LEU A N 1 ATOM 1132 C CA . LEU A 1 142 ? 16.945 14.142 25.941 1.00 5.34 ? 228 LEU A CA 1 ATOM 1133 C C . LEU A 1 142 ? 17.337 12.943 25.073 1.00 5.57 ? 228 LEU A C 1 ATOM 1134 O O . LEU A 1 142 ? 17.240 11.790 25.522 1.00 5.90 ? 228 LEU A O 1 ATOM 1135 C CB . LEU A 1 142 ? 15.440 14.330 25.939 1.00 6.19 ? 228 LEU A CB 1 ATOM 1136 C CG . LEU A 1 142 ? 14.873 15.246 27.046 1.00 8.29 ? 228 LEU A CG 1 ATOM 1137 C CD1 . LEU A 1 142 ? 13.409 15.483 26.772 1.00 10.53 ? 228 LEU A CD1 1 ATOM 1138 C CD2 . LEU A 1 142 ? 15.116 14.712 28.418 1.00 10.21 ? 228 LEU A CD2 1 ATOM 1139 N N . ALA A 1 143 ? 17.879 13.180 23.875 1.00 5.44 ? 229 ALA A N 1 ATOM 1140 C CA . ALA A 1 143 ? 18.337 12.044 23.080 1.00 5.48 ? 229 ALA A CA 1 ATOM 1141 C C . ALA A 1 143 ? 19.420 11.279 23.859 1.00 5.42 ? 229 ALA A C 1 ATOM 1142 O O . ALA A 1 143 ? 19.592 10.058 23.729 1.00 5.98 ? 229 ALA A O 1 ATOM 1143 C CB . ALA A 1 143 ? 18.884 12.501 21.715 1.00 5.28 ? 229 ALA A CB 1 ATOM 1144 N N . ASN A 1 144 ? 20.176 12.013 24.679 1.00 5.94 ? 230 ASN A N 1 ATOM 1145 C CA . ASN A 1 144 ? 21.208 11.384 25.507 1.00 5.49 ? 230 ASN A CA 1 ATOM 1146 C C . ASN A 1 144 ? 20.642 10.420 26.558 1.00 6.16 ? 230 ASN A C 1 ATOM 1147 O O . ASN A 1 144 ? 21.321 9.485 27.000 1.00 6.40 ? 230 ASN A O 1 ATOM 1148 C CB . ASN A 1 144 ? 22.055 12.425 26.235 1.00 5.98 ? 230 ASN A CB 1 ATOM 1149 C CG . ASN A 1 144 ? 22.926 13.215 25.298 1.00 6.98 ? 230 ASN A CG 1 ATOM 1150 O OD1 . ASN A 1 144 ? 23.872 12.677 24.696 1.00 8.17 ? 230 ASN A OD1 1 ATOM 1151 N ND2 . ASN A 1 144 ? 22.573 14.497 25.089 1.00 7.22 ? 230 ASN A ND2 1 ATOM 1152 N N . MET A 1 145 ? 19.444 10.688 27.027 1.00 6.00 ? 231 MET A N 1 ATOM 1153 C CA . MET A 1 145 ? 18.792 9.760 27.972 1.00 7.42 ? 231 MET A CA 1 ATOM 1154 C C . MET A 1 145 ? 18.423 8.424 27.326 1.00 8.23 ? 231 MET A C 1 ATOM 1155 O O . MET A 1 145 ? 18.168 7.442 28.022 1.00 9.74 ? 231 MET A O 1 ATOM 1156 C CB . MET A 1 145 ? 17.543 10.395 28.646 1.00 6.82 ? 231 MET A CB 1 ATOM 1157 C CG . MET A 1 145 ? 17.844 11.244 29.894 1.00 7.72 ? 231 MET A CG 1 ATOM 1158 S SD . MET A 1 145 ? 18.605 12.825 29.559 1.00 7.99 ? 231 MET A SD 1 ATOM 1159 C CE . MET A 1 145 ? 20.319 12.474 29.790 1.00 9.62 ? 231 MET A CE 1 ATOM 1160 N N . VAL A 1 146 ? 18.323 8.386 26.005 1.00 7.51 ? 232 VAL A N 1 ATOM 1161 C CA . VAL A 1 146 ? 18.000 7.174 25.305 1.00 7.93 ? 232 VAL A CA 1 ATOM 1162 C C . VAL A 1 146 ? 19.222 6.268 25.217 1.00 8.09 ? 232 VAL A C 1 ATOM 1163 O O . VAL A 1 146 ? 19.087 5.063 25.461 1.00 10.64 ? 232 VAL A O 1 ATOM 1164 C CB . VAL A 1 146 ? 17.429 7.423 23.926 1.00 8.03 ? 232 VAL A CB 1 ATOM 1165 C CG1 . VAL A 1 146 ? 17.052 6.090 23.250 1.00 8.75 ? 232 VAL A CG1 1 ATOM 1166 C CG2 . VAL A 1 146 ? 16.210 8.371 24.023 1.00 9.02 ? 232 VAL A CG2 1 ATOM 1167 N N . THR A 1 147 ? 20.388 6.794 24.841 1.00 7.78 ? 233 THR A N 1 ATOM 1168 C CA . THR A 1 147 ? 21.528 5.939 24.525 1.00 7.38 ? 233 THR A CA 1 ATOM 1169 C C . THR A 1 147 ? 22.779 6.131 25.368 1.00 7.60 ? 233 THR A C 1 ATOM 1170 O O . THR A 1 147 ? 23.688 5.323 25.287 1.00 9.62 ? 233 THR A O 1 ATOM 1171 C CB . THR A 1 147 ? 21.968 6.096 23.033 1.00 7.81 ? 233 THR A CB 1 ATOM 1172 O OG1 . THR A 1 147 ? 22.500 7.431 22.847 1.00 7.92 ? 233 THR A OG1 1 ATOM 1173 C CG2 . THR A 1 147 ? 20.832 5.850 22.065 1.00 10.14 ? 233 THR A CG2 1 ATOM 1174 N N . ASN A 1 148 ? 22.844 7.200 26.152 1.00 6.66 ? 234 ASN A N 1 ATOM 1175 C CA . ASN A 1 148 ? 24.051 7.601 26.877 1.00 6.72 ? 234 ASN A CA 1 ATOM 1176 C C . ASN A 1 148 ? 23.938 7.608 28.422 1.00 7.33 ? 234 ASN A C 1 ATOM 1177 O O . ASN A 1 148 ? 24.722 8.278 29.084 1.00 8.77 ? 234 ASN A O 1 ATOM 1178 C CB . ASN A 1 148 ? 24.542 8.972 26.379 1.00 6.32 ? 234 ASN A CB 1 ATOM 1179 C CG . ASN A 1 148 ? 25.046 8.928 24.972 1.00 9.09 ? 234 ASN A CG 1 ATOM 1180 O OD1 . ASN A 1 148 ? 25.726 7.976 24.577 1.00 13.58 ? 234 ASN A OD1 1 ATOM 1181 N ND2 . ASN A 1 148 ? 24.794 9.990 24.195 1.00 9.17 ? 234 ASN A ND2 1 ATOM 1182 N N . MET A 1 149 ? 23.031 6.818 28.987 1.00 7.67 ? 235 MET A N 1 ATOM 1183 C CA . MET A 1 149 ? 22.864 6.770 30.440 1.00 8.35 ? 235 MET A CA 1 ATOM 1184 C C . MET A 1 149 ? 24.034 6.057 31.117 1.00 8.79 ? 235 MET A C 1 ATOM 1185 O O . MET A 1 149 ? 24.187 6.173 32.334 1.00 10.26 ? 235 MET A O 1 ATOM 1186 C CB . MET A 1 149 ? 21.541 6.141 30.844 1.00 8.82 ? 235 MET A CB 1 ATOM 1187 C CG . MET A 1 149 ? 20.328 7.038 30.576 1.00 10.06 ? 235 MET A CG 1 ATOM 1188 S SD . MET A 1 149 ? 20.330 8.555 31.511 1.00 11.35 ? 235 MET A SD 1 ATOM 1189 C CE . MET A 1 149 ? 19.925 7.897 33.104 1.00 11.19 ? 235 MET A CE 1 ATOM 1190 N N . ASN A 1 150 ? 24.889 5.410 30.326 1.00 9.58 ? 236 ASN A N 1 ATOM 1191 C CA . ASN A 1 150 ? 26.142 4.880 30.856 1.00 10.36 ? 236 ASN A CA 1 ATOM 1192 C C . ASN A 1 150 ? 27.178 5.974 31.140 1.00 9.42 ? 236 ASN A C 1 ATOM 1193 O O . ASN A 1 150 ? 28.146 5.769 31.862 1.00 11.30 ? 236 ASN A O 1 ATOM 1194 C CB . ASN A 1 150 ? 26.733 3.843 29.910 1.00 11.67 ? 236 ASN A CB 1 ATOM 1195 C CG . ASN A 1 150 ? 26.972 4.397 28.515 1.00 14.20 ? 236 ASN A CG 1 ATOM 1196 O OD1 . ASN A 1 150 ? 26.022 4.783 27.814 1.00 16.38 ? 236 ASN A OD1 1 ATOM 1197 N ND2 . ASN A 1 150 ? 28.226 4.446 28.116 1.00 18.67 ? 236 ASN A ND2 1 ATOM 1198 N N . VAL A 1 151 ? 27.009 7.160 30.569 1.00 8.59 ? 237 VAL A N 1 ATOM 1199 C CA . VAL A 1 151 ? 27.964 8.237 30.756 1.00 8.31 ? 237 VAL A CA 1 ATOM 1200 C C . VAL A 1 151 ? 27.648 8.937 32.086 1.00 8.35 ? 237 VAL A C 1 ATOM 1201 O O . VAL A 1 151 ? 26.536 9.411 32.290 1.00 8.98 ? 237 VAL A O 1 ATOM 1202 C CB . VAL A 1 151 ? 27.846 9.302 29.610 1.00 8.94 ? 237 VAL A CB 1 ATOM 1203 C CG1 . VAL A 1 151 ? 28.822 10.473 29.824 1.00 10.73 ? 237 VAL A CG1 1 ATOM 1204 C CG2 . VAL A 1 151 ? 28.111 8.652 28.221 1.00 11.52 ? 237 VAL A CG2 1 ATOM 1205 N N . PRO A 1 152 ? 28.576 8.997 33.023 1.00 7.56 ? 238 PRO A N 1 ATOM 1206 C CA . PRO A 1 152 ? 28.246 9.553 34.327 1.00 7.33 ? 238 PRO A CA 1 ATOM 1207 C C . PRO A 1 152 ? 27.581 10.938 34.311 1.00 6.84 ? 238 PRO A C 1 ATOM 1208 O O . PRO A 1 152 ? 26.585 11.148 35.032 1.00 8.68 ? 238 PRO A O 1 ATOM 1209 C CB . PRO A 1 152 ? 29.600 9.585 35.072 1.00 8.12 ? 238 PRO A CB 1 ATOM 1210 C CG . PRO A 1 152 ? 30.394 8.469 34.427 1.00 8.97 ? 238 PRO A CG 1 ATOM 1211 C CD . PRO A 1 152 ? 29.957 8.482 32.975 1.00 7.90 ? 238 PRO A CD 1 ATOM 1212 N N . LYS A 1 153 ? 28.093 11.869 33.500 1.00 7.10 ? 239 LYS A N 1 ATOM 1213 C CA . LYS A 1 153 ? 27.473 13.205 33.442 1.00 6.47 ? 239 LYS A CA 1 ATOM 1214 C C . LYS A 1 153 ? 26.030 13.129 32.974 1.00 5.93 ? 239 LYS A C 1 ATOM 1215 O O . LYS A 1 153 ? 25.190 13.897 33.441 1.00 7.80 ? 239 LYS A O 1 ATOM 1216 C CB . LYS A 1 153 ? 28.294 14.126 32.555 1.00 7.64 ? 239 LYS A CB 1 ATOM 1217 C CG . LYS A 1 153 ? 27.842 15.586 32.601 1.00 8.66 ? 239 LYS A CG 1 ATOM 1218 C CD . LYS A 1 153 ? 28.782 16.483 31.868 1.00 10.33 ? 239 LYS A CD 1 ATOM 1219 C CE . LYS A 1 153 ? 28.370 17.946 31.791 1.00 12.11 ? 239 LYS A CE 1 ATOM 1220 N NZ . LYS A 1 153 ? 29.415 18.796 31.140 1.00 14.07 ? 239 LYS A NZ 1 ATOM 1221 N N . CYS A 1 154 ? 25.749 12.253 32.037 1.00 6.50 ? 240 CYS A N 1 ATOM 1222 C CA . CYS A 1 154 ? 24.352 12.107 31.558 1.00 6.17 ? 240 CYS A CA 1 ATOM 1223 C C . CYS A 1 154 ? 23.474 11.517 32.619 1.00 6.85 ? 240 CYS A C 1 ATOM 1224 O O . CYS A 1 154 ? 22.360 11.986 32.827 1.00 7.50 ? 240 CYS A O 1 ATOM 1225 C CB . CYS A 1 154 ? 24.234 11.295 30.275 1.00 6.93 ? 240 CYS A CB 1 ATOM 1226 S SG . CYS A 1 154 ? 25.030 12.060 28.844 1.00 9.62 ? 240 CYS A SG 1 ATOM 1227 N N . SER A 1 155 ? 23.931 10.446 33.277 1.00 7.66 ? 241 SER A N 1 ATOM 1228 C CA . SER A 1 155 ? 23.136 9.852 34.318 1.00 8.62 ? 241 SER A CA 1 ATOM 1229 C C . SER A 1 155 ? 22.856 10.855 35.430 1.00 7.58 ? 241 SER A C 1 ATOM 1230 O O . SER A 1 155 ? 21.761 10.857 36.011 1.00 8.31 ? 241 SER A O 1 ATOM 1231 C CB . SER A 1 155 ? 23.873 8.602 34.883 1.00 10.46 ? 241 SER A CB 1 ATOM 1232 O OG . SER A 1 155 ? 23.072 8.028 35.880 1.00 16.97 ? 241 SER A OG 1 ATOM 1233 N N . GLY A 1 156 ? 23.848 11.641 35.771 1.00 7.99 ? 242 GLY A N 1 ATOM 1234 C CA . GLY A 1 156 ? 23.729 12.635 36.809 1.00 7.97 ? 242 GLY A CA 1 ATOM 1235 C C . GLY A 1 156 ? 22.833 13.813 36.430 1.00 8.12 ? 242 GLY A C 1 ATOM 1236 O O . GLY A 1 156 ? 22.241 14.410 37.320 1.00 10.08 ? 242 GLY A O 1 ATOM 1237 N N . ALA A 1 157 ? 22.724 14.074 35.131 1.00 6.58 ? 243 ALA A N 1 ATOM 1238 C CA . ALA A 1 157 ? 21.920 15.185 34.620 1.00 6.64 ? 243 ALA A CA 1 ATOM 1239 C C . ALA A 1 157 ? 20.510 14.783 34.218 1.00 7.21 ? 243 ALA A C 1 ATOM 1240 O O . ALA A 1 157 ? 19.692 15.666 33.987 1.00 7.26 ? 243 ALA A O 1 ATOM 1241 C CB . ALA A 1 157 ? 22.580 15.876 33.473 1.00 7.08 ? 243 ALA A CB 1 ATOM 1242 N N . ALA A 1 158 ? 20.225 13.508 34.147 1.00 7.35 ? 244 ALA A N 1 ATOM 1243 C CA . ALA A 1 158 ? 18.990 13.053 33.490 1.00 6.32 ? 244 ALA A CA 1 ATOM 1244 C C . ALA A 1 158 ? 17.730 13.634 34.154 1.00 6.65 ? 244 ALA A C 1 ATOM 1245 O O . ALA A 1 158 ? 16.839 14.136 33.459 1.00 7.25 ? 244 ALA A O 1 ATOM 1246 C CB . ALA A 1 158 ? 18.931 11.572 33.454 1.00 7.02 ? 244 ALA A CB 1 ATOM 1247 N N . SER A 1 159 ? 17.649 13.596 35.475 1.00 7.09 ? 245 SER A N 1 ATOM 1248 C CA . SER A 1 159 ? 16.463 14.112 36.143 1.00 7.68 ? 245 SER A CA 1 ATOM 1249 C C . SER A 1 159 ? 16.319 15.601 35.913 1.00 7.51 ? 245 SER A C 1 ATOM 1250 O O . SER A 1 159 ? 15.185 16.112 35.797 1.00 8.16 ? 245 SER A O 1 ATOM 1251 C CB . SER A 1 159 ? 16.460 13.777 37.645 1.00 9.50 ? 245 SER A CB 1 ATOM 1252 O OG . SER A 1 159 ? 17.491 14.421 38.331 1.00 13.25 ? 245 SER A OG 1 ATOM 1253 N N . THR A 1 160 ? 17.453 16.287 35.842 1.00 6.11 ? 246 THR A N 1 ATOM 1254 C CA . THR A 1 160 ? 17.475 17.728 35.571 1.00 6.26 ? 246 THR A CA 1 ATOM 1255 C C . THR A 1 160 ? 17.032 18.048 34.145 1.00 6.51 ? 246 THR A C 1 ATOM 1256 O O . THR A 1 160 ? 16.166 18.909 33.932 1.00 6.49 ? 246 THR A O 1 ATOM 1257 C CB . THR A 1 160 ? 18.872 18.316 35.881 1.00 6.92 ? 246 THR A CB 1 ATOM 1258 O OG1 . THR A 1 160 ? 19.142 18.155 37.290 1.00 8.67 ? 246 THR A OG1 1 ATOM 1259 C CG2 . THR A 1 160 ? 18.911 19.789 35.580 1.00 8.70 ? 246 THR A CG2 1 ATOM 1260 N N . TYR A 1 161 ? 17.544 17.315 33.173 1.00 6.54 ? 247 TYR A N 1 ATOM 1261 C CA . TYR A 1 161 ? 17.094 17.444 31.815 1.00 6.18 ? 247 TYR A CA 1 ATOM 1262 C C . TYR A 1 161 ? 15.592 17.227 31.699 1.00 5.96 ? 247 TYR A C 1 ATOM 1263 O O . TYR A 1 161 ? 14.908 18.024 31.072 1.00 6.03 ? 247 TYR A O 1 ATOM 1264 C CB . TYR A 1 161 ? 17.822 16.541 30.782 1.00 6.12 ? 247 TYR A CB 1 ATOM 1265 C CG . TYR A 1 161 ? 19.246 16.895 30.346 1.00 5.30 ? 247 TYR A CG 1 ATOM 1266 C CD1 . TYR A 1 161 ? 20.037 17.845 30.995 1.00 5.82 ? 247 TYR A CD1 1 ATOM 1267 C CD2 . TYR A 1 161 ? 19.780 16.209 29.289 1.00 6.71 ? 247 TYR A CD2 1 ATOM 1268 C CE1 . TYR A 1 161 ? 21.320 18.080 30.542 1.00 5.27 ? 247 TYR A CE1 1 ATOM 1269 C CE2 . TYR A 1 161 ? 21.055 16.413 28.861 1.00 5.51 ? 247 TYR A CE2 1 ATOM 1270 C CZ . TYR A 1 161 ? 21.830 17.348 29.495 1.00 5.91 ? 247 TYR A CZ 1 ATOM 1271 O OH . TYR A 1 161 ? 23.138 17.537 29.072 1.00 6.35 ? 247 TYR A OH 1 ATOM 1272 N N . ARG A 1 162 ? 15.082 16.188 32.328 1.00 6.27 ? 248 ARG A N 1 ATOM 1273 C CA . ARG A 1 162 ? 13.683 15.883 32.222 1.00 7.04 ? 248 ARG A CA 1 ATOM 1274 C C . ARG A 1 162 ? 12.841 16.989 32.895 1.00 5.92 ? 248 ARG A C 1 ATOM 1275 O O . ARG A 1 162 ? 11.888 17.485 32.306 1.00 7.58 ? 248 ARG A O 1 ATOM 1276 C CB A ARG A 1 162 ? 13.415 14.500 32.766 0.65 7.42 ? 248 ARG A CB 1 ATOM 1277 C CB B ARG A 1 162 ? 13.385 14.566 32.929 0.35 7.62 ? 248 ARG A CB 1 ATOM 1278 C CG A ARG A 1 162 ? 14.042 13.381 31.929 0.65 8.21 ? 248 ARG A CG 1 ATOM 1279 C CG B ARG A 1 162 ? 11.895 14.316 33.175 0.35 9.49 ? 248 ARG A CG 1 ATOM 1280 C CD A ARG A 1 162 ? 13.839 11.995 32.519 0.65 11.23 ? 248 ARG A CD 1 ATOM 1281 C CD B ARG A 1 162 ? 11.580 12.993 33.845 0.35 10.82 ? 248 ARG A CD 1 ATOM 1282 N NE A ARG A 1 162 ? 12.454 11.620 32.634 0.65 14.26 ? 248 ARG A NE 1 ATOM 1283 N NE B ARG A 1 162 ? 10.149 12.894 34.047 0.35 11.13 ? 248 ARG A NE 1 ATOM 1284 C CZ A ARG A 1 162 ? 11.994 10.405 32.328 0.65 16.40 ? 248 ARG A CZ 1 ATOM 1285 C CZ B ARG A 1 162 ? 9.544 13.413 35.096 0.35 12.91 ? 248 ARG A CZ 1 ATOM 1286 N NH1 A ARG A 1 162 ? 12.821 9.446 31.918 0.65 17.50 ? 248 ARG A NH1 1 ATOM 1287 N NH1 B ARG A 1 162 ? 10.265 14.026 36.021 0.35 15.14 ? 248 ARG A NH1 1 ATOM 1288 N NH2 A ARG A 1 162 ? 10.694 10.133 32.432 0.65 18.20 ? 248 ARG A NH2 1 ATOM 1289 N NH2 B ARG A 1 162 ? 8.234 13.337 35.240 0.35 13.37 ? 248 ARG A NH2 1 ATOM 1290 N N . GLU A 1 163 ? 13.172 17.336 34.134 1.00 6.79 ? 249 GLU A N 1 ATOM 1291 C CA . GLU A 1 163 ? 12.414 18.344 34.913 1.00 6.96 ? 249 GLU A CA 1 ATOM 1292 C C . GLU A 1 163 ? 12.437 19.704 34.227 1.00 5.45 ? 249 GLU A C 1 ATOM 1293 O O . GLU A 1 163 ? 11.428 20.386 34.168 1.00 5.94 ? 249 GLU A O 1 ATOM 1294 C CB A GLU A 1 163 ? 12.847 18.395 36.355 0.60 7.60 ? 249 GLU A CB 1 ATOM 1295 C CB B GLU A 1 163 ? 13.095 18.528 36.319 0.40 8.00 ? 249 GLU A CB 1 ATOM 1296 C CG A GLU A 1 163 ? 12.493 17.086 37.056 0.60 9.68 ? 249 GLU A CG 1 ATOM 1297 C CG B GLU A 1 163 ? 12.548 19.613 37.285 0.40 11.43 ? 249 GLU A CG 1 ATOM 1298 C CD A GLU A 1 163 ? 13.190 16.947 38.416 0.60 15.40 ? 249 GLU A CD 1 ATOM 1299 C CD B GLU A 1 163 ? 13.598 20.354 38.180 0.40 15.62 ? 249 GLU A CD 1 ATOM 1300 O OE1 A GLU A 1 163 ? 13.795 17.933 38.906 0.60 19.92 ? 249 GLU A OE1 1 ATOM 1301 O OE1 B GLU A 1 163 ? 14.830 20.053 38.190 0.40 15.35 ? 249 GLU A OE1 1 ATOM 1302 O OE2 A GLU A 1 163 ? 13.134 15.842 38.991 0.60 18.22 ? 249 GLU A OE2 1 ATOM 1303 O OE2 B GLU A 1 163 ? 13.168 21.294 38.906 0.40 17.91 ? 249 GLU A OE2 1 ATOM 1304 N N . LEU A 1 164 ? 13.590 20.126 33.730 1.00 5.83 ? 250 LEU A N 1 ATOM 1305 C CA . LEU A 1 164 ? 13.695 21.448 33.139 1.00 5.74 ? 250 LEU A CA 1 ATOM 1306 C C . LEU A 1 164 ? 13.047 21.446 31.746 1.00 6.05 ? 250 LEU A C 1 ATOM 1307 O O . LEU A 1 164 ? 12.573 22.495 31.301 1.00 7.19 ? 250 LEU A O 1 ATOM 1308 C CB . LEU A 1 164 ? 15.156 21.906 33.059 1.00 5.38 ? 250 LEU A CB 1 ATOM 1309 C CG . LEU A 1 164 ? 15.758 22.232 34.425 1.00 6.85 ? 250 LEU A CG 1 ATOM 1310 C CD1 . LEU A 1 164 ? 17.162 22.735 34.314 1.00 7.78 ? 250 LEU A CD1 1 ATOM 1311 C CD2 . LEU A 1 164 ? 14.955 23.287 35.207 1.00 9.34 ? 250 LEU A CD2 1 ATOM 1312 N N . THR A 1 165 ? 13.042 20.319 31.053 1.00 5.21 ? 251 THR A N 1 ATOM 1313 C CA . THR A 1 165 ? 12.306 20.238 29.772 1.00 5.60 ? 251 THR A CA 1 ATOM 1314 C C . THR A 1 165 ? 10.812 20.433 30.011 1.00 6.06 ? 251 THR A C 1 ATOM 1315 O O . THR A 1 165 ? 10.158 21.268 29.380 1.00 6.51 ? 251 THR A O 1 ATOM 1316 C CB . THR A 1 165 ? 12.585 18.926 29.017 1.00 7.01 ? 251 THR A CB 1 ATOM 1317 O OG1 . THR A 1 165 ? 13.985 18.826 28.723 1.00 9.21 ? 251 THR A OG1 1 ATOM 1318 C CG2 . THR A 1 165 ? 11.861 18.935 27.683 1.00 6.87 ? 251 THR A CG2 1 ATOM 1319 N N . ILE A 1 166 ? 10.282 19.729 31.000 1.00 6.33 ? 252 ILE A N 1 ATOM 1320 C CA . ILE A 1 166 ? 8.875 19.883 31.366 1.00 6.46 ? 252 ILE A CA 1 ATOM 1321 C C . ILE A 1 166 ? 8.600 21.343 31.749 1.00 6.54 ? 252 ILE A C 1 ATOM 1322 O O . ILE A 1 166 ? 7.574 21.917 31.324 1.00 5.93 ? 252 ILE A O 1 ATOM 1323 C CB . ILE A 1 166 ? 8.532 18.898 32.468 1.00 6.90 ? 252 ILE A CB 1 ATOM 1324 C CG1 . ILE A 1 166 ? 8.574 17.471 31.889 1.00 8.17 ? 252 ILE A CG1 1 ATOM 1325 C CG2 . ILE A 1 166 ? 7.143 19.186 33.080 1.00 6.83 ? 252 ILE A CG2 1 ATOM 1326 C CD1 . ILE A 1 166 ? 8.631 16.356 32.926 1.00 9.72 ? 252 ILE A CD1 1 ATOM 1327 N N . TYR A 1 167 ? 9.523 21.949 32.481 1.00 6.89 ? 253 TYR A N 1 ATOM 1328 C CA . TYR A 1 167 ? 9.375 23.343 32.914 1.00 6.55 ? 253 TYR A CA 1 ATOM 1329 C C . TYR A 1 167 ? 9.240 24.251 31.690 1.00 6.20 ? 253 TYR A C 1 ATOM 1330 O O . TYR A 1 167 ? 8.337 25.098 31.635 1.00 7.03 ? 253 TYR A O 1 ATOM 1331 C CB . TYR A 1 167 ? 10.540 23.767 33.781 1.00 7.48 ? 253 TYR A CB 1 ATOM 1332 C CG . TYR A 1 167 ? 10.391 25.112 34.442 1.00 7.49 ? 253 TYR A CG 1 ATOM 1333 C CD1 . TYR A 1 167 ? 9.646 25.263 35.587 1.00 11.20 ? 253 TYR A CD1 1 ATOM 1334 C CD2 . TYR A 1 167 ? 10.921 26.249 33.865 1.00 7.08 ? 253 TYR A CD2 1 ATOM 1335 C CE1 . TYR A 1 167 ? 9.519 26.509 36.196 1.00 11.45 ? 253 TYR A CE1 1 ATOM 1336 C CE2 . TYR A 1 167 ? 10.784 27.499 34.463 1.00 8.82 ? 253 TYR A CE2 1 ATOM 1337 C CZ . TYR A 1 167 ? 10.096 27.612 35.641 1.00 9.66 ? 253 TYR A CZ 1 ATOM 1338 O OH . TYR A 1 167 ? 9.908 28.844 36.282 1.00 10.79 ? 253 TYR A OH 1 ATOM 1339 N N . ALA A 1 168 ? 10.125 24.095 30.707 1.00 6.15 ? 254 ALA A N 1 ATOM 1340 C CA . ALA A 1 168 ? 10.085 24.910 29.491 1.00 7.13 ? 254 ALA A CA 1 ATOM 1341 C C . ALA A 1 168 ? 8.793 24.662 28.710 1.00 6.45 ? 254 ALA A C 1 ATOM 1342 O O . ALA A 1 168 ? 8.179 25.595 28.196 1.00 7.19 ? 254 ALA A O 1 ATOM 1343 C CB . ALA A 1 168 ? 11.316 24.666 28.641 1.00 6.69 ? 254 ALA A CB 1 ATOM 1344 N N . LEU A 1 169 ? 8.403 23.387 28.574 1.00 5.99 ? 255 LEU A N 1 ATOM 1345 C CA . LEU A 1 169 ? 7.194 23.071 27.805 1.00 5.83 ? 255 LEU A CA 1 ATOM 1346 C C . LEU A 1 169 ? 5.950 23.725 28.417 1.00 5.98 ? 255 LEU A C 1 ATOM 1347 O O . LEU A 1 169 ? 5.061 24.132 27.666 1.00 7.54 ? 255 LEU A O 1 ATOM 1348 C CB . LEU A 1 169 ? 6.952 21.564 27.664 1.00 5.23 ? 255 LEU A CB 1 ATOM 1349 C CG . LEU A 1 169 ? 8.014 20.749 26.970 1.00 7.73 ? 255 LEU A CG 1 ATOM 1350 C CD1 . LEU A 1 169 ? 7.578 19.291 26.886 1.00 8.32 ? 255 LEU A CD1 1 ATOM 1351 C CD2 . LEU A 1 169 ? 8.405 21.246 25.626 1.00 7.74 ? 255 LEU A CD2 1 ATOM 1352 N N . LYS A 1 170 ? 5.875 23.797 29.727 1.00 6.12 ? 256 LYS A N 1 ATOM 1353 C CA . LYS A 1 170 ? 4.711 24.398 30.397 1.00 6.52 ? 256 LYS A CA 1 ATOM 1354 C C . LYS A 1 170 ? 4.803 25.926 30.393 1.00 6.56 ? 256 LYS A C 1 ATOM 1355 O O . LYS A 1 170 ? 3.823 26.634 30.161 1.00 7.21 ? 256 LYS A O 1 ATOM 1356 C CB . LYS A 1 170 ? 4.562 23.869 31.814 1.00 7.41 ? 256 LYS A CB 1 ATOM 1357 C CG . LYS A 1 170 ? 4.185 22.390 31.870 1.00 10.05 ? 256 LYS A CG 1 ATOM 1358 C CD . LYS A 1 170 ? 4.065 22.021 33.344 1.00 14.50 ? 256 LYS A CD 1 ATOM 1359 C CE . LYS A 1 170 ? 3.398 20.757 33.608 1.00 19.82 ? 256 LYS A CE 1 ATOM 1360 N NZ . LYS A 1 170 ? 3.001 20.783 35.074 1.00 24.37 ? 256 LYS A NZ 1 ATOM 1361 N N . GLN A 1 171 ? 6.003 26.453 30.657 1.00 5.86 ? 257 GLN A N 1 ATOM 1362 C CA . GLN A 1 171 ? 6.151 27.902 30.757 1.00 6.11 ? 257 GLN A CA 1 ATOM 1363 C C . GLN A 1 171 ? 6.032 28.604 29.408 1.00 5.81 ? 257 GLN A C 1 ATOM 1364 O O . GLN A 1 171 ? 5.608 29.764 29.358 1.00 6.82 ? 257 GLN A O 1 ATOM 1365 C CB A GLN A 1 171 ? 7.462 28.305 31.453 0.50 6.53 ? 257 GLN A CB 1 ATOM 1366 C CB B GLN A 1 171 ? 7.498 28.272 31.401 0.50 6.62 ? 257 GLN A CB 1 ATOM 1367 C CG A GLN A 1 171 ? 7.542 27.964 32.922 0.50 9.22 ? 257 GLN A CG 1 ATOM 1368 C CG B GLN A 1 171 ? 7.565 28.140 32.892 0.50 9.17 ? 257 GLN A CG 1 ATOM 1369 C CD A GLN A 1 171 ? 6.400 28.565 33.726 0.50 10.45 ? 257 GLN A CD 1 ATOM 1370 C CD B GLN A 1 171 ? 6.724 29.184 33.576 0.50 11.50 ? 257 GLN A CD 1 ATOM 1371 O OE1 A GLN A 1 171 ? 6.172 29.792 33.685 0.50 12.64 ? 257 GLN A OE1 1 ATOM 1372 O OE1 B GLN A 1 171 ? 5.497 29.024 33.668 0.50 11.42 ? 257 GLN A OE1 1 ATOM 1373 N NE2 A GLN A 1 171 ? 5.637 27.715 34.376 0.50 13.69 ? 257 GLN A NE2 1 ATOM 1374 N NE2 B GLN A 1 171 ? 7.343 30.289 33.967 0.50 12.56 ? 257 GLN A NE2 1 ATOM 1375 N N . LEU A 1 172 ? 6.386 27.883 28.338 1.00 4.95 ? 258 LEU A N 1 ATOM 1376 C CA . LEU A 1 172 ? 6.360 28.448 26.985 1.00 4.72 ? 258 LEU A CA 1 ATOM 1377 C C . LEU A 1 172 ? 5.116 28.029 26.212 1.00 4.96 ? 258 LEU A C 1 ATOM 1378 O O . LEU A 1 172 ? 5.005 28.309 25.044 1.00 5.44 ? 258 LEU A O 1 ATOM 1379 C CB . LEU A 1 172 ? 7.666 28.240 26.222 1.00 6.01 ? 258 LEU A CB 1 ATOM 1380 C CG . LEU A 1 172 ? 8.919 28.699 26.956 1.00 5.76 ? 258 LEU A CG 1 ATOM 1381 C CD1 . LEU A 1 172 ? 10.160 28.420 26.125 1.00 7.89 ? 258 LEU A CD1 1 ATOM 1382 C CD2 . LEU A 1 172 ? 8.891 30.168 27.335 1.00 7.13 ? 258 LEU A CD2 1 ATOM 1383 N N . ASP A 1 173 ? 4.185 27.374 26.920 1.00 5.10 ? 259 ASP A N 1 ATOM 1384 C CA . ASP A 1 173 ? 2.923 26.939 26.305 1.00 5.99 ? 259 ASP A CA 1 ATOM 1385 C C . ASP A 1 173 ? 1.985 28.149 26.212 1.00 5.75 ? 259 ASP A C 1 ATOM 1386 O O . ASP A 1 173 ? 1.101 28.366 27.052 1.00 6.92 ? 259 ASP A O 1 ATOM 1387 C CB . ASP A 1 173 ? 2.313 25.836 27.148 1.00 5.82 ? 259 ASP A CB 1 ATOM 1388 C CG . ASP A 1 173 ? 0.984 25.332 26.629 1.00 7.07 ? 259 ASP A CG 1 ATOM 1389 O OD1 . ASP A 1 173 ? 0.770 25.394 25.391 1.00 6.98 ? 259 ASP A OD1 1 ATOM 1390 O OD2 . ASP A 1 173 ? 0.157 24.878 27.469 1.00 8.40 ? 259 ASP A OD2 1 ATOM 1391 N N . LEU A 1 174 ? 2.209 28.926 25.188 1.00 5.44 ? 260 LEU A N 1 ATOM 1392 C CA . LEU A 1 174 ? 1.484 30.176 24.929 1.00 5.65 ? 260 LEU A CA 1 ATOM 1393 C C . LEU A 1 174 ? 0.760 30.054 23.589 1.00 5.68 ? 260 LEU A C 1 ATOM 1394 O O . LEU A 1 174 ? 1.273 29.421 22.655 1.00 5.50 ? 260 LEU A O 1 ATOM 1395 C CB . LEU A 1 174 ? 2.448 31.371 24.881 1.00 6.16 ? 260 LEU A CB 1 ATOM 1396 C CG . LEU A 1 174 ? 3.278 31.594 26.130 1.00 6.90 ? 260 LEU A CG 1 ATOM 1397 C CD1 . LEU A 1 174 ? 4.313 32.669 25.875 1.00 7.70 ? 260 LEU A CD1 1 ATOM 1398 C CD2 . LEU A 1 174 ? 2.387 31.934 27.325 1.00 8.02 ? 260 LEU A CD2 1 ATOM 1399 N N . PRO A 1 175 ? -0.421 30.664 23.437 1.00 5.97 ? 261 PRO A N 1 ATOM 1400 C CA . PRO A 1 175 ? -1.168 30.500 22.174 1.00 6.05 ? 261 PRO A CA 1 ATOM 1401 C C . PRO A 1 175 ? -0.496 30.885 20.867 1.00 6.35 ? 261 PRO A C 1 ATOM 1402 O O . PRO A 1 175 ? -0.822 30.335 19.819 1.00 7.23 ? 261 PRO A O 1 ATOM 1403 C CB . PRO A 1 175 ? -2.442 31.330 22.420 1.00 7.01 ? 261 PRO A CB 1 ATOM 1404 C CG . PRO A 1 175 ? -2.643 31.227 23.897 1.00 7.53 ? 261 PRO A CG 1 ATOM 1405 C CD . PRO A 1 175 ? -1.244 31.299 24.482 1.00 6.69 ? 261 PRO A CD 1 ATOM 1406 N N . HIS A 1 176 ? 0.466 31.799 20.891 1.00 5.47 ? 262 HIS A N 1 ATOM 1407 C CA . HIS A 1 176 ? 1.145 32.195 19.680 1.00 5.64 ? 262 HIS A CA 1 ATOM 1408 C C . HIS A 1 176 ? 2.424 31.411 19.402 1.00 5.92 ? 262 HIS A C 1 ATOM 1409 O O . HIS A 1 176 ? 3.135 31.739 18.447 1.00 5.43 ? 262 HIS A O 1 ATOM 1410 C CB . HIS A 1 176 ? 1.431 33.697 19.690 1.00 5.98 ? 262 HIS A CB 1 ATOM 1411 C CG . HIS A 1 176 ? 2.521 34.118 20.626 1.00 5.58 ? 262 HIS A CG 1 ATOM 1412 N ND1 . HIS A 1 176 ? 2.365 34.115 21.986 1.00 5.93 ? 262 HIS A ND1 1 ATOM 1413 C CD2 . HIS A 1 176 ? 3.765 34.601 20.385 1.00 5.49 ? 262 HIS A CD2 1 ATOM 1414 C CE1 . HIS A 1 176 ? 3.472 34.552 22.558 1.00 6.10 ? 262 HIS A CE1 1 ATOM 1415 N NE2 . HIS A 1 176 ? 4.357 34.845 21.606 1.00 5.45 ? 262 HIS A NE2 1 ATOM 1416 N N . VAL A 1 177 ? 2.687 30.418 20.248 1.00 5.38 ? 263 VAL A N 1 ATOM 1417 C CA . VAL A 1 177 ? 3.945 29.640 20.198 1.00 5.33 ? 263 VAL A CA 1 ATOM 1418 C C . VAL A 1 177 ? 3.684 28.200 19.731 1.00 5.57 ? 263 VAL A C 1 ATOM 1419 O O . VAL A 1 177 ? 2.650 27.615 20.003 1.00 5.60 ? 263 VAL A O 1 ATOM 1420 C CB . VAL A 1 177 ? 4.619 29.635 21.579 1.00 5.42 ? 263 VAL A CB 1 ATOM 1421 C CG1 . VAL A 1 177 ? 5.812 28.650 21.660 1.00 5.83 ? 263 VAL A CG1 1 ATOM 1422 C CG2 . VAL A 1 177 ? 5.044 31.044 21.991 1.00 5.83 ? 263 VAL A CG2 1 ATOM 1423 N N . ALA A 1 178 ? 4.652 27.674 18.985 1.00 4.95 ? 264 ALA A N 1 ATOM 1424 C CA . ALA A 1 178 ? 4.762 26.249 18.729 1.00 4.86 ? 264 ALA A CA 1 ATOM 1425 C C . ALA A 1 178 ? 6.107 25.786 19.199 1.00 5.30 ? 264 ALA A C 1 ATOM 1426 O O . ALA A 1 178 ? 7.105 26.492 19.032 1.00 5.64 ? 264 ALA A O 1 ATOM 1427 C CB . ALA A 1 178 ? 4.626 25.968 17.225 1.00 6.46 ? 264 ALA A CB 1 ATOM 1428 N N . MET A 1 179 ? 6.134 24.577 19.746 1.00 5.24 ? 265 MET A N 1 ATOM 1429 C CA . MET A 1 179 ? 7.377 23.926 20.183 1.00 4.01 ? 265 MET A CA 1 ATOM 1430 C C . MET A 1 179 ? 7.552 22.546 19.551 1.00 4.91 ? 265 MET A C 1 ATOM 1431 O O . MET A 1 179 ? 6.628 21.737 19.458 1.00 5.33 ? 265 MET A O 1 ATOM 1432 C CB . MET A 1 179 ? 7.405 23.726 21.684 1.00 4.73 ? 265 MET A CB 1 ATOM 1433 C CG . MET A 1 179 ? 7.713 24.980 22.472 1.00 5.88 ? 265 MET A CG 1 ATOM 1434 S SD . MET A 1 179 ? 7.594 24.857 24.247 1.00 5.61 ? 265 MET A SD 1 ATOM 1435 C CE . MET A 1 179 ? 5.801 24.951 24.469 1.00 6.31 ? 265 MET A CE 1 ATOM 1436 N N . TYR A 1 180 ? 8.810 22.280 19.180 1.00 3.75 ? 266 TYR A N 1 ATOM 1437 C CA . TYR A 1 180 ? 9.308 20.985 18.687 1.00 4.65 ? 266 TYR A CA 1 ATOM 1438 C C . TYR A 1 180 ? 10.484 20.575 19.553 1.00 4.41 ? 266 TYR A C 1 ATOM 1439 O O . TYR A 1 180 ? 11.499 21.300 19.602 1.00 5.00 ? 266 TYR A O 1 ATOM 1440 C CB . TYR A 1 180 ? 9.740 21.079 17.216 1.00 5.27 ? 266 TYR A CB 1 ATOM 1441 C CG . TYR A 1 180 ? 8.604 21.454 16.277 1.00 5.03 ? 266 TYR A CG 1 ATOM 1442 C CD1 . TYR A 1 180 ? 8.275 22.808 16.067 1.00 4.35 ? 266 TYR A CD1 1 ATOM 1443 C CD2 . TYR A 1 180 ? 7.871 20.499 15.572 1.00 5.31 ? 266 TYR A CD2 1 ATOM 1444 C CE1 . TYR A 1 180 ? 7.248 23.177 15.229 1.00 4.91 ? 266 TYR A CE1 1 ATOM 1445 C CE2 . TYR A 1 180 ? 6.839 20.880 14.743 1.00 3.90 ? 266 TYR A CE2 1 ATOM 1446 C CZ . TYR A 1 180 ? 6.547 22.220 14.548 1.00 4.55 ? 266 TYR A CZ 1 ATOM 1447 O OH . TYR A 1 180 ? 5.532 22.622 13.701 1.00 5.85 ? 266 TYR A OH 1 ATOM 1448 N N . MET A 1 181 ? 10.364 19.461 20.276 1.00 3.75 ? 267 MET A N 1 ATOM 1449 C CA . MET A 1 181 ? 11.514 18.999 21.051 1.00 3.99 ? 267 MET A CA 1 ATOM 1450 C C . MET A 1 181 ? 12.524 18.369 20.108 1.00 3.71 ? 267 MET A C 1 ATOM 1451 O O . MET A 1 181 ? 12.191 17.630 19.197 1.00 4.27 ? 267 MET A O 1 ATOM 1452 C CB . MET A 1 181 ? 11.158 17.953 22.096 1.00 4.61 ? 267 MET A CB 1 ATOM 1453 C CG . MET A 1 181 ? 10.421 18.511 23.301 1.00 5.33 ? 267 MET A CG 1 ATOM 1454 S SD . MET A 1 181 ? 9.963 17.253 24.530 1.00 6.26 ? 267 MET A SD 1 ATOM 1455 C CE . MET A 1 181 ? 8.577 16.546 23.707 1.00 7.58 ? 267 MET A CE 1 ATOM 1456 N N . ASP A 1 182 ? 13.793 18.585 20.383 1.00 4.13 ? 268 ASP A N 1 ATOM 1457 C CA . ASP A 1 182 ? 14.833 17.858 19.611 1.00 4.44 ? 268 ASP A CA 1 ATOM 1458 C C . ASP A 1 182 ? 14.695 16.354 19.775 1.00 4.91 ? 268 ASP A C 1 ATOM 1459 O O . ASP A 1 182 ? 14.492 15.844 20.867 1.00 5.17 ? 268 ASP A O 1 ATOM 1460 C CB . ASP A 1 182 ? 16.210 18.287 20.066 1.00 4.61 ? 268 ASP A CB 1 ATOM 1461 C CG . ASP A 1 182 ? 17.293 17.628 19.291 1.00 5.55 ? 268 ASP A CG 1 ATOM 1462 O OD1 . ASP A 1 182 ? 17.621 18.176 18.230 1.00 6.99 ? 268 ASP A OD1 1 ATOM 1463 O OD2 . ASP A 1 182 ? 17.807 16.552 19.680 1.00 5.79 ? 268 ASP A OD2 1 ATOM 1464 N N . ALA A 1 183 ? 14.879 15.648 18.670 1.00 4.51 ? 269 ALA A N 1 ATOM 1465 C CA . ALA A 1 183 ? 14.834 14.177 18.699 1.00 3.68 ? 269 ALA A CA 1 ATOM 1466 C C . ALA A 1 183 ? 15.977 13.562 17.886 1.00 4.95 ? 269 ALA A C 1 ATOM 1467 O O . ALA A 1 183 ? 15.788 12.571 17.162 1.00 5.50 ? 269 ALA A O 1 ATOM 1468 C CB . ALA A 1 183 ? 13.472 13.620 18.293 1.00 5.05 ? 269 ALA A CB 1 ATOM 1469 N N . GLY A 1 184 ? 17.173 14.113 18.009 1.00 4.35 ? 270 GLY A N 1 ATOM 1470 C CA . GLY A 1 184 ? 18.303 13.491 17.357 1.00 5.14 ? 270 GLY A CA 1 ATOM 1471 C C . GLY A 1 184 ? 18.124 13.413 15.852 1.00 5.05 ? 270 GLY A C 1 ATOM 1472 O O . GLY A 1 184 ? 17.579 14.297 15.200 1.00 5.88 ? 270 GLY A O 1 ATOM 1473 N N . HIS A 1 185 ? 18.574 12.314 15.276 1.00 4.82 ? 271 HIS A N 1 ATOM 1474 C CA . HIS A 1 185 ? 18.543 12.113 13.835 1.00 4.73 ? 271 HIS A CA 1 ATOM 1475 C C . HIS A 1 185 ? 18.511 10.622 13.518 1.00 4.92 ? 271 HIS A C 1 ATOM 1476 O O . HIS A 1 185 ? 18.625 9.779 14.429 1.00 5.00 ? 271 HIS A O 1 ATOM 1477 C CB . HIS A 1 185 ? 19.692 12.858 13.136 1.00 4.58 ? 271 HIS A CB 1 ATOM 1478 C CG . HIS A 1 185 ? 21.043 12.303 13.410 1.00 5.75 ? 271 HIS A CG 1 ATOM 1479 N ND1 . HIS A 1 185 ? 21.660 11.374 12.599 1.00 5.95 ? 271 HIS A ND1 1 ATOM 1480 C CD2 . HIS A 1 185 ? 21.915 12.572 14.406 1.00 5.65 ? 271 HIS A CD2 1 ATOM 1481 C CE1 . HIS A 1 185 ? 22.866 11.124 13.083 1.00 6.45 ? 271 HIS A CE1 1 ATOM 1482 N NE2 . HIS A 1 185 ? 23.035 11.810 14.194 1.00 7.49 ? 271 HIS A NE2 1 ATOM 1483 N N . ALA A 1 186 ? 18.337 10.281 12.257 1.00 5.23 ? 272 ALA A N 1 ATOM 1484 C CA . ALA A 1 186 ? 18.218 8.879 11.865 1.00 5.40 ? 272 ALA A CA 1 ATOM 1485 C C . ALA A 1 186 ? 19.366 8.005 12.300 1.00 5.49 ? 272 ALA A C 1 ATOM 1486 O O . ALA A 1 186 ? 19.176 6.825 12.603 1.00 6.02 ? 272 ALA A O 1 ATOM 1487 C CB . ALA A 1 186 ? 18.060 8.756 10.321 1.00 5.85 ? 272 ALA A CB 1 ATOM 1488 N N . GLY A 1 187 ? 20.559 8.584 12.343 1.00 5.55 ? 273 GLY A N 1 ATOM 1489 C CA . GLY A 1 187 ? 21.741 7.839 12.718 1.00 4.96 ? 273 GLY A CA 1 ATOM 1490 C C . GLY A 1 187 ? 22.069 7.828 14.178 1.00 5.24 ? 273 GLY A C 1 ATOM 1491 O O . GLY A 1 187 ? 23.132 7.303 14.594 1.00 6.70 ? 273 GLY A O 1 ATOM 1492 N N . TRP A 1 188 ? 21.159 8.372 14.991 1.00 4.98 ? 274 TRP A N 1 ATOM 1493 C CA . TRP A 1 188 ? 21.238 8.329 16.454 1.00 4.97 ? 274 TRP A CA 1 ATOM 1494 C C . TRP A 1 188 ? 20.050 7.530 16.968 1.00 5.69 ? 274 TRP A C 1 ATOM 1495 O O . TRP A 1 188 ? 20.147 6.340 17.259 1.00 7.15 ? 274 TRP A O 1 ATOM 1496 C CB . TRP A 1 188 ? 21.316 9.748 17.045 1.00 5.54 ? 274 TRP A CB 1 ATOM 1497 C CG . TRP A 1 188 ? 21.553 9.781 18.546 1.00 5.03 ? 274 TRP A CG 1 ATOM 1498 C CD1 . TRP A 1 188 ? 21.631 8.718 19.399 1.00 6.55 ? 274 TRP A CD1 1 ATOM 1499 C CD2 . TRP A 1 188 ? 21.768 10.953 19.346 1.00 6.62 ? 274 TRP A CD2 1 ATOM 1500 N NE1 . TRP A 1 188 ? 21.875 9.165 20.672 1.00 7.19 ? 274 TRP A NE1 1 ATOM 1501 C CE2 . TRP A 1 188 ? 21.978 10.531 20.668 1.00 7.18 ? 274 TRP A CE2 1 ATOM 1502 C CE3 . TRP A 1 188 ? 21.805 12.317 19.074 1.00 5.94 ? 274 TRP A CE3 1 ATOM 1503 C CZ2 . TRP A 1 188 ? 22.286 11.420 21.703 1.00 6.88 ? 274 TRP A CZ2 1 ATOM 1504 C CZ3 . TRP A 1 188 ? 22.098 13.202 20.093 1.00 6.82 ? 274 TRP A CZ3 1 ATOM 1505 C CH2 . TRP A 1 188 ? 22.316 12.753 21.403 1.00 8.06 ? 274 TRP A CH2 1 ATOM 1506 N N . LEU A 1 189 ? 18.899 8.153 17.038 1.00 5.19 ? 275 LEU A N 1 ATOM 1507 C CA . LEU A 1 189 ? 17.715 7.490 17.548 1.00 5.71 ? 275 LEU A CA 1 ATOM 1508 C C . LEU A 1 189 ? 16.974 6.624 16.555 1.00 6.79 ? 275 LEU A C 1 ATOM 1509 O O . LEU A 1 189 ? 16.125 5.838 16.984 1.00 6.63 ? 275 LEU A O 1 ATOM 1510 C CB . LEU A 1 189 ? 16.782 8.517 18.169 1.00 5.67 ? 275 LEU A CB 1 ATOM 1511 C CG . LEU A 1 189 ? 17.369 9.370 19.296 1.00 6.38 ? 275 LEU A CG 1 ATOM 1512 C CD1 . LEU A 1 189 ? 16.294 10.312 19.929 1.00 5.71 ? 275 LEU A CD1 1 ATOM 1513 C CD2 . LEU A 1 189 ? 18.040 8.562 20.408 1.00 6.60 ? 275 LEU A CD2 1 ATOM 1514 N N . GLY A 1 190 ? 17.310 6.742 15.277 1.00 6.40 ? 276 GLY A N 1 ATOM 1515 C CA . GLY A 1 190 ? 16.638 5.969 14.238 1.00 6.48 ? 276 GLY A CA 1 ATOM 1516 C C . GLY A 1 190 ? 17.124 4.539 14.077 1.00 7.46 ? 276 GLY A C 1 ATOM 1517 O O . GLY A 1 190 ? 16.474 3.746 13.393 1.00 8.12 ? 276 GLY A O 1 ATOM 1518 N N . TRP A 1 191 ? 18.243 4.177 14.697 1.00 7.54 ? 277 TRP A N 1 ATOM 1519 C CA . TRP A 1 191 ? 18.662 2.764 14.657 1.00 6.78 ? 277 TRP A CA 1 ATOM 1520 C C . TRP A 1 191 ? 17.548 1.942 15.274 1.00 7.18 ? 277 TRP A C 1 ATOM 1521 O O . TRP A 1 191 ? 16.993 2.337 16.291 1.00 6.80 ? 277 TRP A O 1 ATOM 1522 C CB . TRP A 1 191 ? 19.947 2.564 15.481 1.00 7.13 ? 277 TRP A CB 1 ATOM 1523 C CG . TRP A 1 191 ? 21.156 3.087 14.769 1.00 6.04 ? 277 TRP A CG 1 ATOM 1524 C CD1 . TRP A 1 191 ? 21.699 4.310 14.869 1.00 8.33 ? 277 TRP A CD1 1 ATOM 1525 C CD2 . TRP A 1 191 ? 21.939 2.381 13.793 1.00 7.40 ? 277 TRP A CD2 1 ATOM 1526 N NE1 . TRP A 1 191 ? 22.773 4.433 14.018 1.00 7.41 ? 277 TRP A NE1 1 ATOM 1527 C CE2 . TRP A 1 191 ? 22.937 3.246 13.346 1.00 8.07 ? 277 TRP A CE2 1 ATOM 1528 C CE3 . TRP A 1 191 ? 21.905 1.080 13.287 1.00 9.38 ? 277 TRP A CE3 1 ATOM 1529 C CZ2 . TRP A 1 191 ? 23.911 2.861 12.425 1.00 9.76 ? 277 TRP A CZ2 1 ATOM 1530 C CZ3 . TRP A 1 191 ? 22.872 0.702 12.348 1.00 10.64 ? 277 TRP A CZ3 1 ATOM 1531 C CH2 . TRP A 1 191 ? 23.850 1.585 11.930 1.00 10.44 ? 277 TRP A CH2 1 ATOM 1532 N N . PRO A 1 192 ? 17.220 0.785 14.695 1.00 7.82 ? 278 PRO A N 1 ATOM 1533 C CA . PRO A 1 192 ? 16.135 -0.049 15.233 1.00 9.74 ? 278 PRO A CA 1 ATOM 1534 C C . PRO A 1 192 ? 16.211 -0.327 16.729 1.00 9.78 ? 278 PRO A C 1 ATOM 1535 O O . PRO A 1 192 ? 15.135 -0.293 17.356 1.00 11.99 ? 278 PRO A O 1 ATOM 1536 C CB . PRO A 1 192 ? 16.223 -1.310 14.375 1.00 11.24 ? 278 PRO A CB 1 ATOM 1537 C CG . PRO A 1 192 ? 16.671 -0.794 13.035 1.00 10.18 ? 278 PRO A CG 1 ATOM 1538 C CD . PRO A 1 192 ? 17.721 0.256 13.415 1.00 8.52 ? 278 PRO A CD 1 ATOM 1539 N N . ALA A 1 193 ? 17.372 -0.537 17.294 1.00 10.02 ? 279 ALA A N 1 ATOM 1540 C CA . ALA A 1 193 ? 17.496 -0.815 18.729 1.00 10.90 ? 279 ALA A CA 1 ATOM 1541 C C . ALA A 1 193 ? 17.087 0.385 19.607 1.00 10.51 ? 279 ALA A C 1 ATOM 1542 O O . ALA A 1 193 ? 16.786 0.184 20.806 1.00 11.71 ? 279 ALA A O 1 ATOM 1543 C CB . ALA A 1 193 ? 18.874 -1.248 19.085 1.00 12.22 ? 279 ALA A CB 1 ATOM 1544 N N . ASN A 1 194 ? 17.119 1.598 19.036 1.00 8.30 ? 280 ASN A N 1 ATOM 1545 C CA . ASN A 1 194 ? 16.916 2.824 19.809 1.00 7.83 ? 280 ASN A CA 1 ATOM 1546 C C . ASN A 1 194 ? 15.562 3.459 19.655 1.00 7.81 ? 280 ASN A C 1 ATOM 1547 O O . ASN A 1 194 ? 15.149 4.302 20.463 1.00 8.28 ? 280 ASN A O 1 ATOM 1548 C CB . ASN A 1 194 ? 17.950 3.888 19.386 1.00 6.83 ? 280 ASN A CB 1 ATOM 1549 C CG . ASN A 1 194 ? 19.362 3.491 19.721 1.00 7.92 ? 280 ASN A CG 1 ATOM 1550 O OD1 . ASN A 1 194 ? 19.593 2.632 20.619 1.00 10.39 ? 280 ASN A OD1 1 ATOM 1551 N ND2 . ASN A 1 194 ? 20.354 4.096 19.025 1.00 6.73 ? 280 ASN A ND2 1 ATOM 1552 N N . ILE A 1 195 ? 14.861 3.103 18.604 1.00 7.69 ? 281 ILE A N 1 ATOM 1553 C CA . ILE A 1 195 ? 13.659 3.840 18.224 1.00 8.00 ? 281 ILE A CA 1 ATOM 1554 C C . ILE A 1 195 ? 12.469 3.682 19.191 1.00 8.02 ? 281 ILE A C 1 ATOM 1555 O O . ILE A 1 195 ? 11.802 4.656 19.564 1.00 7.06 ? 281 ILE A O 1 ATOM 1556 C CB . ILE A 1 195 ? 13.348 3.563 16.744 1.00 9.04 ? 281 ILE A CB 1 ATOM 1557 C CG1 . ILE A 1 195 ? 12.435 4.634 16.208 1.00 10.87 ? 281 ILE A CG1 1 ATOM 1558 C CG2 . ILE A 1 195 ? 12.890 2.144 16.559 1.00 11.10 ? 281 ILE A CG2 1 ATOM 1559 C CD1 . ILE A 1 195 ? 12.341 4.535 14.683 1.00 11.35 ? 281 ILE A CD1 1 ATOM 1560 N N . GLN A 1 196 ? 12.251 2.473 19.706 1.00 8.65 ? 282 GLN A N 1 ATOM 1561 C CA . GLN A 1 196 ? 11.162 2.282 20.697 1.00 9.10 ? 282 GLN A CA 1 ATOM 1562 C C . GLN A 1 196 ? 11.493 2.942 22.043 1.00 7.95 ? 282 GLN A C 1 ATOM 1563 O O . GLN A 1 196 ? 10.649 3.678 22.584 1.00 7.91 ? 282 GLN A O 1 ATOM 1564 C CB . GLN A 1 196 ? 10.768 0.817 20.868 1.00 10.59 ? 282 GLN A CB 1 ATOM 1565 C CG . GLN A 1 196 ? 9.502 0.683 21.765 1.00 13.69 ? 282 GLN A CG 1 ATOM 1566 C CD . GLN A 1 196 ? 9.071 -0.763 21.944 1.00 21.77 ? 282 GLN A CD 1 ATOM 1567 O OE1 . GLN A 1 196 ? 8.959 -1.518 20.954 1.00 27.24 ? 282 GLN A OE1 1 ATOM 1568 N NE2 . GLN A 1 196 ? 8.836 -1.158 23.210 1.00 24.79 ? 282 GLN A NE2 1 ATOM 1569 N N . PRO A 1 197 ? 12.684 2.777 22.592 1.00 8.15 ? 283 PRO A N 1 ATOM 1570 C CA . PRO A 1 197 ? 13.028 3.506 23.827 1.00 7.70 ? 283 PRO A CA 1 ATOM 1571 C C . PRO A 1 197 ? 12.899 5.028 23.630 1.00 6.63 ? 283 PRO A C 1 ATOM 1572 O O . PRO A 1 197 ? 12.489 5.734 24.533 1.00 7.36 ? 283 PRO A O 1 ATOM 1573 C CB . PRO A 1 197 ? 14.471 3.079 24.111 1.00 9.12 ? 283 PRO A CB 1 ATOM 1574 C CG . PRO A 1 197 ? 14.626 1.771 23.388 1.00 9.77 ? 283 PRO A CG 1 ATOM 1575 C CD . PRO A 1 197 ? 13.712 1.774 22.223 1.00 8.91 ? 283 PRO A CD 1 ATOM 1576 N N . ALA A 1 198 ? 13.304 5.532 22.463 1.00 6.12 ? 284 ALA A N 1 ATOM 1577 C CA . ALA A 1 198 ? 13.143 6.960 22.176 1.00 5.68 ? 284 ALA A CA 1 ATOM 1578 C C . ALA A 1 198 ? 11.679 7.362 22.180 1.00 5.52 ? 284 ALA A C 1 ATOM 1579 O O . ALA A 1 198 ? 11.326 8.392 22.776 1.00 6.20 ? 284 ALA A O 1 ATOM 1580 C CB . ALA A 1 198 ? 13.780 7.354 20.847 1.00 6.27 ? 284 ALA A CB 1 ATOM 1581 N N . ALA A 1 199 ? 10.832 6.588 21.507 1.00 5.61 ? 285 ALA A N 1 ATOM 1582 C CA . ALA A 1 199 ? 9.393 6.898 21.527 1.00 5.13 ? 285 ALA A CA 1 ATOM 1583 C C . ALA A 1 199 ? 8.823 6.887 22.944 1.00 6.41 ? 285 ALA A C 1 ATOM 1584 O O . ALA A 1 199 ? 8.018 7.763 23.314 1.00 6.65 ? 285 ALA A O 1 ATOM 1585 C CB . ALA A 1 199 ? 8.636 5.896 20.662 1.00 6.18 ? 285 ALA A CB 1 ATOM 1586 N N . GLU A 1 200 ? 9.228 5.911 23.759 1.00 6.13 ? 286 GLU A N 1 ATOM 1587 C CA . GLU A 1 200 ? 8.781 5.836 25.128 1.00 6.76 ? 286 GLU A CA 1 ATOM 1588 C C . GLU A 1 200 ? 9.147 7.118 25.903 1.00 6.01 ? 286 GLU A C 1 ATOM 1589 O O . GLU A 1 200 ? 8.346 7.666 26.633 1.00 6.77 ? 286 GLU A O 1 ATOM 1590 C CB A GLU A 1 200 ? 9.288 4.552 25.810 0.55 6.52 ? 286 GLU A CB 1 ATOM 1591 C CB B GLU A 1 200 ? 9.366 4.603 25.836 0.45 6.90 ? 286 GLU A CB 1 ATOM 1592 C CG A GLU A 1 200 ? 8.659 4.405 27.173 0.55 9.32 ? 286 GLU A CG 1 ATOM 1593 C CG B GLU A 1 200 ? 8.912 3.275 25.259 0.45 9.93 ? 286 GLU A CG 1 ATOM 1594 C CD A GLU A 1 200 ? 8.924 3.090 27.846 0.55 12.62 ? 286 GLU A CD 1 ATOM 1595 C CD B GLU A 1 200 ? 8.966 2.171 26.275 0.45 14.32 ? 286 GLU A CD 1 ATOM 1596 O OE1 A GLU A 1 200 ? 8.413 2.028 27.396 0.55 13.41 ? 286 GLU A OE1 1 ATOM 1597 O OE1 B GLU A 1 200 ? 9.286 2.475 27.443 0.45 17.42 ? 286 GLU A OE1 1 ATOM 1598 O OE2 A GLU A 1 200 ? 9.604 3.140 28.875 0.55 15.02 ? 286 GLU A OE2 1 ATOM 1599 O OE2 B GLU A 1 200 ? 8.678 1.007 25.921 0.45 16.34 ? 286 GLU A OE2 1 ATOM 1600 N N . LEU A 1 201 ? 10.390 7.572 25.764 1.00 6.30 ? 287 LEU A N 1 ATOM 1601 C CA . LEU A 1 201 ? 10.858 8.734 26.507 1.00 6.19 ? 287 LEU A CA 1 ATOM 1602 C C . LEU A 1 201 ? 10.095 9.985 26.102 1.00 6.19 ? 287 LEU A C 1 ATOM 1603 O O . LEU A 1 201 ? 9.590 10.709 26.969 1.00 6.03 ? 287 LEU A O 1 ATOM 1604 C CB A LEU A 1 201 ? 12.368 8.911 26.263 0.65 6.11 ? 287 LEU A CB 1 ATOM 1605 C CB B LEU A 1 201 ? 12.376 8.939 26.331 0.35 6.32 ? 287 LEU A CB 1 ATOM 1606 C CG A LEU A 1 201 ? 12.951 10.189 26.878 0.65 7.11 ? 287 LEU A CG 1 ATOM 1607 C CG B LEU A 1 201 ? 12.987 10.104 27.138 0.35 7.08 ? 287 LEU A CG 1 ATOM 1608 C CD1 A LEU A 1 201 ? 12.828 10.154 28.388 0.65 8.40 ? 287 LEU A CD1 1 ATOM 1609 C CD1 B LEU A 1 201 ? 14.452 9.880 27.406 0.35 8.91 ? 287 LEU A CD1 1 ATOM 1610 C CD2 A LEU A 1 201 ? 14.380 10.408 26.393 0.65 7.88 ? 287 LEU A CD2 1 ATOM 1611 C CD2 B LEU A 1 201 ? 12.809 11.436 26.436 0.35 8.18 ? 287 LEU A CD2 1 ATOM 1612 N N . PHE A 1 202 ? 10.036 10.295 24.808 1.00 5.88 ? 288 PHE A N 1 ATOM 1613 C CA . PHE A 1 202 ? 9.441 11.561 24.374 1.00 5.68 ? 288 PHE A CA 1 ATOM 1614 C C . PHE A 1 202 ? 7.938 11.553 24.631 1.00 5.79 ? 288 PHE A C 1 ATOM 1615 O O . PHE A 1 202 ? 7.377 12.559 25.064 1.00 5.25 ? 288 PHE A O 1 ATOM 1616 C CB . PHE A 1 202 ? 9.747 11.855 22.903 1.00 5.78 ? 288 PHE A CB 1 ATOM 1617 C CG . PHE A 1 202 ? 11.157 12.316 22.689 1.00 5.38 ? 288 PHE A CG 1 ATOM 1618 C CD1 . PHE A 1 202 ? 11.517 13.556 23.122 1.00 6.99 ? 288 PHE A CD1 1 ATOM 1619 C CD2 . PHE A 1 202 ? 12.122 11.475 22.208 1.00 7.38 ? 288 PHE A CD2 1 ATOM 1620 C CE1 . PHE A 1 202 ? 12.851 13.991 22.998 1.00 6.92 ? 288 PHE A CE1 1 ATOM 1621 C CE2 . PHE A 1 202 ? 13.435 11.891 22.087 1.00 7.87 ? 288 PHE A CE2 1 ATOM 1622 C CZ . PHE A 1 202 ? 13.790 13.161 22.460 1.00 7.27 ? 288 PHE A CZ 1 ATOM 1623 N N . ALA A 1 203 ? 7.303 10.394 24.492 1.00 5.81 ? 289 ALA A N 1 ATOM 1624 C CA . ALA A 1 203 ? 5.856 10.331 24.779 1.00 6.28 ? 289 ALA A CA 1 ATOM 1625 C C . ALA A 1 203 ? 5.615 10.495 26.291 1.00 6.08 ? 289 ALA A C 1 ATOM 1626 O O . ALA A 1 203 ? 4.632 11.133 26.695 1.00 5.83 ? 289 ALA A O 1 ATOM 1627 C CB . ALA A 1 203 ? 5.220 9.037 24.282 1.00 7.17 ? 289 ALA A CB 1 ATOM 1628 N N . LYS A 1 204 ? 6.506 10.013 27.143 1.00 6.89 ? 290 LYS A N 1 ATOM 1629 C CA . LYS A 1 204 ? 6.353 10.179 28.602 1.00 7.51 ? 290 LYS A CA 1 ATOM 1630 C C . LYS A 1 204 ? 6.521 11.663 29.006 1.00 6.83 ? 290 LYS A C 1 ATOM 1631 O O . LYS A 1 204 ? 5.776 12.199 29.814 1.00 6.71 ? 290 LYS A O 1 ATOM 1632 C CB . LYS A 1 204 ? 7.294 9.275 29.412 1.00 9.28 ? 290 LYS A CB 1 ATOM 1633 C CG . LYS A 1 204 ? 7.175 9.422 30.894 1.00 13.84 ? 290 LYS A CG 1 ATOM 1634 C CD . LYS A 1 204 ? 5.828 8.856 31.396 1.00 19.68 ? 290 LYS A CD 1 ATOM 1635 C CE . LYS A 1 204 ? 5.740 8.705 32.966 1.00 23.79 ? 290 LYS A CE 1 ATOM 1636 N NZ . LYS A 1 204 ? 6.846 9.335 33.741 1.00 25.66 ? 290 LYS A NZ 1 ATOM 1637 N N . ILE A 1 205 ? 7.513 12.316 28.437 1.00 5.71 ? 291 ILE A N 1 ATOM 1638 C CA . ILE A 1 205 ? 7.751 13.753 28.686 1.00 6.11 ? 291 ILE A CA 1 ATOM 1639 C C . ILE A 1 205 ? 6.523 14.553 28.296 1.00 6.09 ? 291 ILE A C 1 ATOM 1640 O O . ILE A 1 205 ? 6.048 15.420 29.054 1.00 5.40 ? 291 ILE A O 1 ATOM 1641 C CB . ILE A 1 205 ? 8.998 14.255 27.944 1.00 6.73 ? 291 ILE A CB 1 ATOM 1642 C CG1 . ILE A 1 205 ? 10.256 13.614 28.526 1.00 8.21 ? 291 ILE A CG1 1 ATOM 1643 C CG2 . ILE A 1 205 ? 9.126 15.776 27.998 1.00 8.96 ? 291 ILE A CG2 1 ATOM 1644 C CD1 . ILE A 1 205 ? 10.703 14.085 29.896 1.00 11.66 ? 291 ILE A CD1 1 ATOM 1645 N N . TYR A 1 206 ? 5.984 14.232 27.141 1.00 5.60 ? 292 TYR A N 1 ATOM 1646 C CA . TYR A 1 206 ? 4.801 14.921 26.624 1.00 5.56 ? 292 TYR A CA 1 ATOM 1647 C C . TYR A 1 206 ? 3.632 14.760 27.613 1.00 5.98 ? 292 TYR A C 1 ATOM 1648 O O . TYR A 1 206 ? 2.990 15.754 27.985 1.00 5.83 ? 292 TYR A O 1 ATOM 1649 C CB . TYR A 1 206 ? 4.442 14.363 25.259 1.00 5.72 ? 292 TYR A CB 1 ATOM 1650 C CG . TYR A 1 206 ? 3.283 14.996 24.540 1.00 6.07 ? 292 TYR A CG 1 ATOM 1651 C CD1 . TYR A 1 206 ? 3.233 16.341 24.257 1.00 6.70 ? 292 TYR A CD1 1 ATOM 1652 C CD2 . TYR A 1 206 ? 2.260 14.219 24.080 1.00 6.36 ? 292 TYR A CD2 1 ATOM 1653 C CE1 . TYR A 1 206 ? 2.154 16.894 23.557 1.00 6.46 ? 292 TYR A CE1 1 ATOM 1654 C CE2 . TYR A 1 206 ? 1.210 14.754 23.402 1.00 6.26 ? 292 TYR A CE2 1 ATOM 1655 C CZ . TYR A 1 206 ? 1.130 16.092 23.140 1.00 6.91 ? 292 TYR A CZ 1 ATOM 1656 O OH . TYR A 1 206 ? 0.074 16.613 22.409 1.00 6.74 ? 292 TYR A OH 1 ATOM 1657 N N . GLU A 1 207 ? 3.384 13.539 28.070 1.00 6.55 ? 293 GLU A N 1 ATOM 1658 C CA . GLU A 1 207 ? 2.367 13.231 29.098 1.00 8.36 ? 293 GLU A CA 1 ATOM 1659 C C . GLU A 1 207 ? 2.623 13.998 30.394 1.00 8.04 ? 293 GLU A C 1 ATOM 1660 O O . GLU A 1 207 ? 1.717 14.605 30.991 1.00 8.84 ? 293 GLU A O 1 ATOM 1661 C CB . GLU A 1 207 ? 2.408 11.705 29.468 1.00 9.75 ? 293 GLU A CB 1 ATOM 1662 C CG . GLU A 1 207 ? 1.579 10.912 28.562 1.00 12.40 ? 293 GLU A CG 1 ATOM 1663 C CD . GLU A 1 207 ? 1.682 9.422 28.861 1.00 11.33 ? 293 GLU A CD 1 ATOM 1664 O OE1 . GLU A 1 207 ? 2.168 9.002 29.966 1.00 14.20 ? 293 GLU A OE1 1 ATOM 1665 O OE2 . GLU A 1 207 ? 1.302 8.667 28.011 1.00 14.30 ? 293 GLU A OE2 1 ATOM 1666 N N . ASP A 1 208 ? 3.859 13.931 30.863 1.00 8.33 ? 294 ASP A N 1 ATOM 1667 C CA . ASP A 1 208 ? 4.189 14.493 32.168 1.00 9.18 ? 294 ASP A CA 1 ATOM 1668 C C . ASP A 1 208 ? 4.078 16.038 32.154 1.00 8.13 ? 294 ASP A C 1 ATOM 1669 O O . ASP A 1 208 ? 3.885 16.666 33.223 1.00 10.07 ? 294 ASP A O 1 ATOM 1670 C CB . ASP A 1 208 ? 5.545 14.047 32.637 1.00 10.16 ? 294 ASP A CB 1 ATOM 1671 C CG . ASP A 1 208 ? 5.577 12.570 33.035 1.00 12.90 ? 294 ASP A CG 1 ATOM 1672 O OD1 . ASP A 1 208 ? 4.516 11.915 33.173 1.00 17.06 ? 294 ASP A OD1 1 ATOM 1673 O OD2 . ASP A 1 208 ? 6.667 12.003 33.192 1.00 16.74 ? 294 ASP A OD2 1 ATOM 1674 N N . ALA A 1 209 ? 4.202 16.657 30.979 1.00 6.60 ? 295 ALA A N 1 ATOM 1675 C CA . ALA A 1 209 ? 4.021 18.105 30.820 1.00 6.91 ? 295 ALA A CA 1 ATOM 1676 C C . ALA A 1 209 ? 2.544 18.485 30.653 1.00 7.09 ? 295 ALA A C 1 ATOM 1677 O O . ALA A 1 209 ? 2.211 19.649 30.445 1.00 8.27 ? 295 ALA A O 1 ATOM 1678 C CB . ALA A 1 209 ? 4.822 18.632 29.622 1.00 7.40 ? 295 ALA A CB 1 ATOM 1679 N N . GLY A 1 210 ? 1.670 17.493 30.660 1.00 6.97 ? 296 GLY A N 1 ATOM 1680 C CA . GLY A 1 210 ? 0.239 17.726 30.462 1.00 7.79 ? 296 GLY A CA 1 ATOM 1681 C C . GLY A 1 210 ? -0.191 17.925 29.023 1.00 7.65 ? 296 GLY A C 1 ATOM 1682 O O . GLY A 1 210 ? -1.207 18.536 28.747 1.00 8.34 ? 296 GLY A O 1 ATOM 1683 N N . LYS A 1 211 ? 0.586 17.398 28.075 1.00 6.16 ? 297 LYS A N 1 ATOM 1684 C CA . LYS A 1 211 ? 0.293 17.475 26.633 1.00 6.78 ? 297 LYS A CA 1 ATOM 1685 C C . LYS A 1 211 ? -0.012 18.910 26.225 1.00 7.14 ? 297 LYS A C 1 ATOM 1686 O O . LYS A 1 211 ? -1.109 19.236 25.718 1.00 7.55 ? 297 LYS A O 1 ATOM 1687 C CB . LYS A 1 211 ? -0.821 16.510 26.230 1.00 6.36 ? 297 LYS A CB 1 ATOM 1688 C CG . LYS A 1 211 ? -0.500 15.055 26.614 1.00 6.58 ? 297 LYS A CG 1 ATOM 1689 C CD . LYS A 1 211 ? -1.299 14.036 25.823 1.00 4.87 ? 297 LYS A CD 1 ATOM 1690 C CE . LYS A 1 211 ? -0.893 12.629 26.197 1.00 5.94 ? 297 LYS A CE 1 ATOM 1691 N NZ . LYS A 1 211 ? -1.553 11.582 25.354 1.00 6.25 ? 297 LYS A NZ 1 ATOM 1692 N N . PRO A 1 212 ? 0.932 19.823 26.469 1.00 7.11 ? 298 PRO A N 1 ATOM 1693 C CA . PRO A 1 212 ? 0.682 21.249 26.208 1.00 6.53 ? 298 PRO A CA 1 ATOM 1694 C C . PRO A 1 212 ? 0.330 21.473 24.758 1.00 6.28 ? 298 PRO A C 1 ATOM 1695 O O . PRO A 1 212 ? 0.921 20.918 23.831 1.00 6.59 ? 298 PRO A O 1 ATOM 1696 C CB . PRO A 1 212 ? 2.014 21.954 26.563 1.00 6.92 ? 298 PRO A CB 1 ATOM 1697 C CG . PRO A 1 212 ? 2.825 20.977 27.351 1.00 9.02 ? 298 PRO A CG 1 ATOM 1698 C CD . PRO A 1 212 ? 2.298 19.616 26.907 1.00 7.69 ? 298 PRO A CD 1 ATOM 1699 N N . ARG A 1 213 ? -0.678 22.315 24.553 1.00 6.72 ? 299 ARG A N 1 ATOM 1700 C CA . ARG A 1 213 ? -1.172 22.579 23.215 1.00 7.59 ? 299 ARG A CA 1 ATOM 1701 C C . ARG A 1 213 ? -0.091 23.105 22.252 1.00 6.87 ? 299 ARG A C 1 ATOM 1702 O O . ARG A 1 213 ? -0.101 22.818 21.056 1.00 7.67 ? 299 ARG A O 1 ATOM 1703 C CB . ARG A 1 213 ? -2.313 23.594 23.294 1.00 9.49 ? 299 ARG A CB 1 ATOM 1704 C CG . ARG A 1 213 ? -2.761 24.098 21.953 1.00 16.21 ? 299 ARG A CG 1 ATOM 1705 C CD . ARG A 1 213 ? -3.948 25.006 22.056 1.00 22.28 ? 299 ARG A CD 1 ATOM 1706 N NE . ARG A 1 213 ? -4.236 25.674 20.804 1.00 25.58 ? 299 ARG A NE 1 ATOM 1707 C CZ . ARG A 1 213 ? -5.404 25.539 20.181 1.00 24.60 ? 299 ARG A CZ 1 ATOM 1708 N NH1 . ARG A 1 213 ? -6.343 24.743 20.719 1.00 22.24 ? 299 ARG A NH1 1 ATOM 1709 N NH2 . ARG A 1 213 ? -5.658 26.189 19.045 1.00 26.59 ? 299 ARG A NH2 1 ATOM 1710 N N . ALA A 1 214 ? 0.824 23.892 22.798 1.00 5.96 ? 300 ALA A N 1 ATOM 1711 C CA . ALA A 1 214 ? 1.868 24.502 21.964 1.00 6.16 ? 300 ALA A CA 1 ATOM 1712 C C . ALA A 1 214 ? 2.846 23.463 21.407 1.00 6.08 ? 300 ALA A C 1 ATOM 1713 O O . ALA A 1 214 ? 3.569 23.742 20.451 1.00 7.33 ? 300 ALA A O 1 ATOM 1714 C CB . ALA A 1 214 ? 2.629 25.550 22.750 1.00 6.89 ? 300 ALA A CB 1 ATOM 1715 N N . VAL A 1 215 ? 2.923 22.301 22.037 1.00 5.53 ? 301 VAL A N 1 ATOM 1716 C CA . VAL A 1 215 ? 3.861 21.275 21.572 1.00 5.98 ? 301 VAL A CA 1 ATOM 1717 C C . VAL A 1 215 ? 3.294 20.611 20.303 1.00 6.42 ? 301 VAL A C 1 ATOM 1718 O O . VAL A 1 215 ? 2.300 19.863 20.384 1.00 9.27 ? 301 VAL A O 1 ATOM 1719 C CB . VAL A 1 215 ? 4.179 20.252 22.656 1.00 6.70 ? 301 VAL A CB 1 ATOM 1720 C CG1 . VAL A 1 215 ? 5.095 19.135 22.119 1.00 8.21 ? 301 VAL A CG1 1 ATOM 1721 C CG2 . VAL A 1 215 ? 4.837 20.918 23.796 1.00 8.53 ? 301 VAL A CG2 1 ATOM 1722 N N . ARG A 1 216 ? 3.917 20.846 19.163 1.00 6.15 ? 302 ARG A N 1 ATOM 1723 C CA . ARG A 1 216 ? 3.519 20.291 17.881 1.00 6.14 ? 302 ARG A CA 1 ATOM 1724 C C . ARG A 1 216 ? 4.150 18.916 17.639 1.00 4.86 ? 302 ARG A C 1 ATOM 1725 O O . ARG A 1 216 ? 3.589 18.089 16.948 1.00 5.87 ? 302 ARG A O 1 ATOM 1726 C CB . ARG A 1 216 ? 3.884 21.184 16.669 1.00 9.08 ? 302 ARG A CB 1 ATOM 1727 C CG . ARG A 1 216 ? 2.948 22.228 16.264 1.00 12.48 ? 302 ARG A CG 1 ATOM 1728 C CD . ARG A 1 216 ? 1.606 21.619 15.780 1.00 11.35 ? 302 ARG A CD 1 ATOM 1729 N NE . ARG A 1 216 ? 1.603 21.094 14.399 1.00 9.83 ? 302 ARG A NE 1 ATOM 1730 C CZ . ARG A 1 216 ? 0.494 20.667 13.785 1.00 8.00 ? 302 ARG A CZ 1 ATOM 1731 N NH1 . ARG A 1 216 ? -0.661 20.700 14.465 1.00 10.13 ? 302 ARG A NH1 1 ATOM 1732 N NH2 . ARG A 1 216 ? 0.505 20.250 12.538 1.00 7.57 ? 302 ARG A NH2 1 ATOM 1733 N N . GLY A 1 217 ? 5.338 18.689 18.194 1.00 5.34 ? 303 GLY A N 1 ATOM 1734 C CA . GLY A 1 217 ? 6.072 17.471 17.940 1.00 5.47 ? 303 GLY A CA 1 ATOM 1735 C C . GLY A 1 217 ? 7.550 17.610 18.214 1.00 5.24 ? 303 GLY A C 1 ATOM 1736 O O . GLY A 1 217 ? 7.964 18.042 19.309 1.00 4.83 ? 303 GLY A O 1 ATOM 1737 N N . LEU A 1 218 ? 8.329 17.147 17.218 1.00 4.82 ? 304 LEU A N 1 ATOM 1738 C CA . LEU A 1 218 ? 9.760 16.934 17.365 1.00 3.96 ? 304 LEU A CA 1 ATOM 1739 C C . LEU A 1 218 ? 10.505 17.515 16.166 1.00 4.41 ? 304 LEU A C 1 ATOM 1740 O O . LEU A 1 218 ? 9.975 17.634 15.039 1.00 4.55 ? 304 LEU A O 1 ATOM 1741 C CB . LEU A 1 218 ? 10.028 15.418 17.443 1.00 4.84 ? 304 LEU A CB 1 ATOM 1742 C CG . LEU A 1 218 ? 9.321 14.667 18.554 1.00 4.65 ? 304 LEU A CG 1 ATOM 1743 C CD1 . LEU A 1 218 ? 9.589 13.186 18.467 1.00 5.54 ? 304 LEU A CD1 1 ATOM 1744 C CD2 . LEU A 1 218 ? 9.735 15.171 19.951 1.00 5.80 ? 304 LEU A CD2 1 ATOM 1745 N N . ALA A 1 219 ? 11.773 17.844 16.423 1.00 3.92 ? 305 ALA A N 1 ATOM 1746 C CA . ALA A 1 219 ? 12.710 18.319 15.386 1.00 4.28 ? 305 ALA A CA 1 ATOM 1747 C C . ALA A 1 219 ? 13.776 17.298 15.186 1.00 4.66 ? 305 ALA A C 1 ATOM 1748 O O . ALA A 1 219 ? 14.303 16.749 16.152 1.00 5.12 ? 305 ALA A O 1 ATOM 1749 C CB . ALA A 1 219 ? 13.355 19.641 15.805 1.00 5.54 ? 305 ALA A CB 1 ATOM 1750 N N . THR A 1 220 ? 14.112 17.007 13.929 1.00 4.21 ? 306 THR A N 1 ATOM 1751 C CA . THR A 1 220 ? 15.194 16.055 13.658 1.00 4.80 ? 306 THR A CA 1 ATOM 1752 C C . THR A 1 220 ? 16.252 16.632 12.755 1.00 4.41 ? 306 THR A C 1 ATOM 1753 O O . THR A 1 220 ? 16.049 17.594 12.010 1.00 4.51 ? 306 THR A O 1 ATOM 1754 C CB . THR A 1 220 ? 14.703 14.709 13.083 1.00 5.40 ? 306 THR A CB 1 ATOM 1755 O OG1 . THR A 1 220 ? 14.234 14.902 11.749 1.00 7.02 ? 306 THR A OG1 1 ATOM 1756 C CG2 . THR A 1 220 ? 13.574 14.121 13.925 1.00 6.70 ? 306 THR A CG2 1 ATOM 1757 N N . ASN A 1 221 ? 17.425 15.982 12.797 1.00 4.12 ? 307 ASN A N 1 ATOM 1758 C CA . ASN A 1 221 ? 18.574 16.340 11.984 1.00 3.89 ? 307 ASN A CA 1 ATOM 1759 C C . ASN A 1 221 ? 19.180 17.719 12.313 1.00 4.13 ? 307 ASN A C 1 ATOM 1760 O O . ASN A 1 221 ? 19.990 18.224 11.547 1.00 4.20 ? 307 ASN A O 1 ATOM 1761 C CB . ASN A 1 221 ? 18.272 16.266 10.464 1.00 3.93 ? 307 ASN A CB 1 ATOM 1762 C CG . ASN A 1 221 ? 19.532 16.117 9.620 1.00 5.32 ? 307 ASN A CG 1 ATOM 1763 O OD1 . ASN A 1 221 ? 20.436 15.311 9.958 1.00 5.49 ? 307 ASN A OD1 1 ATOM 1764 N ND2 . ASN A 1 221 ? 19.618 16.861 8.494 1.00 5.69 ? 307 ASN A ND2 1 ATOM 1765 N N . VAL A 1 222 ? 18.843 18.275 13.465 1.00 3.92 ? 308 VAL A N 1 ATOM 1766 C CA . VAL A 1 222 ? 19.362 19.604 13.849 1.00 4.33 ? 308 VAL A CA 1 ATOM 1767 C C . VAL A 1 222 ? 20.873 19.578 13.909 1.00 4.56 ? 308 VAL A C 1 ATOM 1768 O O . VAL A 1 222 ? 21.450 18.740 14.607 1.00 5.23 ? 308 VAL A O 1 ATOM 1769 C CB . VAL A 1 222 ? 18.794 20.061 15.195 1.00 4.28 ? 308 VAL A CB 1 ATOM 1770 C CG1 . VAL A 1 222 ? 19.439 21.363 15.660 1.00 4.68 ? 308 VAL A CG1 1 ATOM 1771 C CG2 . VAL A 1 222 ? 17.281 20.231 15.090 1.00 6.07 ? 308 VAL A CG2 1 ATOM 1772 N N . ALA A 1 223 ? 21.516 20.445 13.110 1.00 4.53 ? 309 ALA A N 1 ATOM 1773 C CA . ALA A 1 223 ? 22.976 20.583 13.047 1.00 4.92 ? 309 ALA A CA 1 ATOM 1774 C C . ALA A 1 223 ? 23.661 19.372 12.424 1.00 4.97 ? 309 ALA A C 1 ATOM 1775 O O . ALA A 1 223 ? 24.887 19.257 12.466 1.00 6.64 ? 309 ALA A O 1 ATOM 1776 C CB . ALA A 1 223 ? 23.573 20.881 14.417 1.00 5.50 ? 309 ALA A CB 1 ATOM 1777 N N . ASN A 1 224 ? 22.874 18.474 11.855 1.00 4.30 ? 310 ASN A N 1 ATOM 1778 C CA . ASN A 1 224 ? 23.418 17.331 11.119 1.00 5.44 ? 310 ASN A CA 1 ATOM 1779 C C . ASN A 1 224 ? 23.158 17.480 9.614 1.00 5.33 ? 310 ASN A C 1 ATOM 1780 O O . ASN A 1 224 ? 22.703 18.498 9.154 1.00 4.99 ? 310 ASN A O 1 ATOM 1781 C CB . ASN A 1 224 ? 22.866 16.035 11.701 1.00 5.82 ? 310 ASN A CB 1 ATOM 1782 C CG . ASN A 1 224 ? 23.751 15.506 12.777 1.00 8.37 ? 310 ASN A CG 1 ATOM 1783 O OD1 . ASN A 1 224 ? 24.760 14.859 12.511 1.00 13.05 ? 310 ASN A OD1 1 ATOM 1784 N ND2 . ASN A 1 224 ? 23.443 15.876 14.000 1.00 12.60 ? 310 ASN A ND2 1 ATOM 1785 N N . TYR A 1 225 ? 23.568 16.453 8.858 1.00 4.65 ? 311 TYR A N 1 ATOM 1786 C CA . TYR A 1 225 ? 23.685 16.570 7.404 1.00 4.56 ? 311 TYR A CA 1 ATOM 1787 C C . TYR A 1 225 ? 22.841 15.562 6.663 1.00 4.78 ? 311 TYR A C 1 ATOM 1788 O O . TYR A 1 225 ? 22.984 15.430 5.433 1.00 5.48 ? 311 TYR A O 1 ATOM 1789 C CB . TYR A 1 225 ? 25.133 16.380 7.022 1.00 4.73 ? 311 TYR A CB 1 ATOM 1790 C CG . TYR A 1 225 ? 26.095 17.190 7.839 1.00 4.44 ? 311 TYR A CG 1 ATOM 1791 C CD1 . TYR A 1 225 ? 26.403 18.474 7.493 1.00 5.33 ? 311 TYR A CD1 1 ATOM 1792 C CD2 . TYR A 1 225 ? 26.726 16.646 8.978 1.00 5.67 ? 311 TYR A CD2 1 ATOM 1793 C CE1 . TYR A 1 225 ? 27.286 19.247 8.237 1.00 4.69 ? 311 TYR A CE1 1 ATOM 1794 C CE2 . TYR A 1 225 ? 27.596 17.391 9.724 1.00 5.12 ? 311 TYR A CE2 1 ATOM 1795 C CZ . TYR A 1 225 ? 27.887 18.700 9.355 1.00 4.67 ? 311 TYR A CZ 1 ATOM 1796 O OH . TYR A 1 225 ? 28.814 19.403 10.092 1.00 6.20 ? 311 TYR A OH 1 ATOM 1797 N N . ASN A 1 226 ? 21.929 14.873 7.335 1.00 4.40 ? 312 ASN A N 1 ATOM 1798 C CA . ASN A 1 226 ? 21.248 13.746 6.741 1.00 4.10 ? 312 ASN A CA 1 ATOM 1799 C C . ASN A 1 226 ? 20.336 14.120 5.581 1.00 4.23 ? 312 ASN A C 1 ATOM 1800 O O . ASN A 1 226 ? 19.810 15.247 5.487 1.00 4.62 ? 312 ASN A O 1 ATOM 1801 C CB . ASN A 1 226 ? 20.401 12.974 7.761 1.00 3.84 ? 312 ASN A CB 1 ATOM 1802 C CG . ASN A 1 226 ? 21.246 12.365 8.859 1.00 4.77 ? 312 ASN A CG 1 ATOM 1803 O OD1 . ASN A 1 226 ? 22.488 12.408 8.822 1.00 6.45 ? 312 ASN A OD1 1 ATOM 1804 N ND2 . ASN A 1 226 ? 20.571 11.815 9.849 1.00 5.32 ? 312 ASN A ND2 1 ATOM 1805 N N . ALA A 1 227 ? 20.126 13.156 4.687 1.00 4.42 ? 313 ALA A N 1 ATOM 1806 C CA . ALA A 1 227 ? 19.121 13.312 3.652 1.00 4.43 ? 313 ALA A CA 1 ATOM 1807 C C . ALA A 1 227 ? 17.725 13.295 4.231 1.00 4.80 ? 313 ALA A C 1 ATOM 1808 O O . ALA A 1 227 ? 17.461 12.584 5.183 1.00 5.82 ? 313 ALA A O 1 ATOM 1809 C CB . ALA A 1 227 ? 19.257 12.189 2.641 1.00 5.45 ? 313 ALA A CB 1 ATOM 1810 N N . TRP A 1 228 ? 16.827 14.037 3.586 1.00 6.25 ? 314 TRP A N 1 ATOM 1811 C CA . TRP A 1 228 ? 15.389 13.794 3.788 1.00 5.69 ? 314 TRP A CA 1 ATOM 1812 C C . TRP A 1 228 ? 15.006 12.451 3.151 1.00 6.32 ? 314 TRP A C 1 ATOM 1813 O O . TRP A 1 228 ? 14.582 11.537 3.812 1.00 7.52 ? 314 TRP A O 1 ATOM 1814 C CB . TRP A 1 228 ? 14.514 14.966 3.305 1.00 6.60 ? 314 TRP A CB 1 ATOM 1815 C CG . TRP A 1 228 ? 13.094 14.570 3.004 1.00 6.22 ? 314 TRP A CG 1 ATOM 1816 C CD1 . TRP A 1 228 ? 12.491 14.586 1.799 1.00 6.76 ? 314 TRP A CD1 1 ATOM 1817 C CD2 . TRP A 1 228 ? 12.115 14.079 3.938 1.00 4.85 ? 314 TRP A CD2 1 ATOM 1818 N NE1 . TRP A 1 228 ? 11.204 14.100 1.903 1.00 6.76 ? 314 TRP A NE1 1 ATOM 1819 C CE2 . TRP A 1 228 ? 10.947 13.795 3.217 1.00 6.04 ? 314 TRP A CE2 1 ATOM 1820 C CE3 . TRP A 1 228 ? 12.113 13.859 5.327 1.00 5.28 ? 314 TRP A CE3 1 ATOM 1821 C CZ2 . TRP A 1 228 ? 9.789 13.304 3.839 1.00 6.93 ? 314 TRP A CZ2 1 ATOM 1822 C CZ3 . TRP A 1 228 ? 10.963 13.387 5.932 1.00 6.88 ? 314 TRP A CZ3 1 ATOM 1823 C CH2 . TRP A 1 228 ? 9.817 13.087 5.179 1.00 6.11 ? 314 TRP A CH2 1 ATOM 1824 N N . SER A 1 229 ? 15.191 12.323 1.818 1.00 7.26 ? 315 SER A N 1 ATOM 1825 C CA . SER A 1 229 ? 14.777 11.115 1.107 1.00 8.49 ? 315 SER A CA 1 ATOM 1826 C C . SER A 1 229 ? 15.677 10.875 -0.095 1.00 9.22 ? 315 SER A C 1 ATOM 1827 O O . SER A 1 229 ? 15.679 11.686 -1.067 1.00 11.57 ? 315 SER A O 1 ATOM 1828 C CB . SER A 1 229 ? 13.347 11.201 0.626 1.00 8.98 ? 315 SER A CB 1 ATOM 1829 O OG . SER A 1 229 ? 12.926 10.007 -0.030 1.00 10.28 ? 315 SER A OG 1 ATOM 1830 N N . VAL A 1 230 ? 16.468 9.824 -0.007 1.00 9.99 ? 316 VAL A N 1 ATOM 1831 C CA . VAL A 1 230 ? 17.329 9.422 -1.147 1.00 10.82 ? 316 VAL A CA 1 ATOM 1832 C C . VAL A 1 230 ? 17.109 7.962 -1.465 1.00 11.27 ? 316 VAL A C 1 ATOM 1833 O O . VAL A 1 230 ? 16.644 7.210 -0.638 1.00 10.44 ? 316 VAL A O 1 ATOM 1834 C CB . VAL A 1 230 ? 18.801 9.723 -0.933 1.00 11.84 ? 316 VAL A CB 1 ATOM 1835 C CG1 . VAL A 1 230 ? 19.033 11.207 -1.042 1.00 12.37 ? 316 VAL A CG1 1 ATOM 1836 C CG2 . VAL A 1 230 ? 19.314 9.098 0.384 1.00 12.97 ? 316 VAL A CG2 1 ATOM 1837 N N . SER A 1 231 ? 17.369 7.582 -2.727 1.00 13.34 ? 317 SER A N 1 ATOM 1838 C CA . SER A 1 231 ? 17.064 6.228 -3.197 1.00 15.10 ? 317 SER A CA 1 ATOM 1839 C C . SER A 1 231 ? 18.081 5.177 -2.748 1.00 14.92 ? 317 SER A C 1 ATOM 1840 O O . SER A 1 231 ? 17.761 4.004 -2.700 1.00 16.94 ? 317 SER A O 1 ATOM 1841 C CB . SER A 1 231 ? 16.942 6.196 -4.747 1.00 16.52 ? 317 SER A CB 1 ATOM 1842 O OG . SER A 1 231 ? 18.173 6.640 -5.238 1.00 23.02 ? 317 SER A OG 1 ATOM 1843 N N . SER A 1 232 ? 19.279 5.598 -2.419 1.00 14.80 ? 318 SER A N 1 ATOM 1844 C CA . SER A 1 232 ? 20.292 4.644 -1.999 1.00 15.77 ? 318 SER A CA 1 ATOM 1845 C C . SER A 1 232 ? 20.941 5.084 -0.689 1.00 14.12 ? 318 SER A C 1 ATOM 1846 O O . SER A 1 232 ? 21.251 6.270 -0.516 1.00 13.70 ? 318 SER A O 1 ATOM 1847 C CB A SER A 1 232 ? 21.395 4.516 -3.028 0.50 16.44 ? 318 SER A CB 1 ATOM 1848 C CB B SER A 1 232 ? 21.363 4.444 -3.064 0.50 16.63 ? 318 SER A CB 1 ATOM 1849 O OG A SER A 1 232 ? 22.196 3.399 -2.687 0.50 19.02 ? 318 SER A OG 1 ATOM 1850 O OG B SER A 1 232 ? 21.947 5.666 -3.449 0.50 18.82 ? 318 SER A OG 1 ATOM 1851 N N . PRO A 1 233 ? 21.173 4.138 0.206 1.00 13.15 ? 319 PRO A N 1 ATOM 1852 C CA . PRO A 1 233 ? 21.773 4.481 1.496 1.00 11.72 ? 319 PRO A CA 1 ATOM 1853 C C . PRO A 1 233 ? 23.194 5.022 1.349 1.00 11.04 ? 319 PRO A C 1 ATOM 1854 O O . PRO A 1 233 ? 24.034 4.354 0.730 1.00 10.19 ? 319 PRO A O 1 ATOM 1855 C CB . PRO A 1 233 ? 21.726 3.169 2.281 1.00 12.39 ? 319 PRO A CB 1 ATOM 1856 C CG . PRO A 1 233 ? 20.908 2.246 1.471 1.00 15.38 ? 319 PRO A CG 1 ATOM 1857 C CD . PRO A 1 233 ? 20.891 2.710 0.096 1.00 14.21 ? 319 PRO A CD 1 ATOM 1858 N N . PRO A 1 234 ? 23.508 6.190 1.896 1.00 9.01 ? 320 PRO A N 1 ATOM 1859 C CA . PRO A 1 234 ? 24.899 6.626 1.915 1.00 9.98 ? 320 PRO A CA 1 ATOM 1860 C C . PRO A 1 234 ? 25.750 5.594 2.623 1.00 9.60 ? 320 PRO A C 1 ATOM 1861 O O . PRO A 1 234 ? 25.313 4.872 3.542 1.00 9.19 ? 320 PRO A O 1 ATOM 1862 C CB . PRO A 1 234 ? 24.869 7.959 2.678 1.00 9.40 ? 320 PRO A CB 1 ATOM 1863 C CG . PRO A 1 234 ? 23.464 8.475 2.469 1.00 9.95 ? 320 PRO A CG 1 ATOM 1864 C CD . PRO A 1 234 ? 22.611 7.199 2.479 1.00 9.81 ? 320 PRO A CD 1 ATOM 1865 N N . PRO A 1 235 ? 26.999 5.468 2.208 1.00 10.17 ? 321 PRO A N 1 ATOM 1866 C CA . PRO A 1 235 ? 27.818 4.362 2.703 1.00 10.49 ? 321 PRO A CA 1 ATOM 1867 C C . PRO A 1 235 ? 28.038 4.330 4.215 1.00 10.05 ? 321 PRO A C 1 ATOM 1868 O O . PRO A 1 235 ? 28.156 3.247 4.814 1.00 11.64 ? 321 PRO A O 1 ATOM 1869 C CB . PRO A 1 235 ? 29.147 4.524 1.938 1.00 11.61 ? 321 PRO A CB 1 ATOM 1870 C CG . PRO A 1 235 ? 29.171 5.861 1.386 1.00 14.24 ? 321 PRO A CG 1 ATOM 1871 C CD . PRO A 1 235 ? 27.704 6.289 1.207 1.00 12.55 ? 321 PRO A CD 1 ATOM 1872 N N . TYR A 1 236 ? 28.064 5.496 4.863 1.00 8.44 ? 322 TYR A N 1 ATOM 1873 C CA . TYR A 1 236 ? 28.346 5.582 6.310 1.00 7.29 ? 322 TYR A CA 1 ATOM 1874 C C . TYR A 1 236 ? 27.097 5.233 7.144 1.00 7.51 ? 322 TYR A C 1 ATOM 1875 O O . TYR A 1 236 ? 27.158 5.177 8.380 1.00 8.21 ? 322 TYR A O 1 ATOM 1876 C CB . TYR A 1 236 ? 28.910 6.972 6.656 1.00 8.51 ? 322 TYR A CB 1 ATOM 1877 C CG . TYR A 1 236 ? 28.174 8.063 5.913 1.00 7.44 ? 322 TYR A CG 1 ATOM 1878 C CD1 . TYR A 1 236 ? 26.941 8.508 6.361 1.00 8.00 ? 322 TYR A CD1 1 ATOM 1879 C CD2 . TYR A 1 236 ? 28.697 8.609 4.735 1.00 8.32 ? 322 TYR A CD2 1 ATOM 1880 C CE1 . TYR A 1 236 ? 26.248 9.506 5.634 1.00 8.93 ? 322 TYR A CE1 1 ATOM 1881 C CE2 . TYR A 1 236 ? 28.031 9.587 4.022 1.00 7.62 ? 322 TYR A CE2 1 ATOM 1882 C CZ . TYR A 1 236 ? 26.804 10.033 4.480 1.00 7.94 ? 322 TYR A CZ 1 ATOM 1883 O OH . TYR A 1 236 ? 26.090 10.959 3.738 1.00 6.97 ? 322 TYR A OH 1 ATOM 1884 N N . THR A 1 237 ? 25.979 5.020 6.459 1.00 8.31 ? 323 THR A N 1 ATOM 1885 C CA . THR A 1 237 ? 24.737 4.646 7.160 1.00 7.48 ? 323 THR A CA 1 ATOM 1886 C C . THR A 1 237 ? 24.564 3.160 7.407 1.00 8.57 ? 323 THR A C 1 ATOM 1887 O O . THR A 1 237 ? 23.748 2.740 8.229 1.00 8.62 ? 323 THR A O 1 ATOM 1888 C CB . THR A 1 237 ? 23.492 5.207 6.489 1.00 7.63 ? 323 THR A CB 1 ATOM 1889 O OG1 . THR A 1 237 ? 23.206 4.544 5.245 1.00 8.54 ? 323 THR A OG1 1 ATOM 1890 C CG2 . THR A 1 237 ? 23.579 6.717 6.270 1.00 7.00 ? 323 THR A CG2 1 ATOM 1891 N N . SER A 1 238 ? 25.337 2.333 6.695 1.00 10.36 ? 324 SER A N 1 ATOM 1892 C CA . SER A 1 238 ? 25.123 0.888 6.752 1.00 11.76 ? 324 SER A CA 1 ATOM 1893 C C . SER A 1 238 ? 25.440 0.316 8.127 1.00 11.28 ? 324 SER A C 1 ATOM 1894 O O . SER A 1 238 ? 26.435 0.746 8.732 1.00 12.63 ? 324 SER A O 1 ATOM 1895 C CB . SER A 1 238 ? 26.056 0.229 5.733 1.00 13.48 ? 324 SER A CB 1 ATOM 1896 O OG . SER A 1 238 ? 25.931 -1.171 5.833 1.00 18.20 ? 324 SER A OG 1 ATOM 1897 N N . PRO A 1 239 ? 24.660 -0.652 8.646 1.00 11.39 ? 325 PRO A N 1 ATOM 1898 C CA . PRO A 1 239 ? 23.464 -1.234 8.058 1.00 10.83 ? 325 PRO A CA 1 ATOM 1899 C C . PRO A 1 239 ? 22.126 -0.780 8.620 1.00 10.05 ? 325 PRO A C 1 ATOM 1900 O O . PRO A 1 239 ? 21.170 -1.540 8.710 1.00 11.63 ? 325 PRO A O 1 ATOM 1901 C CB . PRO A 1 239 ? 23.636 -2.701 8.473 1.00 11.66 ? 325 PRO A CB 1 ATOM 1902 C CG . PRO A 1 239 ? 24.188 -2.596 9.796 1.00 12.53 ? 325 PRO A CG 1 ATOM 1903 C CD . PRO A 1 239 ? 25.038 -1.414 9.854 1.00 13.11 ? 325 PRO A CD 1 ATOM 1904 N N . ASN A 1 240 ? 22.028 0.489 8.976 1.00 8.69 ? 326 ASN A N 1 ATOM 1905 C CA . ASN A 1 240 ? 20.756 1.032 9.457 1.00 8.19 ? 326 ASN A CA 1 ATOM 1906 C C . ASN A 1 240 ? 19.713 1.077 8.340 1.00 8.04 ? 326 ASN A C 1 ATOM 1907 O O . ASN A 1 240 ? 19.915 1.791 7.349 1.00 9.13 ? 326 ASN A O 1 ATOM 1908 C CB . ASN A 1 240 ? 21.008 2.453 10.025 1.00 7.34 ? 326 ASN A CB 1 ATOM 1909 C CG . ASN A 1 240 ? 19.845 2.998 10.843 1.00 6.16 ? 326 ASN A CG 1 ATOM 1910 O OD1 . ASN A 1 240 ? 18.756 2.454 10.859 1.00 7.31 ? 326 ASN A OD1 1 ATOM 1911 N ND2 . ASN A 1 240 ? 20.095 4.121 11.524 1.00 5.83 ? 326 ASN A ND2 1 ATOM 1912 N N . PRO A 1 241 ? 18.574 0.409 8.488 1.00 8.45 ? 327 PRO A N 1 ATOM 1913 C CA . PRO A 1 241 ? 17.539 0.518 7.466 1.00 8.85 ? 327 PRO A CA 1 ATOM 1914 C C . PRO A 1 241 ? 16.946 1.916 7.417 1.00 7.52 ? 327 PRO A C 1 ATOM 1915 O O . PRO A 1 241 ? 16.387 2.310 6.405 1.00 8.76 ? 327 PRO A O 1 ATOM 1916 C CB . PRO A 1 241 ? 16.491 -0.491 7.927 1.00 9.55 ? 327 PRO A CB 1 ATOM 1917 C CG . PRO A 1 241 ? 16.705 -0.617 9.366 1.00 10.76 ? 327 PRO A CG 1 ATOM 1918 C CD . PRO A 1 241 ? 18.173 -0.497 9.572 1.00 9.27 ? 327 PRO A CD 1 ATOM 1919 N N . ASN A 1 242 ? 17.051 2.656 8.521 1.00 7.12 ? 328 ASN A N 1 ATOM 1920 C CA . ASN A 1 242 ? 16.579 4.040 8.560 1.00 6.79 ? 328 ASN A CA 1 ATOM 1921 C C . ASN A 1 242 ? 17.683 4.993 8.220 1.00 6.87 ? 328 ASN A C 1 ATOM 1922 O O . ASN A 1 242 ? 18.281 5.640 9.088 1.00 6.87 ? 328 ASN A O 1 ATOM 1923 C CB . ASN A 1 242 ? 15.909 4.326 9.882 1.00 6.69 ? 328 ASN A CB 1 ATOM 1924 C CG . ASN A 1 242 ? 14.698 3.420 10.115 1.00 7.09 ? 328 ASN A CG 1 ATOM 1925 O OD1 . ASN A 1 242 ? 13.951 3.134 9.181 1.00 10.16 ? 328 ASN A OD1 1 ATOM 1926 N ND2 . ASN A 1 242 ? 14.539 2.906 11.330 1.00 9.10 ? 328 ASN A ND2 1 ATOM 1927 N N . TYR A 1 243 ? 17.980 5.082 6.925 1.00 6.68 ? 329 TYR A N 1 ATOM 1928 C CA . TYR A 1 243 ? 19.218 5.709 6.456 1.00 6.93 ? 329 TYR A CA 1 ATOM 1929 C C . TYR A 1 243 ? 19.024 7.182 6.052 1.00 5.90 ? 329 TYR A C 1 ATOM 1930 O O . TYR A 1 243 ? 19.984 7.854 5.720 1.00 6.91 ? 329 TYR A O 1 ATOM 1931 C CB . TYR A 1 243 ? 19.842 4.869 5.310 1.00 7.31 ? 329 TYR A CB 1 ATOM 1932 C CG . TYR A 1 243 ? 18.956 4.772 4.093 1.00 7.79 ? 329 TYR A CG 1 ATOM 1933 C CD1 . TYR A 1 243 ? 18.845 5.836 3.234 1.00 8.83 ? 329 TYR A CD1 1 ATOM 1934 C CD2 . TYR A 1 243 ? 18.208 3.619 3.827 1.00 10.98 ? 329 TYR A CD2 1 ATOM 1935 C CE1 . TYR A 1 243 ? 18.023 5.802 2.116 1.00 9.21 ? 329 TYR A CE1 1 ATOM 1936 C CE2 . TYR A 1 243 ? 17.372 3.569 2.704 1.00 11.94 ? 329 TYR A CE2 1 ATOM 1937 C CZ . TYR A 1 243 ? 17.283 4.683 1.858 1.00 11.66 ? 329 TYR A CZ 1 ATOM 1938 O OH . TYR A 1 243 ? 16.471 4.678 0.731 1.00 15.79 ? 329 TYR A OH 1 ATOM 1939 N N . ASP A 1 244 ? 17.784 7.641 6.081 1.00 6.22 ? 330 ASP A N 1 ATOM 1940 C CA . ASP A 1 244 ? 17.440 9.037 5.825 1.00 5.68 ? 330 ASP A CA 1 ATOM 1941 C C . ASP A 1 244 ? 16.336 9.443 6.810 1.00 5.65 ? 330 ASP A C 1 ATOM 1942 O O . ASP A 1 244 ? 15.803 8.595 7.560 1.00 5.92 ? 330 ASP A O 1 ATOM 1943 C CB . ASP A 1 244 ? 17.130 9.295 4.344 1.00 6.19 ? 330 ASP A CB 1 ATOM 1944 C CG . ASP A 1 244 ? 15.984 8.503 3.807 1.00 6.10 ? 330 ASP A CG 1 ATOM 1945 O OD1 . ASP A 1 244 ? 15.128 8.031 4.609 1.00 7.32 ? 330 ASP A OD1 1 ATOM 1946 O OD2 . ASP A 1 244 ? 15.867 8.364 2.556 1.00 8.07 ? 330 ASP A OD2 1 ATOM 1947 N N . GLU A 1 245 ? 16.010 10.732 6.811 1.00 4.25 ? 331 GLU A N 1 ATOM 1948 C CA . GLU A 1 245 ? 15.055 11.247 7.795 1.00 4.62 ? 331 GLU A CA 1 ATOM 1949 C C . GLU A 1 245 ? 13.640 10.753 7.507 1.00 4.81 ? 331 GLU A C 1 ATOM 1950 O O . GLU A 1 245 ? 12.853 10.527 8.447 1.00 5.16 ? 331 GLU A O 1 ATOM 1951 C CB . GLU A 1 245 ? 15.168 12.749 7.938 1.00 4.80 ? 331 GLU A CB 1 ATOM 1952 C CG . GLU A 1 245 ? 16.501 13.242 8.526 1.00 4.49 ? 331 GLU A CG 1 ATOM 1953 C CD . GLU A 1 245 ? 16.726 12.708 9.928 1.00 6.91 ? 331 GLU A CD 1 ATOM 1954 O OE1 . GLU A 1 245 ? 15.871 12.890 10.807 1.00 7.14 ? 331 GLU A OE1 1 ATOM 1955 O OE2 . GLU A 1 245 ? 17.774 12.056 10.161 1.00 7.33 ? 331 GLU A OE2 1 ATOM 1956 N N . LYS A 1 246 ? 13.279 10.594 6.229 1.00 5.41 ? 332 LYS A N 1 ATOM 1957 C CA . LYS A 1 246 ? 11.955 10.046 5.886 1.00 5.82 ? 332 LYS A CA 1 ATOM 1958 C C . LYS A 1 246 ? 11.774 8.658 6.500 1.00 6.29 ? 332 LYS A C 1 ATOM 1959 O O . LYS A 1 246 ? 10.756 8.351 7.087 1.00 5.88 ? 332 LYS A O 1 ATOM 1960 C CB . LYS A 1 246 ? 11.737 10.016 4.375 1.00 6.64 ? 332 LYS A CB 1 ATOM 1961 C CG . LYS A 1 246 ? 10.365 9.495 3.986 1.00 7.42 ? 332 LYS A CG 1 ATOM 1962 C CD . LYS A 1 246 ? 10.113 9.653 2.501 1.00 7.94 ? 332 LYS A CD 1 ATOM 1963 C CE . LYS A 1 246 ? 8.825 8.987 2.053 1.00 9.67 ? 332 LYS A CE 1 ATOM 1964 N NZ . LYS A 1 246 ? 8.849 7.512 2.191 1.00 11.03 ? 332 LYS A NZ 1 ATOM 1965 N N . HIS A 1 247 ? 12.771 7.787 6.343 1.00 5.49 ? 333 HIS A N 1 ATOM 1966 C CA . HIS A 1 247 ? 12.642 6.414 6.889 1.00 6.56 ? 333 HIS A CA 1 ATOM 1967 C C . HIS A 1 247 ? 12.483 6.498 8.430 1.00 6.11 ? 333 HIS A C 1 ATOM 1968 O O . HIS A 1 247 ? 11.698 5.795 9.031 1.00 6.04 ? 333 HIS A O 1 ATOM 1969 C CB . HIS A 1 247 ? 13.827 5.500 6.580 1.00 6.57 ? 333 HIS A CB 1 ATOM 1970 C CG . HIS A 1 247 ? 13.816 4.915 5.205 1.00 7.63 ? 333 HIS A CG 1 ATOM 1971 N ND1 . HIS A 1 247 ? 14.195 5.639 4.084 1.00 9.19 ? 333 HIS A ND1 1 ATOM 1972 C CD2 . HIS A 1 247 ? 13.537 3.656 4.783 1.00 9.61 ? 333 HIS A CD2 1 ATOM 1973 C CE1 . HIS A 1 247 ? 14.139 4.833 3.028 1.00 10.19 ? 333 HIS A CE1 1 ATOM 1974 N NE2 . HIS A 1 247 ? 13.717 3.639 3.417 1.00 10.02 ? 333 HIS A NE2 1 ATOM 1975 N N . TYR A 1 248 ? 13.319 7.296 9.077 1.00 5.58 ? 334 TYR A N 1 ATOM 1976 C CA . TYR A 1 248 ? 13.288 7.483 10.520 1.00 5.87 ? 334 TYR A CA 1 ATOM 1977 C C . TYR A 1 248 ? 11.913 7.941 10.980 1.00 5.91 ? 334 TYR A C 1 ATOM 1978 O O . TYR A 1 248 ? 11.316 7.313 11.858 1.00 5.40 ? 334 TYR A O 1 ATOM 1979 C CB . TYR A 1 248 ? 14.390 8.492 10.944 1.00 5.12 ? 334 TYR A CB 1 ATOM 1980 C CG . TYR A 1 248 ? 14.418 8.965 12.394 1.00 4.83 ? 334 TYR A CG 1 ATOM 1981 C CD1 . TYR A 1 248 ? 14.047 8.133 13.459 1.00 5.03 ? 334 TYR A CD1 1 ATOM 1982 C CD2 . TYR A 1 248 ? 14.844 10.237 12.698 1.00 5.81 ? 334 TYR A CD2 1 ATOM 1983 C CE1 . TYR A 1 248 ? 14.103 8.566 14.770 1.00 4.75 ? 334 TYR A CE1 1 ATOM 1984 C CE2 . TYR A 1 248 ? 14.931 10.679 14.007 1.00 6.21 ? 334 TYR A CE2 1 ATOM 1985 C CZ . TYR A 1 248 ? 14.542 9.835 15.050 1.00 5.19 ? 334 TYR A CZ 1 ATOM 1986 O OH . TYR A 1 248 ? 14.586 10.281 16.369 1.00 6.11 ? 334 TYR A OH 1 ATOM 1987 N N . ILE A 1 249 ? 11.410 9.017 10.400 1.00 5.47 ? 335 ILE A N 1 ATOM 1988 C CA . ILE A 1 249 ? 10.146 9.590 10.820 1.00 6.08 ? 335 ILE A CA 1 ATOM 1989 C C . ILE A 1 249 ? 8.992 8.618 10.589 1.00 6.53 ? 335 ILE A C 1 ATOM 1990 O O . ILE A 1 249 ? 8.092 8.479 11.443 1.00 6.25 ? 335 ILE A O 1 ATOM 1991 C CB . ILE A 1 249 ? 9.950 10.955 10.160 1.00 5.70 ? 335 ILE A CB 1 ATOM 1992 C CG1 . ILE A 1 249 ? 10.907 11.932 10.874 1.00 6.15 ? 335 ILE A CG1 1 ATOM 1993 C CG2 . ILE A 1 249 ? 8.501 11.419 10.223 1.00 8.99 ? 335 ILE A CG2 1 ATOM 1994 C CD1 . ILE A 1 249 ? 11.147 13.224 10.182 1.00 7.81 ? 335 ILE A CD1 1 ATOM 1995 N N . GLU A 1 250 ? 9.020 7.927 9.452 1.00 6.55 ? 336 GLU A N 1 ATOM 1996 C CA . GLU A 1 250 ? 7.948 6.954 9.162 1.00 6.36 ? 336 GLU A CA 1 ATOM 1997 C C . GLU A 1 250 ? 7.956 5.777 10.107 1.00 6.51 ? 336 GLU A C 1 ATOM 1998 O O . GLU A 1 250 ? 6.879 5.209 10.396 1.00 8.44 ? 336 GLU A O 1 ATOM 1999 C CB . GLU A 1 250 ? 7.968 6.495 7.696 1.00 6.24 ? 336 GLU A CB 1 ATOM 2000 C CG . GLU A 1 250 ? 7.525 7.641 6.780 1.00 7.52 ? 336 GLU A CG 1 ATOM 2001 C CD . GLU A 1 250 ? 7.460 7.352 5.291 1.00 10.39 ? 336 GLU A CD 1 ATOM 2002 O OE1 . GLU A 1 250 ? 8.112 6.414 4.863 1.00 10.66 ? 336 GLU A OE1 1 ATOM 2003 O OE2 . GLU A 1 250 ? 6.770 8.087 4.546 1.00 12.56 ? 336 GLU A OE2 1 ATOM 2004 N N . ALA A 1 251 ? 9.127 5.383 10.603 1.00 6.31 ? 337 ALA A N 1 ATOM 2005 C CA . ALA A 1 251 ? 9.205 4.333 11.631 1.00 6.35 ? 337 ALA A CA 1 ATOM 2006 C C . ALA A 1 251 ? 8.891 4.820 13.058 1.00 6.22 ? 337 ALA A C 1 ATOM 2007 O O . ALA A 1 251 ? 8.371 4.087 13.901 1.00 7.65 ? 337 ALA A O 1 ATOM 2008 C CB . ALA A 1 251 ? 10.587 3.701 11.603 1.00 7.33 ? 337 ALA A CB 1 ATOM 2009 N N . PHE A 1 252 ? 9.250 6.067 13.318 1.00 5.90 ? 338 PHE A N 1 ATOM 2010 C CA . PHE A 1 252 ? 9.165 6.688 14.640 1.00 6.27 ? 338 PHE A CA 1 ATOM 2011 C C . PHE A 1 252 ? 7.752 7.114 15.017 1.00 5.96 ? 338 PHE A C 1 ATOM 2012 O O . PHE A 1 252 ? 7.258 6.812 16.115 1.00 5.81 ? 338 PHE A O 1 ATOM 2013 C CB . PHE A 1 252 ? 10.103 7.908 14.616 1.00 7.09 ? 338 PHE A CB 1 ATOM 2014 C CG . PHE A 1 252 ? 10.507 8.435 15.944 1.00 6.21 ? 338 PHE A CG 1 ATOM 2015 C CD1 . PHE A 1 252 ? 10.384 7.673 17.074 1.00 6.31 ? 338 PHE A CD1 1 ATOM 2016 C CD2 . PHE A 1 252 ? 11.032 9.733 16.057 1.00 5.45 ? 338 PHE A CD2 1 ATOM 2017 C CE1 . PHE A 1 252 ? 10.756 8.148 18.294 1.00 5.66 ? 338 PHE A CE1 1 ATOM 2018 C CE2 . PHE A 1 252 ? 11.431 10.238 17.308 1.00 5.96 ? 338 PHE A CE2 1 ATOM 2019 C CZ . PHE A 1 252 ? 11.282 9.401 18.423 1.00 5.66 ? 338 PHE A CZ 1 ATOM 2020 N N . ARG A 1 253 ? 7.084 7.792 14.099 1.00 5.93 ? 339 ARG A N 1 ATOM 2021 C CA . ARG A 1 253 ? 5.751 8.340 14.377 1.00 5.82 ? 339 ARG A CA 1 ATOM 2022 C C . ARG A 1 253 ? 4.741 7.293 14.875 1.00 6.56 ? 339 ARG A C 1 ATOM 2023 O O . ARG A 1 253 ? 4.038 7.562 15.839 1.00 6.98 ? 339 ARG A O 1 ATOM 2024 C CB . ARG A 1 253 ? 5.222 9.086 13.158 1.00 6.68 ? 339 ARG A CB 1 ATOM 2025 C CG . ARG A 1 253 ? 3.735 9.479 13.241 1.00 7.40 ? 339 ARG A CG 1 ATOM 2026 C CD . ARG A 1 253 ? 3.349 10.373 14.423 1.00 7.84 ? 339 ARG A CD 1 ATOM 2027 N NE . ARG A 1 253 ? 1.908 10.609 14.300 1.00 7.90 ? 339 ARG A NE 1 ATOM 2028 C CZ . ARG A 1 253 ? 1.387 11.616 13.631 1.00 8.47 ? 339 ARG A CZ 1 ATOM 2029 N NH1 . ARG A 1 253 ? 2.135 12.620 13.202 1.00 8.86 ? 339 ARG A NH1 1 ATOM 2030 N NH2 . ARG A 1 253 ? 0.078 11.654 13.378 1.00 10.61 ? 339 ARG A NH2 1 ATOM 2031 N N . PRO A 1 254 ? 4.644 6.123 14.274 1.00 6.92 ? 340 PRO A N 1 ATOM 2032 C CA . PRO A 1 254 ? 3.663 5.150 14.798 1.00 6.63 ? 340 PRO A CA 1 ATOM 2033 C C . PRO A 1 254 ? 3.913 4.738 16.250 1.00 6.80 ? 340 PRO A C 1 ATOM 2034 O O . PRO A 1 254 ? 2.977 4.507 17.035 1.00 7.75 ? 340 PRO A O 1 ATOM 2035 C CB . PRO A 1 254 ? 3.758 3.956 13.838 1.00 7.64 ? 340 PRO A CB 1 ATOM 2036 C CG . PRO A 1 254 ? 4.532 4.433 12.690 1.00 11.25 ? 340 PRO A CG 1 ATOM 2037 C CD . PRO A 1 254 ? 5.284 5.669 13.035 1.00 7.16 ? 340 PRO A CD 1 ATOM 2038 N N . LEU A 1 255 ? 5.190 4.614 16.607 1.00 6.70 ? 341 LEU A N 1 ATOM 2039 C CA . LEU A 1 255 ? 5.557 4.241 17.967 1.00 7.34 ? 341 LEU A CA 1 ATOM 2040 C C . LEU A 1 255 ? 5.218 5.363 18.961 1.00 7.23 ? 341 LEU A C 1 ATOM 2041 O O . LEU A 1 255 ? 4.721 5.119 20.070 1.00 7.40 ? 341 LEU A O 1 ATOM 2042 C CB . LEU A 1 255 ? 7.046 3.923 18.057 1.00 8.95 ? 341 LEU A CB 1 ATOM 2043 C CG . LEU A 1 255 ? 7.527 2.775 17.130 1.00 11.60 ? 341 LEU A CG 1 ATOM 2044 C CD1 . LEU A 1 255 ? 9.086 2.757 17.045 1.00 13.48 ? 341 LEU A CD1 1 ATOM 2045 C CD2 . LEU A 1 255 ? 6.992 1.483 17.655 1.00 14.44 ? 341 LEU A CD2 1 ATOM 2046 N N . LEU A 1 256 ? 5.473 6.597 18.569 1.00 5.97 ? 342 LEU A N 1 ATOM 2047 C CA . LEU A 1 256 ? 5.122 7.756 19.395 1.00 5.92 ? 342 LEU A CA 1 ATOM 2048 C C . LEU A 1 256 ? 3.612 7.859 19.554 1.00 5.69 ? 342 LEU A C 1 ATOM 2049 O O . LEU A 1 256 ? 3.099 8.136 20.646 1.00 5.58 ? 342 LEU A O 1 ATOM 2050 C CB . LEU A 1 256 ? 5.656 9.057 18.759 1.00 5.34 ? 342 LEU A CB 1 ATOM 2051 C CG . LEU A 1 256 ? 7.164 9.254 18.809 1.00 5.36 ? 342 LEU A CG 1 ATOM 2052 C CD1 . LEU A 1 256 ? 7.643 10.131 17.646 1.00 5.16 ? 342 LEU A CD1 1 ATOM 2053 C CD2 . LEU A 1 256 ? 7.608 9.842 20.151 1.00 5.71 ? 342 LEU A CD2 1 ATOM 2054 N N . GLU A 1 257 ? 2.903 7.676 18.450 1.00 5.96 ? 343 GLU A N 1 ATOM 2055 C CA . GLU A 1 257 ? 1.436 7.836 18.427 1.00 6.45 ? 343 GLU A CA 1 ATOM 2056 C C . GLU A 1 257 ? 0.737 6.779 19.300 1.00 7.07 ? 343 GLU A C 1 ATOM 2057 O O . GLU A 1 257 ? -0.141 7.109 20.126 1.00 7.01 ? 343 GLU A O 1 ATOM 2058 C CB . GLU A 1 257 ? 0.924 7.842 17.007 1.00 7.19 ? 343 GLU A CB 1 ATOM 2059 C CG . GLU A 1 257 ? -0.601 8.000 16.936 1.00 8.93 ? 343 GLU A CG 1 ATOM 2060 C CD . GLU A 1 257 ? -1.089 8.553 15.631 1.00 14.49 ? 343 GLU A CD 1 ATOM 2061 O OE1 . GLU A 1 257 ? -0.303 8.790 14.667 1.00 11.56 ? 343 GLU A OE1 1 ATOM 2062 O OE2 . GLU A 1 257 ? -2.328 8.838 15.569 1.00 20.06 ? 343 GLU A OE2 1 ATOM 2063 N N . ALA A 1 258 ? 1.185 5.531 19.232 1.00 6.29 ? 344 ALA A N 1 ATOM 2064 C CA . ALA A 1 258 ? 0.647 4.504 20.117 1.00 6.85 ? 344 ALA A CA 1 ATOM 2065 C C . ALA A 1 258 ? 0.873 4.830 21.582 1.00 7.54 ? 344 ALA A C 1 ATOM 2066 O O . ALA A 1 258 ? 0.156 4.306 22.443 1.00 8.23 ? 344 ALA A O 1 ATOM 2067 C CB . ALA A 1 258 ? 1.229 3.117 19.807 1.00 7.40 ? 344 ALA A CB 1 ATOM 2068 N N . ARG A 1 259 ? 1.875 5.655 21.882 1.00 6.04 ? 345 ARG A N 1 ATOM 2069 C CA . ARG A 1 259 ? 2.224 6.036 23.213 1.00 7.44 ? 345 ARG A CA 1 ATOM 2070 C C . ARG A 1 259 ? 1.668 7.408 23.577 1.00 5.78 ? 345 ARG A C 1 ATOM 2071 O O . ARG A 1 259 ? 2.022 7.969 24.604 1.00 7.20 ? 345 ARG A O 1 ATOM 2072 C CB . ARG A 1 259 ? 3.733 5.920 23.402 1.00 6.94 ? 345 ARG A CB 1 ATOM 2073 C CG . ARG A 1 259 ? 4.185 4.489 23.337 1.00 7.10 ? 345 ARG A CG 1 ATOM 2074 C CD . ARG A 1 259 ? 5.677 4.263 23.226 1.00 8.60 ? 345 ARG A CD 1 ATOM 2075 N NE . ARG A 1 259 ? 5.925 2.813 23.210 1.00 10.09 ? 345 ARG A NE 1 ATOM 2076 C CZ . ARG A 1 259 ? 5.653 1.981 22.206 1.00 11.29 ? 345 ARG A CZ 1 ATOM 2077 N NH1 . ARG A 1 259 ? 5.248 2.439 21.024 1.00 11.07 ? 345 ARG A NH1 1 ATOM 2078 N NH2 . ARG A 1 259 ? 5.797 0.658 22.399 1.00 12.96 ? 345 ARG A NH2 1 ATOM 2079 N N . GLY A 1 260 ? 0.734 7.914 22.797 1.00 5.92 ? 346 GLY A N 1 ATOM 2080 C CA . GLY A 1 260 ? -0.003 9.123 23.146 1.00 5.58 ? 346 GLY A CA 1 ATOM 2081 C C . GLY A 1 260 ? 0.439 10.433 22.550 1.00 5.67 ? 346 GLY A C 1 ATOM 2082 O O . GLY A 1 260 ? -0.116 11.472 22.842 1.00 6.41 ? 346 GLY A O 1 ATOM 2083 N N . PHE A 1 261 ? 1.456 10.381 21.697 1.00 5.18 ? 347 PHE A N 1 ATOM 2084 C CA . PHE A 1 261 ? 2.100 11.605 21.160 1.00 5.78 ? 347 PHE A CA 1 ATOM 2085 C C . PHE A 1 261 ? 2.152 11.539 19.641 1.00 5.34 ? 347 PHE A C 1 ATOM 2086 O O . PHE A 1 261 ? 3.125 11.035 19.075 1.00 6.08 ? 347 PHE A O 1 ATOM 2087 C CB . PHE A 1 261 ? 3.508 11.712 21.778 1.00 6.31 ? 347 PHE A CB 1 ATOM 2088 C CG . PHE A 1 261 ? 4.265 12.984 21.454 1.00 5.58 ? 347 PHE A CG 1 ATOM 2089 C CD1 . PHE A 1 261 ? 3.647 14.106 20.955 1.00 6.07 ? 347 PHE A CD1 1 ATOM 2090 C CD2 . PHE A 1 261 ? 5.610 13.057 21.786 1.00 6.43 ? 347 PHE A CD2 1 ATOM 2091 C CE1 . PHE A 1 261 ? 4.379 15.279 20.723 1.00 5.39 ? 347 PHE A CE1 1 ATOM 2092 C CE2 . PHE A 1 261 ? 6.321 14.213 21.574 1.00 5.76 ? 347 PHE A CE2 1 ATOM 2093 C CZ . PHE A 1 261 ? 5.721 15.312 21.055 1.00 5.81 ? 347 PHE A CZ 1 ATOM 2094 N N . PRO A 1 262 ? 1.120 12.013 18.954 1.00 6.88 ? 348 PRO A N 1 ATOM 2095 C CA . PRO A 1 262 ? 1.095 12.004 17.490 1.00 6.89 ? 348 PRO A CA 1 ATOM 2096 C C . PRO A 1 262 ? 1.890 13.169 16.904 1.00 6.91 ? 348 PRO A C 1 ATOM 2097 O O . PRO A 1 262 ? 1.401 14.096 16.288 1.00 7.86 ? 348 PRO A O 1 ATOM 2098 C CB . PRO A 1 262 ? -0.378 12.078 17.147 1.00 8.66 ? 348 PRO A CB 1 ATOM 2099 C CG . PRO A 1 262 ? -0.937 12.862 18.274 1.00 8.83 ? 348 PRO A CG 1 ATOM 2100 C CD . PRO A 1 262 ? -0.181 12.423 19.514 1.00 8.29 ? 348 PRO A CD 1 ATOM 2101 N N . ALA A 1 263 ? 3.187 13.066 17.115 1.00 5.81 ? 349 ALA A N 1 ATOM 2102 C CA . ALA A 1 263 ? 4.100 14.175 16.842 1.00 5.56 ? 349 ALA A CA 1 ATOM 2103 C C . ALA A 1 263 ? 4.206 14.491 15.370 1.00 5.56 ? 349 ALA A C 1 ATOM 2104 O O . ALA A 1 263 ? 4.420 13.609 14.545 1.00 6.11 ? 349 ALA A O 1 ATOM 2105 C CB . ALA A 1 263 ? 5.479 13.802 17.362 1.00 5.34 ? 349 ALA A CB 1 ATOM 2106 N N . GLN A 1 264 ? 4.093 15.781 15.034 1.00 5.35 ? 350 GLN A N 1 ATOM 2107 C CA . GLN A 1 264 ? 4.510 16.272 13.752 1.00 5.49 ? 350 GLN A CA 1 ATOM 2108 C C . GLN A 1 264 ? 5.976 16.673 13.821 1.00 6.04 ? 350 GLN A C 1 ATOM 2109 O O . GLN A 1 264 ? 6.507 16.930 14.892 1.00 7.42 ? 350 GLN A O 1 ATOM 2110 C CB . GLN A 1 264 ? 3.662 17.480 13.342 1.00 6.25 ? 350 GLN A CB 1 ATOM 2111 C CG . GLN A 1 264 ? 2.243 17.079 13.078 1.00 5.50 ? 350 GLN A CG 1 ATOM 2112 C CD . GLN A 1 264 ? 2.024 16.300 11.768 1.00 6.61 ? 350 GLN A CD 1 ATOM 2113 O OE1 . GLN A 1 264 ? 1.725 15.102 11.796 1.00 10.22 ? 350 GLN A OE1 1 ATOM 2114 N NE2 . GLN A 1 264 ? 2.229 16.958 10.621 1.00 7.82 ? 350 GLN A NE2 1 ATOM 2115 N N . PHE A 1 265 ? 6.622 16.737 12.676 1.00 5.28 ? 351 PHE A N 1 ATOM 2116 C CA . PHE A 1 265 ? 8.090 16.927 12.622 1.00 4.93 ? 351 PHE A CA 1 ATOM 2117 C C . PHE A 1 265 ? 8.493 18.142 11.837 1.00 4.41 ? 351 PHE A C 1 ATOM 2118 O O . PHE A 1 265 ? 7.798 18.544 10.860 1.00 5.37 ? 351 PHE A O 1 ATOM 2119 C CB . PHE A 1 265 ? 8.768 15.704 11.988 1.00 5.97 ? 351 PHE A CB 1 ATOM 2120 C CG . PHE A 1 265 ? 8.724 14.490 12.864 1.00 5.77 ? 351 PHE A CG 1 ATOM 2121 C CD1 . PHE A 1 265 ? 7.586 13.706 12.952 1.00 6.11 ? 351 PHE A CD1 1 ATOM 2122 C CD2 . PHE A 1 265 ? 9.839 14.141 13.636 1.00 5.20 ? 351 PHE A CD2 1 ATOM 2123 C CE1 . PHE A 1 265 ? 7.550 12.600 13.814 1.00 6.98 ? 351 PHE A CE1 1 ATOM 2124 C CE2 . PHE A 1 265 ? 9.796 13.055 14.483 1.00 5.66 ? 351 PHE A CE2 1 ATOM 2125 C CZ . PHE A 1 265 ? 8.647 12.284 14.571 1.00 5.49 ? 351 PHE A CZ 1 ATOM 2126 N N . ILE A 1 266 ? 9.622 18.711 12.259 1.00 4.55 ? 352 ILE A N 1 ATOM 2127 C CA . ILE A 1 266 ? 10.371 19.596 11.377 1.00 4.05 ? 352 ILE A CA 1 ATOM 2128 C C . ILE A 1 266 ? 11.744 18.987 11.201 1.00 4.53 ? 352 ILE A C 1 ATOM 2129 O O . ILE A 1 266 ? 12.252 18.362 12.121 1.00 5.15 ? 352 ILE A O 1 ATOM 2130 C CB . ILE A 1 266 ? 10.451 21.075 11.810 1.00 4.93 ? 352 ILE A CB 1 ATOM 2131 C CG1 . ILE A 1 266 ? 11.133 21.214 13.179 1.00 5.28 ? 352 ILE A CG1 1 ATOM 2132 C CG2 . ILE A 1 266 ? 9.042 21.665 11.852 1.00 5.47 ? 352 ILE A CG2 1 ATOM 2133 C CD1 . ILE A 1 266 ? 11.231 22.678 13.652 1.00 5.81 ? 352 ILE A CD1 1 ATOM 2134 N N . VAL A 1 267 ? 12.301 19.149 10.002 1.00 4.24 ? 353 VAL A N 1 ATOM 2135 C CA . VAL A 1 267 ? 13.559 18.468 9.649 1.00 4.79 ? 353 VAL A CA 1 ATOM 2136 C C . VAL A 1 267 ? 14.556 19.493 9.149 1.00 5.30 ? 353 VAL A C 1 ATOM 2137 O O . VAL A 1 267 ? 14.282 20.205 8.159 1.00 4.71 ? 353 VAL A O 1 ATOM 2138 C CB . VAL A 1 267 ? 13.340 17.353 8.581 1.00 4.82 ? 353 VAL A CB 1 ATOM 2139 C CG1 . VAL A 1 267 ? 14.639 16.672 8.221 1.00 5.51 ? 353 VAL A CG1 1 ATOM 2140 C CG2 . VAL A 1 267 ? 12.309 16.315 9.004 1.00 4.89 ? 353 VAL A CG2 1 ATOM 2141 N N . ASP A 1 268 ? 15.711 19.580 9.820 1.00 4.62 ? 354 ASP A N 1 ATOM 2142 C CA . ASP A 1 268 ? 16.772 20.477 9.336 1.00 4.25 ? 354 ASP A CA 1 ATOM 2143 C C . ASP A 1 268 ? 17.295 19.941 8.014 1.00 4.52 ? 354 ASP A C 1 ATOM 2144 O O . ASP A 1 268 ? 17.568 18.748 7.892 1.00 4.16 ? 354 ASP A O 1 ATOM 2145 C CB . ASP A 1 268 ? 17.911 20.468 10.366 1.00 4.43 ? 354 ASP A CB 1 ATOM 2146 C CG . ASP A 1 268 ? 18.828 21.664 10.298 1.00 4.75 ? 354 ASP A CG 1 ATOM 2147 O OD1 . ASP A 1 268 ? 18.795 22.442 9.321 1.00 5.17 ? 354 ASP A OD1 1 ATOM 2148 O OD2 . ASP A 1 268 ? 19.642 21.876 11.245 1.00 4.61 ? 354 ASP A OD2 1 ATOM 2149 N N . GLN A 1 269 ? 17.395 20.837 7.031 1.00 4.31 ? 355 GLN A N 1 ATOM 2150 C CA . GLN A 1 269 ? 18.004 20.533 5.745 1.00 5.17 ? 355 GLN A CA 1 ATOM 2151 C C . GLN A 1 269 ? 19.020 21.609 5.350 1.00 4.29 ? 355 GLN A C 1 ATOM 2152 O O . GLN A 1 269 ? 19.496 21.624 4.197 1.00 5.24 ? 355 GLN A O 1 ATOM 2153 C CB . GLN A 1 269 ? 16.965 20.370 4.621 1.00 5.02 ? 355 GLN A CB 1 ATOM 2154 C CG . GLN A 1 269 ? 16.051 19.112 4.773 1.00 4.98 ? 355 GLN A CG 1 ATOM 2155 C CD . GLN A 1 269 ? 16.863 17.846 4.434 1.00 6.59 ? 355 GLN A CD 1 ATOM 2156 O OE1 . GLN A 1 269 ? 17.090 17.598 3.259 1.00 8.02 ? 355 GLN A OE1 1 ATOM 2157 N NE2 . GLN A 1 269 ? 17.338 17.096 5.440 1.00 6.85 ? 355 GLN A NE2 1 ATOM 2158 N N . GLY A 1 270 ? 19.406 22.455 6.296 1.00 4.62 ? 356 GLY A N 1 ATOM 2159 C CA . GLY A 1 270 ? 20.311 23.549 5.990 1.00 4.48 ? 356 GLY A CA 1 ATOM 2160 C C . GLY A 1 270 ? 21.711 23.190 5.505 1.00 4.78 ? 356 GLY A C 1 ATOM 2161 O O . GLY A 1 270 ? 22.343 23.986 4.816 1.00 5.07 ? 356 GLY A O 1 ATOM 2162 N N . ARG A 1 271 ? 22.152 21.965 5.794 1.00 3.74 ? 357 ARG A N 1 ATOM 2163 C CA . ARG A 1 271 ? 23.441 21.446 5.326 1.00 3.72 ? 357 ARG A CA 1 ATOM 2164 C C . ARG A 1 271 ? 23.296 20.058 4.720 1.00 5.04 ? 357 ARG A C 1 ATOM 2165 O O . ARG A 1 271 ? 24.237 19.281 4.709 1.00 4.43 ? 357 ARG A O 1 ATOM 2166 C CB . ARG A 1 271 ? 24.534 21.523 6.409 1.00 4.23 ? 357 ARG A CB 1 ATOM 2167 C CG . ARG A 1 271 ? 24.712 22.894 7.007 1.00 5.54 ? 357 ARG A CG 1 ATOM 2168 C CD . ARG A 1 271 ? 25.923 23.000 7.913 1.00 5.58 ? 357 ARG A CD 1 ATOM 2169 N NE . ARG A 1 271 ? 25.751 22.248 9.150 1.00 4.81 ? 357 ARG A NE 1 ATOM 2170 C CZ . ARG A 1 271 ? 26.699 22.091 10.048 1.00 5.32 ? 357 ARG A CZ 1 ATOM 2171 N NH1 . ARG A 1 271 ? 27.891 22.659 9.825 1.00 7.35 ? 357 ARG A NH1 1 ATOM 2172 N NH2 . ARG A 1 271 ? 26.461 21.344 11.126 1.00 4.80 ? 357 ARG A NH2 1 ATOM 2173 N N . SER A 1 272 ? 22.161 19.815 4.097 1.00 4.73 ? 358 SER A N 1 ATOM 2174 C CA . SER A 1 272 ? 21.801 18.507 3.545 1.00 5.34 ? 358 SER A CA 1 ATOM 2175 C C . SER A 1 272 ? 21.686 18.433 2.018 1.00 5.47 ? 358 SER A C 1 ATOM 2176 O O . SER A 1 272 ? 21.299 17.387 1.472 1.00 5.41 ? 358 SER A O 1 ATOM 2177 C CB . SER A 1 272 ? 20.416 18.104 4.108 1.00 4.69 ? 358 SER A CB 1 ATOM 2178 O OG . SER A 1 272 ? 20.508 17.825 5.505 1.00 5.75 ? 358 SER A OG 1 ATOM 2179 N N . GLY A 1 273 ? 22.024 19.505 1.297 1.00 5.64 ? 359 GLY A N 1 ATOM 2180 C CA . GLY A 1 273 ? 21.758 19.494 -0.134 1.00 6.29 ? 359 GLY A CA 1 ATOM 2181 C C . GLY A 1 273 ? 22.600 18.511 -0.929 1.00 6.03 ? 359 GLY A C 1 ATOM 2182 O O . GLY A 1 273 ? 22.135 18.007 -1.958 1.00 7.17 ? 359 GLY A O 1 ATOM 2183 N N . LYS A 1 274 ? 23.805 18.206 -0.476 1.00 5.67 ? 360 LYS A N 1 ATOM 2184 C CA . LYS A 1 274 ? 24.687 17.234 -1.163 1.00 6.24 ? 360 LYS A CA 1 ATOM 2185 C C . LYS A 1 274 ? 24.593 15.883 -0.449 1.00 5.68 ? 360 LYS A C 1 ATOM 2186 O O . LYS A 1 274 ? 24.855 15.776 0.763 1.00 5.71 ? 360 LYS A O 1 ATOM 2187 C CB . LYS A 1 274 ? 26.121 17.694 -1.161 1.00 6.63 ? 360 LYS A CB 1 ATOM 2188 C CG . LYS A 1 274 ? 27.036 16.692 -1.856 1.00 8.20 ? 360 LYS A CG 1 ATOM 2189 C CD . LYS A 1 274 ? 28.426 17.240 -2.035 1.00 9.24 ? 360 LYS A CD 1 ATOM 2190 C CE . LYS A 1 274 ? 29.431 16.126 -2.276 1.00 9.46 ? 360 LYS A CE 1 ATOM 2191 N NZ . LYS A 1 274 ? 29.546 15.177 -1.109 1.00 10.58 ? 360 LYS A NZ 1 ATOM 2192 N N . GLN A 1 275 ? 24.227 14.849 -1.200 1.00 6.21 ? 361 GLN A N 1 ATOM 2193 C CA . GLN A 1 275 ? 24.104 13.491 -0.674 1.00 6.25 ? 361 GLN A CA 1 ATOM 2194 C C . GLN A 1 275 ? 24.758 12.508 -1.657 1.00 7.04 ? 361 GLN A C 1 ATOM 2195 O O . GLN A 1 275 ? 24.530 12.636 -2.865 1.00 8.82 ? 361 GLN A O 1 ATOM 2196 C CB . GLN A 1 275 ? 22.631 13.107 -0.487 1.00 6.41 ? 361 GLN A CB 1 ATOM 2197 C CG . GLN A 1 275 ? 21.899 13.941 0.515 1.00 6.46 ? 361 GLN A CG 1 ATOM 2198 C CD . GLN A 1 275 ? 22.423 13.821 1.918 1.00 5.65 ? 361 GLN A CD 1 ATOM 2199 O OE1 . GLN A 1 275 ? 22.956 12.769 2.303 1.00 7.40 ? 361 GLN A OE1 1 ATOM 2200 N NE2 . GLN A 1 275 ? 22.210 14.876 2.724 1.00 5.31 ? 361 GLN A NE2 1 ATOM 2201 N N . PRO A 1 276 ? 25.565 11.570 -1.182 1.00 7.08 ? 362 PRO A N 1 ATOM 2202 C CA . PRO A 1 276 ? 26.044 11.470 0.199 1.00 7.39 ? 362 PRO A CA 1 ATOM 2203 C C . PRO A 1 276 ? 26.964 12.661 0.501 1.00 6.37 ? 362 PRO A C 1 ATOM 2204 O O . PRO A 1 276 ? 27.396 13.398 -0.387 1.00 7.12 ? 362 PRO A O 1 ATOM 2205 C CB . PRO A 1 276 ? 26.843 10.163 0.189 1.00 8.37 ? 362 PRO A CB 1 ATOM 2206 C CG . PRO A 1 276 ? 27.279 9.978 -1.166 1.00 12.18 ? 362 PRO A CG 1 ATOM 2207 C CD . PRO A 1 276 ? 26.235 10.560 -2.038 1.00 8.84 ? 362 PRO A CD 1 ATOM 2208 N N . THR A 1 277 ? 27.244 12.865 1.773 1.00 6.72 ? 363 THR A N 1 ATOM 2209 C CA . THR A 1 277 ? 28.136 13.910 2.222 1.00 5.80 ? 363 THR A CA 1 ATOM 2210 C C . THR A 1 277 ? 29.597 13.418 2.132 1.00 6.17 ? 363 THR A C 1 ATOM 2211 O O . THR A 1 277 ? 29.853 12.282 1.717 1.00 6.63 ? 363 THR A O 1 ATOM 2212 C CB . THR A 1 277 ? 27.855 14.284 3.670 1.00 6.70 ? 363 THR A CB 1 ATOM 2213 O OG1 . THR A 1 277 ? 28.245 13.200 4.502 1.00 6.76 ? 363 THR A OG1 1 ATOM 2214 C CG2 . THR A 1 277 ? 26.404 14.584 3.877 1.00 7.22 ? 363 THR A CG2 1 ATOM 2215 N N . GLY A 1 278 ? 30.522 14.243 2.611 1.00 5.75 ? 364 GLY A N 1 ATOM 2216 C CA . GLY A 1 278 ? 31.931 13.838 2.774 1.00 6.17 ? 364 GLY A CA 1 ATOM 2217 C C . GLY A 1 278 ? 32.255 13.261 4.142 1.00 5.76 ? 364 GLY A C 1 ATOM 2218 O O . GLY A 1 278 ? 33.433 13.034 4.477 1.00 7.02 ? 364 GLY A O 1 ATOM 2219 N N . GLN A 1 279 ? 31.244 12.970 4.942 1.00 5.57 ? 365 GLN A N 1 ATOM 2220 C CA . GLN A 1 279 ? 31.490 12.276 6.221 1.00 5.96 ? 365 GLN A CA 1 ATOM 2221 C C . GLN A 1 279 ? 32.043 10.887 5.976 1.00 6.51 ? 365 GLN A C 1 ATOM 2222 O O . GLN A 1 279 ? 31.534 10.143 5.135 1.00 7.87 ? 365 GLN A O 1 ATOM 2223 C CB . GLN A 1 279 ? 30.172 12.130 6.987 1.00 6.05 ? 365 GLN A CB 1 ATOM 2224 C CG . GLN A 1 279 ? 29.602 13.453 7.518 1.00 7.17 ? 365 GLN A CG 1 ATOM 2225 C CD . GLN A 1 279 ? 28.137 13.293 7.923 1.00 6.19 ? 365 GLN A CD 1 ATOM 2226 O OE1 . GLN A 1 279 ? 27.264 13.182 7.054 1.00 6.38 ? 365 GLN A OE1 1 ATOM 2227 N NE2 . GLN A 1 279 ? 27.850 13.258 9.257 1.00 6.93 ? 365 GLN A NE2 1 ATOM 2228 N N . LYS A 1 280 ? 33.085 10.533 6.723 1.00 6.68 ? 366 LYS A N 1 ATOM 2229 C CA . LYS A 1 280 ? 33.609 9.173 6.675 1.00 7.19 ? 366 LYS A CA 1 ATOM 2230 C C . LYS A 1 280 ? 32.860 8.199 7.575 1.00 6.59 ? 366 LYS A C 1 ATOM 2231 O O . LYS A 1 280 ? 32.814 6.969 7.351 1.00 8.59 ? 366 LYS A O 1 ATOM 2232 C CB . LYS A 1 280 ? 35.101 9.220 7.011 1.00 8.45 ? 366 LYS A CB 1 ATOM 2233 C CG . LYS A 1 280 ? 35.894 9.895 5.942 1.00 13.44 ? 366 LYS A CG 1 ATOM 2234 C CD . LYS A 1 280 ? 35.972 9.041 4.714 1.00 20.59 ? 366 LYS A CD 1 ATOM 2235 C CE . LYS A 1 280 ? 37.313 8.331 4.631 1.00 27.10 ? 366 LYS A CE 1 ATOM 2236 N NZ . LYS A 1 280 ? 38.297 9.443 4.324 1.00 31.80 ? 366 LYS A NZ 1 ATOM 2237 N N . GLU A 1 281 ? 32.257 8.758 8.621 1.00 6.62 ? 367 GLU A N 1 ATOM 2238 C CA . GLU A 1 281 ? 31.424 8.026 9.564 1.00 6.39 ? 367 GLU A CA 1 ATOM 2239 C C . GLU A 1 281 ? 30.229 8.913 9.912 1.00 5.91 ? 367 GLU A C 1 ATOM 2240 O O . GLU A 1 281 ? 30.319 10.143 9.907 1.00 6.28 ? 367 GLU A O 1 ATOM 2241 C CB . GLU A 1 281 ? 32.167 7.654 10.838 1.00 6.75 ? 367 GLU A CB 1 ATOM 2242 C CG . GLU A 1 281 ? 33.449 6.868 10.658 1.00 7.84 ? 367 GLU A CG 1 ATOM 2243 C CD . GLU A 1 281 ? 33.282 5.483 10.084 1.00 8.39 ? 367 GLU A CD 1 ATOM 2244 O OE1 . GLU A 1 281 ? 32.157 4.901 10.038 1.00 9.21 ? 367 GLU A OE1 1 ATOM 2245 O OE2 . GLU A 1 281 ? 34.352 4.922 9.696 1.00 9.67 ? 367 GLU A OE2 1 ATOM 2246 N N . TRP A 1 282 ? 29.102 8.291 10.217 1.00 6.04 ? 368 TRP A N 1 ATOM 2247 C CA . TRP A 1 282 ? 27.851 9.043 10.480 1.00 6.50 ? 368 TRP A CA 1 ATOM 2248 C C . TRP A 1 282 ? 27.914 9.964 11.689 1.00 5.85 ? 368 TRP A C 1 ATOM 2249 O O . TRP A 1 282 ? 27.315 11.026 11.702 1.00 6.86 ? 368 TRP A O 1 ATOM 2250 C CB . TRP A 1 282 ? 26.708 8.047 10.626 1.00 5.64 ? 368 TRP A CB 1 ATOM 2251 C CG . TRP A 1 282 ? 25.360 8.533 10.177 1.00 6.00 ? 368 TRP A CG 1 ATOM 2252 C CD1 . TRP A 1 282 ? 24.989 9.800 9.867 1.00 7.29 ? 368 TRP A CD1 1 ATOM 2253 C CD2 . TRP A 1 282 ? 24.205 7.728 10.034 1.00 5.23 ? 368 TRP A CD2 1 ATOM 2254 N NE1 . TRP A 1 282 ? 23.664 9.823 9.474 1.00 6.04 ? 368 TRP A NE1 1 ATOM 2255 C CE2 . TRP A 1 282 ? 23.165 8.553 9.579 1.00 5.77 ? 368 TRP A CE2 1 ATOM 2256 C CE3 . TRP A 1 282 ? 23.958 6.349 10.183 1.00 7.59 ? 368 TRP A CE3 1 ATOM 2257 C CZ2 . TRP A 1 282 ? 21.894 8.060 9.278 1.00 6.14 ? 368 TRP A CZ2 1 ATOM 2258 C CZ3 . TRP A 1 282 ? 22.684 5.874 9.906 1.00 6.77 ? 368 TRP A CZ3 1 ATOM 2259 C CH2 . TRP A 1 282 ? 21.672 6.734 9.474 1.00 7.81 ? 368 TRP A CH2 1 ATOM 2260 N N . GLY A 1 283 ? 28.678 9.558 12.690 1.00 6.24 ? 369 GLY A N 1 ATOM 2261 C CA . GLY A 1 283 ? 28.862 10.309 13.901 1.00 6.66 ? 369 GLY A CA 1 ATOM 2262 C C . GLY A 1 283 ? 29.831 11.471 13.845 1.00 6.80 ? 369 GLY A C 1 ATOM 2263 O O . GLY A 1 283 ? 30.097 12.112 14.859 1.00 8.69 ? 369 GLY A O 1 ATOM 2264 N N . HIS A 1 284 ? 30.383 11.759 12.664 1.00 6.63 ? 370 HIS A N 1 ATOM 2265 C CA . HIS A 1 284 ? 31.306 12.877 12.444 1.00 6.75 ? 370 HIS A CA 1 ATOM 2266 C C . HIS A 1 284 ? 30.464 14.093 12.100 1.00 6.38 ? 370 HIS A C 1 ATOM 2267 O O . HIS A 1 284 ? 30.053 14.304 10.975 1.00 7.41 ? 370 HIS A O 1 ATOM 2268 C CB . HIS A 1 284 ? 32.276 12.544 11.331 1.00 6.76 ? 370 HIS A CB 1 ATOM 2269 C CG . HIS A 1 284 ? 33.236 11.438 11.673 1.00 7.09 ? 370 HIS A CG 1 ATOM 2270 N ND1 . HIS A 1 284 ? 34.218 11.021 10.802 1.00 8.49 ? 370 HIS A ND1 1 ATOM 2271 C CD2 . HIS A 1 284 ? 33.346 10.654 12.769 1.00 7.96 ? 370 HIS A CD2 1 ATOM 2272 C CE1 . HIS A 1 284 ? 34.928 10.064 11.380 1.00 7.72 ? 370 HIS A CE1 1 ATOM 2273 N NE2 . HIS A 1 284 ? 34.403 9.798 12.560 1.00 6.98 ? 370 HIS A NE2 1 ATOM 2274 N N . TRP A 1 285 ? 30.145 14.845 13.121 1.00 5.69 ? 371 TRP A N 1 ATOM 2275 C CA . TRP A 1 285 ? 29.258 15.990 13.029 1.00 5.71 ? 371 TRP A CA 1 ATOM 2276 C C . TRP A 1 285 ? 29.903 17.342 12.876 1.00 6.13 ? 371 TRP A C 1 ATOM 2277 O O . TRP A 1 285 ? 29.185 18.318 12.567 1.00 6.81 ? 371 TRP A O 1 ATOM 2278 C CB . TRP A 1 285 ? 28.316 16.086 14.287 1.00 6.13 ? 371 TRP A CB 1 ATOM 2279 C CG . TRP A 1 285 ? 29.038 16.064 15.578 1.00 6.23 ? 371 TRP A CG 1 ATOM 2280 C CD1 . TRP A 1 285 ? 29.266 14.946 16.380 1.00 8.27 ? 371 TRP A CD1 1 ATOM 2281 C CD2 . TRP A 1 285 ? 29.706 17.147 16.221 1.00 7.58 ? 371 TRP A CD2 1 ATOM 2282 N NE1 . TRP A 1 285 ? 29.994 15.300 17.487 1.00 8.76 ? 371 TRP A NE1 1 ATOM 2283 C CE2 . TRP A 1 285 ? 30.269 16.643 17.418 1.00 5.49 ? 371 TRP A CE2 1 ATOM 2284 C CE3 . TRP A 1 285 ? 29.832 18.515 15.946 1.00 8.57 ? 371 TRP A CE3 1 ATOM 2285 C CZ2 . TRP A 1 285 ? 31.014 17.461 18.299 1.00 7.53 ? 371 TRP A CZ2 1 ATOM 2286 C CZ3 . TRP A 1 285 ? 30.555 19.310 16.790 1.00 7.47 ? 371 TRP A CZ3 1 ATOM 2287 C CH2 . TRP A 1 285 ? 31.127 18.780 17.977 1.00 8.20 ? 371 TRP A CH2 1 ATOM 2288 N N . CYS A 1 286 ? 31.203 17.455 13.127 1.00 6.21 ? 372 CYS A N 1 ATOM 2289 C CA . CYS A 1 286 ? 31.827 18.776 13.186 1.00 6.18 ? 372 CYS A CA 1 ATOM 2290 C C . CYS A 1 286 ? 32.360 19.292 11.853 1.00 6.04 ? 372 CYS A C 1 ATOM 2291 O O . CYS A 1 286 ? 33.249 18.662 11.279 1.00 6.49 ? 372 CYS A O 1 ATOM 2292 C CB . CYS A 1 286 ? 32.960 18.787 14.203 1.00 6.01 ? 372 CYS A CB 1 ATOM 2293 S SG . CYS A 1 286 ? 33.548 20.469 14.473 1.00 7.15 ? 372 CYS A SG 1 ATOM 2294 N N . ASN A 1 287 ? 31.785 20.379 11.344 1.00 5.62 ? 373 ASN A N 1 ATOM 2295 C CA . ASN A 1 287 ? 32.299 21.062 10.162 1.00 5.21 ? 373 ASN A CA 1 ATOM 2296 C C . ASN A 1 287 ? 32.573 20.072 9.022 1.00 5.74 ? 373 ASN A C 1 ATOM 2297 O O . ASN A 1 287 ? 33.627 20.081 8.387 1.00 5.99 ? 373 ASN A O 1 ATOM 2298 C CB . ASN A 1 287 ? 33.589 21.846 10.491 1.00 5.27 ? 373 ASN A CB 1 ATOM 2299 C CG . ASN A 1 287 ? 33.407 22.869 11.581 1.00 5.46 ? 373 ASN A CG 1 ATOM 2300 O OD1 . ASN A 1 287 ? 32.329 23.508 11.722 1.00 6.53 ? 373 ASN A OD1 1 ATOM 2301 N ND2 . ASN A 1 287 ? 34.453 22.984 12.433 1.00 6.33 ? 373 ASN A ND2 1 ATOM 2302 N N . ALA A 1 288 ? 31.626 19.191 8.734 1.00 5.57 ? 374 ALA A N 1 ATOM 2303 C CA . ALA A 1 288 ? 31.872 18.093 7.801 1.00 4.98 ? 374 ALA A CA 1 ATOM 2304 C C . ALA A 1 288 ? 32.084 18.581 6.380 1.00 5.79 ? 374 ALA A C 1 ATOM 2305 O O . ALA A 1 288 ? 31.377 19.429 5.865 1.00 5.04 ? 374 ALA A O 1 ATOM 2306 C CB . ALA A 1 288 ? 30.744 17.112 7.836 1.00 6.15 ? 374 ALA A CB 1 ATOM 2307 N N . ILE A 1 289 ? 33.124 18.030 5.772 1.00 6.06 ? 375 ILE A N 1 ATOM 2308 C CA . ILE A 1 289 ? 33.391 18.356 4.361 1.00 6.47 ? 375 ILE A CA 1 ATOM 2309 C C . ILE A 1 289 ? 32.353 17.737 3.426 1.00 7.03 ? 375 ILE A C 1 ATOM 2310 O O . ILE A 1 289 ? 31.615 16.834 3.762 1.00 6.05 ? 375 ILE A O 1 ATOM 2311 C CB . ILE A 1 289 ? 34.847 17.956 3.950 1.00 6.66 ? 375 ILE A CB 1 ATOM 2312 C CG1 . ILE A 1 289 ? 35.060 16.452 4.026 1.00 8.29 ? 375 ILE A CG1 1 ATOM 2313 C CG2 . ILE A 1 289 ? 35.836 18.756 4.772 1.00 7.06 ? 375 ILE A CG2 1 ATOM 2314 C CD1 . ILE A 1 289 ? 36.499 15.995 3.600 1.00 9.41 ? 375 ILE A CD1 1 ATOM 2315 N N . GLY A 1 290 ? 32.336 18.239 2.211 1.00 7.64 ? 376 GLY A N 1 ATOM 2316 C CA . GLY A 1 290 ? 31.484 17.662 1.215 1.00 6.57 ? 376 GLY A CA 1 ATOM 2317 C C . GLY A 1 290 ? 29.999 17.795 1.476 1.00 6.19 ? 376 GLY A C 1 ATOM 2318 O O . GLY A 1 290 ? 29.227 16.881 1.140 1.00 6.12 ? 376 GLY A O 1 ATOM 2319 N N . THR A 1 291 ? 29.614 18.927 2.057 1.00 6.60 ? 377 THR A N 1 ATOM 2320 C CA . THR A 1 291 ? 28.211 19.233 2.298 1.00 5.55 ? 377 THR A CA 1 ATOM 2321 C C . THR A 1 291 ? 27.805 20.500 1.599 1.00 5.76 ? 377 THR A C 1 ATOM 2322 O O . THR A 1 291 ? 28.643 21.363 1.311 1.00 5.54 ? 377 THR A O 1 ATOM 2323 C CB . THR A 1 291 ? 27.937 19.396 3.807 1.00 5.66 ? 377 THR A CB 1 ATOM 2324 O OG1 . THR A 1 291 ? 28.714 20.511 4.288 1.00 6.18 ? 377 THR A OG1 1 ATOM 2325 C CG2 . THR A 1 291 ? 28.336 18.134 4.605 1.00 7.23 ? 377 THR A CG2 1 ATOM 2326 N N . GLY A 1 292 ? 26.507 20.625 1.373 1.00 5.65 ? 378 GLY A N 1 ATOM 2327 C CA . GLY A 1 292 ? 25.913 21.775 0.704 1.00 4.61 ? 378 GLY A CA 1 ATOM 2328 C C . GLY A 1 292 ? 24.662 22.317 1.379 1.00 4.81 ? 378 GLY A C 1 ATOM 2329 O O . GLY A 1 292 ? 23.942 21.578 2.045 1.00 5.36 ? 378 GLY A O 1 ATOM 2330 N N . PHE A 1 293 ? 24.402 23.594 1.183 1.00 5.18 ? 379 PHE A N 1 ATOM 2331 C CA . PHE A 1 293 ? 23.094 24.164 1.503 1.00 5.15 ? 379 PHE A CA 1 ATOM 2332 C C . PHE A 1 293 ? 22.012 23.314 0.849 1.00 6.00 ? 379 PHE A C 1 ATOM 2333 O O . PHE A 1 293 ? 22.175 22.894 -0.282 1.00 5.97 ? 379 PHE A O 1 ATOM 2334 C CB . PHE A 1 293 ? 22.917 25.614 1.004 1.00 6.66 ? 379 PHE A CB 1 ATOM 2335 C CG . PHE A 1 293 ? 23.675 26.649 1.797 1.00 6.83 ? 379 PHE A CG 1 ATOM 2336 C CD1 . PHE A 1 293 ? 23.448 26.796 3.173 1.00 6.23 ? 379 PHE A CD1 1 ATOM 2337 C CD2 . PHE A 1 293 ? 24.633 27.457 1.214 1.00 6.84 ? 379 PHE A CD2 1 ATOM 2338 C CE1 . PHE A 1 293 ? 24.128 27.738 3.924 1.00 6.37 ? 379 PHE A CE1 1 ATOM 2339 C CE2 . PHE A 1 293 ? 25.337 28.384 1.973 1.00 7.35 ? 379 PHE A CE2 1 ATOM 2340 C CZ . PHE A 1 293 ? 25.075 28.537 3.324 1.00 6.83 ? 379 PHE A CZ 1 ATOM 2341 N N . GLY A 1 294 ? 20.946 23.022 1.563 1.00 5.91 ? 380 GLY A N 1 ATOM 2342 C CA . GLY A 1 294 ? 19.895 22.148 1.047 1.00 6.30 ? 380 GLY A CA 1 ATOM 2343 C C . GLY A 1 294 ? 18.565 22.790 0.730 1.00 7.05 ? 380 GLY A C 1 ATOM 2344 O O . GLY A 1 294 ? 18.480 23.998 0.457 1.00 7.23 ? 380 GLY A O 1 ATOM 2345 N N A MET A 1 295 ? 17.517 21.979 0.777 0.65 7.61 ? 381 MET A N 1 ATOM 2346 N N B MET A 1 295 ? 17.525 21.959 0.767 0.35 7.58 ? 381 MET A N 1 ATOM 2347 C CA A MET A 1 295 ? 16.239 22.500 0.322 0.65 9.13 ? 381 MET A CA 1 ATOM 2348 C CA B MET A 1 295 ? 16.157 22.386 0.461 0.35 8.68 ? 381 MET A CA 1 ATOM 2349 C C A MET A 1 295 ? 15.789 23.653 1.199 0.65 8.50 ? 381 MET A C 1 ATOM 2350 C C B MET A 1 295 ? 15.779 23.651 1.220 0.35 8.39 ? 381 MET A C 1 ATOM 2351 O O A MET A 1 295 ? 16.038 23.703 2.401 0.65 7.92 ? 381 MET A O 1 ATOM 2352 O O B MET A 1 295 ? 16.025 23.753 2.412 0.35 8.06 ? 381 MET A O 1 ATOM 2353 C CB A MET A 1 295 ? 15.203 21.429 0.281 0.65 10.20 ? 381 MET A CB 1 ATOM 2354 C CB B MET A 1 295 ? 15.192 21.287 0.859 0.35 9.26 ? 381 MET A CB 1 ATOM 2355 C CG A MET A 1 295 ? 15.105 20.632 1.557 0.65 11.17 ? 381 MET A CG 1 ATOM 2356 C CG B MET A 1 295 ? 15.080 20.180 -0.197 0.35 11.02 ? 381 MET A CG 1 ATOM 2357 S SD A MET A 1 295 ? 13.688 19.534 1.580 0.65 14.86 ? 381 MET A SD 1 ATOM 2358 S SD B MET A 1 295 ? 13.674 19.077 0.024 0.35 16.82 ? 381 MET A SD 1 ATOM 2359 C CE A MET A 1 295 ? 13.712 18.981 -0.148 0.65 17.41 ? 381 MET A CE 1 ATOM 2360 C CE B MET A 1 295 ? 13.428 19.390 1.724 0.35 14.41 ? 381 MET A CE 1 ATOM 2361 N N . ARG A 1 296 ? 15.154 24.603 0.523 1.00 8.47 ? 382 ARG A N 1 ATOM 2362 C CA . ARG A 1 296 ? 14.788 25.862 1.150 1.00 8.27 ? 382 ARG A CA 1 ATOM 2363 C C . ARG A 1 296 ? 13.666 25.641 2.139 1.00 6.80 ? 382 ARG A C 1 ATOM 2364 O O . ARG A 1 296 ? 12.770 24.785 1.935 1.00 7.88 ? 382 ARG A O 1 ATOM 2365 C CB A ARG A 1 296 ? 14.367 26.900 0.111 0.50 8.74 ? 382 ARG A CB 1 ATOM 2366 C CB B ARG A 1 296 ? 14.383 26.919 0.122 0.50 8.58 ? 382 ARG A CB 1 ATOM 2367 C CG A ARG A 1 296 ? 15.381 27.065 -1.032 0.50 10.55 ? 382 ARG A CG 1 ATOM 2368 C CG B ARG A 1 296 ? 15.403 27.084 -1.016 0.50 10.01 ? 382 ARG A CG 1 ATOM 2369 C CD A ARG A 1 296 ? 16.724 27.616 -0.583 0.50 11.00 ? 382 ARG A CD 1 ATOM 2370 C CD B ARG A 1 296 ? 16.809 27.459 -0.551 0.50 9.74 ? 382 ARG A CD 1 ATOM 2371 N NE A ARG A 1 296 ? 17.548 27.954 -1.746 0.50 11.31 ? 382 ARG A NE 1 ATOM 2372 N NE B ARG A 1 296 ? 17.784 27.299 -1.634 0.50 8.83 ? 382 ARG A NE 1 ATOM 2373 C CZ A ARG A 1 296 ? 18.430 27.177 -2.358 0.50 11.52 ? 382 ARG A CZ 1 ATOM 2374 C CZ B ARG A 1 296 ? 17.826 28.076 -2.730 0.50 10.35 ? 382 ARG A CZ 1 ATOM 2375 N NH1 A ARG A 1 296 ? 18.760 25.979 -1.906 0.50 11.62 ? 382 ARG A NH1 1 ATOM 2376 N NH1 B ARG A 1 296 ? 16.985 29.104 -2.885 0.50 11.29 ? 382 ARG A NH1 1 ATOM 2377 N NH2 A ARG A 1 296 ? 19.029 27.653 -3.436 0.50 12.96 ? 382 ARG A NH2 1 ATOM 2378 N NH2 B ARG A 1 296 ? 18.704 27.835 -3.673 0.50 10.21 ? 382 ARG A NH2 1 ATOM 2379 N N . PRO A 1 297 ? 13.654 26.375 3.235 1.00 6.72 ? 383 PRO A N 1 ATOM 2380 C CA . PRO A 1 297 ? 12.556 26.247 4.199 1.00 6.79 ? 383 PRO A CA 1 ATOM 2381 C C . PRO A 1 297 ? 11.190 26.379 3.587 1.00 6.99 ? 383 PRO A C 1 ATOM 2382 O O . PRO A 1 297 ? 10.952 27.266 2.750 1.00 8.10 ? 383 PRO A O 1 ATOM 2383 C CB . PRO A 1 297 ? 12.829 27.361 5.194 1.00 7.38 ? 383 PRO A CB 1 ATOM 2384 C CG . PRO A 1 297 ? 14.332 27.500 5.152 1.00 6.97 ? 383 PRO A CG 1 ATOM 2385 C CD . PRO A 1 297 ? 14.670 27.345 3.679 1.00 7.55 ? 383 PRO A CD 1 ATOM 2386 N N . THR A 1 298 ? 10.293 25.514 3.992 1.00 6.50 ? 384 THR A N 1 ATOM 2387 C CA . THR A 1 298 ? 8.942 25.539 3.450 1.00 6.90 ? 384 THR A CA 1 ATOM 2388 C C . THR A 1 298 ? 8.004 24.746 4.321 1.00 7.37 ? 384 THR A C 1 ATOM 2389 O O . THR A 1 298 ? 8.370 23.716 4.907 1.00 6.63 ? 384 THR A O 1 ATOM 2390 C CB . THR A 1 298 ? 8.951 24.977 2.020 1.00 7.68 ? 384 THR A CB 1 ATOM 2391 O OG1 . THR A 1 298 ? 7.596 25.052 1.470 1.00 10.09 ? 384 THR A OG1 1 ATOM 2392 C CG2 . THR A 1 298 ? 9.356 23.512 1.996 1.00 9.11 ? 384 THR A CG2 1 ATOM 2393 N N . ALA A 1 299 ? 6.756 25.211 4.326 1.00 7.49 ? 385 ALA A N 1 ATOM 2394 C CA . ALA A 1 299 ? 5.666 24.467 4.898 1.00 8.69 ? 385 ALA A CA 1 ATOM 2395 C C . ALA A 1 299 ? 5.139 23.394 3.941 1.00 9.14 ? 385 ALA A C 1 ATOM 2396 O O . ALA A 1 299 ? 4.389 22.485 4.354 1.00 10.24 ? 385 ALA A O 1 ATOM 2397 C CB . ALA A 1 299 ? 4.548 25.408 5.282 1.00 9.75 ? 385 ALA A CB 1 ATOM 2398 N N . ASN A 1 300 ? 5.479 23.511 2.679 1.00 8.17 ? 386 ASN A N 1 ATOM 2399 C CA . ASN A 1 300 ? 4.909 22.622 1.672 1.00 10.43 ? 386 ASN A CA 1 ATOM 2400 C C . ASN A 1 300 ? 5.783 21.397 1.453 1.00 8.93 ? 386 ASN A C 1 ATOM 2401 O O . ASN A 1 300 ? 6.440 21.216 0.426 1.00 10.38 ? 386 ASN A O 1 ATOM 2402 C CB . ASN A 1 300 ? 4.657 23.408 0.387 1.00 12.27 ? 386 ASN A CB 1 ATOM 2403 C CG . ASN A 1 300 ? 3.673 24.533 0.595 1.00 14.84 ? 386 ASN A CG 1 ATOM 2404 O OD1 . ASN A 1 300 ? 2.685 24.400 1.327 1.00 17.07 ? 386 ASN A OD1 1 ATOM 2405 N ND2 . ASN A 1 300 ? 3.944 25.672 -0.030 1.00 17.01 ? 386 ASN A ND2 1 ATOM 2406 N N . THR A 1 301 ? 5.812 20.561 2.480 1.00 8.46 ? 387 THR A N 1 ATOM 2407 C CA . THR A 1 301 ? 6.683 19.421 2.508 1.00 7.69 ? 387 THR A CA 1 ATOM 2408 C C . THR A 1 301 ? 6.227 18.263 1.642 1.00 7.26 ? 387 THR A C 1 ATOM 2409 O O . THR A 1 301 ? 7.038 17.430 1.229 1.00 9.06 ? 387 THR A O 1 ATOM 2410 C CB . THR A 1 301 ? 6.871 18.867 3.930 1.00 7.59 ? 387 THR A CB 1 ATOM 2411 O OG1 . THR A 1 301 ? 5.619 18.322 4.359 1.00 8.18 ? 387 THR A OG1 1 ATOM 2412 C CG2 . THR A 1 301 ? 7.263 19.975 4.906 1.00 8.75 ? 387 THR A CG2 1 ATOM 2413 N N . GLY A 1 302 ? 4.922 18.183 1.434 1.00 7.01 ? 388 GLY A N 1 ATOM 2414 C CA . GLY A 1 302 ? 4.329 17.039 0.778 1.00 7.34 ? 388 GLY A CA 1 ATOM 2415 C C . GLY A 1 302 ? 4.185 15.801 1.595 1.00 6.42 ? 388 GLY A C 1 ATOM 2416 O O . GLY A 1 302 ? 3.679 14.799 1.087 1.00 8.29 ? 388 GLY A O 1 ATOM 2417 N N . HIS A 1 303 ? 4.599 15.834 2.851 1.00 5.41 ? 389 HIS A N 1 ATOM 2418 C CA . HIS A 1 303 ? 4.558 14.631 3.719 1.00 5.76 ? 389 HIS A CA 1 ATOM 2419 C C . HIS A 1 303 ? 3.636 14.861 4.908 1.00 6.69 ? 389 HIS A C 1 ATOM 2420 O O . HIS A 1 303 ? 3.721 15.895 5.612 1.00 7.71 ? 389 HIS A O 1 ATOM 2421 C CB . HIS A 1 303 ? 5.960 14.257 4.230 1.00 5.87 ? 389 HIS A CB 1 ATOM 2422 C CG . HIS A 1 303 ? 6.004 12.880 4.823 1.00 5.12 ? 389 HIS A CG 1 ATOM 2423 N ND1 . HIS A 1 303 ? 5.468 12.543 6.058 1.00 6.70 ? 389 HIS A ND1 1 ATOM 2424 C CD2 . HIS A 1 303 ? 6.460 11.731 4.289 1.00 7.98 ? 389 HIS A CD2 1 ATOM 2425 C CE1 . HIS A 1 303 ? 5.611 11.243 6.245 1.00 7.99 ? 389 HIS A CE1 1 ATOM 2426 N NE2 . HIS A 1 303 ? 6.214 10.731 5.181 1.00 7.00 ? 389 HIS A NE2 1 ATOM 2427 N N . GLN A 1 304 ? 2.773 13.893 5.153 1.00 7.29 ? 390 GLN A N 1 ATOM 2428 C CA . GLN A 1 304 ? 1.735 14.010 6.178 1.00 8.00 ? 390 GLN A CA 1 ATOM 2429 C C . GLN A 1 304 ? 2.262 14.275 7.607 1.00 6.91 ? 390 GLN A C 1 ATOM 2430 O O . GLN A 1 304 ? 1.555 14.886 8.407 1.00 8.82 ? 390 GLN A O 1 ATOM 2431 C CB . GLN A 1 304 ? 0.798 12.759 6.181 1.00 8.69 ? 390 GLN A CB 1 ATOM 2432 C CG . GLN A 1 304 ? 1.493 11.403 6.469 1.00 10.49 ? 390 GLN A CG 1 ATOM 2433 C CD . GLN A 1 304 ? 0.556 10.161 6.383 1.00 14.51 ? 390 GLN A CD 1 ATOM 2434 O OE1 . GLN A 1 304 ? -0.666 10.317 6.340 1.00 17.70 ? 390 GLN A OE1 1 ATOM 2435 N NE2 . GLN A 1 304 ? 1.145 8.956 6.335 1.00 15.37 ? 390 GLN A NE2 1 ATOM 2436 N N . TYR A 1 305 ? 3.451 13.776 7.923 1.00 7.24 ? 391 TYR A N 1 ATOM 2437 C CA . TYR A 1 305 ? 3.968 13.908 9.270 1.00 6.35 ? 391 TYR A CA 1 ATOM 2438 C C . TYR A 1 305 ? 4.951 15.079 9.449 1.00 6.23 ? 391 TYR A C 1 ATOM 2439 O O . TYR A 1 305 ? 5.487 15.247 10.535 1.00 6.49 ? 391 TYR A O 1 ATOM 2440 C CB . TYR A 1 305 ? 4.653 12.601 9.701 1.00 7.13 ? 391 TYR A CB 1 ATOM 2441 C CG . TYR A 1 305 ? 3.782 11.354 9.745 1.00 8.20 ? 391 TYR A CG 1 ATOM 2442 C CD1 . TYR A 1 305 ? 2.442 11.452 10.028 1.00 9.42 ? 391 TYR A CD1 1 ATOM 2443 C CD2 . TYR A 1 305 ? 4.315 10.091 9.540 1.00 9.16 ? 391 TYR A CD2 1 ATOM 2444 C CE1 . TYR A 1 305 ? 1.625 10.313 10.104 1.00 11.64 ? 391 TYR A CE1 1 ATOM 2445 C CE2 . TYR A 1 305 ? 3.490 8.965 9.599 1.00 10.93 ? 391 TYR A CE2 1 ATOM 2446 C CZ . TYR A 1 305 ? 2.159 9.115 9.877 1.00 11.30 ? 391 TYR A CZ 1 ATOM 2447 O OH . TYR A 1 305 ? 1.284 8.023 9.948 1.00 15.95 ? 391 TYR A OH 1 ATOM 2448 N N . VAL A 1 306 ? 5.213 15.841 8.382 1.00 4.55 ? 392 VAL A N 1 ATOM 2449 C CA . VAL A 1 306 ? 6.269 16.858 8.393 1.00 5.30 ? 392 VAL A CA 1 ATOM 2450 C C . VAL A 1 306 ? 5.630 18.227 8.180 1.00 5.27 ? 392 VAL A C 1 ATOM 2451 O O . VAL A 1 306 ? 5.141 18.557 7.099 1.00 6.67 ? 392 VAL A O 1 ATOM 2452 C CB . VAL A 1 306 ? 7.403 16.585 7.396 1.00 5.63 ? 392 VAL A CB 1 ATOM 2453 C CG1 . VAL A 1 306 ? 8.580 17.519 7.610 1.00 6.42 ? 392 VAL A CG1 1 ATOM 2454 C CG2 . VAL A 1 306 ? 7.926 15.170 7.507 1.00 7.02 ? 392 VAL A CG2 1 ATOM 2455 N N . ASP A 1 307 ? 5.623 19.030 9.247 1.00 5.64 ? 393 ASP A N 1 ATOM 2456 C CA . ASP A 1 307 ? 5.102 20.402 9.204 1.00 5.60 ? 393 ASP A CA 1 ATOM 2457 C C . ASP A 1 307 ? 5.964 21.313 8.304 1.00 5.26 ? 393 ASP A C 1 ATOM 2458 O O . ASP A 1 307 ? 5.477 22.229 7.665 1.00 7.47 ? 393 ASP A O 1 ATOM 2459 C CB . ASP A 1 307 ? 5.045 21.026 10.605 1.00 4.97 ? 393 ASP A CB 1 ATOM 2460 C CG . ASP A 1 307 ? 3.859 20.560 11.431 1.00 5.52 ? 393 ASP A CG 1 ATOM 2461 O OD1 . ASP A 1 307 ? 2.909 19.896 10.892 1.00 5.66 ? 393 ASP A OD1 1 ATOM 2462 O OD2 . ASP A 1 307 ? 3.848 20.825 12.651 1.00 5.84 ? 393 ASP A OD2 1 ATOM 2463 N N . ALA A 1 308 ? 7.298 21.135 8.358 1.00 5.54 ? 394 ALA A N 1 ATOM 2464 C CA . ALA A 1 308 ? 8.196 21.973 7.591 1.00 5.75 ? 394 ALA A CA 1 ATOM 2465 C C . ALA A 1 308 ? 9.561 21.368 7.393 1.00 4.91 ? 394 ALA A C 1 ATOM 2466 O O . ALA A 1 308 ? 10.047 20.661 8.264 1.00 5.07 ? 394 ALA A O 1 ATOM 2467 C CB . ALA A 1 308 ? 8.330 23.324 8.235 1.00 5.67 ? 394 ALA A CB 1 ATOM 2468 N N . PHE A 1 309 ? 10.164 21.681 6.251 1.00 4.51 ? 395 PHE A N 1 ATOM 2469 C CA . PHE A 1 309 ? 11.607 21.616 6.088 1.00 5.26 ? 395 PHE A CA 1 ATOM 2470 C C . PHE A 1 309 ? 12.162 22.964 6.507 1.00 5.95 ? 395 PHE A C 1 ATOM 2471 O O . PHE A 1 309 ? 11.625 24.008 6.141 1.00 6.35 ? 395 PHE A O 1 ATOM 2472 C CB . PHE A 1 309 ? 12.030 21.233 4.663 1.00 5.74 ? 395 PHE A CB 1 ATOM 2473 C CG . PHE A 1 309 ? 11.527 19.904 4.252 1.00 6.85 ? 395 PHE A CG 1 ATOM 2474 C CD1 . PHE A 1 309 ? 11.935 18.770 4.929 1.00 7.51 ? 395 PHE A CD1 1 ATOM 2475 C CD2 . PHE A 1 309 ? 10.656 19.751 3.169 1.00 8.39 ? 395 PHE A CD2 1 ATOM 2476 C CE1 . PHE A 1 309 ? 11.468 17.509 4.565 1.00 9.45 ? 395 PHE A CE1 1 ATOM 2477 C CE2 . PHE A 1 309 ? 10.223 18.433 2.806 1.00 9.75 ? 395 PHE A CE2 1 ATOM 2478 C CZ . PHE A 1 309 ? 10.608 17.368 3.543 1.00 9.43 ? 395 PHE A CZ 1 ATOM 2479 N N . VAL A 1 310 ? 13.185 22.937 7.329 1.00 4.63 ? 396 VAL A N 1 ATOM 2480 C CA . VAL A 1 310 ? 13.744 24.152 7.910 1.00 4.94 ? 396 VAL A CA 1 ATOM 2481 C C . VAL A 1 310 ? 15.245 24.172 7.815 1.00 4.43 ? 396 VAL A C 1 ATOM 2482 O O . VAL A 1 310 ? 15.876 23.160 7.545 1.00 4.94 ? 396 VAL A O 1 ATOM 2483 C CB . VAL A 1 310 ? 13.304 24.284 9.389 1.00 4.90 ? 396 VAL A CB 1 ATOM 2484 C CG1 . VAL A 1 310 ? 11.814 24.613 9.483 1.00 5.86 ? 396 VAL A CG1 1 ATOM 2485 C CG2 . VAL A 1 310 ? 13.549 22.998 10.138 1.00 6.62 ? 396 VAL A CG2 1 ATOM 2486 N N . TRP A 1 311 ? 15.819 25.331 8.091 1.00 4.83 ? 397 TRP A N 1 ATOM 2487 C CA . TRP A 1 311 ? 17.262 25.495 8.280 1.00 4.70 ? 397 TRP A CA 1 ATOM 2488 C C . TRP A 1 311 ? 17.453 25.858 9.746 1.00 4.80 ? 397 TRP A C 1 ATOM 2489 O O . TRP A 1 311 ? 17.182 26.986 10.133 1.00 5.57 ? 397 TRP A O 1 ATOM 2490 C CB . TRP A 1 311 ? 17.838 26.581 7.373 1.00 5.24 ? 397 TRP A CB 1 ATOM 2491 C CG . TRP A 1 311 ? 17.975 26.220 5.925 1.00 4.90 ? 397 TRP A CG 1 ATOM 2492 C CD1 . TRP A 1 311 ? 17.388 25.176 5.248 1.00 5.39 ? 397 TRP A CD1 1 ATOM 2493 C CD2 . TRP A 1 311 ? 18.814 26.885 4.990 1.00 5.03 ? 397 TRP A CD2 1 ATOM 2494 N NE1 . TRP A 1 311 ? 17.787 25.195 3.933 1.00 5.86 ? 397 TRP A NE1 1 ATOM 2495 C CE2 . TRP A 1 311 ? 18.659 26.241 3.754 1.00 5.33 ? 397 TRP A CE2 1 ATOM 2496 C CE3 . TRP A 1 311 ? 19.661 27.999 5.059 1.00 5.80 ? 397 TRP A CE3 1 ATOM 2497 C CZ2 . TRP A 1 311 ? 19.399 26.632 2.605 1.00 6.31 ? 397 TRP A CZ2 1 ATOM 2498 C CZ3 . TRP A 1 311 ? 20.366 28.390 3.952 1.00 6.96 ? 397 TRP A CZ3 1 ATOM 2499 C CH2 . TRP A 1 311 ? 20.222 27.702 2.734 1.00 7.10 ? 397 TRP A CH2 1 ATOM 2500 N N . VAL A 1 312 ? 17.821 24.861 10.553 1.00 4.85 ? 398 VAL A N 1 ATOM 2501 C CA . VAL A 1 312 ? 17.956 25.102 11.994 1.00 4.30 ? 398 VAL A CA 1 ATOM 2502 C C . VAL A 1 312 ? 19.364 25.606 12.298 1.00 5.01 ? 398 VAL A C 1 ATOM 2503 O O . VAL A 1 312 ? 19.523 26.750 12.718 1.00 5.06 ? 398 VAL A O 1 ATOM 2504 C CB . VAL A 1 312 ? 17.561 23.900 12.849 1.00 4.40 ? 398 VAL A CB 1 ATOM 2505 C CG1 . VAL A 1 312 ? 17.485 24.338 14.343 1.00 4.60 ? 398 VAL A CG1 1 ATOM 2506 C CG2 . VAL A 1 312 ? 16.207 23.377 12.465 1.00 5.07 ? 398 VAL A CG2 1 ATOM 2507 N N . LYS A 1 313 ? 20.383 24.767 12.103 1.00 4.96 ? 399 LYS A N 1 ATOM 2508 C CA . LYS A 1 313 ? 21.767 25.217 12.256 1.00 6.19 ? 399 LYS A CA 1 ATOM 2509 C C . LYS A 1 313 ? 22.162 26.123 11.073 1.00 5.92 ? 399 LYS A C 1 ATOM 2510 O O . LYS A 1 313 ? 22.077 25.697 9.923 1.00 6.50 ? 399 LYS A O 1 ATOM 2511 C CB A LYS A 1 313 ? 22.655 23.977 12.382 0.60 6.17 ? 399 LYS A CB 1 ATOM 2512 C CB B LYS A 1 313 ? 22.701 24.016 12.332 0.40 6.35 ? 399 LYS A CB 1 ATOM 2513 C CG A LYS A 1 313 ? 24.157 24.234 12.460 0.60 8.90 ? 399 LYS A CG 1 ATOM 2514 C CG B LYS A 1 313 ? 24.195 24.378 12.344 0.40 8.66 ? 399 LYS A CG 1 ATOM 2515 C CD A LYS A 1 313 ? 24.643 24.972 13.675 0.60 11.42 ? 399 LYS A CD 1 ATOM 2516 C CD B LYS A 1 313 ? 24.601 25.296 13.484 0.40 11.41 ? 399 LYS A CD 1 ATOM 2517 C CE A LYS A 1 313 ? 25.984 25.653 13.256 0.60 12.28 ? 399 LYS A CE 1 ATOM 2518 C CE B LYS A 1 313 ? 24.278 24.725 14.844 0.40 11.64 ? 399 LYS A CE 1 ATOM 2519 N NZ A LYS A 1 313 ? 26.767 26.249 14.381 0.60 11.89 ? 399 LYS A NZ 1 ATOM 2520 N NZ B LYS A 1 313 ? 25.251 25.136 15.940 0.40 12.39 ? 399 LYS A NZ 1 ATOM 2521 N N . PRO A 1 314 ? 22.533 27.377 11.309 1.00 5.99 ? 400 PRO A N 1 ATOM 2522 C CA . PRO A 1 314 ? 22.843 28.280 10.186 1.00 6.30 ? 400 PRO A CA 1 ATOM 2523 C C . PRO A 1 314 ? 24.190 27.960 9.570 1.00 6.96 ? 400 PRO A C 1 ATOM 2524 O O . PRO A 1 314 ? 25.195 27.981 10.228 1.00 8.14 ? 400 PRO A O 1 ATOM 2525 C CB . PRO A 1 314 ? 22.774 29.660 10.820 1.00 6.71 ? 400 PRO A CB 1 ATOM 2526 C CG . PRO A 1 314 ? 22.090 29.442 12.095 1.00 7.48 ? 400 PRO A CG 1 ATOM 2527 C CD . PRO A 1 314 ? 22.567 28.120 12.579 1.00 6.26 ? 400 PRO A CD 1 ATOM 2528 N N . GLY A 1 315 ? 24.192 27.653 8.287 1.00 6.84 ? 401 GLY A N 1 ATOM 2529 C CA . GLY A 1 315 ? 25.418 27.282 7.583 1.00 6.50 ? 401 GLY A CA 1 ATOM 2530 C C . GLY A 1 315 ? 26.415 28.428 7.485 1.00 6.81 ? 401 GLY A C 1 ATOM 2531 O O . GLY A 1 315 ? 26.107 29.517 7.061 1.00 7.87 ? 401 GLY A O 1 ATOM 2532 N N . GLY A 1 316 ? 27.647 28.159 7.900 1.00 6.55 ? 402 GLY A N 1 ATOM 2533 C CA . GLY A 1 316 ? 28.735 29.128 7.951 1.00 6.87 ? 402 GLY A CA 1 ATOM 2534 C C . GLY A 1 316 ? 29.183 29.447 9.373 1.00 6.72 ? 402 GLY A C 1 ATOM 2535 O O . GLY A 1 316 ? 30.302 29.900 9.561 1.00 8.80 ? 402 GLY A O 1 ATOM 2536 N N . GLU A 1 317 ? 28.311 29.228 10.352 1.00 7.16 ? 403 GLU A N 1 ATOM 2537 C CA . GLU A 1 317 ? 28.673 29.392 11.777 1.00 8.04 ? 403 GLU A CA 1 ATOM 2538 C C . GLU A 1 317 ? 29.371 28.117 12.233 1.00 8.91 ? 403 GLU A C 1 ATOM 2539 O O . GLU A 1 317 ? 28.826 26.998 12.113 1.00 10.55 ? 403 GLU A O 1 ATOM 2540 C CB . GLU A 1 317 ? 27.472 29.735 12.643 1.00 7.86 ? 403 GLU A CB 1 ATOM 2541 C CG . GLU A 1 317 ? 26.774 31.031 12.201 1.00 8.06 ? 403 GLU A CG 1 ATOM 2542 C CD . GLU A 1 317 ? 25.520 31.391 12.928 1.00 8.50 ? 403 GLU A CD 1 ATOM 2543 O OE1 . GLU A 1 317 ? 25.086 30.602 13.815 1.00 13.65 ? 403 GLU A OE1 1 ATOM 2544 O OE2 . GLU A 1 317 ? 24.859 32.401 12.562 1.00 7.34 ? 403 GLU A OE2 1 ATOM 2545 N N . CYS A 1 318 ? 30.594 28.282 12.714 1.00 8.78 ? 404 CYS A N 1 ATOM 2546 C CA . CYS A 1 318 ? 31.471 27.137 13.006 1.00 8.65 ? 404 CYS A CA 1 ATOM 2547 C C . CYS A 1 318 ? 30.906 26.226 14.081 1.00 8.98 ? 404 CYS A C 1 ATOM 2548 O O . CYS A 1 318 ? 30.302 26.701 15.058 1.00 10.76 ? 404 CYS A O 1 ATOM 2549 C CB . CYS A 1 318 ? 32.807 27.625 13.497 1.00 8.57 ? 404 CYS A CB 1 ATOM 2550 S SG . CYS A 1 318 ? 34.030 26.309 13.419 1.00 9.42 ? 404 CYS A SG 1 ATOM 2551 N N . ASN A 1 319 ? 31.087 24.920 13.926 1.00 7.34 ? 405 ASN A N 1 ATOM 2552 C CA . ASN A 1 319 ? 30.663 23.933 14.929 1.00 7.24 ? 405 ASN A CA 1 ATOM 2553 C C . ASN A 1 319 ? 31.693 23.709 16.068 1.00 7.27 ? 405 ASN A C 1 ATOM 2554 O O . ASN A 1 319 ? 31.378 23.040 17.055 1.00 8.85 ? 405 ASN A O 1 ATOM 2555 C CB . ASN A 1 319 ? 30.356 22.577 14.309 1.00 6.24 ? 405 ASN A CB 1 ATOM 2556 C CG . ASN A 1 319 ? 29.324 22.622 13.198 1.00 8.85 ? 405 ASN A CG 1 ATOM 2557 O OD1 . ASN A 1 319 ? 29.415 21.882 12.227 1.00 7.06 ? 405 ASN A OD1 1 ATOM 2558 N ND2 . ASN A 1 319 ? 28.362 23.534 13.314 1.00 14.42 ? 405 ASN A ND2 1 ATOM 2559 N N . GLY A 1 320 ? 32.895 24.234 15.877 1.00 6.69 ? 406 GLY A N 1 ATOM 2560 C CA . GLY A 1 320 ? 33.970 24.064 16.833 1.00 6.95 ? 406 GLY A CA 1 ATOM 2561 C C . GLY A 1 320 ? 35.338 24.210 16.217 1.00 7.36 ? 406 GLY A C 1 ATOM 2562 O O . GLY A 1 320 ? 35.568 23.949 15.037 1.00 7.52 ? 406 GLY A O 1 ATOM 2563 N N . THR A 1 321 ? 36.283 24.622 17.051 1.00 6.93 ? 407 THR A N 1 ATOM 2564 C CA . THR A 1 321 ? 37.624 24.859 16.617 1.00 8.80 ? 407 THR A CA 1 ATOM 2565 C C . THR A 1 321 ? 38.393 23.584 16.349 1.00 7.98 ? 407 THR A C 1 ATOM 2566 O O . THR A 1 321 ? 38.189 22.547 16.966 1.00 7.41 ? 407 THR A O 1 ATOM 2567 C CB . THR A 1 321 ? 38.386 25.748 17.646 1.00 8.61 ? 407 THR A CB 1 ATOM 2568 O OG1 . THR A 1 321 ? 39.645 26.069 17.059 1.00 12.27 ? 407 THR A OG1 1 ATOM 2569 C CG2 . THR A 1 321 ? 38.655 24.988 18.980 1.00 11.29 ? 407 THR A CG2 1 ATOM 2570 N N . SER A 1 322 ? 39.296 23.705 15.399 1.00 8.95 ? 408 SER A N 1 ATOM 2571 C CA . SER A 1 322 ? 40.254 22.640 15.064 1.00 9.93 ? 408 SER A CA 1 ATOM 2572 C C . SER A 1 322 ? 41.571 22.772 15.870 1.00 10.99 ? 408 SER A C 1 ATOM 2573 O O . SER A 1 322 ? 42.441 21.929 15.744 1.00 11.10 ? 408 SER A O 1 ATOM 2574 C CB . SER A 1 322 ? 40.542 22.553 13.568 1.00 11.30 ? 408 SER A CB 1 ATOM 2575 O OG . SER A 1 322 ? 41.115 23.754 13.131 1.00 11.69 ? 408 SER A OG 1 ATOM 2576 N N . ASP A 1 323 ? 41.694 23.825 16.661 1.00 10.37 ? 409 ASP A N 1 ATOM 2577 C CA . ASP A 1 323 ? 42.866 24.052 17.542 1.00 11.10 ? 409 ASP A CA 1 ATOM 2578 C C . ASP A 1 323 ? 42.826 23.087 18.722 1.00 10.50 ? 409 ASP A C 1 ATOM 2579 O O . ASP A 1 323 ? 42.063 23.269 19.665 1.00 10.35 ? 409 ASP A O 1 ATOM 2580 C CB . ASP A 1 323 ? 42.845 25.479 18.013 1.00 11.97 ? 409 ASP A CB 1 ATOM 2581 C CG . ASP A 1 323 ? 44.048 25.847 18.876 1.00 14.47 ? 409 ASP A CG 1 ATOM 2582 O OD1 . ASP A 1 323 ? 44.873 24.978 19.230 1.00 14.73 ? 409 ASP A OD1 1 ATOM 2583 O OD2 . ASP A 1 323 ? 44.180 27.030 19.239 1.00 19.35 ? 409 ASP A OD2 1 ATOM 2584 N N . THR A 1 324 ? 43.695 22.086 18.665 1.00 12.08 ? 410 THR A N 1 ATOM 2585 C CA . THR A 1 324 ? 43.734 21.027 19.683 1.00 12.41 ? 410 THR A CA 1 ATOM 2586 C C . THR A 1 324 ? 44.130 21.492 21.064 1.00 13.52 ? 410 THR A C 1 ATOM 2587 O O . THR A 1 324 ? 43.936 20.754 22.024 1.00 15.64 ? 410 THR A O 1 ATOM 2588 C CB . THR A 1 324 ? 44.674 19.885 19.285 1.00 13.74 ? 410 THR A CB 1 ATOM 2589 O OG1 . THR A 1 324 ? 46.023 20.384 19.268 1.00 16.17 ? 410 THR A OG1 1 ATOM 2590 C CG2 . THR A 1 324 ? 44.381 19.312 17.915 1.00 12.89 ? 410 THR A CG2 1 ATOM 2591 N N . THR A 1 325 ? 44.684 22.698 21.158 1.00 12.95 ? 411 THR A N 1 ATOM 2592 C CA . THR A 1 325 ? 45.089 23.294 22.430 1.00 14.27 ? 411 THR A CA 1 ATOM 2593 C C . THR A 1 325 ? 44.040 24.173 23.090 1.00 13.26 ? 411 THR A C 1 ATOM 2594 O O . THR A 1 325 ? 44.200 24.617 24.232 1.00 15.45 ? 411 THR A O 1 ATOM 2595 C CB . THR A 1 325 ? 46.369 24.135 22.287 1.00 15.49 ? 411 THR A CB 1 ATOM 2596 O OG1 . THR A 1 325 ? 46.092 25.403 21.688 1.00 17.25 ? 411 THR A OG1 1 ATOM 2597 C CG2 . THR A 1 325 ? 47.430 23.460 21.466 1.00 18.17 ? 411 THR A CG2 1 ATOM 2598 N N . ALA A 1 326 ? 42.937 24.406 22.392 1.00 12.27 ? 412 ALA A N 1 ATOM 2599 C CA . ALA A 1 326 ? 41.866 25.259 22.907 1.00 11.78 ? 412 ALA A CA 1 ATOM 2600 C C . ALA A 1 326 ? 41.137 24.616 24.102 1.00 11.87 ? 412 ALA A C 1 ATOM 2601 O O . ALA A 1 326 ? 40.936 23.408 24.166 1.00 11.66 ? 412 ALA A O 1 ATOM 2602 C CB . ALA A 1 326 ? 40.847 25.593 21.791 1.00 12.34 ? 412 ALA A CB 1 ATOM 2603 N N . ALA A 1 327 ? 40.713 25.439 25.048 1.00 13.22 ? 413 ALA A N 1 ATOM 2604 C CA . ALA A 1 327 ? 40.066 24.934 26.269 1.00 13.67 ? 413 ALA A CA 1 ATOM 2605 C C . ALA A 1 327 ? 38.889 23.980 26.007 1.00 14.09 ? 413 ALA A C 1 ATOM 2606 O O . ALA A 1 327 ? 38.705 22.986 26.695 1.00 16.38 ? 413 ALA A O 1 ATOM 2607 C CB . ALA A 1 327 ? 39.563 26.121 27.132 1.00 15.34 ? 413 ALA A CB 1 ATOM 2608 N N . ARG A 1 328 ? 38.074 24.335 25.027 1.00 12.12 ? 414 ARG A N 1 ATOM 2609 C CA . ARG A 1 328 ? 36.876 23.541 24.756 1.00 12.48 ? 414 ARG A CA 1 ATOM 2610 C C . ARG A 1 328 ? 36.951 22.810 23.420 1.00 10.58 ? 414 ARG A C 1 ATOM 2611 O O . ARG A 1 328 ? 35.952 22.508 22.799 1.00 9.39 ? 414 ARG A O 1 ATOM 2612 C CB . ARG A 1 328 ? 35.614 24.372 24.842 1.00 14.85 ? 414 ARG A CB 1 ATOM 2613 C CG . ARG A 1 328 ? 35.463 24.931 26.263 1.00 17.49 ? 414 ARG A CG 1 ATOM 2614 C CD . ARG A 1 328 ? 34.265 25.769 26.519 1.00 22.51 ? 414 ARG A CD 1 ATOM 2615 N NE . ARG A 1 328 ? 34.420 26.198 27.908 1.00 28.77 ? 414 ARG A NE 1 ATOM 2616 C CZ . ARG A 1 328 ? 35.052 27.321 28.316 1.00 29.95 ? 414 ARG A CZ 1 ATOM 2617 N NH1 . ARG A 1 328 ? 35.527 28.229 27.437 1.00 26.83 ? 414 ARG A NH1 1 ATOM 2618 N NH2 . ARG A 1 328 ? 35.176 27.547 29.628 1.00 32.38 ? 414 ARG A NH2 1 ATOM 2619 N N . TYR A 1 329 ? 38.160 22.406 23.071 1.00 9.61 ? 415 TYR A N 1 ATOM 2620 C CA . TYR A 1 329 ? 38.401 21.628 21.865 1.00 8.39 ? 415 TYR A CA 1 ATOM 2621 C C . TYR A 1 329 ? 37.696 20.270 21.964 1.00 7.74 ? 415 TYR A C 1 ATOM 2622 O O . TYR A 1 329 ? 37.810 19.533 22.962 1.00 8.16 ? 415 TYR A O 1 ATOM 2623 C CB . TYR A 1 329 ? 39.900 21.361 21.687 1.00 8.91 ? 415 TYR A CB 1 ATOM 2624 C CG . TYR A 1 329 ? 40.220 20.388 20.565 1.00 7.92 ? 415 TYR A CG 1 ATOM 2625 C CD1 . TYR A 1 329 ? 40.036 20.739 19.255 1.00 8.16 ? 415 TYR A CD1 1 ATOM 2626 C CD2 . TYR A 1 329 ? 40.682 19.110 20.829 1.00 7.23 ? 415 TYR A CD2 1 ATOM 2627 C CE1 . TYR A 1 329 ? 40.334 19.882 18.239 1.00 9.41 ? 415 TYR A CE1 1 ATOM 2628 C CE2 . TYR A 1 329 ? 40.998 18.231 19.842 1.00 7.96 ? 415 TYR A CE2 1 ATOM 2629 C CZ . TYR A 1 329 ? 40.813 18.604 18.531 1.00 8.46 ? 415 TYR A CZ 1 ATOM 2630 O OH . TYR A 1 329 ? 41.122 17.754 17.490 1.00 9.52 ? 415 TYR A OH 1 ATOM 2631 N N . ASP A 1 330 ? 36.961 19.951 20.900 1.00 6.53 ? 416 ASP A N 1 ATOM 2632 C CA . ASP A 1 330 ? 36.278 18.704 20.734 1.00 6.60 ? 416 ASP A CA 1 ATOM 2633 C C . ASP A 1 330 ? 36.996 17.965 19.605 1.00 6.24 ? 416 ASP A C 1 ATOM 2634 O O . ASP A 1 330 ? 37.070 18.457 18.466 1.00 6.24 ? 416 ASP A O 1 ATOM 2635 C CB . ASP A 1 330 ? 34.825 18.968 20.359 1.00 6.27 ? 416 ASP A CB 1 ATOM 2636 C CG . ASP A 1 330 ? 33.995 17.746 20.377 1.00 7.92 ? 416 ASP A CG 1 ATOM 2637 O OD1 . ASP A 1 330 ? 34.387 16.740 19.730 1.00 7.46 ? 416 ASP A OD1 1 ATOM 2638 O OD2 . ASP A 1 330 ? 32.896 17.706 21.034 1.00 8.40 ? 416 ASP A OD2 1 ATOM 2639 N N . TYR A 1 331 ? 37.493 16.754 19.878 1.00 6.07 ? 417 TYR A N 1 ATOM 2640 C CA . TYR A 1 331 ? 38.258 15.972 18.899 1.00 6.69 ? 417 TYR A CA 1 ATOM 2641 C C . TYR A 1 331 ? 37.512 15.707 17.566 1.00 6.03 ? 417 TYR A C 1 ATOM 2642 O O . TYR A 1 331 ? 38.139 15.450 16.535 1.00 7.18 ? 417 TYR A O 1 ATOM 2643 C CB . TYR A 1 331 ? 38.729 14.643 19.481 1.00 7.63 ? 417 TYR A CB 1 ATOM 2644 C CG . TYR A 1 331 ? 37.673 13.587 19.630 1.00 7.34 ? 417 TYR A CG 1 ATOM 2645 C CD1 . TYR A 1 331 ? 37.360 12.691 18.584 1.00 7.43 ? 417 TYR A CD1 1 ATOM 2646 C CD2 . TYR A 1 331 ? 36.937 13.505 20.785 1.00 8.20 ? 417 TYR A CD2 1 ATOM 2647 C CE1 . TYR A 1 331 ? 36.364 11.744 18.722 1.00 7.01 ? 417 TYR A CE1 1 ATOM 2648 C CE2 . TYR A 1 331 ? 35.953 12.556 20.930 1.00 7.92 ? 417 TYR A CE2 1 ATOM 2649 C CZ . TYR A 1 331 ? 35.667 11.663 19.900 1.00 7.69 ? 417 TYR A CZ 1 ATOM 2650 O OH . TYR A 1 331 ? 34.692 10.712 20.021 1.00 9.66 ? 417 TYR A OH 1 ATOM 2651 N N . HIS A 1 332 ? 36.199 15.777 17.591 1.00 5.84 ? 418 HIS A N 1 ATOM 2652 C CA . HIS A 1 332 ? 35.430 15.599 16.352 1.00 6.54 ? 418 HIS A CA 1 ATOM 2653 C C . HIS A 1 332 ? 35.828 16.671 15.322 1.00 6.86 ? 418 HIS A C 1 ATOM 2654 O O . HIS A 1 332 ? 35.766 16.427 14.112 1.00 6.90 ? 418 HIS A O 1 ATOM 2655 C CB . HIS A 1 332 ? 33.930 15.688 16.610 1.00 6.89 ? 418 HIS A CB 1 ATOM 2656 C CG . HIS A 1 332 ? 33.384 14.497 17.332 1.00 7.94 ? 418 HIS A CG 1 ATOM 2657 N ND1 . HIS A 1 332 ? 33.327 14.440 18.714 1.00 8.35 ? 418 HIS A ND1 1 ATOM 2658 C CD2 . HIS A 1 332 ? 32.952 13.292 16.883 1.00 9.45 ? 418 HIS A CD2 1 ATOM 2659 C CE1 . HIS A 1 332 ? 32.835 13.269 19.074 1.00 9.04 ? 418 HIS A CE1 1 ATOM 2660 N NE2 . HIS A 1 332 ? 32.598 12.551 17.987 1.00 10.69 ? 418 HIS A NE2 1 ATOM 2661 N N . CYS A 1 333 ? 36.230 17.833 15.839 1.00 5.90 ? 419 CYS A N 1 ATOM 2662 C CA . CYS A 1 333 ? 36.596 18.973 14.967 1.00 6.34 ? 419 CYS A CA 1 ATOM 2663 C C . CYS A 1 333 ? 38.022 18.910 14.387 1.00 6.44 ? 419 CYS A C 1 ATOM 2664 O O . CYS A 1 333 ? 38.422 19.716 13.547 1.00 7.63 ? 419 CYS A O 1 ATOM 2665 C CB . CYS A 1 333 ? 36.335 20.289 15.720 1.00 5.66 ? 419 CYS A CB 1 ATOM 2666 S SG . CYS A 1 333 ? 34.637 20.426 16.252 1.00 7.81 ? 419 CYS A SG 1 ATOM 2667 N N . GLY A 1 334 ? 38.734 17.874 14.792 1.00 6.77 ? 420 GLY A N 1 ATOM 2668 C CA . GLY A 1 334 ? 40.072 17.586 14.287 1.00 7.13 ? 420 GLY A CA 1 ATOM 2669 C C . GLY A 1 334 ? 40.167 16.419 13.368 1.00 7.32 ? 420 GLY A C 1 ATOM 2670 O O . GLY A 1 334 ? 41.280 16.067 12.887 1.00 9.61 ? 420 GLY A O 1 ATOM 2671 N N . LEU A 1 335 ? 39.040 15.799 13.061 1.00 7.83 ? 421 LEU A N 1 ATOM 2672 C CA . LEU A 1 335 ? 39.041 14.616 12.209 1.00 7.64 ? 421 LEU A CA 1 ATOM 2673 C C . LEU A 1 335 ? 39.328 14.929 10.734 1.00 8.21 ? 421 LEU A C 1 ATOM 2674 O O . LEU A 1 335 ? 39.219 16.070 10.288 1.00 7.68 ? 421 LEU A O 1 ATOM 2675 C CB . LEU A 1 335 ? 37.710 13.850 12.356 1.00 8.29 ? 421 LEU A CB 1 ATOM 2676 C CG . LEU A 1 335 ? 37.411 13.396 13.774 1.00 7.89 ? 421 LEU A CG 1 ATOM 2677 C CD1 . LEU A 1 335 ? 36.028 12.690 13.785 1.00 7.89 ? 421 LEU A CD1 1 ATOM 2678 C CD2 . LEU A 1 335 ? 38.468 12.466 14.370 1.00 10.19 ? 421 LEU A CD2 1 ATOM 2679 N N . GLU A 1 336 ? 39.670 13.897 9.973 1.00 8.47 ? 422 GLU A N 1 ATOM 2680 C CA . GLU A 1 336 ? 40.072 14.034 8.565 1.00 9.64 ? 422 GLU A CA 1 ATOM 2681 C C . GLU A 1 336 ? 38.987 14.633 7.669 1.00 8.79 ? 422 GLU A C 1 ATOM 2682 O O . GLU A 1 336 ? 39.306 15.242 6.649 1.00 11.33 ? 422 GLU A O 1 ATOM 2683 C CB . GLU A 1 336 ? 40.528 12.683 7.964 1.00 11.16 ? 422 GLU A CB 1 ATOM 2684 C CG . GLU A 1 336 ? 39.455 11.576 7.963 1.00 16.37 ? 422 GLU A CG 1 ATOM 2685 C CD . GLU A 1 336 ? 39.925 10.222 7.404 1.00 23.46 ? 422 GLU A CD 1 ATOM 2686 O OE1 . GLU A 1 336 ? 40.972 10.220 6.729 1.00 27.13 ? 422 GLU A OE1 1 ATOM 2687 O OE2 . GLU A 1 336 ? 39.247 9.167 7.667 1.00 24.85 ? 422 GLU A OE2 1 ATOM 2688 N N . ASP A 1 337 ? 37.737 14.485 8.087 1.00 8.07 ? 423 ASP A N 1 ATOM 2689 C CA . ASP A 1 337 ? 36.576 14.931 7.332 1.00 7.18 ? 423 ASP A CA 1 ATOM 2690 C C . ASP A 1 337 ? 35.966 16.209 7.913 1.00 6.26 ? 423 ASP A C 1 ATOM 2691 O O . ASP A 1 337 ? 34.871 16.586 7.507 1.00 7.86 ? 423 ASP A O 1 ATOM 2692 C CB . ASP A 1 337 ? 35.530 13.832 7.175 1.00 7.28 ? 423 ASP A CB 1 ATOM 2693 C CG . ASP A 1 337 ? 35.040 13.265 8.483 1.00 7.49 ? 423 ASP A CG 1 ATOM 2694 O OD1 . ASP A 1 337 ? 35.298 13.900 9.533 1.00 7.63 ? 423 ASP A OD1 1 ATOM 2695 O OD2 . ASP A 1 337 ? 34.347 12.214 8.500 1.00 8.30 ? 423 ASP A OD2 1 ATOM 2696 N N . ALA A 1 338 ? 36.702 16.900 8.792 1.00 7.03 ? 424 ALA A N 1 ATOM 2697 C CA . ALA A 1 338 ? 36.298 18.178 9.368 1.00 6.69 ? 424 ALA A CA 1 ATOM 2698 C C . ALA A 1 338 ? 37.134 19.241 8.676 1.00 8.04 ? 424 ALA A C 1 ATOM 2699 O O . ALA A 1 338 ? 38.357 19.096 8.587 1.00 9.28 ? 424 ALA A O 1 ATOM 2700 C CB . ALA A 1 338 ? 36.500 18.215 10.896 1.00 7.04 ? 424 ALA A CB 1 ATOM 2701 N N . LEU A 1 339 ? 36.498 20.294 8.183 1.00 7.42 ? 425 LEU A N 1 ATOM 2702 C CA . LEU A 1 339 ? 37.237 21.326 7.453 1.00 7.60 ? 425 LEU A CA 1 ATOM 2703 C C . LEU A 1 339 ? 38.106 22.123 8.422 1.00 7.74 ? 425 LEU A C 1 ATOM 2704 O O . LEU A 1 339 ? 37.667 22.518 9.469 1.00 6.84 ? 425 LEU A O 1 ATOM 2705 C CB . LEU A 1 339 ? 36.276 22.262 6.736 1.00 7.20 ? 425 LEU A CB 1 ATOM 2706 C CG . LEU A 1 339 ? 36.897 23.221 5.706 1.00 8.25 ? 425 LEU A CG 1 ATOM 2707 C CD1 . LEU A 1 339 ? 37.545 22.512 4.533 1.00 10.58 ? 425 LEU A CD1 1 ATOM 2708 C CD2 . LEU A 1 339 ? 35.814 24.152 5.167 1.00 8.61 ? 425 LEU A CD2 1 ATOM 2709 N N . LYS A 1 340 ? 39.348 22.384 8.026 1.00 9.88 ? 426 LYS A N 1 ATOM 2710 C CA . LYS A 1 340 ? 40.338 23.012 8.905 1.00 12.86 ? 426 LYS A CA 1 ATOM 2711 C C . LYS A 1 340 ? 41.199 23.957 8.077 1.00 14.76 ? 426 LYS A C 1 ATOM 2712 O O . LYS A 1 340 ? 41.348 23.769 6.838 1.00 15.71 ? 426 LYS A O 1 ATOM 2713 C CB . LYS A 1 340 ? 41.258 21.955 9.524 1.00 14.12 ? 426 LYS A CB 1 ATOM 2714 C CG . LYS A 1 340 ? 40.583 20.865 10.194 1.00 16.68 ? 426 LYS A CG 1 ATOM 2715 C CD . LYS A 1 340 ? 41.607 19.894 10.813 1.00 19.49 ? 426 LYS A CD 1 ATOM 2716 C CE . LYS A 1 340 ? 41.133 18.550 10.686 1.00 19.95 ? 426 LYS A CE 1 ATOM 2717 N NZ . LYS A 1 340 ? 40.968 18.127 9.272 1.00 21.40 ? 426 LYS A NZ 1 ATOM 2718 N N . PRO A 1 341 ? 41.762 24.970 8.706 1.00 14.89 ? 427 PRO A N 1 ATOM 2719 C CA . PRO A 1 341 ? 41.569 25.320 10.108 1.00 14.70 ? 427 PRO A CA 1 ATOM 2720 C C . PRO A 1 341 ? 40.231 25.977 10.343 1.00 13.74 ? 427 PRO A C 1 ATOM 2721 O O . PRO A 1 341 ? 39.694 26.717 9.480 1.00 15.17 ? 427 PRO A O 1 ATOM 2722 C CB . PRO A 1 341 ? 42.708 26.326 10.362 1.00 15.20 ? 427 PRO A CB 1 ATOM 2723 C CG . PRO A 1 341 ? 42.782 27.043 9.005 1.00 17.80 ? 427 PRO A CG 1 ATOM 2724 C CD . PRO A 1 341 ? 42.697 25.897 8.022 1.00 15.92 ? 427 PRO A CD 1 ATOM 2725 N N . ALA A 1 342 ? 39.662 25.674 11.497 1.00 11.20 ? 428 ALA A N 1 ATOM 2726 C CA . ALA A 1 342 ? 38.367 26.136 11.933 1.00 10.31 ? 428 ALA A CA 1 ATOM 2727 C C . ALA A 1 342 ? 38.437 26.989 13.196 1.00 10.24 ? 428 ALA A C 1 ATOM 2728 O O . ALA A 1 342 ? 39.166 26.627 14.141 1.00 10.74 ? 428 ALA A O 1 ATOM 2729 C CB . ALA A 1 342 ? 37.456 24.931 12.181 1.00 9.39 ? 428 ALA A CB 1 ATOM 2730 N N . PRO A 1 343 ? 37.677 28.083 13.233 1.00 11.15 ? 429 PRO A N 1 ATOM 2731 C CA . PRO A 1 343 ? 37.655 28.965 14.402 1.00 11.92 ? 429 PRO A CA 1 ATOM 2732 C C . PRO A 1 343 ? 36.796 28.412 15.539 1.00 12.21 ? 429 PRO A C 1 ATOM 2733 O O . PRO A 1 343 ? 36.208 27.322 15.446 1.00 12.50 ? 429 PRO A O 1 ATOM 2734 C CB . PRO A 1 343 ? 37.094 30.258 13.831 1.00 12.98 ? 429 PRO A CB 1 ATOM 2735 C CG . PRO A 1 343 ? 36.102 29.770 12.823 1.00 11.82 ? 429 PRO A CG 1 ATOM 2736 C CD . PRO A 1 343 ? 36.762 28.544 12.177 1.00 11.45 ? 429 PRO A CD 1 ATOM 2737 N N . GLU A 1 344 ? 36.669 29.169 16.639 1.00 14.53 ? 430 GLU A N 1 ATOM 2738 C CA . GLU A 1 344 ? 35.819 28.722 17.738 1.00 14.99 ? 430 GLU A CA 1 ATOM 2739 C C . GLU A 1 344 ? 34.364 28.578 17.351 1.00 13.23 ? 430 GLU A C 1 ATOM 2740 O O . GLU A 1 344 ? 33.868 29.207 16.392 1.00 12.62 ? 430 GLU A O 1 ATOM 2741 C CB . GLU A 1 344 ? 35.940 29.604 19.008 1.00 17.43 ? 430 GLU A CB 1 ATOM 2742 C CG . GLU A 1 344 ? 37.324 29.555 19.635 1.00 21.52 ? 430 GLU A CG 1 ATOM 2743 C CD . GLU A 1 344 ? 37.593 28.446 20.655 1.00 27.49 ? 430 GLU A CD 1 ATOM 2744 O OE1 . GLU A 1 344 ? 36.689 27.704 21.128 1.00 29.75 ? 430 GLU A OE1 1 ATOM 2745 O OE2 . GLU A 1 344 ? 38.791 28.319 21.007 1.00 32.80 ? 430 GLU A OE2 1 ATOM 2746 N N . ALA A 1 345 ? 33.681 27.712 18.066 1.00 13.05 ? 431 ALA A N 1 ATOM 2747 C CA . ALA A 1 345 ? 32.282 27.465 17.862 1.00 13.03 ? 431 ALA A CA 1 ATOM 2748 C C . ALA A 1 345 ? 31.546 28.817 17.841 1.00 13.32 ? 431 ALA A C 1 ATOM 2749 O O . ALA A 1 345 ? 31.807 29.709 18.685 1.00 13.90 ? 431 ALA A O 1 ATOM 2750 C CB . ALA A 1 345 ? 31.707 26.563 18.933 1.00 13.54 ? 431 ALA A CB 1 ATOM 2751 N N . GLY A 1 346 ? 30.715 28.992 16.818 1.00 12.31 ? 432 GLY A N 1 ATOM 2752 C CA . GLY A 1 346 ? 29.886 30.186 16.712 1.00 12.42 ? 432 GLY A CA 1 ATOM 2753 C C . GLY A 1 346 ? 30.527 31.297 15.898 1.00 12.52 ? 432 GLY A C 1 ATOM 2754 O O . GLY A 1 346 ? 29.813 32.223 15.492 1.00 14.39 ? 432 GLY A O 1 ATOM 2755 N N . GLN A 1 347 ? 31.821 31.247 15.662 1.00 12.30 ? 433 GLN A N 1 ATOM 2756 C CA . GLN A 1 347 ? 32.504 32.251 14.865 1.00 11.94 ? 433 GLN A CA 1 ATOM 2757 C C . GLN A 1 347 ? 32.235 31.909 13.400 1.00 11.14 ? 433 GLN A C 1 ATOM 2758 O O . GLN A 1 347 ? 32.069 30.751 13.033 1.00 10.31 ? 433 GLN A O 1 ATOM 2759 C CB A GLN A 1 347 ? 34.037 32.248 15.087 0.50 12.55 ? 433 GLN A CB 1 ATOM 2760 C CB B GLN A 1 347 ? 33.962 32.340 15.228 0.50 12.55 ? 433 GLN A CB 1 ATOM 2761 C CG A GLN A 1 347 ? 34.736 33.517 14.531 0.50 13.99 ? 433 GLN A CG 1 ATOM 2762 C CG B GLN A 1 347 ? 34.083 32.598 16.721 0.50 13.66 ? 433 GLN A CG 1 ATOM 2763 C CD A GLN A 1 347 ? 36.240 33.629 14.778 0.50 13.27 ? 433 GLN A CD 1 ATOM 2764 C CD B GLN A 1 347 ? 35.487 32.840 17.151 0.50 14.49 ? 433 GLN A CD 1 ATOM 2765 O OE1 A GLN A 1 347 ? 36.743 33.149 15.780 0.50 15.43 ? 433 GLN A OE1 1 ATOM 2766 O OE1 B GLN A 1 347 ? 36.330 33.064 16.319 0.50 14.20 ? 433 GLN A OE1 1 ATOM 2767 N NE2 A GLN A 1 347 ? 36.947 34.303 13.872 0.50 14.68 ? 433 GLN A NE2 1 ATOM 2768 N NE2 B GLN A 1 347 ? 35.746 32.813 18.463 0.50 16.57 ? 433 GLN A NE2 1 ATOM 2769 N N . TRP A 1 348 ? 32.163 32.944 12.591 1.00 11.00 ? 434 TRP A N 1 ATOM 2770 C CA . TRP A 1 348 ? 31.971 32.769 11.160 1.00 9.83 ? 434 TRP A CA 1 ATOM 2771 C C . TRP A 1 348 ? 33.160 32.018 10.587 1.00 9.44 ? 434 TRP A C 1 ATOM 2772 O O . TRP A 1 348 ? 34.321 32.345 10.886 1.00 11.26 ? 434 TRP A O 1 ATOM 2773 C CB . TRP A 1 348 ? 31.785 34.116 10.490 1.00 10.03 ? 434 TRP A CB 1 ATOM 2774 C CG . TRP A 1 348 ? 31.336 33.978 9.073 1.00 9.30 ? 434 TRP A CG 1 ATOM 2775 C CD1 . TRP A 1 348 ? 32.078 34.162 7.937 1.00 9.26 ? 434 TRP A CD1 1 ATOM 2776 C CD2 . TRP A 1 348 ? 30.043 33.549 8.650 1.00 8.44 ? 434 TRP A CD2 1 ATOM 2777 N NE1 . TRP A 1 348 ? 31.313 33.877 6.824 1.00 8.60 ? 434 TRP A NE1 1 ATOM 2778 C CE2 . TRP A 1 348 ? 30.033 33.568 7.237 1.00 6.15 ? 434 TRP A CE2 1 ATOM 2779 C CE3 . TRP A 1 348 ? 28.865 33.238 9.325 1.00 8.09 ? 434 TRP A CE3 1 ATOM 2780 C CZ2 . TRP A 1 348 ? 28.904 33.186 6.485 1.00 7.20 ? 434 TRP A CZ2 1 ATOM 2781 C CZ3 . TRP A 1 348 ? 27.734 32.884 8.576 1.00 8.04 ? 434 TRP A CZ3 1 ATOM 2782 C CH2 . TRP A 1 348 ? 27.766 32.874 7.173 1.00 7.58 ? 434 TRP A CH2 1 ATOM 2783 N N . PHE A 1 349 ? 32.868 31.007 9.752 1.00 8.11 ? 435 PHE A N 1 ATOM 2784 C CA . PHE A 1 349 ? 33.859 30.143 9.141 1.00 7.42 ? 435 PHE A CA 1 ATOM 2785 C C . PHE A 1 349 ? 33.681 30.264 7.631 1.00 7.56 ? 435 PHE A C 1 ATOM 2786 O O . PHE A 1 349 ? 32.930 29.532 6.996 1.00 7.05 ? 435 PHE A O 1 ATOM 2787 C CB . PHE A 1 349 ? 33.643 28.717 9.668 1.00 7.43 ? 435 PHE A CB 1 ATOM 2788 C CG . PHE A 1 349 ? 34.670 27.686 9.253 1.00 7.87 ? 435 PHE A CG 1 ATOM 2789 C CD1 . PHE A 1 349 ? 35.786 27.970 8.491 1.00 8.96 ? 435 PHE A CD1 1 ATOM 2790 C CD2 . PHE A 1 349 ? 34.493 26.355 9.682 1.00 7.27 ? 435 PHE A CD2 1 ATOM 2791 C CE1 . PHE A 1 349 ? 36.666 26.984 8.156 1.00 8.56 ? 435 PHE A CE1 1 ATOM 2792 C CE2 . PHE A 1 349 ? 35.396 25.405 9.398 1.00 7.72 ? 435 PHE A CE2 1 ATOM 2793 C CZ . PHE A 1 349 ? 36.498 25.696 8.588 1.00 9.01 ? 435 PHE A CZ 1 ATOM 2794 N N . ASN A 1 350 ? 34.353 31.242 7.025 1.00 7.63 ? 436 ASN A N 1 ATOM 2795 C CA . ASN A 1 350 ? 34.038 31.586 5.624 1.00 8.08 ? 436 ASN A CA 1 ATOM 2796 C C . ASN A 1 350 ? 34.341 30.490 4.632 1.00 8.23 ? 436 ASN A C 1 ATOM 2797 O O . ASN A 1 350 ? 33.584 30.298 3.721 1.00 8.72 ? 436 ASN A O 1 ATOM 2798 C CB . ASN A 1 350 ? 34.706 32.887 5.154 1.00 9.14 ? 436 ASN A CB 1 ATOM 2799 C CG . ASN A 1 350 ? 33.922 33.544 4.059 1.00 11.20 ? 436 ASN A CG 1 ATOM 2800 O OD1 . ASN A 1 350 ? 32.716 33.739 4.176 1.00 12.39 ? 436 ASN A OD1 1 ATOM 2801 N ND2 . ASN A 1 350 ? 34.593 33.816 2.921 1.00 14.46 ? 436 ASN A ND2 1 ATOM 2802 N N . GLU A 1 351 ? 35.427 29.741 4.832 1.00 7.78 ? 437 GLU A N 1 ATOM 2803 C CA . GLU A 1 351 ? 35.750 28.663 3.920 1.00 8.86 ? 437 GLU A CA 1 ATOM 2804 C C . GLU A 1 351 ? 34.612 27.618 3.921 1.00 7.86 ? 437 GLU A C 1 ATOM 2805 O O . GLU A 1 351 ? 34.291 27.011 2.894 1.00 7.48 ? 437 GLU A O 1 ATOM 2806 C CB . GLU A 1 351 ? 37.096 28.034 4.239 1.00 10.28 ? 437 GLU A CB 1 ATOM 2807 C CG . GLU A 1 351 ? 38.282 28.923 3.836 1.00 16.05 ? 437 GLU A CG 1 ATOM 2808 C CD . GLU A 1 351 ? 38.302 29.219 2.322 1.00 23.66 ? 437 GLU A CD 1 ATOM 2809 O OE1 . GLU A 1 351 ? 38.383 28.250 1.537 1.00 27.27 ? 437 GLU A OE1 1 ATOM 2810 O OE2 . GLU A 1 351 ? 38.197 30.416 1.912 1.00 30.66 ? 437 GLU A OE2 1 ATOM 2811 N N . TYR A 1 352 ? 34.001 27.441 5.083 1.00 7.86 ? 438 TYR A N 1 ATOM 2812 C CA . TYR A 1 352 ? 32.892 26.457 5.191 1.00 7.75 ? 438 TYR A CA 1 ATOM 2813 C C . TYR A 1 352 ? 31.643 27.021 4.483 1.00 6.53 ? 438 TYR A C 1 ATOM 2814 O O . TYR A 1 352 ? 30.926 26.306 3.816 1.00 5.80 ? 438 TYR A O 1 ATOM 2815 C CB . TYR A 1 352 ? 32.580 26.130 6.670 1.00 7.44 ? 438 TYR A CB 1 ATOM 2816 C CG . TYR A 1 352 ? 31.800 24.865 6.775 1.00 6.24 ? 438 TYR A CG 1 ATOM 2817 C CD1 . TYR A 1 352 ? 32.459 23.652 6.825 1.00 5.74 ? 438 TYR A CD1 1 ATOM 2818 C CD2 . TYR A 1 352 ? 30.403 24.850 6.732 1.00 6.37 ? 438 TYR A CD2 1 ATOM 2819 C CE1 . TYR A 1 352 ? 31.774 22.439 6.829 1.00 6.24 ? 438 TYR A CE1 1 ATOM 2820 C CE2 . TYR A 1 352 ? 29.724 23.639 6.726 1.00 7.65 ? 438 TYR A CE2 1 ATOM 2821 C CZ . TYR A 1 352 ? 30.392 22.452 6.823 1.00 6.07 ? 438 TYR A CZ 1 ATOM 2822 O OH . TYR A 1 352 ? 29.695 21.288 6.842 1.00 5.68 ? 438 TYR A OH 1 ATOM 2823 N N . PHE A 1 353 ? 31.376 28.314 4.637 1.00 7.02 ? 439 PHE A N 1 ATOM 2824 C CA . PHE A 1 353 ? 30.273 28.965 3.916 1.00 6.29 ? 439 PHE A CA 1 ATOM 2825 C C . PHE A 1 353 ? 30.446 28.793 2.419 1.00 7.21 ? 439 PHE A C 1 ATOM 2826 O O . PHE A 1 353 ? 29.500 28.467 1.719 1.00 7.61 ? 439 PHE A O 1 ATOM 2827 C CB . PHE A 1 353 ? 30.251 30.445 4.313 1.00 5.84 ? 439 PHE A CB 1 ATOM 2828 C CG . PHE A 1 353 ? 29.186 31.252 3.638 1.00 5.32 ? 439 PHE A CG 1 ATOM 2829 C CD1 . PHE A 1 353 ? 27.869 31.113 4.001 1.00 6.50 ? 439 PHE A CD1 1 ATOM 2830 C CD2 . PHE A 1 353 ? 29.517 32.183 2.656 1.00 8.27 ? 439 PHE A CD2 1 ATOM 2831 C CE1 . PHE A 1 353 ? 26.898 31.852 3.430 1.00 7.79 ? 439 PHE A CE1 1 ATOM 2832 C CE2 . PHE A 1 353 ? 28.519 32.946 2.051 1.00 9.07 ? 439 PHE A CE2 1 ATOM 2833 C CZ . PHE A 1 353 ? 27.211 32.789 2.424 1.00 7.47 ? 439 PHE A CZ 1 ATOM 2834 N N . ILE A 1 354 ? 31.681 28.998 1.919 1.00 7.92 ? 440 ILE A N 1 ATOM 2835 C CA . ILE A 1 354 ? 31.901 28.847 0.484 1.00 8.10 ? 440 ILE A CA 1 ATOM 2836 C C . ILE A 1 354 ? 31.660 27.393 0.022 1.00 7.46 ? 440 ILE A C 1 ATOM 2837 O O . ILE A 1 354 ? 31.039 27.145 -1.023 1.00 7.06 ? 440 ILE A O 1 ATOM 2838 C CB . ILE A 1 354 ? 33.319 29.326 0.070 1.00 9.28 ? 440 ILE A CB 1 ATOM 2839 C CG1 . ILE A 1 354 ? 33.445 30.817 0.292 1.00 10.32 ? 440 ILE A CG1 1 ATOM 2840 C CG2 . ILE A 1 354 ? 33.590 28.972 -1.385 1.00 11.70 ? 440 ILE A CG2 1 ATOM 2841 C CD1 . ILE A 1 354 ? 34.856 31.324 0.232 1.00 15.13 ? 440 ILE A CD1 1 ATOM 2842 N N . GLN A 1 355 ? 32.124 26.409 0.827 1.00 7.00 ? 441 GLN A N 1 ATOM 2843 C CA . GLN A 1 355 ? 31.840 25.020 0.558 1.00 7.48 ? 441 GLN A CA 1 ATOM 2844 C C . GLN A 1 355 ? 30.331 24.795 0.397 1.00 6.58 ? 441 GLN A C 1 ATOM 2845 O O . GLN A 1 355 ? 29.882 24.136 -0.542 1.00 6.78 ? 441 GLN A O 1 ATOM 2846 C CB . GLN A 1 355 ? 32.399 24.124 1.682 1.00 6.66 ? 441 GLN A CB 1 ATOM 2847 C CG . GLN A 1 355 ? 32.010 22.655 1.517 1.00 7.80 ? 441 GLN A CG 1 ATOM 2848 C CD . GLN A 1 355 ? 32.324 21.841 2.751 1.00 7.66 ? 441 GLN A CD 1 ATOM 2849 O OE1 . GLN A 1 355 ? 33.501 21.663 3.104 1.00 8.20 ? 441 GLN A OE1 1 ATOM 2850 N NE2 . GLN A 1 355 ? 31.280 21.362 3.445 1.00 6.75 ? 441 GLN A NE2 1 ATOM 2851 N N . LEU A 1 356 ? 29.549 25.300 1.376 1.00 6.31 ? 442 LEU A N 1 ATOM 2852 C CA . LEU A 1 356 ? 28.090 25.122 1.340 1.00 7.16 ? 442 LEU A CA 1 ATOM 2853 C C . LEU A 1 356 ? 27.470 25.712 0.097 1.00 6.83 ? 442 LEU A C 1 ATOM 2854 O O . LEU A 1 356 ? 26.520 25.155 -0.467 1.00 6.57 ? 442 LEU A O 1 ATOM 2855 C CB . LEU A 1 356 ? 27.421 25.713 2.585 1.00 6.57 ? 442 LEU A CB 1 ATOM 2856 C CG . LEU A 1 356 ? 27.725 24.899 3.851 1.00 4.90 ? 442 LEU A CG 1 ATOM 2857 C CD1 . LEU A 1 356 ? 27.243 25.729 5.050 1.00 5.54 ? 442 LEU A CD1 1 ATOM 2858 C CD2 . LEU A 1 356 ? 27.090 23.535 3.837 1.00 6.43 ? 442 LEU A CD2 1 ATOM 2859 N N . LEU A 1 357 ? 27.972 26.877 -0.298 1.00 7.97 ? 443 LEU A N 1 ATOM 2860 C CA . LEU A 1 357 ? 27.496 27.523 -1.528 1.00 8.32 ? 443 LEU A CA 1 ATOM 2861 C C . LEU A 1 357 ? 27.834 26.705 -2.766 1.00 8.55 ? 443 LEU A C 1 ATOM 2862 O O . LEU A 1 357 ? 26.985 26.484 -3.638 1.00 9.47 ? 443 LEU A O 1 ATOM 2863 C CB . LEU A 1 357 ? 28.110 28.911 -1.707 1.00 9.89 ? 443 LEU A CB 1 ATOM 2864 C CG . LEU A 1 357 ? 27.546 30.061 -0.916 1.00 12.79 ? 443 LEU A CG 1 ATOM 2865 C CD1 . LEU A 1 357 ? 28.374 31.331 -1.260 1.00 14.82 ? 443 LEU A CD1 1 ATOM 2866 C CD2 . LEU A 1 357 ? 26.114 30.296 -1.256 1.00 13.88 ? 443 LEU A CD2 1 ATOM 2867 N N . ARG A 1 358 ? 29.079 26.277 -2.877 1.00 8.32 ? 444 ARG A N 1 ATOM 2868 C CA . ARG A 1 358 ? 29.494 25.477 -4.043 1.00 8.83 ? 444 ARG A CA 1 ATOM 2869 C C . ARG A 1 358 ? 28.697 24.182 -4.235 1.00 8.50 ? 444 ARG A C 1 ATOM 2870 O O . ARG A 1 358 ? 28.417 23.758 -5.345 1.00 10.43 ? 444 ARG A O 1 ATOM 2871 C CB . ARG A 1 358 ? 30.961 25.059 -3.935 1.00 10.49 ? 444 ARG A CB 1 ATOM 2872 C CG . ARG A 1 358 ? 31.948 26.184 -4.142 1.00 13.43 ? 444 ARG A CG 1 ATOM 2873 C CD . ARG A 1 358 ? 33.397 25.597 -4.172 1.00 19.65 ? 444 ARG A CD 1 ATOM 2874 N NE . ARG A 1 358 ? 34.465 26.598 -4.211 1.00 23.91 ? 444 ARG A NE 1 ATOM 2875 C CZ . ARG A 1 358 ? 34.925 27.155 -5.296 1.00 27.26 ? 444 ARG A CZ 1 ATOM 2876 N NH1 . ARG A 1 358 ? 34.426 26.838 -6.498 1.00 27.92 ? 444 ARG A NH1 1 ATOM 2877 N NH2 . ARG A 1 358 ? 35.913 28.039 -5.168 1.00 29.63 ? 444 ARG A NH2 1 ATOM 2878 N N . ASN A 1 359 ? 28.366 23.518 -3.126 1.00 7.79 ? 445 ASN A N 1 ATOM 2879 C CA . ASN A 1 359 ? 27.640 22.268 -3.113 1.00 7.60 ? 445 ASN A CA 1 ATOM 2880 C C . ASN A 1 359 ? 26.134 22.434 -2.918 1.00 7.21 ? 445 ASN A C 1 ATOM 2881 O O . ASN A 1 359 ? 25.414 21.448 -2.795 1.00 7.77 ? 445 ASN A O 1 ATOM 2882 C CB . ASN A 1 359 ? 28.158 21.365 -1.978 1.00 7.42 ? 445 ASN A CB 1 ATOM 2883 C CG . ASN A 1 359 ? 29.547 20.879 -2.219 1.00 10.70 ? 445 ASN A CG 1 ATOM 2884 O OD1 . ASN A 1 359 ? 29.869 20.483 -3.357 1.00 13.50 ? 445 ASN A OD1 1 ATOM 2885 N ND2 . ASN A 1 359 ? 30.374 20.796 -1.158 1.00 11.03 ? 445 ASN A ND2 1 ATOM 2886 N N . ALA A 1 360 ? 25.624 23.664 -2.971 1.00 7.24 ? 446 ALA A N 1 ATOM 2887 C CA . ALA A 1 360 ? 24.192 23.905 -2.741 1.00 7.21 ? 446 ALA A CA 1 ATOM 2888 C C . ALA A 1 360 ? 23.322 23.176 -3.724 1.00 7.82 ? 446 ALA A C 1 ATOM 2889 O O . ALA A 1 360 ? 23.572 23.152 -4.933 1.00 9.02 ? 446 ALA A O 1 ATOM 2890 C CB . ALA A 1 360 ? 23.856 25.379 -2.763 1.00 8.31 ? 446 ALA A CB 1 ATOM 2891 N N . ASN A 1 361 ? 22.255 22.630 -3.185 1.00 7.09 ? 447 ASN A N 1 ATOM 2892 C CA . ASN A 1 361 ? 21.243 21.940 -3.986 1.00 8.85 ? 447 ASN A CA 1 ATOM 2893 C C . ASN A 1 361 ? 19.897 22.094 -3.321 1.00 9.44 ? 447 ASN A C 1 ATOM 2894 O O . ASN A 1 361 ? 19.671 21.498 -2.265 1.00 9.16 ? 447 ASN A O 1 ATOM 2895 C CB . ASN A 1 361 ? 21.629 20.476 -4.171 1.00 9.84 ? 447 ASN A CB 1 ATOM 2896 C CG . ASN A 1 361 ? 20.576 19.692 -4.862 1.00 13.66 ? 447 ASN A CG 1 ATOM 2897 O OD1 . ASN A 1 361 ? 19.967 20.157 -5.794 1.00 15.14 ? 447 ASN A OD1 1 ATOM 2898 N ND2 . ASN A 1 361 ? 20.343 18.481 -4.384 1.00 19.14 ? 447 ASN A ND2 1 ATOM 2899 N N . PRO A 1 362 ? 18.973 22.853 -3.909 1.00 9.80 ? 448 PRO A N 1 ATOM 2900 C CA . PRO A 1 362 ? 19.159 23.555 -5.181 1.00 10.73 ? 448 PRO A CA 1 ATOM 2901 C C . PRO A 1 362 ? 20.222 24.653 -5.123 1.00 10.24 ? 448 PRO A C 1 ATOM 2902 O O . PRO A 1 362 ? 20.461 25.240 -4.082 1.00 10.08 ? 448 PRO A O 1 ATOM 2903 C CB . PRO A 1 362 ? 17.781 24.181 -5.467 1.00 11.75 ? 448 PRO A CB 1 ATOM 2904 C CG . PRO A 1 362 ? 16.880 23.596 -4.558 1.00 14.62 ? 448 PRO A CG 1 ATOM 2905 C CD . PRO A 1 362 ? 17.634 23.109 -3.349 1.00 11.42 ? 448 PRO A CD 1 ATOM 2906 N N . PRO A 1 363 ? 20.872 24.916 -6.253 1.00 11.39 ? 449 PRO A N 1 ATOM 2907 C CA . PRO A 1 363 ? 21.901 25.945 -6.311 1.00 11.34 ? 449 PRO A CA 1 ATOM 2908 C C . PRO A 1 363 ? 21.352 27.363 -6.121 1.00 11.70 ? 449 PRO A C 1 ATOM 2909 O O . PRO A 1 363 ? 20.175 27.614 -6.322 1.00 11.88 ? 449 PRO A O 1 ATOM 2910 C CB . PRO A 1 363 ? 22.521 25.735 -7.700 1.00 12.46 ? 449 PRO A CB 1 ATOM 2911 C CG . PRO A 1 363 ? 21.446 25.158 -8.460 1.00 14.73 ? 449 PRO A CG 1 ATOM 2912 C CD . PRO A 1 363 ? 20.681 24.251 -7.552 1.00 11.86 ? 449 PRO A CD 1 ATOM 2913 N N . PHE A 1 364 ? 22.235 28.243 -5.661 1.00 13.71 ? 450 PHE A N 1 ATOM 2914 C CA . PHE A 1 364 ? 22.014 29.682 -5.589 1.00 14.43 ? 450 PHE A CA 1 ATOM 2915 C C . PHE A 1 364 ? 22.490 30.439 -6.828 1.00 18.29 ? 450 PHE A C 1 ATOM 2916 O O . PHE A 1 364 ? 23.191 29.851 -7.635 1.00 19.42 ? 450 PHE A O 1 ATOM 2917 C CB . PHE A 1 364 ? 22.653 30.256 -4.329 1.00 14.41 ? 450 PHE A CB 1 ATOM 2918 C CG . PHE A 1 364 ? 21.896 29.911 -3.096 1.00 11.68 ? 450 PHE A CG 1 ATOM 2919 C CD1 . PHE A 1 364 ? 20.773 30.629 -2.695 1.00 11.21 ? 450 PHE A CD1 1 ATOM 2920 C CD2 . PHE A 1 364 ? 22.274 28.818 -2.320 1.00 11.74 ? 450 PHE A CD2 1 ATOM 2921 C CE1 . PHE A 1 364 ? 20.064 30.280 -1.591 1.00 12.66 ? 450 PHE A CE1 1 ATOM 2922 C CE2 . PHE A 1 364 ? 21.554 28.489 -1.196 1.00 11.19 ? 450 PHE A CE2 1 ATOM 2923 C CZ . PHE A 1 364 ? 20.457 29.195 -0.826 1.00 13.52 ? 450 PHE A CZ 1 ATOM 2924 O OXT . PHE A 1 364 ? 22.074 31.598 -6.904 1.00 22.29 ? 450 PHE A OXT 1 HETATM 2925 C C1 . NAG B 2 . ? 20.601 36.063 32.313 1.00 5.11 ? 500 NAG A C1 1 HETATM 2926 C C2 . NAG B 2 . ? 21.309 36.349 33.632 1.00 5.91 ? 500 NAG A C2 1 HETATM 2927 C C3 . NAG B 2 . ? 20.432 37.262 34.490 1.00 6.52 ? 500 NAG A C3 1 HETATM 2928 C C4 . NAG B 2 . ? 19.877 38.443 33.713 1.00 6.87 ? 500 NAG A C4 1 HETATM 2929 C C5 . NAG B 2 . ? 19.277 37.976 32.390 1.00 6.80 ? 500 NAG A C5 1 HETATM 2930 C C6 . NAG B 2 . ? 18.779 39.136 31.546 1.00 6.86 ? 500 NAG A C6 1 HETATM 2931 C C7 . NAG B 2 . ? 22.746 34.796 34.904 1.00 6.67 ? 500 NAG A C7 1 HETATM 2932 C C8 . NAG B 2 . ? 22.777 33.475 35.623 1.00 6.47 ? 500 NAG A C8 1 HETATM 2933 N N2 . NAG B 2 . ? 21.606 35.100 34.301 1.00 6.78 ? 500 NAG A N2 1 HETATM 2934 O O3 . NAG B 2 . ? 21.171 37.699 35.624 1.00 8.30 ? 500 NAG A O3 1 HETATM 2935 O O4 . NAG B 2 . ? 18.925 39.106 34.540 1.00 7.79 ? 500 NAG A O4 1 HETATM 2936 O O5 . NAG B 2 . ? 20.232 37.264 31.645 1.00 6.79 ? 500 NAG A O5 1 HETATM 2937 O O6 . NAG B 2 . ? 18.100 38.633 30.416 1.00 6.83 ? 500 NAG A O6 1 HETATM 2938 O O7 . NAG B 2 . ? 23.704 35.570 34.901 1.00 9.55 ? 500 NAG A O7 1 HETATM 2939 CA CA . CA C 3 . ? 31.715 2.704 9.035 1.00 25.95 ? 501 CA A CA 1 HETATM 2940 C C1 . GOL D 4 . ? 17.063 14.713 -0.413 1.00 19.12 ? 510 GOL A C1 1 HETATM 2941 O O1 . GOL D 4 . ? 15.796 14.657 0.191 1.00 17.59 ? 510 GOL A O1 1 HETATM 2942 C C2 . GOL D 4 . ? 17.835 15.934 0.099 1.00 18.07 ? 510 GOL A C2 1 HETATM 2943 O O2 . GOL D 4 . ? 18.108 15.730 1.488 1.00 16.53 ? 510 GOL A O2 1 HETATM 2944 C C3 . GOL D 4 . ? 19.156 16.154 -0.642 1.00 18.82 ? 510 GOL A C3 1 HETATM 2945 O O3 . GOL D 4 . ? 18.891 16.624 -1.952 1.00 22.45 ? 510 GOL A O3 1 HETATM 2946 C C1 A GOL E 4 . ? 21.852 34.286 16.377 0.50 18.31 ? 511 GOL A C1 1 HETATM 2947 C C1 B GOL E 4 . ? 22.333 32.942 16.890 0.50 15.68 ? 511 GOL A C1 1 HETATM 2948 O O1 A GOL E 4 . ? 21.133 34.264 15.158 0.50 17.81 ? 511 GOL A O1 1 HETATM 2949 O O1 B GOL E 4 . ? 21.834 31.944 16.004 0.50 14.31 ? 511 GOL A O1 1 HETATM 2950 C C2 A GOL E 4 . ? 22.191 32.860 16.813 0.50 18.02 ? 511 GOL A C2 1 HETATM 2951 C C2 B GOL E 4 . ? 23.630 32.477 17.574 0.50 16.05 ? 511 GOL A C2 1 HETATM 2952 O O2 A GOL E 4 . ? 21.876 31.853 15.882 0.50 15.35 ? 511 GOL A O2 1 HETATM 2953 O O2 B GOL E 4 . ? 24.615 32.182 16.592 0.50 16.76 ? 511 GOL A O2 1 HETATM 2954 C C3 A GOL E 4 . ? 23.469 32.590 17.627 0.50 18.52 ? 511 GOL A C3 1 HETATM 2955 C C3 B GOL E 4 . ? 24.139 33.492 18.594 0.50 17.33 ? 511 GOL A C3 1 HETATM 2956 O O3 A GOL E 4 . ? 23.568 33.463 18.705 0.50 20.59 ? 511 GOL A O3 1 HETATM 2957 O O3 B GOL E 4 . ? 24.960 32.899 19.588 0.50 14.36 ? 511 GOL A O3 1 HETATM 2958 C C1 . GOL F 4 . ? 25.624 10.154 19.077 0.50 22.60 ? 512 GOL A C1 1 HETATM 2959 O O1 . GOL F 4 . ? 25.123 9.598 17.887 0.50 24.92 ? 512 GOL A O1 1 HETATM 2960 C C2 . GOL F 4 . ? 25.466 9.141 20.187 0.50 20.81 ? 512 GOL A C2 1 HETATM 2961 O O2 . GOL F 4 . ? 25.725 7.849 19.722 0.50 21.45 ? 512 GOL A O2 1 HETATM 2962 C C3 . GOL F 4 . ? 26.333 9.466 21.383 0.50 17.55 ? 512 GOL A C3 1 HETATM 2963 O O3 . GOL F 4 . ? 26.224 10.820 21.722 0.50 14.84 ? 512 GOL A O3 1 HETATM 2964 C C1 . GOL G 4 . ? 1.115 16.626 18.940 1.00 20.32 ? 514 GOL A C1 1 HETATM 2965 O O1 . GOL G 4 . ? 0.713 15.553 19.767 1.00 21.05 ? 514 GOL A O1 1 HETATM 2966 C C2 . GOL G 4 . ? -0.112 17.209 18.259 1.00 21.99 ? 514 GOL A C2 1 HETATM 2967 O O2 . GOL G 4 . ? -1.045 17.636 19.209 1.00 23.63 ? 514 GOL A O2 1 HETATM 2968 C C3 . GOL G 4 . ? 0.200 18.405 17.416 1.00 21.90 ? 514 GOL A C3 1 HETATM 2969 O O3 . GOL G 4 . ? 0.858 17.988 16.239 1.00 22.04 ? 514 GOL A O3 1 HETATM 2970 C C1 . GOL H 4 . ? 32.441 10.075 25.110 1.00 23.85 ? 515 GOL A C1 1 HETATM 2971 O O1 . GOL H 4 . ? 32.126 11.462 24.774 1.00 23.41 ? 515 GOL A O1 1 HETATM 2972 C C2 . GOL H 4 . ? 31.765 9.525 26.378 1.00 22.45 ? 515 GOL A C2 1 HETATM 2973 O O2 . GOL H 4 . ? 31.119 8.279 26.155 1.00 21.58 ? 515 GOL A O2 1 HETATM 2974 C C3 . GOL H 4 . ? 32.809 9.329 27.495 1.00 21.49 ? 515 GOL A C3 1 HETATM 2975 O O3 . GOL H 4 . ? 32.259 8.725 28.717 1.00 18.38 ? 515 GOL A O3 1 HETATM 2976 C C1 . GOL I 4 . ? 24.999 15.578 16.502 0.50 20.29 ? 516 GOL A C1 1 HETATM 2977 O O1 . GOL I 4 . ? 24.412 14.371 16.825 0.50 21.13 ? 516 GOL A O1 1 HETATM 2978 C C2 . GOL I 4 . ? 24.913 16.613 17.603 0.50 21.58 ? 516 GOL A C2 1 HETATM 2979 O O2 . GOL I 4 . ? 24.018 17.617 17.182 0.50 22.46 ? 516 GOL A O2 1 HETATM 2980 C C3 . GOL I 4 . ? 26.213 17.372 17.783 0.50 21.88 ? 516 GOL A C3 1 HETATM 2981 O O3 . GOL I 4 . ? 26.069 18.567 17.041 0.50 23.27 ? 516 GOL A O3 1 HETATM 2982 C C1 . GOL J 4 . ? 1.565 28.349 4.150 1.00 30.20 ? 517 GOL A C1 1 HETATM 2983 O O1 . GOL J 4 . ? 0.354 29.057 4.151 1.00 32.32 ? 517 GOL A O1 1 HETATM 2984 C C2 . GOL J 4 . ? 2.814 29.196 3.921 1.00 32.04 ? 517 GOL A C2 1 HETATM 2985 O O2 . GOL J 4 . ? 3.338 28.633 2.725 1.00 33.50 ? 517 GOL A O2 1 HETATM 2986 C C3 . GOL J 4 . ? 2.551 30.708 3.809 1.00 32.87 ? 517 GOL A C3 1 HETATM 2987 O O3 . GOL J 4 . ? 3.565 31.398 3.103 1.00 34.64 ? 517 GOL A O3 1 HETATM 2988 O O . HOH K 5 . ? -1.956 35.040 21.481 1.00 11.45 ? 2001 HOH A O 1 HETATM 2989 O O . HOH K 5 . ? -0.119 33.251 15.750 1.00 15.66 ? 2002 HOH A O 1 HETATM 2990 O O . HOH K 5 . ? -2.778 33.490 13.650 1.00 28.99 ? 2003 HOH A O 1 HETATM 2991 O O . HOH K 5 . ? -4.524 29.325 12.291 1.00 19.76 ? 2004 HOH A O 1 HETATM 2992 O O . HOH K 5 . ? -1.390 22.988 16.764 1.00 22.16 ? 2005 HOH A O 1 HETATM 2993 O O . HOH K 5 . ? -1.749 27.493 11.108 1.00 21.11 ? 2006 HOH A O 1 HETATM 2994 O O . HOH K 5 . ? 5.993 29.355 6.371 1.00 16.65 ? 2007 HOH A O 1 HETATM 2995 O O . HOH K 5 . ? 0.209 21.838 6.482 0.50 19.61 ? 2008 HOH A O 1 HETATM 2996 O O . HOH K 5 . ? -2.588 22.923 9.387 1.00 23.04 ? 2009 HOH A O 1 HETATM 2997 O O . HOH K 5 . ? -2.633 33.713 8.850 1.00 40.39 ? 2010 HOH A O 1 HETATM 2998 O O . HOH K 5 . ? 5.806 40.717 2.193 1.00 30.16 ? 2011 HOH A O 1 HETATM 2999 O O . HOH K 5 . ? 8.849 31.940 4.129 0.50 12.97 ? 2012 HOH A O 1 HETATM 3000 O O . HOH K 5 . ? 11.315 34.496 3.885 1.00 23.32 ? 2013 HOH A O 1 HETATM 3001 O O . HOH K 5 . ? 11.904 32.954 11.075 1.00 9.66 ? 2014 HOH A O 1 HETATM 3002 O O . HOH K 5 . ? 12.975 38.008 5.800 1.00 19.77 ? 2015 HOH A O 1 HETATM 3003 O O . HOH K 5 . ? 14.605 44.857 9.720 1.00 24.21 ? 2016 HOH A O 1 HETATM 3004 O O . HOH K 5 . ? 14.213 39.980 6.630 1.00 29.64 ? 2017 HOH A O 1 HETATM 3005 O O . HOH K 5 . ? 21.668 42.975 8.494 1.00 29.95 ? 2018 HOH A O 1 HETATM 3006 O O . HOH K 5 . ? 24.989 42.017 13.789 1.00 30.43 ? 2019 HOH A O 1 HETATM 3007 O O . HOH K 5 . ? 29.458 43.444 1.680 1.00 20.50 ? 2020 HOH A O 1 HETATM 3008 O O . HOH K 5 . ? 26.932 43.475 0.593 1.00 24.41 ? 2021 HOH A O 1 HETATM 3009 O O . HOH K 5 . ? 29.745 42.981 11.427 1.00 25.89 ? 2022 HOH A O 1 HETATM 3010 O O . HOH K 5 . ? 33.151 44.176 6.755 1.00 27.90 ? 2023 HOH A O 1 HETATM 3011 O O . HOH K 5 . ? 35.504 40.356 6.365 0.50 21.18 ? 2024 HOH A O 1 HETATM 3012 O O . HOH K 5 . ? 38.581 32.612 5.594 1.00 31.87 ? 2025 HOH A O 1 HETATM 3013 O O . HOH K 5 . ? 35.055 35.606 9.270 1.00 32.88 ? 2026 HOH A O 1 HETATM 3014 O O . HOH K 5 . ? -4.619 34.154 21.912 1.00 15.55 ? 2027 HOH A O 1 HETATM 3015 O O . HOH K 5 . ? -3.459 35.979 13.490 1.00 39.70 ? 2028 HOH A O 1 HETATM 3016 O O . HOH K 5 . ? 36.632 39.282 -9.282 1.00 24.11 ? 2029 HOH A O 1 HETATM 3017 O O . HOH K 5 . ? 35.726 34.409 -4.515 1.00 29.01 ? 2030 HOH A O 1 HETATM 3018 O O . HOH K 5 . ? 31.642 34.832 -11.605 1.00 33.90 ? 2031 HOH A O 1 HETATM 3019 O O . HOH K 5 . ? 27.632 39.734 -8.014 1.00 21.71 ? 2032 HOH A O 1 HETATM 3020 O O . HOH K 5 . ? 25.291 33.664 -8.747 1.00 36.59 ? 2033 HOH A O 1 HETATM 3021 O O . HOH K 5 . ? 23.167 43.699 6.489 1.00 38.36 ? 2034 HOH A O 1 HETATM 3022 O O . HOH K 5 . ? 22.447 41.163 15.365 1.00 32.91 ? 2035 HOH A O 1 HETATM 3023 O O . HOH K 5 . ? 31.642 43.458 -0.175 1.00 21.63 ? 2036 HOH A O 1 HETATM 3024 O O . HOH K 5 . ? 28.194 42.805 -4.807 0.50 26.44 ? 2037 HOH A O 1 HETATM 3025 O O . HOH K 5 . ? 35.837 41.718 8.321 0.50 30.43 ? 2038 HOH A O 1 HETATM 3026 O O . HOH K 5 . ? 21.732 37.799 -5.295 1.00 23.64 ? 2039 HOH A O 1 HETATM 3027 O O . HOH K 5 . ? 26.466 42.290 -2.151 0.50 22.99 ? 2040 HOH A O 1 HETATM 3028 O O . HOH K 5 . ? 26.387 41.210 -4.281 0.50 27.75 ? 2041 HOH A O 1 HETATM 3029 O O . HOH K 5 . ? 20.524 42.014 -0.369 1.00 31.35 ? 2042 HOH A O 1 HETATM 3030 O O . HOH K 5 . ? 19.952 38.955 -3.094 1.00 32.97 ? 2043 HOH A O 1 HETATM 3031 O O . HOH K 5 . ? 25.802 40.614 -6.259 0.50 23.55 ? 2044 HOH A O 1 HETATM 3032 O O . HOH K 5 . ? 30.262 32.860 -13.403 1.00 42.73 ? 2045 HOH A O 1 HETATM 3033 O O . HOH K 5 . ? 17.198 33.627 -1.343 1.00 22.80 ? 2046 HOH A O 1 HETATM 3034 O O . HOH K 5 . ? 19.171 35.802 7.459 1.00 8.44 ? 2047 HOH A O 1 HETATM 3035 O O . HOH K 5 . ? 20.990 39.735 1.032 1.00 11.27 ? 2048 HOH A O 1 HETATM 3036 O O . HOH K 5 . ? 13.592 36.433 3.397 1.00 25.01 ? 2049 HOH A O 1 HETATM 3037 O O . HOH K 5 . ? 14.424 33.486 0.751 1.00 25.58 ? 2050 HOH A O 1 HETATM 3038 O O . HOH K 5 . ? 14.012 27.503 8.538 1.00 7.40 ? 2051 HOH A O 1 HETATM 3039 O O . HOH K 5 . ? 20.033 31.349 6.631 1.00 7.40 ? 2052 HOH A O 1 HETATM 3040 O O . HOH K 5 . ? 15.261 33.919 11.433 1.00 6.93 ? 2053 HOH A O 1 HETATM 3041 O O . HOH K 5 . ? 17.785 33.829 8.823 1.00 8.11 ? 2054 HOH A O 1 HETATM 3042 O O . HOH K 5 . ? 20.057 32.233 11.684 1.00 6.82 ? 2055 HOH A O 1 HETATM 3043 O O . HOH K 5 . ? 24.809 37.908 31.601 0.40 11.38 ? 2056 HOH A O 1 HETATM 3044 O O . HOH K 5 . ? 26.819 27.798 22.750 1.00 18.93 ? 2057 HOH A O 1 HETATM 3045 O O . HOH K 5 . ? 27.828 30.824 20.098 1.00 32.16 ? 2058 HOH A O 1 HETATM 3046 O O . HOH K 5 . ? 25.252 26.788 19.640 1.00 34.74 ? 2059 HOH A O 1 HETATM 3047 O O . HOH K 5 . ? 21.749 43.289 13.464 1.00 41.75 ? 2060 HOH A O 1 HETATM 3048 O O . HOH K 5 . ? 26.703 36.434 19.244 1.00 28.59 ? 2061 HOH A O 1 HETATM 3049 O O . HOH K 5 . ? 28.676 35.853 25.203 1.00 33.56 ? 2062 HOH A O 1 HETATM 3050 O O . HOH K 5 . ? 11.136 45.858 7.871 1.00 33.29 ? 2063 HOH A O 1 HETATM 3051 O O . HOH K 5 . ? 19.872 38.408 28.197 1.00 5.53 ? 2064 HOH A O 1 HETATM 3052 O O . HOH K 5 . ? 24.438 35.566 31.476 0.60 7.27 ? 2065 HOH A O 1 HETATM 3053 O O . HOH K 5 . ? 17.513 35.729 30.523 1.00 7.18 ? 2066 HOH A O 1 HETATM 3054 O O . HOH K 5 . ? 6.087 52.495 13.437 1.00 34.97 ? 2067 HOH A O 1 HETATM 3055 O O . HOH K 5 . ? 16.134 41.785 31.942 1.00 12.12 ? 2068 HOH A O 1 HETATM 3056 O O . HOH K 5 . ? 15.401 44.436 27.484 1.00 21.06 ? 2069 HOH A O 1 HETATM 3057 O O . HOH K 5 . ? 17.159 45.019 25.704 1.00 30.22 ? 2070 HOH A O 1 HETATM 3058 O O . HOH K 5 . ? 25.883 15.307 38.071 1.00 32.98 ? 2071 HOH A O 1 HETATM 3059 O O . HOH K 5 . ? 30.214 20.986 37.435 1.00 26.91 ? 2072 HOH A O 1 HETATM 3060 O O . HOH K 5 . ? 26.784 18.400 39.240 1.00 33.82 ? 2073 HOH A O 1 HETATM 3061 O O . HOH K 5 . ? 29.781 14.286 36.204 1.00 31.19 ? 2074 HOH A O 1 HETATM 3062 O O . HOH K 5 . ? 29.155 20.741 20.636 1.00 35.83 ? 2075 HOH A O 1 HETATM 3063 O O . HOH K 5 . ? 20.913 44.824 21.798 0.50 16.26 ? 2076 HOH A O 1 HETATM 3064 O O . HOH K 5 . ? 28.022 35.479 27.797 1.00 24.60 ? 2077 HOH A O 1 HETATM 3065 O O . HOH K 5 . ? 18.633 39.408 14.685 1.00 26.37 ? 2078 HOH A O 1 HETATM 3066 O O . HOH K 5 . ? 20.227 21.545 41.468 1.00 18.58 ? 2079 HOH A O 1 HETATM 3067 O O . HOH K 5 . ? 8.799 47.095 16.675 1.00 15.90 ? 2080 HOH A O 1 HETATM 3068 O O . HOH K 5 . ? 19.332 43.533 14.225 0.50 15.20 ? 2081 HOH A O 1 HETATM 3069 O O . HOH K 5 . ? 16.298 40.007 12.881 1.00 9.95 ? 2082 HOH A O 1 HETATM 3070 O O . HOH K 5 . ? 19.098 34.145 37.139 1.00 14.52 ? 2083 HOH A O 1 HETATM 3071 O O . HOH K 5 . ? 8.064 47.196 19.345 1.00 24.23 ? 2084 HOH A O 1 HETATM 3072 O O . HOH K 5 . ? 11.951 45.396 10.416 1.00 15.12 ? 2085 HOH A O 1 HETATM 3073 O O . HOH K 5 . ? 6.283 49.387 10.848 1.00 15.66 ? 2086 HOH A O 1 HETATM 3074 O O . HOH K 5 . ? 11.754 41.091 36.615 1.00 24.46 ? 2087 HOH A O 1 HETATM 3075 O O . HOH K 5 . ? 7.236 44.636 5.571 1.00 23.15 ? 2088 HOH A O 1 HETATM 3076 O O . HOH K 5 . ? 8.303 46.331 23.815 1.00 41.82 ? 2089 HOH A O 1 HETATM 3077 O O . HOH K 5 . ? 3.360 41.066 14.086 0.70 14.50 ? 2090 HOH A O 1 HETATM 3078 O O . HOH K 5 . ? -3.708 31.045 8.236 1.00 34.89 ? 2091 HOH A O 1 HETATM 3079 O O . HOH K 5 . ? 5.857 49.944 13.371 1.00 27.17 ? 2092 HOH A O 1 HETATM 3080 O O . HOH K 5 . ? 0.648 48.628 7.147 1.00 30.58 ? 2093 HOH A O 1 HETATM 3081 O O . HOH K 5 . ? 6.870 48.546 15.499 1.00 30.74 ? 2094 HOH A O 1 HETATM 3082 O O . HOH K 5 . ? 1.686 50.482 16.275 1.00 33.94 ? 2095 HOH A O 1 HETATM 3083 O O . HOH K 5 . ? 16.829 5.234 31.829 1.00 34.43 ? 2096 HOH A O 1 HETATM 3084 O O . HOH K 5 . ? -0.652 36.778 7.581 1.00 28.17 ? 2097 HOH A O 1 HETATM 3085 O O . HOH K 5 . ? 0.781 36.994 12.077 1.00 33.41 ? 2098 HOH A O 1 HETATM 3086 O O . HOH K 5 . ? 3.347 36.374 13.090 1.00 11.54 ? 2099 HOH A O 1 HETATM 3087 O O . HOH K 5 . ? 17.737 9.900 36.901 1.00 32.51 ? 2100 HOH A O 1 HETATM 3088 O O . HOH K 5 . ? 21.734 17.054 40.823 1.00 33.78 ? 2101 HOH A O 1 HETATM 3089 O O . HOH K 5 . ? 13.758 34.076 13.856 1.00 7.88 ? 2102 HOH A O 1 HETATM 3090 O O . HOH K 5 . ? 7.092 22.164 35.652 1.00 23.12 ? 2103 HOH A O 1 HETATM 3091 O O . HOH K 5 . ? 14.719 10.968 35.991 1.00 35.98 ? 2104 HOH A O 1 HETATM 3092 O O . HOH K 5 . ? 23.767 21.224 18.908 0.40 20.35 ? 2105 HOH A O 1 HETATM 3093 O O . HOH K 5 . ? -4.237 25.158 26.224 1.00 30.34 ? 2106 HOH A O 1 HETATM 3094 O O . HOH K 5 . ? -3.236 27.455 25.308 1.00 29.43 ? 2107 HOH A O 1 HETATM 3095 O O . HOH K 5 . ? 24.489 25.851 29.846 1.00 8.08 ? 2108 HOH A O 1 HETATM 3096 O O . HOH K 5 . ? 27.456 20.319 37.521 1.00 13.25 ? 2109 HOH A O 1 HETATM 3097 O O . HOH K 5 . ? 28.866 20.935 33.848 1.00 23.24 ? 2110 HOH A O 1 HETATM 3098 O O . HOH K 5 . ? 28.971 17.797 35.799 1.00 23.61 ? 2111 HOH A O 1 HETATM 3099 O O . HOH K 5 . ? 25.520 15.872 35.534 1.00 11.73 ? 2112 HOH A O 1 HETATM 3100 O O . HOH K 5 . ? 29.804 17.751 28.459 1.00 21.12 ? 2113 HOH A O 1 HETATM 3101 O O . HOH K 5 . ? 28.257 22.819 23.174 1.00 12.35 ? 2114 HOH A O 1 HETATM 3102 O O . HOH K 5 . ? 22.186 19.247 26.474 1.00 6.80 ? 2115 HOH A O 1 HETATM 3103 O O . HOH K 5 . ? 30.872 13.974 28.544 0.45 14.75 ? 2116 HOH A O 1 HETATM 3104 O O . HOH K 5 . ? 30.675 13.455 29.980 0.55 13.91 ? 2117 HOH A O 1 HETATM 3105 O O . HOH K 5 . ? 25.787 14.998 24.463 1.00 12.49 ? 2118 HOH A O 1 HETATM 3106 O O . HOH K 5 . ? 10.759 -0.866 16.205 1.00 42.57 ? 2119 HOH A O 1 HETATM 3107 O O . HOH K 5 . ? 38.066 15.338 25.338 0.50 27.27 ? 2120 HOH A O 1 HETATM 3108 O O . HOH K 5 . ? 36.976 18.552 27.207 1.00 31.34 ? 2121 HOH A O 1 HETATM 3109 O O . HOH K 5 . ? 28.874 19.807 22.784 1.00 24.43 ? 2122 HOH A O 1 HETATM 3110 O O . HOH K 5 . ? 33.721 20.988 28.258 1.00 28.76 ? 2123 HOH A O 1 HETATM 3111 O O . HOH K 5 . ? -4.001 15.938 23.865 1.00 34.88 ? 2124 HOH A O 1 HETATM 3112 O O . HOH K 5 . ? 28.037 29.113 25.135 1.00 27.79 ? 2125 HOH A O 1 HETATM 3113 O O . HOH K 5 . ? 28.488 24.531 20.930 1.00 31.43 ? 2126 HOH A O 1 HETATM 3114 O O . HOH K 5 . ? 31.483 25.377 28.615 1.00 22.61 ? 2127 HOH A O 1 HETATM 3115 O O . HOH K 5 . ? 27.823 32.915 31.639 1.00 21.05 ? 2128 HOH A O 1 HETATM 3116 O O . HOH K 5 . ? 25.472 34.573 28.618 1.00 9.96 ? 2129 HOH A O 1 HETATM 3117 O O . HOH K 5 . ? 25.940 28.688 27.022 1.00 11.61 ? 2130 HOH A O 1 HETATM 3118 O O . HOH K 5 . ? 28.683 32.436 27.770 1.00 29.63 ? 2131 HOH A O 1 HETATM 3119 O O . HOH K 5 . ? 29.864 26.157 33.713 1.00 35.16 ? 2132 HOH A O 1 HETATM 3120 O O . HOH K 5 . ? 25.701 33.479 33.182 1.00 17.27 ? 2133 HOH A O 1 HETATM 3121 O O . HOH K 5 . ? 26.650 23.519 30.412 1.00 13.38 ? 2134 HOH A O 1 HETATM 3122 O O . HOH K 5 . ? 21.514 23.710 40.117 1.00 10.02 ? 2135 HOH A O 1 HETATM 3123 O O . HOH K 5 . ? 26.103 27.673 36.257 1.00 12.23 ? 2136 HOH A O 1 HETATM 3124 O O . HOH K 5 . ? 31.224 23.472 38.172 1.00 36.20 ? 2137 HOH A O 1 HETATM 3125 O O . HOH K 5 . ? 30.198 26.861 36.418 1.00 33.22 ? 2138 HOH A O 1 HETATM 3126 O O . HOH K 5 . ? 28.282 29.559 35.866 1.00 31.40 ? 2139 HOH A O 1 HETATM 3127 O O . HOH K 5 . ? 8.110 11.845 -0.131 1.00 25.86 ? 2140 HOH A O 1 HETATM 3128 O O . HOH K 5 . ? 11.386 13.631 -2.231 1.00 31.88 ? 2141 HOH A O 1 HETATM 3129 O O . HOH K 5 . ? 19.421 31.635 42.543 1.00 31.42 ? 2142 HOH A O 1 HETATM 3130 O O . HOH K 5 . ? 24.003 24.873 42.850 1.00 26.53 ? 2143 HOH A O 1 HETATM 3131 O O . HOH K 5 . ? 20.130 25.999 41.044 1.00 10.54 ? 2144 HOH A O 1 HETATM 3132 O O . HOH K 5 . ? 22.272 9.478 -3.308 1.00 34.74 ? 2145 HOH A O 1 HETATM 3133 O O . HOH K 5 . ? 25.309 6.892 -1.720 1.00 30.84 ? 2146 HOH A O 1 HETATM 3134 O O . HOH K 5 . ? 27.548 4.323 12.383 1.00 28.60 ? 2147 HOH A O 1 HETATM 3135 O O . HOH K 5 . ? 14.030 29.455 40.506 1.00 34.94 ? 2148 HOH A O 1 HETATM 3136 O O . HOH K 5 . ? 15.347 31.025 39.126 1.00 20.70 ? 2149 HOH A O 1 HETATM 3137 O O . HOH K 5 . ? 17.928 24.653 42.662 1.00 36.38 ? 2150 HOH A O 1 HETATM 3138 O O . HOH K 5 . ? 22.004 -0.294 4.162 1.00 29.41 ? 2151 HOH A O 1 HETATM 3139 O O . HOH K 5 . ? 10.296 0.307 14.166 1.00 40.49 ? 2152 HOH A O 1 HETATM 3140 O O . HOH K 5 . ? 19.179 33.382 34.316 1.00 6.72 ? 2153 HOH A O 1 HETATM 3141 O O . HOH K 5 . ? 25.701 30.776 38.417 1.00 14.52 ? 2154 HOH A O 1 HETATM 3142 O O . HOH K 5 . ? 19.586 32.229 38.926 1.00 16.32 ? 2155 HOH A O 1 HETATM 3143 O O . HOH K 5 . ? 5.533 0.307 14.424 1.00 33.06 ? 2156 HOH A O 1 HETATM 3144 O O . HOH K 5 . ? 13.560 35.600 34.948 1.00 15.76 ? 2157 HOH A O 1 HETATM 3145 O O . HOH K 5 . ? 17.297 35.129 33.262 1.00 7.37 ? 2158 HOH A O 1 HETATM 3146 O O . HOH K 5 . ? 7.737 34.592 33.272 1.00 15.63 ? 2159 HOH A O 1 HETATM 3147 O O . HOH K 5 . ? 10.707 30.804 39.092 1.00 27.69 ? 2160 HOH A O 1 HETATM 3148 O O . HOH K 5 . ? 12.727 34.368 37.223 1.00 15.39 ? 2161 HOH A O 1 HETATM 3149 O O . HOH K 5 . ? 13.613 42.489 32.846 1.00 30.24 ? 2162 HOH A O 1 HETATM 3150 O O . HOH K 5 . ? 9.333 42.462 29.575 1.00 32.39 ? 2163 HOH A O 1 HETATM 3151 O O . HOH K 5 . ? 1.756 28.712 29.852 1.00 21.65 ? 2164 HOH A O 1 HETATM 3152 O O . HOH K 5 . ? -0.008 30.474 31.018 1.00 30.02 ? 2165 HOH A O 1 HETATM 3153 O O . HOH K 5 . ? 5.344 35.666 32.494 1.00 18.39 ? 2166 HOH A O 1 HETATM 3154 O O . HOH K 5 . ? 2.933 35.069 33.206 1.00 25.22 ? 2167 HOH A O 1 HETATM 3155 O O . HOH K 5 . ? 24.414 17.147 -5.169 1.00 31.44 ? 2168 HOH A O 1 HETATM 3156 O O . HOH K 5 . ? 11.975 40.705 34.102 1.00 24.08 ? 2169 HOH A O 1 HETATM 3157 O O . HOH K 5 . ? 11.344 36.713 34.977 1.00 40.04 ? 2170 HOH A O 1 HETATM 3158 O O . HOH K 5 . ? 9.569 40.430 35.961 1.00 33.74 ? 2171 HOH A O 1 HETATM 3159 O O . HOH K 5 . ? 5.697 40.282 29.586 1.00 13.22 ? 2172 HOH A O 1 HETATM 3160 O O . HOH K 5 . ? 31.867 1.450 7.311 1.00 18.23 ? 2173 HOH A O 1 HETATM 3161 O O . HOH K 5 . ? 32.688 6.240 3.413 1.00 33.67 ? 2174 HOH A O 1 HETATM 3162 O O . HOH K 5 . ? 4.267 42.255 28.458 1.00 20.67 ? 2175 HOH A O 1 HETATM 3163 O O . HOH K 5 . ? 9.684 42.907 27.141 1.00 43.84 ? 2176 HOH A O 1 HETATM 3164 O O . HOH K 5 . ? 5.837 45.048 23.283 1.00 19.71 ? 2177 HOH A O 1 HETATM 3165 O O . HOH K 5 . ? 6.773 36.107 20.531 1.00 5.43 ? 2178 HOH A O 1 HETATM 3166 O O . HOH K 5 . ? 0.554 35.833 16.825 1.00 15.02 ? 2179 HOH A O 1 HETATM 3167 O O . HOH K 5 . ? 14.290 21.501 -3.455 1.00 18.87 ? 2180 HOH A O 1 HETATM 3168 O O . HOH K 5 . ? 13.684 25.915 -3.981 1.00 26.75 ? 2181 HOH A O 1 HETATM 3169 O O . HOH K 5 . ? 11.010 21.107 -0.924 0.50 18.95 ? 2182 HOH A O 1 HETATM 3170 O O . HOH K 5 . ? 10.229 25.469 -1.692 1.00 33.05 ? 2183 HOH A O 1 HETATM 3171 O O . HOH K 5 . ? 1.075 44.597 18.442 1.00 22.40 ? 2184 HOH A O 1 HETATM 3172 O O . HOH K 5 . ? -0.096 37.144 14.584 1.00 33.09 ? 2185 HOH A O 1 HETATM 3173 O O . HOH K 5 . ? 2.696 42.874 14.658 0.30 11.65 ? 2186 HOH A O 1 HETATM 3174 O O . HOH K 5 . ? 10.875 31.822 2.723 0.50 17.96 ? 2187 HOH A O 1 HETATM 3175 O O . HOH K 5 . ? 14.221 30.620 1.002 1.00 19.27 ? 2188 HOH A O 1 HETATM 3176 O O . HOH K 5 . ? 10.646 17.969 -1.102 1.00 44.62 ? 2189 HOH A O 1 HETATM 3177 O O . HOH K 5 . ? -2.497 29.912 10.588 1.00 21.14 ? 2190 HOH A O 1 HETATM 3178 O O . HOH K 5 . ? 13.731 18.837 24.093 1.00 7.73 ? 2191 HOH A O 1 HETATM 3179 O O . HOH K 5 . ? 20.523 21.018 25.240 1.00 6.07 ? 2192 HOH A O 1 HETATM 3180 O O . HOH K 5 . ? 27.901 17.754 20.724 1.00 26.62 ? 2193 HOH A O 1 HETATM 3181 O O . HOH K 5 . ? 30.319 11.052 20.740 1.00 23.49 ? 2194 HOH A O 1 HETATM 3182 O O . HOH K 5 . ? 41.271 18.995 25.789 1.00 31.19 ? 2195 HOH A O 1 HETATM 3183 O O . HOH K 5 . ? 16.572 7.205 30.310 1.00 22.54 ? 2196 HOH A O 1 HETATM 3184 O O . HOH K 5 . ? 41.571 29.420 6.062 1.00 34.82 ? 2197 HOH A O 1 HETATM 3185 O O . HOH K 5 . ? 39.702 18.886 3.694 1.00 32.90 ? 2198 HOH A O 1 HETATM 3186 O O . HOH K 5 . ? 16.762 3.784 26.846 1.00 31.22 ? 2199 HOH A O 1 HETATM 3187 O O . HOH K 5 . ? 40.943 29.903 12.533 1.00 37.21 ? 2200 HOH A O 1 HETATM 3188 O O . HOH K 5 . ? 24.166 2.765 24.162 1.00 32.05 ? 2201 HOH A O 1 HETATM 3189 O O . HOH K 5 . ? 40.372 31.933 14.155 1.00 34.64 ? 2202 HOH A O 1 HETATM 3190 O O . HOH K 5 . ? 25.327 5.532 34.810 1.00 9.39 ? 2203 HOH A O 1 HETATM 3191 O O . HOH K 5 . ? 21.244 4.862 27.712 1.00 14.58 ? 2204 HOH A O 1 HETATM 3192 O O . HOH K 5 . ? 27.975 5.847 34.637 1.00 11.07 ? 2205 HOH A O 1 HETATM 3193 O O . HOH K 5 . ? 26.864 5.266 25.140 1.00 26.86 ? 2206 HOH A O 1 HETATM 3194 O O . HOH K 5 . ? 28.220 21.018 30.112 1.00 10.39 ? 2207 HOH A O 1 HETATM 3195 O O . HOH K 5 . ? 31.900 17.757 29.986 1.00 38.92 ? 2208 HOH A O 1 HETATM 3196 O O . HOH K 5 . ? 31.808 18.597 32.786 1.00 32.93 ? 2209 HOH A O 1 HETATM 3197 O O . HOH K 5 . ? 30.836 11.811 32.367 1.00 12.50 ? 2210 HOH A O 1 HETATM 3198 O O . HOH K 5 . ? 17.819 24.947 -9.754 1.00 29.81 ? 2211 HOH A O 1 HETATM 3199 O O . HOH K 5 . ? 15.566 26.423 -7.237 1.00 37.34 ? 2212 HOH A O 1 HETATM 3200 O O . HOH K 5 . ? 21.693 27.133 -11.392 1.00 33.75 ? 2213 HOH A O 1 HETATM 3201 O O . HOH K 5 . ? 20.031 8.248 36.769 1.00 36.86 ? 2214 HOH A O 1 HETATM 3202 O O . HOH K 5 . ? 19.541 12.020 37.190 1.00 11.18 ? 2215 HOH A O 1 HETATM 3203 O O . HOH K 5 . ? 23.081 5.464 36.355 1.00 28.12 ? 2216 HOH A O 1 HETATM 3204 O O . HOH K 5 . ? 19.832 15.552 37.520 1.00 11.05 ? 2217 HOH A O 1 HETATM 3205 O O . HOH K 5 . ? 23.363 15.146 39.785 1.00 30.21 ? 2218 HOH A O 1 HETATM 3206 O O . HOH K 5 . ? 20.130 12.955 39.575 0.50 19.71 ? 2219 HOH A O 1 HETATM 3207 O O . HOH K 5 . ? 16.343 16.502 39.645 1.00 24.10 ? 2220 HOH A O 1 HETATM 3208 O O . HOH K 5 . ? 17.291 19.075 39.215 1.00 22.78 ? 2221 HOH A O 1 HETATM 3209 O O . HOH K 5 . ? 15.658 9.259 31.991 1.00 28.75 ? 2222 HOH A O 1 HETATM 3210 O O . HOH K 5 . ? 5.961 14.733 36.615 1.00 44.17 ? 2223 HOH A O 1 HETATM 3211 O O . HOH K 5 . ? 9.162 12.384 32.319 0.50 22.19 ? 2224 HOH A O 1 HETATM 3212 O O . HOH K 5 . ? 12.889 13.163 37.059 1.00 41.60 ? 2225 HOH A O 1 HETATM 3213 O O . HOH K 5 . ? 10.560 22.231 38.069 1.00 37.73 ? 2226 HOH A O 1 HETATM 3214 O O . HOH K 5 . ? 9.370 20.589 36.010 1.00 17.85 ? 2227 HOH A O 1 HETATM 3215 O O . HOH K 5 . ? 15.005 19.234 26.356 1.00 8.69 ? 2228 HOH A O 1 HETATM 3216 O O . HOH K 5 . ? 1.373 25.837 31.488 1.00 37.05 ? 2229 HOH A O 1 HETATM 3217 O O . HOH K 5 . ? 1.470 23.113 36.605 1.00 41.15 ? 2230 HOH A O 1 HETATM 3218 O O . HOH K 5 . ? 17.133 36.506 37.399 1.00 30.41 ? 2231 HOH A O 1 HETATM 3219 O O . HOH K 5 . ? 3.399 30.662 34.517 1.00 28.99 ? 2232 HOH A O 1 HETATM 3220 O O . HOH K 5 . ? 6.028 24.838 35.817 1.00 36.46 ? 2233 HOH A O 1 HETATM 3221 O O . HOH K 5 . ? -0.936 27.225 24.109 1.00 12.56 ? 2234 HOH A O 1 HETATM 3222 O O . HOH K 5 . ? -2.018 23.583 26.735 1.00 10.57 ? 2235 HOH A O 1 HETATM 3223 O O . HOH K 5 . ? 0.870 24.049 29.976 1.00 17.85 ? 2236 HOH A O 1 HETATM 3224 O O . HOH K 5 . ? -1.829 28.567 26.927 1.00 31.99 ? 2237 HOH A O 1 HETATM 3225 O O . HOH K 5 . ? 16.012 19.552 -3.142 1.00 28.32 ? 2238 HOH A O 1 HETATM 3226 O O . HOH K 5 . ? -0.136 27.035 21.263 1.00 12.92 ? 2239 HOH A O 1 HETATM 3227 O O . HOH K 5 . ? -3.019 28.837 19.466 1.00 13.63 ? 2240 HOH A O 1 HETATM 3228 O O . HOH K 5 . ? -0.052 34.285 23.341 1.00 7.84 ? 2241 HOH A O 1 HETATM 3229 O O . HOH K 5 . ? 15.287 16.604 23.378 1.00 6.27 ? 2242 HOH A O 1 HETATM 3230 O O . HOH K 5 . ? 20.378 16.701 18.791 1.00 13.16 ? 2243 HOH A O 1 HETATM 3231 O O . HOH K 5 . ? 17.721 15.853 22.417 1.00 5.44 ? 2244 HOH A O 1 HETATM 3232 O O . HOH K 5 . ? 17.886 16.916 15.827 1.00 7.23 ? 2245 HOH A O 1 HETATM 3233 O O . HOH K 5 . ? 25.695 8.642 14.361 1.00 23.93 ? 2246 HOH A O 1 HETATM 3234 O O . HOH K 5 . ? 25.889 5.597 13.758 1.00 32.26 ? 2247 HOH A O 1 HETATM 3235 O O . HOH K 5 . ? 13.403 -0.240 19.332 1.00 14.88 ? 2248 HOH A O 1 HETATM 3236 O O . HOH K 5 . ? 19.794 -1.045 15.787 1.00 14.49 ? 2249 HOH A O 1 HETATM 3237 O O . HOH K 5 . ? 14.641 -1.691 21.719 1.00 20.62 ? 2250 HOH A O 1 HETATM 3238 O O . HOH K 5 . ? 18.454 0.101 23.144 1.00 40.14 ? 2251 HOH A O 1 HETATM 3239 O O . HOH K 5 . ? 21.656 0.819 20.118 1.00 27.90 ? 2252 HOH A O 1 HETATM 3240 O O . HOH K 5 . ? 23.198 3.942 19.554 1.00 25.48 ? 2253 HOH A O 1 HETATM 3241 O O . HOH K 5 . ? 11.469 -2.237 19.323 1.00 32.03 ? 2254 HOH A O 1 HETATM 3242 O O . HOH K 5 . ? 8.245 -3.917 24.572 1.00 45.75 ? 2255 HOH A O 1 HETATM 3243 O O . HOH K 5 . ? 12.957 5.170 27.232 1.00 25.55 ? 2256 HOH A O 1 HETATM 3244 O O . HOH K 5 . ? 8.521 -0.616 28.267 1.00 43.74 ? 2257 HOH A O 1 HETATM 3245 O O . HOH K 5 . ? 5.934 6.399 27.322 1.00 13.36 ? 2258 HOH A O 1 HETATM 3246 O O . HOH K 5 . ? 10.796 6.481 29.516 1.00 32.03 ? 2259 HOH A O 1 HETATM 3247 O O . HOH K 5 . ? 6.118 1.817 25.964 1.00 18.09 ? 2260 HOH A O 1 HETATM 3248 O O . HOH K 5 . ? 2.191 10.869 25.176 1.00 6.03 ? 2261 HOH A O 1 HETATM 3249 O O . HOH K 5 . ? -2.334 15.260 21.915 0.50 19.24 ? 2262 HOH A O 1 HETATM 3250 O O . HOH K 5 . ? 2.351 9.462 32.653 1.00 24.03 ? 2263 HOH A O 1 HETATM 3251 O O . HOH K 5 . ? 3.353 7.523 26.969 1.00 13.64 ? 2264 HOH A O 1 HETATM 3252 O O . HOH K 5 . ? 5.479 17.040 35.907 1.00 36.51 ? 2265 HOH A O 1 HETATM 3253 O O . HOH K 5 . ? 0.143 21.496 30.374 1.00 17.96 ? 2266 HOH A O 1 HETATM 3254 O O . HOH K 5 . ? -2.214 21.463 28.647 1.00 24.84 ? 2267 HOH A O 1 HETATM 3255 O O . HOH K 5 . ? -3.356 18.715 30.431 1.00 18.24 ? 2268 HOH A O 1 HETATM 3256 O O . HOH K 5 . ? -3.478 19.781 27.256 1.00 32.48 ? 2269 HOH A O 1 HETATM 3257 O O . HOH K 5 . ? -3.145 18.683 23.929 1.00 28.92 ? 2270 HOH A O 1 HETATM 3258 O O . HOH K 5 . ? -5.124 29.121 21.429 1.00 26.97 ? 2271 HOH A O 1 HETATM 3259 O O . HOH K 5 . ? -1.477 20.691 19.810 1.00 25.32 ? 2272 HOH A O 1 HETATM 3260 O O . HOH K 5 . ? -1.943 26.269 19.256 1.00 20.88 ? 2273 HOH A O 1 HETATM 3261 O O . HOH K 5 . ? 0.583 23.584 18.408 1.00 17.16 ? 2274 HOH A O 1 HETATM 3262 O O . HOH K 5 . ? 0.170 19.228 21.864 1.00 8.83 ? 2275 HOH A O 1 HETATM 3263 O O . HOH K 5 . ? -3.055 19.611 13.317 1.00 29.45 ? 2276 HOH A O 1 HETATM 3264 O O . HOH K 5 . ? 20.576 16.021 14.898 1.00 11.63 ? 2277 HOH A O 1 HETATM 3265 O O . HOH K 5 . ? 27.189 19.816 13.808 1.00 8.90 ? 2278 HOH A O 1 HETATM 3266 O O . HOH K 5 . ? 24.724 13.832 9.880 1.00 6.49 ? 2279 HOH A O 1 HETATM 3267 O O . HOH K 5 . ? 21.070 10.520 5.380 1.00 7.00 ? 2280 HOH A O 1 HETATM 3268 O O . HOH K 5 . ? 9.548 13.908 -0.390 1.00 17.95 ? 2281 HOH A O 1 HETATM 3269 O O . HOH K 5 . ? 10.291 10.435 -1.197 1.00 29.19 ? 2282 HOH A O 1 HETATM 3270 O O . HOH K 5 . ? 16.392 12.279 -3.638 1.00 33.07 ? 2283 HOH A O 1 HETATM 3271 O O . HOH K 5 . ? 13.548 6.168 -1.177 1.00 32.77 ? 2284 HOH A O 1 HETATM 3272 O O . HOH K 5 . ? 13.820 7.816 -3.235 1.00 43.78 ? 2285 HOH A O 1 HETATM 3273 O O . HOH K 5 . ? 18.133 9.842 -4.489 1.00 26.85 ? 2286 HOH A O 1 HETATM 3274 O O . HOH K 5 . ? 20.363 8.126 -4.016 1.00 33.41 ? 2287 HOH A O 1 HETATM 3275 O O . HOH K 5 . ? 23.036 8.276 -1.229 1.00 21.08 ? 2288 HOH A O 1 HETATM 3276 O O . HOH K 5 . ? 31.374 4.337 4.695 1.00 26.90 ? 2289 HOH A O 1 HETATM 3277 O O . HOH K 5 . ? 23.633 11.538 4.574 1.00 6.34 ? 2290 HOH A O 1 HETATM 3278 O O . HOH K 5 . ? 29.253 5.474 10.202 1.00 11.47 ? 2291 HOH A O 1 HETATM 3279 O O . HOH K 5 . ? 26.750 3.209 10.256 1.00 23.04 ? 2292 HOH A O 1 HETATM 3280 O O . HOH K 5 . ? 29.529 2.019 8.377 1.00 25.57 ? 2293 HOH A O 1 HETATM 3281 O O . HOH K 5 . ? 21.986 1.885 5.578 1.00 11.15 ? 2294 HOH A O 1 HETATM 3282 O O . HOH K 5 . ? 15.757 0.529 4.437 1.00 19.89 ? 2295 HOH A O 1 HETATM 3283 O O . HOH K 5 . ? 12.277 1.587 8.013 1.00 24.94 ? 2296 HOH A O 1 HETATM 3284 O O . HOH K 5 . ? 12.683 0.727 12.174 1.00 17.99 ? 2297 HOH A O 1 HETATM 3285 O O . HOH K 5 . ? 13.633 7.670 1.394 1.00 10.39 ? 2298 HOH A O 1 HETATM 3286 O O . HOH K 5 . ? 9.587 7.686 -0.919 1.00 28.91 ? 2299 HOH A O 1 HETATM 3287 O O . HOH K 5 . ? 6.603 6.451 0.404 1.00 23.16 ? 2300 HOH A O 1 HETATM 3288 O O . HOH K 5 . ? 11.327 6.223 2.128 1.00 20.97 ? 2301 HOH A O 1 HETATM 3289 O O . HOH K 5 . ? 13.513 1.618 1.481 1.00 30.99 ? 2302 HOH A O 1 HETATM 3290 O O . HOH K 5 . ? 10.504 3.609 7.734 1.00 13.31 ? 2303 HOH A O 1 HETATM 3291 O O . HOH K 5 . ? 4.524 5.591 9.200 0.50 12.97 ? 2304 HOH A O 1 HETATM 3292 O O . HOH K 5 . ? 10.099 4.674 5.143 1.00 20.85 ? 2305 HOH A O 1 HETATM 3293 O O . HOH K 5 . ? 5.229 7.649 2.387 1.00 19.19 ? 2306 HOH A O 1 HETATM 3294 O O . HOH K 5 . ? 7.956 1.402 13.430 1.00 19.32 ? 2307 HOH A O 1 HETATM 3295 O O . HOH K 5 . ? 0.482 3.709 16.052 1.00 21.94 ? 2308 HOH A O 1 HETATM 3296 O O . HOH K 5 . ? -1.934 9.197 12.604 0.50 24.91 ? 2309 HOH A O 1 HETATM 3297 O O . HOH K 5 . ? 1.185 6.801 13.058 1.00 29.04 ? 2310 HOH A O 1 HETATM 3298 O O . HOH K 5 . ? -2.806 10.643 13.790 0.50 22.07 ? 2311 HOH A O 1 HETATM 3299 O O . HOH K 5 . ? -4.705 8.312 16.856 1.00 18.48 ? 2312 HOH A O 1 HETATM 3300 O O . HOH K 5 . ? 5.893 -1.250 20.224 1.00 35.74 ? 2313 HOH A O 1 HETATM 3301 O O . HOH K 5 . ? 5.514 -1.560 24.648 1.00 33.00 ? 2314 HOH A O 1 HETATM 3302 O O . HOH K 5 . ? 3.952 0.459 19.197 1.00 20.93 ? 2315 HOH A O 1 HETATM 3303 O O . HOH K 5 . ? -2.559 12.797 22.045 0.50 5.82 ? 2316 HOH A O 1 HETATM 3304 O O . HOH K 5 . ? -0.691 15.227 14.978 1.00 25.34 ? 2317 HOH A O 1 HETATM 3305 O O . HOH K 5 . ? -0.483 13.760 11.077 1.00 26.85 ? 2318 HOH A O 1 HETATM 3306 O O . HOH K 5 . ? 21.461 23.154 8.921 1.00 4.92 ? 2319 HOH A O 1 HETATM 3307 O O . HOH K 5 . ? 18.239 19.228 1.314 1.00 7.88 ? 2320 HOH A O 1 HETATM 3308 O O . HOH K 5 . ? 22.260 26.383 6.444 1.00 7.29 ? 2321 HOH A O 1 HETATM 3309 O O . HOH K 5 . ? 23.185 21.235 9.909 1.00 4.71 ? 2322 HOH A O 1 HETATM 3310 O O . HOH K 5 . ? 20.976 19.853 7.360 1.00 5.15 ? 2323 HOH A O 1 HETATM 3311 O O . HOH K 5 . ? 30.323 12.731 -2.518 1.00 13.92 ? 2324 HOH A O 1 HETATM 3312 O O . HOH K 5 . ? 25.056 18.151 2.238 1.00 4.40 ? 2325 HOH A O 1 HETATM 3313 O O . HOH K 5 . ? 22.818 15.537 -3.727 1.00 20.72 ? 2326 HOH A O 1 HETATM 3314 O O . HOH K 5 . ? 27.613 13.446 -3.285 1.00 30.68 ? 2327 HOH A O 1 HETATM 3315 O O . HOH K 5 . ? 30.303 9.548 1.035 1.00 18.42 ? 2328 HOH A O 1 HETATM 3316 O O . HOH K 5 . ? 35.421 12.574 2.795 1.00 20.07 ? 2329 HOH A O 1 HETATM 3317 O O . HOH K 5 . ? 24.577 12.687 6.788 1.00 7.05 ? 2330 HOH A O 1 HETATM 3318 O O . HOH K 5 . ? 32.252 8.788 2.880 1.00 19.02 ? 2331 HOH A O 1 HETATM 3319 O O . HOH K 5 . ? 34.094 2.279 9.085 1.00 8.81 ? 2332 HOH A O 1 HETATM 3320 O O . HOH K 5 . ? 36.591 5.867 10.860 1.00 11.07 ? 2333 HOH A O 1 HETATM 3321 O O . HOH K 5 . ? 35.750 5.423 7.066 1.00 35.70 ? 2334 HOH A O 1 HETATM 3322 O O . HOH K 5 . ? 31.495 4.346 7.313 0.50 9.68 ? 2335 HOH A O 1 HETATM 3323 O O . HOH K 5 . ? 26.761 13.075 13.425 1.00 15.25 ? 2336 HOH A O 1 HETATM 3324 O O . HOH K 5 . ? 27.643 7.063 15.120 1.00 28.81 ? 2337 HOH A O 1 HETATM 3325 O O . HOH K 5 . ? 29.918 7.089 13.617 1.00 13.67 ? 2338 HOH A O 1 HETATM 3326 O O . HOH K 5 . ? 28.939 11.472 17.258 1.00 22.64 ? 2339 HOH A O 1 HETATM 3327 O O . HOH K 5 . ? 34.320 9.331 15.634 1.00 32.72 ? 2340 HOH A O 1 HETATM 3328 O O . HOH K 5 . ? 29.587 13.228 19.519 1.00 21.00 ? 2341 HOH A O 1 HETATM 3329 O O . HOH K 5 . ? 29.016 15.351 20.817 1.00 19.09 ? 2342 HOH A O 1 HETATM 3330 O O . HOH K 5 . ? 30.693 24.638 9.974 1.00 13.62 ? 2343 HOH A O 1 HETATM 3331 O O . HOH K 5 . ? 34.565 19.425 0.593 1.00 15.63 ? 2344 HOH A O 1 HETATM 3332 O O . HOH K 5 . ? 14.093 23.925 -2.179 1.00 10.92 ? 2345 HOH A O 1 HETATM 3333 O O . HOH K 5 . ? 17.853 30.261 -5.047 1.00 25.92 ? 2346 HOH A O 1 HETATM 3334 O O . HOH K 5 . ? 16.697 30.568 -2.211 0.50 20.86 ? 2347 HOH A O 1 HETATM 3335 O O . HOH K 5 . ? 19.862 25.450 -1.283 0.50 7.19 ? 2348 HOH A O 1 HETATM 3336 O O . HOH K 5 . ? 11.974 23.802 -0.412 1.00 12.61 ? 2349 HOH A O 1 HETATM 3337 O O . HOH K 5 . ? 10.337 28.053 0.061 1.00 36.03 ? 2350 HOH A O 1 HETATM 3338 O O . HOH K 5 . ? 12.302 29.688 2.323 1.00 19.34 ? 2351 HOH A O 1 HETATM 3339 O O . HOH K 5 . ? 7.192 27.520 0.501 1.00 33.80 ? 2352 HOH A O 1 HETATM 3340 O O . HOH K 5 . ? 3.270 20.491 5.884 1.00 20.42 ? 2353 HOH A O 1 HETATM 3341 O O . HOH K 5 . ? 6.234 27.904 3.419 1.00 20.28 ? 2354 HOH A O 1 HETATM 3342 O O . HOH K 5 . ? 7.840 22.765 -1.681 1.00 34.46 ? 2355 HOH A O 1 HETATM 3343 O O . HOH K 5 . ? 2.426 28.080 0.068 1.00 32.37 ? 2356 HOH A O 1 HETATM 3344 O O . HOH K 5 . ? 9.061 19.954 -0.340 0.50 24.01 ? 2357 HOH A O 1 HETATM 3345 O O . HOH K 5 . ? 1.518 21.908 1.424 1.00 23.18 ? 2358 HOH A O 1 HETATM 3346 O O . HOH K 5 . ? 5.574 19.567 -1.625 1.00 23.77 ? 2359 HOH A O 1 HETATM 3347 O O . HOH K 5 . ? 8.036 16.305 -0.774 1.00 28.14 ? 2360 HOH A O 1 HETATM 3348 O O . HOH K 5 . ? 2.507 19.857 2.075 1.00 21.05 ? 2361 HOH A O 1 HETATM 3349 O O . HOH K 5 . ? 6.282 13.225 0.308 1.00 34.44 ? 2362 HOH A O 1 HETATM 3350 O O . HOH K 5 . ? 2.012 17.874 6.855 1.00 30.92 ? 2363 HOH A O 1 HETATM 3351 O O . HOH K 5 . ? -2.535 8.983 7.548 1.00 32.83 ? 2364 HOH A O 1 HETATM 3352 O O . HOH K 5 . ? 3.773 8.160 5.787 1.00 24.82 ? 2365 HOH A O 1 HETATM 3353 O O . HOH K 5 . ? -2.726 10.916 4.430 1.00 20.17 ? 2366 HOH A O 1 HETATM 3354 O O . HOH K 5 . ? 1.337 19.568 8.620 1.00 19.40 ? 2367 HOH A O 1 HETATM 3355 O O . HOH K 5 . ? 24.983 22.869 17.307 1.00 32.61 ? 2368 HOH A O 1 HETATM 3356 O O . HOH K 5 . ? 27.347 23.991 16.199 0.60 24.71 ? 2369 HOH A O 1 HETATM 3357 O O . HOH K 5 . ? 24.620 27.456 17.159 0.50 19.31 ? 2370 HOH A O 1 HETATM 3358 O O . HOH K 5 . ? 25.322 28.291 15.156 0.50 15.41 ? 2371 HOH A O 1 HETATM 3359 O O . HOH K 5 . ? 21.884 29.036 7.056 1.00 30.58 ? 2372 HOH A O 1 HETATM 3360 O O . HOH K 5 . ? 28.268 25.633 9.239 1.00 7.21 ? 2373 HOH A O 1 HETATM 3361 O O . HOH K 5 . ? 23.548 29.983 15.467 1.00 26.03 ? 2374 HOH A O 1 HETATM 3362 O O . HOH K 5 . ? 26.867 25.784 11.380 0.40 3.95 ? 2375 HOH A O 1 HETATM 3363 O O . HOH K 5 . ? 26.801 29.515 16.210 0.50 22.25 ? 2376 HOH A O 1 HETATM 3364 O O . HOH K 5 . ? 28.920 22.611 17.883 1.00 36.89 ? 2377 HOH A O 1 HETATM 3365 O O . HOH K 5 . ? 32.303 22.605 19.752 1.00 18.81 ? 2378 HOH A O 1 HETATM 3366 O O . HOH K 5 . ? 40.432 28.528 17.419 1.00 28.56 ? 2379 HOH A O 1 HETATM 3367 O O . HOH K 5 . ? 36.334 21.926 18.915 1.00 9.09 ? 2380 HOH A O 1 HETATM 3368 O O . HOH K 5 . ? 42.947 19.767 14.185 1.00 23.66 ? 2381 HOH A O 1 HETATM 3369 O O . HOH K 5 . ? 43.633 23.601 12.788 0.75 21.37 ? 2382 HOH A O 1 HETATM 3370 O O . HOH K 5 . ? 43.867 25.390 14.080 0.25 17.07 ? 2383 HOH A O 1 HETATM 3371 O O . HOH K 5 . ? 46.713 28.306 19.254 1.00 35.90 ? 2384 HOH A O 1 HETATM 3372 O O . HOH K 5 . ? 42.628 29.010 18.625 1.00 36.03 ? 2385 HOH A O 1 HETATM 3373 O O . HOH K 5 . ? 43.648 18.053 22.644 1.00 32.68 ? 2386 HOH A O 1 HETATM 3374 O O . HOH K 5 . ? 45.897 22.293 16.527 1.00 27.59 ? 2387 HOH A O 1 HETATM 3375 O O . HOH K 5 . ? 42.661 21.263 24.369 1.00 23.53 ? 2388 HOH A O 1 HETATM 3376 O O . HOH K 5 . ? 43.504 23.660 26.663 1.00 33.30 ? 2389 HOH A O 1 HETATM 3377 O O . HOH K 5 . ? 47.938 27.422 21.963 1.00 41.10 ? 2390 HOH A O 1 HETATM 3378 O O . HOH K 5 . ? 41.406 28.296 24.833 1.00 23.69 ? 2391 HOH A O 1 HETATM 3379 O O . HOH K 5 . ? 35.297 29.759 31.300 1.00 32.37 ? 2392 HOH A O 1 HETATM 3380 O O . HOH K 5 . ? 38.054 26.978 23.795 1.00 23.55 ? 2393 HOH A O 1 HETATM 3381 O O . HOH K 5 . ? 33.054 22.346 23.023 1.00 21.20 ? 2394 HOH A O 1 HETATM 3382 O O . HOH K 5 . ? 34.621 23.469 20.520 1.00 17.02 ? 2395 HOH A O 1 HETATM 3383 O O . HOH K 5 . ? 37.818 25.167 30.540 1.00 34.97 ? 2396 HOH A O 1 HETATM 3384 O O . HOH K 5 . ? 38.073 16.677 22.766 1.00 11.08 ? 2397 HOH A O 1 HETATM 3385 O O . HOH K 5 . ? 38.591 20.038 25.606 1.00 20.28 ? 2398 HOH A O 1 HETATM 3386 O O . HOH K 5 . ? 42.381 15.463 18.276 1.00 16.66 ? 2399 HOH A O 1 HETATM 3387 O O . HOH K 5 . ? 31.770 15.264 21.302 1.00 9.91 ? 2400 HOH A O 1 HETATM 3388 O O . HOH K 5 . ? 31.729 20.235 21.281 1.00 15.90 ? 2401 HOH A O 1 HETATM 3389 O O . HOH K 5 . ? 40.690 14.360 16.244 1.00 11.16 ? 2402 HOH A O 1 HETATM 3390 O O . HOH K 5 . ? 32.720 11.420 21.848 1.00 15.74 ? 2403 HOH A O 1 HETATM 3391 O O . HOH K 5 . ? 35.011 8.573 18.301 1.00 12.27 ? 2404 HOH A O 1 HETATM 3392 O O . HOH K 5 . ? 33.320 15.371 13.207 1.00 6.23 ? 2405 HOH A O 1 HETATM 3393 O O . HOH K 5 . ? 31.412 10.043 17.847 1.00 18.62 ? 2406 HOH A O 1 HETATM 3394 O O . HOH K 5 . ? 36.820 21.472 12.000 1.00 7.73 ? 2407 HOH A O 1 HETATM 3395 O O . HOH K 5 . ? 43.581 17.161 14.198 1.00 28.33 ? 2408 HOH A O 1 HETATM 3396 O O . HOH K 5 . ? 42.546 8.246 6.076 1.00 34.64 ? 2409 HOH A O 1 HETATM 3397 O O . HOH K 5 . ? 39.336 17.908 5.937 1.00 26.53 ? 2410 HOH A O 1 HETATM 3398 O O . HOH K 5 . ? 37.336 8.438 9.642 1.00 17.43 ? 2411 HOH A O 1 HETATM 3399 O O . HOH K 5 . ? 40.419 11.410 11.210 1.00 14.12 ? 2412 HOH A O 1 HETATM 3400 O O . HOH K 5 . ? 33.387 15.858 10.462 1.00 7.72 ? 2413 HOH A O 1 HETATM 3401 O O . HOH K 5 . ? 40.458 20.506 5.952 1.00 22.06 ? 2414 HOH A O 1 HETATM 3402 O O . HOH K 5 . ? 39.437 25.978 5.524 0.40 16.33 ? 2415 HOH A O 1 HETATM 3403 O O . HOH K 5 . ? 39.579 29.551 10.148 1.00 28.71 ? 2416 HOH A O 1 HETATM 3404 O O . HOH K 5 . ? 39.728 27.689 6.835 0.60 17.52 ? 2417 HOH A O 1 HETATM 3405 O O . HOH K 5 . ? 41.858 27.271 14.292 1.00 27.97 ? 2418 HOH A O 1 HETATM 3406 O O . HOH K 5 . ? 34.211 27.960 22.393 1.00 37.01 ? 2419 HOH A O 1 HETATM 3407 O O . HOH K 5 . ? 38.948 31.004 16.713 1.00 25.08 ? 2420 HOH A O 1 HETATM 3408 O O . HOH K 5 . ? 35.309 25.823 19.703 1.00 17.00 ? 2421 HOH A O 1 HETATM 3409 O O . HOH K 5 . ? 27.319 33.103 15.417 1.00 19.08 ? 2422 HOH A O 1 HETATM 3410 O O . HOH K 5 . ? 34.016 33.141 20.584 1.00 41.65 ? 2423 HOH A O 1 HETATM 3411 O O . HOH K 5 . ? 38.651 32.837 19.500 1.00 37.97 ? 2424 HOH A O 1 HETATM 3412 O O . HOH K 5 . ? 37.461 31.130 9.474 1.00 27.10 ? 2425 HOH A O 1 HETATM 3413 O O . HOH K 5 . ? 36.100 32.968 8.476 1.00 18.05 ? 2426 HOH A O 1 HETATM 3414 O O . HOH K 5 . ? 37.392 32.721 2.687 1.00 26.88 ? 2427 HOH A O 1 HETATM 3415 O O . HOH K 5 . ? 35.850 26.367 0.607 1.00 23.55 ? 2428 HOH A O 1 HETATM 3416 O O . HOH K 5 . ? 37.670 30.215 6.600 1.00 14.36 ? 2429 HOH A O 1 HETATM 3417 O O . HOH K 5 . ? 35.597 21.768 1.400 1.00 13.65 ? 2430 HOH A O 1 HETATM 3418 O O . HOH K 5 . ? 25.132 27.765 -5.237 0.70 11.94 ? 2431 HOH A O 1 HETATM 3419 O O . HOH K 5 . ? 29.394 25.122 -7.675 1.00 30.48 ? 2432 HOH A O 1 HETATM 3420 O O . HOH K 5 . ? 36.954 27.644 -8.484 1.00 25.06 ? 2433 HOH A O 1 HETATM 3421 O O . HOH K 5 . ? 32.463 24.168 -7.131 0.50 18.73 ? 2434 HOH A O 1 HETATM 3422 O O . HOH K 5 . ? 33.120 20.023 -1.567 1.00 11.20 ? 2435 HOH A O 1 HETATM 3423 O O . HOH K 5 . ? 31.646 18.508 -3.470 1.00 10.73 ? 2436 HOH A O 1 HETATM 3424 O O . HOH K 5 . ? 23.600 21.405 -7.244 1.00 35.99 ? 2437 HOH A O 1 HETATM 3425 O O . HOH K 5 . ? 25.671 23.980 -6.384 1.00 17.37 ? 2438 HOH A O 1 HETATM 3426 O O . HOH K 5 . ? 17.981 26.853 -7.820 1.00 22.77 ? 2439 HOH A O 1 HETATM 3427 O O . HOH K 5 . ? 22.958 33.890 -7.738 1.00 33.80 ? 2440 HOH A O 1 HETATM 3428 O O . HOH K 5 . ? 19.412 32.257 -5.941 1.00 26.74 ? 2441 HOH A O 1 HETATM 3429 O O . HOH K 5 . ? 25.325 30.785 -9.053 0.50 23.91 ? 2442 HOH A O 1 HETATM 3430 O O . HOH K 5 . ? 24.573 29.192 -10.661 0.50 18.92 ? 2443 HOH A O 1 HETATM 3431 O O . HOH K 5 . ? 26.221 28.783 -6.440 0.30 16.89 ? 2444 HOH A O 1 HETATM 3432 O O . HOH K 5 . ? 16.278 39.550 33.977 1.00 21.51 ? 2445 HOH A O 1 HETATM 3433 O O . HOH K 5 . ? 16.093 36.973 34.809 1.00 20.38 ? 2446 HOH A O 1 HETATM 3434 O O . HOH K 5 . ? 19.172 39.922 37.080 1.00 16.89 ? 2447 HOH A O 1 HETATM 3435 O O . HOH K 5 . ? 24.693 37.975 34.233 1.00 17.46 ? 2448 HOH A O 1 HETATM 3436 O O . HOH K 5 . ? 26.290 34.814 35.467 1.00 13.80 ? 2449 HOH A O 1 HETATM 3437 O O . HOH K 5 . ? 13.958 15.145 -1.558 1.00 32.47 ? 2450 HOH A O 1 HETATM 3438 O O . HOH K 5 . ? 18.232 19.225 -1.583 1.00 11.42 ? 2451 HOH A O 1 HETATM 3439 O O . HOH K 5 . ? 27.518 32.895 18.627 1.00 28.41 ? 2452 HOH A O 1 HETATM 3440 O O . HOH K 5 . ? 22.297 33.046 13.174 1.00 9.69 ? 2453 HOH A O 1 HETATM 3441 O O . HOH K 5 . ? 25.315 10.968 15.817 0.50 19.85 ? 2454 HOH A O 1 HETATM 3442 O O . HOH K 5 . ? 25.882 13.546 21.776 1.00 36.51 ? 2455 HOH A O 1 HETATM 3443 O O . HOH K 5 . ? 28.887 10.584 22.871 1.00 34.68 ? 2456 HOH A O 1 HETATM 3444 O O . HOH K 5 . ? 25.126 6.981 22.172 1.00 19.56 ? 2457 HOH A O 1 HETATM 3445 O O . HOH K 5 . ? -3.133 19.479 21.222 1.00 34.63 ? 2458 HOH A O 1 HETATM 3446 O O . HOH K 5 . ? 28.703 8.323 24.439 1.00 24.80 ? 2459 HOH A O 1 HETATM 3447 O O . HOH K 5 . ? 32.673 10.519 30.775 1.00 22.90 ? 2460 HOH A O 1 HETATM 3448 O O . HOH K 5 . ? 23.908 19.555 18.351 0.60 22.10 ? 2461 HOH A O 1 HETATM 3449 O O . HOH K 5 . ? 27.192 21.392 16.134 1.00 23.30 ? 2462 HOH A O 1 HETATM 3450 O O . HOH K 5 . ? 25.634 12.380 15.832 0.50 15.86 ? 2463 HOH A O 1 HETATM 3451 O O . HOH K 5 . ? 21.719 18.784 17.433 1.00 17.84 ? 2464 HOH A O 1 HETATM 3452 O O . HOH K 5 . ? 21.636 14.965 17.052 1.00 12.56 ? 2465 HOH A O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . ALA A 1 ? 0.1171 0.1330 0.1477 0.0139 0.0001 -0.0044 87 ALA A N 2 C CA . ALA A 1 ? 0.1623 0.1475 0.1649 0.0036 -0.0037 -0.0066 87 ALA A CA 3 C C . ALA A 1 ? 0.1500 0.1379 0.1607 0.0089 -0.0036 -0.0071 87 ALA A C 4 O O . ALA A 1 ? 0.1373 0.1357 0.1626 0.0155 -0.0147 -0.0246 87 ALA A O 5 C CB . ALA A 1 ? 0.1670 0.1511 0.1640 0.0015 -0.0019 -0.0028 87 ALA A CB 6 N N . PRO A 2 ? 0.1587 0.1603 0.1697 0.0145 -0.0030 -0.0108 88 PRO A N 7 C CA . PRO A 2 ? 0.1582 0.1567 0.1578 0.0059 -0.0115 0.0027 88 PRO A CA 8 C C . PRO A 2 ? 0.1628 0.1462 0.1619 0.0080 0.0005 -0.0037 88 PRO A C 9 O O . PRO A 2 ? 0.1770 0.1483 0.1541 0.0103 -0.0119 -0.0075 88 PRO A O 10 C CB . PRO A 2 ? 0.1823 0.1819 0.1895 0.0045 -0.0021 -0.0039 88 PRO A CB 11 C CG . PRO A 2 ? 0.1804 0.1898 0.1990 0.0045 -0.0101 0.0003 88 PRO A CG 12 C CD . PRO A 2 ? 0.1496 0.1725 0.1833 0.0047 0.0033 -0.0001 88 PRO A CD 13 N N . TYR A 3 ? 0.1636 0.1511 0.1614 0.0046 -0.0055 -0.0003 89 TYR A N 14 C CA . TYR A 3 ? 0.1418 0.1429 0.1423 0.0032 -0.0072 -0.0067 89 TYR A CA 15 C C . TYR A 3 ? 0.1431 0.1524 0.1568 -0.0009 0.0046 -0.0003 89 TYR A C 16 O O . TYR A 3 ? 0.1441 0.1517 0.1620 -0.0056 -0.0093 -0.0145 89 TYR A O 17 C CB . TYR A 3 ? 0.1519 0.1314 0.1262 0.0015 -0.0051 -0.0027 89 TYR A CB 18 C CG . TYR A 3 ? 0.1316 0.1213 0.1312 -0.0070 -0.0024 -0.0087 89 TYR A CG 19 C CD1 . TYR A 3 ? 0.1282 0.1184 0.1281 0.0077 -0.0120 -0.0014 89 TYR A CD1 20 C CD2 . TYR A 3 ? 0.1396 0.1186 0.1165 -0.0005 -0.0007 0.0041 89 TYR A CD2 21 C CE1 . TYR A 3 ? 0.1031 0.0834 0.1099 -0.0086 -0.0106 -0.0116 89 TYR A CE1 22 C CE2 . TYR A 3 ? 0.0933 0.1044 0.1116 -0.0106 0.0051 -0.0192 89 TYR A CE2 23 C CZ . TYR A 3 ? 0.0872 0.0949 0.1086 0.0083 -0.0082 -0.0097 89 TYR A CZ 24 O OH . TYR A 3 ? 0.0926 0.1055 0.1364 -0.0028 -0.0078 -0.0172 89 TYR A OH 25 N N . ASN A 4 ? 0.1619 0.1834 0.1969 0.0022 -0.0015 -0.0056 90 ASN A N 26 C CA . ASN A 4 ? 0.1791 0.1907 0.1985 0.0038 -0.0001 -0.0080 90 ASN A CA 27 C C . ASN A 4 ? 0.1763 0.1784 0.1809 -0.0016 0.0006 -0.0087 90 ASN A C 28 O O . ASN A 4 ? 0.1954 0.1823 0.1933 0.0088 0.0037 -0.0223 90 ASN A O 29 C CB . ASN A 4 ? 0.1916 0.2181 0.2215 -0.0035 0.0009 -0.0084 90 ASN A CB 30 C CG . ASN A 4 ? 0.2391 0.2657 0.2391 0.0084 0.0041 -0.0083 90 ASN A CG 31 O OD1 . ASN A 4 ? 0.2718 0.3171 0.2563 -0.0002 0.0133 -0.0076 90 ASN A OD1 32 N ND2 . ASN A 4 ? 0.3049 0.3118 0.3141 0.0235 -0.0099 0.0058 90 ASN A ND2 33 N N . GLY A 5 ? 0.1607 0.1646 0.1656 -0.0042 0.0124 -0.0090 91 GLY A N 34 C CA . GLY A 5 ? 0.1273 0.1412 0.1519 -0.0029 0.0038 -0.0075 91 GLY A CA 35 C C . GLY A 5 ? 0.1113 0.1188 0.1190 -0.0032 0.0016 -0.0046 91 GLY A C 36 O O . GLY A 5 ? 0.1243 0.1429 0.1296 -0.0027 0.0081 -0.0123 91 GLY A O 37 N N . ASN A 6 ? 0.1027 0.1082 0.1221 0.0005 -0.0021 -0.0073 92 ASN A N 38 C CA . ASN A 6 ? 0.0890 0.0886 0.0936 -0.0028 -0.0029 -0.0037 92 ASN A CA 39 C C . ASN A 6 ? 0.0860 0.0790 0.0900 -0.0027 -0.0048 0.0025 92 ASN A C 40 O O . ASN A 6 ? 0.0853 0.0950 0.0948 -0.0109 -0.0239 0.0043 92 ASN A O 41 C CB . ASN A 6 ? 0.0764 0.0993 0.0978 -0.0011 -0.0109 0.0000 92 ASN A CB 42 C CG . ASN A 6 ? 0.0915 0.0978 0.1039 0.0144 0.0046 0.0001 92 ASN A CG 43 O OD1 . ASN A 6 ? 0.0856 0.0844 0.1075 0.0143 0.0028 -0.0074 92 ASN A OD1 44 N ND2 . ASN A 6 ? 0.0987 0.1100 0.1186 0.0145 -0.0036 -0.0053 92 ASN A ND2 45 N N . PRO A 7 ? 0.0893 0.0853 0.1019 0.0002 -0.0043 -0.0046 93 PRO A N 46 C CA . PRO A 7 ? 0.0884 0.0800 0.1044 0.0075 -0.0018 -0.0085 93 PRO A CA 47 C C . PRO A 7 ? 0.0898 0.0861 0.0977 0.0024 -0.0071 -0.0055 93 PRO A C 48 O O . PRO A 7 ? 0.0981 0.0751 0.0953 0.0120 -0.0133 -0.0052 93 PRO A O 49 C CB . PRO A 7 ? 0.0889 0.0881 0.0944 0.0101 0.0096 -0.0143 93 PRO A CB 50 C CG . PRO A 7 ? 0.0842 0.0893 0.1139 0.0075 -0.0129 0.0034 93 PRO A CG 51 C CD . PRO A 7 ? 0.0996 0.0903 0.1084 -0.0004 -0.0084 -0.0033 93 PRO A CD 52 N N . PHE A 8 ? 0.0771 0.0909 0.0982 0.0066 0.0008 -0.0056 94 PHE A N 53 C CA . PHE A 8 ? 0.0986 0.0853 0.0957 0.0058 -0.0045 0.0012 94 PHE A CA 54 C C . PHE A 8 ? 0.0997 0.0865 0.0989 0.0014 -0.0070 -0.0014 94 PHE A C 55 O O . PHE A 8 ? 0.1165 0.1133 0.1056 0.0058 -0.0156 0.0127 94 PHE A O 56 C CB . PHE A 8 ? 0.1029 0.0893 0.0937 0.0032 -0.0062 -0.0017 94 PHE A CB 57 C CG . PHE A 8 ? 0.0722 0.0634 0.0879 0.0051 -0.0048 -0.0050 94 PHE A CG 58 C CD1 . PHE A 8 ? 0.0691 0.0801 0.1089 -0.0089 -0.0017 0.0005 94 PHE A CD1 59 C CD2 . PHE A 8 ? 0.0857 0.0808 0.0774 -0.0009 0.0031 -0.0001 94 PHE A CD2 60 C CE1 . PHE A 8 ? 0.0817 0.0774 0.0931 -0.0048 0.0018 -0.0012 94 PHE A CE1 61 C CE2 . PHE A 8 ? 0.0778 0.0842 0.0887 0.0156 0.0097 -0.0016 94 PHE A CE2 62 C CZ . PHE A 8 ? 0.0776 0.0856 0.0809 -0.0028 0.0005 0.0015 94 PHE A CZ 63 N N . GLU A 9 ? 0.1031 0.0986 0.1122 0.0042 -0.0059 0.0050 95 GLU A N 64 C CA . GLU A 9 ? 0.1302 0.1291 0.1261 0.0009 -0.0074 0.0061 95 GLU A CA 65 C C . GLU A 9 ? 0.1244 0.1440 0.1275 0.0020 -0.0104 0.0013 95 GLU A C 66 O O . GLU A 9 ? 0.1278 0.1451 0.1351 0.0226 -0.0211 -0.0045 95 GLU A O 67 C CB A GLU A 9 ? 0.1357 0.1406 0.1414 -0.0020 -0.0017 0.0024 95 GLU A CB 68 C CB B GLU A 9 ? 0.1296 0.1424 0.1345 -0.0017 -0.0073 0.0053 95 GLU A CB 69 C CG A GLU A 9 ? 0.1823 0.1965 0.1821 0.0002 -0.0076 0.0017 95 GLU A CG 70 C CG B GLU A 9 ? 0.1832 0.1650 0.1809 0.0071 -0.0019 -0.0029 95 GLU A CG 71 C CD A GLU A 9 ? 0.2452 0.2355 0.2606 -0.0109 -0.0025 -0.0016 95 GLU A CD 72 C CD B GLU A 9 ? 0.2220 0.2174 0.2363 -0.0060 -0.0030 -0.0012 95 GLU A CD 73 O OE1 A GLU A 9 ? 0.2988 0.2798 0.2894 -0.0012 -0.0074 0.0027 95 GLU A OE1 74 O OE1 B GLU A 9 ? 0.2437 0.2608 0.2627 -0.0058 -0.0045 -0.0086 95 GLU A OE1 75 O OE2 A GLU A 9 ? 0.2714 0.2984 0.2953 -0.0008 -0.0160 -0.0026 95 GLU A OE2 76 O OE2 B GLU A 9 ? 0.2618 0.2308 0.2426 0.0044 -0.0022 -0.0099 95 GLU A OE2 77 N N . GLY A 10 ? 0.1446 0.1453 0.1567 -0.0042 -0.0111 0.0025 96 GLY A N 78 C CA . GLY A 10 ? 0.1550 0.1602 0.1767 0.0076 -0.0192 0.0035 96 GLY A CA 79 C C . GLY A 10 ? 0.1440 0.1443 0.1687 0.0029 -0.0056 0.0004 96 GLY A C 80 O O . GLY A 10 ? 0.1684 0.1654 0.2154 0.0168 -0.0115 0.0026 96 GLY A O 81 N N . VAL A 11 ? 0.1346 0.1263 0.1601 0.0072 -0.0119 0.0011 97 VAL A N 82 C CA . VAL A 11 ? 0.1274 0.1136 0.1321 -0.0012 -0.0079 0.0086 97 VAL A CA 83 C C . VAL A 11 ? 0.1280 0.1185 0.1250 0.0090 -0.0162 0.0021 97 VAL A C 84 O O . VAL A 11 ? 0.1584 0.1422 0.1638 0.0027 -0.0061 -0.0031 97 VAL A O 85 C CB . VAL A 11 ? 0.1247 0.1207 0.1263 -0.0037 -0.0050 -0.0052 97 VAL A CB 86 C CG1 . VAL A 11 ? 0.1472 0.1212 0.1230 0.0023 -0.0009 0.0062 97 VAL A CG1 87 C CG2 . VAL A 11 ? 0.1272 0.1244 0.1175 -0.0033 -0.0064 -0.0018 97 VAL A CG2 88 N N . GLN A 12 ? 0.1172 0.1294 0.1303 0.0106 -0.0099 0.0150 98 GLN A N 89 C CA . GLN A 12 ? 0.1253 0.1454 0.1320 0.0010 -0.0060 0.0036 98 GLN A CA 90 C C . GLN A 12 ? 0.1058 0.1261 0.1142 0.0069 -0.0024 0.0046 98 GLN A C 91 O O . GLN A 12 ? 0.1043 0.1317 0.1080 0.0168 -0.0137 -0.0004 98 GLN A O 92 C CB . GLN A 12 ? 0.1460 0.1731 0.1599 0.0067 0.0025 0.0150 98 GLN A CB 93 C CG . GLN A 12 ? 0.1965 0.2150 0.2071 0.0110 -0.0008 0.0104 98 GLN A CG 94 C CD . GLN A 12 ? 0.2377 0.2252 0.2473 0.0006 0.0098 0.0143 98 GLN A CD 95 O OE1 . GLN A 12 ? 0.2530 0.2270 0.2658 -0.0036 0.0313 -0.0043 98 GLN A OE1 96 N NE2 . GLN A 12 ? 0.2668 0.2179 0.2053 0.0045 -0.0028 -0.0040 98 GLN A NE2 97 N N . LEU A 13 ? 0.1056 0.1133 0.0983 0.0041 -0.0035 0.0024 99 LEU A N 98 C CA . LEU A 13 ? 0.0942 0.0935 0.0979 0.0064 -0.0029 -0.0021 99 LEU A CA 99 C C . LEU A 13 ? 0.0807 0.0921 0.0902 0.0072 -0.0011 0.0056 99 LEU A C 100 O O . LEU A 13 ? 0.1155 0.1073 0.1061 0.0022 0.0047 0.0012 99 LEU A O 101 C CB . LEU A 13 ? 0.0952 0.0853 0.1119 0.0033 0.0017 -0.0032 99 LEU A CB 102 C CG . LEU A 13 ? 0.1107 0.0930 0.1048 -0.0061 0.0130 -0.0037 99 LEU A CG 103 C CD1 . LEU A 13 ? 0.1338 0.1049 0.1239 0.0099 0.0181 0.0067 99 LEU A CD1 104 C CD2 . LEU A 13 ? 0.1035 0.1065 0.1224 0.0022 0.0171 -0.0079 99 LEU A CD2 105 N N . TRP A 14 ? 0.0923 0.0911 0.0891 0.0001 0.0114 0.0011 100 TRP A N 106 C CA . TRP A 14 ? 0.1002 0.1021 0.1087 0.0014 0.0015 -0.0001 100 TRP A CA 107 C C . TRP A 14 ? 0.0967 0.0910 0.1109 -0.0026 0.0014 0.0017 100 TRP A C 108 O O . TRP A 14 ? 0.0857 0.1071 0.0907 -0.0020 -0.0041 0.0029 100 TRP A O 109 C CB . TRP A 14 ? 0.1156 0.1077 0.1183 0.0023 0.0000 -0.0021 100 TRP A CB 110 C CG . TRP A 14 ? 0.0968 0.1020 0.1012 0.0044 0.0105 -0.0057 100 TRP A CG 111 C CD1 . TRP A 14 ? 0.1095 0.1153 0.1014 0.0051 0.0168 0.0037 100 TRP A CD1 112 C CD2 . TRP A 14 ? 0.1347 0.1309 0.1198 0.0024 0.0110 -0.0017 100 TRP A CD2 113 N NE1 . TRP A 14 ? 0.1185 0.1089 0.1039 0.0093 0.0037 -0.0057 100 TRP A NE1 114 C CE2 . TRP A 14 ? 0.1325 0.1193 0.1042 0.0091 0.0064 -0.0047 100 TRP A CE2 115 C CE3 . TRP A 14 ? 0.1436 0.1253 0.1467 0.0055 -0.0041 -0.0011 100 TRP A CE3 116 C CZ2 . TRP A 14 ? 0.1665 0.1322 0.1322 -0.0118 0.0095 -0.0002 100 TRP A CZ2 117 C CZ3 . TRP A 14 ? 0.1618 0.1548 0.1813 0.0011 -0.0013 0.0003 100 TRP A CZ3 118 C CH2 . TRP A 14 ? 0.1583 0.1197 0.1607 -0.0058 -0.0029 0.0015 100 TRP A CH2 119 N N . ALA A 15 ? 0.0953 0.0923 0.0912 0.0020 0.0010 0.0038 101 ALA A N 120 C CA . ALA A 15 ? 0.0933 0.0976 0.1062 -0.0021 -0.0007 0.0041 101 ALA A CA 121 C C . ALA A 15 ? 0.0874 0.0856 0.0892 0.0041 -0.0020 0.0029 101 ALA A C 122 O O . ALA A 15 ? 0.1176 0.1019 0.1358 -0.0004 0.0064 0.0047 101 ALA A O 123 C CB . ALA A 15 ? 0.0959 0.1104 0.1048 0.0034 -0.0042 0.0039 101 ALA A CB 124 N N . ASN A 16 ? 0.0927 0.0819 0.0921 -0.0068 -0.0016 0.0033 102 ASN A N 125 C CA . ASN A 16 ? 0.0945 0.0870 0.0999 0.0011 -0.0005 -0.0021 102 ASN A CA 126 C C . ASN A 16 ? 0.0986 0.0955 0.1006 0.0003 0.0091 -0.0011 102 ASN A C 127 O O . ASN A 16 ? 0.1011 0.0929 0.0881 0.0092 0.0074 -0.0070 102 ASN A O 128 C CB . ASN A 16 ? 0.1014 0.0988 0.0939 -0.0059 -0.0019 -0.0081 102 ASN A CB 129 C CG . ASN A 16 ? 0.1085 0.1041 0.1091 0.0001 -0.0097 -0.0013 102 ASN A CG 130 O OD1 . ASN A 16 ? 0.1135 0.0923 0.1172 0.0026 0.0112 -0.0143 102 ASN A OD1 131 N ND2 . ASN A 16 ? 0.0879 0.0827 0.1011 0.0044 0.0080 -0.0015 102 ASN A ND2 132 N N . ASN A 17 ? 0.0999 0.0957 0.0993 -0.0042 0.0133 -0.0026 103 ASN A N 133 C CA . ASN A 17 ? 0.1127 0.0911 0.1147 -0.0060 0.0062 -0.0084 103 ASN A CA 134 C C . ASN A 17 ? 0.1130 0.0917 0.1037 -0.0005 0.0097 -0.0097 103 ASN A C 135 O O . ASN A 17 ? 0.1204 0.0914 0.1444 -0.0085 0.0079 -0.0071 103 ASN A O 136 C CB . ASN A 17 ? 0.1221 0.1042 0.1310 -0.0033 0.0104 -0.0097 103 ASN A CB 137 C CG . ASN A 17 ? 0.1614 0.1375 0.1626 -0.0032 -0.0007 0.0022 103 ASN A CG 138 O OD1 . ASN A 17 ? 0.2501 0.1924 0.1781 0.0128 0.0138 0.0145 103 ASN A OD1 139 N ND2 . ASN A 17 ? 0.1847 0.1671 0.2051 -0.0184 0.0187 -0.0114 103 ASN A ND2 140 N N . TYR A 18 ? 0.1040 0.0977 0.1021 -0.0076 0.0030 -0.0085 104 TYR A N 141 C CA . TYR A 18 ? 0.1016 0.0889 0.0866 -0.0003 0.0058 0.0002 104 TYR A CA 142 C C . TYR A 18 ? 0.0856 0.0868 0.0785 0.0022 -0.0019 -0.0024 104 TYR A C 143 O O . TYR A 18 ? 0.1064 0.0832 0.0857 -0.0065 -0.0029 -0.0004 104 TYR A O 144 C CB . TYR A 18 ? 0.1066 0.1016 0.0997 -0.0070 0.0062 0.0002 104 TYR A CB 145 C CG . TYR A 18 ? 0.1118 0.1092 0.1006 -0.0041 0.0037 -0.0049 104 TYR A CG 146 C CD1 . TYR A 18 ? 0.1154 0.1051 0.1243 0.0012 0.0065 0.0000 104 TYR A CD1 147 C CD2 . TYR A 18 ? 0.1218 0.1079 0.1010 -0.0133 0.0089 -0.0040 104 TYR A CD2 148 C CE1 . TYR A 18 ? 0.1161 0.1191 0.1040 -0.0068 0.0141 -0.0051 104 TYR A CE1 149 C CE2 . TYR A 18 ? 0.1307 0.1382 0.1213 -0.0071 0.0067 -0.0111 104 TYR A CE2 150 C CZ . TYR A 18 ? 0.1150 0.1277 0.1380 -0.0165 0.0032 0.0043 104 TYR A CZ 151 O OH . TYR A 18 ? 0.1619 0.1620 0.1711 -0.0287 -0.0042 0.0314 104 TYR A OH 152 N N . TYR A 19 ? 0.0932 0.0970 0.0758 -0.0013 0.0017 -0.0053 105 TYR A N 153 C CA . TYR A 19 ? 0.0796 0.0778 0.0850 0.0056 -0.0029 -0.0008 105 TYR A CA 154 C C . TYR A 19 ? 0.0843 0.0759 0.0778 0.0008 0.0007 -0.0095 105 TYR A C 155 O O . TYR A 19 ? 0.0758 0.0850 0.0866 -0.0054 0.0028 -0.0006 105 TYR A O 156 C CB . TYR A 19 ? 0.0858 0.0891 0.0867 0.0046 -0.0061 -0.0051 105 TYR A CB 157 C CG . TYR A 19 ? 0.0738 0.0705 0.0761 -0.0055 -0.0061 0.0011 105 TYR A CG 158 C CD1 . TYR A 19 ? 0.0627 0.0875 0.0755 0.0123 -0.0077 -0.0022 105 TYR A CD1 159 C CD2 . TYR A 19 ? 0.1018 0.0840 0.0896 0.0097 -0.0061 0.0089 105 TYR A CD2 160 C CE1 . TYR A 19 ? 0.1168 0.1038 0.0975 0.0045 -0.0104 0.0007 105 TYR A CE1 161 C CE2 . TYR A 19 ? 0.0964 0.0905 0.0888 0.0050 -0.0041 -0.0057 105 TYR A CE2 162 C CZ . TYR A 19 ? 0.0979 0.0900 0.0913 -0.0089 -0.0011 -0.0029 105 TYR A CZ 163 O OH . TYR A 19 ? 0.1074 0.0826 0.0910 -0.0001 -0.0021 -0.0107 105 TYR A OH 164 N N . ARG A 20 ? 0.0889 0.0957 0.0887 -0.0025 -0.0037 0.0016 106 ARG A N 165 C CA . ARG A 20 ? 0.0952 0.0907 0.0897 0.0034 0.0054 0.0013 106 ARG A CA 166 C C . ARG A 20 ? 0.1053 0.0873 0.0933 0.0041 0.0010 -0.0015 106 ARG A C 167 O O . ARG A 20 ? 0.1119 0.0948 0.1069 -0.0014 0.0057 0.0086 106 ARG A O 168 C CB . ARG A 20 ? 0.1073 0.0980 0.1135 0.0032 0.0053 0.0099 106 ARG A CB 169 C CG . ARG A 20 ? 0.1189 0.1101 0.1036 0.0048 0.0034 -0.0025 106 ARG A CG 170 C CD . ARG A 20 ? 0.1408 0.1257 0.1372 0.0152 0.0038 -0.0019 106 ARG A CD 171 N NE . ARG A 20 ? 0.1449 0.1367 0.1507 0.0097 0.0032 0.0029 106 ARG A NE 172 C CZ . ARG A 20 ? 0.1837 0.1807 0.1794 0.0060 0.0055 0.0036 106 ARG A CZ 173 N NH1 . ARG A 20 ? 0.2105 0.1956 0.1966 0.0145 0.0123 -0.0100 106 ARG A NH1 174 N NH2 . ARG A 20 ? 0.2114 0.2089 0.2031 -0.0026 -0.0056 -0.0026 106 ARG A NH2 175 N N . SER A 21 ? 0.1132 0.0951 0.1079 0.0003 -0.0001 -0.0018 107 SER A N 176 C CA . SER A 21 ? 0.1164 0.1065 0.1105 -0.0052 0.0014 0.0013 107 SER A CA 177 C C . SER A 21 ? 0.1159 0.1001 0.1070 -0.0064 0.0006 -0.0035 107 SER A C 178 O O . SER A 21 ? 0.1230 0.0987 0.1098 -0.0147 0.0025 -0.0034 107 SER A O 179 C CB A SER A 21 ? 0.1230 0.1124 0.1263 -0.0024 0.0008 -0.0042 107 SER A CB 180 C CB B SER A 21 ? 0.1221 0.1077 0.1211 -0.0030 -0.0006 -0.0010 107 SER A CB 181 O OG A SER A 21 ? 0.1555 0.1321 0.1438 -0.0063 -0.0016 -0.0004 107 SER A OG 182 O OG B SER A 21 ? 0.1459 0.1323 0.1710 0.0105 -0.0001 0.0006 107 SER A OG 183 N N . GLU A 22 ? 0.1049 0.0912 0.0972 -0.0105 0.0040 0.0051 108 GLU A N 184 C CA . GLU A 22 ? 0.0928 0.0772 0.0819 -0.0105 -0.0027 -0.0040 108 GLU A CA 185 C C . GLU A 22 ? 0.0920 0.0780 0.0901 -0.0046 0.0022 0.0109 108 GLU A C 186 O O . GLU A 22 ? 0.0863 0.0849 0.0905 -0.0035 -0.0022 0.0112 108 GLU A O 187 C CB . GLU A 22 ? 0.0821 0.0829 0.0839 -0.0024 0.0060 0.0058 108 GLU A CB 188 C CG . GLU A 22 ? 0.1182 0.0784 0.0878 -0.0172 -0.0053 0.0000 108 GLU A CG 189 C CD . GLU A 22 ? 0.1050 0.0802 0.0832 -0.0090 -0.0011 0.0028 108 GLU A CD 190 O OE1 . GLU A 22 ? 0.0906 0.1114 0.0902 -0.0137 -0.0082 0.0020 108 GLU A OE1 191 O OE2 . GLU A 22 ? 0.1084 0.1027 0.0993 -0.0017 0.0106 0.0033 108 GLU A OE2 192 N N . VAL A 23 ? 0.1048 0.0937 0.0972 -0.0096 0.0036 0.0053 109 VAL A N 193 C CA . VAL A 23 ? 0.1003 0.0974 0.0937 -0.0032 -0.0008 0.0096 109 VAL A CA 194 C C . VAL A 23 ? 0.1039 0.1012 0.1041 -0.0065 -0.0030 0.0064 109 VAL A C 195 O O . VAL A 23 ? 0.1131 0.1139 0.1165 0.0020 0.0025 0.0129 109 VAL A O 196 C CB . VAL A 23 ? 0.0950 0.0881 0.0947 0.0002 -0.0088 0.0058 109 VAL A CB 197 C CG1 . VAL A 23 ? 0.0979 0.1068 0.1153 -0.0076 -0.0011 0.0006 109 VAL A CG1 198 C CG2 . VAL A 23 ? 0.0930 0.0870 0.1042 0.0006 0.0041 -0.0044 109 VAL A CG2 199 N N . HIS A 24 ? 0.1130 0.1057 0.1038 -0.0083 0.0083 0.0067 110 HIS A N 200 C CA . HIS A 24 ? 0.1183 0.1104 0.1159 -0.0058 0.0054 0.0086 110 HIS A CA 201 C C . HIS A 24 ? 0.1380 0.1322 0.1354 -0.0123 0.0009 0.0004 110 HIS A C 202 O O . HIS A 24 ? 0.1662 0.1398 0.1386 -0.0245 0.0111 0.0102 110 HIS A O 203 C CB . HIS A 24 ? 0.1291 0.0983 0.1156 -0.0016 -0.0025 0.0180 110 HIS A CB 204 C CG . HIS A 24 ? 0.1094 0.1296 0.1205 0.0048 -0.0161 0.0208 110 HIS A CG 205 N ND1 . HIS A 24 ? 0.1734 0.1942 0.1636 -0.0147 -0.0027 0.0246 110 HIS A ND1 206 C CD2 . HIS A 24 ? 0.1660 0.1253 0.1340 -0.0202 0.0080 0.0125 110 HIS A CD2 207 C CE1 . HIS A 24 ? 0.1805 0.1945 0.1853 -0.0151 -0.0082 0.0097 110 HIS A CE1 208 N NE2 . HIS A 24 ? 0.1501 0.1573 0.1460 0.0052 -0.0166 0.0250 110 HIS A NE2 209 N N . THR A 25 ? 0.1430 0.1321 0.1363 -0.0142 0.0068 -0.0040 111 THR A N 210 C CA . THR A 25 ? 0.1332 0.1265 0.1426 -0.0080 0.0005 0.0005 111 THR A CA 211 C C . THR A 25 ? 0.1331 0.1264 0.1481 -0.0102 0.0020 0.0070 111 THR A C 212 O O . THR A 25 ? 0.1546 0.1335 0.1454 -0.0200 0.0001 0.0229 111 THR A O 213 C CB . THR A 25 ? 0.1544 0.1589 0.1544 -0.0072 0.0014 0.0004 111 THR A CB 214 O OG1 . THR A 25 ? 0.1795 0.1753 0.1718 -0.0172 0.0105 0.0032 111 THR A OG1 215 C CG2 . THR A 25 ? 0.1605 0.1444 0.1673 0.0036 0.0004 -0.0112 111 THR A CG2 216 N N . LEU A 26 ? 0.1315 0.1078 0.1154 -0.0124 0.0004 -0.0031 112 LEU A N 217 C CA . LEU A 26 ? 0.1212 0.1238 0.1286 -0.0162 0.0022 0.0019 112 LEU A CA 218 C C . LEU A 26 ? 0.1173 0.1356 0.1246 -0.0052 0.0007 -0.0034 112 LEU A C 219 O O . LEU A 26 ? 0.1382 0.1829 0.1678 -0.0119 0.0217 -0.0184 112 LEU A O 220 C CB . LEU A 26 ? 0.1252 0.1197 0.1127 -0.0173 -0.0025 0.0003 112 LEU A CB 221 C CG . LEU A 26 ? 0.1151 0.1242 0.1110 -0.0095 -0.0021 0.0009 112 LEU A CG 222 C CD1 . LEU A 26 ? 0.1236 0.1108 0.1246 -0.0119 0.0020 -0.0062 112 LEU A CD1 223 C CD2 . LEU A 26 ? 0.1527 0.1357 0.1330 -0.0152 -0.0099 0.0045 112 LEU A CD2 224 N N . ALA A 27 ? 0.1085 0.1028 0.1119 -0.0192 0.0101 -0.0016 113 ALA A N 225 C CA . ALA A 27 ? 0.1115 0.1187 0.1081 -0.0058 0.0054 -0.0002 113 ALA A CA 226 C C . ALA A 27 ? 0.1118 0.1150 0.1046 -0.0019 -0.0012 -0.0047 113 ALA A C 227 O O . ALA A 27 ? 0.1268 0.1486 0.1017 -0.0226 0.0113 0.0052 113 ALA A O 228 C CB . ALA A 27 ? 0.1216 0.1339 0.1131 -0.0065 0.0127 -0.0033 113 ALA A CB 229 N N . ILE A 28 ? 0.1145 0.1292 0.1124 -0.0076 0.0063 0.0084 114 ILE A N 230 C CA . ILE A 28 ? 0.1344 0.1287 0.1168 -0.0064 0.0038 0.0044 114 ILE A CA 231 C C . ILE A 28 ? 0.1392 0.1359 0.1281 -0.0096 0.0074 0.0005 114 ILE A C 232 O O . ILE A 28 ? 0.1415 0.1407 0.1182 -0.0246 0.0213 0.0109 114 ILE A O 233 C CB . ILE A 28 ? 0.1478 0.1321 0.1292 -0.0059 0.0071 0.0087 114 ILE A CB 234 C CG1 . ILE A 28 ? 0.1451 0.1206 0.1061 -0.0040 -0.0028 0.0038 114 ILE A CG1 235 C CG2 . ILE A 28 ? 0.1717 0.1501 0.1356 -0.0003 0.0013 0.0201 114 ILE A CG2 236 C CD1 . ILE A 28 ? 0.1522 0.1440 0.1308 -0.0175 0.0050 -0.0052 114 ILE A CD1 237 N N . PRO A 29 ? 0.1494 0.1399 0.1433 -0.0177 0.0094 0.0024 115 PRO A N 238 C CA . PRO A 29 ? 0.1636 0.1583 0.1654 -0.0194 0.0066 0.0026 115 PRO A CA 239 C C . PRO A 29 ? 0.1763 0.1785 0.1775 -0.0155 0.0090 -0.0001 115 PRO A C 240 O O . PRO A 29 ? 0.2113 0.2133 0.2082 -0.0364 0.0196 0.0011 115 PRO A O 241 C CB . PRO A 29 ? 0.1649 0.1536 0.1629 -0.0158 0.0079 0.0012 115 PRO A CB 242 C CG . PRO A 29 ? 0.1695 0.1411 0.1697 -0.0133 0.0028 -0.0032 115 PRO A CG 243 C CD . PRO A 29 ? 0.1294 0.1114 0.1431 -0.0123 0.0028 0.0004 115 PRO A CD 244 N N . GLN A 30 ? 0.1980 0.1890 0.1981 -0.0070 0.0074 -0.0009 116 GLN A N 245 C CA . GLN A 30 ? 0.1977 0.2055 0.2123 -0.0077 0.0042 -0.0036 116 GLN A CA 246 C C . GLN A 30 ? 0.2086 0.2166 0.2148 -0.0001 0.0056 0.0006 116 GLN A C 247 O O . GLN A 30 ? 0.2283 0.2295 0.2477 0.0001 0.0093 -0.0212 116 GLN A O 248 C CB . GLN A 30 ? 0.2023 0.2127 0.2252 0.0017 0.0012 0.0014 116 GLN A CB 249 C CG . GLN A 30 ? 0.2463 0.2642 0.2481 -0.0029 0.0016 -0.0003 116 GLN A CG 250 C CD . GLN A 30 ? 0.3134 0.3136 0.3230 0.0046 -0.0034 0.0169 116 GLN A CD 251 O OE1 . GLN A 30 ? 0.3445 0.3883 0.4072 0.0241 0.0081 0.0006 116 GLN A OE1 252 N NE2 . GLN A 30 ? 0.3466 0.3665 0.3624 -0.0042 0.0146 0.0055 116 GLN A NE2 253 N N . ILE A 31 ? 0.2016 0.2036 0.2091 -0.0112 0.0100 0.0017 117 ILE A N 254 C CA . ILE A 31 ? 0.2149 0.2166 0.2093 -0.0036 0.0068 0.0014 117 ILE A CA 255 C C . ILE A 31 ? 0.2293 0.2283 0.2251 -0.0012 0.0085 0.0037 117 ILE A C 256 O O . ILE A 31 ? 0.2224 0.2363 0.2280 -0.0009 0.0230 0.0073 117 ILE A O 257 C CB . ILE A 31 ? 0.2118 0.2066 0.2030 -0.0034 0.0006 0.0011 117 ILE A CB 258 C CG1 . ILE A 31 ? 0.1873 0.1941 0.1970 -0.0058 0.0032 -0.0052 117 ILE A CG1 259 C CG2 . ILE A 31 ? 0.2444 0.2406 0.2214 -0.0150 0.0058 -0.0054 117 ILE A CG2 260 C CD1 . ILE A 31 ? 0.2053 0.2139 0.2134 -0.0054 0.0102 -0.0106 117 ILE A CD1 261 N N . THR A 32 ? 0.2435 0.2479 0.2453 -0.0018 0.0102 -0.0003 118 THR A N 262 C CA . THR A 32 ? 0.2527 0.2613 0.2537 -0.0048 0.0043 0.0007 118 THR A CA 263 C C . THR A 32 ? 0.2511 0.2540 0.2502 -0.0087 0.0049 -0.0001 118 THR A C 264 O O . THR A 32 ? 0.2651 0.2574 0.2581 -0.0112 0.0009 0.0024 118 THR A O 265 C CB . THR A 32 ? 0.2621 0.2682 0.2673 -0.0066 0.0079 0.0045 118 THR A CB 266 O OG1 . THR A 32 ? 0.2620 0.2897 0.2867 0.0085 0.0300 0.0030 118 THR A OG1 267 C CG2 . THR A 32 ? 0.2793 0.2977 0.2854 -0.0078 -0.0014 0.0020 118 THR A CG2 268 N N . ASP A 33 ? 0.2464 0.2411 0.2313 -0.0047 0.0100 -0.0014 119 ASP A N 269 C CA . ASP A 33 ? 0.2417 0.2430 0.2330 -0.0065 0.0088 0.0011 119 ASP A CA 270 C C . ASP A 33 ? 0.2379 0.2404 0.2305 -0.0124 0.0082 -0.0018 119 ASP A C 271 O O . ASP A 33 ? 0.2281 0.2291 0.2044 -0.0233 0.0258 -0.0097 119 ASP A O 272 C CB A ASP A 33 ? 0.2467 0.2484 0.2404 -0.0045 0.0109 -0.0040 119 ASP A CB 273 C CB B ASP A 33 ? 0.2409 0.2443 0.2353 -0.0053 0.0100 -0.0027 119 ASP A CB 274 C CG A ASP A 33 ? 0.2559 0.2668 0.2490 -0.0041 0.0031 -0.0090 119 ASP A CG 275 C CG B ASP A 33 ? 0.2463 0.2464 0.2321 -0.0063 0.0049 -0.0027 119 ASP A CG 276 O OD1 A ASP A 33 ? 0.2492 0.2559 0.2410 0.0032 0.0157 -0.0080 119 ASP A OD1 277 O OD1 B ASP A 33 ? 0.2417 0.2299 0.2415 -0.0058 0.0092 0.0149 119 ASP A OD1 278 O OD2 A ASP A 33 ? 0.2619 0.2802 0.2820 0.0132 0.0165 -0.0070 119 ASP A OD2 279 O OD2 B ASP A 33 ? 0.2452 0.2272 0.2123 -0.0009 0.0138 0.0011 119 ASP A OD2 280 N N . PRO A 34 ? 0.2352 0.2402 0.2215 -0.0179 0.0121 0.0023 120 PRO A N 281 C CA . PRO A 34 ? 0.2415 0.2410 0.2330 -0.0139 0.0073 -0.0042 120 PRO A CA 282 C C . PRO A 34 ? 0.2382 0.2358 0.2322 -0.0121 0.0123 -0.0011 120 PRO A C 283 O O . PRO A 34 ? 0.2415 0.2388 0.2082 -0.0240 0.0186 -0.0066 120 PRO A O 284 C CB . PRO A 34 ? 0.2450 0.2518 0.2485 -0.0106 0.0055 -0.0017 120 PRO A CB 285 C CG . PRO A 34 ? 0.2398 0.2491 0.2378 -0.0106 0.0091 0.0003 120 PRO A CG 286 C CD . PRO A 34 ? 0.2345 0.2462 0.2228 -0.0107 0.0160 -0.0010 120 PRO A CD 287 N N . ALA A 35 ? 0.2357 0.2482 0.2226 -0.0159 0.0173 -0.0025 121 ALA A N 288 C CA . ALA A 35 ? 0.2447 0.2390 0.2364 -0.0127 0.0077 -0.0019 121 ALA A CA 289 C C . ALA A 35 ? 0.2274 0.2303 0.2203 -0.0075 0.0081 -0.0088 121 ALA A C 290 O O . ALA A 35 ? 0.2208 0.2356 0.2143 -0.0263 0.0159 -0.0098 121 ALA A O 291 C CB . ALA A 35 ? 0.2518 0.2518 0.2399 -0.0111 0.0084 -0.0053 121 ALA A CB 292 N N . LEU A 36 ? 0.2142 0.2117 0.1980 -0.0080 0.0124 -0.0082 122 LEU A N 293 C CA . LEU A 36 ? 0.2018 0.1914 0.2029 -0.0112 0.0128 0.0007 122 LEU A CA 294 C C . LEU A 36 ? 0.2137 0.1869 0.1970 -0.0095 0.0180 0.0030 122 LEU A C 295 O O . LEU A 36 ? 0.1827 0.1677 0.1746 -0.0069 0.0330 -0.0031 122 LEU A O 296 C CB . LEU A 36 ? 0.2264 0.2128 0.2184 -0.0107 0.0082 -0.0028 122 LEU A CB 297 C CG . LEU A 36 ? 0.2548 0.2402 0.2564 -0.0018 0.0153 0.0029 122 LEU A CG 298 C CD1 . LEU A 36 ? 0.2899 0.2780 0.2775 -0.0069 0.0021 0.0073 122 LEU A CD1 299 C CD2 . LEU A 36 ? 0.2791 0.2766 0.2837 -0.0213 0.0026 0.0046 122 LEU A CD2 300 N N . ARG A 37 ? 0.1834 0.1654 0.1739 -0.0114 0.0203 0.0058 123 ARG A N 301 C CA . ARG A 37 ? 0.1873 0.1672 0.1681 -0.0087 0.0112 0.0079 123 ARG A CA 302 C C . ARG A 37 ? 0.1787 0.1538 0.1567 -0.0158 0.0070 0.0009 123 ARG A C 303 O O . ARG A 37 ? 0.1731 0.1439 0.1420 -0.0165 0.0163 0.0040 123 ARG A O 304 C CB . ARG A 37 ? 0.1990 0.1719 0.1735 -0.0091 0.0070 0.0009 123 ARG A CB 305 C CG . ARG A 37 ? 0.1991 0.1708 0.1836 -0.0168 0.0062 0.0039 123 ARG A CG 306 C CD . ARG A 37 ? 0.2053 0.1803 0.1892 -0.0156 0.0093 0.0086 123 ARG A CD 307 N NE . ARG A 37 ? 0.2094 0.1762 0.1784 -0.0269 0.0213 0.0148 123 ARG A NE 308 C CZ . ARG A 37 ? 0.1495 0.1291 0.1568 -0.0293 0.0086 0.0187 123 ARG A CZ 309 N NH1 . ARG A 37 ? 0.2060 0.1765 0.1878 -0.0142 0.0027 0.0149 123 ARG A NH1 310 N NH2 . ARG A 37 ? 0.1986 0.1823 0.1555 -0.0059 0.0199 0.0228 123 ARG A NH2 311 N N . ALA A 38 ? 0.1847 0.1751 0.1525 -0.0132 0.0093 0.0145 124 ALA A N 312 C CA . ALA A 38 ? 0.1831 0.1722 0.1577 -0.0114 0.0002 0.0096 124 ALA A CA 313 C C . ALA A 38 ? 0.1585 0.1590 0.1471 -0.0059 0.0022 0.0141 124 ALA A C 314 O O . ALA A 38 ? 0.1856 0.1645 0.1476 -0.0063 0.0022 0.0087 124 ALA A O 315 C CB . ALA A 38 ? 0.2016 0.1990 0.1770 -0.0094 -0.0014 0.0110 124 ALA A CB 316 N N . ALA A 39 ? 0.1667 0.1570 0.1253 -0.0127 0.0073 0.0042 125 ALA A N 317 C CA . ALA A 39 ? 0.1474 0.1375 0.1347 -0.0101 0.0032 -0.0015 125 ALA A CA 318 C C . ALA A 39 ? 0.1345 0.1328 0.1266 -0.0128 0.0068 -0.0062 125 ALA A C 319 O O . ALA A 39 ? 0.1387 0.1277 0.1500 -0.0334 0.0036 -0.0054 125 ALA A O 320 C CB . ALA A 39 ? 0.1693 0.1546 0.1514 -0.0030 -0.0001 0.0000 125 ALA A CB 321 N N . ALA A 40 ? 0.1332 0.1114 0.1257 -0.0050 -0.0033 -0.0004 126 ALA A N 322 C CA . ALA A 40 ? 0.1264 0.1147 0.1190 -0.0078 0.0037 0.0094 126 ALA A CA 323 C C . ALA A 40 ? 0.1086 0.1053 0.1043 -0.0088 -0.0039 0.0087 126 ALA A C 324 O O . ALA A 40 ? 0.1197 0.1058 0.1074 -0.0156 0.0008 0.0098 126 ALA A O 325 C CB . ALA A 40 ? 0.1195 0.1124 0.1103 -0.0107 -0.0001 0.0039 126 ALA A CB 326 N N . SER A 41 ? 0.1226 0.1076 0.1225 -0.0116 -0.0052 0.0114 127 SER A N 327 C CA . SER A 41 ? 0.1417 0.1220 0.1170 -0.0008 0.0008 0.0011 127 SER A CA 328 C C . SER A 41 ? 0.1402 0.1169 0.1210 -0.0018 0.0020 0.0039 127 SER A C 329 O O . SER A 41 ? 0.1449 0.1163 0.1186 -0.0026 -0.0016 0.0003 127 SER A O 330 C CB A SER A 41 ? 0.1497 0.1286 0.1272 -0.0049 0.0014 0.0037 127 SER A CB 331 C CB B SER A 41 ? 0.1471 0.1284 0.1299 -0.0023 0.0017 0.0043 127 SER A CB 332 O OG A SER A 41 ? 0.1656 0.1277 0.1427 0.0046 -0.0017 0.0050 127 SER A OG 333 O OG B SER A 41 ? 0.1488 0.1382 0.1670 -0.0060 -0.0073 0.0009 127 SER A OG 334 N N . ALA A 42 ? 0.1323 0.1112 0.1129 -0.0021 0.0020 0.0073 128 ALA A N 335 C CA . ALA A 42 ? 0.1142 0.1056 0.1034 0.0005 -0.0047 0.0031 128 ALA A CA 336 C C . ALA A 42 ? 0.1020 0.0967 0.0959 0.0031 -0.0053 -0.0011 128 ALA A C 337 O O . ALA A 42 ? 0.1059 0.0996 0.0975 0.0037 -0.0116 0.0045 128 ALA A O 338 C CB . ALA A 42 ? 0.1051 0.1105 0.1037 -0.0056 0.0021 0.0056 128 ALA A CB 339 N N . VAL A 43 ? 0.0950 0.1020 0.0928 0.0012 -0.0064 0.0054 129 VAL A N 340 C CA . VAL A 43 ? 0.1055 0.0958 0.1035 -0.0006 0.0019 0.0036 129 VAL A CA 341 C C . VAL A 43 ? 0.0971 0.0870 0.0992 0.0004 0.0052 0.0098 129 VAL A C 342 O O . VAL A 43 ? 0.0937 0.0890 0.0916 0.0023 0.0117 0.0194 129 VAL A O 343 C CB A VAL A 43 ? 0.1198 0.1050 0.0988 0.0034 0.0071 0.0109 129 VAL A CB 344 C CB B VAL A 43 ? 0.1159 0.1059 0.1076 0.0008 0.0047 0.0048 129 VAL A CB 345 C CG1 A VAL A 43 ? 0.1349 0.1325 0.1264 0.0063 0.0034 0.0016 129 VAL A CG1 346 C CG1 B VAL A 43 ? 0.1271 0.1116 0.1153 0.0045 0.0014 -0.0017 129 VAL A CG1 347 C CG2 A VAL A 43 ? 0.0875 0.0920 0.0870 0.0149 0.0159 0.0135 129 VAL A CG2 348 C CG2 B VAL A 43 ? 0.1366 0.1430 0.1421 0.0063 0.0068 -0.0043 129 VAL A CG2 349 N N . ALA A 44 ? 0.1054 0.1003 0.1020 -0.0024 0.0040 0.0000 130 ALA A N 350 C CA . ALA A 44 ? 0.1056 0.0938 0.1018 -0.0002 -0.0075 0.0085 130 ALA A CA 351 C C . ALA A 44 ? 0.1158 0.0947 0.1092 -0.0025 0.0053 0.0090 130 ALA A C 352 O O . ALA A 44 ? 0.1257 0.1114 0.1119 0.0012 0.0031 -0.0011 130 ALA A O 353 C CB . ALA A 44 ? 0.1170 0.1104 0.1132 -0.0119 -0.0032 0.0068 130 ALA A CB 354 N N . GLU A 45 ? 0.1086 0.1002 0.0960 -0.0014 -0.0012 0.0071 131 GLU A N 355 C CA . GLU A 45 ? 0.1053 0.1016 0.1026 -0.0004 0.0036 0.0098 131 GLU A CA 356 C C . GLU A 45 ? 0.0831 0.0855 0.0954 0.0058 -0.0022 0.0075 131 GLU A C 357 O O . GLU A 45 ? 0.0963 0.0938 0.1230 -0.0004 0.0141 0.0199 131 GLU A O 358 C CB . GLU A 45 ? 0.1013 0.1000 0.1104 0.0000 -0.0097 0.0065 131 GLU A CB 359 C CG . GLU A 45 ? 0.1170 0.1207 0.1309 -0.0064 0.0012 0.0161 131 GLU A CG 360 C CD . GLU A 45 ? 0.1475 0.1362 0.1424 -0.0047 0.0058 0.0168 131 GLU A CD 361 O OE1 . GLU A 45 ? 0.1645 0.1731 0.1877 0.0049 -0.0001 0.0060 131 GLU A OE1 362 O OE2 . GLU A 45 ? 0.1859 0.1619 0.1657 -0.0102 -0.0019 0.0108 131 GLU A OE2 363 N N . VAL A 46 ? 0.0909 0.0760 0.0841 0.0020 -0.0021 0.0052 132 VAL A N 364 C CA . VAL A 46 ? 0.0833 0.0823 0.0876 -0.0009 -0.0001 0.0041 132 VAL A CA 365 C C . VAL A 46 ? 0.0860 0.0865 0.0870 -0.0031 -0.0012 0.0111 132 VAL A C 366 O O . VAL A 46 ? 0.0956 0.1068 0.0899 -0.0207 0.0017 0.0166 132 VAL A O 367 C CB . VAL A 46 ? 0.1018 0.0933 0.1012 0.0005 0.0044 -0.0028 132 VAL A CB 368 C CG1 . VAL A 46 ? 0.0896 0.1003 0.1000 0.0002 -0.0053 0.0106 132 VAL A CG1 369 C CG2 . VAL A 46 ? 0.1075 0.0886 0.1058 -0.0050 0.0045 0.0027 132 VAL A CG2 370 N N . PRO A 47 ? 0.0829 0.0965 0.0807 -0.0063 -0.0035 0.0066 133 PRO A N 371 C CA . PRO A 47 ? 0.0937 0.0887 0.0884 0.0012 -0.0081 0.0033 133 PRO A CA 372 C C . PRO A 47 ? 0.0980 0.0948 0.0925 -0.0051 -0.0094 0.0080 133 PRO A C 373 O O . PRO A 47 ? 0.1392 0.1108 0.1270 -0.0042 -0.0254 -0.0020 133 PRO A O 374 C CB . PRO A 47 ? 0.0974 0.1027 0.0856 -0.0054 0.0057 -0.0010 133 PRO A CB 375 C CG . PRO A 47 ? 0.0797 0.1181 0.0926 -0.0076 -0.0055 -0.0016 133 PRO A CG 376 C CD . PRO A 47 ? 0.0715 0.0867 0.0778 0.0018 -0.0053 0.0084 133 PRO A CD 377 N N . SER A 48 ? 0.0835 0.0719 0.0756 0.0021 -0.0048 0.0050 134 SER A N 378 C CA . SER A 48 ? 0.0747 0.0566 0.0658 0.0057 -0.0019 0.0007 134 SER A CA 379 C C . SER A 48 ? 0.0883 0.0583 0.0602 -0.0001 -0.0006 0.0015 134 SER A C 380 O O . SER A 48 ? 0.0812 0.0703 0.0681 0.0215 -0.0058 0.0069 134 SER A O 381 C CB . SER A 48 ? 0.0848 0.0796 0.0896 0.0004 0.0083 -0.0067 134 SER A CB 382 O OG . SER A 48 ? 0.0745 0.0722 0.0892 -0.0031 0.0037 0.0033 134 SER A OG 383 N N . PHE A 49 ? 0.0782 0.0571 0.0599 0.0036 0.0014 0.0022 135 PHE A N 384 C CA . PHE A 49 ? 0.0618 0.0694 0.0631 -0.0007 0.0038 0.0027 135 PHE A CA 385 C C . PHE A 49 ? 0.0627 0.0649 0.0540 0.0019 0.0007 0.0042 135 PHE A C 386 O O . PHE A 49 ? 0.0576 0.0763 0.0599 0.0033 0.0090 0.0034 135 PHE A O 387 C CB . PHE A 49 ? 0.0495 0.0536 0.0562 0.0099 0.0036 -0.0016 135 PHE A CB 388 C CG . PHE A 49 ? 0.0487 0.0653 0.0631 0.0071 0.0015 -0.0071 135 PHE A CG 389 C CD1 . PHE A 49 ? 0.0508 0.0680 0.0673 0.0020 0.0075 -0.0094 135 PHE A CD1 390 C CD2 . PHE A 49 ? 0.0572 0.0635 0.0550 -0.0051 -0.0049 0.0007 135 PHE A CD2 391 C CE1 . PHE A 49 ? 0.0616 0.0710 0.0556 0.0074 0.0010 0.0011 135 PHE A CE1 392 C CE2 . PHE A 49 ? 0.0703 0.0526 0.0627 0.0050 -0.0056 -0.0035 135 PHE A CE2 393 C CZ . PHE A 49 ? 0.0495 0.0639 0.0574 -0.0087 -0.0078 0.0032 135 PHE A CZ 394 N N . GLN A 50 ? 0.0591 0.0759 0.0826 0.0000 0.0057 -0.0021 136 GLN A N 395 C CA . GLN A 50 ? 0.0810 0.0857 0.0703 -0.0056 0.0061 0.0061 136 GLN A CA 396 C C . GLN A 50 ? 0.0620 0.0704 0.0703 0.0003 0.0015 0.0059 136 GLN A C 397 O O . GLN A 50 ? 0.0849 0.0880 0.0740 -0.0024 0.0004 0.0048 136 GLN A O 398 C CB . GLN A 50 ? 0.1024 0.1032 0.0985 0.0006 0.0086 -0.0001 136 GLN A CB 399 C CG . GLN A 50 ? 0.1574 0.1379 0.1564 -0.0023 -0.0038 0.0026 136 GLN A CG 400 C CD . GLN A 50 ? 0.1788 0.1445 0.1996 -0.0057 0.0050 -0.0071 136 GLN A CD 401 O OE1 . GLN A 50 ? 0.1923 0.1949 0.2047 -0.0009 0.0079 0.0085 136 GLN A OE1 402 N NE2 . GLN A 50 ? 0.1766 0.1273 0.1911 -0.0082 -0.0081 -0.0165 136 GLN A NE2 403 N N . TRP A 51 ? 0.0815 0.0766 0.0750 -0.0057 0.0026 0.0031 137 TRP A N 404 C CA . TRP A 51 ? 0.0689 0.0698 0.0619 -0.0028 0.0020 -0.0010 137 TRP A CA 405 C C . TRP A 51 ? 0.0763 0.0739 0.0719 -0.0090 0.0036 -0.0048 137 TRP A C 406 O O . TRP A 51 ? 0.0913 0.0814 0.0780 -0.0214 0.0114 -0.0038 137 TRP A O 407 C CB . TRP A 51 ? 0.0667 0.0636 0.0715 -0.0022 0.0006 0.0037 137 TRP A CB 408 C CG . TRP A 51 ? 0.0621 0.0666 0.0516 -0.0047 -0.0118 0.0023 137 TRP A CG 409 C CD1 . TRP A 51 ? 0.0845 0.0751 0.0735 0.0023 -0.0042 0.0093 137 TRP A CD1 410 C CD2 . TRP A 51 ? 0.0432 0.0741 0.0728 0.0025 0.0056 0.0012 137 TRP A CD2 411 N NE1 . TRP A 51 ? 0.0827 0.0883 0.0689 -0.0044 0.0045 -0.0099 137 TRP A NE1 412 C CE2 . TRP A 51 ? 0.0741 0.0730 0.0840 -0.0018 0.0015 -0.0041 137 TRP A CE2 413 C CE3 . TRP A 51 ? 0.0926 0.0897 0.0727 -0.0007 -0.0059 -0.0023 137 TRP A CE3 414 C CZ2 . TRP A 51 ? 0.0879 0.0863 0.0750 -0.0013 0.0023 -0.0096 137 TRP A CZ2 415 C CZ3 . TRP A 51 ? 0.0946 0.0885 0.0874 -0.0150 0.0028 0.0039 137 TRP A CZ3 416 C CH2 . TRP A 51 ? 0.0869 0.0945 0.0900 0.0086 0.0067 -0.0104 137 TRP A CH2 417 N N . LEU A 52 ? 0.0731 0.0696 0.0702 -0.0077 0.0033 -0.0011 138 LEU A N 418 C CA . LEU A 52 ? 0.0673 0.0776 0.0713 -0.0044 0.0024 -0.0030 138 LEU A CA 419 C C . LEU A 52 ? 0.0682 0.0762 0.0704 -0.0011 0.0029 -0.0002 138 LEU A C 420 O O . LEU A 52 ? 0.0727 0.0810 0.0806 0.0037 -0.0058 0.0164 138 LEU A O 421 C CB . LEU A 52 ? 0.0634 0.0801 0.0660 -0.0082 0.0029 -0.0043 138 LEU A CB 422 C CG . LEU A 52 ? 0.0655 0.0832 0.0657 -0.0092 -0.0033 -0.0056 138 LEU A CG 423 C CD1 . LEU A 52 ? 0.0746 0.0918 0.0733 0.0172 0.0015 -0.0031 138 LEU A CD1 424 C CD2 . LEU A 52 ? 0.0653 0.0814 0.0795 0.0054 -0.0076 0.0042 138 LEU A CD2 425 N N . ASP A 53 ? 0.0772 0.0771 0.0639 0.0038 0.0002 0.0051 139 ASP A N 426 C CA . ASP A 53 ? 0.0824 0.0831 0.0810 0.0036 0.0027 -0.0014 139 ASP A CA 427 C C . ASP A 53 ? 0.0804 0.0836 0.0842 -0.0021 -0.0003 0.0090 139 ASP A C 428 O O . ASP A 53 ? 0.0773 0.0895 0.0944 0.0004 -0.0056 -0.0016 139 ASP A O 429 C CB . ASP A 53 ? 0.0818 0.0931 0.0855 0.0189 -0.0013 0.0051 139 ASP A CB 430 C CG . ASP A 53 ? 0.1455 0.1426 0.1410 0.0057 0.0218 0.0107 139 ASP A CG 431 O OD1 . ASP A 53 ? 0.1110 0.1439 0.1681 -0.0028 0.0508 0.0218 139 ASP A OD1 432 O OD2 . ASP A 53 ? 0.2122 0.2847 0.3100 0.0073 0.0430 0.0200 139 ASP A OD2 433 N N . ARG A 54 ? 0.0918 0.0881 0.0889 -0.0004 -0.0089 -0.0061 140 ARG A N 434 C CA . ARG A 54 ? 0.1017 0.0953 0.0910 -0.0002 0.0000 -0.0108 140 ARG A CA 435 C C . ARG A 54 ? 0.0898 0.0831 0.0885 0.0017 -0.0018 -0.0043 140 ARG A C 436 O O . ARG A 54 ? 0.0772 0.0904 0.0832 0.0083 -0.0046 -0.0232 140 ARG A O 437 C CB . ARG A 54 ? 0.1126 0.1400 0.1192 -0.0024 0.0070 -0.0168 140 ARG A CB 438 C CG . ARG A 54 ? 0.2084 0.2132 0.2155 0.0148 0.0123 -0.0172 140 ARG A CG 439 C CD . ARG A 54 ? 0.2617 0.2743 0.2835 -0.0059 0.0158 0.0042 140 ARG A CD 440 N NE . ARG A 54 ? 0.3104 0.3380 0.3158 0.0046 -0.0032 -0.0041 140 ARG A NE 441 C CZ . ARG A 54 ? 0.3209 0.3475 0.3332 0.0063 0.0136 0.0025 140 ARG A CZ 442 N NH1 . ARG A 54 ? 0.3561 0.3744 0.3699 0.0041 0.0074 -0.0101 140 ARG A NH1 443 N NH2 . ARG A 54 ? 0.3451 0.4086 0.3636 0.0135 0.0052 0.0003 140 ARG A NH2 444 N N . ASN A 55 ? 0.0751 0.0777 0.0853 0.0083 -0.0044 -0.0038 141 ASN A N 445 C CA . ASN A 55 ? 0.0683 0.0746 0.0751 0.0020 0.0010 -0.0053 141 ASN A CA 446 C C . ASN A 55 ? 0.0667 0.0685 0.0584 -0.0037 0.0020 -0.0053 141 ASN A C 447 O O . ASN A 55 ? 0.0665 0.0749 0.0619 -0.0020 -0.0046 -0.0086 141 ASN A O 448 C CB . ASN A 55 ? 0.0742 0.0751 0.0731 -0.0037 0.0078 -0.0006 141 ASN A CB 449 C CG . ASN A 55 ? 0.0730 0.0939 0.0923 0.0117 -0.0007 -0.0137 141 ASN A CG 450 O OD1 . ASN A 55 ? 0.0834 0.0761 0.0986 -0.0043 0.0018 -0.0074 141 ASN A OD1 451 N ND2 . ASN A 55 ? 0.0816 0.0722 0.0746 -0.0149 0.0034 0.0046 141 ASN A ND2 452 N N . VAL A 56 ? 0.0604 0.0706 0.0697 -0.0019 0.0073 -0.0039 142 VAL A N 453 C CA . VAL A 56 ? 0.0725 0.0687 0.0792 0.0056 0.0019 -0.0020 142 VAL A CA 454 C C . VAL A 56 ? 0.0733 0.0769 0.0743 -0.0015 0.0040 -0.0071 142 VAL A C 455 O O . VAL A 56 ? 0.0973 0.0943 0.1035 -0.0036 -0.0084 -0.0110 142 VAL A O 456 C CB . VAL A 56 ? 0.0920 0.0875 0.0933 0.0016 0.0061 -0.0071 142 VAL A CB 457 C CG1 . VAL A 56 ? 0.1182 0.1082 0.1213 -0.0070 -0.0023 -0.0024 142 VAL A CG1 458 C CG2 . VAL A 56 ? 0.0863 0.0955 0.1173 -0.0100 -0.0009 -0.0047 142 VAL A CG2 459 N N . THR A 57 ? 0.0690 0.0638 0.0820 0.0051 -0.0025 -0.0011 143 THR A N 460 C CA . THR A 57 ? 0.0740 0.0825 0.0782 -0.0014 0.0014 -0.0015 143 THR A CA 461 C C . THR A 57 ? 0.0777 0.0755 0.0754 0.0005 0.0028 0.0020 143 THR A C 462 O O . THR A 57 ? 0.0936 0.0970 0.0783 -0.0079 -0.0050 -0.0038 143 THR A O 463 C CB . THR A 57 ? 0.0736 0.0795 0.0759 0.0084 0.0015 0.0033 143 THR A CB 464 O OG1 . THR A 57 ? 0.0930 0.0859 0.0980 -0.0198 -0.0038 -0.0128 143 THR A OG1 465 C CG2 . THR A 57 ? 0.0918 0.0985 0.0994 0.0090 0.0037 -0.0068 143 THR A CG2 466 N N . VAL A 58 ? 0.0711 0.0642 0.0651 -0.0062 0.0015 -0.0067 144 VAL A N 467 C CA . VAL A 58 ? 0.0702 0.0688 0.0808 0.0012 0.0015 0.0012 144 VAL A CA 468 C C . VAL A 58 ? 0.0745 0.0736 0.0854 0.0021 -0.0007 -0.0078 144 VAL A C 469 O O . VAL A 58 ? 0.0752 0.0751 0.0752 -0.0019 -0.0109 -0.0100 144 VAL A O 470 C CB . VAL A 58 ? 0.0612 0.0776 0.0764 -0.0010 0.0013 -0.0016 144 VAL A CB 471 C CG1 . VAL A 58 ? 0.0640 0.0638 0.0810 -0.0014 0.0118 0.0002 144 VAL A CG1 472 C CG2 . VAL A 58 ? 0.0846 0.0908 0.1002 -0.0056 0.0065 -0.0057 144 VAL A CG2 473 N N . ASP A 59 ? 0.0730 0.0744 0.0768 0.0013 -0.0017 -0.0103 145 ASP A N 474 C CA . ASP A 59 ? 0.0886 0.0814 0.0846 0.0052 -0.0037 -0.0013 145 ASP A CA 475 C C . ASP A 59 ? 0.0914 0.0826 0.0914 0.0014 0.0009 -0.0048 145 ASP A C 476 O O . ASP A 59 ? 0.1407 0.1006 0.1305 -0.0018 0.0231 0.0099 145 ASP A O 477 C CB . ASP A 59 ? 0.0725 0.0676 0.0729 0.0026 0.0094 -0.0023 145 ASP A CB 478 C CG . ASP A 59 ? 0.0975 0.1199 0.1059 -0.0006 0.0104 0.0115 145 ASP A CG 479 O OD1 . ASP A 59 ? 0.1192 0.1331 0.1350 -0.0038 0.0190 0.0040 145 ASP A OD1 480 O OD2 . ASP A 59 ? 0.0803 0.1014 0.1068 0.0005 0.0036 0.0127 145 ASP A OD2 481 N N . THR A 60 ? 0.0844 0.0877 0.0846 -0.0069 0.0047 0.0010 146 THR A N 482 C CA . THR A 60 ? 0.0897 0.0849 0.0845 -0.0021 -0.0028 0.0026 146 THR A CA 483 C C . THR A 60 ? 0.0895 0.0907 0.0855 -0.0016 0.0056 0.0020 146 THR A C 484 O O . THR A 60 ? 0.0966 0.1033 0.0955 0.0066 -0.0078 0.0050 146 THR A O 485 C CB . THR A 60 ? 0.0999 0.0933 0.0961 0.0001 0.0088 0.0032 146 THR A CB 486 O OG1 . THR A 60 ? 0.0953 0.0762 0.1003 -0.0066 0.0158 -0.0094 146 THR A OG1 487 C CG2 . THR A 60 ? 0.1068 0.1020 0.1120 -0.0138 0.0100 0.0006 146 THR A CG2 488 N N . LEU A 61 ? 0.0923 0.0954 0.0843 -0.0001 -0.0040 0.0045 147 LEU A N 489 C CA . LEU A 61 ? 0.1002 0.0893 0.0881 0.0024 -0.0027 -0.0049 147 LEU A CA 490 C C . LEU A 61 ? 0.0900 0.0779 0.0790 -0.0032 -0.0027 0.0008 147 LEU A C 491 O O . LEU A 61 ? 0.0919 0.0759 0.0872 0.0036 -0.0058 0.0026 147 LEU A O 492 C CB . LEU A 61 ? 0.0988 0.0996 0.1001 0.0071 -0.0052 -0.0037 147 LEU A CB 493 C CG . LEU A 61 ? 0.1276 0.1366 0.1279 0.0074 -0.0013 -0.0044 147 LEU A CG 494 C CD1 . LEU A 61 ? 0.1440 0.1518 0.1396 0.0048 0.0117 -0.0081 147 LEU A CD1 495 C CD2 . LEU A 61 ? 0.1287 0.1715 0.1610 -0.0076 0.0141 0.0032 147 LEU A CD2 496 N N . LEU A 62 ? 0.0717 0.0782 0.0729 0.0025 0.0000 0.0001 148 LEU A N 497 C CA . LEU A 62 ? 0.0665 0.0734 0.0839 0.0018 -0.0012 0.0021 148 LEU A CA 498 C C . LEU A 62 ? 0.0726 0.0692 0.0737 0.0049 -0.0011 0.0008 148 LEU A C 499 O O . LEU A 62 ? 0.0798 0.0749 0.0792 0.0008 -0.0080 0.0017 148 LEU A O 500 C CB . LEU A 62 ? 0.0593 0.0631 0.0600 0.0144 -0.0042 -0.0022 148 LEU A CB 501 C CG . LEU A 62 ? 0.0636 0.0610 0.0679 0.0061 0.0070 -0.0034 148 LEU A CG 502 C CD1 . LEU A 62 ? 0.0683 0.0830 0.0714 0.0022 0.0099 0.0014 148 LEU A CD1 503 C CD2 . LEU A 62 ? 0.0797 0.0956 0.0901 0.0070 0.0024 -0.0054 148 LEU A CD2 504 N N . VAL A 63 ? 0.0763 0.0693 0.0787 0.0057 -0.0064 -0.0033 149 VAL A N 505 C CA . VAL A 63 ? 0.0854 0.0771 0.0890 0.0060 -0.0088 0.0060 149 VAL A CA 506 C C . VAL A 63 ? 0.0848 0.0795 0.0843 0.0005 0.0023 0.0011 149 VAL A C 507 O O . VAL A 63 ? 0.0975 0.0822 0.0920 -0.0008 0.0057 0.0050 149 VAL A O 508 C CB . VAL A 63 ? 0.0994 0.0757 0.0884 0.0126 -0.0045 0.0041 149 VAL A CB 509 C CG1 . VAL A 63 ? 0.1298 0.0937 0.1180 0.0205 0.0013 -0.0046 149 VAL A CG1 510 C CG2 . VAL A 63 ? 0.1050 0.0953 0.0992 -0.0135 0.0031 -0.0123 149 VAL A CG2 511 N N . GLN A 64 ? 0.0909 0.0880 0.0846 0.0015 0.0063 0.0007 150 GLN A N 512 C CA . GLN A 64 ? 0.1020 0.1006 0.1004 0.0000 0.0020 0.0020 150 GLN A CA 513 C C . GLN A 64 ? 0.0891 0.0812 0.0918 0.0017 0.0030 0.0045 150 GLN A C 514 O O . GLN A 64 ? 0.1053 0.0939 0.0987 -0.0017 0.0049 0.0159 150 GLN A O 515 C CB A GLN A 64 ? 0.1077 0.1124 0.1111 0.0025 0.0041 0.0061 150 GLN A CB 516 C CB B GLN A 64 ? 0.1056 0.1125 0.1104 0.0001 0.0014 -0.0004 150 GLN A CB 517 C CG A GLN A 64 ? 0.1585 0.1525 0.1491 -0.0062 -0.0009 -0.0022 150 GLN A CG 518 C CG B GLN A 64 ? 0.1449 0.1556 0.1329 -0.0033 -0.0026 0.0119 150 GLN A CG 519 C CD A GLN A 64 ? 0.1861 0.2053 0.2068 0.0045 -0.0020 0.0019 150 GLN A CD 520 C CD B GLN A 64 ? 0.2185 0.1912 0.2095 -0.0007 -0.0050 -0.0010 150 GLN A CD 521 O OE1 A GLN A 64 ? 0.2583 0.2624 0.2472 -0.0171 -0.0169 -0.0070 150 GLN A OE1 522 O OE1 B GLN A 64 ? 0.2792 0.2647 0.2205 -0.0005 -0.0075 -0.0053 150 GLN A OE1 523 N NE2 A GLN A 64 ? 0.2063 0.2021 0.2210 -0.0065 0.0087 0.0029 150 GLN A NE2 524 N NE2 B GLN A 64 ? 0.2047 0.2105 0.2018 -0.0097 -0.0134 0.0033 150 GLN A NE2 525 N N . THR A 65 ? 0.0836 0.0705 0.0672 0.0043 0.0012 0.0051 151 THR A N 526 C CA . THR A 65 ? 0.0888 0.0855 0.0860 0.0020 -0.0008 0.0032 151 THR A CA 527 C C . THR A 65 ? 0.0898 0.0916 0.0874 0.0045 0.0037 0.0009 151 THR A C 528 O O . THR A 65 ? 0.0964 0.0993 0.0804 0.0053 0.0126 0.0045 151 THR A O 529 C CB . THR A 65 ? 0.1109 0.0984 0.1052 0.0028 0.0009 -0.0092 151 THR A CB 530 O OG1 . THR A 65 ? 0.1378 0.1456 0.1405 0.0183 0.0062 -0.0177 151 THR A OG1 531 C CG2 . THR A 65 ? 0.1280 0.1183 0.1274 -0.0014 -0.0082 0.0017 151 THR A CG2 532 N N . LEU A 66 ? 0.0809 0.0811 0.0797 0.0011 0.0047 0.0080 152 LEU A N 533 C CA . LEU A 66 ? 0.0865 0.0822 0.0884 0.0088 -0.0078 0.0004 152 LEU A CA 534 C C . LEU A 66 ? 0.0936 0.0894 0.0996 -0.0001 0.0012 0.0079 152 LEU A C 535 O O . LEU A 66 ? 0.1014 0.0859 0.0955 0.0025 -0.0069 0.0096 152 LEU A O 536 C CB . LEU A 66 ? 0.0860 0.0910 0.1008 0.0034 -0.0003 -0.0016 152 LEU A CB 537 C CG . LEU A 66 ? 0.0947 0.0916 0.0716 0.0048 -0.0074 0.0081 152 LEU A CG 538 C CD1 . LEU A 66 ? 0.0920 0.0749 0.0961 0.0096 -0.0024 0.0138 152 LEU A CD1 539 C CD2 . LEU A 66 ? 0.1313 0.1155 0.1003 -0.0060 -0.0011 0.0096 152 LEU A CD2 540 N N . SER A 67 ? 0.1090 0.0857 0.1015 0.0030 -0.0061 0.0028 153 SER A N 541 C CA . SER A 67 ? 0.1054 0.0980 0.1056 0.0097 0.0019 0.0051 153 SER A CA 542 C C . SER A 67 ? 0.1109 0.1064 0.1090 0.0091 0.0017 0.0050 153 SER A C 543 O O . SER A 67 ? 0.1128 0.0966 0.1197 0.0117 0.0028 0.0062 153 SER A O 544 C CB . SER A 67 ? 0.1415 0.1179 0.1183 0.0066 -0.0035 -0.0031 153 SER A CB 545 O OG . SER A 67 ? 0.1954 0.1849 0.1566 0.0001 0.0033 -0.0021 153 SER A OG 546 N N . GLU A 68 ? 0.0965 0.0718 0.0941 0.0096 -0.0013 0.0027 154 GLU A N 547 C CA . GLU A 68 ? 0.1092 0.0883 0.1133 0.0123 -0.0042 0.0063 154 GLU A CA 548 C C . GLU A 68 ? 0.1076 0.0927 0.1096 0.0049 0.0001 -0.0006 154 GLU A C 549 O O . GLU A 68 ? 0.1303 0.1054 0.1202 0.0119 -0.0090 0.0126 154 GLU A O 550 C CB . GLU A 68 ? 0.1108 0.0911 0.1071 0.0058 0.0020 0.0067 154 GLU A CB 551 C CG . GLU A 68 ? 0.1179 0.1009 0.1293 0.0013 0.0027 -0.0048 154 GLU A CG 552 C CD . GLU A 68 ? 0.1482 0.1633 0.1885 0.0004 0.0083 -0.0095 154 GLU A CD 553 O OE1 . GLU A 68 ? 0.1630 0.1513 0.1639 0.0134 0.0186 -0.0190 154 GLU A OE1 554 O OE2 . GLU A 68 ? 0.1871 0.2133 0.2364 -0.0156 0.0004 -0.0201 154 GLU A OE2 555 N N . ILE A 69 ? 0.0945 0.0890 0.0913 0.0024 -0.0016 0.0077 155 ILE A N 556 C CA . ILE A 69 ? 0.1067 0.0895 0.1034 0.0032 -0.0024 0.0053 155 ILE A CA 557 C C . ILE A 69 ? 0.0939 0.0890 0.0938 0.0009 -0.0042 -0.0023 155 ILE A C 558 O O . ILE A 69 ? 0.1145 0.0901 0.0992 0.0120 -0.0077 0.0189 155 ILE A O 559 C CB . ILE A 69 ? 0.1108 0.0856 0.0933 0.0063 0.0014 0.0102 155 ILE A CB 560 C CG1 . ILE A 69 ? 0.1168 0.1054 0.1082 -0.0042 0.0011 0.0060 155 ILE A CG1 561 C CG2 . ILE A 69 ? 0.1042 0.0889 0.1073 0.0172 0.0026 0.0012 155 ILE A CG2 562 C CD1 . ILE A 69 ? 0.1021 0.1033 0.0974 0.0098 -0.0003 0.0109 155 ILE A CD1 563 N N . ARG A 70 ? 0.0950 0.0975 0.1034 0.0130 -0.0087 0.0007 156 ARG A N 564 C CA . ARG A 70 ? 0.1052 0.0965 0.1046 0.0101 -0.0057 -0.0009 156 ARG A CA 565 C C . ARG A 70 ? 0.1188 0.1028 0.1077 0.0031 -0.0037 -0.0004 156 ARG A C 566 O O . ARG A 70 ? 0.1226 0.1017 0.1260 0.0208 -0.0137 0.0143 156 ARG A O 567 C CB . ARG A 70 ? 0.1162 0.0999 0.1026 0.0098 0.0025 0.0000 156 ARG A CB 568 C CG . ARG A 70 ? 0.1057 0.0962 0.1153 0.0137 -0.0071 0.0045 156 ARG A CG 569 C CD . ARG A 70 ? 0.1430 0.1267 0.1339 -0.0111 0.0063 0.0063 156 ARG A CD 570 N NE . ARG A 70 ? 0.1249 0.0975 0.1026 0.0199 0.0078 0.0051 156 ARG A NE 571 C CZ . ARG A 70 ? 0.1495 0.1299 0.1248 -0.0056 -0.0052 0.0049 156 ARG A CZ 572 N NH1 . ARG A 70 ? 0.1923 0.1462 0.1232 -0.0249 -0.0032 -0.0008 156 ARG A NH1 573 N NH2 . ARG A 70 ? 0.1457 0.1079 0.1125 -0.0052 0.0077 -0.0030 156 ARG A NH2 574 N N . GLU A 71 ? 0.1009 0.0824 0.0853 0.0097 -0.0067 0.0107 157 GLU A N 575 C CA . GLU A 71 ? 0.1316 0.0981 0.1172 0.0064 -0.0023 0.0080 157 GLU A CA 576 C C . GLU A 71 ? 0.1353 0.1135 0.1196 0.0133 -0.0060 0.0049 157 GLU A C 577 O O . GLU A 71 ? 0.1482 0.1280 0.1366 0.0276 -0.0095 0.0177 157 GLU A O 578 C CB . GLU A 71 ? 0.1471 0.1192 0.1361 0.0036 -0.0012 0.0125 157 GLU A CB 579 C CG . GLU A 71 ? 0.1777 0.1561 0.1617 0.0087 -0.0093 0.0199 157 GLU A CG 580 C CD . GLU A 71 ? 0.2252 0.2505 0.2712 -0.0119 0.0035 0.0038 157 GLU A CD 581 O OE1 . GLU A 71 ? 0.2521 0.2483 0.2927 -0.0104 0.0089 0.0113 157 GLU A OE1 582 O OE2 . GLU A 71 ? 0.3239 0.2893 0.3605 -0.0007 -0.0023 -0.0146 157 GLU A OE2 583 N N . ALA A 72 ? 0.1384 0.1184 0.1252 0.0181 -0.0025 0.0079 158 ALA A N 584 C CA . ALA A 72 ? 0.1407 0.1164 0.1284 0.0086 -0.0001 0.0022 158 ALA A CA 585 C C . ALA A 72 ? 0.1457 0.1195 0.1255 0.0086 -0.0050 -0.0019 158 ALA A C 586 O O . ALA A 72 ? 0.1630 0.1170 0.1316 0.0155 -0.0121 0.0207 158 ALA A O 587 C CB . ALA A 72 ? 0.1515 0.1130 0.1065 0.0134 0.0016 -0.0031 158 ALA A CB 588 N N . ASN A 73 ? 0.1309 0.1152 0.1157 0.0037 -0.0003 -0.0016 159 ASN A N 589 C CA . ASN A 73 ? 0.1230 0.1058 0.1166 0.0104 -0.0065 -0.0014 159 ASN A CA 590 C C . ASN A 73 ? 0.1358 0.1292 0.1465 0.0191 -0.0149 -0.0091 159 ASN A C 591 O O . ASN A 73 ? 0.1433 0.1317 0.1584 0.0272 -0.0289 0.0039 159 ASN A O 592 C CB . ASN A 73 ? 0.1174 0.1181 0.1087 0.0196 -0.0001 0.0012 159 ASN A CB 593 C CG . ASN A 73 ? 0.1379 0.1104 0.1312 0.0089 0.0039 0.0114 159 ASN A CG 594 O OD1 . ASN A 73 ? 0.1624 0.1081 0.1294 0.0190 -0.0166 0.0132 159 ASN A OD1 595 N ND2 . ASN A 73 ? 0.1336 0.1309 0.1262 -0.0002 -0.0209 0.0362 159 ASN A ND2 596 N N . GLN A 74 ? 0.1404 0.1252 0.1442 0.0197 -0.0197 -0.0008 160 GLN A N 597 C CA . GLN A 74 ? 0.1660 0.1474 0.1624 0.0182 -0.0066 -0.0019 160 GLN A CA 598 C C . GLN A 74 ? 0.1799 0.1596 0.1647 0.0100 -0.0065 0.0006 160 GLN A C 599 O O . GLN A 74 ? 0.2210 0.1794 0.1936 0.0240 -0.0155 -0.0001 160 GLN A O 600 C CB . GLN A 74 ? 0.1523 0.1470 0.1618 0.0209 0.0001 -0.0052 160 GLN A CB 601 C CG . GLN A 74 ? 0.1778 0.1653 0.1691 0.0190 0.0022 0.0042 160 GLN A CG 602 C CD . GLN A 74 ? 0.1562 0.1638 0.1762 0.0120 0.0001 0.0064 160 GLN A CD 603 O OE1 . GLN A 74 ? 0.1890 0.2448 0.2016 0.0300 0.0184 0.0016 160 GLN A OE1 604 N NE2 . GLN A 74 ? 0.1953 0.1688 0.1474 -0.0038 0.0179 -0.0023 160 GLN A NE2 605 N N . ALA A 75 ? 0.1880 0.1555 0.1682 0.0116 -0.0068 0.0110 161 ALA A N 606 C CA . ALA A 75 ? 0.2042 0.1736 0.1784 0.0082 -0.0032 0.0087 161 ALA A CA 607 C C . ALA A 75 ? 0.2008 0.1794 0.1815 0.0124 -0.0064 0.0104 161 ALA A C 608 O O . ALA A 75 ? 0.2325 0.2167 0.1973 0.0216 0.0076 0.0059 161 ALA A O 609 C CB . ALA A 75 ? 0.2155 0.1781 0.1812 0.0020 -0.0072 0.0078 161 ALA A CB 610 N N . GLY A 76 ? 0.2045 0.1876 0.1974 0.0118 -0.0101 0.0069 162 GLY A N 611 C CA . GLY A 76 ? 0.2238 0.1938 0.1914 0.0119 -0.0139 0.0065 162 GLY A CA 612 C C . GLY A 76 ? 0.2191 0.1926 0.1986 0.0100 -0.0166 0.0018 162 GLY A C 613 O O . GLY A 76 ? 0.2588 0.1920 0.1986 0.0173 -0.0287 0.0085 162 GLY A O 614 N N . ALA A 77 ? 0.2255 0.1840 0.1824 0.0129 -0.0170 0.0043 163 ALA A N 615 C CA . ALA A 77 ? 0.2098 0.1902 0.1885 0.0118 -0.0094 0.0025 163 ALA A CA 616 C C . ALA A 77 ? 0.2172 0.1948 0.1935 0.0133 -0.0117 0.0108 163 ALA A C 617 O O . ALA A 77 ? 0.2267 0.1987 0.2094 0.0237 -0.0199 0.0140 163 ALA A O 618 C CB . ALA A 77 ? 0.2126 0.1861 0.1864 0.0081 -0.0111 0.0074 163 ALA A CB 619 N N . ASN A 78 ? 0.2463 0.2109 0.2146 0.0094 -0.0083 0.0046 164 ASN A N 620 C CA . ASN A 78 ? 0.2426 0.2300 0.2260 0.0057 -0.0078 0.0062 164 ASN A CA 621 C C . ASN A 78 ? 0.2524 0.2202 0.2211 -0.0016 -0.0042 0.0025 164 ASN A C 622 O O . ASN A 78 ? 0.2811 0.2376 0.2254 0.0063 -0.0080 0.0004 164 ASN A O 623 C CB . ASN A 78 ? 0.2654 0.2503 0.2494 0.0061 -0.0111 0.0108 164 ASN A CB 624 C CG . ASN A 78 ? 0.3018 0.3172 0.3160 -0.0103 -0.0150 0.0062 164 ASN A CG 625 O OD1 . ASN A 78 ? 0.3296 0.3246 0.3416 -0.0099 -0.0273 0.0194 164 ASN A OD1 626 N ND2 . ASN A 78 ? 0.3885 0.3906 0.3610 -0.0019 -0.0245 0.0116 164 ASN A ND2 627 N N . PRO A 79 ? 0.2411 0.2145 0.2126 0.0067 -0.0107 0.0000 165 PRO A N 628 C CA . PRO A 79 ? 0.2085 0.1884 0.2018 0.0013 -0.0094 -0.0007 165 PRO A CA 629 C C . PRO A 79 ? 0.1744 0.1585 0.1757 0.0093 -0.0106 0.0023 165 PRO A C 630 O O . PRO A 79 ? 0.1879 0.1441 0.1715 0.0145 -0.0205 0.0097 165 PRO A O 631 C CB . PRO A 79 ? 0.2286 0.1963 0.2009 -0.0028 -0.0131 0.0023 165 PRO A CB 632 C CG . PRO A 79 ? 0.2427 0.2313 0.2438 0.0064 0.0039 0.0052 165 PRO A CG 633 C CD . PRO A 79 ? 0.2476 0.2175 0.2231 0.0021 -0.0091 -0.0027 165 PRO A CD 634 N N . GLN A 80 ? 0.1591 0.1392 0.1670 0.0101 -0.0212 0.0046 166 GLN A N 635 C CA . GLN A 80 ? 0.1501 0.1396 0.1554 0.0116 -0.0106 0.0022 166 GLN A CA 636 C C . GLN A 80 ? 0.1293 0.1161 0.1357 0.0077 -0.0159 0.0017 166 GLN A C 637 O O . GLN A 80 ? 0.1208 0.1309 0.1285 0.0104 -0.0166 -0.0037 166 GLN A O 638 C CB . GLN A 80 ? 0.1528 0.1514 0.1718 0.0123 -0.0099 0.0015 166 GLN A CB 639 C CG . GLN A 80 ? 0.1930 0.2186 0.2286 0.0206 -0.0100 0.0063 166 GLN A CG 640 C CD . GLN A 80 ? 0.2715 0.2669 0.2612 0.0125 -0.0016 -0.0005 166 GLN A CD 641 O OE1 . GLN A 80 ? 0.3389 0.3450 0.3221 0.0029 0.0061 0.0172 166 GLN A OE1 642 N NE2 . GLN A 80 ? 0.3494 0.2928 0.3399 -0.0111 -0.0037 -0.0016 166 GLN A NE2 643 N N . TYR A 81 ? 0.1061 0.1035 0.1204 0.0101 -0.0053 0.0117 167 TYR A N 644 C CA . TYR A 81 ? 0.0987 0.0932 0.0916 0.0120 -0.0056 0.0004 167 TYR A CA 645 C C . TYR A 81 ? 0.0925 0.0930 0.0969 0.0078 0.0076 0.0051 167 TYR A C 646 O O . TYR A 81 ? 0.0875 0.0935 0.1070 0.0240 -0.0040 0.0027 167 TYR A O 647 C CB . TYR A 81 ? 0.0957 0.1045 0.1029 0.0038 -0.0064 0.0225 167 TYR A CB 648 C CG . TYR A 81 ? 0.1224 0.1224 0.1336 0.0108 0.0041 -0.0142 167 TYR A CG 649 C CD1 . TYR A 81 ? 0.1119 0.1372 0.1015 0.0006 -0.0016 0.0168 167 TYR A CD1 650 C CD2 . TYR A 81 ? 0.1496 0.1317 0.1378 0.0053 0.0026 0.0132 167 TYR A CD2 651 C CE1 . TYR A 81 ? 0.1678 0.1474 0.1495 0.0038 0.0085 -0.0030 167 TYR A CE1 652 C CE2 . TYR A 81 ? 0.1761 0.1517 0.1640 -0.0026 0.0075 0.0152 167 TYR A CE2 653 C CZ . TYR A 81 ? 0.1967 0.1930 0.1642 0.0013 0.0268 0.0175 167 TYR A CZ 654 O OH . TYR A 81 ? 0.2859 0.2603 0.1988 -0.0052 0.0232 0.0229 167 TYR A OH 655 N N . ALA A 82 ? 0.1000 0.0936 0.0915 0.0148 0.0025 0.0034 168 ALA A N 656 C CA . ALA A 82 ? 0.0850 0.0855 0.0837 0.0088 0.0032 -0.0054 168 ALA A CA 657 C C . ALA A 82 ? 0.0859 0.0670 0.0865 0.0034 -0.0015 0.0007 168 ALA A C 658 O O . ALA A 82 ? 0.0965 0.0638 0.0754 0.0142 -0.0035 0.0125 168 ALA A O 659 C CB . ALA A 82 ? 0.1040 0.0914 0.0846 0.0103 -0.0012 0.0089 168 ALA A CB 660 N N . ALA A 83 ? 0.0831 0.0664 0.0866 0.0117 0.0022 -0.0013 169 ALA A N 661 C CA . ALA A 83 ? 0.0833 0.0664 0.0866 0.0019 -0.0040 0.0017 169 ALA A CA 662 C C . ALA A 83 ? 0.0662 0.0635 0.0679 0.0041 0.0025 -0.0013 169 ALA A C 663 O O . ALA A 83 ? 0.0640 0.0730 0.0700 0.0142 0.0052 -0.0010 169 ALA A O 664 C CB . ALA A 83 ? 0.0868 0.0780 0.0815 0.0051 0.0037 0.0071 169 ALA A CB 665 N N . GLN A 84 ? 0.0715 0.0663 0.0738 0.0101 -0.0015 -0.0020 170 GLN A N 666 C CA . GLN A 84 ? 0.0686 0.0625 0.0616 0.0023 -0.0072 0.0018 170 GLN A CA 667 C C . GLN A 84 ? 0.0650 0.0628 0.0638 -0.0014 0.0017 -0.0031 170 GLN A C 668 O O . GLN A 84 ? 0.0649 0.0627 0.0729 -0.0055 0.0059 0.0034 170 GLN A O 669 C CB . GLN A 84 ? 0.0611 0.0806 0.0720 0.0095 0.0049 0.0071 170 GLN A CB 670 C CG . GLN A 84 ? 0.0856 0.0748 0.0836 0.0004 0.0037 0.0135 170 GLN A CG 671 C CD . GLN A 84 ? 0.1075 0.1076 0.1010 0.0008 -0.0087 -0.0016 170 GLN A CD 672 O OE1 . GLN A 84 ? 0.1115 0.0985 0.1105 -0.0003 0.0034 0.0079 170 GLN A OE1 673 N NE2 . GLN A 84 ? 0.1165 0.0987 0.1004 0.0043 0.0031 0.0167 170 GLN A NE2 674 N N . ILE A 85 ? 0.0525 0.0502 0.0541 -0.0028 0.0001 -0.0009 171 ILE A N 675 C CA . ILE A 85 ? 0.0520 0.0634 0.0490 -0.0002 0.0007 0.0014 171 ILE A CA 676 C C . ILE A 85 ? 0.0619 0.0623 0.0619 -0.0021 0.0010 -0.0006 171 ILE A C 677 O O . ILE A 85 ? 0.0587 0.0661 0.0563 -0.0024 -0.0043 0.0037 171 ILE A O 678 C CB . ILE A 85 ? 0.0702 0.0742 0.0568 0.0034 -0.0040 -0.0070 171 ILE A CB 679 C CG1 . ILE A 85 ? 0.1043 0.0828 0.0798 0.0092 0.0080 -0.0097 171 ILE A CG1 680 C CG2 . ILE A 85 ? 0.0900 0.0934 0.0664 -0.0020 0.0086 -0.0044 171 ILE A CG2 681 C CD1 . ILE A 85 ? 0.1509 0.1151 0.1298 -0.0027 0.0109 0.0015 171 ILE A CD1 682 N N . VAL A 86 ? 0.0446 0.0500 0.0475 -0.0070 -0.0018 0.0111 172 VAL A N 683 C CA . VAL A 86 ? 0.0473 0.0480 0.0639 0.0017 0.0049 -0.0037 172 VAL A CA 684 C C . VAL A 86 ? 0.0581 0.0696 0.0671 -0.0025 0.0075 -0.0016 172 VAL A C 685 O O . VAL A 86 ? 0.0683 0.0572 0.0544 -0.0111 0.0027 -0.0074 172 VAL A O 686 C CB . VAL A 86 ? 0.0473 0.0560 0.0603 0.0016 0.0036 -0.0001 172 VAL A CB 687 C CG1 . VAL A 86 ? 0.0593 0.0686 0.0616 -0.0027 0.0027 0.0006 172 VAL A CG1 688 C CG2 . VAL A 86 ? 0.0778 0.0627 0.0762 0.0009 0.0049 0.0022 172 VAL A CG2 689 N N . VAL A 87 ? 0.0624 0.0580 0.0541 0.0013 -0.0022 -0.0024 173 VAL A N 690 C CA . VAL A 87 ? 0.0599 0.0527 0.0557 -0.0045 -0.0032 0.0017 173 VAL A CA 691 C C . VAL A 87 ? 0.0562 0.0605 0.0504 0.0075 -0.0083 0.0068 173 VAL A C 692 O O . VAL A 87 ? 0.0653 0.0488 0.0626 -0.0074 -0.0034 -0.0037 173 VAL A O 693 C CB . VAL A 87 ? 0.0553 0.0567 0.0667 0.0036 -0.0055 -0.0075 173 VAL A CB 694 C CG1 . VAL A 87 ? 0.0560 0.0816 0.0741 -0.0104 0.0102 -0.0057 173 VAL A CG1 695 C CG2 . VAL A 87 ? 0.0691 0.0701 0.0761 -0.0037 -0.0062 0.0032 173 VAL A CG2 696 N N . TYR A 88 ? 0.0592 0.0573 0.0559 -0.0003 0.0068 -0.0045 174 TYR A N 697 C CA . TYR A 88 ? 0.0491 0.0593 0.0604 0.0050 -0.0045 0.0062 174 TYR A CA 698 C C . TYR A 88 ? 0.0668 0.0693 0.0590 -0.0031 0.0027 -0.0055 174 TYR A C 699 O O . TYR A 88 ? 0.0705 0.0820 0.0732 -0.0047 -0.0105 0.0040 174 TYR A O 700 C CB . TYR A 88 ? 0.0498 0.0636 0.0599 0.0043 -0.0052 -0.0049 174 TYR A CB 701 C CG . TYR A 88 ? 0.0737 0.0566 0.0575 -0.0035 -0.0050 0.0149 174 TYR A CG 702 C CD1 . TYR A 88 ? 0.0653 0.0818 0.0673 0.0084 -0.0157 -0.0141 174 TYR A CD1 703 C CD2 . TYR A 88 ? 0.0596 0.0850 0.0956 0.0048 0.0121 -0.0041 174 TYR A CD2 704 C CE1 . TYR A 88 ? 0.0899 0.0611 0.0662 -0.0185 -0.0029 0.0166 174 TYR A CE1 705 C CE2 . TYR A 88 ? 0.0828 0.0936 0.0853 0.0038 0.0080 0.0168 174 TYR A CE2 706 C CZ . TYR A 88 ? 0.0570 0.0615 0.0704 0.0251 -0.0076 0.0008 174 TYR A CZ 707 O OH . TYR A 88 ? 0.0900 0.0951 0.1039 0.0164 0.0081 0.0061 174 TYR A OH 708 N N . ASP A 89 ? 0.0552 0.0717 0.0696 -0.0030 -0.0042 -0.0068 175 ASP A N 709 C CA . ASP A 89 ? 0.0633 0.0547 0.0596 0.0024 -0.0061 -0.0033 175 ASP A CA 710 C C . ASP A 89 ? 0.0522 0.0647 0.0645 0.0017 -0.0025 0.0000 175 ASP A C 711 O O . ASP A 89 ? 0.0596 0.0604 0.0708 -0.0037 0.0007 -0.0011 175 ASP A O 712 C CB . ASP A 89 ? 0.0767 0.0547 0.0728 0.0039 0.0002 -0.0058 175 ASP A CB 713 C CG . ASP A 89 ? 0.0880 0.0829 0.1014 0.0193 -0.0076 -0.0071 175 ASP A CG 714 O OD1 . ASP A 89 ? 0.0689 0.0565 0.0808 0.0006 -0.0002 0.0011 175 ASP A OD1 715 O OD2 . ASP A 89 ? 0.0769 0.0649 0.0837 0.0042 -0.0082 -0.0180 175 ASP A OD2 716 N N . LEU A 90 ? 0.0675 0.0558 0.0636 0.0071 -0.0049 -0.0026 176 LEU A N 717 C CA . LEU A 90 ? 0.0615 0.0683 0.0640 0.0035 0.0017 -0.0008 176 LEU A CA 718 C C . LEU A 90 ? 0.0595 0.0659 0.0713 0.0004 -0.0029 0.0045 176 LEU A C 719 O O . LEU A 90 ? 0.0691 0.0760 0.0770 0.0122 0.0046 -0.0016 176 LEU A O 720 C CB . LEU A 90 ? 0.0625 0.0636 0.0795 0.0020 -0.0026 0.0042 176 LEU A CB 721 C CG . LEU A 90 ? 0.0648 0.0671 0.0766 -0.0011 0.0073 0.0012 176 LEU A CG 722 C CD1 . LEU A 90 ? 0.0746 0.0787 0.0642 0.0000 -0.0050 -0.0035 176 LEU A CD1 723 C CD2 . LEU A 90 ? 0.0677 0.0565 0.0710 0.0117 0.0006 0.0133 176 LEU A CD2 724 N N . PRO A 91 ? 0.0527 0.0750 0.0679 0.0011 0.0031 -0.0017 177 PRO A N 725 C CA . PRO A 91 ? 0.0626 0.0651 0.0599 -0.0015 0.0005 -0.0018 177 PRO A CA 726 C C . PRO A 91 ? 0.0546 0.0573 0.0556 -0.0014 -0.0041 0.0006 177 PRO A C 727 O O . PRO A 91 ? 0.0540 0.0756 0.0717 -0.0083 -0.0096 0.0030 177 PRO A O 728 C CB . PRO A 91 ? 0.0666 0.0752 0.0654 0.0103 0.0010 -0.0062 177 PRO A CB 729 C CG . PRO A 91 ? 0.0822 0.0921 0.0755 0.0085 -0.0022 0.0027 177 PRO A CG 730 C CD . PRO A 91 ? 0.0632 0.0799 0.0583 0.0073 0.0082 0.0009 177 PRO A CD 731 N N . ASP A 92 ? 0.0572 0.0651 0.0688 0.0087 -0.0078 -0.0090 178 ASP A N 732 C CA . ASP A 92 ? 0.0788 0.0636 0.0774 0.0017 -0.0099 -0.0055 178 ASP A CA 733 C C . ASP A 92 ? 0.0782 0.0738 0.0746 0.0023 -0.0047 0.0001 178 ASP A C 734 O O . ASP A 92 ? 0.0689 0.0735 0.0812 0.0111 -0.0075 0.0047 178 ASP A O 735 C CB . ASP A 92 ? 0.0866 0.0898 0.0898 0.0020 -0.0124 0.0014 178 ASP A CB 736 C CG . ASP A 92 ? 0.1311 0.1007 0.1003 -0.0071 -0.0099 0.0003 178 ASP A CG 737 O OD1 . ASP A 92 ? 0.1000 0.1036 0.1122 0.0034 -0.0200 -0.0020 178 ASP A OD1 738 O OD2 . ASP A 92 ? 0.1868 0.1352 0.1475 -0.0023 -0.0468 0.0018 178 ASP A OD2 739 N N . ARG A 93 ? 0.0815 0.0723 0.0761 0.0027 -0.0057 -0.0015 179 ARG A N 740 C CA . ARG A 93 ? 0.0717 0.0673 0.0731 0.0057 -0.0017 -0.0009 179 ARG A CA 741 C C . ARG A 93 ? 0.0649 0.0790 0.0585 0.0051 -0.0019 -0.0013 179 ARG A C 742 O O . ARG A 93 ? 0.0627 0.0914 0.0887 0.0110 0.0028 -0.0078 179 ARG A O 743 C CB . ARG A 93 ? 0.0770 0.0666 0.0643 0.0117 0.0080 -0.0095 179 ARG A CB 744 C CG . ARG A 93 ? 0.0776 0.0965 0.0913 -0.0007 0.0045 0.0049 179 ARG A CG 745 C CD . ARG A 93 ? 0.0639 0.0859 0.0995 0.0035 0.0062 -0.0076 179 ARG A CD 746 N NE . ARG A 93 ? 0.0639 0.0834 0.0520 0.0034 0.0063 0.0097 179 ARG A NE 747 C CZ . ARG A 93 ? 0.0810 0.0881 0.0827 0.0049 -0.0053 -0.0029 179 ARG A CZ 748 N NH1 . ARG A 93 ? 0.0810 0.0622 0.0921 -0.0041 -0.0103 0.0058 179 ARG A NH1 749 N NH2 . ARG A 93 ? 0.0932 0.1231 0.1257 0.0057 0.0081 0.0113 179 ARG A NH2 750 N N . ASP A 94 ? 0.0769 0.0676 0.0756 0.0036 -0.0038 -0.0011 180 ASP A N 751 C CA . ASP A 94 ? 0.0630 0.0764 0.0814 -0.0001 0.0045 0.0010 180 ASP A CA 752 C C . ASP A 94 ? 0.0792 0.0884 0.0823 -0.0004 0.0025 0.0047 180 ASP A C 753 O O . ASP A 94 ? 0.0734 0.0902 0.0960 -0.0051 0.0118 0.0029 180 ASP A O 754 C CB . ASP A 94 ? 0.0759 0.0916 0.0937 0.0092 0.0070 0.0064 180 ASP A CB 755 C CG . ASP A 94 ? 0.0805 0.0909 0.0832 0.0033 0.0068 0.0005 180 ASP A CG 756 O OD1 . ASP A 94 ? 0.0904 0.1079 0.0996 0.0043 0.0067 0.0033 180 ASP A OD1 757 O OD2 . ASP A 94 ? 0.1020 0.1053 0.1149 0.0046 0.0188 0.0039 180 ASP A OD2 758 N N . CYS A 95 ? 0.0664 0.0830 0.0787 -0.0041 0.0028 0.0094 181 CYS A N 759 C CA . CYS A 95 ? 0.0824 0.0977 0.0797 0.0038 0.0066 0.0023 181 CYS A CA 760 C C . CYS A 95 ? 0.0786 0.0876 0.0789 0.0046 0.0033 0.0041 181 CYS A C 761 O O . CYS A 95 ? 0.0816 0.1147 0.0764 0.0050 -0.0043 -0.0017 181 CYS A O 762 C CB . CYS A 95 ? 0.0954 0.1075 0.0987 -0.0053 0.0112 -0.0004 181 CYS A CB 763 S SG . CYS A 95 ? 0.1101 0.1389 0.1038 -0.0165 0.0056 0.0107 181 CYS A SG 764 N N . ALA A 96 ? 0.0635 0.0915 0.0725 0.0126 0.0024 -0.0047 182 ALA A N 765 C CA . ALA A 96 ? 0.0922 0.0979 0.0967 0.0128 0.0042 0.0014 182 ALA A CA 766 C C . ALA A 96 ? 0.0960 0.1092 0.1037 0.0064 0.0049 -0.0018 182 ALA A C 767 O O . ALA A 96 ? 0.1184 0.1276 0.1324 0.0233 0.0132 -0.0025 182 ALA A O 768 C CB . ALA A 96 ? 0.0788 0.0955 0.1045 0.0064 0.0210 -0.0002 182 ALA A CB 769 N N . ALA A 97 ? 0.0887 0.1228 0.1089 0.0061 0.0118 0.0017 183 ALA A N 770 C CA . ALA A 97 ? 0.0967 0.1064 0.0929 0.0004 0.0035 0.0052 183 ALA A CA 771 C C . ALA A 97 ? 0.0976 0.1311 0.0946 0.0029 0.0100 0.0015 183 ALA A C 772 O O . ALA A 97 ? 0.1122 0.1572 0.1174 0.0112 -0.0024 0.0072 183 ALA A O 773 C CB . ALA A 97 ? 0.1036 0.1094 0.0967 0.0007 0.0102 -0.0003 183 ALA A CB 774 N N . ALA A 98 ? 0.0996 0.1279 0.0955 0.0077 0.0090 -0.0034 184 ALA A N 775 C CA . ALA A 98 ? 0.1110 0.1202 0.1050 0.0080 -0.0014 0.0041 184 ALA A CA 776 C C . ALA A 98 ? 0.1129 0.1174 0.1159 0.0029 0.0016 0.0076 184 ALA A C 777 O O . ALA A 98 ? 0.1412 0.1640 0.1493 0.0131 -0.0077 0.0097 184 ALA A O 778 C CB . ALA A 98 ? 0.1188 0.1103 0.1213 0.0119 0.0118 0.0056 184 ALA A CB 779 N N . ALA A 99 ? 0.1169 0.1276 0.1323 0.0073 -0.0082 0.0049 185 ALA A N 780 C CA . ALA A 99 ? 0.1252 0.1377 0.1334 0.0005 -0.0017 -0.0001 185 ALA A CA 781 C C . ALA A 99 ? 0.1377 0.1292 0.1445 0.0074 -0.0059 -0.0071 185 ALA A C 782 O O . ALA A 99 ? 0.1541 0.1553 0.1733 0.0129 -0.0019 -0.0130 185 ALA A O 783 C CB . ALA A 99 ? 0.1321 0.1281 0.1425 -0.0025 -0.0061 -0.0013 185 ALA A CB 784 N N . SER A 100 ? 0.1126 0.1413 0.1322 0.0127 0.0018 -0.0100 186 SER A N 785 C CA . SER A 100 ? 0.1144 0.1281 0.1150 0.0098 -0.0055 0.0011 186 SER A CA 786 C C . SER A 100 ? 0.1234 0.1303 0.1116 0.0041 -0.0017 -0.0004 186 SER A C 787 O O . SER A 100 ? 0.1107 0.1444 0.1512 -0.0003 -0.0130 0.0050 186 SER A O 788 C CB . SER A 100 ? 0.1064 0.1142 0.1096 0.0038 -0.0044 0.0078 186 SER A CB 789 O OG . SER A 100 ? 0.1044 0.1043 0.1361 0.0062 0.0124 -0.0020 186 SER A OG 790 N N . ASN A 101 ? 0.1119 0.1264 0.1183 0.0053 0.0069 0.0000 187 ASN A N 791 C CA . ASN A 101 ? 0.1304 0.1327 0.1286 -0.0007 0.0066 0.0032 187 ASN A CA 792 C C . ASN A 101 ? 0.1268 0.1146 0.1246 -0.0018 0.0088 0.0045 187 ASN A C 793 O O . ASN A 101 ? 0.1511 0.1343 0.1604 0.0083 0.0258 0.0026 187 ASN A O 794 C CB . ASN A 101 ? 0.1643 0.1579 0.1528 0.0023 0.0155 0.0108 187 ASN A CB 795 C CG . ASN A 101 ? 0.2025 0.1896 0.2078 0.0018 0.0157 0.0091 187 ASN A CG 796 O OD1 . ASN A 101 ? 0.2931 0.2375 0.2252 -0.0095 0.0203 0.0188 187 ASN A OD1 797 N ND2 . ASN A 101 ? 0.2094 0.2810 0.2436 0.0064 0.0170 0.0445 187 ASN A ND2 798 N N . GLY A 102 ? 0.1069 0.1161 0.1135 -0.0017 0.0017 0.0001 188 GLY A N 799 C CA . GLY A 102 ? 0.1069 0.0863 0.1065 -0.0048 0.0000 0.0006 188 GLY A CA 800 C C . GLY A 102 ? 0.0907 0.0909 0.0856 0.0037 -0.0049 0.0003 188 GLY A C 801 O O . GLY A 102 ? 0.1134 0.1007 0.1317 0.0140 -0.0088 0.0042 188 GLY A O 802 N N . GLU A 103 ? 0.0791 0.0834 0.0833 0.0031 -0.0116 -0.0052 189 GLU A N 803 C CA . GLU A 103 ? 0.0728 0.0931 0.0789 0.0005 -0.0075 -0.0042 189 GLU A CA 804 C C . GLU A 103 ? 0.0687 0.0787 0.0790 0.0017 0.0008 0.0002 189 GLU A C 805 O O . GLU A 103 ? 0.0981 0.1127 0.1056 -0.0200 -0.0070 -0.0118 189 GLU A O 806 C CB . GLU A 103 ? 0.0717 0.0909 0.0893 -0.0003 -0.0085 -0.0004 189 GLU A CB 807 C CG . GLU A 103 ? 0.0592 0.0931 0.0779 -0.0090 -0.0015 -0.0009 189 GLU A CG 808 C CD . GLU A 103 ? 0.0969 0.1053 0.1257 0.0101 -0.0004 -0.0120 189 GLU A CD 809 O OE1 . GLU A 103 ? 0.1237 0.1397 0.1955 0.0083 -0.0154 0.0187 189 GLU A OE1 810 O OE2 . GLU A 103 ? 0.0833 0.0812 0.1043 -0.0034 -0.0038 -0.0013 189 GLU A OE2 811 N N . TRP A 104 ? 0.0736 0.0866 0.0782 -0.0039 -0.0078 -0.0010 190 TRP A N 812 C CA . TRP A 104 ? 0.0764 0.0876 0.0889 -0.0016 0.0039 -0.0032 190 TRP A CA 813 C C . TRP A 104 ? 0.0869 0.0888 0.0794 -0.0040 0.0038 -0.0020 190 TRP A C 814 O O . TRP A 104 ? 0.0978 0.0914 0.1010 -0.0041 -0.0013 -0.0082 190 TRP A O 815 C CB . TRP A 104 ? 0.0727 0.0886 0.0922 -0.0015 -0.0041 0.0055 190 TRP A CB 816 C CG . TRP A 104 ? 0.0763 0.0865 0.0932 0.0037 0.0026 -0.0040 190 TRP A CG 817 C CD1 . TRP A 104 ? 0.0844 0.0869 0.1082 0.0050 -0.0049 -0.0109 190 TRP A CD1 818 C CD2 . TRP A 104 ? 0.0798 0.0887 0.0780 0.0125 0.0046 -0.0045 190 TRP A CD2 819 N NE1 . TRP A 104 ? 0.0725 0.0791 0.1005 0.0003 -0.0154 -0.0108 190 TRP A NE1 820 C CE2 . TRP A 104 ? 0.0576 0.0925 0.0958 -0.0093 -0.0094 -0.0061 190 TRP A CE2 821 C CE3 . TRP A 104 ? 0.0818 0.0593 0.0790 -0.0026 0.0082 -0.0016 190 TRP A CE3 822 C CZ2 . TRP A 104 ? 0.0781 0.0641 0.0829 -0.0048 0.0088 0.0043 190 TRP A CZ2 823 C CZ3 . TRP A 104 ? 0.0830 0.0984 0.1068 -0.0022 0.0040 -0.0022 190 TRP A CZ3 824 C CH2 . TRP A 104 ? 0.0904 0.0886 0.0808 -0.0013 -0.0038 -0.0081 190 TRP A CH2 825 N N . ALA A 105 ? 0.1105 0.0997 0.0891 -0.0036 -0.0081 -0.0059 191 ALA A N 826 C CA . ALA A 105 ? 0.0934 0.0899 0.0901 -0.0001 -0.0071 -0.0044 191 ALA A CA 827 C C . ALA A 105 ? 0.0967 0.0891 0.0898 0.0053 -0.0088 -0.0013 191 ALA A C 828 O O . ALA A 105 ? 0.1079 0.0982 0.0908 0.0119 -0.0122 -0.0064 191 ALA A O 829 C CB . ALA A 105 ? 0.1071 0.1269 0.1126 0.0035 -0.0033 0.0048 191 ALA A CB 830 N N . ILE A 106 ? 0.0814 0.0859 0.0873 -0.0080 -0.0062 -0.0039 192 ILE A N 831 C CA . ILE A 106 ? 0.1038 0.1117 0.0913 0.0003 -0.0043 -0.0042 192 ILE A CA 832 C C . ILE A 106 ? 0.1228 0.1288 0.1065 0.0056 -0.0058 -0.0014 192 ILE A C 833 O O . ILE A 106 ? 0.1289 0.1443 0.1101 0.0045 -0.0038 -0.0009 192 ILE A O 834 C CB . ILE A 106 ? 0.1132 0.1170 0.0945 -0.0006 -0.0039 -0.0024 192 ILE A CB 835 C CG1 . ILE A 106 ? 0.1059 0.1157 0.1011 0.0040 -0.0058 -0.0128 192 ILE A CG1 836 C CG2 . ILE A 106 ? 0.1280 0.1378 0.1245 -0.0122 -0.0031 -0.0016 192 ILE A CG2 837 C CD1 . ILE A 106 ? 0.1116 0.1186 0.1054 -0.0133 0.0061 0.0126 192 ILE A CD1 838 N N . ALA A 107 ? 0.1339 0.1509 0.1237 0.0019 -0.0090 -0.0040 193 ALA A N 839 C CA . ALA A 107 ? 0.1670 0.1647 0.1457 0.0044 -0.0100 -0.0080 193 ALA A CA 840 C C . ALA A 107 ? 0.1750 0.1644 0.1460 0.0018 -0.0119 -0.0064 193 ALA A C 841 O O . ALA A 107 ? 0.1853 0.1908 0.1379 0.0011 -0.0231 -0.0028 193 ALA A O 842 C CB . ALA A 107 ? 0.1758 0.1753 0.1649 -0.0002 -0.0210 -0.0095 193 ALA A CB 843 N N . ASN A 108 ? 0.1665 0.1599 0.1517 0.0018 -0.0057 -0.0008 194 ASN A N 844 C CA . ASN A 108 ? 0.1552 0.1512 0.1439 0.0005 -0.0037 -0.0030 194 ASN A CA 845 C C . ASN A 108 ? 0.1340 0.1314 0.1200 -0.0047 -0.0003 -0.0037 194 ASN A C 846 O O . ASN A 108 ? 0.1363 0.1185 0.1332 -0.0045 -0.0074 -0.0122 194 ASN A O 847 C CB A ASN A 108 ? 0.1666 0.1702 0.1739 -0.0050 -0.0050 -0.0029 194 ASN A CB 848 C CB B ASN A 108 ? 0.1596 0.1609 0.1619 -0.0010 -0.0038 -0.0018 194 ASN A CB 849 C CG A ASN A 108 ? 0.1825 0.1899 0.1999 -0.0025 -0.0038 -0.0031 194 ASN A CG 850 C CG B ASN A 108 ? 0.1810 0.1650 0.1774 -0.0020 -0.0036 -0.0048 194 ASN A CG 851 O OD1 A ASN A 108 ? 0.2096 0.2475 0.2204 -0.0120 -0.0021 -0.0020 194 ASN A OD1 852 O OD1 B ASN A 108 ? 0.2421 0.2048 0.1984 0.0050 0.0089 -0.0034 194 ASN A OD1 853 N ND2 A ASN A 108 ? 0.2262 0.2491 0.2124 -0.0051 -0.0117 0.0030 194 ASN A ND2 854 N ND2 B ASN A 108 ? 0.1878 0.1861 0.1969 0.0037 0.0045 0.0016 194 ASN A ND2 855 N N . ASN A 109 ? 0.1106 0.1213 0.1180 -0.0086 -0.0081 -0.0056 195 ASN A N 856 C CA . ASN A 109 ? 0.1181 0.1094 0.1106 0.0000 -0.0005 -0.0017 195 ASN A CA 857 C C . ASN A 109 ? 0.1057 0.0960 0.0991 0.0012 -0.0012 -0.0040 195 ASN A C 858 O O . ASN A 109 ? 0.1033 0.0873 0.0892 0.0074 -0.0063 -0.0120 195 ASN A O 859 C CB . ASN A 109 ? 0.1270 0.1127 0.1031 -0.0018 0.0003 -0.0086 195 ASN A CB 860 C CG . ASN A 109 ? 0.1472 0.1539 0.1459 0.0003 -0.0020 0.0001 195 ASN A CG 861 O OD1 . ASN A 109 ? 0.1690 0.1642 0.1600 -0.0161 0.0147 -0.0027 195 ASN A OD1 862 N ND2 . ASN A 109 ? 0.2021 0.1638 0.1798 0.0066 -0.0040 0.0056 195 ASN A ND2 863 N N . GLY A 110 ? 0.1054 0.0910 0.0865 0.0079 -0.0069 -0.0064 196 GLY A N 864 C CA . GLY A 110 ? 0.0946 0.0747 0.0745 0.0051 -0.0046 -0.0015 196 GLY A CA 865 C C . GLY A 110 ? 0.0946 0.0766 0.0825 0.0030 -0.0059 -0.0039 196 GLY A C 866 O O . GLY A 110 ? 0.1037 0.0818 0.0730 -0.0024 -0.0147 -0.0130 196 GLY A O 867 N N . VAL A 111 ? 0.0833 0.0851 0.0829 -0.0036 -0.0065 -0.0005 197 VAL A N 868 C CA . VAL A 111 ? 0.0944 0.0962 0.0897 -0.0058 -0.0038 -0.0004 197 VAL A CA 869 C C . VAL A 111 ? 0.0815 0.0897 0.0760 -0.0069 0.0025 0.0003 197 VAL A C 870 O O . VAL A 111 ? 0.0782 0.0850 0.0881 -0.0063 -0.0056 0.0062 197 VAL A O 871 C CB . VAL A 111 ? 0.1196 0.1091 0.0974 -0.0019 -0.0021 0.0021 197 VAL A CB 872 C CG1 . VAL A 111 ? 0.1390 0.1380 0.1434 -0.0205 0.0003 0.0227 197 VAL A CG1 873 C CG2 . VAL A 111 ? 0.1392 0.1063 0.1044 -0.0063 -0.0047 0.0124 197 VAL A CG2 874 N N . ASN A 112 ? 0.0939 0.0950 0.0893 -0.0110 -0.0066 0.0014 198 ASN A N 875 C CA . ASN A 112 ? 0.0914 0.0990 0.0944 -0.0075 -0.0025 -0.0037 198 ASN A CA 876 C C . ASN A 112 ? 0.0820 0.0770 0.0772 -0.0045 -0.0051 -0.0093 198 ASN A C 877 O O . ASN A 112 ? 0.0922 0.0782 0.0738 0.0024 -0.0033 -0.0086 198 ASN A O 878 C CB . ASN A 112 ? 0.1162 0.1229 0.1079 -0.0027 -0.0009 -0.0019 198 ASN A CB 879 C CG . ASN A 112 ? 0.1686 0.1699 0.1352 -0.0049 0.0030 0.0072 198 ASN A CG 880 O OD1 . ASN A 112 ? 0.2071 0.2551 0.1758 -0.0134 0.0252 0.0149 198 ASN A OD1 881 N ND2 . ASN A 112 ? 0.2243 0.2413 0.1774 0.0000 -0.0104 0.0066 198 ASN A ND2 882 N N . ASN A 113 ? 0.0766 0.0741 0.0666 0.0019 -0.0038 -0.0048 199 ASN A N 883 C CA . ASN A 113 ? 0.0751 0.0815 0.0704 -0.0015 -0.0003 -0.0050 199 ASN A CA 884 C C . ASN A 113 ? 0.0680 0.0762 0.0664 0.0016 0.0028 -0.0032 199 ASN A C 885 O O . ASN A 113 ? 0.0649 0.0795 0.0705 0.0073 0.0100 -0.0043 199 ASN A O 886 C CB . ASN A 113 ? 0.0664 0.0814 0.0750 0.0051 -0.0083 -0.0053 199 ASN A CB 887 C CG . ASN A 113 ? 0.0850 0.1011 0.1003 -0.0077 -0.0033 0.0023 199 ASN A CG 888 O OD1 . ASN A 113 ? 0.0948 0.1182 0.1262 -0.0140 0.0020 -0.0263 199 ASN A OD1 889 N ND2 . ASN A 113 ? 0.0913 0.1192 0.1242 -0.0023 0.0044 0.0109 199 ASN A ND2 890 N N . TYR A 114 ? 0.0565 0.0680 0.0601 0.0013 -0.0020 0.0031 200 TYR A N 891 C CA . TYR A 114 ? 0.0605 0.0665 0.0603 0.0024 0.0007 -0.0052 200 TYR A CA 892 C C . TYR A 114 ? 0.0638 0.0672 0.0675 -0.0025 0.0008 -0.0030 200 TYR A C 893 O O . TYR A 114 ? 0.0572 0.0604 0.0583 0.0033 0.0032 -0.0088 200 TYR A O 894 C CB . TYR A 114 ? 0.0599 0.0646 0.0773 0.0012 -0.0019 -0.0075 200 TYR A CB 895 C CG . TYR A 114 ? 0.0644 0.0430 0.0597 -0.0029 -0.0008 0.0062 200 TYR A CG 896 C CD1 . TYR A 114 ? 0.0554 0.0561 0.0584 0.0030 -0.0049 -0.0184 200 TYR A CD1 897 C CD2 . TYR A 114 ? 0.0718 0.0931 0.0858 -0.0049 -0.0126 0.0002 200 TYR A CD2 898 C CE1 . TYR A 114 ? 0.0683 0.0835 0.0539 0.0025 0.0093 -0.0116 200 TYR A CE1 899 C CE2 . TYR A 114 ? 0.0778 0.0806 0.0547 -0.0041 -0.0024 -0.0041 200 TYR A CE2 900 C CZ . TYR A 114 ? 0.0748 0.0631 0.0632 0.0034 0.0054 -0.0110 200 TYR A CZ 901 O OH . TYR A 114 ? 0.0730 0.0805 0.0892 0.0030 -0.0107 -0.0113 200 TYR A OH 902 N N . LYS A 115 ? 0.0644 0.0729 0.0668 -0.0032 0.0028 -0.0009 201 LYS A N 903 C CA . LYS A 115 ? 0.0709 0.0769 0.0785 -0.0016 -0.0013 0.0019 201 LYS A CA 904 C C . LYS A 115 ? 0.0707 0.0695 0.0591 0.0023 0.0022 0.0032 201 LYS A C 905 O O . LYS A 115 ? 0.0557 0.0871 0.0785 -0.0036 0.0052 -0.0004 201 LYS A O 906 C CB A LYS A 115 ? 0.0852 0.0957 0.0855 -0.0003 0.0006 -0.0093 201 LYS A CB 907 C CB B LYS A 115 ? 0.0861 0.0958 0.0856 -0.0011 0.0007 -0.0077 201 LYS A CB 908 C CG A LYS A 115 ? 0.0987 0.1067 0.0918 0.0017 -0.0061 0.0082 201 LYS A CG 909 C CG B LYS A 115 ? 0.1024 0.1093 0.1016 0.0008 -0.0050 0.0046 201 LYS A CG 910 C CD A LYS A 115 ? 0.1330 0.1305 0.1328 -0.0014 0.0119 0.0095 201 LYS A CD 911 C CD B LYS A 115 ? 0.1548 0.1388 0.1373 -0.0087 0.0081 0.0112 201 LYS A CD 912 C CE A LYS A 115 ? 0.1712 0.1415 0.1662 -0.0034 0.0077 0.0007 201 LYS A CE 913 C CE B LYS A 115 ? 0.1680 0.1720 0.1687 0.0014 0.0002 0.0018 201 LYS A CE 914 N NZ A LYS A 115 ? 0.2132 0.2033 0.1717 0.0074 0.0105 0.0143 201 LYS A NZ 915 N NZ B LYS A 115 ? 0.2257 0.2132 0.1892 -0.0100 0.0107 0.0070 201 LYS A NZ 916 N N . ALA A 116 ? 0.0639 0.0670 0.0572 0.0018 0.0047 0.0024 202 ALA A N 917 C CA . ALA A 116 ? 0.0593 0.0647 0.0623 0.0004 0.0020 0.0021 202 ALA A CA 918 C C . ALA A 116 ? 0.0658 0.0594 0.0659 -0.0060 0.0026 -0.0064 202 ALA A C 919 O O . ALA A 116 ? 0.0694 0.0806 0.0793 -0.0052 -0.0007 -0.0060 202 ALA A O 920 C CB . ALA A 116 ? 0.0807 0.0775 0.0714 -0.0020 0.0108 -0.0118 202 ALA A CB 921 N N . TYR A 117 ? 0.0627 0.0620 0.0606 -0.0067 -0.0020 -0.0017 203 TYR A N 922 C CA . TYR A 117 ? 0.0618 0.0617 0.0593 -0.0051 0.0017 -0.0024 203 TYR A CA 923 C C . TYR A 117 ? 0.0681 0.0627 0.0663 0.0023 -0.0003 -0.0005 203 TYR A C 924 O O . TYR A 117 ? 0.0698 0.0713 0.0695 0.0009 0.0017 0.0009 203 TYR A O 925 C CB . TYR A 117 ? 0.0587 0.0593 0.0599 -0.0031 -0.0010 -0.0099 203 TYR A CB 926 C CG . TYR A 117 ? 0.0699 0.0724 0.0629 -0.0019 0.0030 -0.0067 203 TYR A CG 927 C CD1 . TYR A 117 ? 0.0538 0.0565 0.0636 -0.0042 -0.0094 -0.0065 203 TYR A CD1 928 C CD2 . TYR A 117 ? 0.0631 0.0698 0.0802 -0.0042 0.0116 -0.0009 203 TYR A CD2 929 C CE1 . TYR A 117 ? 0.0816 0.0696 0.0719 -0.0115 0.0080 0.0023 203 TYR A CE1 930 C CE2 . TYR A 117 ? 0.0477 0.0634 0.0718 -0.0048 -0.0043 -0.0058 203 TYR A CE2 931 C CZ . TYR A 117 ? 0.0530 0.0580 0.0558 -0.0051 -0.0003 0.0023 203 TYR A CZ 932 O OH . TYR A 117 ? 0.0659 0.0538 0.0693 0.0044 0.0055 -0.0097 203 TYR A OH 933 N N . ILE A 118 ? 0.0523 0.0559 0.0613 0.0016 -0.0002 0.0037 204 ILE A N 934 C CA . ILE A 118 ? 0.0671 0.0658 0.0666 0.0022 0.0004 -0.0021 204 ILE A CA 935 C C . ILE A 118 ? 0.0645 0.0624 0.0756 -0.0016 -0.0041 -0.0069 204 ILE A C 936 O O . ILE A 118 ? 0.0620 0.0576 0.0547 -0.0009 -0.0001 0.0034 204 ILE A O 937 C CB . ILE A 118 ? 0.0686 0.0683 0.0630 0.0015 0.0019 -0.0027 204 ILE A CB 938 C CG1 . ILE A 118 ? 0.0709 0.0669 0.0653 -0.0021 -0.0027 0.0041 204 ILE A CG1 939 C CG2 . ILE A 118 ? 0.0801 0.0683 0.0977 -0.0089 0.0075 0.0029 204 ILE A CG2 940 C CD1 . ILE A 118 ? 0.0872 0.0691 0.0626 0.0008 0.0073 -0.0028 204 ILE A CD1 941 N N . ASN A 119 ? 0.0615 0.0707 0.0681 0.0043 -0.0021 0.0015 205 ASN A N 942 C CA . ASN A 119 ? 0.0704 0.0623 0.0772 0.0062 -0.0037 -0.0020 205 ASN A CA 943 C C . ASN A 119 ? 0.0708 0.0765 0.0702 0.0008 0.0052 -0.0019 205 ASN A C 944 O O . ASN A 119 ? 0.0676 0.0659 0.0699 0.0028 -0.0082 -0.0042 205 ASN A O 945 C CB . ASN A 119 ? 0.0922 0.0790 0.0911 0.0106 0.0056 -0.0045 205 ASN A CB 946 C CG . ASN A 119 ? 0.1058 0.1168 0.1041 0.0024 -0.0015 -0.0050 205 ASN A CG 947 O OD1 . ASN A 119 ? 0.1304 0.1166 0.1303 -0.0247 0.0327 -0.0066 205 ASN A OD1 948 N ND2 . ASN A 119 ? 0.1623 0.1757 0.1264 0.0017 0.0088 -0.0197 205 ASN A ND2 949 N N . ARG A 120 ? 0.0607 0.0646 0.0709 0.0061 0.0022 -0.0022 206 ARG A N 950 C CA . ARG A 120 ? 0.0667 0.0735 0.0857 -0.0006 -0.0021 -0.0051 206 ARG A CA 951 C C . ARG A 120 ? 0.0670 0.0667 0.0658 -0.0009 0.0057 -0.0002 206 ARG A C 952 O O . ARG A 120 ? 0.0545 0.0648 0.0718 0.0077 0.0096 -0.0015 206 ARG A O 953 C CB . ARG A 120 ? 0.0523 0.0636 0.0727 -0.0022 0.0005 -0.0115 206 ARG A CB 954 C CG . ARG A 120 ? 0.0480 0.0782 0.0796 -0.0001 -0.0046 -0.0062 206 ARG A CG 955 C CD . ARG A 120 ? 0.0766 0.0729 0.1005 -0.0084 0.0065 -0.0126 206 ARG A CD 956 N NE . ARG A 120 ? 0.0819 0.0815 0.0945 0.0037 0.0161 0.0018 206 ARG A NE 957 C CZ . ARG A 120 ? 0.0969 0.0932 0.1126 -0.0002 0.0058 0.0063 206 ARG A CZ 958 N NH1 . ARG A 120 ? 0.0952 0.1293 0.1498 0.0075 0.0136 0.0030 206 ARG A NH1 959 N NH2 . ARG A 120 ? 0.1238 0.1324 0.1512 -0.0006 0.0162 0.0090 206 ARG A NH2 960 N N . ILE A 121 ? 0.0722 0.0703 0.0619 0.0023 -0.0017 0.0032 207 ILE A N 961 C CA . ILE A 121 ? 0.0700 0.0701 0.0711 0.0009 0.0009 -0.0013 207 ILE A CA 962 C C . ILE A 121 ? 0.0605 0.0604 0.0654 0.0022 -0.0004 -0.0022 207 ILE A C 963 O O . ILE A 121 ? 0.0673 0.0654 0.0591 0.0037 0.0107 0.0002 207 ILE A O 964 C CB . ILE A 121 ? 0.0610 0.0682 0.0568 0.0038 0.0035 -0.0008 207 ILE A CB 965 C CG1 . ILE A 121 ? 0.0535 0.0556 0.0656 -0.0091 0.0010 -0.0019 207 ILE A CG1 966 C CG2 . ILE A 121 ? 0.0664 0.0587 0.0756 -0.0036 -0.0008 0.0003 207 ILE A CG2 967 C CD1 . ILE A 121 ? 0.0523 0.0585 0.0632 -0.0082 0.0250 -0.0022 207 ILE A CD1 968 N N . ARG A 122 ? 0.0623 0.0623 0.0617 0.0114 -0.0041 -0.0017 208 ARG A N 969 C CA . ARG A 122 ? 0.0590 0.0576 0.0618 -0.0076 0.0010 -0.0031 208 ARG A CA 970 C C . ARG A 122 ? 0.0532 0.0612 0.0615 -0.0027 -0.0029 -0.0021 208 ARG A C 971 O O . ARG A 122 ? 0.0618 0.0569 0.0821 -0.0100 -0.0014 0.0025 208 ARG A O 972 C CB . ARG A 122 ? 0.0628 0.0726 0.0787 -0.0022 -0.0084 0.0083 208 ARG A CB 973 C CG . ARG A 122 ? 0.0734 0.0750 0.0982 0.0024 -0.0031 0.0028 208 ARG A CG 974 C CD . ARG A 122 ? 0.0881 0.0989 0.0935 -0.0130 0.0015 0.0016 208 ARG A CD 975 N NE . ARG A 122 ? 0.1438 0.1707 0.1615 0.0076 0.0007 0.0044 208 ARG A NE 976 C CZ . ARG A 122 ? 0.1658 0.1512 0.1444 -0.0011 -0.0015 -0.0009 208 ARG A CZ 977 N NH1 . ARG A 122 ? 0.1516 0.1469 0.1626 0.0150 0.0190 -0.0122 208 ARG A NH1 978 N NH2 . ARG A 122 ? 0.1833 0.1954 0.1998 0.0133 0.0236 0.0096 208 ARG A NH2 979 N N . GLU A 123 ? 0.0679 0.0576 0.0695 -0.0056 0.0025 -0.0020 209 GLU A N 980 C CA . GLU A 123 ? 0.0675 0.0727 0.0705 0.0040 0.0000 -0.0047 209 GLU A CA 981 C C . GLU A 123 ? 0.0729 0.0683 0.0742 -0.0023 0.0069 0.0014 209 GLU A C 982 O O . GLU A 123 ? 0.0772 0.0777 0.0862 0.0024 -0.0070 0.0022 209 GLU A O 983 C CB . GLU A 123 ? 0.0617 0.0751 0.0732 -0.0005 -0.0049 -0.0050 209 GLU A CB 984 C CG . GLU A 123 ? 0.0841 0.1039 0.1017 -0.0002 0.0054 -0.0023 209 GLU A CG 985 C CD . GLU A 123 ? 0.1563 0.1947 0.1330 -0.0316 0.0032 -0.0163 209 GLU A CD 986 O OE1 . GLU A 123 ? 0.1497 0.1701 0.1380 -0.0218 0.0220 -0.0016 209 GLU A OE1 987 O OE2 . GLU A 123 ? 0.2185 0.2551 0.1501 -0.0414 0.0077 -0.0095 209 GLU A OE2 988 N N . ILE A 124 ? 0.0588 0.0644 0.0638 0.0072 -0.0017 -0.0027 210 ILE A N 989 C CA . ILE A 124 ? 0.0614 0.0611 0.0671 -0.0035 -0.0017 0.0027 210 ILE A CA 990 C C . ILE A 124 ? 0.0563 0.0670 0.0576 -0.0047 0.0064 0.0086 210 ILE A C 991 O O . ILE A 124 ? 0.0667 0.0581 0.0863 0.0100 0.0064 -0.0042 210 ILE A O 992 C CB . ILE A 124 ? 0.0707 0.0647 0.0713 0.0041 0.0009 0.0046 210 ILE A CB 993 C CG1 . ILE A 124 ? 0.0737 0.0670 0.0750 -0.0060 0.0052 0.0022 210 ILE A CG1 994 C CG2 . ILE A 124 ? 0.0711 0.0729 0.0773 0.0050 0.0037 0.0003 210 ILE A CG2 995 C CD1 . ILE A 124 ? 0.0724 0.0766 0.0705 -0.0110 0.0066 -0.0058 210 ILE A CD1 996 N N . LEU A 125 ? 0.0467 0.0588 0.0586 0.0074 -0.0036 -0.0105 211 LEU A N 997 C CA . LEU A 125 ? 0.0542 0.0663 0.0587 -0.0020 -0.0043 -0.0013 211 LEU A CA 998 C C . LEU A 125 ? 0.0728 0.0707 0.0740 0.0004 -0.0026 -0.0023 211 LEU A C 999 O O . LEU A 125 ? 0.0817 0.0853 0.0834 0.0047 -0.0053 0.0130 211 LEU A O 1000 C CB . LEU A 125 ? 0.0606 0.0644 0.0637 0.0001 0.0004 -0.0060 211 LEU A CB 1001 C CG . LEU A 125 ? 0.0554 0.0680 0.0733 0.0027 -0.0121 0.0024 211 LEU A CG 1002 C CD1 . LEU A 125 ? 0.0847 0.0901 0.1194 0.0025 -0.0065 0.0016 211 LEU A CD1 1003 C CD2 . LEU A 125 ? 0.1048 0.0934 0.1137 0.0157 0.0070 0.0050 211 LEU A CD2 1004 N N . ILE A 126 ? 0.0610 0.0645 0.0678 0.0049 0.0000 0.0094 212 ILE A N 1005 C CA . ILE A 126 ? 0.0710 0.0800 0.0812 0.0045 -0.0002 0.0040 212 ILE A CA 1006 C C . ILE A 126 ? 0.0720 0.0739 0.0717 0.0051 0.0030 -0.0038 212 ILE A C 1007 O O . ILE A 126 ? 0.0601 0.0860 0.0797 0.0010 0.0029 0.0013 212 ILE A O 1008 C CB . ILE A 126 ? 0.0630 0.0902 0.0858 0.0156 0.0060 0.0039 212 ILE A CB 1009 C CG1 . ILE A 126 ? 0.0688 0.0986 0.1013 0.0088 0.0050 -0.0079 212 ILE A CG1 1010 C CG2 . ILE A 126 ? 0.0881 0.0907 0.1005 0.0131 -0.0059 -0.0030 212 ILE A CG2 1011 C CD1 . ILE A 126 ? 0.0964 0.0879 0.1070 0.0075 0.0074 0.0023 212 ILE A CD1 1012 N N . SER A 127 ? 0.0626 0.0739 0.0719 0.0050 0.0037 0.0000 213 SER A N 1013 C CA . SER A 127 ? 0.0746 0.0745 0.0841 0.0075 0.0075 -0.0053 213 SER A CA 1014 C C . SER A 127 ? 0.0740 0.0680 0.0847 0.0000 0.0024 0.0013 213 SER A C 1015 O O . SER A 127 ? 0.0791 0.0846 0.0953 0.0123 0.0007 0.0006 213 SER A O 1016 C CB A SER A 127 ? 0.1022 0.0773 0.0902 0.0003 -0.0072 -0.0080 213 SER A CB 1017 C CB B SER A 127 ? 0.0950 0.0727 0.0880 -0.0001 -0.0040 -0.0049 213 SER A CB 1018 O OG A SER A 127 ? 0.1308 0.0995 0.1431 0.0070 -0.0056 -0.0034 213 SER A OG 1019 O OG B SER A 127 ? 0.1038 0.1208 0.0961 -0.0083 0.0044 -0.0135 213 SER A OG 1020 N N . PHE A 128 ? 0.0727 0.0649 0.0817 0.0115 0.0043 -0.0017 214 PHE A N 1021 C CA . PHE A 128 ? 0.0636 0.0637 0.0706 0.0078 0.0027 0.0104 214 PHE A CA 1022 C C . PHE A 128 ? 0.0647 0.0673 0.0661 0.0117 -0.0019 0.0017 214 PHE A C 1023 O O . PHE A 128 ? 0.0719 0.0848 0.0934 0.0193 -0.0085 -0.0033 214 PHE A O 1024 C CB . PHE A 128 ? 0.0689 0.0780 0.1032 0.0091 0.0008 0.0007 214 PHE A CB 1025 C CG . PHE A 128 ? 0.0711 0.0775 0.0923 0.0083 0.0081 -0.0001 214 PHE A CG 1026 C CD1 . PHE A 128 ? 0.0980 0.0912 0.1012 0.0022 0.0104 0.0041 214 PHE A CD1 1027 C CD2 . PHE A 128 ? 0.0955 0.0718 0.0879 0.0099 0.0087 0.0089 214 PHE A CD2 1028 C CE1 . PHE A 128 ? 0.1077 0.1003 0.1088 0.0000 0.0144 0.0094 214 PHE A CE1 1029 C CE2 . PHE A 128 ? 0.0950 0.1172 0.1142 0.0058 -0.0196 -0.0010 214 PHE A CE2 1030 C CZ . PHE A 128 ? 0.1130 0.1065 0.1353 -0.0240 0.0120 0.0057 214 PHE A CZ 1031 N N . SER A 129 ? 0.0675 0.0621 0.0851 0.0020 -0.0014 -0.0001 215 SER A N 1032 C CA . SER A 129 ? 0.0608 0.0575 0.0798 0.0108 0.0025 -0.0059 215 SER A CA 1033 C C . SER A 129 ? 0.0594 0.0669 0.0983 0.0107 -0.0007 -0.0027 215 SER A C 1034 O O . SER A 129 ? 0.0842 0.0778 0.1083 0.0184 -0.0121 -0.0072 215 SER A O 1035 C CB . SER A 129 ? 0.0715 0.0700 0.0801 -0.0040 0.0038 0.0082 215 SER A CB 1036 O OG . SER A 129 ? 0.0696 0.0739 0.0919 0.0146 0.0050 -0.0073 215 SER A OG 1037 N N . ASP A 130 ? 0.0814 0.0809 0.0871 0.0155 -0.0014 -0.0008 216 ASP A N 1038 C CA . ASP A 130 ? 0.0899 0.0791 0.0824 0.0114 0.0051 0.0000 216 ASP A CA 1039 C C . ASP A 130 ? 0.0858 0.0926 0.0798 0.0131 -0.0017 -0.0036 216 ASP A C 1040 O O . ASP A 130 ? 0.1311 0.1449 0.0976 0.0315 0.0012 0.0054 216 ASP A O 1041 C CB . ASP A 130 ? 0.0876 0.0724 0.0925 0.0143 0.0030 0.0063 216 ASP A CB 1042 C CG . ASP A 130 ? 0.1274 0.1162 0.1336 -0.0028 -0.0066 0.0053 216 ASP A CG 1043 O OD1 . ASP A 130 ? 0.1369 0.0996 0.1399 -0.0155 -0.0198 0.0040 216 ASP A OD1 1044 O OD2 . ASP A 130 ? 0.1940 0.1604 0.1681 -0.0207 -0.0282 0.0254 216 ASP A OD2 1045 N N . VAL A 131 ? 0.0739 0.0837 0.0572 0.0159 -0.0013 0.0018 217 VAL A N 1046 C CA . VAL A 131 ? 0.0781 0.0794 0.0699 0.0096 0.0031 -0.0016 217 VAL A CA 1047 C C . VAL A 131 ? 0.0626 0.0762 0.0597 0.0071 0.0070 0.0000 217 VAL A C 1048 O O . VAL A 131 ? 0.0784 0.0686 0.0667 0.0123 0.0089 -0.0039 217 VAL A O 1049 C CB . VAL A 131 ? 0.0926 0.0744 0.0703 -0.0003 0.0040 -0.0021 217 VAL A CB 1050 C CG1 . VAL A 131 ? 0.0998 0.0894 0.1053 0.0117 0.0049 0.0002 217 VAL A CG1 1051 C CG2 . VAL A 131 ? 0.0903 0.0812 0.0927 -0.0081 0.0019 0.0080 217 VAL A CG2 1052 N N . ARG A 132 ? 0.0788 0.0751 0.0899 0.0027 0.0033 -0.0008 218 ARG A N 1053 C CA . ARG A 132 ? 0.0681 0.0684 0.0813 0.0005 -0.0021 0.0002 218 ARG A CA 1054 C C . ARG A 132 ? 0.0715 0.0681 0.0705 -0.0001 -0.0047 0.0000 218 ARG A C 1055 O O . ARG A 132 ? 0.0657 0.0842 0.0856 0.0166 -0.0051 -0.0041 218 ARG A O 1056 C CB . ARG A 132 ? 0.0759 0.0932 0.0955 0.0068 -0.0038 -0.0015 218 ARG A CB 1057 C CG . ARG A 132 ? 0.1113 0.0983 0.1208 0.0241 -0.0087 -0.0070 218 ARG A CG 1058 C CD . ARG A 132 ? 0.0947 0.0898 0.1218 0.0114 -0.0055 -0.0054 218 ARG A CD 1059 N NE . ARG A 132 ? 0.1079 0.1255 0.1399 0.0136 -0.0209 -0.0074 218 ARG A NE 1060 C CZ . ARG A 132 ? 0.1278 0.1304 0.1441 0.0038 -0.0123 -0.0111 218 ARG A CZ 1061 N NH1 . ARG A 132 ? 0.0816 0.1303 0.1306 0.0045 -0.0159 -0.0077 218 ARG A NH1 1062 N NH2 . ARG A 132 ? 0.1349 0.1620 0.2020 0.0094 -0.0141 -0.0034 218 ARG A NH2 1063 N N . THR A 133 ? 0.0745 0.0625 0.0734 0.0040 -0.0034 -0.0044 219 THR A N 1064 C CA . THR A 133 ? 0.0632 0.0570 0.0614 -0.0014 0.0005 -0.0017 219 THR A CA 1065 C C . THR A 133 ? 0.0591 0.0576 0.0606 0.0058 0.0066 -0.0004 219 THR A C 1066 O O . THR A 133 ? 0.0764 0.0567 0.0760 0.0037 0.0069 -0.0044 219 THR A O 1067 C CB . THR A 133 ? 0.0608 0.0590 0.0707 0.0000 -0.0030 -0.0055 219 THR A CB 1068 O OG1 . THR A 133 ? 0.0794 0.0642 0.0653 0.0020 0.0007 -0.0095 219 THR A OG1 1069 C CG2 . THR A 133 ? 0.0766 0.0646 0.0811 -0.0020 -0.0107 -0.0034 219 THR A CG2 1070 N N . ILE A 134 ? 0.0568 0.0635 0.0532 0.0037 0.0030 0.0016 220 ILE A N 1071 C CA . ILE A 134 ? 0.0737 0.0712 0.0658 -0.0028 0.0038 -0.0014 220 ILE A CA 1072 C C . ILE A 134 ? 0.0644 0.0597 0.0604 0.0028 0.0065 -0.0050 220 ILE A C 1073 O O . ILE A 134 ? 0.0712 0.0614 0.0866 -0.0027 -0.0056 0.0058 220 ILE A O 1074 C CB . ILE A 134 ? 0.0789 0.0717 0.0753 -0.0004 0.0045 -0.0060 220 ILE A CB 1075 C CG1 . ILE A 134 ? 0.1112 0.1261 0.1070 0.0043 0.0014 -0.0043 220 ILE A CG1 1076 C CG2 . ILE A 134 ? 0.1013 0.0985 0.0861 0.0015 0.0100 -0.0032 220 ILE A CG2 1077 C CD1 . ILE A 134 ? 0.1065 0.1157 0.1121 0.0066 -0.0013 -0.0006 220 ILE A CD1 1078 N N . LEU A 135 ? 0.0485 0.0567 0.0540 -0.0043 -0.0032 -0.0023 221 LEU A N 1079 C CA . LEU A 135 ? 0.0536 0.0686 0.0574 -0.0006 0.0038 -0.0045 221 LEU A CA 1080 C C . LEU A 135 ? 0.0550 0.0578 0.0636 -0.0021 -0.0037 -0.0021 221 LEU A C 1081 O O . LEU A 135 ? 0.0560 0.0502 0.0643 -0.0059 0.0087 0.0097 221 LEU A O 1082 C CB . LEU A 135 ? 0.0499 0.0709 0.0576 -0.0075 -0.0024 -0.0032 221 LEU A CB 1083 C CG . LEU A 135 ? 0.0592 0.0832 0.0765 -0.0090 -0.0063 -0.0048 221 LEU A CG 1084 C CD1 . LEU A 135 ? 0.0847 0.0608 0.0934 -0.0150 0.0047 0.0027 221 LEU A CD1 1085 C CD2 . LEU A 135 ? 0.0930 0.0598 0.0980 0.0003 0.0044 -0.0027 221 LEU A CD2 1086 N N . VAL A 136 ? 0.0688 0.0615 0.0649 -0.0019 0.0048 -0.0001 222 VAL A N 1087 C CA . VAL A 136 ? 0.0574 0.0619 0.0594 -0.0024 -0.0011 -0.0011 222 VAL A CA 1088 C C . VAL A 136 ? 0.0564 0.0534 0.0545 0.0012 0.0008 -0.0034 222 VAL A C 1089 O O . VAL A 136 ? 0.0629 0.0625 0.0630 -0.0004 0.0015 -0.0056 222 VAL A O 1090 C CB . VAL A 136 ? 0.0701 0.0486 0.0605 0.0021 0.0084 0.0005 222 VAL A CB 1091 C CG1 . VAL A 136 ? 0.0705 0.0825 0.0769 0.0141 0.0024 -0.0048 222 VAL A CG1 1092 C CG2 . VAL A 136 ? 0.0695 0.0601 0.0752 0.0132 0.0053 0.0042 222 VAL A CG2 1093 N N . ILE A 137 ? 0.0481 0.0423 0.0510 -0.0026 0.0014 -0.0007 223 ILE A N 1094 C CA . ILE A 137 ? 0.0521 0.0348 0.0566 -0.0023 0.0040 0.0008 223 ILE A CA 1095 C C . ILE A 137 ? 0.0575 0.0525 0.0680 -0.0013 -0.0021 -0.0030 223 ILE A C 1096 O O . ILE A 137 ? 0.0476 0.0536 0.0554 -0.0052 0.0018 -0.0040 223 ILE A O 1097 C CB . ILE A 137 ? 0.0550 0.0496 0.0583 0.0042 0.0020 0.0014 223 ILE A CB 1098 C CG1 . ILE A 137 ? 0.0592 0.0521 0.0628 0.0029 -0.0044 0.0010 223 ILE A CG1 1099 C CG2 . ILE A 137 ? 0.0712 0.0660 0.0796 0.0026 0.0002 -0.0025 223 ILE A CG2 1100 C CD1 . ILE A 137 ? 0.0655 0.0637 0.0653 0.0004 -0.0052 0.0000 223 ILE A CD1 1101 N N . GLU A 138 ? 0.0483 0.0540 0.0531 0.0022 -0.0115 0.0068 224 GLU A N 1102 C CA . GLU A 138 ? 0.0483 0.0573 0.0632 0.0003 -0.0016 -0.0037 224 GLU A CA 1103 C C . GLU A 138 ? 0.0356 0.0542 0.0431 -0.0025 -0.0024 -0.0068 224 GLU A C 1104 O O . GLU A 138 ? 0.0531 0.0662 0.0498 0.0008 0.0052 -0.0070 224 GLU A O 1105 C CB . GLU A 138 ? 0.0623 0.0619 0.0690 0.0010 -0.0041 0.0028 224 GLU A CB 1106 C CG . GLU A 138 ? 0.0595 0.0659 0.0631 0.0041 -0.0061 0.0039 224 GLU A CG 1107 C CD . GLU A 138 ? 0.0696 0.0631 0.0552 0.0008 -0.0090 0.0009 224 GLU A CD 1108 O OE1 . GLU A 138 ? 0.0648 0.0764 0.0607 0.0007 0.0029 -0.0029 224 GLU A OE1 1109 O OE2 . GLU A 138 ? 0.0589 0.0609 0.0635 0.0115 -0.0016 0.0010 224 GLU A OE2 1110 N N . PRO A 139 ? 0.0465 0.0487 0.0579 -0.0002 0.0020 0.0029 225 PRO A N 1111 C CA . PRO A 139 ? 0.0616 0.0573 0.0557 -0.0062 0.0023 -0.0013 225 PRO A CA 1112 C C . PRO A 139 ? 0.0499 0.0607 0.0611 0.0010 0.0024 -0.0040 225 PRO A C 1113 O O . PRO A 139 ? 0.0588 0.0678 0.0705 -0.0017 0.0042 -0.0024 225 PRO A O 1114 C CB . PRO A 139 ? 0.0787 0.0892 0.0675 0.0055 0.0110 0.0024 225 PRO A CB 1115 C CG . PRO A 139 ? 0.0774 0.0749 0.0582 -0.0077 0.0046 -0.0015 225 PRO A CG 1116 C CD . PRO A 139 ? 0.0534 0.0552 0.0568 -0.0049 -0.0027 -0.0102 225 PRO A CD 1117 N N . ASP A 140 ? 0.0700 0.0632 0.0686 0.0001 -0.0012 0.0006 226 ASP A N 1118 C CA . ASP A 140 ? 0.0720 0.0695 0.0699 0.0055 -0.0004 0.0074 226 ASP A CA 1119 C C . ASP A 140 ? 0.0706 0.0634 0.0739 0.0054 -0.0029 0.0050 226 ASP A C 1120 O O . ASP A 140 ? 0.0786 0.0629 0.0932 0.0029 -0.0029 0.0029 226 ASP A O 1121 C CB . ASP A 140 ? 0.0832 0.0946 0.0740 0.0061 0.0116 0.0006 226 ASP A CB 1122 C CG . ASP A 140 ? 0.1190 0.1132 0.0929 0.0056 -0.0013 0.0048 226 ASP A CG 1123 O OD1 . ASP A 140 ? 0.1284 0.1168 0.1340 -0.0111 0.0025 0.0022 226 ASP A OD1 1124 O OD2 . ASP A 140 ? 0.1181 0.1153 0.1389 0.0084 -0.0145 -0.0023 226 ASP A OD2 1125 N N . SER A 141 ? 0.0597 0.0734 0.0638 0.0064 -0.0091 0.0106 227 SER A N 1126 C CA . SER A 141 ? 0.0641 0.0623 0.0709 0.0032 -0.0022 -0.0024 227 SER A CA 1127 C C . SER A 141 ? 0.0570 0.0612 0.0658 0.0019 -0.0009 0.0029 227 SER A C 1128 O O . SER A 141 ? 0.0733 0.0619 0.0684 0.0035 -0.0132 -0.0010 227 SER A O 1129 C CB . SER A 141 ? 0.0640 0.0687 0.0634 0.0051 0.0056 0.0015 227 SER A CB 1130 O OG . SER A 141 ? 0.0597 0.0818 0.0648 -0.0054 0.0021 -0.0027 227 SER A OG 1131 N N . LEU A 142 ? 0.0615 0.0655 0.0559 -0.0019 -0.0052 0.0044 228 LEU A N 1132 C CA . LEU A 142 ? 0.0705 0.0669 0.0655 0.0026 0.0014 0.0062 228 LEU A CA 1133 C C . LEU A 142 ? 0.0681 0.0698 0.0737 -0.0013 -0.0024 0.0021 228 LEU A C 1134 O O . LEU A 142 ? 0.0694 0.0763 0.0782 0.0007 -0.0001 0.0121 228 LEU A O 1135 C CB . LEU A 142 ? 0.0679 0.0875 0.0796 -0.0066 0.0000 0.0033 228 LEU A CB 1136 C CG . LEU A 142 ? 0.1098 0.0929 0.1121 -0.0068 -0.0047 -0.0047 228 LEU A CG 1137 C CD1 . LEU A 142 ? 0.1252 0.1198 0.1549 0.0032 0.0114 -0.0003 228 LEU A CD1 1138 C CD2 . LEU A 142 ? 0.1271 0.1345 0.1260 -0.0028 0.0051 -0.0084 228 LEU A CD2 1139 N N . ALA A 143 ? 0.0756 0.0596 0.0715 -0.0007 0.0006 0.0065 229 ALA A N 1140 C CA . ALA A 143 ? 0.0636 0.0750 0.0694 -0.0028 0.0044 -0.0038 229 ALA A CA 1141 C C . ALA A 143 ? 0.0709 0.0651 0.0700 -0.0043 0.0009 0.0022 229 ALA A C 1142 O O . ALA A 143 ? 0.0837 0.0735 0.0698 -0.0071 0.0029 -0.0042 229 ALA A O 1143 C CB . ALA A 143 ? 0.0681 0.0627 0.0697 0.0053 -0.0054 0.0041 229 ALA A CB 1144 N N . ASN A 144 ? 0.0825 0.0707 0.0722 0.0066 -0.0082 0.0010 230 ASN A N 1145 C CA . ASN A 144 ? 0.0674 0.0737 0.0675 0.0028 -0.0042 0.0018 230 ASN A CA 1146 C C . ASN A 144 ? 0.0830 0.0698 0.0810 -0.0008 -0.0005 0.0006 230 ASN A C 1147 O O . ASN A 144 ? 0.0773 0.0808 0.0849 0.0050 -0.0028 0.0083 230 ASN A O 1148 C CB . ASN A 144 ? 0.0825 0.0593 0.0852 0.0123 -0.0106 0.0005 230 ASN A CB 1149 C CG . ASN A 144 ? 0.0896 0.0892 0.0863 0.0036 -0.0061 0.0001 230 ASN A CG 1150 O OD1 . ASN A 144 ? 0.0881 0.1011 0.1212 -0.0022 0.0050 0.0133 230 ASN A OD1 1151 N ND2 . ASN A 144 ? 0.0855 0.0893 0.0994 0.0027 -0.0260 0.0109 230 ASN A ND2 1152 N N . MET A 145 ? 0.0774 0.0700 0.0803 -0.0059 -0.0047 0.0026 231 MET A N 1153 C CA . MET A 145 ? 0.0953 0.0961 0.0903 -0.0019 0.0077 0.0024 231 MET A CA 1154 C C . MET A 145 ? 0.1046 0.1058 0.1022 -0.0051 0.0027 0.0010 231 MET A C 1155 O O . MET A 145 ? 0.1422 0.1167 0.1110 -0.0108 -0.0054 0.0068 231 MET A O 1156 C CB . MET A 145 ? 0.0846 0.0854 0.0887 -0.0046 0.0055 0.0058 231 MET A CB 1157 C CG . MET A 145 ? 0.0911 0.1026 0.0995 -0.0033 0.0083 0.0083 231 MET A CG 1158 S SD . MET A 145 ? 0.1065 0.1010 0.0961 -0.0002 0.0065 0.0066 231 MET A SD 1159 C CE . MET A 145 ? 0.1200 0.1322 0.1132 0.0042 0.0097 -0.0098 231 MET A CE 1160 N N . VAL A 146 ? 0.1060 0.0888 0.0902 0.0015 0.0001 0.0086 232 VAL A N 1161 C CA . VAL A 146 ? 0.0944 0.1034 0.1032 -0.0104 -0.0052 0.0060 232 VAL A CA 1162 C C . VAL A 146 ? 0.1102 0.0940 0.1032 -0.0025 -0.0023 -0.0002 232 VAL A C 1163 O O . VAL A 146 ? 0.1558 0.1166 0.1318 -0.0066 -0.0032 0.0136 232 VAL A O 1164 C CB . VAL A 146 ? 0.1054 0.1041 0.0956 -0.0076 -0.0008 0.0031 232 VAL A CB 1165 C CG1 . VAL A 146 ? 0.1043 0.1114 0.1165 -0.0091 0.0002 0.0008 232 VAL A CG1 1166 C CG2 . VAL A 146 ? 0.1088 0.1182 0.1155 -0.0107 -0.0130 -0.0008 232 VAL A CG2 1167 N N . THR A 147 ? 0.1066 0.0945 0.0942 0.0049 -0.0030 0.0003 233 THR A N 1168 C CA . THR A 147 ? 0.1068 0.0830 0.0905 0.0036 -0.0018 0.0040 233 THR A CA 1169 C C . THR A 147 ? 0.0963 0.0853 0.1069 0.0113 -0.0068 -0.0005 233 THR A C 1170 O O . THR A 147 ? 0.1320 0.1018 0.1315 0.0346 -0.0130 -0.0079 233 THR A O 1171 C CB . THR A 147 ? 0.1110 0.0939 0.0918 0.0060 -0.0023 0.0036 233 THR A CB 1172 O OG1 . THR A 147 ? 0.1252 0.0950 0.0805 0.0103 -0.0007 0.0056 233 THR A OG1 1173 C CG2 . THR A 147 ? 0.1386 0.1141 0.1326 -0.0093 -0.0020 0.0004 233 THR A CG2 1174 N N . ASN A 148 ? 0.0855 0.0872 0.0801 0.0098 -0.0061 0.0002 234 ASN A N 1175 C CA . ASN A 148 ? 0.0865 0.0819 0.0869 0.0052 -0.0042 0.0020 234 ASN A CA 1176 C C . ASN A 148 ? 0.0919 0.0934 0.0930 -0.0002 -0.0063 0.0026 234 ASN A C 1177 O O . ASN A 148 ? 0.1111 0.1052 0.1168 0.0003 -0.0207 0.0013 234 ASN A O 1178 C CB . ASN A 148 ? 0.0731 0.0828 0.0839 0.0086 -0.0066 0.0064 234 ASN A CB 1179 C CG . ASN A 148 ? 0.1159 0.1081 0.1212 -0.0019 0.0089 0.0084 234 ASN A CG 1180 O OD1 . ASN A 148 ? 0.1989 0.1396 0.1773 0.0279 0.0336 0.0000 234 ASN A OD1 1181 N ND2 . ASN A 148 ? 0.1211 0.1171 0.1101 0.0181 -0.0065 0.0152 234 ASN A ND2 1182 N N . MET A 149 ? 0.0991 0.1018 0.0905 -0.0027 -0.0016 0.0075 235 MET A N 1183 C CA . MET A 149 ? 0.1110 0.1041 0.1021 -0.0002 -0.0040 0.0018 235 MET A CA 1184 C C . MET A 149 ? 0.1087 0.1202 0.1049 0.0015 -0.0037 -0.0041 235 MET A C 1185 O O . MET A 149 ? 0.1336 0.1450 0.1110 0.0065 -0.0053 0.0058 235 MET A O 1186 C CB . MET A 149 ? 0.1090 0.1168 0.1092 -0.0022 -0.0096 0.0045 235 MET A CB 1187 C CG . MET A 149 ? 0.1165 0.1261 0.1395 -0.0037 -0.0046 0.0145 235 MET A CG 1188 S SD . MET A 149 ? 0.1465 0.1380 0.1465 0.0204 -0.0030 0.0224 235 MET A SD 1189 C CE . MET A 149 ? 0.1492 0.1419 0.1341 -0.0049 0.0033 -0.0087 235 MET A CE 1190 N N . ASN A 150 ? 0.1219 0.1309 0.1112 0.0051 -0.0053 -0.0019 236 ASN A N 1191 C CA . ASN A 150 ? 0.1339 0.1362 0.1233 0.0113 0.0022 0.0062 236 ASN A CA 1192 C C . ASN A 150 ? 0.1168 0.1223 0.1187 0.0154 0.0026 0.0036 236 ASN A C 1193 O O . ASN A 150 ? 0.1329 0.1479 0.1482 0.0107 -0.0128 0.0215 236 ASN A O 1194 C CB . ASN A 150 ? 0.1508 0.1483 0.1443 0.0193 -0.0051 0.0027 236 ASN A CB 1195 C CG . ASN A 150 ? 0.1822 0.1951 0.1620 0.0058 0.0003 0.0065 236 ASN A CG 1196 O OD1 . ASN A 150 ? 0.2184 0.2110 0.1930 0.0460 -0.0008 0.0028 236 ASN A OD1 1197 N ND2 . ASN A 150 ? 0.2251 0.2645 0.2198 0.0083 0.0165 0.0020 236 ASN A ND2 1198 N N . VAL A 151 ? 0.1086 0.1111 0.1066 0.0093 0.0095 0.0091 237 VAL A N 1199 C CA . VAL A 151 ? 0.0982 0.1132 0.1043 0.0166 0.0000 -0.0006 237 VAL A CA 1200 C C . VAL A 151 ? 0.0986 0.1189 0.0996 0.0091 0.0055 -0.0036 237 VAL A C 1201 O O . VAL A 151 ? 0.0991 0.1240 0.1180 0.0178 -0.0111 0.0047 237 VAL A O 1202 C CB . VAL A 151 ? 0.1253 0.1089 0.1053 0.0096 0.0078 0.0083 237 VAL A CB 1203 C CG1 . VAL A 151 ? 0.1256 0.1441 0.1380 0.0117 -0.0150 0.0112 237 VAL A CG1 1204 C CG2 . VAL A 151 ? 0.1361 0.1609 0.1404 0.0100 0.0013 -0.0008 237 VAL A CG2 1205 N N . PRO A 152 ? 0.0896 0.1042 0.0935 0.0185 -0.0004 0.0024 238 PRO A N 1206 C CA . PRO A 152 ? 0.0963 0.0956 0.0863 0.0068 -0.0036 0.0017 238 PRO A CA 1207 C C . PRO A 152 ? 0.0876 0.0908 0.0814 0.0072 -0.0013 0.0059 238 PRO A C 1208 O O . PRO A 152 ? 0.0993 0.1226 0.1077 0.0089 -0.0032 0.0076 238 PRO A O 1209 C CB . PRO A 152 ? 0.0998 0.0997 0.1090 0.0093 -0.0076 0.0046 238 PRO A CB 1210 C CG . PRO A 152 ? 0.1207 0.1168 0.1031 0.0173 0.0088 0.0076 238 PRO A CG 1211 C CD . PRO A 152 ? 0.0861 0.1076 0.1066 0.0059 -0.0064 -0.0017 238 PRO A CD 1212 N N . LYS A 153 ? 0.0822 0.0928 0.0947 0.0047 -0.0029 0.0022 239 LYS A N 1213 C CA . LYS A 153 ? 0.0736 0.0827 0.0895 -0.0020 -0.0084 -0.0034 239 LYS A CA 1214 C C . LYS A 153 ? 0.0711 0.0731 0.0810 0.0046 0.0000 0.0051 239 LYS A C 1215 O O . LYS A 153 ? 0.0997 0.1007 0.0959 0.0159 0.0069 -0.0003 239 LYS A O 1216 C CB . LYS A 153 ? 0.0924 0.0933 0.1046 0.0017 -0.0124 0.0084 239 LYS A CB 1217 C CG . LYS A 153 ? 0.1066 0.1015 0.1208 0.0134 -0.0125 -0.0007 239 LYS A CG 1218 C CD . LYS A 153 ? 0.1091 0.1368 0.1466 0.0021 -0.0062 0.0000 239 LYS A CD 1219 C CE . LYS A 153 ? 0.1348 0.1528 0.1725 0.0085 -0.0052 0.0025 239 LYS A CE 1220 N NZ . LYS A 153 ? 0.1522 0.1607 0.2215 -0.0094 -0.0109 0.0062 239 LYS A NZ 1221 N N . CYS A 154 ? 0.0663 0.0913 0.0892 0.0066 0.0050 -0.0012 240 CYS A N 1222 C CA . CYS A 154 ? 0.0768 0.0812 0.0763 -0.0001 -0.0036 0.0066 240 CYS A CA 1223 C C . CYS A 154 ? 0.0839 0.0828 0.0933 0.0018 0.0004 0.0099 240 CYS A C 1224 O O . CYS A 154 ? 0.0853 0.1083 0.0914 0.0146 -0.0017 0.0042 240 CYS A O 1225 C CB . CYS A 154 ? 0.0902 0.0873 0.0859 -0.0018 0.0060 0.0089 240 CYS A CB 1226 S SG . CYS A 154 ? 0.1201 0.1461 0.0993 -0.0156 0.0006 0.0080 240 CYS A SG 1227 N N . SER A 155 ? 0.0936 0.1026 0.0945 0.0084 -0.0034 0.0048 241 SER A N 1228 C CA . SER A 155 ? 0.1087 0.1130 0.1057 0.0082 -0.0038 0.0030 241 SER A CA 1229 C C . SER A 155 ? 0.1032 0.0941 0.0903 0.0056 -0.0001 0.0147 241 SER A C 1230 O O . SER A 155 ? 0.0916 0.1275 0.0966 0.0056 -0.0009 0.0121 241 SER A O 1231 C CB . SER A 155 ? 0.1507 0.1200 0.1266 0.0083 0.0059 0.0015 241 SER A CB 1232 O OG . SER A 155 ? 0.2511 0.1994 0.1940 -0.0186 -0.0047 0.0213 241 SER A OG 1233 N N . GLY A 156 ? 0.1124 0.1077 0.0834 0.0154 -0.0062 0.0124 242 GLY A N 1234 C CA . GLY A 156 ? 0.1070 0.0957 0.1001 0.0181 -0.0062 0.0055 242 GLY A CA 1235 C C . GLY A 156 ? 0.1100 0.1007 0.0978 0.0245 -0.0037 0.0005 242 GLY A C 1236 O O . GLY A 156 ? 0.1404 0.1348 0.1078 0.0316 0.0069 0.0109 242 GLY A O 1237 N N . ALA A 157 ? 0.0755 0.0813 0.0928 0.0176 -0.0001 0.0089 243 ALA A N 1238 C CA . ALA A 157 ? 0.0791 0.0787 0.0943 0.0056 -0.0060 0.0101 243 ALA A CA 1239 C C . ALA A 157 ? 0.0916 0.0907 0.0917 0.0055 -0.0064 0.0018 243 ALA A C 1240 O O . ALA A 157 ? 0.0827 0.1025 0.0904 0.0189 0.0064 0.0063 243 ALA A O 1241 C CB . ALA A 157 ? 0.0693 0.0992 0.1002 0.0060 0.0019 0.0031 243 ALA A CB 1242 N N . ALA A 158 ? 0.0871 0.0940 0.0979 0.0005 -0.0083 0.0091 244 ALA A N 1243 C CA . ALA A 158 ? 0.0763 0.0832 0.0805 0.0001 -0.0034 0.0058 244 ALA A CA 1244 C C . ALA A 158 ? 0.0806 0.0880 0.0838 -0.0013 -0.0041 0.0034 244 ALA A C 1245 O O . ALA A 158 ? 0.0829 0.0863 0.1061 0.0085 -0.0079 0.0161 244 ALA A O 1246 C CB . ALA A 158 ? 0.0786 0.0944 0.0935 -0.0004 0.0000 -0.0024 244 ALA A CB 1247 N N . SER A 159 ? 0.0819 0.0950 0.0925 0.0022 0.0004 0.0044 245 SER A N 1248 C CA . SER A 159 ? 0.0945 0.1045 0.0926 0.0003 0.0046 0.0051 245 SER A CA 1249 C C . SER A 159 ? 0.0900 0.0992 0.0960 0.0030 0.0039 -0.0014 245 SER A C 1250 O O . SER A 159 ? 0.0935 0.1082 0.1082 0.0063 0.0008 0.0015 245 SER A O 1251 C CB . SER A 159 ? 0.1146 0.1417 0.1045 -0.0016 0.0112 0.0013 245 SER A CB 1252 O OG . SER A 159 ? 0.1718 0.1900 0.1413 -0.0013 -0.0005 -0.0030 245 SER A OG 1253 N N . THR A 160 ? 0.0715 0.0826 0.0778 0.0106 0.0006 0.0025 246 THR A N 1254 C CA . THR A 160 ? 0.0737 0.0810 0.0828 -0.0049 0.0041 -0.0036 246 THR A CA 1255 C C . THR A 160 ? 0.0709 0.0864 0.0898 -0.0029 0.0049 0.0007 246 THR A C 1256 O O . THR A 160 ? 0.0839 0.0657 0.0970 0.0007 -0.0033 0.0053 246 THR A O 1257 C CB . THR A 160 ? 0.0763 0.0965 0.0901 -0.0003 0.0008 -0.0049 246 THR A CB 1258 O OG1 . THR A 160 ? 0.1092 0.1187 0.1015 -0.0094 -0.0081 -0.0101 246 THR A OG1 1259 C CG2 . THR A 160 ? 0.0976 0.1121 0.1207 0.0061 -0.0028 0.0045 246 THR A CG2 1260 N N . TYR A 161 ? 0.0810 0.0758 0.0917 0.0063 0.0043 -0.0013 247 TYR A N 1261 C CA . TYR A 161 ? 0.0726 0.0786 0.0833 -0.0001 0.0008 -0.0033 247 TYR A CA 1262 C C . TYR A 161 ? 0.0685 0.0718 0.0862 -0.0020 -0.0033 0.0083 247 TYR A C 1263 O O . TYR A 161 ? 0.0543 0.0890 0.0855 0.0014 -0.0019 0.0111 247 TYR A O 1264 C CB . TYR A 161 ? 0.0735 0.0870 0.0718 -0.0021 0.0062 -0.0062 247 TYR A CB 1265 C CG . TYR A 161 ? 0.0675 0.0636 0.0702 0.0052 -0.0118 0.0085 247 TYR A CG 1266 C CD1 . TYR A 161 ? 0.0720 0.0693 0.0797 0.0038 0.0015 0.0036 247 TYR A CD1 1267 C CD2 . TYR A 161 ? 0.0743 0.0896 0.0910 0.0059 -0.0043 0.0050 247 TYR A CD2 1268 C CE1 . TYR A 161 ? 0.0606 0.0738 0.0658 -0.0009 -0.0086 -0.0047 247 TYR A CE1 1269 C CE2 . TYR A 161 ? 0.0634 0.0729 0.0730 -0.0026 0.0058 -0.0020 247 TYR A CE2 1270 C CZ . TYR A 161 ? 0.0761 0.0721 0.0762 -0.0034 -0.0002 0.0049 247 TYR A CZ 1271 O OH . TYR A 161 ? 0.0633 0.0998 0.0781 0.0090 0.0128 -0.0105 247 TYR A OH 1272 N N . ARG A 162 ? 0.0684 0.0824 0.0872 0.0005 -0.0083 0.0116 248 ARG A N 1273 C CA . ARG A 162 ? 0.0816 0.0910 0.0946 -0.0021 -0.0052 0.0048 248 ARG A CA 1274 C C . ARG A 162 ? 0.0712 0.0705 0.0831 -0.0074 -0.0032 0.0063 248 ARG A C 1275 O O . ARG A 162 ? 0.0781 0.0933 0.1166 -0.0044 -0.0019 0.0153 248 ARG A O 1276 C CB A ARG A 162 ? 0.0843 0.0967 0.1007 -0.0040 0.0027 0.0079 248 ARG A CB 1277 C CB B ARG A 162 ? 0.0909 0.0953 0.1032 -0.0024 -0.0021 0.0053 248 ARG A CB 1278 C CG A ARG A 162 ? 0.0986 0.1099 0.1034 -0.0002 0.0013 0.0047 248 ARG A CG 1279 C CG B ARG A 162 ? 0.1053 0.1205 0.1346 -0.0025 -0.0001 0.0021 248 ARG A CG 1280 C CD A ARG A 162 ? 0.1601 0.1256 0.1407 0.0033 -0.0051 -0.0053 248 ARG A CD 1281 C CD B ARG A 162 ? 0.1402 0.1241 0.1466 0.0044 -0.0006 0.0004 248 ARG A CD 1282 N NE A ARG A 162 ? 0.1832 0.1738 0.1846 -0.0041 0.0162 -0.0022 248 ARG A NE 1283 N NE B ARG A 162 ? 0.1474 0.1145 0.1607 -0.0060 0.0140 0.0048 248 ARG A NE 1284 C CZ A ARG A 162 ? 0.2068 0.1932 0.2228 -0.0063 0.0047 -0.0076 248 ARG A CZ 1285 C CZ B ARG A 162 ? 0.1728 0.1571 0.1604 -0.0019 0.0069 -0.0019 248 ARG A CZ 1286 N NH1 A ARG A 162 ? 0.2144 0.2300 0.2204 0.0066 0.0077 -0.0028 248 ARG A NH1 1287 N NH1 B ARG A 162 ? 0.1905 0.1970 0.1878 -0.0056 -0.0065 0.0000 248 ARG A NH1 1288 N NH2 A ARG A 162 ? 0.2095 0.2319 0.2499 0.0044 0.0035 0.0019 248 ARG A NH2 1289 N NH2 B ARG A 162 ? 0.1703 0.1703 0.1673 -0.0051 -0.0019 0.0009 248 ARG A NH2 1290 N N . GLU A 163 ? 0.0815 0.0812 0.0951 -0.0078 0.0008 -0.0022 249 GLU A N 1291 C CA . GLU A 163 ? 0.0852 0.0881 0.0911 -0.0004 0.0040 0.0039 249 GLU A CA 1292 C C . GLU A 163 ? 0.0649 0.0675 0.0746 0.0008 0.0070 0.0061 249 GLU A C 1293 O O . GLU A 163 ? 0.0699 0.0777 0.0778 0.0094 0.0069 0.0070 249 GLU A O 1294 C CB A GLU A 163 ? 0.0963 0.0964 0.0961 0.0007 0.0012 0.0005 249 GLU A CB 1295 C CB B GLU A 163 ? 0.0999 0.1024 0.1015 -0.0017 0.0014 0.0051 249 GLU A CB 1296 C CG A GLU A 163 ? 0.1326 0.1153 0.1197 -0.0120 0.0100 0.0069 249 GLU A CG 1297 C CG B GLU A 163 ? 0.1460 0.1473 0.1408 0.0055 0.0044 -0.0057 249 GLU A CG 1298 C CD A GLU A 163 ? 0.2112 0.1980 0.1756 0.0013 -0.0163 0.0106 249 GLU A CD 1299 C CD B GLU A 163 ? 0.1909 0.2008 0.2017 -0.0012 -0.0067 -0.0122 249 GLU A CD 1300 O OE1 A GLU A 163 ? 0.2758 0.2560 0.2251 -0.0192 -0.0075 0.0074 249 GLU A OE1 1301 O OE1 B GLU A 163 ? 0.1809 0.2083 0.1941 -0.0020 -0.0045 0.0000 249 GLU A OE1 1302 O OE2 A GLU A 163 ? 0.2409 0.2353 0.2159 -0.0101 -0.0115 0.0300 249 GLU A OE2 1303 O OE2 B GLU A 163 ? 0.2477 0.2330 0.1994 0.0079 0.0122 -0.0117 249 GLU A OE2 1304 N N . LEU A 164 ? 0.0667 0.0756 0.0789 0.0126 0.0057 0.0109 250 LEU A N 1305 C CA . LEU A 164 ? 0.0733 0.0706 0.0742 0.0008 0.0010 -0.0004 250 LEU A CA 1306 C C . LEU A 164 ? 0.0749 0.0778 0.0770 -0.0024 -0.0044 0.0087 250 LEU A C 1307 O O . LEU A 164 ? 0.0876 0.0793 0.1062 0.0069 -0.0107 0.0084 250 LEU A O 1308 C CB . LEU A 164 ? 0.0602 0.0701 0.0739 0.0064 0.0078 0.0013 250 LEU A CB 1309 C CG . LEU A 164 ? 0.0815 0.0841 0.0944 -0.0084 0.0007 -0.0035 250 LEU A CG 1310 C CD1 . LEU A 164 ? 0.0855 0.0965 0.1134 -0.0067 0.0125 -0.0037 250 LEU A CD1 1311 C CD2 . LEU A 164 ? 0.1169 0.1207 0.1171 0.0097 0.0021 -0.0049 250 LEU A CD2 1312 N N . THR A 165 ? 0.0631 0.0717 0.0632 0.0058 0.0010 0.0094 251 THR A N 1313 C CA . THR A 165 ? 0.0771 0.0681 0.0674 0.0024 0.0037 0.0062 251 THR A CA 1314 C C . THR A 165 ? 0.0788 0.0796 0.0715 0.0009 0.0003 0.0063 251 THR A C 1315 O O . THR A 165 ? 0.0869 0.0784 0.0820 0.0086 0.0026 0.0111 251 THR A O 1316 C CB . THR A 165 ? 0.0923 0.0888 0.0849 0.0060 0.0086 -0.0006 251 THR A CB 1317 O OG1 . THR A 165 ? 0.1061 0.1177 0.1260 0.0097 0.0051 0.0110 251 THR A OG1 1318 C CG2 . THR A 165 ? 0.0942 0.0741 0.0924 0.0133 0.0014 0.0131 251 THR A CG2 1319 N N . ILE A 166 ? 0.0837 0.0710 0.0858 -0.0005 0.0040 0.0023 252 ILE A N 1320 C CA . ILE A 166 ? 0.0768 0.0800 0.0884 -0.0010 0.0008 0.0014 252 ILE A CA 1321 C C . ILE A 166 ? 0.0695 0.0833 0.0956 -0.0007 0.0011 -0.0010 252 ILE A C 1322 O O . ILE A 166 ? 0.0750 0.0701 0.0801 0.0025 -0.0016 -0.0050 252 ILE A O 1323 C CB . ILE A 166 ? 0.0719 0.0943 0.0959 -0.0027 0.0007 -0.0004 252 ILE A CB 1324 C CG1 . ILE A 166 ? 0.0987 0.1054 0.1063 0.0055 0.0075 0.0011 252 ILE A CG1 1325 C CG2 . ILE A 166 ? 0.0722 0.0950 0.0922 0.0095 0.0014 -0.0074 252 ILE A CG2 1326 C CD1 . ILE A 166 ? 0.1320 0.1121 0.1250 -0.0046 0.0073 -0.0014 252 ILE A CD1 1327 N N . TYR A 167 ? 0.0828 0.0787 0.1001 0.0070 0.0078 -0.0039 253 TYR A N 1328 C CA . TYR A 167 ? 0.0738 0.0843 0.0905 0.0001 0.0033 -0.0092 253 TYR A CA 1329 C C . TYR A 167 ? 0.0766 0.0762 0.0826 0.0041 0.0033 -0.0068 253 TYR A C 1330 O O . TYR A 167 ? 0.0909 0.0838 0.0922 0.0117 0.0061 0.0004 253 TYR A O 1331 C CB . TYR A 167 ? 0.0945 0.1005 0.0890 0.0036 -0.0072 -0.0084 253 TYR A CB 1332 C CG . TYR A 167 ? 0.0958 0.0902 0.0985 0.0072 -0.0062 0.0025 253 TYR A CG 1333 C CD1 . TYR A 167 ? 0.1772 0.1133 0.1347 -0.0087 0.0218 -0.0016 253 TYR A CD1 1334 C CD2 . TYR A 167 ? 0.0797 0.0941 0.0950 0.0002 -0.0028 0.0010 253 TYR A CD2 1335 C CE1 . TYR A 167 ? 0.1877 0.1324 0.1148 -0.0022 0.0248 -0.0074 253 TYR A CE1 1336 C CE2 . TYR A 167 ? 0.1030 0.1078 0.1242 0.0026 -0.0015 0.0008 253 TYR A CE2 1337 C CZ . TYR A 167 ? 0.1302 0.1089 0.1279 -0.0012 0.0107 -0.0143 253 TYR A CZ 1338 O OH . TYR A 167 ? 0.1585 0.1254 0.1258 -0.0078 0.0156 -0.0245 253 TYR A OH 1339 N N . ALA A 168 ? 0.0737 0.0766 0.0831 0.0002 0.0008 0.0033 254 ALA A N 1340 C CA . ALA A 168 ? 0.0914 0.0879 0.0916 -0.0063 0.0016 -0.0034 254 ALA A CA 1341 C C . ALA A 168 ? 0.0868 0.0807 0.0774 0.0062 -0.0016 0.0023 254 ALA A C 1342 O O . ALA A 168 ? 0.0974 0.0876 0.0880 0.0053 0.0075 -0.0021 254 ALA A O 1343 C CB . ALA A 168 ? 0.0754 0.0822 0.0964 -0.0030 -0.0049 0.0002 254 ALA A CB 1344 N N . LEU A 169 ? 0.0723 0.0791 0.0761 -0.0069 -0.0014 -0.0005 255 LEU A N 1345 C CA . LEU A 169 ? 0.0654 0.0797 0.0763 0.0007 0.0035 -0.0002 255 LEU A CA 1346 C C . LEU A 169 ? 0.0694 0.0762 0.0812 -0.0011 0.0033 -0.0023 255 LEU A C 1347 O O . LEU A 169 ? 0.0847 0.1099 0.0918 0.0096 0.0041 0.0085 255 LEU A O 1348 C CB . LEU A 169 ? 0.0653 0.0717 0.0616 -0.0042 0.0114 0.0004 255 LEU A CB 1349 C CG . LEU A 169 ? 0.0797 0.0970 0.1168 0.0035 0.0044 0.0015 255 LEU A CG 1350 C CD1 . LEU A 169 ? 0.1121 0.0939 0.1101 0.0006 0.0132 0.0000 255 LEU A CD1 1351 C CD2 . LEU A 169 ? 0.1082 0.0771 0.1088 0.0061 -0.0023 -0.0006 255 LEU A CD2 1352 N N . LYS A 170 ? 0.0644 0.0814 0.0866 -0.0015 0.0008 -0.0026 256 LYS A N 1353 C CA . LYS A 170 ? 0.0751 0.0837 0.0887 0.0009 0.0028 -0.0059 256 LYS A CA 1354 C C . LYS A 170 ? 0.0793 0.0846 0.0850 -0.0023 0.0050 -0.0024 256 LYS A C 1355 O O . LYS A 170 ? 0.0888 0.0987 0.0861 -0.0040 0.0006 -0.0043 256 LYS A O 1356 C CB . LYS A 170 ? 0.0806 0.0971 0.1035 -0.0078 0.0114 -0.0048 256 LYS A CB 1357 C CG . LYS A 170 ? 0.1268 0.1160 0.1390 0.0006 0.0076 -0.0017 256 LYS A CG 1358 C CD . LYS A 170 ? 0.2111 0.1742 0.1655 0.0040 0.0079 0.0132 256 LYS A CD 1359 C CE . LYS A 170 ? 0.2637 0.2440 0.2454 -0.0146 0.0019 0.0005 256 LYS A CE 1360 N NZ . LYS A 170 ? 0.3430 0.3196 0.2632 -0.0091 0.0249 -0.0009 256 LYS A NZ 1361 N N . GLN A 171 ? 0.0661 0.0761 0.0803 0.0018 -0.0020 -0.0069 257 GLN A N 1362 C CA . GLN A 171 ? 0.0726 0.0812 0.0782 0.0003 0.0005 -0.0006 257 GLN A CA 1363 C C . GLN A 171 ? 0.0712 0.0696 0.0796 -0.0001 0.0001 -0.0016 257 GLN A C 1364 O O . GLN A 171 ? 0.0993 0.0788 0.0810 -0.0017 0.0099 0.0028 257 GLN A O 1365 C CB A GLN A 171 ? 0.0786 0.0825 0.0870 -0.0023 0.0009 -0.0069 257 GLN A CB 1366 C CB B GLN A 171 ? 0.0794 0.0837 0.0884 -0.0022 0.0006 -0.0070 257 GLN A CB 1367 C CG A GLN A 171 ? 0.1114 0.1276 0.1112 0.0028 -0.0017 0.0007 257 GLN A CG 1368 C CG B GLN A 171 ? 0.1064 0.1318 0.1102 0.0011 -0.0022 0.0018 257 GLN A CG 1369 C CD A GLN A 171 ? 0.1307 0.1387 0.1275 0.0127 0.0037 -0.0022 257 GLN A CD 1370 C CD B GLN A 171 ? 0.1377 0.1537 0.1454 0.0082 -0.0004 -0.0116 257 GLN A CD 1371 O OE1 A GLN A 171 ? 0.1743 0.1456 0.1603 -0.0010 0.0215 -0.0246 257 GLN A OE1 1372 O OE1 B GLN A 171 ? 0.1368 0.1675 0.1295 -0.0048 0.0219 -0.0153 257 GLN A OE1 1373 N NE2 A GLN A 171 ? 0.1854 0.1663 0.1681 0.0068 0.0125 -0.0025 257 GLN A NE2 1374 N NE2 B GLN A 171 ? 0.1453 0.1820 0.1496 0.0010 -0.0045 -0.0204 257 GLN A NE2 1375 N N . LEU A 172 ? 0.0666 0.0606 0.0608 -0.0073 -0.0021 0.0031 258 LEU A N 1376 C CA . LEU A 172 ? 0.0628 0.0582 0.0584 0.0005 -0.0016 0.0008 258 LEU A CA 1377 C C . LEU A 172 ? 0.0612 0.0584 0.0686 -0.0007 -0.0010 -0.0015 258 LEU A C 1378 O O . LEU A 172 ? 0.0640 0.0635 0.0790 0.0106 0.0019 -0.0125 258 LEU A O 1379 C CB . LEU A 172 ? 0.0756 0.0800 0.0725 0.0024 -0.0026 -0.0014 258 LEU A CB 1380 C CG . LEU A 172 ? 0.0802 0.0781 0.0604 -0.0019 -0.0039 -0.0047 258 LEU A CG 1381 C CD1 . LEU A 172 ? 0.0860 0.1120 0.1019 0.0009 0.0050 -0.0019 258 LEU A CD1 1382 C CD2 . LEU A 172 ? 0.0870 0.0942 0.0895 -0.0066 -0.0013 -0.0110 258 LEU A CD2 1383 N N . ASP A 173 ? 0.0638 0.0727 0.0573 -0.0032 -0.0089 0.0040 259 ASP A N 1384 C CA . ASP A 173 ? 0.0696 0.0709 0.0869 0.0003 -0.0061 -0.0062 259 ASP A CA 1385 C C . ASP A 173 ? 0.0648 0.0734 0.0800 0.0002 -0.0023 -0.0027 259 ASP A C 1386 O O . ASP A 173 ? 0.0862 0.0789 0.0976 0.0043 0.0152 0.0085 259 ASP A O 1387 C CB . ASP A 173 ? 0.0643 0.0805 0.0763 -0.0046 -0.0009 -0.0050 259 ASP A CB 1388 C CG . ASP A 173 ? 0.0953 0.0799 0.0932 0.0004 -0.0028 -0.0007 259 ASP A CG 1389 O OD1 . ASP A 173 ? 0.0797 0.0951 0.0904 -0.0093 -0.0014 -0.0042 259 ASP A OD1 1390 O OD2 . ASP A 173 ? 0.0940 0.1067 0.1184 -0.0049 0.0074 0.0065 259 ASP A OD2 1391 N N . LEU A 174 ? 0.0611 0.0667 0.0788 0.0018 -0.0028 -0.0035 260 LEU A N 1392 C CA . LEU A 174 ? 0.0634 0.0673 0.0837 0.0019 -0.0019 -0.0020 260 LEU A CA 1393 C C . LEU A 174 ? 0.0694 0.0780 0.0683 0.0012 0.0030 -0.0043 260 LEU A C 1394 O O . LEU A 174 ? 0.0695 0.0693 0.0701 0.0036 -0.0062 -0.0104 260 LEU A O 1395 C CB . LEU A 174 ? 0.0769 0.0721 0.0850 -0.0016 0.0084 -0.0102 260 LEU A CB 1396 C CG . LEU A 174 ? 0.0819 0.0953 0.0850 -0.0046 0.0004 -0.0048 260 LEU A CG 1397 C CD1 . LEU A 174 ? 0.1027 0.1039 0.0860 0.0000 0.0065 -0.0059 260 LEU A CD1 1398 C CD2 . LEU A 174 ? 0.0916 0.1091 0.1041 0.0013 -0.0031 -0.0014 260 LEU A CD2 1399 N N . PRO A 175 ? 0.0728 0.0794 0.0744 0.0042 -0.0004 -0.0106 261 PRO A N 1400 C CA . PRO A 175 ? 0.0652 0.0745 0.0900 0.0074 -0.0065 -0.0013 261 PRO A CA 1401 C C . PRO A 175 ? 0.0741 0.0771 0.0899 0.0025 -0.0064 -0.0057 261 PRO A C 1402 O O . PRO A 175 ? 0.0830 0.1011 0.0903 0.0007 -0.0013 -0.0134 261 PRO A O 1403 C CB . PRO A 175 ? 0.0746 0.0861 0.1054 0.0115 -0.0016 -0.0053 261 PRO A CB 1404 C CG . PRO A 175 ? 0.0848 0.0844 0.1166 0.0150 0.0006 -0.0049 261 PRO A CG 1405 C CD . PRO A 175 ? 0.0831 0.0836 0.0875 0.0084 -0.0037 -0.0144 261 PRO A CD 1406 N N . HIS A 176 ? 0.0589 0.0651 0.0836 0.0014 -0.0130 -0.0045 262 HIS A N 1407 C CA . HIS A 176 ? 0.0595 0.0683 0.0865 0.0026 -0.0076 -0.0078 262 HIS A CA 1408 C C . HIS A 176 ? 0.0702 0.0758 0.0788 0.0021 -0.0027 -0.0055 262 HIS A C 1409 O O . HIS A 176 ? 0.0640 0.0697 0.0725 0.0205 -0.0040 0.0045 262 HIS A O 1410 C CB . HIS A 176 ? 0.0594 0.0750 0.0926 0.0055 -0.0060 0.0048 262 HIS A CB 1411 C CG . HIS A 176 ? 0.0813 0.0553 0.0751 0.0025 -0.0073 -0.0057 262 HIS A CG 1412 N ND1 . HIS A 176 ? 0.0615 0.0818 0.0818 0.0060 0.0001 0.0078 262 HIS A ND1 1413 C CD2 . HIS A 176 ? 0.0714 0.0666 0.0705 0.0018 0.0000 -0.0003 262 HIS A CD2 1414 C CE1 . HIS A 176 ? 0.0688 0.0867 0.0759 -0.0022 -0.0061 -0.0010 262 HIS A CE1 1415 N NE2 . HIS A 176 ? 0.0813 0.0655 0.0600 0.0019 0.0042 0.0048 262 HIS A NE2 1416 N N . VAL A 177 ? 0.0587 0.0669 0.0787 0.0078 0.0035 -0.0039 263 VAL A N 1417 C CA . VAL A 177 ? 0.0624 0.0560 0.0841 0.0039 -0.0030 -0.0036 263 VAL A CA 1418 C C . VAL A 177 ? 0.0657 0.0604 0.0856 0.0052 0.0016 -0.0040 263 VAL A C 1419 O O . VAL A 177 ? 0.0667 0.0714 0.0746 -0.0011 0.0047 0.0009 263 VAL A O 1420 C CB . VAL A 177 ? 0.0622 0.0633 0.0803 0.0025 0.0027 -0.0034 263 VAL A CB 1421 C CG1 . VAL A 177 ? 0.0657 0.0828 0.0729 0.0101 0.0017 -0.0054 263 VAL A CG1 1422 C CG2 . VAL A 177 ? 0.0685 0.0819 0.0709 0.0003 0.0013 0.0011 263 VAL A CG2 1423 N N . ALA A 178 ? 0.0694 0.0589 0.0598 -0.0003 0.0099 -0.0035 264 ALA A N 1424 C CA . ALA A 178 ? 0.0603 0.0571 0.0672 -0.0009 0.0036 0.0014 264 ALA A CA 1425 C C . ALA A 178 ? 0.0669 0.0586 0.0758 -0.0010 -0.0016 -0.0018 264 ALA A C 1426 O O . ALA A 178 ? 0.0554 0.0687 0.0899 0.0021 -0.0088 0.0204 264 ALA A O 1427 C CB . ALA A 178 ? 0.0776 0.0766 0.0912 0.0040 0.0041 -0.0047 264 ALA A CB 1428 N N . MET A 179 ? 0.0652 0.0646 0.0692 0.0017 0.0016 0.0055 265 MET A N 1429 C CA . MET A 179 ? 0.0525 0.0453 0.0543 -0.0044 -0.0008 0.0046 265 MET A CA 1430 C C . MET A 179 ? 0.0613 0.0642 0.0608 -0.0003 0.0023 -0.0014 265 MET A C 1431 O O . MET A 179 ? 0.0700 0.0582 0.0741 -0.0068 0.0007 0.0005 265 MET A O 1432 C CB . MET A 179 ? 0.0611 0.0558 0.0625 -0.0041 0.0019 -0.0021 265 MET A CB 1433 C CG . MET A 179 ? 0.0872 0.0590 0.0770 0.0031 -0.0015 0.0023 265 MET A CG 1434 S SD . MET A 179 ? 0.0712 0.0732 0.0685 0.0079 0.0004 -0.0037 265 MET A SD 1435 C CE . MET A 179 ? 0.0808 0.0756 0.0833 0.0015 0.0061 -0.0086 265 MET A CE 1436 N N . TYR A 180 ? 0.0443 0.0515 0.0464 -0.0014 0.0008 -0.0008 266 TYR A N 1437 C CA . TYR A 180 ? 0.0520 0.0576 0.0669 -0.0036 -0.0040 -0.0066 266 TYR A CA 1438 C C . TYR A 180 ? 0.0539 0.0520 0.0615 0.0005 -0.0017 0.0025 266 TYR A C 1439 O O . TYR A 180 ? 0.0590 0.0556 0.0754 -0.0006 -0.0143 0.0001 266 TYR A O 1440 C CB . TYR A 180 ? 0.0645 0.0663 0.0695 -0.0125 -0.0058 0.0044 266 TYR A CB 1441 C CG . TYR A 180 ? 0.0514 0.0664 0.0731 0.0069 0.0047 -0.0055 266 TYR A CG 1442 C CD1 . TYR A 180 ? 0.0507 0.0548 0.0598 -0.0009 0.0051 0.0058 266 TYR A CD1 1443 C CD2 . TYR A 180 ? 0.0653 0.0669 0.0694 0.0029 0.0022 0.0005 266 TYR A CD2 1444 C CE1 . TYR A 180 ? 0.0667 0.0509 0.0688 -0.0007 0.0010 -0.0070 266 TYR A CE1 1445 C CE2 . TYR A 180 ? 0.0430 0.0551 0.0498 -0.0047 -0.0009 -0.0104 266 TYR A CE2 1446 C CZ . TYR A 180 ? 0.0472 0.0618 0.0638 -0.0012 -0.0028 -0.0028 266 TYR A CZ 1447 O OH . TYR A 180 ? 0.0652 0.0805 0.0764 -0.0069 -0.0124 0.0063 266 TYR A OH 1448 N N . MET A 181 ? 0.0408 0.0435 0.0579 0.0055 0.0005 0.0063 267 MET A N 1449 C CA . MET A 181 ? 0.0479 0.0500 0.0534 0.0017 -0.0027 0.0010 267 MET A CA 1450 C C . MET A 181 ? 0.0494 0.0474 0.0442 0.0007 -0.0016 0.0038 267 MET A C 1451 O O . MET A 181 ? 0.0466 0.0533 0.0624 0.0006 -0.0001 -0.0025 267 MET A O 1452 C CB . MET A 181 ? 0.0635 0.0570 0.0547 -0.0012 -0.0072 -0.0028 267 MET A CB 1453 C CG . MET A 181 ? 0.0658 0.0672 0.0694 0.0039 -0.0037 0.0051 267 MET A CG 1454 S SD . MET A 181 ? 0.0845 0.0858 0.0673 -0.0072 0.0065 0.0070 267 MET A SD 1455 C CE . MET A 181 ? 0.0844 0.1087 0.0948 -0.0054 -0.0100 0.0127 267 MET A CE 1456 N N . ASP A 182 ? 0.0454 0.0577 0.0538 0.0082 0.0041 -0.0060 268 ASP A N 1457 C CA . ASP A 182 ? 0.0529 0.0564 0.0593 0.0074 0.0051 -0.0079 268 ASP A CA 1458 C C . ASP A 182 ? 0.0636 0.0609 0.0619 0.0024 -0.0003 -0.0024 268 ASP A C 1459 O O . ASP A 182 ? 0.0720 0.0586 0.0655 -0.0008 0.0034 -0.0100 268 ASP A O 1460 C CB . ASP A 182 ? 0.0639 0.0547 0.0565 0.0054 0.0001 -0.0162 268 ASP A CB 1461 C CG . ASP A 182 ? 0.0660 0.0700 0.0748 -0.0055 -0.0050 -0.0070 268 ASP A CG 1462 O OD1 . ASP A 182 ? 0.1072 0.0830 0.0752 -0.0049 0.0041 -0.0155 268 ASP A OD1 1463 O OD2 . ASP A 182 ? 0.0779 0.0703 0.0719 0.0050 -0.0099 -0.0072 268 ASP A OD2 1464 N N . ALA A 183 ? 0.0630 0.0467 0.0615 0.0037 0.0056 -0.0039 269 ALA A N 1465 C CA . ALA A 183 ? 0.0517 0.0393 0.0485 0.0038 -0.0022 0.0053 269 ALA A CA 1466 C C . ALA A 183 ? 0.0596 0.0674 0.0609 -0.0042 0.0042 -0.0002 269 ALA A C 1467 O O . ALA A 183 ? 0.0719 0.0590 0.0780 0.0061 -0.0006 0.0000 269 ALA A O 1468 C CB . ALA A 183 ? 0.0580 0.0573 0.0766 0.0090 0.0030 -0.0046 269 ALA A CB 1469 N N . GLY A 184 ? 0.0684 0.0458 0.0509 0.0046 -0.0017 0.0005 270 GLY A N 1470 C CA . GLY A 184 ? 0.0631 0.0674 0.0647 0.0043 0.0022 0.0078 270 GLY A CA 1471 C C . GLY A 184 ? 0.0663 0.0640 0.0614 0.0062 -0.0035 -0.0005 270 GLY A C 1472 O O . GLY A 184 ? 0.0736 0.0704 0.0792 0.0086 0.0120 0.0059 270 GLY A O 1473 N N . HIS A 185 ? 0.0667 0.0596 0.0569 0.0139 -0.0033 0.0063 271 HIS A N 1474 C CA . HIS A 185 ? 0.0613 0.0574 0.0610 0.0069 -0.0001 0.0040 271 HIS A CA 1475 C C . HIS A 185 ? 0.0642 0.0591 0.0634 0.0101 0.0028 0.0044 271 HIS A C 1476 O O . HIS A 185 ? 0.0729 0.0620 0.0550 0.0064 0.0100 0.0103 271 HIS A O 1477 C CB . HIS A 185 ? 0.0639 0.0559 0.0540 0.0062 -0.0045 0.0008 271 HIS A CB 1478 C CG . HIS A 185 ? 0.0707 0.0710 0.0766 0.0003 0.0059 0.0045 271 HIS A CG 1479 N ND1 . HIS A 185 ? 0.0750 0.0934 0.0576 0.0097 0.0056 0.0001 271 HIS A ND1 1480 C CD2 . HIS A 185 ? 0.0731 0.0645 0.0768 -0.0075 0.0089 -0.0049 271 HIS A CD2 1481 C CE1 . HIS A 185 ? 0.0747 0.0852 0.0851 0.0090 0.0107 -0.0007 271 HIS A CE1 1482 N NE2 . HIS A 185 ? 0.0923 0.0994 0.0928 0.0093 0.0106 0.0000 271 HIS A NE2 1483 N N . ALA A 186 ? 0.0671 0.0646 0.0669 0.0000 0.0067 0.0068 272 ALA A N 1484 C CA . ALA A 186 ? 0.0707 0.0716 0.0628 0.0008 -0.0059 -0.0060 272 ALA A CA 1485 C C . ALA A 186 ? 0.0708 0.0678 0.0698 0.0002 0.0062 0.0020 272 ALA A C 1486 O O . ALA A 186 ? 0.0725 0.0651 0.0909 -0.0021 -0.0010 0.0019 272 ALA A O 1487 C CB . ALA A 186 ? 0.0898 0.0759 0.0563 -0.0019 0.0089 0.0044 272 ALA A CB 1488 N N . GLY A 187 ? 0.0640 0.0715 0.0754 0.0015 -0.0043 0.0063 273 GLY A N 1489 C CA . GLY A 187 ? 0.0552 0.0577 0.0756 -0.0006 0.0030 -0.0001 273 GLY A CA 1490 C C . GLY A 187 ? 0.0616 0.0607 0.0765 0.0002 0.0030 -0.0040 273 GLY A C 1491 O O . GLY A 187 ? 0.0842 0.0874 0.0829 0.0131 -0.0124 -0.0066 273 GLY A O 1492 N N . TRP A 188 ? 0.0584 0.0663 0.0645 0.0073 0.0037 0.0021 274 TRP A N 1493 C CA . TRP A 188 ? 0.0581 0.0627 0.0681 0.0051 0.0026 0.0018 274 TRP A CA 1494 C C . TRP A 188 ? 0.0721 0.0639 0.0801 0.0000 0.0076 0.0009 274 TRP A C 1495 O O . TRP A 188 ? 0.0903 0.0769 0.1043 0.0141 0.0202 0.0067 274 TRP A O 1496 C CB . TRP A 188 ? 0.0682 0.0779 0.0642 -0.0046 0.0127 0.0015 274 TRP A CB 1497 C CG . TRP A 188 ? 0.0575 0.0760 0.0576 -0.0030 -0.0016 0.0013 274 TRP A CG 1498 C CD1 . TRP A 188 ? 0.0752 0.0774 0.0962 0.0016 -0.0016 0.0011 274 TRP A CD1 1499 C CD2 . TRP A 188 ? 0.0727 0.0882 0.0903 -0.0023 0.0105 -0.0016 274 TRP A CD2 1500 N NE1 . TRP A 188 ? 0.1013 0.0805 0.0914 0.0058 -0.0004 0.0121 274 TRP A NE1 1501 C CE2 . TRP A 188 ? 0.0920 0.0829 0.0978 0.0167 -0.0031 -0.0066 274 TRP A CE2 1502 C CE3 . TRP A 188 ? 0.0841 0.0784 0.0631 -0.0051 0.0036 0.0063 274 TRP A CE3 1503 C CZ2 . TRP A 188 ? 0.0804 0.0968 0.0842 0.0149 0.0028 -0.0027 274 TRP A CZ2 1504 C CZ3 . TRP A 188 ? 0.0934 0.0782 0.0873 0.0087 -0.0009 0.0012 274 TRP A CZ3 1505 C CH2 . TRP A 188 ? 0.1147 0.0993 0.0922 0.0022 0.0051 -0.0067 274 TRP A CH2 1506 N N . LEU A 189 ? 0.0696 0.0539 0.0736 -0.0010 0.0100 0.0107 275 LEU A N 1507 C CA . LEU A 189 ? 0.0744 0.0680 0.0744 -0.0056 -0.0014 0.0015 275 LEU A CA 1508 C C . LEU A 189 ? 0.0835 0.0889 0.0853 -0.0047 0.0045 -0.0069 275 LEU A C 1509 O O . LEU A 189 ? 0.1008 0.0635 0.0875 -0.0085 0.0063 0.0010 275 LEU A O 1510 C CB . LEU A 189 ? 0.0649 0.0749 0.0755 -0.0031 0.0050 0.0007 275 LEU A CB 1511 C CG . LEU A 189 ? 0.0705 0.0751 0.0967 -0.0011 -0.0029 -0.0054 275 LEU A CG 1512 C CD1 . LEU A 189 ? 0.0559 0.0919 0.0691 0.0017 0.0013 -0.0083 275 LEU A CD1 1513 C CD2 . LEU A 189 ? 0.0765 0.0830 0.0910 -0.0021 -0.0003 -0.0048 275 LEU A CD2 1514 N N . GLY A 190 ? 0.0869 0.0795 0.0767 -0.0048 -0.0003 0.0042 276 GLY A N 1515 C CA . GLY A 190 ? 0.0785 0.0868 0.0808 0.0027 0.0018 -0.0024 276 GLY A CA 1516 C C . GLY A 190 ? 0.0956 0.0908 0.0968 0.0008 -0.0071 0.0028 276 GLY A C 1517 O O . GLY A 190 ? 0.1010 0.0885 0.1190 0.0128 -0.0125 -0.0160 276 GLY A O 1518 N N . TRP A 191 ? 0.0849 0.0901 0.1114 0.0029 0.0025 0.0009 277 TRP A N 1519 C CA . TRP A 191 ? 0.0977 0.0775 0.0822 -0.0011 0.0042 -0.0013 277 TRP A CA 1520 C C . TRP A 191 ? 0.0927 0.0906 0.0893 -0.0015 0.0075 -0.0033 277 TRP A C 1521 O O . TRP A 191 ? 0.0896 0.0775 0.0910 0.0126 0.0148 -0.0089 277 TRP A O 1522 C CB . TRP A 191 ? 0.0976 0.0728 0.1004 0.0045 0.0053 0.0034 277 TRP A CB 1523 C CG . TRP A 191 ? 0.0755 0.0636 0.0901 0.0155 0.0046 0.0052 277 TRP A CG 1524 C CD1 . TRP A 191 ? 0.1027 0.1008 0.1126 0.0095 -0.0005 -0.0129 277 TRP A CD1 1525 C CD2 . TRP A 191 ? 0.0836 0.0897 0.1075 0.0051 0.0042 -0.0071 277 TRP A CD2 1526 N NE1 . TRP A 191 ? 0.1035 0.0794 0.0984 -0.0048 0.0063 0.0053 277 TRP A NE1 1527 C CE2 . TRP A 191 ? 0.1032 0.0909 0.1123 0.0137 0.0042 0.0076 277 TRP A CE2 1528 C CE3 . TRP A 191 ? 0.1385 0.0994 0.1182 0.0008 0.0081 0.0038 277 TRP A CE3 1529 C CZ2 . TRP A 191 ? 0.1230 0.1203 0.1275 -0.0025 0.0076 -0.0051 277 TRP A CZ2 1530 C CZ3 . TRP A 191 ? 0.1323 0.1149 0.1569 0.0110 0.0093 -0.0052 277 TRP A CZ3 1531 C CH2 . TRP A 191 ? 0.1283 0.1203 0.1480 0.0156 0.0141 -0.0065 277 TRP A CH2 1532 N N . PRO A 192 ? 0.1123 0.0903 0.0943 -0.0128 0.0151 -0.0043 278 PRO A N 1533 C CA . PRO A 192 ? 0.1234 0.1174 0.1289 -0.0085 0.0125 -0.0116 278 PRO A CA 1534 C C . PRO A 192 ? 0.1267 0.1100 0.1346 -0.0109 0.0111 -0.0105 278 PRO A C 1535 O O . PRO A 192 ? 0.1556 0.1430 0.1568 -0.0235 0.0292 -0.0267 278 PRO A O 1536 C CB . PRO A 192 ? 0.1556 0.1299 0.1415 -0.0153 0.0137 -0.0150 278 PRO A CB 1537 C CG . PRO A 192 ? 0.1383 0.1197 0.1286 -0.0043 0.0047 -0.0074 278 PRO A CG 1538 C CD . PRO A 192 ? 0.1184 0.0906 0.1147 0.0051 0.0146 -0.0031 278 PRO A CD 1539 N N . ALA A 193 ? 0.1440 0.1154 0.1213 -0.0096 0.0107 -0.0065 279 ALA A N 1540 C CA . ALA A 193 ? 0.1454 0.1358 0.1330 -0.0008 0.0048 -0.0057 279 ALA A CA 1541 C C . ALA A 193 ? 0.1547 0.1133 0.1311 0.0014 0.0118 0.0002 279 ALA A C 1542 O O . ALA A 193 ? 0.1809 0.1182 0.1456 -0.0015 0.0257 0.0009 279 ALA A O 1543 C CB . ALA A 193 ? 0.1619 0.1556 0.1464 0.0081 0.0032 0.0029 279 ALA A CB 1544 N N . ASN A 194 ? 0.1132 0.0998 0.1021 -0.0018 0.0164 0.0027 280 ASN A N 1545 C CA . ASN A 194 ? 0.1040 0.0966 0.0966 -0.0024 0.0072 -0.0021 280 ASN A CA 1546 C C . ASN A 194 ? 0.1060 0.0933 0.0971 -0.0051 0.0052 0.0027 280 ASN A C 1547 O O . ASN A 194 ? 0.1118 0.1017 0.1010 -0.0035 0.0118 -0.0159 280 ASN A O 1548 C CB . ASN A 194 ? 0.1093 0.0723 0.0778 0.0016 0.0125 0.0070 280 ASN A CB 1549 C CG . ASN A 194 ? 0.0983 0.0924 0.1102 -0.0089 0.0153 0.0078 280 ASN A CG 1550 O OD1 . ASN A 194 ? 0.1520 0.1273 0.1152 -0.0035 -0.0077 0.0296 280 ASN A OD1 1551 N ND2 . ASN A 194 ? 0.1006 0.0729 0.0821 -0.0119 0.0246 0.0008 280 ASN A ND2 1552 N N . ILE A 195 ? 0.1082 0.0872 0.0968 -0.0089 0.0038 -0.0002 281 ILE A N 1553 C CA . ILE A 195 ? 0.1113 0.0913 0.1011 -0.0014 0.0011 -0.0018 281 ILE A CA 1554 C C . ILE A 195 ? 0.1052 0.0920 0.1072 -0.0020 -0.0022 -0.0079 281 ILE A C 1555 O O . ILE A 195 ? 0.0928 0.0784 0.0969 0.0027 -0.0052 -0.0052 281 ILE A O 1556 C CB . ILE A 195 ? 0.1223 0.1007 0.1204 0.0035 -0.0016 -0.0025 281 ILE A CB 1557 C CG1 . ILE A 195 ? 0.1543 0.1271 0.1312 0.0058 -0.0163 0.0004 281 ILE A CG1 1558 C CG2 . ILE A 195 ? 0.1463 0.1269 0.1483 -0.0083 -0.0040 -0.0077 281 ILE A CG2 1559 C CD1 . ILE A 195 ? 0.1592 0.1514 0.1207 -0.0022 0.0103 0.0050 281 ILE A CD1 1560 N N . GLN A 196 ? 0.1203 0.1032 0.1049 -0.0012 0.0118 0.0040 282 GLN A N 1561 C CA . GLN A 196 ? 0.1192 0.1075 0.1190 -0.0038 0.0046 0.0012 282 GLN A CA 1562 C C . GLN A 196 ? 0.1105 0.0928 0.0986 -0.0023 0.0081 0.0089 282 GLN A C 1563 O O . GLN A 196 ? 0.1029 0.1007 0.0969 -0.0050 0.0086 0.0025 282 GLN A O 1564 C CB . GLN A 196 ? 0.1489 0.1165 0.1367 -0.0120 0.0084 0.0041 282 GLN A CB 1565 C CG . GLN A 196 ? 0.1688 0.1762 0.1749 0.0001 0.0077 -0.0021 282 GLN A CG 1566 C CD . GLN A 196 ? 0.2923 0.2471 0.2875 -0.0125 0.0084 0.0068 282 GLN A CD 1567 O OE1 . GLN A 196 ? 0.3805 0.3166 0.3379 -0.0348 0.0011 -0.0094 282 GLN A OE1 1568 N NE2 . GLN A 196 ? 0.3214 0.3042 0.3160 -0.0048 0.0077 0.0214 282 GLN A NE2 1569 N N . PRO A 197 ? 0.1090 0.0942 0.1064 0.0088 0.0137 -0.0004 283 PRO A N 1570 C CA . PRO A 197 ? 0.0985 0.0904 0.1034 0.0003 0.0047 0.0027 283 PRO A CA 1571 C C . PRO A 197 ? 0.0895 0.0800 0.0823 0.0009 0.0033 0.0011 283 PRO A C 1572 O O . PRO A 197 ? 0.1032 0.0787 0.0975 0.0002 0.0175 -0.0025 283 PRO A O 1573 C CB . PRO A 197 ? 0.1202 0.1004 0.1258 -0.0057 -0.0075 0.0096 283 PRO A CB 1574 C CG . PRO A 197 ? 0.1168 0.1274 0.1271 0.0109 0.0115 -0.0062 283 PRO A CG 1575 C CD . PRO A 197 ? 0.1036 0.1047 0.1300 0.0072 0.0084 0.0003 283 PRO A CD 1576 N N . ALA A 198 ? 0.0831 0.0726 0.0768 0.0057 0.0106 -0.0006 284 ALA A N 1577 C CA . ALA A 198 ? 0.0726 0.0709 0.0723 -0.0047 0.0015 -0.0008 284 ALA A CA 1578 C C . ALA A 198 ? 0.0736 0.0735 0.0624 -0.0013 0.0006 0.0001 284 ALA A C 1579 O O . ALA A 198 ? 0.0823 0.0708 0.0822 -0.0040 0.0083 -0.0003 284 ALA A O 1580 C CB . ALA A 198 ? 0.0685 0.0836 0.0858 -0.0077 0.0022 0.0069 284 ALA A CB 1581 N N . ALA A 199 ? 0.0686 0.0713 0.0731 -0.0016 0.0031 0.0051 285 ALA A N 1582 C CA . ALA A 199 ? 0.0585 0.0658 0.0707 0.0048 -0.0025 -0.0088 285 ALA A CA 1583 C C . ALA A 199 ? 0.0745 0.0868 0.0820 0.0023 -0.0034 0.0042 285 ALA A C 1584 O O . ALA A 199 ? 0.0783 0.0785 0.0957 -0.0058 0.0028 0.0005 285 ALA A O 1585 C CB . ALA A 199 ? 0.0672 0.0857 0.0817 -0.0065 -0.0031 -0.0064 285 ALA A CB 1586 N N . GLU A 200 ? 0.0708 0.0751 0.0868 0.0044 0.0071 -0.0057 286 GLU A N 1587 C CA . GLU A 200 ? 0.0841 0.0862 0.0864 0.0008 -0.0023 0.0033 286 GLU A CA 1588 C C . GLU A 200 ? 0.0670 0.0858 0.0755 0.0004 0.0041 0.0008 286 GLU A C 1589 O O . GLU A 200 ? 0.0853 0.0784 0.0936 0.0001 -0.0002 -0.0014 286 GLU A O 1590 C CB A GLU A 200 ? 0.0821 0.0805 0.0851 -0.0019 0.0024 -0.0002 286 GLU A CB 1591 C CB B GLU A 200 ? 0.0864 0.0906 0.0851 0.0000 0.0040 0.0033 286 GLU A CB 1592 C CG A GLU A 200 ? 0.1195 0.1258 0.1087 0.0000 0.0102 0.0037 286 GLU A CG 1593 C CG B GLU A 200 ? 0.1260 0.1268 0.1242 -0.0024 -0.0075 -0.0077 286 GLU A CG 1594 C CD A GLU A 200 ? 0.1646 0.1496 0.1650 0.0079 0.0026 0.0071 286 GLU A CD 1595 C CD B GLU A 200 ? 0.1947 0.1709 0.1783 -0.0066 0.0004 0.0086 286 GLU A CD 1596 O OE1 A GLU A 200 ? 0.1592 0.1859 0.1642 -0.0137 0.0011 -0.0023 286 GLU A OE1 1597 O OE1 B GLU A 200 ? 0.2374 0.2223 0.2022 -0.0022 -0.0025 0.0002 286 GLU A OE1 1598 O OE2 A GLU A 200 ? 0.1925 0.1946 0.1834 -0.0114 -0.0215 -0.0055 286 GLU A OE2 1599 O OE2 B GLU A 200 ? 0.2120 0.1854 0.2234 -0.0070 -0.0099 -0.0006 286 GLU A OE2 1600 N N . LEU A 201 ? 0.0802 0.0788 0.0801 -0.0092 0.0042 -0.0064 287 LEU A N 1601 C CA . LEU A 201 ? 0.0832 0.0756 0.0762 -0.0074 0.0096 0.0003 287 LEU A CA 1602 C C . LEU A 201 ? 0.0764 0.0895 0.0690 0.0053 0.0056 0.0002 287 LEU A C 1603 O O . LEU A 201 ? 0.0843 0.0712 0.0736 0.0078 0.0025 -0.0111 287 LEU A O 1604 C CB A LEU A 201 ? 0.0712 0.0707 0.0902 0.0059 0.0041 0.0021 287 LEU A CB 1605 C CB B LEU A 201 ? 0.0774 0.0765 0.0863 0.0024 0.0030 0.0016 287 LEU A CB 1606 C CG A LEU A 201 ? 0.0842 0.0916 0.0942 0.0018 0.0007 -0.0008 287 LEU A CG 1607 C CG B LEU A 201 ? 0.0925 0.0923 0.0842 -0.0011 0.0013 0.0013 287 LEU A CG 1608 C CD1 A LEU A 201 ? 0.1008 0.1038 0.1143 -0.0036 -0.0021 -0.0075 287 LEU A CD1 1609 C CD1 B LEU A 201 ? 0.1060 0.1160 0.1164 0.0032 -0.0034 -0.0042 287 LEU A CD1 1610 C CD2 A LEU A 201 ? 0.0937 0.0984 0.1074 -0.0043 0.0063 0.0137 287 LEU A CD2 1611 C CD2 B LEU A 201 ? 0.1049 0.0962 0.1094 -0.0035 0.0020 0.0047 287 LEU A CD2 1612 N N . PHE A 202 ? 0.0816 0.0728 0.0690 0.0015 0.0056 -0.0014 288 PHE A N 1613 C CA . PHE A 202 ? 0.0663 0.0748 0.0745 0.0025 -0.0004 0.0000 288 PHE A CA 1614 C C . PHE A 202 ? 0.0701 0.0711 0.0785 -0.0039 0.0043 -0.0008 288 PHE A C 1615 O O . PHE A 202 ? 0.0584 0.0669 0.0741 -0.0029 0.0118 0.0040 288 PHE A O 1616 C CB . PHE A 202 ? 0.0648 0.0708 0.0838 -0.0061 0.0067 0.0008 288 PHE A CB 1617 C CG . PHE A 202 ? 0.0684 0.0711 0.0648 -0.0106 0.0180 0.0022 288 PHE A CG 1618 C CD1 . PHE A 202 ? 0.0852 0.0847 0.0956 -0.0036 0.0069 -0.0009 288 PHE A CD1 1619 C CD2 . PHE A 202 ? 0.0960 0.0759 0.1083 -0.0107 0.0060 0.0095 288 PHE A CD2 1620 C CE1 . PHE A 202 ? 0.0889 0.0762 0.0977 -0.0116 0.0066 -0.0032 288 PHE A CE1 1621 C CE2 . PHE A 202 ? 0.0875 0.1001 0.1113 0.0028 0.0097 -0.0016 288 PHE A CE2 1622 C CZ . PHE A 202 ? 0.0823 0.0921 0.1018 -0.0075 0.0092 0.0059 288 PHE A CZ 1623 N N . ALA A 203 ? 0.0733 0.0689 0.0784 0.0033 0.0082 0.0004 289 ALA A N 1624 C CA . ALA A 203 ? 0.0715 0.0778 0.0893 -0.0029 0.0054 0.0045 289 ALA A CA 1625 C C . ALA A 203 ? 0.0739 0.0702 0.0867 -0.0025 -0.0026 -0.0048 289 ALA A C 1626 O O . ALA A 203 ? 0.0548 0.0757 0.0909 0.0028 0.0107 -0.0040 289 ALA A O 1627 C CB . ALA A 203 ? 0.0892 0.0960 0.0871 0.0034 0.0053 -0.0096 289 ALA A CB 1628 N N . LYS A 204 ? 0.0754 0.0891 0.0969 -0.0037 0.0045 0.0057 290 LYS A N 1629 C CA . LYS A 204 ? 0.0930 0.0901 0.1022 0.0015 0.0072 0.0029 290 LYS A CA 1630 C C . LYS A 204 ? 0.0931 0.0861 0.0803 -0.0014 0.0033 -0.0007 290 LYS A C 1631 O O . LYS A 204 ? 0.0819 0.0840 0.0890 0.0048 0.0096 0.0137 290 LYS A O 1632 C CB . LYS A 204 ? 0.1135 0.1142 0.1248 0.0065 -0.0021 0.0075 290 LYS A CB 1633 C CG . LYS A 204 ? 0.1852 0.1729 0.1676 0.0101 -0.0103 0.0078 290 LYS A CG 1634 C CD . LYS A 204 ? 0.2388 0.2589 0.2498 -0.0080 0.0003 0.0012 290 LYS A CD 1635 C CE . LYS A 204 ? 0.3110 0.3168 0.2760 -0.0094 0.0021 0.0090 290 LYS A CE 1636 N NZ . LYS A 204 ? 0.3257 0.3236 0.3254 -0.0071 -0.0080 -0.0035 290 LYS A NZ 1637 N N . ILE A 205 ? 0.0678 0.0727 0.0762 -0.0040 0.0051 -0.0010 291 ILE A N 1638 C CA . ILE A 205 ? 0.0753 0.0749 0.0817 0.0025 0.0080 -0.0050 291 ILE A CA 1639 C C . ILE A 205 ? 0.0757 0.0725 0.0831 0.0014 -0.0006 0.0016 291 ILE A C 1640 O O . ILE A 205 ? 0.0729 0.0625 0.0696 -0.0029 0.0015 -0.0072 291 ILE A O 1641 C CB . ILE A 205 ? 0.0848 0.0760 0.0947 -0.0123 0.0068 -0.0024 291 ILE A CB 1642 C CG1 . ILE A 205 ? 0.0963 0.0984 0.1173 -0.0095 0.0102 -0.0125 291 ILE A CG1 1643 C CG2 . ILE A 205 ? 0.1114 0.0996 0.1291 -0.0004 0.0105 -0.0077 291 ILE A CG2 1644 C CD1 . ILE A 205 ? 0.1423 0.1525 0.1480 0.0096 -0.0088 -0.0050 291 ILE A CD1 1645 N N . TYR A 206 ? 0.0685 0.0594 0.0846 -0.0001 0.0039 -0.0058 292 TYR A N 1646 C CA . TYR A 206 ? 0.0715 0.0633 0.0762 -0.0013 -0.0005 -0.0056 292 TYR A CA 1647 C C . TYR A 206 ? 0.0753 0.0726 0.0790 0.0057 0.0057 -0.0031 292 TYR A C 1648 O O . TYR A 206 ? 0.0679 0.0646 0.0888 0.0074 0.0008 -0.0119 292 TYR A O 1649 C CB . TYR A 206 ? 0.0677 0.0747 0.0746 0.0032 0.0008 -0.0041 292 TYR A CB 1650 C CG . TYR A 206 ? 0.0743 0.0779 0.0783 0.0022 0.0007 0.0013 292 TYR A CG 1651 C CD1 . TYR A 206 ? 0.0827 0.0720 0.0997 -0.0025 -0.0079 -0.0057 292 TYR A CD1 1652 C CD2 . TYR A 206 ? 0.0802 0.0780 0.0834 -0.0082 0.0057 -0.0075 292 TYR A CD2 1653 C CE1 . TYR A 206 ? 0.0779 0.0720 0.0956 -0.0050 -0.0012 -0.0036 292 TYR A CE1 1654 C CE2 . TYR A 206 ? 0.0686 0.0806 0.0885 -0.0049 0.0055 0.0009 292 TYR A CE2 1655 C CZ . TYR A 206 ? 0.0758 0.0872 0.0993 -0.0087 -0.0021 0.0043 292 TYR A CZ 1656 O OH . TYR A 206 ? 0.0855 0.0776 0.0928 -0.0049 0.0105 -0.0030 292 TYR A OH 1657 N N . GLU A 207 ? 0.0850 0.0821 0.0815 -0.0047 0.0026 -0.0097 293 GLU A N 1658 C CA . GLU A 207 ? 0.1001 0.1033 0.1143 0.0003 0.0067 -0.0020 293 GLU A CA 1659 C C . GLU A 207 ? 0.0987 0.0969 0.1099 -0.0064 0.0086 0.0015 293 GLU A C 1660 O O . GLU A 207 ? 0.1079 0.1022 0.1257 -0.0102 0.0106 -0.0104 293 GLU A O 1661 C CB . GLU A 207 ? 0.1176 0.1216 0.1310 0.0033 0.0127 -0.0034 293 GLU A CB 1662 C CG . GLU A 207 ? 0.1402 0.1656 0.1653 -0.0065 0.0128 -0.0057 293 GLU A CG 1663 C CD . GLU A 207 ? 0.1480 0.1377 0.1447 0.0022 0.0107 0.0086 293 GLU A CD 1664 O OE1 . GLU A 207 ? 0.1783 0.1673 0.1937 -0.0366 -0.0287 -0.0118 293 GLU A OE1 1665 O OE2 . GLU A 207 ? 0.1698 0.1858 0.1875 -0.0012 -0.0091 0.0038 293 GLU A OE2 1666 N N . ASP A 208 ? 0.1034 0.1006 0.1124 -0.0009 0.0079 -0.0027 294 ASP A N 1667 C CA . ASP A 208 ? 0.1191 0.1146 0.1150 -0.0049 0.0080 0.0044 294 ASP A CA 1668 C C . ASP A 208 ? 0.1122 0.0978 0.0986 -0.0043 0.0045 -0.0065 294 ASP A C 1669 O O . ASP A 208 ? 0.1560 0.1286 0.0979 0.0007 0.0231 -0.0010 294 ASP A O 1670 C CB . ASP A 208 ? 0.1290 0.1320 0.1248 0.0054 0.0074 -0.0020 294 ASP A CB 1671 C CG . ASP A 208 ? 0.1647 0.1643 0.1610 -0.0022 -0.0007 0.0089 294 ASP A CG 1672 O OD1 . ASP A 208 ? 0.2328 0.1887 0.2265 -0.0048 0.0041 0.0190 294 ASP A OD1 1673 O OD2 . ASP A 208 ? 0.2337 0.2051 0.1973 0.0386 -0.0078 -0.0009 294 ASP A OD2 1674 N N . ALA A 209 ? 0.0773 0.0867 0.0866 -0.0030 0.0054 -0.0070 295 ALA A N 1675 C CA . ALA A 209 ? 0.0875 0.0907 0.0841 -0.0005 0.0039 -0.0022 295 ALA A CA 1676 C C . ALA A 209 ? 0.0863 0.0880 0.0949 -0.0015 0.0075 -0.0042 295 ALA A C 1677 O O . ALA A 209 ? 0.0913 0.1029 0.1198 -0.0021 0.0075 -0.0062 295 ALA A O 1678 C CB . ALA A 209 ? 0.0932 0.0911 0.0967 -0.0071 0.0080 -0.0006 295 ALA A CB 1679 N N . GLY A 210 ? 0.0870 0.0851 0.0924 -0.0024 0.0035 -0.0033 296 GLY A N 1680 C CA . GLY A 210 ? 0.0920 0.0925 0.1113 -0.0034 0.0085 -0.0024 296 GLY A CA 1681 C C . GLY A 210 ? 0.0860 0.0950 0.1096 -0.0009 0.0065 -0.0021 296 GLY A C 1682 O O . GLY A 210 ? 0.0982 0.1001 0.1184 0.0028 0.0070 0.0106 296 GLY A O 1683 N N . LYS A 211 ? 0.0737 0.0724 0.0878 -0.0051 0.0079 -0.0059 297 LYS A N 1684 C CA . LYS A 211 ? 0.0718 0.0881 0.0974 -0.0056 0.0064 -0.0043 297 LYS A CA 1685 C C . LYS A 211 ? 0.0781 0.0850 0.1082 -0.0057 -0.0015 -0.0057 297 LYS A C 1686 O O . LYS A 211 ? 0.0824 0.0877 0.1167 -0.0042 -0.0038 0.0022 297 LYS A O 1687 C CB . LYS A 211 ? 0.0682 0.0907 0.0826 -0.0050 -0.0010 -0.0105 297 LYS A CB 1688 C CG . LYS A 211 ? 0.0662 0.0983 0.0854 -0.0072 0.0018 -0.0078 297 LYS A CG 1689 C CD . LYS A 211 ? 0.0439 0.0743 0.0666 -0.0110 0.0167 -0.0106 297 LYS A CD 1690 C CE . LYS A 211 ? 0.0593 0.0832 0.0829 -0.0096 -0.0059 -0.0024 297 LYS A CE 1691 N NZ . LYS A 211 ? 0.0829 0.0723 0.0820 -0.0151 0.0042 -0.0004 297 LYS A NZ 1692 N N . PRO A 212 ? 0.0831 0.0838 0.1032 -0.0114 -0.0007 -0.0007 298 PRO A N 1693 C CA . PRO A 212 ? 0.0711 0.0795 0.0975 -0.0001 0.0016 -0.0007 298 PRO A CA 1694 C C . PRO A 212 ? 0.0858 0.0559 0.0967 -0.0024 0.0032 0.0008 298 PRO A C 1695 O O . PRO A 212 ? 0.0875 0.0659 0.0970 -0.0095 0.0183 -0.0090 298 PRO A O 1696 C CB . PRO A 212 ? 0.0718 0.0833 0.1075 -0.0063 -0.0029 -0.0032 298 PRO A CB 1697 C CG . PRO A 212 ? 0.1118 0.0906 0.1401 -0.0018 0.0000 0.0089 298 PRO A CG 1698 C CD . PRO A 212 ? 0.0819 0.0970 0.1131 0.0093 0.0086 -0.0061 298 PRO A CD 1699 N N . ARG A 213 ? 0.0798 0.0812 0.0941 -0.0106 0.0078 -0.0081 299 ARG A N 1700 C CA . ARG A 213 ? 0.0902 0.0896 0.1086 -0.0035 0.0080 0.0002 299 ARG A CA 1701 C C . ARG A 213 ? 0.0872 0.0809 0.0930 0.0000 -0.0009 0.0050 299 ARG A C 1702 O O . ARG A 213 ? 0.0972 0.0891 0.1051 -0.0020 0.0042 0.0060 299 ARG A O 1703 C CB . ARG A 213 ? 0.1063 0.1253 0.1290 -0.0040 0.0021 0.0052 299 ARG A CB 1704 C CG . ARG A 213 ? 0.1966 0.2234 0.1957 0.0029 0.0039 0.0030 299 ARG A CG 1705 C CD . ARG A 213 ? 0.2796 0.2799 0.2870 0.0191 -0.0084 -0.0008 299 ARG A CD 1706 N NE . ARG A 213 ? 0.3178 0.3362 0.3178 0.0006 -0.0101 0.0133 299 ARG A NE 1707 C CZ . ARG A 213 ? 0.3036 0.3201 0.3108 -0.0292 0.0042 0.0221 299 ARG A CZ 1708 N NH1 . ARG A 213 ? 0.2667 0.2940 0.2843 -0.0223 -0.0019 0.0082 299 ARG A NH1 1709 N NH2 . ARG A 213 ? 0.3393 0.3484 0.3224 -0.0082 -0.0079 0.0107 299 ARG A NH2 1710 N N . ALA A 214 ? 0.0684 0.0734 0.0846 0.0080 -0.0058 0.0010 300 ALA A N 1711 C CA . ALA A 214 ? 0.0760 0.0838 0.0739 0.0054 0.0022 -0.0016 300 ALA A CA 1712 C C . ALA A 214 ? 0.0776 0.0812 0.0721 0.0086 0.0051 -0.0040 300 ALA A C 1713 O O . ALA A 214 ? 0.0753 0.0944 0.1086 0.0010 0.0070 0.0033 300 ALA A O 1714 C CB . ALA A 214 ? 0.0771 0.0896 0.0949 -0.0059 0.0007 -0.0067 300 ALA A CB 1715 N N . VAL A 215 ? 0.0565 0.0738 0.0799 0.0013 0.0063 -0.0045 301 VAL A N 1716 C CA . VAL A 215 ? 0.0689 0.0769 0.0813 0.0042 0.0048 -0.0068 301 VAL A CA 1717 C C . VAL A 215 ? 0.0757 0.0717 0.0964 -0.0019 0.0064 -0.0091 301 VAL A C 1718 O O . VAL A 215 ? 0.0995 0.1080 0.1448 -0.0181 0.0141 -0.0118 301 VAL A O 1719 C CB . VAL A 215 ? 0.0743 0.0842 0.0960 0.0010 0.0104 -0.0049 301 VAL A CB 1720 C CG1 . VAL A 215 ? 0.1023 0.0936 0.1161 0.0153 0.0146 -0.0035 301 VAL A CG1 1721 C CG2 . VAL A 215 ? 0.1045 0.0985 0.1209 0.0040 -0.0104 0.0076 301 VAL A CG2 1722 N N . ARG A 216 ? 0.0635 0.0712 0.0988 0.0024 0.0015 0.0038 302 ARG A N 1723 C CA . ARG A 216 ? 0.0623 0.0751 0.0958 -0.0022 0.0061 0.0022 302 ARG A CA 1724 C C . ARG A 216 ? 0.0549 0.0594 0.0703 -0.0006 0.0057 -0.0044 302 ARG A C 1725 O O . ARG A 216 ? 0.0580 0.0807 0.0841 -0.0022 0.0035 -0.0013 302 ARG A O 1726 C CB . ARG A 216 ? 0.0956 0.1152 0.1340 0.0021 0.0122 0.0148 302 ARG A CB 1727 C CG . ARG A 216 ? 0.1485 0.1601 0.1655 -0.0061 -0.0072 0.0098 302 ARG A CG 1728 C CD . ARG A 216 ? 0.1134 0.1847 0.1330 -0.0089 0.0041 0.0134 302 ARG A CD 1729 N NE . ARG A 216 ? 0.0834 0.1495 0.1403 0.0128 -0.0080 -0.0066 302 ARG A NE 1730 C CZ . ARG A 216 ? 0.0905 0.1228 0.0906 -0.0002 0.0028 0.0078 302 ARG A CZ 1731 N NH1 . ARG A 216 ? 0.1032 0.1617 0.1199 0.0134 0.0135 0.0026 302 ARG A NH1 1732 N NH2 . ARG A 216 ? 0.0734 0.0937 0.1204 0.0037 -0.0095 -0.0123 302 ARG A NH2 1733 N N . GLY A 217 ? 0.0652 0.0587 0.0789 -0.0009 0.0026 -0.0003 303 GLY A N 1734 C CA . GLY A 217 ? 0.0683 0.0700 0.0692 -0.0013 -0.0002 0.0029 303 GLY A CA 1735 C C . GLY A 217 ? 0.0643 0.0721 0.0623 -0.0022 0.0076 -0.0011 303 GLY A C 1736 O O . GLY A 217 ? 0.0536 0.0622 0.0675 -0.0041 0.0008 0.0030 303 GLY A O 1737 N N . LEU A 218 ? 0.0576 0.0654 0.0598 -0.0065 0.0003 -0.0052 304 LEU A N 1738 C CA . LEU A 218 ? 0.0520 0.0466 0.0516 -0.0022 0.0038 0.0033 304 LEU A CA 1739 C C . LEU A 218 ? 0.0606 0.0639 0.0429 -0.0059 0.0009 0.0034 304 LEU A C 1740 O O . LEU A 218 ? 0.0551 0.0566 0.0611 -0.0057 -0.0066 0.0108 304 LEU A O 1741 C CB . LEU A 218 ? 0.0528 0.0678 0.0630 -0.0033 -0.0046 -0.0029 304 LEU A CB 1742 C CG . LEU A 218 ? 0.0527 0.0618 0.0621 0.0009 -0.0030 -0.0075 304 LEU A CG 1743 C CD1 . LEU A 218 ? 0.0744 0.0668 0.0691 -0.0066 0.0062 0.0082 304 LEU A CD1 1744 C CD2 . LEU A 218 ? 0.0821 0.0679 0.0702 -0.0091 0.0042 -0.0086 304 LEU A CD2 1745 N N . ALA A 219 ? 0.0471 0.0505 0.0512 -0.0041 0.0013 -0.0055 305 ALA A N 1746 C CA . ALA A 219 ? 0.0566 0.0573 0.0488 0.0011 -0.0046 0.0004 305 ALA A CA 1747 C C . ALA A 219 ? 0.0650 0.0561 0.0557 0.0030 -0.0038 -0.0017 305 ALA A C 1748 O O . ALA A 219 ? 0.0705 0.0770 0.0469 0.0070 0.0060 0.0044 305 ALA A O 1749 C CB . ALA A 219 ? 0.0685 0.0690 0.0730 -0.0022 0.0006 -0.0021 305 ALA A CB 1750 N N . THR A 220 ? 0.0479 0.0584 0.0534 0.0086 -0.0024 -0.0021 306 THR A N 1751 C CA . THR A 220 ? 0.0686 0.0507 0.0630 0.0066 0.0028 -0.0017 306 THR A CA 1752 C C . THR A 220 ? 0.0591 0.0425 0.0658 0.0076 0.0005 -0.0029 306 THR A C 1753 O O . THR A 220 ? 0.0537 0.0615 0.0562 0.0104 -0.0091 0.0076 306 THR A O 1754 C CB . THR A 220 ? 0.0756 0.0703 0.0593 -0.0047 0.0036 0.0014 306 THR A CB 1755 O OG1 . THR A 220 ? 0.0879 0.0927 0.0859 -0.0031 -0.0104 -0.0061 306 THR A OG1 1756 C CG2 . THR A 220 ? 0.0769 0.0920 0.0856 0.0017 0.0102 -0.0025 306 THR A CG2 1757 N N . ASN A 221 ? 0.0508 0.0472 0.0582 0.0062 0.0016 -0.0007 307 ASN A N 1758 C CA . ASN A 221 ? 0.0521 0.0515 0.0440 -0.0017 -0.0016 -0.0003 307 ASN A CA 1759 C C . ASN A 221 ? 0.0478 0.0507 0.0581 -0.0013 0.0026 0.0048 307 ASN A C 1760 O O . ASN A 221 ? 0.0514 0.0570 0.0510 -0.0023 0.0071 -0.0008 307 ASN A O 1761 C CB . ASN A 221 ? 0.0461 0.0523 0.0508 -0.0024 -0.0121 -0.0064 307 ASN A CB 1762 C CG . ASN A 221 ? 0.0728 0.0791 0.0499 0.0076 -0.0041 0.0031 307 ASN A CG 1763 O OD1 . ASN A 221 ? 0.0745 0.0726 0.0615 0.0205 -0.0033 -0.0026 307 ASN A OD1 1764 N ND2 . ASN A 221 ? 0.0738 0.0748 0.0673 0.0118 0.0063 0.0055 307 ASN A ND2 1765 N N . VAL A 222 ? 0.0430 0.0513 0.0548 -0.0029 0.0012 -0.0007 308 VAL A N 1766 C CA . VAL A 222 ? 0.0559 0.0557 0.0529 0.0013 0.0006 -0.0007 308 VAL A CA 1767 C C . VAL A 222 ? 0.0580 0.0574 0.0577 0.0003 -0.0013 0.0078 308 VAL A C 1768 O O . VAL A 222 ? 0.0730 0.0573 0.0682 0.0052 -0.0005 0.0124 308 VAL A O 1769 C CB . VAL A 222 ? 0.0511 0.0614 0.0501 -0.0015 0.0038 -0.0005 308 VAL A CB 1770 C CG1 . VAL A 222 ? 0.0610 0.0655 0.0512 0.0088 0.0020 -0.0074 308 VAL A CG1 1771 C CG2 . VAL A 222 ? 0.0737 0.0793 0.0775 0.0005 0.0013 -0.0069 308 VAL A CG2 1772 N N . ALA A 223 ? 0.0486 0.0542 0.0690 -0.0007 0.0020 0.0011 309 ALA A N 1773 C CA . ALA A 223 ? 0.0585 0.0672 0.0611 0.0026 0.0013 -0.0024 309 ALA A CA 1774 C C . ALA A 223 ? 0.0622 0.0607 0.0659 0.0045 0.0026 0.0119 309 ALA A C 1775 O O . ALA A 223 ? 0.0743 0.0835 0.0944 0.0023 -0.0019 0.0021 309 ALA A O 1776 C CB . ALA A 223 ? 0.0512 0.0797 0.0781 -0.0048 0.0021 -0.0110 309 ALA A CB 1777 N N . ASN A 224 ? 0.0500 0.0667 0.0466 0.0070 0.0152 -0.0094 310 ASN A N 1778 C CA . ASN A 224 ? 0.0675 0.0654 0.0738 0.0032 0.0023 0.0032 310 ASN A CA 1779 C C . ASN A 224 ? 0.0465 0.0797 0.0762 0.0102 -0.0018 -0.0023 310 ASN A C 1780 O O . ASN A 224 ? 0.0567 0.0625 0.0702 0.0017 0.0164 0.0015 310 ASN A O 1781 C CB . ASN A 224 ? 0.0665 0.0830 0.0716 0.0075 0.0111 -0.0033 310 ASN A CB 1782 C CG . ASN A 224 ? 0.0997 0.1079 0.1102 -0.0052 0.0088 -0.0037 310 ASN A CG 1783 O OD1 . ASN A 224 ? 0.1553 0.1585 0.1818 0.0273 -0.0159 -0.0057 310 ASN A OD1 1784 N ND2 . ASN A 224 ? 0.1627 0.2007 0.1152 0.0089 -0.0068 -0.0007 310 ASN A ND2 1785 N N . TYR A 225 ? 0.0595 0.0646 0.0524 0.0072 0.0003 -0.0015 311 TYR A N 1786 C CA . TYR A 225 ? 0.0552 0.0556 0.0621 0.0005 -0.0048 -0.0028 311 TYR A CA 1787 C C . TYR A 225 ? 0.0649 0.0562 0.0602 0.0050 0.0012 -0.0010 311 TYR A C 1788 O O . TYR A 225 ? 0.0675 0.0650 0.0756 -0.0030 0.0072 0.0016 311 TYR A O 1789 C CB . TYR A 225 ? 0.0579 0.0668 0.0546 0.0088 -0.0039 0.0041 311 TYR A CB 1790 C CG . TYR A 225 ? 0.0521 0.0622 0.0542 0.0000 0.0149 0.0052 311 TYR A CG 1791 C CD1 . TYR A 225 ? 0.0581 0.0794 0.0649 0.0032 -0.0016 -0.0074 311 TYR A CD1 1792 C CD2 . TYR A 225 ? 0.0595 0.0852 0.0705 0.0038 -0.0018 0.0180 311 TYR A CD2 1793 C CE1 . TYR A 225 ? 0.0612 0.0590 0.0580 0.0077 0.0099 0.0132 311 TYR A CE1 1794 C CE2 . TYR A 225 ? 0.0664 0.0608 0.0672 0.0056 0.0087 -0.0034 311 TYR A CE2 1795 C CZ . TYR A 225 ? 0.0487 0.0710 0.0577 -0.0086 0.0124 -0.0111 311 TYR A CZ 1796 O OH . TYR A 225 ? 0.0750 0.0872 0.0731 0.0009 0.0026 0.0041 311 TYR A OH 1797 N N . ASN A 226 ? 0.0512 0.0564 0.0596 -0.0033 0.0067 -0.0022 312 ASN A N 1798 C CA . ASN A 226 ? 0.0547 0.0560 0.0449 0.0021 0.0068 -0.0080 312 ASN A CA 1799 C C . ASN A 226 ? 0.0507 0.0492 0.0608 0.0002 0.0000 -0.0040 312 ASN A C 1800 O O . ASN A 226 ? 0.0568 0.0541 0.0646 0.0013 -0.0015 0.0010 312 ASN A O 1801 C CB . ASN A 226 ? 0.0516 0.0564 0.0376 0.0002 0.0073 -0.0007 312 ASN A CB 1802 C CG . ASN A 226 ? 0.0663 0.0581 0.0566 0.0104 0.0103 -0.0013 312 ASN A CG 1803 O OD1 . ASN A 226 ? 0.0852 0.0786 0.0812 0.0054 -0.0085 -0.0011 312 ASN A OD1 1804 N ND2 . ASN A 226 ? 0.0715 0.0649 0.0656 0.0043 0.0067 0.0067 312 ASN A ND2 1805 N N . ALA A 227 ? 0.0484 0.0606 0.0589 0.0091 -0.0002 -0.0082 313 ALA A N 1806 C CA . ALA A 227 ? 0.0502 0.0597 0.0585 0.0040 0.0015 0.0037 313 ALA A CA 1807 C C . ALA A 227 ? 0.0535 0.0629 0.0658 0.0034 0.0000 0.0049 313 ALA A C 1808 O O . ALA A 227 ? 0.0611 0.0886 0.0714 0.0026 -0.0014 -0.0062 313 ALA A O 1809 C CB . ALA A 227 ? 0.0685 0.0765 0.0619 -0.0053 0.0008 -0.0084 313 ALA A CB 1810 N N . TRP A 228 ? 0.0611 0.0894 0.0868 -0.0011 -0.0014 0.0163 314 TRP A N 1811 C CA . TRP A 228 ? 0.0584 0.0821 0.0757 0.0017 0.0042 0.0042 314 TRP A CA 1812 C C . TRP A 228 ? 0.0766 0.0864 0.0769 0.0070 0.0040 0.0057 314 TRP A C 1813 O O . TRP A 228 ? 0.0860 0.1093 0.0902 0.0089 -0.0016 0.0032 314 TRP A O 1814 C CB . TRP A 228 ? 0.0827 0.0880 0.0797 0.0034 0.0056 0.0031 314 TRP A CB 1815 C CG . TRP A 228 ? 0.0714 0.0855 0.0794 -0.0030 0.0019 0.0006 314 TRP A CG 1816 C CD1 . TRP A 228 ? 0.0851 0.0804 0.0910 -0.0030 0.0042 -0.0070 314 TRP A CD1 1817 C CD2 . TRP A 228 ? 0.0622 0.0588 0.0632 0.0014 -0.0020 0.0027 314 TRP A CD2 1818 N NE1 . TRP A 228 ? 0.0761 0.0884 0.0923 -0.0074 -0.0133 -0.0078 314 TRP A NE1 1819 C CE2 . TRP A 228 ? 0.0747 0.0738 0.0809 -0.0002 0.0033 0.0120 314 TRP A CE2 1820 C CE3 . TRP A 228 ? 0.0601 0.0707 0.0698 0.0051 -0.0034 0.0143 314 TRP A CE3 1821 C CZ2 . TRP A 228 ? 0.0836 0.0968 0.0828 -0.0080 -0.0032 -0.0020 314 TRP A CZ2 1822 C CZ3 . TRP A 228 ? 0.0678 0.1010 0.0925 -0.0038 -0.0036 -0.0043 314 TRP A CZ3 1823 C CH2 . TRP A 228 ? 0.0674 0.0872 0.0775 -0.0022 -0.0114 0.0086 314 TRP A CH2 1824 N N . SER A 229 ? 0.0983 0.1009 0.0766 0.0031 0.0094 -0.0035 315 SER A N 1825 C CA . SER A 229 ? 0.1094 0.1112 0.1019 0.0030 0.0102 -0.0007 315 SER A CA 1826 C C . SER A 229 ? 0.1339 0.1190 0.0972 0.0075 0.0182 -0.0001 315 SER A C 1827 O O . SER A 229 ? 0.1641 0.1345 0.1408 0.0183 0.0260 0.0075 315 SER A O 1828 C CB . SER A 229 ? 0.1206 0.1110 0.1094 -0.0103 0.0004 -0.0022 315 SER A CB 1829 O OG . SER A 229 ? 0.1556 0.1249 0.1099 -0.0058 -0.0100 -0.0125 315 SER A OG 1830 N N . VAL A 230 ? 0.1409 0.1263 0.1123 0.0040 0.0258 0.0039 316 VAL A N 1831 C CA . VAL A 230 ? 0.1451 0.1425 0.1232 0.0069 0.0147 -0.0009 316 VAL A CA 1832 C C . VAL A 230 ? 0.1559 0.1404 0.1320 0.0132 0.0129 -0.0003 316 VAL A C 1833 O O . VAL A 230 ? 0.1599 0.1160 0.1205 0.0256 0.0103 -0.0115 316 VAL A O 1834 C CB . VAL A 230 ? 0.1571 0.1484 0.1442 -0.0021 0.0124 -0.0086 316 VAL A CB 1835 C CG1 . VAL A 230 ? 0.1594 0.1597 0.1508 0.0063 0.0089 0.0033 316 VAL A CG1 1836 C CG2 . VAL A 230 ? 0.1435 0.1712 0.1782 0.0072 0.0028 -0.0080 316 VAL A CG2 1837 N N . SER A 231 ? 0.1921 0.1642 0.1502 0.0115 0.0101 -0.0042 317 SER A N 1838 C CA . SER A 231 ? 0.2068 0.1902 0.1768 0.0061 -0.0027 -0.0015 317 SER A CA 1839 C C . SER A 231 ? 0.1957 0.1883 0.1829 0.0078 0.0114 -0.0108 317 SER A C 1840 O O . SER A 231 ? 0.2219 0.1985 0.2230 0.0136 0.0177 -0.0050 317 SER A O 1841 C CB . SER A 231 ? 0.2305 0.2119 0.1850 0.0116 0.0022 -0.0103 317 SER A CB 1842 O OG . SER A 231 ? 0.3016 0.2871 0.2856 -0.0010 0.0093 0.0015 317 SER A OG 1843 N N . SER A 232 ? 0.1991 0.1814 0.1816 0.0097 0.0020 -0.0142 318 SER A N 1844 C CA . SER A 232 ? 0.2017 0.2042 0.1931 0.0033 -0.0061 -0.0055 318 SER A CA 1845 C C . SER A 232 ? 0.1838 0.1857 0.1670 0.0009 -0.0067 -0.0049 318 SER A C 1846 O O . SER A 232 ? 0.1789 0.1785 0.1628 0.0037 -0.0136 -0.0067 318 SER A O 1847 C CB A SER A 232 ? 0.2130 0.2068 0.2048 0.0013 -0.0022 -0.0050 318 SER A CB 1848 C CB B SER A 232 ? 0.2133 0.2118 0.2068 0.0047 -0.0024 -0.0055 318 SER A CB 1849 O OG A SER A 232 ? 0.2449 0.2273 0.2503 0.0111 -0.0120 -0.0018 318 SER A OG 1850 O OG B SER A 232 ? 0.2391 0.2416 0.2343 -0.0059 0.0084 -0.0023 318 SER A OG 1851 N N . PRO A 233 ? 0.1659 0.1628 0.1708 -0.0013 -0.0024 -0.0094 319 PRO A N 1852 C CA . PRO A 233 ? 0.1476 0.1533 0.1444 0.0031 0.0071 -0.0077 319 PRO A CA 1853 C C . PRO A 233 ? 0.1376 0.1420 0.1399 0.0044 0.0102 -0.0163 319 PRO A C 1854 O O . PRO A 233 ? 0.1317 0.1313 0.1241 0.0234 0.0234 -0.0311 319 PRO A O 1855 C CB . PRO A 233 ? 0.1564 0.1612 0.1530 0.0063 0.0026 -0.0139 319 PRO A CB 1856 C CG . PRO A 233 ? 0.2070 0.1871 0.1902 -0.0147 -0.0008 0.0019 319 PRO A CG 1857 C CD . PRO A 233 ? 0.1896 0.1763 0.1736 -0.0025 -0.0047 -0.0062 319 PRO A CD 1858 N N . PRO A 234 ? 0.1164 0.1178 0.1079 0.0071 0.0110 -0.0092 320 PRO A N 1859 C CA . PRO A 234 ? 0.1310 0.1292 0.1186 -0.0023 0.0070 -0.0118 320 PRO A CA 1860 C C . PRO A 234 ? 0.1238 0.1243 0.1164 0.0031 0.0098 -0.0096 320 PRO A C 1861 O O . PRO A 234 ? 0.1263 0.1113 0.1116 0.0036 0.0162 -0.0048 320 PRO A O 1862 C CB . PRO A 234 ? 0.1307 0.1205 0.1058 -0.0010 0.0078 -0.0121 320 PRO A CB 1863 C CG . PRO A 234 ? 0.1264 0.1383 0.1133 0.0011 0.0088 -0.0029 320 PRO A CG 1864 C CD . PRO A 234 ? 0.1212 0.1346 0.1169 0.0140 0.0027 -0.0108 320 PRO A CD 1865 N N . PRO A 235 ? 0.1279 0.1401 0.1183 -0.0008 0.0135 0.0025 321 PRO A N 1866 C CA . PRO A 235 ? 0.1295 0.1355 0.1335 0.0041 0.0095 -0.0029 321 PRO A CA 1867 C C . PRO A 235 ? 0.1294 0.1203 0.1319 0.0132 0.0087 0.0011 321 PRO A C 1868 O O . PRO A 235 ? 0.1656 0.1274 0.1489 0.0269 0.0123 -0.0006 321 PRO A O 1869 C CB . PRO A 235 ? 0.1363 0.1629 0.1419 0.0164 0.0151 -0.0023 321 PRO A CB 1870 C CG . PRO A 235 ? 0.1656 0.1956 0.1796 0.0034 0.0204 0.0057 321 PRO A CG 1871 C CD . PRO A 235 ? 0.1518 0.1720 0.1529 0.0061 0.0142 0.0076 321 PRO A CD 1872 N N . TYR A 236 ? 0.1031 0.1077 0.1098 0.0162 0.0009 -0.0071 322 TYR A N 1873 C CA . TYR A 236 ? 0.0847 0.0998 0.0923 0.0162 0.0106 0.0024 322 TYR A CA 1874 C C . TYR A 236 ? 0.0883 0.0954 0.1013 0.0091 0.0030 0.0096 322 TYR A C 1875 O O . TYR A 236 ? 0.1021 0.1077 0.1019 0.0210 0.0162 -0.0015 322 TYR A O 1876 C CB . TYR A 236 ? 0.0938 0.1158 0.1137 0.0080 0.0088 0.0049 322 TYR A CB 1877 C CG . TYR A 236 ? 0.0931 0.1051 0.0844 0.0137 0.0025 -0.0003 322 TYR A CG 1878 C CD1 . TYR A 236 ? 0.1152 0.0907 0.0980 0.0010 0.0015 0.0069 322 TYR A CD1 1879 C CD2 . TYR A 236 ? 0.1109 0.1113 0.0940 -0.0028 -0.0117 0.0033 322 TYR A CD2 1880 C CE1 . TYR A 236 ? 0.1100 0.1277 0.1015 0.0180 0.0086 0.0025 322 TYR A CE1 1881 C CE2 . TYR A 236 ? 0.0877 0.1007 0.1010 0.0028 0.0096 -0.0052 322 TYR A CE2 1882 C CZ . TYR A 236 ? 0.1095 0.0826 0.1093 0.0224 0.0092 0.0002 322 TYR A CZ 1883 O OH . TYR A 236 ? 0.0861 0.0997 0.0789 0.0142 0.0146 0.0001 322 TYR A OH 1884 N N . THR A 237 ? 0.0997 0.1097 0.1063 0.0116 0.0080 -0.0053 323 THR A N 1885 C CA . THR A 237 ? 0.0976 0.1015 0.0849 0.0036 0.0132 -0.0061 323 THR A CA 1886 C C . THR A 237 ? 0.1051 0.1061 0.1143 0.0055 0.0178 -0.0017 323 THR A C 1887 O O . THR A 237 ? 0.1152 0.0910 0.1212 0.0181 0.0276 0.0024 323 THR A O 1888 C CB . THR A 237 ? 0.1059 0.1034 0.0806 0.0034 0.0154 -0.0055 323 THR A CB 1889 O OG1 . THR A 237 ? 0.1141 0.1100 0.1002 -0.0043 -0.0011 -0.0145 323 THR A OG1 1890 C CG2 . THR A 237 ? 0.0859 0.0989 0.0810 0.0061 0.0048 -0.0058 323 THR A CG2 1891 N N . SER A 238 ? 0.1309 0.1200 0.1426 0.0122 0.0255 -0.0087 324 SER A N 1892 C CA . SER A 238 ? 0.1544 0.1389 0.1532 0.0068 0.0181 -0.0074 324 SER A CA 1893 C C . SER A 238 ? 0.1446 0.1304 0.1533 0.0172 0.0127 -0.0122 324 SER A C 1894 O O . SER A 238 ? 0.1623 0.1371 0.1804 0.0259 0.0071 -0.0138 324 SER A O 1895 C CB . SER A 238 ? 0.1818 0.1529 0.1775 -0.0013 0.0299 -0.0132 324 SER A CB 1896 O OG . SER A 238 ? 0.2620 0.1895 0.2399 0.0098 0.0199 -0.0093 324 SER A OG 1897 N N . PRO A 239 ? 0.1478 0.1349 0.1498 0.0118 0.0070 -0.0041 325 PRO A N 1898 C CA . PRO A 239 ? 0.1444 0.1218 0.1450 0.0091 0.0065 -0.0005 325 PRO A CA 1899 C C . PRO A 239 ? 0.1316 0.1171 0.1329 -0.0048 0.0043 -0.0075 325 PRO A C 1900 O O . PRO A 239 ? 0.1588 0.1212 0.1618 -0.0093 0.0236 -0.0118 325 PRO A O 1901 C CB . PRO A 239 ? 0.1495 0.1290 0.1646 0.0088 0.0076 0.0001 325 PRO A CB 1902 C CG . PRO A 239 ? 0.1625 0.1400 0.1736 0.0218 0.0059 0.0019 325 PRO A CG 1903 C CD . PRO A 239 ? 0.1610 0.1627 0.1743 0.0167 0.0049 -0.0035 325 PRO A CD 1904 N N . ASN A 240 ? 0.1117 0.0989 0.1195 0.0102 0.0036 -0.0040 326 ASN A N 1905 C CA . ASN A 240 ? 0.1050 0.0972 0.1089 -0.0037 0.0094 -0.0015 326 ASN A CA 1906 C C . ASN A 240 ? 0.1092 0.0888 0.1072 0.0027 0.0092 -0.0069 326 ASN A C 1907 O O . ASN A 240 ? 0.1287 0.1068 0.1112 0.0194 -0.0006 -0.0101 326 ASN A O 1908 C CB . ASN A 240 ? 0.0907 0.0865 0.1016 0.0053 0.0073 -0.0087 326 ASN A CB 1909 C CG . ASN A 240 ? 0.0800 0.0730 0.0808 -0.0023 0.0052 -0.0044 326 ASN A CG 1910 O OD1 . ASN A 240 ? 0.1065 0.0749 0.0964 0.0008 0.0006 -0.0062 326 ASN A OD1 1911 N ND2 . ASN A 240 ? 0.0882 0.0732 0.0602 0.0027 0.0151 -0.0056 326 ASN A ND2 1912 N N . PRO A 241 ? 0.1170 0.0992 0.1046 0.0007 -0.0036 -0.0066 327 PRO A N 1913 C CA . PRO A 241 ? 0.1147 0.1031 0.1184 0.0012 -0.0022 0.0005 327 PRO A CA 1914 C C . PRO A 241 ? 0.0992 0.0927 0.0935 0.0068 -0.0033 -0.0058 327 PRO A C 1915 O O . PRO A 241 ? 0.1157 0.1028 0.1140 0.0019 0.0024 -0.0028 327 PRO A O 1916 C CB . PRO A 241 ? 0.1247 0.1094 0.1286 0.0000 0.0004 0.0052 327 PRO A CB 1917 C CG . PRO A 241 ? 0.1397 0.1298 0.1391 -0.0074 -0.0041 -0.0052 327 PRO A CG 1918 C CD . PRO A 241 ? 0.1231 0.1078 0.1213 0.0031 0.0058 -0.0067 327 PRO A CD 1919 N N . ASN A 242 ? 0.0999 0.0841 0.0864 0.0034 -0.0032 -0.0035 328 ASN A N 1920 C CA . ASN A 242 ? 0.0883 0.0880 0.0816 0.0095 -0.0109 0.0045 328 ASN A CA 1921 C C . ASN A 242 ? 0.0923 0.0840 0.0844 0.0074 -0.0074 -0.0013 328 ASN A C 1922 O O . ASN A 242 ? 0.0878 0.0900 0.0829 -0.0032 -0.0105 -0.0018 328 ASN A O 1923 C CB . ASN A 242 ? 0.0843 0.0819 0.0879 0.0081 -0.0002 0.0029 328 ASN A CB 1924 C CG . ASN A 242 ? 0.0886 0.0867 0.0941 0.0043 0.0054 -0.0068 328 ASN A CG 1925 O OD1 . ASN A 242 ? 0.1218 0.1411 0.1229 -0.0026 -0.0039 -0.0018 328 ASN A OD1 1926 N ND2 . ASN A 242 ? 0.1256 0.1217 0.0983 -0.0134 -0.0212 0.0168 328 ASN A ND2 1927 N N . TYR A 243 ? 0.0805 0.0913 0.0819 -0.0043 0.0008 -0.0039 329 TYR A N 1928 C CA . TYR A 243 ? 0.0857 0.0871 0.0903 -0.0003 0.0027 -0.0034 329 TYR A CA 1929 C C . TYR A 243 ? 0.0751 0.0785 0.0704 -0.0055 0.0022 0.0015 329 TYR A C 1930 O O . TYR A 243 ? 0.0802 0.0821 0.1002 0.0006 0.0142 0.0048 329 TYR A O 1931 C CB . TYR A 243 ? 0.0906 0.0965 0.0906 -0.0019 0.0105 -0.0065 329 TYR A CB 1932 C CG . TYR A 243 ? 0.0939 0.1035 0.0985 0.0067 0.0121 -0.0110 329 TYR A CG 1933 C CD1 . TYR A 243 ? 0.0987 0.1332 0.1033 0.0014 0.0142 -0.0045 329 TYR A CD1 1934 C CD2 . TYR A 243 ? 0.1426 0.1376 0.1368 -0.0153 -0.0035 0.0032 329 TYR A CD2 1935 C CE1 . TYR A 243 ? 0.1079 0.1400 0.1021 0.0122 0.0141 -0.0141 329 TYR A CE1 1936 C CE2 . TYR A 243 ? 0.1651 0.1423 0.1461 -0.0160 -0.0069 0.0005 329 TYR A CE2 1937 C CZ . TYR A 243 ? 0.1426 0.1600 0.1402 -0.0060 0.0079 0.0030 329 TYR A CZ 1938 O OH . TYR A 243 ? 0.2008 0.2380 0.1610 -0.0070 -0.0078 -0.0038 329 TYR A OH 1939 N N . ASP A 244 ? 0.0858 0.0628 0.0875 0.0020 0.0040 -0.0038 330 ASP A N 1940 C CA . ASP A 244 ? 0.0701 0.0718 0.0736 0.0008 0.0052 0.0026 330 ASP A CA 1941 C C . ASP A 244 ? 0.0779 0.0636 0.0730 0.0025 0.0068 0.0006 330 ASP A C 1942 O O . ASP A 244 ? 0.0826 0.0682 0.0742 0.0093 0.0133 -0.0027 330 ASP A O 1943 C CB . ASP A 244 ? 0.0759 0.0831 0.0760 -0.0060 0.0116 -0.0044 330 ASP A CB 1944 C CG . ASP A 244 ? 0.0840 0.0655 0.0823 0.0000 -0.0034 0.0048 330 ASP A CG 1945 O OD1 . ASP A 244 ? 0.0927 0.0974 0.0878 0.0032 0.0103 -0.0098 330 ASP A OD1 1946 O OD2 . ASP A 244 ? 0.1111 0.0934 0.1019 0.0029 0.0074 -0.0166 330 ASP A OD2 1947 N N . GLU A 245 ? 0.0501 0.0560 0.0554 0.0101 0.0154 -0.0025 331 GLU A N 1948 C CA . GLU A 245 ? 0.0609 0.0630 0.0513 0.0062 0.0118 -0.0020 331 GLU A CA 1949 C C . GLU A 245 ? 0.0648 0.0655 0.0522 0.0060 0.0021 0.0004 331 GLU A C 1950 O O . GLU A 245 ? 0.0631 0.0700 0.0626 0.0113 0.0044 -0.0094 331 GLU A O 1951 C CB . GLU A 245 ? 0.0586 0.0656 0.0579 -0.0027 -0.0054 0.0045 331 GLU A CB 1952 C CG . GLU A 245 ? 0.0462 0.0527 0.0715 0.0123 0.0011 -0.0020 331 GLU A CG 1953 C CD . GLU A 245 ? 0.0784 0.0962 0.0876 -0.0032 0.0033 -0.0030 331 GLU A CD 1954 O OE1 . GLU A 245 ? 0.0950 0.0840 0.0919 0.0173 0.0123 0.0151 331 GLU A OE1 1955 O OE2 . GLU A 245 ? 0.0924 0.0922 0.0936 0.0097 0.0078 0.0067 331 GLU A OE2 1956 N N . LYS A 246 ? 0.0676 0.0769 0.0610 -0.0023 0.0036 -0.0042 332 LYS A N 1957 C CA . LYS A 246 ? 0.0745 0.0779 0.0686 -0.0007 0.0027 -0.0071 332 LYS A CA 1958 C C . LYS A 246 ? 0.0782 0.0861 0.0745 0.0050 -0.0016 -0.0041 332 LYS A C 1959 O O . LYS A 246 ? 0.0707 0.0773 0.0754 -0.0029 -0.0012 -0.0079 332 LYS A O 1960 C CB . LYS A 246 ? 0.0917 0.0831 0.0773 0.0055 -0.0075 -0.0145 332 LYS A CB 1961 C CG . LYS A 246 ? 0.0921 0.0990 0.0908 0.0062 -0.0036 0.0038 332 LYS A CG 1962 C CD . LYS A 246 ? 0.1015 0.1133 0.0867 0.0004 0.0078 -0.0075 332 LYS A CD 1963 C CE . LYS A 246 ? 0.1100 0.1293 0.1279 -0.0015 -0.0042 0.0012 332 LYS A CE 1964 N NZ . LYS A 246 ? 0.1286 0.1396 0.1507 -0.0072 -0.0173 -0.0053 332 LYS A NZ 1965 N N . HIS A 247 ? 0.0581 0.0768 0.0737 0.0068 -0.0003 -0.0027 333 HIS A N 1966 C CA . HIS A 247 ? 0.0738 0.0895 0.0858 0.0029 0.0026 -0.0018 333 HIS A CA 1967 C C . HIS A 247 ? 0.0705 0.0820 0.0795 0.0020 -0.0072 0.0066 333 HIS A C 1968 O O . HIS A 247 ? 0.0733 0.0825 0.0736 -0.0050 0.0082 0.0070 333 HIS A O 1969 C CB . HIS A 247 ? 0.0927 0.0826 0.0744 0.0067 -0.0009 -0.0015 333 HIS A CB 1970 C CG . HIS A 247 ? 0.1127 0.0887 0.0881 0.0025 0.0073 -0.0082 333 HIS A CG 1971 N ND1 . HIS A 247 ? 0.1337 0.1256 0.0898 -0.0021 0.0070 -0.0093 333 HIS A ND1 1972 C CD2 . HIS A 247 ? 0.1428 0.1100 0.1120 -0.0034 0.0081 0.0022 333 HIS A CD2 1973 C CE1 . HIS A 247 ? 0.1421 0.1246 0.1202 -0.0026 0.0110 -0.0107 333 HIS A CE1 1974 N NE2 . HIS A 247 ? 0.1522 0.1214 0.1070 0.0025 0.0114 -0.0058 333 HIS A NE2 1975 N N . TYR A 248 ? 0.0673 0.0699 0.0748 -0.0098 0.0092 0.0018 334 TYR A N 1976 C CA . TYR A 248 ? 0.0718 0.0727 0.0782 -0.0003 -0.0062 -0.0008 334 TYR A CA 1977 C C . TYR A 248 ? 0.0753 0.0708 0.0781 -0.0065 0.0025 -0.0038 334 TYR A C 1978 O O . TYR A 248 ? 0.0761 0.0636 0.0655 -0.0050 0.0023 0.0069 334 TYR A O 1979 C CB . TYR A 248 ? 0.0611 0.0607 0.0725 -0.0057 0.0031 -0.0072 334 TYR A CB 1980 C CG . TYR A 248 ? 0.0519 0.0649 0.0664 0.0054 0.0011 0.0030 334 TYR A CG 1981 C CD1 . TYR A 248 ? 0.0655 0.0660 0.0595 -0.0025 0.0047 -0.0053 334 TYR A CD1 1982 C CD2 . TYR A 248 ? 0.0715 0.0730 0.0762 0.0015 0.0111 0.0089 334 TYR A CD2 1983 C CE1 . TYR A 248 ? 0.0682 0.0539 0.0580 -0.0029 0.0069 0.0038 334 TYR A CE1 1984 C CE2 . TYR A 248 ? 0.0733 0.0779 0.0847 -0.0016 0.0029 0.0005 334 TYR A CE2 1985 C CZ . TYR A 248 ? 0.0770 0.0606 0.0594 -0.0039 0.0056 -0.0041 334 TYR A CZ 1986 O OH . TYR A 248 ? 0.0939 0.0682 0.0699 -0.0094 0.0058 -0.0038 334 TYR A OH 1987 N N . ILE A 249 ? 0.0631 0.0791 0.0656 -0.0072 0.0002 -0.0003 335 ILE A N 1988 C CA . ILE A 249 ? 0.0764 0.0838 0.0706 -0.0005 0.0005 -0.0044 335 ILE A CA 1989 C C . ILE A 249 ? 0.0817 0.0816 0.0848 -0.0052 0.0084 -0.0075 335 ILE A C 1990 O O . ILE A 249 ? 0.0744 0.0847 0.0781 -0.0002 -0.0017 0.0021 335 ILE A O 1991 C CB . ILE A 249 ? 0.0649 0.0804 0.0713 0.0007 -0.0001 -0.0008 335 ILE A CB 1992 C CG1 . ILE A 249 ? 0.0840 0.0754 0.0741 -0.0038 0.0128 -0.0091 335 ILE A CG1 1993 C CG2 . ILE A 249 ? 0.0994 0.1178 0.1242 0.0067 0.0003 0.0028 335 ILE A CG2 1994 C CD1 . ILE A 249 ? 0.1163 0.0795 0.1009 0.0184 0.0065 -0.0089 335 ILE A CD1 1995 N N . GLU A 250 ? 0.0827 0.0882 0.0779 -0.0069 0.0013 -0.0056 336 GLU A N 1996 C CA . GLU A 250 ? 0.0766 0.0848 0.0803 -0.0030 -0.0011 -0.0041 336 GLU A CA 1997 C C . GLU A 250 ? 0.0812 0.0825 0.0834 -0.0054 -0.0019 -0.0077 336 GLU A C 1998 O O . GLU A 250 ? 0.1043 0.1128 0.1033 -0.0183 0.0110 -0.0035 336 GLU A O 1999 C CB . GLU A 250 ? 0.0750 0.0796 0.0823 0.0007 0.0035 -0.0061 336 GLU A CB 2000 C CG . GLU A 250 ? 0.0941 0.0923 0.0993 0.0109 -0.0071 0.0000 336 GLU A CG 2001 C CD . GLU A 250 ? 0.1475 0.1282 0.1191 0.0126 -0.0112 -0.0093 336 GLU A CD 2002 O OE1 . GLU A 250 ? 0.1578 0.1312 0.1160 0.0128 -0.0009 -0.0190 336 GLU A OE1 2003 O OE2 . GLU A 250 ? 0.1855 0.1441 0.1475 0.0195 -0.0299 -0.0256 336 GLU A OE2 2004 N N . ALA A 251 ? 0.0847 0.0703 0.0846 -0.0072 -0.0012 -0.0020 337 ALA A N 2005 C CA . ALA A 251 ? 0.0885 0.0726 0.0800 -0.0108 -0.0030 0.0002 337 ALA A CA 2006 C C . ALA A 251 ? 0.0825 0.0790 0.0747 -0.0069 -0.0067 -0.0009 337 ALA A C 2007 O O . ALA A 251 ? 0.1081 0.0937 0.0886 -0.0171 0.0032 0.0050 337 ALA A O 2008 C CB . ALA A 251 ? 0.1056 0.0822 0.0905 -0.0046 -0.0032 -0.0033 337 ALA A CB 2009 N N . PHE A 252 ? 0.0853 0.0624 0.0763 -0.0115 0.0021 0.0053 338 PHE A N 2010 C CA . PHE A 252 ? 0.0800 0.0769 0.0810 -0.0010 0.0062 0.0015 338 PHE A CA 2011 C C . PHE A 252 ? 0.0711 0.0812 0.0738 -0.0124 -0.0029 0.0020 338 PHE A C 2012 O O . PHE A 252 ? 0.0685 0.0880 0.0643 -0.0123 0.0081 0.0067 338 PHE A O 2013 C CB . PHE A 252 ? 0.0802 0.0873 0.1018 -0.0146 0.0075 -0.0119 338 PHE A CB 2014 C CG . PHE A 252 ? 0.0713 0.0843 0.0803 0.0070 0.0176 0.0272 338 PHE A CG 2015 C CD1 . PHE A 252 ? 0.0952 0.0924 0.0518 -0.0046 -0.0090 -0.0170 338 PHE A CD1 2016 C CD2 . PHE A 252 ? 0.0578 0.0754 0.0739 0.0100 -0.0002 0.0030 338 PHE A CD2 2017 C CE1 . PHE A 252 ? 0.0609 0.0644 0.0895 0.0071 0.0138 0.0104 338 PHE A CE1 2018 C CE2 . PHE A 252 ? 0.0716 0.0533 0.1012 0.0031 -0.0020 -0.0183 338 PHE A CE2 2019 C CZ . PHE A 252 ? 0.0639 0.1144 0.0367 0.0115 -0.0017 -0.0087 338 PHE A CZ 2020 N N . ARG A 253 ? 0.0651 0.0760 0.0838 -0.0007 0.0079 0.0008 339 ARG A N 2021 C CA . ARG A 253 ? 0.0581 0.0794 0.0834 -0.0016 0.0073 0.0016 339 ARG A CA 2022 C C . ARG A 253 ? 0.0761 0.0895 0.0833 -0.0072 -0.0029 -0.0045 339 ARG A C 2023 O O . ARG A 253 ? 0.0689 0.1010 0.0951 0.0014 0.0076 0.0000 339 ARG A O 2024 C CB . ARG A 253 ? 0.0724 0.0927 0.0885 0.0010 0.0058 0.0004 339 ARG A CB 2025 C CG . ARG A 253 ? 0.0838 0.1020 0.0952 0.0031 -0.0027 0.0053 339 ARG A CG 2026 C CD . ARG A 253 ? 0.0835 0.1052 0.1090 -0.0064 0.0002 0.0028 339 ARG A CD 2027 N NE . ARG A 253 ? 0.0665 0.1154 0.1182 -0.0008 -0.0007 0.0117 339 ARG A NE 2028 C CZ . ARG A 253 ? 0.1060 0.1127 0.1031 -0.0036 0.0031 -0.0015 339 ARG A CZ 2029 N NH1 . ARG A 253 ? 0.0941 0.1256 0.1168 -0.0062 -0.0040 0.0028 339 ARG A NH1 2030 N NH2 . ARG A 253 ? 0.1116 0.1550 0.1362 -0.0063 -0.0012 0.0017 339 ARG A NH2 2031 N N . PRO A 254 ? 0.0843 0.0847 0.0939 0.0021 0.0046 -0.0007 340 PRO A N 2032 C CA . PRO A 254 ? 0.0792 0.0815 0.0909 0.0003 0.0033 -0.0053 340 PRO A CA 2033 C C . PRO A 254 ? 0.0876 0.0757 0.0949 -0.0048 0.0010 -0.0052 340 PRO A C 2034 O O . PRO A 254 ? 0.0932 0.0972 0.1041 -0.0058 0.0058 -0.0165 340 PRO A O 2035 C CB . PRO A 254 ? 0.1061 0.0914 0.0926 0.0024 -0.0054 0.0012 340 PRO A CB 2036 C CG . PRO A 254 ? 0.1330 0.1432 0.1509 -0.0170 0.0232 -0.0197 340 PRO A CG 2037 C CD . PRO A 254 ? 0.0825 0.0866 0.1030 0.0000 -0.0022 -0.0074 340 PRO A CD 2038 N N . LEU A 255 ? 0.0861 0.0862 0.0823 0.0037 0.0029 -0.0076 341 LEU A N 2039 C CA . LEU A 255 ? 0.0944 0.0920 0.0924 -0.0052 0.0008 0.0031 341 LEU A CA 2040 C C . LEU A 255 ? 0.0924 0.0899 0.0921 0.0036 0.0007 0.0098 341 LEU A C 2041 O O . LEU A 255 ? 0.0984 0.1014 0.0810 -0.0074 0.0116 -0.0101 341 LEU A O 2042 C CB . LEU A 255 ? 0.1111 0.1149 0.1140 0.0047 0.0006 -0.0084 341 LEU A CB 2043 C CG . LEU A 255 ? 0.1538 0.1349 0.1517 0.0122 0.0071 -0.0085 341 LEU A CG 2044 C CD1 . LEU A 255 ? 0.1676 0.1603 0.1842 0.0064 0.0048 -0.0152 341 LEU A CD1 2045 C CD2 . LEU A 255 ? 0.1775 0.1688 0.2022 -0.0045 0.0082 -0.0104 341 LEU A CD2 2046 N N . LEU A 256 ? 0.0703 0.0735 0.0828 -0.0066 0.0028 0.0042 342 LEU A N 2047 C CA . LEU A 256 ? 0.0780 0.0727 0.0741 -0.0058 -0.0009 0.0071 342 LEU A CA 2048 C C . LEU A 256 ? 0.0771 0.0694 0.0698 -0.0051 0.0100 0.0015 342 LEU A C 2049 O O . LEU A 256 ? 0.0650 0.0729 0.0742 -0.0059 0.0154 0.0041 342 LEU A O 2050 C CB . LEU A 256 ? 0.0702 0.0656 0.0672 -0.0080 -0.0015 0.0080 342 LEU A CB 2051 C CG . LEU A 256 ? 0.0683 0.0583 0.0768 0.0020 0.0052 0.0050 342 LEU A CG 2052 C CD1 . LEU A 256 ? 0.0628 0.0664 0.0665 0.0060 -0.0051 0.0069 342 LEU A CD1 2053 C CD2 . LEU A 256 ? 0.0721 0.0706 0.0741 -0.0184 0.0232 0.0012 342 LEU A CD2 2054 N N . GLU A 257 ? 0.0630 0.0797 0.0836 -0.0014 0.0035 0.0037 343 GLU A N 2055 C CA . GLU A 257 ? 0.0685 0.0873 0.0893 -0.0020 0.0021 -0.0013 343 GLU A CA 2056 C C . GLU A 257 ? 0.0877 0.0863 0.0944 -0.0011 0.0080 -0.0022 343 GLU A C 2057 O O . GLU A 257 ? 0.0663 0.0951 0.1049 -0.0098 0.0107 -0.0098 343 GLU A O 2058 C CB . GLU A 257 ? 0.0742 0.1015 0.0974 -0.0056 0.0059 0.0077 343 GLU A CB 2059 C CG . GLU A 257 ? 0.0801 0.1394 0.1196 0.0026 0.0084 -0.0048 343 GLU A CG 2060 C CD . GLU A 257 ? 0.1690 0.2111 0.1704 0.0016 -0.0005 0.0177 343 GLU A CD 2061 O OE1 . GLU A 257 ? 0.1110 0.1883 0.1397 -0.0099 -0.0191 -0.0015 343 GLU A OE1 2062 O OE2 . GLU A 257 ? 0.1952 0.3081 0.2589 -0.0063 -0.0071 0.0185 343 GLU A OE2 2063 N N . ALA A 258 ? 0.0674 0.0814 0.0900 -0.0014 0.0010 0.0017 344 ALA A N 2064 C CA . ALA A 258 ? 0.0770 0.0916 0.0914 -0.0029 0.0035 0.0022 344 ALA A CA 2065 C C . ALA A 258 ? 0.0877 0.0981 0.1003 -0.0062 0.0035 0.0072 344 ALA A C 2066 O O . ALA A 258 ? 0.0970 0.1058 0.1097 -0.0136 0.0234 -0.0011 344 ALA A O 2067 C CB . ALA A 258 ? 0.0950 0.0933 0.0926 -0.0113 0.0100 -0.0005 344 ALA A CB 2068 N N . ARG A 259 ? 0.0743 0.0742 0.0808 -0.0027 0.0053 0.0054 345 ARG A N 2069 C CA . ARG A 259 ? 0.0852 0.0992 0.0980 -0.0061 0.0042 0.0057 345 ARG A CA 2070 C C . ARG A 259 ? 0.0649 0.0833 0.0715 -0.0145 0.0108 0.0011 345 ARG A C 2071 O O . ARG A 259 ? 0.0759 0.1041 0.0932 -0.0111 0.0077 -0.0173 345 ARG A O 2072 C CB . ARG A 259 ? 0.0808 0.0934 0.0892 0.0011 0.0003 -0.0003 345 ARG A CB 2073 C CG . ARG A 259 ? 0.1051 0.0864 0.0779 -0.0023 0.0050 0.0035 345 ARG A CG 2074 C CD . ARG A 259 ? 0.1035 0.0969 0.1261 0.0005 0.0108 0.0059 345 ARG A CD 2075 N NE . ARG A 259 ? 0.1247 0.1111 0.1473 -0.0091 0.0099 0.0056 345 ARG A NE 2076 C CZ . ARG A 259 ? 0.1368 0.1417 0.1502 0.0137 0.0068 0.0014 345 ARG A CZ 2077 N NH1 . ARG A 259 ? 0.1590 0.1384 0.1231 -0.0049 0.0154 0.0055 345 ARG A NH1 2078 N NH2 . ARG A 259 ? 0.1557 0.1552 0.1813 -0.0006 0.0120 0.0131 345 ARG A NH2 2079 N N . GLY A 260 ? 0.0737 0.0662 0.0850 -0.0077 0.0068 -0.0039 346 GLY A N 2080 C CA . GLY A 260 ? 0.0631 0.0742 0.0747 0.0024 0.0053 0.0069 346 GLY A CA 2081 C C . GLY A 260 ? 0.0675 0.0700 0.0778 -0.0048 0.0089 -0.0028 346 GLY A C 2082 O O . GLY A 260 ? 0.0686 0.0716 0.1033 -0.0063 0.0204 0.0077 346 GLY A O 2083 N N . PHE A 261 ? 0.0547 0.0621 0.0800 -0.0065 0.0129 0.0029 347 PHE A N 2084 C CA . PHE A 261 ? 0.0709 0.0714 0.0770 -0.0019 0.0052 0.0075 347 PHE A CA 2085 C C . PHE A 261 ? 0.0631 0.0702 0.0693 -0.0071 0.0090 0.0037 347 PHE A C 2086 O O . PHE A 261 ? 0.0650 0.0802 0.0857 0.0028 0.0172 0.0037 347 PHE A O 2087 C CB . PHE A 261 ? 0.0820 0.0831 0.0745 -0.0093 0.0053 0.0046 347 PHE A CB 2088 C CG . PHE A 261 ? 0.0652 0.0695 0.0773 0.0006 0.0051 -0.0138 347 PHE A CG 2089 C CD1 . PHE A 261 ? 0.0585 0.0879 0.0840 -0.0168 0.0168 0.0126 347 PHE A CD1 2090 C CD2 . PHE A 261 ? 0.0691 0.0846 0.0905 -0.0072 0.0139 0.0061 347 PHE A CD2 2091 C CE1 . PHE A 261 ? 0.0623 0.0619 0.0802 0.0004 0.0035 0.0043 347 PHE A CE1 2092 C CE2 . PHE A 261 ? 0.0610 0.0793 0.0782 -0.0064 -0.0081 -0.0013 347 PHE A CE2 2093 C CZ . PHE A 261 ? 0.0777 0.0754 0.0675 0.0053 0.0102 -0.0003 347 PHE A CZ 2094 N N . PRO A 262 ? 0.0737 0.1012 0.0863 0.0000 0.0128 0.0090 348 PRO A N 2095 C CA . PRO A 262 ? 0.0778 0.0980 0.0858 -0.0041 0.0017 0.0050 348 PRO A CA 2096 C C . PRO A 262 ? 0.0820 0.0926 0.0879 -0.0002 0.0036 0.0103 348 PRO A C 2097 O O . PRO A 262 ? 0.0887 0.1098 0.1000 0.0019 0.0009 0.0087 348 PRO A O 2098 C CB . PRO A 262 ? 0.0963 0.1342 0.0986 -0.0033 0.0022 0.0153 348 PRO A CB 2099 C CG . PRO A 262 ? 0.0708 0.1506 0.1139 0.0048 -0.0037 -0.0056 348 PRO A CG 2100 C CD . PRO A 262 ? 0.0861 0.1276 0.1009 0.0103 0.0109 0.0146 348 PRO A CD 2101 N N . ALA A 263 ? 0.0735 0.0708 0.0763 -0.0082 -0.0076 -0.0016 349 ALA A N 2102 C CA . ALA A 263 ? 0.0675 0.0682 0.0755 -0.0037 0.0004 0.0050 349 ALA A CA 2103 C C . ALA A 263 ? 0.0655 0.0694 0.0762 -0.0015 -0.0024 -0.0019 349 ALA A C 2104 O O . ALA A 263 ? 0.0878 0.0694 0.0747 -0.0013 0.0082 -0.0056 349 ALA A O 2105 C CB . ALA A 263 ? 0.0758 0.0628 0.0641 0.0001 -0.0038 0.0106 349 ALA A CB 2106 N N . GLN A 264 ? 0.0674 0.0636 0.0722 0.0067 -0.0013 -0.0029 350 GLN A N 2107 C CA . GLN A 264 ? 0.0643 0.0699 0.0741 -0.0088 -0.0067 0.0035 350 GLN A CA 2108 C C . GLN A 264 ? 0.0667 0.0862 0.0763 -0.0036 0.0040 0.0015 350 GLN A C 2109 O O . GLN A 264 ? 0.0717 0.1205 0.0894 -0.0069 0.0072 -0.0193 350 GLN A O 2110 C CB . GLN A 264 ? 0.0689 0.0779 0.0904 0.0010 0.0027 0.0052 350 GLN A CB 2111 C CG . GLN A 264 ? 0.0555 0.0717 0.0817 -0.0008 -0.0030 0.0150 350 GLN A CG 2112 C CD . GLN A 264 ? 0.0581 0.0987 0.0942 0.0070 -0.0052 0.0083 350 GLN A CD 2113 O OE1 . GLN A 264 ? 0.1296 0.1279 0.1305 -0.0042 -0.0128 0.0099 350 GLN A OE1 2114 N NE2 . GLN A 264 ? 0.0910 0.1060 0.0999 0.0103 0.0145 0.0111 350 GLN A NE2 2115 N N . PHE A 265 ? 0.0591 0.0766 0.0648 -0.0025 -0.0032 -0.0012 351 PHE A N 2116 C CA . PHE A 265 ? 0.0503 0.0724 0.0646 -0.0046 0.0004 -0.0029 351 PHE A CA 2117 C C . PHE A 265 ? 0.0438 0.0625 0.0610 -0.0008 0.0030 -0.0024 351 PHE A C 2118 O O . PHE A 265 ? 0.0601 0.0760 0.0676 0.0013 0.0046 -0.0024 351 PHE A O 2119 C CB . PHE A 265 ? 0.0652 0.0778 0.0838 -0.0037 0.0075 -0.0038 351 PHE A CB 2120 C CG . PHE A 265 ? 0.0647 0.0822 0.0722 0.0090 0.0052 -0.0051 351 PHE A CG 2121 C CD1 . PHE A 265 ? 0.0691 0.0799 0.0831 -0.0012 -0.0042 0.0048 351 PHE A CD1 2122 C CD2 . PHE A 265 ? 0.0680 0.0689 0.0606 0.0046 -0.0054 -0.0026 351 PHE A CD2 2123 C CE1 . PHE A 265 ? 0.0861 0.0839 0.0951 -0.0053 -0.0120 0.0044 351 PHE A CE1 2124 C CE2 . PHE A 265 ? 0.0643 0.0733 0.0773 0.0072 -0.0055 -0.0068 351 PHE A CE2 2125 C CZ . PHE A 265 ? 0.0744 0.0609 0.0731 0.0045 0.0036 0.0038 351 PHE A CZ 2126 N N . ILE A 266 ? 0.0603 0.0598 0.0527 -0.0029 -0.0014 -0.0081 352 ILE A N 2127 C CA . ILE A 266 ? 0.0476 0.0505 0.0556 -0.0030 -0.0030 0.0000 352 ILE A CA 2128 C C . ILE A 266 ? 0.0543 0.0677 0.0498 0.0050 0.0033 0.0016 352 ILE A C 2129 O O . ILE A 266 ? 0.0530 0.0657 0.0768 0.0033 0.0020 -0.0059 352 ILE A O 2130 C CB . ILE A 266 ? 0.0647 0.0673 0.0553 -0.0031 0.0070 0.0050 352 ILE A CB 2131 C CG1 . ILE A 266 ? 0.0652 0.0658 0.0696 0.0051 0.0000 -0.0020 352 ILE A CG1 2132 C CG2 . ILE A 266 ? 0.0727 0.0788 0.0563 0.0094 -0.0053 0.0026 352 ILE A CG2 2133 C CD1 . ILE A 266 ? 0.0804 0.0827 0.0577 0.0096 0.0009 -0.0067 352 ILE A CD1 2134 N N . VAL A 267 ? 0.0555 0.0536 0.0517 0.0053 0.0019 0.0129 353 VAL A N 2135 C CA . VAL A 267 ? 0.0638 0.0676 0.0506 -0.0002 0.0025 0.0052 353 VAL A CA 2136 C C . VAL A 267 ? 0.0585 0.0721 0.0706 0.0003 -0.0020 0.0032 353 VAL A C 2137 O O . VAL A 267 ? 0.0523 0.0635 0.0628 0.0004 0.0085 -0.0026 353 VAL A O 2138 C CB . VAL A 267 ? 0.0625 0.0557 0.0647 -0.0002 -0.0019 0.0115 353 VAL A CB 2139 C CG1 . VAL A 267 ? 0.0682 0.0718 0.0692 -0.0071 0.0087 -0.0127 353 VAL A CG1 2140 C CG2 . VAL A 267 ? 0.0626 0.0540 0.0689 0.0023 0.0087 -0.0209 353 VAL A CG2 2141 N N . ASP A 268 ? 0.0510 0.0643 0.0602 -0.0083 -0.0019 0.0028 354 ASP A N 2142 C CA . ASP A 268 ? 0.0515 0.0603 0.0493 -0.0029 -0.0004 0.0033 354 ASP A CA 2143 C C . ASP A 268 ? 0.0592 0.0524 0.0602 -0.0040 0.0048 -0.0008 354 ASP A C 2144 O O . ASP A 268 ? 0.0565 0.0532 0.0482 0.0090 -0.0062 0.0013 354 ASP A O 2145 C CB . ASP A 268 ? 0.0529 0.0654 0.0500 0.0000 -0.0005 0.0031 354 ASP A CB 2146 C CG . ASP A 268 ? 0.0680 0.0598 0.0524 0.0004 -0.0076 -0.0001 354 ASP A CG 2147 O OD1 . ASP A 268 ? 0.0625 0.0617 0.0719 0.0007 -0.0084 -0.0032 354 ASP A OD1 2148 O OD2 . ASP A 268 ? 0.0520 0.0494 0.0735 -0.0147 -0.0078 0.0007 354 ASP A OD2 2149 N N . GLN A 269 ? 0.0581 0.0545 0.0510 0.0116 -0.0032 0.0027 355 GLN A N 2150 C CA . GLN A 269 ? 0.0637 0.0692 0.0634 0.0076 0.0000 0.0015 355 GLN A CA 2151 C C . GLN A 269 ? 0.0537 0.0556 0.0536 0.0077 -0.0013 0.0020 355 GLN A C 2152 O O . GLN A 269 ? 0.0572 0.0753 0.0666 0.0000 0.0034 0.0083 355 GLN A O 2153 C CB . GLN A 269 ? 0.0618 0.0763 0.0523 0.0060 0.0004 0.0017 355 GLN A CB 2154 C CG . GLN A 269 ? 0.0615 0.0686 0.0590 0.0013 -0.0035 -0.0193 355 GLN A CG 2155 C CD . GLN A 269 ? 0.0753 0.0739 0.1008 -0.0019 -0.0048 -0.0037 355 GLN A CD 2156 O OE1 . GLN A 269 ? 0.1090 0.0975 0.0979 -0.0019 -0.0042 0.0085 355 GLN A OE1 2157 N NE2 . GLN A 269 ? 0.0795 0.0914 0.0891 -0.0132 0.0164 0.0111 355 GLN A NE2 2158 N N . GLY A 270 ? 0.0581 0.0541 0.0634 -0.0016 0.0051 0.0074 356 GLY A N 2159 C CA . GLY A 270 ? 0.0592 0.0512 0.0596 -0.0051 0.0055 -0.0042 356 GLY A CA 2160 C C . GLY A 270 ? 0.0593 0.0572 0.0650 -0.0007 0.0031 0.0007 356 GLY A C 2161 O O . GLY A 270 ? 0.0637 0.0626 0.0662 0.0007 0.0078 0.0017 356 GLY A O 2162 N N . ARG A 271 ? 0.0440 0.0469 0.0512 -0.0005 0.0081 0.0046 357 ARG A N 2163 C CA . ARG A 271 ? 0.0395 0.0529 0.0488 -0.0015 0.0048 0.0094 357 ARG A CA 2164 C C . ARG A 271 ? 0.0632 0.0728 0.0554 0.0003 0.0103 0.0053 357 ARG A C 2165 O O . ARG A 271 ? 0.0540 0.0596 0.0545 0.0152 0.0017 -0.0082 357 ARG A O 2166 C CB . ARG A 271 ? 0.0449 0.0629 0.0529 -0.0026 0.0113 0.0074 357 ARG A CB 2167 C CG . ARG A 271 ? 0.0704 0.0712 0.0689 -0.0017 -0.0011 0.0102 357 ARG A CG 2168 C CD . ARG A 271 ? 0.0679 0.0767 0.0672 0.0004 0.0098 -0.0016 357 ARG A CD 2169 N NE . ARG A 271 ? 0.0507 0.0632 0.0689 -0.0041 -0.0067 0.0049 357 ARG A NE 2170 C CZ . ARG A 271 ? 0.0801 0.0552 0.0667 -0.0076 -0.0089 0.0045 357 ARG A CZ 2171 N NH1 . ARG A 271 ? 0.0818 0.1157 0.0816 -0.0006 -0.0036 0.0075 357 ARG A NH1 2172 N NH2 . ARG A 271 ? 0.0493 0.0705 0.0623 -0.0077 -0.0048 0.0042 357 ARG A NH2 2173 N N . SER A 272 ? 0.0657 0.0562 0.0576 0.0093 0.0021 -0.0016 358 SER A N 2174 C CA . SER A 272 ? 0.0640 0.0687 0.0700 -0.0066 -0.0004 0.0004 358 SER A CA 2175 C C . SER A 272 ? 0.0776 0.0634 0.0668 -0.0100 -0.0036 0.0031 358 SER A C 2176 O O . SER A 272 ? 0.0812 0.0625 0.0617 -0.0124 0.0002 0.0038 358 SER A O 2177 C CB . SER A 272 ? 0.0608 0.0575 0.0598 0.0046 0.0110 0.0061 358 SER A CB 2178 O OG . SER A 272 ? 0.0702 0.0801 0.0681 0.0037 0.0066 -0.0083 358 SER A OG 2179 N N . GLY A 273 ? 0.0831 0.0701 0.0609 -0.0091 -0.0047 0.0058 359 GLY A N 2180 C CA . GLY A 273 ? 0.0857 0.0823 0.0708 -0.0010 -0.0044 0.0053 359 GLY A CA 2181 C C . GLY A 273 ? 0.0809 0.0737 0.0742 -0.0037 -0.0012 0.0039 359 GLY A C 2182 O O . GLY A 273 ? 0.0981 0.0983 0.0760 0.0041 -0.0025 0.0036 359 GLY A O 2183 N N . LYS A 274 ? 0.0767 0.0747 0.0637 0.0095 0.0099 -0.0032 360 LYS A N 2184 C CA . LYS A 274 ? 0.0886 0.0778 0.0706 0.0059 0.0054 -0.0057 360 LYS A CA 2185 C C . LYS A 274 ? 0.0726 0.0725 0.0707 0.0000 0.0042 -0.0048 360 LYS A C 2186 O O . LYS A 274 ? 0.0844 0.0755 0.0570 0.0003 0.0074 -0.0045 360 LYS A O 2187 C CB . LYS A 274 ? 0.0977 0.0813 0.0729 0.0086 0.0038 0.0064 360 LYS A CB 2188 C CG . LYS A 274 ? 0.1025 0.1101 0.0989 0.0097 -0.0028 -0.0070 360 LYS A CG 2189 C CD . LYS A 274 ? 0.1277 0.1092 0.1142 -0.0018 0.0103 0.0204 360 LYS A CD 2190 C CE . LYS A 274 ? 0.1129 0.1297 0.1167 0.0040 0.0090 0.0044 360 LYS A CE 2191 N NZ . LYS A 274 ? 0.1222 0.1481 0.1315 0.0193 0.0172 0.0151 360 LYS A NZ 2192 N N . GLN A 275 ? 0.0825 0.0832 0.0702 0.0089 0.0053 -0.0124 361 GLN A N 2193 C CA . GLN A 275 ? 0.0825 0.0823 0.0724 0.0038 0.0017 -0.0103 361 GLN A CA 2194 C C . GLN A 275 ? 0.0911 0.1010 0.0751 0.0082 0.0060 -0.0068 361 GLN A C 2195 O O . GLN A 275 ? 0.1157 0.1296 0.0895 0.0188 -0.0022 -0.0034 361 GLN A O 2196 C CB . GLN A 275 ? 0.0853 0.0773 0.0810 0.0069 0.0032 -0.0102 361 GLN A CB 2197 C CG . GLN A 275 ? 0.0763 0.0859 0.0831 0.0102 0.0010 -0.0123 361 GLN A CG 2198 C CD . GLN A 275 ? 0.0638 0.0695 0.0812 -0.0016 -0.0042 -0.0059 361 GLN A CD 2199 O OE1 . GLN A 275 ? 0.1188 0.0871 0.0749 0.0105 -0.0035 0.0004 361 GLN A OE1 2200 N NE2 . GLN A 275 ? 0.0634 0.0712 0.0669 0.0073 0.0089 -0.0033 361 GLN A NE2 2201 N N . PRO A 276 ? 0.0898 0.0971 0.0818 0.0164 0.0071 -0.0094 362 PRO A N 2202 C CA . PRO A 276 ? 0.0935 0.1002 0.0871 0.0065 0.0098 -0.0057 362 PRO A CA 2203 C C . PRO A 276 ? 0.0744 0.0863 0.0813 0.0088 0.0049 -0.0020 362 PRO A C 2204 O O . PRO A 276 ? 0.0950 0.0957 0.0795 -0.0016 0.0058 -0.0102 362 PRO A O 2205 C CB . PRO A 276 ? 0.1077 0.1093 0.1011 -0.0012 0.0047 0.0023 362 PRO A CB 2206 C CG . PRO A 276 ? 0.1616 0.1590 0.1419 0.0156 0.0030 0.0009 362 PRO A CG 2207 C CD . PRO A 276 ? 0.1209 0.1114 0.1034 0.0176 0.0063 -0.0137 362 PRO A CD 2208 N N . THR A 277 ? 0.0737 0.0973 0.0840 0.0032 0.0121 0.0026 363 THR A N 2209 C CA . THR A 277 ? 0.0766 0.0770 0.0668 0.0078 0.0057 0.0018 363 THR A CA 2210 C C . THR A 277 ? 0.0786 0.0773 0.0783 0.0040 0.0032 0.0010 363 THR A C 2211 O O . THR A 277 ? 0.0755 0.0942 0.0820 0.0107 0.0149 -0.0091 363 THR A O 2212 C CB . THR A 277 ? 0.0879 0.0839 0.0825 0.0036 0.0020 0.0035 363 THR A CB 2213 O OG1 . THR A 277 ? 0.0992 0.0930 0.0645 0.0226 0.0120 -0.0028 363 THR A OG1 2214 C CG2 . THR A 277 ? 0.0946 0.0960 0.0836 0.0094 0.0071 -0.0001 363 THR A CG2 2215 N N . GLY A 278 ? 0.0703 0.0791 0.0691 0.0073 0.0024 -0.0020 364 GLY A N 2216 C CA . GLY A 278 ? 0.0781 0.0807 0.0756 0.0072 -0.0012 0.0069 364 GLY A CA 2217 C C . GLY A 278 ? 0.0718 0.0748 0.0723 0.0063 -0.0014 0.0000 364 GLY A C 2218 O O . GLY A 278 ? 0.0781 0.0942 0.0941 0.0123 -0.0080 0.0112 364 GLY A O 2219 N N . GLN A 279 ? 0.0674 0.0772 0.0669 0.0143 0.0030 -0.0024 365 GLN A N 2220 C CA . GLN A 279 ? 0.0688 0.0802 0.0774 0.0011 0.0004 0.0032 365 GLN A CA 2221 C C . GLN A 279 ? 0.0751 0.0911 0.0811 0.0037 0.0036 0.0006 365 GLN A C 2222 O O . GLN A 279 ? 0.0888 0.1018 0.1082 0.0014 0.0066 -0.0022 365 GLN A O 2223 C CB . GLN A 279 ? 0.0815 0.0815 0.0666 0.0066 0.0047 -0.0010 365 GLN A CB 2224 C CG . GLN A 279 ? 0.1053 0.0747 0.0922 0.0075 -0.0101 -0.0081 365 GLN A CG 2225 C CD . GLN A 279 ? 0.0956 0.0637 0.0757 0.0161 0.0031 -0.0036 365 GLN A CD 2226 O OE1 . GLN A 279 ? 0.0820 0.0801 0.0802 -0.0064 0.0047 -0.0106 365 GLN A OE1 2227 N NE2 . GLN A 279 ? 0.1106 0.0819 0.0705 0.0148 0.0116 0.0078 365 GLN A NE2 2228 N N . LYS A 280 ? 0.0848 0.0840 0.0850 -0.0004 -0.0052 -0.0017 366 LYS A N 2229 C CA . LYS A 280 ? 0.0944 0.0907 0.0877 0.0063 -0.0026 -0.0008 366 LYS A CA 2230 C C . LYS A 280 ? 0.0777 0.0814 0.0911 0.0062 0.0025 -0.0053 366 LYS A C 2231 O O . LYS A 280 ? 0.1099 0.1089 0.1073 0.0119 0.0193 -0.0161 366 LYS A O 2232 C CB . LYS A 280 ? 0.1028 0.0993 0.1191 0.0177 0.0014 0.0008 366 LYS A CB 2233 C CG . LYS A 280 ? 0.1627 0.1648 0.1830 0.0035 0.0070 0.0147 366 LYS A CG 2234 C CD . LYS A 280 ? 0.2668 0.2642 0.2512 -0.0087 0.0115 -0.0074 366 LYS A CD 2235 C CE . LYS A 280 ? 0.3244 0.3509 0.3541 0.0109 -0.0001 -0.0002 366 LYS A CE 2236 N NZ . LYS A 280 ? 0.3957 0.4037 0.4086 -0.0175 0.0133 0.0089 366 LYS A NZ 2237 N N . GLU A 281 ? 0.0861 0.0807 0.0846 0.0052 0.0086 0.0074 367 GLU A N 2238 C CA . GLU A 281 ? 0.0783 0.0770 0.0873 0.0015 0.0010 0.0022 367 GLU A CA 2239 C C . GLU A 281 ? 0.0706 0.0766 0.0772 0.0014 0.0003 -0.0009 367 GLU A C 2240 O O . GLU A 281 ? 0.0754 0.0810 0.0822 0.0055 -0.0022 0.0030 367 GLU A O 2241 C CB . GLU A 281 ? 0.0810 0.0869 0.0883 0.0005 -0.0014 0.0050 367 GLU A CB 2242 C CG . GLU A 281 ? 0.0920 0.0956 0.1101 0.0149 0.0008 0.0079 367 GLU A CG 2243 C CD . GLU A 281 ? 0.0952 0.1141 0.1093 0.0051 -0.0014 0.0059 367 GLU A CD 2244 O OE1 . GLU A 281 ? 0.1258 0.0843 0.1398 -0.0040 -0.0064 0.0098 367 GLU A OE1 2245 O OE2 . GLU A 281 ? 0.1175 0.1218 0.1280 0.0241 0.0142 0.0140 367 GLU A OE2 2246 N N . TRP A 282 ? 0.0663 0.0764 0.0867 0.0048 -0.0025 -0.0003 368 TRP A N 2247 C CA . TRP A 282 ? 0.0799 0.0862 0.0806 0.0051 0.0040 -0.0023 368 TRP A CA 2248 C C . TRP A 282 ? 0.0683 0.0795 0.0744 -0.0003 0.0051 0.0062 368 TRP A C 2249 O O . TRP A 282 ? 0.0855 0.0775 0.0975 -0.0024 0.0060 -0.0022 368 TRP A O 2250 C CB . TRP A 282 ? 0.0610 0.0715 0.0816 0.0067 0.0004 0.0011 368 TRP A CB 2251 C CG . TRP A 282 ? 0.0704 0.0822 0.0753 0.0028 0.0001 0.0057 368 TRP A CG 2252 C CD1 . TRP A 282 ? 0.0729 0.0991 0.1048 -0.0024 0.0116 0.0153 368 TRP A CD1 2253 C CD2 . TRP A 282 ? 0.0675 0.0687 0.0623 -0.0029 -0.0002 0.0021 368 TRP A CD2 2254 N NE1 . TRP A 282 ? 0.0609 0.0853 0.0830 0.0112 -0.0020 0.0001 368 TRP A NE1 2255 C CE2 . TRP A 282 ? 0.0622 0.0856 0.0714 -0.0014 0.0113 0.0015 368 TRP A CE2 2256 C CE3 . TRP A 282 ? 0.0960 0.0852 0.1072 0.0011 0.0069 0.0083 368 TRP A CE3 2257 C CZ2 . TRP A 282 ? 0.0742 0.0813 0.0777 -0.0059 0.0121 -0.0012 368 TRP A CZ2 2258 C CZ3 . TRP A 282 ? 0.0862 0.0819 0.0890 0.0042 0.0153 -0.0067 368 TRP A CZ3 2259 C CH2 . TRP A 282 ? 0.1006 0.0925 0.1034 -0.0028 0.0129 0.0056 368 TRP A CH2 2260 N N . GLY A 283 ? 0.0750 0.0820 0.0797 -0.0025 0.0021 0.0035 369 GLY A N 2261 C CA . GLY A 283 ? 0.0943 0.0827 0.0761 0.0074 0.0082 0.0004 369 GLY A CA 2262 C C . GLY A 283 ? 0.0905 0.0915 0.0761 -0.0010 -0.0005 -0.0027 369 GLY A C 2263 O O . GLY A 283 ? 0.1259 0.0983 0.1057 -0.0087 -0.0089 -0.0054 369 GLY A O 2264 N N . HIS A 284 ? 0.0833 0.0894 0.0790 -0.0093 0.0077 -0.0024 370 HIS A N 2265 C CA . HIS A 284 ? 0.0888 0.0831 0.0844 0.0017 -0.0035 -0.0002 370 HIS A CA 2266 C C . HIS A 284 ? 0.0838 0.0798 0.0785 0.0048 -0.0059 0.0017 370 HIS A C 2267 O O . HIS A 284 ? 0.0990 0.1034 0.0789 0.0105 -0.0078 -0.0002 370 HIS A O 2268 C CB . HIS A 284 ? 0.0931 0.0708 0.0927 -0.0057 0.0031 0.0015 370 HIS A CB 2269 C CG . HIS A 284 ? 0.0801 0.0975 0.0915 -0.0023 -0.0050 -0.0018 370 HIS A CG 2270 N ND1 . HIS A 284 ? 0.0956 0.1027 0.1242 0.0032 -0.0015 0.0021 370 HIS A ND1 2271 C CD2 . HIS A 284 ? 0.0714 0.1160 0.1149 -0.0090 0.0070 0.0005 370 HIS A CD2 2272 C CE1 . HIS A 284 ? 0.0794 0.0938 0.1198 -0.0021 0.0052 0.0026 370 HIS A CE1 2273 N NE2 . HIS A 284 ? 0.0956 0.0793 0.0900 -0.0022 -0.0062 0.0002 370 HIS A NE2 2274 N N . TRP A 285 ? 0.0724 0.0791 0.0645 0.0036 -0.0046 0.0035 371 TRP A N 2275 C CA . TRP A 285 ? 0.0746 0.0722 0.0701 0.0075 0.0022 0.0021 371 TRP A CA 2276 C C . TRP A 285 ? 0.0785 0.0851 0.0692 0.0008 -0.0010 -0.0047 371 TRP A C 2277 O O . TRP A 285 ? 0.0918 0.0788 0.0881 0.0074 0.0003 0.0022 371 TRP A O 2278 C CB . TRP A 285 ? 0.0789 0.0802 0.0737 -0.0120 0.0068 0.0017 371 TRP A CB 2279 C CG . TRP A 285 ? 0.0645 0.0867 0.0853 -0.0059 0.0099 0.0089 371 TRP A CG 2280 C CD1 . TRP A 285 ? 0.1074 0.1019 0.1049 0.0074 0.0006 0.0002 371 TRP A CD1 2281 C CD2 . TRP A 285 ? 0.0959 0.1051 0.0869 0.0028 0.0065 0.0079 371 TRP A CD2 2282 N NE1 . TRP A 285 ? 0.1200 0.1064 0.1065 0.0056 -0.0067 0.0056 371 TRP A NE1 2283 C CE2 . TRP A 285 ? 0.0517 0.0821 0.0745 -0.0098 0.0025 -0.0084 371 TRP A CE2 2284 C CE3 . TRP A 285 ? 0.0955 0.1277 0.1021 -0.0045 0.0016 -0.0067 371 TRP A CE3 2285 C CZ2 . TRP A 285 ? 0.0971 0.1002 0.0886 0.0022 -0.0153 -0.0083 371 TRP A CZ2 2286 C CZ3 . TRP A 285 ? 0.1067 0.0824 0.0946 0.0024 0.0029 0.0115 371 TRP A CZ3 2287 C CH2 . TRP A 285 ? 0.0900 0.1166 0.1049 -0.0232 -0.0073 -0.0008 371 TRP A CH2 2288 N N . CYS A 286 ? 0.0794 0.0789 0.0775 0.0047 -0.0010 0.0019 372 CYS A N 2289 C CA . CYS A 286 ? 0.0794 0.0799 0.0753 0.0032 0.0026 -0.0019 372 CYS A CA 2290 C C . CYS A 286 ? 0.0787 0.0771 0.0735 0.0051 0.0030 0.0034 372 CYS A C 2291 O O . CYS A 286 ? 0.0736 0.0858 0.0869 0.0031 0.0156 0.0107 372 CYS A O 2292 C CB . CYS A 286 ? 0.0650 0.0795 0.0838 -0.0090 -0.0028 0.0126 372 CYS A CB 2293 S SG . CYS A 286 ? 0.0864 0.0883 0.0966 -0.0015 -0.0112 0.0004 372 CYS A SG 2294 N N . ASN A 287 ? 0.0708 0.0747 0.0678 0.0097 0.0135 0.0002 373 ASN A N 2295 C CA . ASN A 287 ? 0.0702 0.0644 0.0631 0.0026 0.0038 0.0031 373 ASN A CA 2296 C C . ASN A 287 ? 0.0696 0.0727 0.0756 -0.0011 0.0029 -0.0005 373 ASN A C 2297 O O . ASN A 287 ? 0.0684 0.0850 0.0741 -0.0020 0.0043 -0.0012 373 ASN A O 2298 C CB . ASN A 287 ? 0.0768 0.0763 0.0470 0.0020 -0.0101 0.0015 373 ASN A CB 2299 C CG . ASN A 287 ? 0.0676 0.0696 0.0703 0.0160 -0.0091 -0.0011 373 ASN A CG 2300 O OD1 . ASN A 287 ? 0.0780 0.0811 0.0890 0.0008 0.0095 -0.0056 373 ASN A OD1 2301 N ND2 . ASN A 287 ? 0.0736 0.0897 0.0770 -0.0034 -0.0079 0.0022 373 ASN A ND2 2302 N N . ALA A 288 ? 0.0733 0.0650 0.0732 0.0011 -0.0020 -0.0031 374 ALA A N 2303 C CA . ALA A 288 ? 0.0595 0.0688 0.0608 0.0061 0.0069 -0.0010 374 ALA A CA 2304 C C . ALA A 288 ? 0.0730 0.0774 0.0697 0.0017 0.0015 0.0036 374 ALA A C 2305 O O . ALA A 288 ? 0.0549 0.0726 0.0639 0.0000 -0.0018 -0.0031 374 ALA A O 2306 C CB . ALA A 288 ? 0.0894 0.0766 0.0675 -0.0005 -0.0009 -0.0008 374 ALA A CB 2307 N N . ILE A 289 ? 0.0726 0.0813 0.0763 0.0073 0.0092 0.0052 375 ILE A N 2308 C CA . ILE A 289 ? 0.0838 0.0888 0.0730 0.0041 -0.0018 -0.0012 375 ILE A CA 2309 C C . ILE A 289 ? 0.0879 0.0920 0.0870 -0.0005 0.0053 0.0002 375 ILE A C 2310 O O . ILE A 289 ? 0.0798 0.0823 0.0677 -0.0057 -0.0040 -0.0091 375 ILE A O 2311 C CB . ILE A 289 ? 0.0782 0.0927 0.0821 -0.0003 0.0024 0.0012 375 ILE A CB 2312 C CG1 . ILE A 289 ? 0.0969 0.1196 0.0984 0.0112 0.0138 0.0126 375 ILE A CG1 2313 C CG2 . ILE A 289 ? 0.0773 0.1038 0.0869 0.0067 -0.0009 0.0090 375 ILE A CG2 2314 C CD1 . ILE A 289 ? 0.1073 0.1464 0.1038 0.0167 0.0015 -0.0042 375 ILE A CD1 2315 N N . GLY A 290 ? 0.1023 0.0928 0.0949 0.0020 0.0012 0.0040 376 GLY A N 2316 C CA . GLY A 290 ? 0.0828 0.0867 0.0799 0.0044 0.0025 0.0076 376 GLY A CA 2317 C C . GLY A 290 ? 0.0775 0.0782 0.0793 -0.0029 0.0051 -0.0029 376 GLY A C 2318 O O . GLY A 290 ? 0.0736 0.0825 0.0765 -0.0082 0.0018 -0.0027 376 GLY A O 2319 N N . THR A 291 ? 0.0755 0.0826 0.0927 -0.0038 0.0018 0.0036 377 THR A N 2320 C CA . THR A 291 ? 0.0672 0.0775 0.0662 0.0014 0.0020 -0.0009 377 THR A CA 2321 C C . THR A 291 ? 0.0742 0.0775 0.0669 -0.0047 0.0022 -0.0060 377 THR A C 2322 O O . THR A 291 ? 0.0727 0.0758 0.0619 -0.0003 0.0134 0.0038 377 THR A O 2323 C CB . THR A 291 ? 0.0697 0.0760 0.0692 0.0057 0.0018 -0.0011 377 THR A CB 2324 O OG1 . THR A 291 ? 0.0745 0.0879 0.0722 -0.0122 0.0134 0.0059 377 THR A OG1 2325 C CG2 . THR A 291 ? 0.0906 0.0891 0.0949 -0.0003 0.0011 0.0079 377 THR A CG2 2326 N N . GLY A 292 ? 0.0743 0.0756 0.0646 0.0071 0.0051 -0.0018 378 GLY A N 2327 C CA . GLY A 292 ? 0.0599 0.0603 0.0549 -0.0008 0.0002 -0.0047 378 GLY A CA 2328 C C . GLY A 292 ? 0.0594 0.0634 0.0600 -0.0046 -0.0025 0.0052 378 GLY A C 2329 O O . GLY A 292 ? 0.0650 0.0677 0.0707 -0.0042 -0.0014 0.0105 378 GLY A O 2330 N N . PHE A 293 ? 0.0733 0.0636 0.0598 0.0046 -0.0007 0.0000 379 PHE A N 2331 C CA . PHE A 293 ? 0.0681 0.0665 0.0608 0.0026 0.0025 -0.0012 379 PHE A CA 2332 C C . PHE A 293 ? 0.0859 0.0683 0.0734 0.0002 0.0015 0.0011 379 PHE A C 2333 O O . PHE A 293 ? 0.0806 0.0799 0.0662 0.0041 0.0046 0.0000 379 PHE A O 2334 C CB . PHE A 293 ? 0.0927 0.0769 0.0835 0.0072 0.0075 -0.0016 379 PHE A CB 2335 C CG . PHE A 293 ? 0.0838 0.0895 0.0861 0.0060 -0.0055 0.0049 379 PHE A CG 2336 C CD1 . PHE A 293 ? 0.0736 0.0775 0.0854 0.0066 -0.0025 0.0064 379 PHE A CD1 2337 C CD2 . PHE A 293 ? 0.0922 0.0798 0.0878 0.0066 -0.0102 0.0092 379 PHE A CD2 2338 C CE1 . PHE A 293 ? 0.0919 0.0880 0.0621 0.0055 0.0063 0.0000 379 PHE A CE1 2339 C CE2 . PHE A 293 ? 0.0982 0.0795 0.1013 0.0037 -0.0035 0.0085 379 PHE A CE2 2340 C CZ . PHE A 293 ? 0.1011 0.0665 0.0918 -0.0159 -0.0093 -0.0029 379 PHE A CZ 2341 N N . GLY A 294 ? 0.0728 0.0728 0.0787 0.0051 -0.0002 0.0006 380 GLY A N 2342 C CA . GLY A 294 ? 0.0766 0.0779 0.0848 -0.0009 -0.0071 0.0032 380 GLY A CA 2343 C C . GLY A 294 ? 0.0898 0.0869 0.0911 0.0028 0.0035 0.0025 380 GLY A C 2344 O O . GLY A 294 ? 0.0848 0.0930 0.0967 0.0085 -0.0016 -0.0009 380 GLY A O 2345 N N A MET A 295 ? 0.0919 0.0997 0.0972 0.0116 -0.0083 0.0033 381 MET A N 2346 N N B MET A 295 ? 0.0930 0.0981 0.0966 0.0069 -0.0053 0.0021 381 MET A N 2347 C CA A MET A 295 ? 0.1047 0.1246 0.1174 0.0059 -0.0002 -0.0027 381 MET A CA 2348 C CA B MET A 295 ? 0.1028 0.1148 0.1121 0.0034 -0.0015 -0.0018 381 MET A CA 2349 C C A MET A 295 ? 0.1007 0.1119 0.1103 0.0110 -0.0033 0.0004 381 MET A C 2350 C C B MET A 295 ? 0.1008 0.1107 0.1070 0.0073 -0.0029 0.0003 381 MET A C 2351 O O A MET A 295 ? 0.0801 0.1243 0.0963 0.0081 -0.0019 -0.0163 381 MET A O 2352 O O B MET A 295 ? 0.0861 0.1199 0.1002 0.0063 -0.0026 -0.0097 381 MET A O 2353 C CB A MET A 295 ? 0.1320 0.1246 0.1309 0.0103 0.0000 -0.0081 381 MET A CB 2354 C CB B MET A 295 ? 0.1169 0.1184 0.1164 0.0071 -0.0021 0.0016 381 MET A CB 2355 C CG A MET A 295 ? 0.1430 0.1441 0.1370 -0.0047 0.0094 0.0049 381 MET A CG 2356 C CG B MET A 295 ? 0.1517 0.1318 0.1351 0.0029 0.0013 -0.0049 381 MET A CG 2357 S SD A MET A 295 ? 0.1723 0.2294 0.1626 -0.0283 0.0239 0.0129 381 MET A SD 2358 S SD B MET A 295 ? 0.2221 0.2058 0.2109 -0.0222 -0.0070 -0.0236 381 MET A SD 2359 C CE A MET A 295 ? 0.2315 0.2191 0.2109 -0.0066 -0.0055 -0.0154 381 MET A CE 2360 C CE B MET A 295 ? 0.1717 0.1931 0.1825 -0.0114 0.0042 0.0043 381 MET A CE 2361 N N . ARG A 296 ? 0.1008 0.1203 0.1005 0.0095 -0.0059 -0.0005 382 ARG A N 2362 C CA . ARG A 296 ? 0.1058 0.1052 0.1031 0.0038 -0.0080 0.0004 382 ARG A CA 2363 C C . ARG A 296 ? 0.0893 0.0791 0.0897 0.0009 -0.0101 0.0054 382 ARG A C 2364 O O . ARG A 296 ? 0.0941 0.0853 0.1200 0.0051 -0.0087 0.0050 382 ARG A O 2365 C CB A ARG A 296 ? 0.1074 0.1097 0.1148 0.0014 -0.0033 0.0062 382 ARG A CB 2366 C CB B ARG A 296 ? 0.1055 0.1079 0.1123 0.0013 -0.0028 0.0059 382 ARG A CB 2367 C CG A ARG A 296 ? 0.1353 0.1401 0.1253 0.0011 0.0024 0.0099 382 ARG A CG 2368 C CG B ARG A 296 ? 0.1276 0.1336 0.1189 0.0011 0.0016 0.0100 382 ARG A CG 2369 C CD A ARG A 296 ? 0.1376 0.1401 0.1400 -0.0058 0.0053 -0.0015 382 ARG A CD 2370 C CD B ARG A 296 ? 0.1230 0.1252 0.1216 -0.0071 0.0091 -0.0005 382 ARG A CD 2371 N NE A ARG A 296 ? 0.1602 0.1458 0.1237 0.0004 0.0013 -0.0061 382 ARG A NE 2372 N NE B ARG A 296 ? 0.1117 0.1221 0.1014 0.0068 0.0010 -0.0018 382 ARG A NE 2373 C CZ A ARG A 296 ? 0.1337 0.1468 0.1570 -0.0020 -0.0036 -0.0009 382 ARG A CZ 2374 C CZ B ARG A 296 ? 0.1224 0.1334 0.1372 -0.0012 0.0046 0.0075 382 ARG A CZ 2375 N NH1 A ARG A 296 ? 0.1558 0.1443 0.1414 -0.0090 0.0044 0.0056 382 ARG A NH1 2376 N NH1 B ARG A 296 ? 0.1392 0.1408 0.1487 -0.0017 0.0072 0.0099 382 ARG A NH1 2377 N NH2 A ARG A 296 ? 0.1701 0.1739 0.1482 -0.0011 -0.0023 0.0009 382 ARG A NH2 2378 N NH2 B ARG A 296 ? 0.1274 0.1413 0.1191 -0.0029 -0.0044 -0.0038 382 ARG A NH2 2379 N N . PRO A 297 ? 0.0866 0.0795 0.0892 0.0032 -0.0048 0.0040 383 PRO A N 2380 C CA . PRO A 297 ? 0.0842 0.0825 0.0911 0.0057 -0.0073 0.0072 383 PRO A CA 2381 C C . PRO A 297 ? 0.0857 0.0869 0.0927 -0.0031 -0.0046 0.0110 383 PRO A C 2382 O O . PRO A 297 ? 0.0967 0.0988 0.1121 0.0135 -0.0165 0.0176 383 PRO A O 2383 C CB . PRO A 297 ? 0.0951 0.0863 0.0989 0.0014 -0.0004 0.0058 383 PRO A CB 2384 C CG . PRO A 297 ? 0.0839 0.0869 0.0937 0.0002 -0.0009 0.0011 383 PRO A CG 2385 C CD . PRO A 297 ? 0.0875 0.0984 0.1007 0.0044 -0.0070 -0.0027 383 PRO A CD 2386 N N . THR A 298 ? 0.0724 0.0843 0.0900 0.0028 -0.0121 0.0136 384 THR A N 2387 C CA . THR A 298 ? 0.0847 0.0886 0.0888 -0.0005 -0.0107 0.0044 384 THR A CA 2388 C C . THR A 298 ? 0.0852 0.0983 0.0964 -0.0028 -0.0061 0.0022 384 THR A C 2389 O O . THR A 298 ? 0.0703 0.0977 0.0837 -0.0033 -0.0134 0.0084 384 THR A O 2390 C CB . THR A 298 ? 0.0840 0.1121 0.0957 0.0110 -0.0126 0.0148 384 THR A CB 2391 O OG1 . THR A 298 ? 0.1145 0.1400 0.1287 -0.0155 -0.0171 0.0105 384 THR A OG1 2392 C CG2 . THR A 298 ? 0.1241 0.1181 0.1036 -0.0136 -0.0068 -0.0153 384 THR A CG2 2393 N N . ALA A 299 ? 0.0924 0.0978 0.0944 0.0079 -0.0102 0.0074 385 ALA A N 2394 C CA . ALA A 299 ? 0.1069 0.1150 0.1082 0.0010 -0.0047 -0.0019 385 ALA A CA 2395 C C . ALA A 299 ? 0.1096 0.1159 0.1217 -0.0068 -0.0121 0.0049 385 ALA A C 2396 O O . ALA A 299 ? 0.1078 0.1485 0.1326 -0.0162 -0.0151 0.0140 385 ALA A O 2397 C CB . ALA A 299 ? 0.1182 0.1314 0.1208 0.0074 -0.0084 0.0012 385 ALA A CB 2398 N N . ASN A 300 ? 0.0946 0.0977 0.1181 -0.0020 -0.0134 -0.0018 386 ASN A N 2399 C CA . ASN A 300 ? 0.1388 0.1331 0.1241 -0.0047 -0.0093 -0.0001 386 ASN A CA 2400 C C . ASN A 300 ? 0.1174 0.1191 0.1027 -0.0046 -0.0084 0.0015 386 ASN A C 2401 O O . ASN A 300 ? 0.1555 0.1230 0.1156 0.0043 0.0017 0.0123 386 ASN A O 2402 C CB . ASN A 300 ? 0.1607 0.1584 0.1468 -0.0039 -0.0078 0.0028 386 ASN A CB 2403 C CG . ASN A 300 ? 0.1967 0.1859 0.1809 -0.0025 -0.0047 0.0086 386 ASN A CG 2404 O OD1 . ASN A 300 ? 0.1862 0.2319 0.2302 0.0095 -0.0198 0.0219 386 ASN A OD1 2405 N ND2 . ASN A 300 ? 0.2306 0.1951 0.2205 -0.0043 -0.0311 0.0211 386 ASN A ND2 2406 N N . THR A 301 ? 0.1108 0.1143 0.0963 -0.0044 0.0005 -0.0021 387 THR A N 2407 C CA . THR A 301 ? 0.1037 0.1026 0.0857 -0.0044 -0.0021 0.0006 387 THR A CA 2408 C C . THR A 301 ? 0.0930 0.0973 0.0854 0.0003 -0.0046 -0.0024 387 THR A C 2409 O O . THR A 301 ? 0.0977 0.1311 0.1152 0.0064 -0.0160 -0.0137 387 THR A O 2410 C CB . THR A 301 ? 0.0998 0.1009 0.0876 -0.0031 -0.0067 0.0030 387 THR A CB 2411 O OG1 . THR A 301 ? 0.1133 0.1061 0.0913 -0.0100 0.0064 -0.0022 387 THR A OG1 2412 C CG2 . THR A 301 ? 0.1124 0.1193 0.1004 -0.0111 0.0056 -0.0057 387 THR A CG2 2413 N N . GLY A 302 ? 0.0906 0.0927 0.0831 -0.0049 -0.0134 -0.0002 388 GLY A N 2414 C CA . GLY A 302 ? 0.1030 0.0908 0.0848 -0.0071 0.0023 0.0002 388 GLY A CA 2415 C C . GLY A 302 ? 0.0869 0.0809 0.0762 -0.0055 -0.0018 -0.0037 388 GLY A C 2416 O O . GLY A 302 ? 0.1195 0.1051 0.0901 -0.0205 -0.0032 -0.0116 388 GLY A O 2417 N N . HIS A 303 ? 0.0761 0.0665 0.0629 -0.0047 -0.0052 0.0022 389 HIS A N 2418 C CA . HIS A 303 ? 0.0776 0.0709 0.0703 -0.0030 -0.0060 -0.0031 389 HIS A CA 2419 C C . HIS A 303 ? 0.0888 0.0846 0.0805 -0.0011 -0.0046 0.0009 389 HIS A C 2420 O O . HIS A 303 ? 0.0981 0.1009 0.0937 -0.0101 0.0017 -0.0123 389 HIS A O 2421 C CB . HIS A 303 ? 0.0809 0.0776 0.0643 -0.0042 -0.0104 -0.0125 389 HIS A CB 2422 C CG . HIS A 303 ? 0.0564 0.0756 0.0624 -0.0081 -0.0152 -0.0053 389 HIS A CG 2423 N ND1 . HIS A 303 ? 0.0846 0.0827 0.0871 -0.0093 -0.0102 -0.0104 389 HIS A ND1 2424 C CD2 . HIS A 303 ? 0.1033 0.1020 0.0978 -0.0078 -0.0066 -0.0022 389 HIS A CD2 2425 C CE1 . HIS A 303 ? 0.1028 0.1084 0.0925 0.0095 -0.0121 -0.0067 389 HIS A CE1 2426 N NE2 . HIS A 303 ? 0.0896 0.1041 0.0722 0.0056 -0.0044 0.0099 389 HIS A NE2 2427 N N . GLN A 304 ? 0.0900 0.1001 0.0865 -0.0002 -0.0090 -0.0017 390 GLN A N 2428 C CA . GLN A 304 ? 0.1011 0.1128 0.0900 -0.0014 -0.0071 -0.0006 390 GLN A CA 2429 C C . GLN A 304 ? 0.0840 0.0953 0.0829 0.0010 -0.0051 -0.0098 390 GLN A C 2430 O O . GLN A 304 ? 0.1055 0.1291 0.1005 0.0101 -0.0134 -0.0090 390 GLN A O 2431 C CB . GLN A 304 ? 0.0990 0.1250 0.1061 -0.0054 -0.0057 -0.0003 390 GLN A CB 2432 C CG . GLN A 304 ? 0.1339 0.1266 0.1379 -0.0112 -0.0061 -0.0061 390 GLN A CG 2433 C CD . GLN A 304 ? 0.1805 0.1628 0.2078 -0.0143 -0.0146 0.0082 390 GLN A CD 2434 O OE1 . GLN A 304 ? 0.1971 0.2175 0.2576 -0.0111 0.0095 0.0157 390 GLN A OE1 2435 N NE2 . GLN A 304 ? 0.2052 0.1746 0.2043 -0.0178 -0.0141 -0.0001 390 GLN A NE2 2436 N N . TYR A 305 ? 0.0962 0.0971 0.0817 -0.0007 -0.0055 -0.0074 391 TYR A N 2437 C CA . TYR A 305 ? 0.0823 0.0857 0.0731 -0.0076 -0.0061 0.0034 391 TYR A CA 2438 C C . TYR A 305 ? 0.0840 0.0810 0.0715 -0.0053 -0.0068 0.0018 391 TYR A C 2439 O O . TYR A 305 ? 0.0792 0.0937 0.0738 -0.0036 -0.0090 -0.0056 391 TYR A O 2440 C CB . TYR A 305 ? 0.0879 0.0943 0.0885 -0.0024 -0.0047 0.0036 391 TYR A CB 2441 C CG . TYR A 305 ? 0.1117 0.1140 0.0857 -0.0025 -0.0112 0.0056 391 TYR A CG 2442 C CD1 . TYR A 305 ? 0.1252 0.1202 0.1125 -0.0164 0.0018 -0.0078 391 TYR A CD1 2443 C CD2 . TYR A 305 ? 0.1237 0.1311 0.0931 -0.0168 0.0018 -0.0006 391 TYR A CD2 2444 C CE1 . TYR A 305 ? 0.1446 0.1506 0.1469 -0.0111 0.0059 0.0037 391 TYR A CE1 2445 C CE2 . TYR A 305 ? 0.1714 0.1191 0.1247 -0.0107 -0.0026 0.0003 391 TYR A CE2 2446 C CZ . TYR A 305 ? 0.1636 0.1356 0.1300 -0.0214 -0.0074 0.0048 391 TYR A CZ 2447 O OH . TYR A 305 ? 0.2104 0.1743 0.2214 -0.0457 -0.0080 -0.0009 391 TYR A OH 2448 N N . VAL A 306 ? 0.0558 0.0631 0.0538 -0.0020 -0.0039 -0.0009 392 VAL A N 2449 C CA . VAL A 306 ? 0.0684 0.0679 0.0650 -0.0003 -0.0054 0.0027 392 VAL A CA 2450 C C . VAL A 306 ? 0.0683 0.0666 0.0652 0.0006 -0.0009 -0.0013 392 VAL A C 2451 O O . VAL A 306 ? 0.0748 0.0935 0.0851 -0.0015 -0.0151 -0.0062 392 VAL A O 2452 C CB . VAL A 306 ? 0.0734 0.0785 0.0617 0.0031 -0.0155 -0.0027 392 VAL A CB 2453 C CG1 . VAL A 306 ? 0.0720 0.0764 0.0954 0.0072 0.0071 0.0109 392 VAL A CG1 2454 C CG2 . VAL A 306 ? 0.0907 0.0793 0.0966 0.0074 0.0013 -0.0010 392 VAL A CG2 2455 N N . ASP A 307 ? 0.0652 0.0801 0.0690 -0.0019 -0.0102 0.0002 393 ASP A N 2456 C CA . ASP A 307 ? 0.0738 0.0734 0.0655 0.0022 0.0003 -0.0008 393 ASP A CA 2457 C C . ASP A 307 ? 0.0599 0.0691 0.0706 -0.0030 -0.0065 -0.0031 393 ASP A C 2458 O O . ASP A 307 ? 0.0856 0.1071 0.0909 0.0012 -0.0104 -0.0008 393 ASP A O 2459 C CB . ASP A 307 ? 0.0662 0.0609 0.0615 0.0101 -0.0011 0.0039 393 ASP A CB 2460 C CG . ASP A 307 ? 0.0575 0.0769 0.0753 0.0069 -0.0009 -0.0040 393 ASP A CG 2461 O OD1 . ASP A 307 ? 0.0597 0.0713 0.0838 0.0063 0.0051 -0.0073 393 ASP A OD1 2462 O OD2 . ASP A 307 ? 0.0648 0.0702 0.0869 0.0075 0.0002 -0.0016 393 ASP A OD2 2463 N N . ALA A 308 ? 0.0633 0.0773 0.0696 0.0003 -0.0020 -0.0015 394 ALA A N 2464 C CA . ALA A 308 ? 0.0724 0.0736 0.0722 0.0050 -0.0035 -0.0011 394 ALA A CA 2465 C C . ALA A 308 ? 0.0581 0.0648 0.0633 -0.0028 -0.0087 -0.0026 394 ALA A C 2466 O O . ALA A 308 ? 0.0746 0.0554 0.0623 -0.0037 -0.0077 0.0031 394 ALA A O 2467 C CB . ALA A 308 ? 0.0720 0.0690 0.0742 -0.0015 0.0018 0.0062 394 ALA A CB 2468 N N . PHE A 309 ? 0.0584 0.0635 0.0495 -0.0075 -0.0133 -0.0041 395 PHE A N 2469 C CA . PHE A 309 ? 0.0733 0.0622 0.0642 0.0000 0.0024 -0.0016 395 PHE A CA 2470 C C . PHE A 309 ? 0.0716 0.0740 0.0803 0.0001 -0.0029 -0.0052 395 PHE A C 2471 O O . PHE A 309 ? 0.0847 0.0818 0.0747 -0.0061 -0.0077 0.0046 395 PHE A O 2472 C CB . PHE A 309 ? 0.0804 0.0750 0.0625 -0.0061 0.0067 -0.0064 395 PHE A CB 2473 C CG . PHE A 309 ? 0.0838 0.0792 0.0972 -0.0055 0.0006 -0.0012 395 PHE A CG 2474 C CD1 . PHE A 309 ? 0.1022 0.0933 0.0899 -0.0083 -0.0054 -0.0002 395 PHE A CD1 2475 C CD2 . PHE A 309 ? 0.1038 0.1027 0.1119 0.0089 -0.0055 -0.0044 395 PHE A CD2 2476 C CE1 . PHE A 309 ? 0.1418 0.1056 0.1116 0.0056 0.0059 -0.0004 395 PHE A CE1 2477 C CE2 . PHE A 309 ? 0.1075 0.1326 0.1303 -0.0005 -0.0179 -0.0053 395 PHE A CE2 2478 C CZ . PHE A 309 ? 0.1205 0.0958 0.1420 -0.0055 -0.0014 -0.0245 395 PHE A CZ 2479 N N . VAL A 310 ? 0.0621 0.0567 0.0567 -0.0010 0.0009 -0.0095 396 VAL A N 2480 C CA . VAL A 310 ? 0.0645 0.0599 0.0633 0.0004 -0.0061 0.0040 396 VAL A CA 2481 C C . VAL A 310 ? 0.0602 0.0568 0.0510 0.0011 0.0022 -0.0047 396 VAL A C 2482 O O . VAL A 310 ? 0.0593 0.0681 0.0602 0.0040 -0.0005 0.0020 396 VAL A O 2483 C CB . VAL A 310 ? 0.0559 0.0669 0.0632 -0.0013 0.0022 -0.0145 396 VAL A CB 2484 C CG1 . VAL A 310 ? 0.0706 0.0797 0.0722 0.0049 0.0072 -0.0049 396 VAL A CG1 2485 C CG2 . VAL A 310 ? 0.0778 0.0978 0.0759 -0.0094 -0.0010 -0.0037 396 VAL A CG2 2486 N N . TRP A 311 ? 0.0539 0.0556 0.0738 0.0023 0.0023 0.0016 397 TRP A N 2487 C CA . TRP A 311 ? 0.0615 0.0583 0.0586 0.0023 -0.0034 -0.0025 397 TRP A CA 2488 C C . TRP A 311 ? 0.0594 0.0620 0.0608 -0.0008 -0.0018 -0.0043 397 TRP A C 2489 O O . TRP A 311 ? 0.0730 0.0751 0.0635 0.0030 -0.0045 -0.0037 397 TRP A O 2490 C CB . TRP A 311 ? 0.0636 0.0703 0.0651 0.0077 0.0034 0.0033 397 TRP A CB 2491 C CG . TRP A 311 ? 0.0569 0.0642 0.0650 0.0072 -0.0085 0.0023 397 TRP A CG 2492 C CD1 . TRP A 311 ? 0.0684 0.0778 0.0585 0.0065 0.0010 0.0029 397 TRP A CD1 2493 C CD2 . TRP A 311 ? 0.0604 0.0612 0.0695 0.0156 -0.0037 0.0104 397 TRP A CD2 2494 N NE1 . TRP A 311 ? 0.0842 0.0752 0.0633 0.0078 0.0078 0.0024 397 TRP A NE1 2495 C CE2 . TRP A 311 ? 0.0628 0.0765 0.0630 0.0020 0.0011 0.0035 397 TRP A CE2 2496 C CE3 . TRP A 311 ? 0.0698 0.0864 0.0643 -0.0016 -0.0005 -0.0078 397 TRP A CE3 2497 C CZ2 . TRP A 311 ? 0.0724 0.0976 0.0697 0.0128 0.0085 0.0008 397 TRP A CZ2 2498 C CZ3 . TRP A 311 ? 0.0993 0.0740 0.0910 0.0041 0.0036 0.0082 397 TRP A CZ3 2499 C CH2 . TRP A 311 ? 0.1023 0.0912 0.0760 0.0081 0.0112 0.0084 397 TRP A CH2 2500 N N . VAL A 312 ? 0.0624 0.0641 0.0575 0.0037 0.0104 -0.0044 398 VAL A N 2501 C CA . VAL A 312 ? 0.0605 0.0428 0.0601 0.0067 -0.0032 -0.0004 398 VAL A CA 2502 C C . VAL A 312 ? 0.0657 0.0648 0.0598 0.0063 0.0031 -0.0026 398 VAL A C 2503 O O . VAL A 312 ? 0.0646 0.0603 0.0670 -0.0078 -0.0034 0.0111 398 VAL A O 2504 C CB . VAL A 312 ? 0.0500 0.0617 0.0552 0.0018 0.0076 0.0001 398 VAL A CB 2505 C CG1 . VAL A 312 ? 0.0512 0.0567 0.0668 -0.0049 0.0039 -0.0074 398 VAL A CG1 2506 C CG2 . VAL A 312 ? 0.0608 0.0606 0.0714 0.0137 -0.0006 -0.0002 398 VAL A CG2 2507 N N . LYS A 313 ? 0.0615 0.0562 0.0705 0.0066 -0.0076 0.0074 399 LYS A N 2508 C CA . LYS A 313 ? 0.0783 0.0758 0.0809 0.0038 -0.0022 0.0032 399 LYS A CA 2509 C C . LYS A 313 ? 0.0774 0.0690 0.0784 0.0106 -0.0004 -0.0003 399 LYS A C 2510 O O . LYS A 313 ? 0.1106 0.0649 0.0715 0.0048 -0.0018 0.0062 399 LYS A O 2511 C CB A LYS A 313 ? 0.0695 0.0840 0.0810 0.0046 -0.0031 -0.0044 399 LYS A CB 2512 C CB B LYS A 313 ? 0.0761 0.0832 0.0816 0.0052 -0.0024 -0.0027 399 LYS A CB 2513 C CG A LYS A 313 ? 0.0940 0.1211 0.1228 -0.0012 0.0030 -0.0004 399 LYS A CG 2514 C CG B LYS A 313 ? 0.0960 0.1129 0.1198 -0.0001 0.0025 0.0011 399 LYS A CG 2515 C CD A LYS A 313 ? 0.1436 0.1348 0.1556 0.0087 -0.0008 -0.0030 399 LYS A CD 2516 C CD B LYS A 313 ? 0.1374 0.1427 0.1531 0.0031 -0.0032 -0.0045 399 LYS A CD 2517 C CE A LYS A 313 ? 0.1412 0.1501 0.1751 0.0057 0.0015 -0.0044 399 LYS A CE 2518 C CE B LYS A 313 ? 0.1472 0.1446 0.1502 -0.0015 0.0007 -0.0051 399 LYS A CE 2519 N NZ A LYS A 313 ? 0.1661 0.1383 0.1473 0.0071 0.0119 -0.0134 399 LYS A NZ 2520 N NZ B LYS A 313 ? 0.1487 0.1750 0.1467 0.0058 -0.0073 -0.0069 399 LYS A NZ 2521 N N . PRO A 314 ? 0.0803 0.0726 0.0745 -0.0025 0.0044 -0.0041 400 PRO A N 2522 C CA . PRO A 314 ? 0.0822 0.0850 0.0720 0.0083 0.0034 -0.0044 400 PRO A CA 2523 C C . PRO A 314 ? 0.0795 0.1003 0.0846 -0.0107 0.0058 0.0021 400 PRO A C 2524 O O . PRO A 314 ? 0.0968 0.1289 0.0835 -0.0028 -0.0010 -0.0055 400 PRO A O 2525 C CB . PRO A 314 ? 0.0792 0.0855 0.0901 -0.0102 0.0095 0.0050 400 PRO A CB 2526 C CG . PRO A 314 ? 0.1097 0.1067 0.0678 0.0043 0.0009 -0.0026 400 PRO A CG 2527 C CD . PRO A 314 ? 0.0819 0.0812 0.0745 0.0023 0.0126 -0.0060 400 PRO A CD 2528 N N . GLY A 315 ? 0.0753 0.1059 0.0784 0.0025 -0.0003 0.0014 401 GLY A N 2529 C CA . GLY A 315 ? 0.0804 0.0905 0.0758 0.0064 0.0038 0.0018 401 GLY A CA 2530 C C . GLY A 315 ? 0.0881 0.0920 0.0784 0.0044 0.0072 -0.0044 401 GLY A C 2531 O O . GLY A 315 ? 0.1027 0.0985 0.0975 0.0033 -0.0024 -0.0005 401 GLY A O 2532 N N . GLY A 316 ? 0.0838 0.0756 0.0894 0.0051 -0.0042 -0.0012 402 GLY A N 2533 C CA . GLY A 316 ? 0.0883 0.0883 0.0841 0.0029 0.0001 -0.0009 402 GLY A CA 2534 C C . GLY A 316 ? 0.0891 0.0752 0.0908 -0.0042 -0.0046 -0.0037 402 GLY A C 2535 O O . GLY A 316 ? 0.1001 0.1099 0.1241 0.0051 -0.0032 0.0015 402 GLY A O 2536 N N . GLU A 317 ? 0.0998 0.0846 0.0876 0.0007 -0.0086 0.0008 403 GLU A N 2537 C CA . GLU A 317 ? 0.1091 0.0970 0.0991 -0.0001 -0.0066 -0.0045 403 GLU A CA 2538 C C . GLU A 317 ? 0.1189 0.1051 0.1142 -0.0004 -0.0016 -0.0014 403 GLU A C 2539 O O . GLU A 317 ? 0.1538 0.1162 0.1306 -0.0038 -0.0134 0.0110 403 GLU A O 2540 C CB . GLU A 317 ? 0.1156 0.0869 0.0960 -0.0039 -0.0013 0.0093 403 GLU A CB 2541 C CG . GLU A 317 ? 0.1116 0.0924 0.1022 -0.0012 -0.0066 0.0100 403 GLU A CG 2542 C CD . GLU A 317 ? 0.1137 0.0966 0.1123 0.0015 -0.0002 -0.0016 403 GLU A CD 2543 O OE1 . GLU A 317 ? 0.1884 0.1680 0.1622 0.0021 0.0206 0.0182 403 GLU A OE1 2544 O OE2 . GLU A 317 ? 0.1070 0.0849 0.0868 -0.0094 -0.0002 0.0049 403 GLU A OE2 2545 N N . CYS A 318 ? 0.1270 0.0931 0.1132 0.0075 -0.0105 0.0062 404 CYS A N 2546 C CA . CYS A 318 ? 0.1134 0.1060 0.1090 0.0138 0.0018 -0.0032 404 CYS A CA 2547 C C . CYS A 318 ? 0.1229 0.1076 0.1106 0.0153 0.0063 0.0001 404 CYS A C 2548 O O . CYS A 318 ? 0.1826 0.1167 0.1094 0.0404 0.0147 -0.0006 404 CYS A O 2549 C CB . CYS A 318 ? 0.1154 0.1038 0.1065 0.0096 0.0031 0.0045 404 CYS A CB 2550 S SG . CYS A 318 ? 0.1340 0.0990 0.1246 0.0198 -0.0155 0.0088 404 CYS A SG 2551 N N . ASN A 319 ? 0.1017 0.0915 0.0857 0.0092 0.0008 0.0038 405 ASN A N 2552 C CA . ASN A 319 ? 0.0895 0.1009 0.0846 0.0109 0.0000 0.0033 405 ASN A CA 2553 C C . ASN A 319 ? 0.0885 0.0929 0.0949 -0.0027 -0.0059 -0.0013 405 ASN A C 2554 O O . ASN A 319 ? 0.1084 0.1213 0.1063 0.0026 -0.0124 -0.0073 405 ASN A O 2555 C CB . ASN A 319 ? 0.0678 0.0921 0.0769 0.0049 -0.0008 0.0026 405 ASN A CB 2556 C CG . ASN A 319 ? 0.1043 0.1270 0.1049 0.0160 -0.0160 -0.0163 405 ASN A CG 2557 O OD1 . ASN A 319 ? 0.0841 0.0964 0.0876 0.0127 -0.0070 -0.0045 405 ASN A OD1 2558 N ND2 . ASN A 319 ? 0.1751 0.2054 0.1674 0.0564 -0.0048 -0.0323 405 ASN A ND2 2559 N N . GLY A 320 ? 0.0817 0.0856 0.0866 0.0153 -0.0054 -0.0083 406 GLY A N 2560 C CA . GLY A 320 ? 0.0885 0.0902 0.0853 0.0092 -0.0071 0.0009 406 GLY A CA 2561 C C . GLY A 320 ? 0.0957 0.0953 0.0886 0.0081 -0.0039 0.0006 406 GLY A C 2562 O O . GLY A 320 ? 0.0969 0.1055 0.0830 0.0129 -0.0132 0.0036 406 GLY A O 2563 N N . THR A 321 ? 0.0890 0.0969 0.0773 0.0034 -0.0054 0.0017 407 THR A N 2564 C CA . THR A 321 ? 0.1108 0.1142 0.1094 0.0008 -0.0082 -0.0021 407 THR A CA 2565 C C . THR A 321 ? 0.1059 0.0973 0.0998 -0.0043 -0.0131 0.0006 407 THR A C 2566 O O . THR A 321 ? 0.0831 0.0975 0.1006 -0.0109 -0.0117 0.0066 407 THR A O 2567 C CB . THR A 321 ? 0.1159 0.1050 0.1060 -0.0029 -0.0044 0.0036 407 THR A CB 2568 O OG1 . THR A 321 ? 0.1318 0.1585 0.1758 -0.0112 0.0026 -0.0043 407 THR A OG1 2569 C CG2 . THR A 321 ? 0.1386 0.1436 0.1467 0.0030 -0.0177 0.0017 407 THR A CG2 2570 N N . SER A 322 ? 0.1051 0.1121 0.1228 -0.0115 -0.0035 0.0021 408 SER A N 2571 C CA . SER A 322 ? 0.1205 0.1231 0.1337 -0.0022 -0.0025 -0.0021 408 SER A CA 2572 C C . SER A 322 ? 0.1312 0.1369 0.1493 -0.0006 0.0000 -0.0010 408 SER A C 2573 O O . SER A 322 ? 0.1278 0.1472 0.1465 0.0108 -0.0042 -0.0004 408 SER A O 2574 C CB . SER A 322 ? 0.1376 0.1340 0.1577 -0.0013 -0.0001 0.0035 408 SER A CB 2575 O OG . SER A 322 ? 0.1465 0.1377 0.1597 -0.0165 -0.0012 0.0179 408 SER A OG 2576 N N . ASP A 323 ? 0.1137 0.1372 0.1431 -0.0054 -0.0061 0.0014 409 ASP A N 2577 C CA . ASP A 323 ? 0.1304 0.1480 0.1430 -0.0044 -0.0053 0.0003 409 ASP A CA 2578 C C . ASP A 323 ? 0.1203 0.1427 0.1359 -0.0003 -0.0059 -0.0032 409 ASP A C 2579 O O . ASP A 323 ? 0.1167 0.1397 0.1366 -0.0129 -0.0129 -0.0058 409 ASP A O 2580 C CB . ASP A 323 ? 0.1433 0.1521 0.1594 -0.0076 -0.0192 0.0037 409 ASP A CB 2581 C CG . ASP A 323 ? 0.1610 0.1868 0.2017 -0.0139 -0.0215 0.0019 409 ASP A CG 2582 O OD1 . ASP A 323 ? 0.1496 0.1961 0.2139 -0.0208 -0.0083 -0.0046 409 ASP A OD1 2583 O OD2 . ASP A 323 ? 0.2480 0.2143 0.2728 0.0029 -0.0440 -0.0138 409 ASP A OD2 2584 N N . THR A 324 ? 0.1428 0.1502 0.1659 -0.0032 -0.0105 0.0046 410 THR A N 2585 C CA . THR A 324 ? 0.1435 0.1613 0.1665 0.0014 0.0008 0.0048 410 THR A CA 2586 C C . THR A 324 ? 0.1551 0.1787 0.1796 0.0024 -0.0061 0.0101 410 THR A C 2587 O O . THR A 324 ? 0.1802 0.2182 0.1958 -0.0038 -0.0110 0.0202 410 THR A O 2588 C CB . THR A 324 ? 0.1586 0.1757 0.1878 0.0016 0.0010 0.0007 410 THR A CB 2589 O OG1 . THR A 324 ? 0.1608 0.2105 0.2429 0.0057 0.0006 -0.0038 410 THR A OG1 2590 C CG2 . THR A 324 ? 0.1345 0.1717 0.1833 0.0073 0.0066 -0.0036 410 THR A CG2 2591 N N . THR A 325 ? 0.1491 0.1725 0.1702 0.0061 -0.0151 0.0030 411 THR A N 2592 C CA . THR A 325 ? 0.1737 0.1898 0.1786 -0.0026 -0.0069 -0.0077 411 THR A CA 2593 C C . THR A 325 ? 0.1570 0.1783 0.1683 0.0006 -0.0103 -0.0016 411 THR A C 2594 O O . THR A 325 ? 0.1661 0.2194 0.2014 -0.0104 -0.0293 -0.0086 411 THR A O 2595 C CB . THR A 325 ? 0.1839 0.2131 0.1913 -0.0083 -0.0125 -0.0070 411 THR A CB 2596 O OG1 . THR A 325 ? 0.1928 0.2316 0.2308 -0.0272 -0.0268 -0.0047 411 THR A OG1 2597 C CG2 . THR A 325 ? 0.2208 0.2525 0.2168 -0.0052 -0.0014 -0.0047 411 THR A CG2 2598 N N . ALA A 326 ? 0.1409 0.1683 0.1567 -0.0050 -0.0149 0.0006 412 ALA A N 2599 C CA . ALA A 326 ? 0.1504 0.1526 0.1442 -0.0037 -0.0119 0.0002 412 ALA A CA 2600 C C . ALA A 326 ? 0.1405 0.1595 0.1506 -0.0015 -0.0057 -0.0038 412 ALA A C 2601 O O . ALA A 326 ? 0.1415 0.1516 0.1496 -0.0057 -0.0162 -0.0121 412 ALA A O 2602 C CB . ALA A 326 ? 0.1512 0.1539 0.1634 0.0071 -0.0158 0.0013 412 ALA A CB 2603 N N . ALA A 327 ? 0.1645 0.1592 0.1785 -0.0091 -0.0086 -0.0164 413 ALA A N 2604 C CA . ALA A 327 ? 0.1694 0.1732 0.1767 0.0014 -0.0055 -0.0125 413 ALA A CA 2605 C C . ALA A 327 ? 0.1833 0.1738 0.1781 0.0004 -0.0017 -0.0084 413 ALA A C 2606 O O . ALA A 327 ? 0.2025 0.2006 0.2194 0.0012 -0.0035 -0.0022 413 ALA A O 2607 C CB . ALA A 327 ? 0.1950 0.1934 0.1941 0.0062 0.0001 -0.0183 413 ALA A CB 2608 N N . ARG A 328 ? 0.1461 0.1513 0.1630 0.0053 -0.0045 -0.0166 414 ARG A N 2609 C CA . ARG A 328 ? 0.1541 0.1542 0.1655 0.0001 -0.0030 -0.0113 414 ARG A CA 2610 C C . ARG A 328 ? 0.1238 0.1436 0.1344 0.0015 0.0000 -0.0052 414 ARG A C 2611 O O . ARG A 328 ? 0.0995 0.1264 0.1306 -0.0094 -0.0041 -0.0091 414 ARG A O 2612 C CB . ARG A 328 ? 0.1771 0.1869 0.1999 0.0089 -0.0063 -0.0145 414 ARG A CB 2613 C CG . ARG A 328 ? 0.2297 0.2143 0.2205 -0.0024 -0.0048 -0.0175 414 ARG A CG 2614 C CD . ARG A 328 ? 0.2639 0.2871 0.3042 -0.0017 0.0026 -0.0077 414 ARG A CD 2615 N NE . ARG A 328 ? 0.3807 0.3640 0.3483 -0.0135 0.0066 -0.0061 414 ARG A NE 2616 C CZ . ARG A 328 ? 0.3882 0.3766 0.3729 -0.0165 0.0035 -0.0031 414 ARG A CZ 2617 N NH1 . ARG A 328 ? 0.3356 0.3347 0.3489 -0.0015 0.0014 -0.0018 414 ARG A NH1 2618 N NH2 . ARG A 328 ? 0.4150 0.4262 0.3889 -0.0158 0.0029 -0.0051 414 ARG A NH2 2619 N N . TYR A 329 ? 0.1109 0.1243 0.1299 0.0037 -0.0030 -0.0095 415 TYR A N 2620 C CA . TYR A 329 ? 0.0942 0.1092 0.1153 0.0077 0.0024 -0.0055 415 TYR A CA 2621 C C . TYR A 329 ? 0.0876 0.1002 0.1061 0.0029 0.0000 0.0042 415 TYR A C 2622 O O . TYR A 329 ? 0.0849 0.1251 0.1000 0.0055 -0.0082 0.0015 415 TYR A O 2623 C CB . TYR A 329 ? 0.0919 0.1220 0.1245 -0.0049 -0.0078 0.0000 415 TYR A CB 2624 C CG . TYR A 329 ? 0.0805 0.1053 0.1151 -0.0114 -0.0017 -0.0017 415 TYR A CG 2625 C CD1 . TYR A 329 ? 0.1063 0.0920 0.1116 0.0006 -0.0052 0.0053 415 TYR A CD1 2626 C CD2 . TYR A 329 ? 0.0860 0.1119 0.0767 0.0019 -0.0066 0.0067 415 TYR A CD2 2627 C CE1 . TYR A 329 ? 0.1257 0.1137 0.1181 0.0028 -0.0107 -0.0036 415 TYR A CE1 2628 C CE2 . TYR A 329 ? 0.0942 0.0977 0.1104 0.0134 -0.0087 0.0024 415 TYR A CE2 2629 C CZ . TYR A 329 ? 0.0940 0.1217 0.1056 0.0120 -0.0044 -0.0090 415 TYR A CZ 2630 O OH . TYR A 329 ? 0.1223 0.1243 0.1149 0.0001 0.0031 -0.0238 415 TYR A OH 2631 N N . ASP A 330 ? 0.0851 0.0759 0.0872 0.0064 0.0023 0.0055 416 ASP A N 2632 C CA . ASP A 330 ? 0.0823 0.0871 0.0814 0.0024 -0.0048 0.0004 416 ASP A CA 2633 C C . ASP A 330 ? 0.0785 0.0795 0.0791 0.0030 -0.0009 0.0046 416 ASP A C 2634 O O . ASP A 330 ? 0.0796 0.0815 0.0759 -0.0003 -0.0061 0.0039 416 ASP A O 2635 C CB . ASP A 330 ? 0.0781 0.0824 0.0776 0.0064 0.0066 -0.0084 416 ASP A CB 2636 C CG . ASP A 330 ? 0.0919 0.1011 0.1080 -0.0020 0.0066 -0.0014 416 ASP A CG 2637 O OD1 . ASP A 330 ? 0.0950 0.0881 0.1003 0.0084 0.0042 0.0138 416 ASP A OD1 2638 O OD2 . ASP A 330 ? 0.0976 0.1228 0.0985 -0.0012 0.0111 0.0012 416 ASP A OD2 2639 N N . TYR A 331 ? 0.0828 0.0754 0.0721 0.0073 0.0015 0.0052 417 TYR A N 2640 C CA . TYR A 331 ? 0.0841 0.0905 0.0793 0.0044 0.0026 0.0049 417 TYR A CA 2641 C C . TYR A 331 ? 0.0785 0.0747 0.0757 0.0027 -0.0034 0.0012 417 TYR A C 2642 O O . TYR A 331 ? 0.0868 0.0913 0.0946 0.0036 0.0000 0.0019 417 TYR A O 2643 C CB . TYR A 331 ? 0.0946 0.1002 0.0948 0.0121 -0.0002 0.0040 417 TYR A CB 2644 C CG . TYR A 331 ? 0.0905 0.0928 0.0953 0.0187 -0.0068 0.0080 417 TYR A CG 2645 C CD1 . TYR A 331 ? 0.0941 0.0768 0.1113 0.0071 -0.0037 -0.0006 417 TYR A CD1 2646 C CD2 . TYR A 331 ? 0.1143 0.0961 0.1010 0.0223 0.0040 0.0085 417 TYR A CD2 2647 C CE1 . TYR A 331 ? 0.0907 0.0823 0.0932 0.0110 0.0079 -0.0148 417 TYR A CE1 2648 C CE2 . TYR A 331 ? 0.0992 0.0967 0.1051 0.0096 -0.0040 0.0033 417 TYR A CE2 2649 C CZ . TYR A 331 ? 0.0938 0.0983 0.0998 0.0019 -0.0026 0.0035 417 TYR A CZ 2650 O OH . TYR A 331 ? 0.1265 0.1021 0.1382 0.0016 0.0095 0.0008 417 TYR A OH 2651 N N . HIS A 332 ? 0.0765 0.0784 0.0667 0.0043 0.0008 0.0053 418 HIS A N 2652 C CA . HIS A 332 ? 0.0760 0.0847 0.0877 -0.0048 -0.0060 0.0045 418 HIS A CA 2653 C C . HIS A 332 ? 0.0826 0.0924 0.0854 -0.0076 0.0004 0.0054 418 HIS A C 2654 O O . HIS A 332 ? 0.0791 0.0943 0.0887 -0.0171 0.0004 0.0054 418 HIS A O 2655 C CB . HIS A 332 ? 0.0855 0.1034 0.0729 0.0041 0.0019 0.0032 418 HIS A CB 2656 C CG . HIS A 332 ? 0.0897 0.1047 0.1071 -0.0123 0.0014 0.0010 418 HIS A CG 2657 N ND1 . HIS A 332 ? 0.1171 0.0971 0.1030 -0.0084 -0.0072 0.0057 418 HIS A ND1 2658 C CD2 . HIS A 332 ? 0.1327 0.1202 0.1060 -0.0004 -0.0038 -0.0041 418 HIS A CD2 2659 C CE1 . HIS A 332 ? 0.1251 0.1211 0.0971 -0.0169 0.0022 0.0146 418 HIS A CE1 2660 N NE2 . HIS A 332 ? 0.1466 0.1361 0.1235 -0.0065 0.0097 -0.0048 418 HIS A NE2 2661 N N . CYS A 333 ? 0.0692 0.0766 0.0783 0.0034 -0.0026 0.0065 419 CYS A N 2662 C CA . CYS A 333 ? 0.0724 0.0811 0.0873 -0.0028 0.0017 0.0066 419 CYS A CA 2663 C C . CYS A 333 ? 0.0797 0.0778 0.0871 0.0009 -0.0026 0.0023 419 CYS A C 2664 O O . CYS A 333 ? 0.0906 0.0993 0.0998 0.0011 0.0112 0.0032 419 CYS A O 2665 C CB . CYS A 333 ? 0.0667 0.0748 0.0735 -0.0025 -0.0014 0.0138 419 CYS A CB 2666 S SG . CYS A 333 ? 0.1014 0.0888 0.1066 0.0065 0.0052 0.0037 419 CYS A SG 2667 N N . GLY A 334 ? 0.0705 0.0893 0.0974 0.0008 0.0022 0.0041 420 GLY A N 2668 C CA . GLY A 334 ? 0.0768 0.0998 0.0941 0.0013 0.0073 0.0043 420 GLY A CA 2669 C C . GLY A 334 ? 0.0802 0.0990 0.0989 0.0051 0.0025 0.0019 420 GLY A C 2670 O O . GLY A 334 ? 0.0954 0.1442 0.1254 0.0155 0.0185 -0.0051 420 GLY A O 2671 N N . LEU A 335 ? 0.0930 0.1032 0.1013 0.0034 0.0042 -0.0024 421 LEU A N 2672 C CA . LEU A 335 ? 0.0858 0.0972 0.1071 0.0037 -0.0032 0.0005 421 LEU A CA 2673 C C . LEU A 335 ? 0.0966 0.1021 0.1131 0.0054 0.0033 0.0057 421 LEU A C 2674 O O . LEU A 335 ? 0.0898 0.0927 0.1093 0.0141 0.0099 0.0047 421 LEU A O 2675 C CB . LEU A 335 ? 0.0945 0.1085 0.1117 -0.0026 0.0076 0.0028 421 LEU A CB 2676 C CG . LEU A 335 ? 0.0973 0.1029 0.0995 -0.0027 -0.0078 -0.0005 421 LEU A CG 2677 C CD1 . LEU A 335 ? 0.1024 0.1012 0.0960 -0.0085 -0.0120 -0.0004 421 LEU A CD1 2678 C CD2 . LEU A 335 ? 0.1361 0.1168 0.1342 0.0042 -0.0028 -0.0006 421 LEU A CD2 2679 N N . GLU A 336 ? 0.1053 0.1113 0.1049 0.0146 0.0022 0.0033 422 GLU A N 2680 C CA . GLU A 336 ? 0.1203 0.1283 0.1176 0.0070 0.0011 0.0047 422 GLU A CA 2681 C C . GLU A 336 ? 0.1089 0.1227 0.1020 0.0076 0.0054 0.0027 422 GLU A C 2682 O O . GLU A 336 ? 0.1333 0.1607 0.1362 0.0117 0.0128 0.0089 422 GLU A O 2683 C CB . GLU A 336 ? 0.1373 0.1532 0.1336 0.0161 0.0069 -0.0039 422 GLU A CB 2684 C CG . GLU A 336 ? 0.2077 0.2043 0.2096 -0.0016 0.0004 -0.0042 422 GLU A CG 2685 C CD . GLU A 336 ? 0.3115 0.2686 0.3110 0.0064 0.0115 -0.0161 422 GLU A CD 2686 O OE1 . GLU A 336 ? 0.3357 0.3370 0.3578 0.0093 0.0295 -0.0098 422 GLU A OE1 2687 O OE2 . GLU A 336 ? 0.3385 0.2779 0.3275 0.0008 0.0056 -0.0062 422 GLU A OE2 2688 N N . ASP A 337 ? 0.1002 0.1101 0.0963 0.0068 -0.0082 0.0056 423 ASP A N 2689 C CA . ASP A 337 ? 0.0859 0.1001 0.0867 0.0092 0.0022 0.0000 423 ASP A CA 2690 C C . ASP A 337 ? 0.0775 0.0774 0.0828 0.0036 0.0003 0.0042 423 ASP A C 2691 O O . ASP A 337 ? 0.1022 0.1033 0.0929 0.0083 -0.0077 0.0078 423 ASP A O 2692 C CB . ASP A 337 ? 0.0972 0.0880 0.0913 0.0149 0.0088 0.0007 423 ASP A CB 2693 C CG . ASP A 337 ? 0.1034 0.0824 0.0985 0.0076 -0.0001 0.0103 423 ASP A CG 2694 O OD1 . ASP A 337 ? 0.1022 0.1005 0.0869 -0.0063 -0.0020 0.0085 423 ASP A OD1 2695 O OD2 . ASP A 337 ? 0.0977 0.1109 0.1065 0.0002 -0.0008 0.0039 423 ASP A OD2 2696 N N . ALA A 338 ? 0.0911 0.0893 0.0867 0.0117 -0.0061 0.0031 424 ALA A N 2697 C CA . ALA A 338 ? 0.0783 0.0848 0.0908 0.0006 -0.0038 0.0042 424 ALA A CA 2698 C C . ALA A 338 ? 0.0886 0.1052 0.1116 0.0034 0.0024 0.0120 424 ALA A C 2699 O O . ALA A 338 ? 0.0845 0.1214 0.1467 0.0018 0.0002 0.0161 424 ALA A O 2700 C CB . ALA A 338 ? 0.0785 0.0908 0.0979 0.0004 0.0051 -0.0060 424 ALA A CB 2701 N N . LEU A 339 ? 0.0833 0.0895 0.1090 0.0021 0.0054 0.0133 425 LEU A N 2702 C CA . LEU A 339 ? 0.0914 0.0971 0.1001 -0.0017 0.0042 0.0069 425 LEU A CA 2703 C C . LEU A 339 ? 0.0953 0.0993 0.0991 0.0013 0.0019 0.0057 425 LEU A C 2704 O O . LEU A 339 ? 0.0752 0.0886 0.0962 -0.0063 -0.0006 0.0083 425 LEU A O 2705 C CB . LEU A 339 ? 0.0881 0.0879 0.0976 -0.0010 0.0030 0.0101 425 LEU A CB 2706 C CG . LEU A 339 ? 0.0956 0.1120 0.1057 -0.0058 0.0069 0.0095 425 LEU A CG 2707 C CD1 . LEU A 339 ? 0.1480 0.1343 0.1197 0.0023 0.0081 0.0127 425 LEU A CD1 2708 C CD2 . LEU A 339 ? 0.1065 0.1101 0.1103 0.0021 0.0094 0.0149 425 LEU A CD2 2709 N N . LYS A 340 ? 0.1128 0.1384 0.1239 -0.0083 0.0036 0.0072 426 LYS A N 2710 C CA . LYS A 340 ? 0.1596 0.1718 0.1572 -0.0093 0.0022 -0.0013 426 LYS A CA 2711 C C . LYS A 340 ? 0.1791 0.2063 0.1751 -0.0231 0.0111 -0.0050 426 LYS A C 2712 O O . LYS A 340 ? 0.1743 0.2525 0.1701 -0.0441 0.0178 -0.0053 426 LYS A O 2713 C CB . LYS A 340 ? 0.1764 0.1877 0.1723 -0.0015 -0.0023 -0.0029 426 LYS A CB 2714 C CG . LYS A 340 ? 0.2118 0.2165 0.2055 0.0030 -0.0017 -0.0039 426 LYS A CG 2715 C CD . LYS A 340 ? 0.2486 0.2494 0.2422 0.0186 -0.0162 -0.0115 426 LYS A CD 2716 C CE . LYS A 340 ? 0.2469 0.2486 0.2623 0.0044 0.0042 0.0187 426 LYS A CE 2717 N NZ . LYS A 340 ? 0.2697 0.2678 0.2755 0.0017 0.0011 -0.0007 426 LYS A NZ 2718 N N . PRO A 341 ? 0.1769 0.2022 0.1863 -0.0291 0.0074 0.0026 427 PRO A N 2719 C CA . PRO A 341 ? 0.1772 0.1937 0.1874 -0.0219 -0.0016 0.0042 427 PRO A CA 2720 C C . PRO A 341 ? 0.1756 0.1754 0.1710 -0.0118 -0.0037 0.0118 427 PRO A C 2721 O O . PRO A 341 ? 0.1716 0.2199 0.1848 -0.0151 -0.0121 0.0357 427 PRO A O 2722 C CB . PRO A 341 ? 0.1836 0.1908 0.2031 -0.0204 -0.0045 0.0014 427 PRO A CB 2723 C CG . PRO A 341 ? 0.2262 0.2291 0.2209 -0.0184 0.0089 0.0013 427 PRO A CG 2724 C CD . PRO A 341 ? 0.1888 0.2144 0.2017 -0.0345 0.0078 0.0135 427 PRO A CD 2725 N N . ALA A 342 ? 0.1373 0.1462 0.1418 -0.0101 -0.0085 0.0034 428 ALA A N 2726 C CA . ALA A 342 ? 0.1358 0.1260 0.1299 -0.0041 -0.0052 0.0069 428 ALA A CA 2727 C C . ALA A 342 ? 0.1308 0.1210 0.1370 -0.0137 -0.0050 0.0061 428 ALA A C 2728 O O . ALA A 342 ? 0.1463 0.1231 0.1383 -0.0148 -0.0223 0.0017 428 ALA A O 2729 C CB . ALA A 342 ? 0.1188 0.1108 0.1272 0.0020 -0.0073 0.0042 428 ALA A CB 2730 N N . PRO A 343 ? 0.1352 0.1432 0.1449 -0.0012 -0.0097 -0.0001 429 PRO A N 2731 C CA . PRO A 343 ? 0.1490 0.1489 0.1550 0.0074 -0.0103 -0.0067 429 PRO A CA 2732 C C . PRO A 343 ? 0.1613 0.1504 0.1519 0.0050 -0.0108 -0.0047 429 PRO A C 2733 O O . PRO A 343 ? 0.1733 0.1667 0.1349 0.0120 -0.0214 -0.0033 429 PRO A O 2734 C CB . PRO A 343 ? 0.1692 0.1542 0.1695 -0.0034 -0.0138 -0.0042 429 PRO A CB 2735 C CG . PRO A 343 ? 0.1533 0.1494 0.1464 0.0118 -0.0168 -0.0001 429 PRO A CG 2736 C CD . PRO A 343 ? 0.1474 0.1356 0.1518 -0.0054 -0.0074 0.0017 429 PRO A CD 2737 N N . GLU A 344 ? 0.1913 0.1854 0.1753 0.0062 -0.0089 -0.0118 430 GLU A N 2738 C CA . GLU A 344 ? 0.2032 0.1839 0.1821 0.0032 -0.0065 -0.0051 430 GLU A CA 2739 C C . GLU A 344 ? 0.1888 0.1618 0.1519 0.0110 -0.0039 -0.0083 430 GLU A C 2740 O O . GLU A 344 ? 0.1967 0.1421 0.1406 0.0136 -0.0261 -0.0152 430 GLU A O 2741 C CB . GLU A 344 ? 0.2357 0.2130 0.2135 -0.0011 -0.0038 -0.0130 430 GLU A CB 2742 C CG . GLU A 344 ? 0.2677 0.2761 0.2737 -0.0029 -0.0096 -0.0119 430 GLU A CG 2743 C CD . GLU A 344 ? 0.3605 0.3405 0.3433 0.0011 -0.0034 0.0082 430 GLU A CD 2744 O OE1 . GLU A 344 ? 0.3803 0.3701 0.3796 -0.0199 0.0066 -0.0075 430 GLU A OE1 2745 O OE2 . GLU A 344 ? 0.3885 0.4341 0.4234 0.0038 -0.0187 0.0007 430 GLU A OE2 2746 N N . ALA A 345 ? 0.1878 0.1572 0.1508 0.0071 -0.0070 -0.0023 431 ALA A N 2747 C CA . ALA A 345 ? 0.1794 0.1586 0.1570 0.0130 0.0023 -0.0029 431 ALA A CA 2748 C C . ALA A 345 ? 0.1898 0.1559 0.1604 0.0165 -0.0127 -0.0031 431 ALA A C 2749 O O . ALA A 345 ? 0.2108 0.1498 0.1675 0.0250 -0.0100 -0.0079 431 ALA A O 2750 C CB . ALA A 345 ? 0.1862 0.1627 0.1654 0.0204 0.0046 0.0022 431 ALA A CB 2751 N N . GLY A 346 ? 0.1751 0.1416 0.1509 0.0214 -0.0136 -0.0073 432 GLY A N 2752 C CA . GLY A 346 ? 0.1706 0.1450 0.1561 0.0162 -0.0045 -0.0104 432 GLY A CA 2753 C C . GLY A 346 ? 0.1702 0.1518 0.1537 0.0123 -0.0055 -0.0078 432 GLY A C 2754 O O . GLY A 346 ? 0.1971 0.1674 0.1822 0.0386 -0.0122 0.0151 432 GLY A O 2755 N N . GLN A 347 ? 0.1765 0.1458 0.1449 0.0066 -0.0058 -0.0035 433 GLN A N 2756 C CA . GLN A 347 ? 0.1642 0.1460 0.1433 0.0027 -0.0045 -0.0048 433 GLN A CA 2757 C C . GLN A 347 ? 0.1650 0.1282 0.1298 0.0003 -0.0111 -0.0004 433 GLN A C 2758 O O . GLN A 347 ? 0.1611 0.1109 0.1194 0.0260 -0.0150 -0.0047 433 GLN A O 2759 C CB A GLN A 347 ? 0.1707 0.1511 0.1549 0.0049 -0.0049 0.0005 433 GLN A CB 2760 C CB B GLN A 347 ? 0.1706 0.1488 0.1575 0.0038 -0.0034 0.0028 433 GLN A CB 2761 C CG A GLN A 347 ? 0.1771 0.1776 0.1770 -0.0018 -0.0032 0.0005 433 GLN A CG 2762 C CG B GLN A 347 ? 0.1901 0.1589 0.1698 0.0038 -0.0042 -0.0059 433 GLN A CG 2763 C CD A GLN A 347 ? 0.1705 0.1634 0.1700 -0.0011 0.0005 -0.0049 433 GLN A CD 2764 C CD B GLN A 347 ? 0.1919 0.1620 0.1963 -0.0032 0.0016 -0.0036 433 GLN A CD 2765 O OE1 A GLN A 347 ? 0.1982 0.1909 0.1970 -0.0043 -0.0223 -0.0087 433 GLN A OE1 2766 O OE1 B GLN A 347 ? 0.1874 0.1758 0.1762 -0.0025 0.0023 -0.0126 433 GLN A OE1 2767 N NE2 A GLN A 347 ? 0.1930 0.1792 0.1855 0.0006 0.0016 -0.0042 433 GLN A NE2 2768 N NE2 B GLN A 347 ? 0.2327 0.1925 0.2041 0.0017 -0.0074 0.0068 433 GLN A NE2 2769 N N . TRP A 348 ? 0.1612 0.1322 0.1243 0.0051 -0.0094 -0.0057 434 TRP A N 2770 C CA . TRP A 348 ? 0.1303 0.1232 0.1200 -0.0026 -0.0054 -0.0015 434 TRP A CA 2771 C C . TRP A 348 ? 0.1243 0.1097 0.1245 0.0001 -0.0079 -0.0040 434 TRP A C 2772 O O . TRP A 348 ? 0.1446 0.1310 0.1521 -0.0020 -0.0166 -0.0048 434 TRP A O 2773 C CB . TRP A 348 ? 0.1433 0.1139 0.1236 0.0016 -0.0111 -0.0020 434 TRP A CB 2774 C CG . TRP A 348 ? 0.1234 0.1142 0.1157 0.0012 -0.0081 -0.0022 434 TRP A CG 2775 C CD1 . TRP A 348 ? 0.1111 0.1180 0.1224 -0.0007 -0.0125 0.0010 434 TRP A CD1 2776 C CD2 . TRP A 348 ? 0.1122 0.1013 0.1071 -0.0081 0.0055 -0.0064 434 TRP A CD2 2777 N NE1 . TRP A 348 ? 0.1138 0.1158 0.0971 0.0012 -0.0054 -0.0058 434 TRP A NE1 2778 C CE2 . TRP A 348 ? 0.0884 0.0615 0.0837 -0.0079 -0.0116 0.0043 434 TRP A CE2 2779 C CE3 . TRP A 348 ? 0.0905 0.1064 0.1104 0.0054 0.0022 -0.0081 434 TRP A CE3 2780 C CZ2 . TRP A 348 ? 0.0927 0.0881 0.0927 0.0067 -0.0028 0.0123 434 TRP A CZ2 2781 C CZ3 . TRP A 348 ? 0.1079 0.1007 0.0966 -0.0020 -0.0132 0.0135 434 TRP A CZ3 2782 C CH2 . TRP A 348 ? 0.0892 0.0992 0.0996 0.0043 -0.0012 0.0106 434 TRP A CH2 2783 N N . PHE A 349 ? 0.0972 0.1013 0.1093 -0.0066 -0.0028 -0.0057 435 PHE A N 2784 C CA . PHE A 349 ? 0.0863 0.0923 0.1033 -0.0101 -0.0056 0.0003 435 PHE A CA 2785 C C . PHE A 349 ? 0.0913 0.0960 0.0997 -0.0131 -0.0034 0.0032 435 PHE A C 2786 O O . PHE A 349 ? 0.0969 0.0797 0.0910 -0.0180 -0.0034 -0.0026 435 PHE A O 2787 C CB . PHE A 349 ? 0.0986 0.0968 0.0869 -0.0093 -0.0029 -0.0044 435 PHE A CB 2788 C CG . PHE A 349 ? 0.1056 0.0958 0.0974 -0.0029 -0.0033 -0.0001 435 PHE A CG 2789 C CD1 . PHE A 349 ? 0.1062 0.1175 0.1168 -0.0080 -0.0094 0.0069 435 PHE A CD1 2790 C CD2 . PHE A 349 ? 0.0988 0.0977 0.0797 -0.0068 -0.0144 0.0123 435 PHE A CD2 2791 C CE1 . PHE A 349 ? 0.1075 0.1167 0.1008 -0.0130 0.0090 0.0003 435 PHE A CE1 2792 C CE2 . PHE A 349 ? 0.1087 0.0984 0.0862 -0.0064 -0.0088 -0.0066 435 PHE A CE2 2793 C CZ . PHE A 349 ? 0.1206 0.1092 0.1124 -0.0026 -0.0021 -0.0030 435 PHE A CZ 2794 N N . ASN A 350 ? 0.0991 0.0976 0.0930 -0.0223 -0.0104 0.0075 436 ASN A N 2795 C CA . ASN A 350 ? 0.1014 0.1008 0.1047 -0.0079 0.0003 0.0096 436 ASN A CA 2796 C C . ASN A 350 ? 0.1058 0.1041 0.1028 -0.0072 -0.0025 0.0078 436 ASN A C 2797 O O . ASN A 350 ? 0.1048 0.1114 0.1149 -0.0158 -0.0003 0.0081 436 ASN A O 2798 C CB . ASN A 350 ? 0.1212 0.0998 0.1261 -0.0142 -0.0043 0.0066 436 ASN A CB 2799 C CG . ASN A 350 ? 0.1497 0.1374 0.1382 -0.0061 0.0027 0.0103 436 ASN A CG 2800 O OD1 . ASN A 350 ? 0.1591 0.1407 0.1708 0.0043 0.0093 0.0261 436 ASN A OD1 2801 N ND2 . ASN A 350 ? 0.1787 0.1909 0.1795 -0.0269 0.0339 0.0252 436 ASN A ND2 2802 N N . GLU A 351 ? 0.0969 0.1004 0.0981 -0.0053 0.0047 0.0102 437 GLU A N 2803 C CA . GLU A 351 ? 0.1130 0.1122 0.1114 -0.0079 0.0032 0.0109 437 GLU A CA 2804 C C . GLU A 351 ? 0.0985 0.0938 0.1062 -0.0038 -0.0024 0.0046 437 GLU A C 2805 O O . GLU A 351 ? 0.0918 0.0956 0.0966 -0.0029 -0.0007 0.0063 437 GLU A O 2806 C CB . GLU A 351 ? 0.1267 0.1275 0.1363 -0.0055 -0.0020 0.0045 437 GLU A CB 2807 C CG . GLU A 351 ? 0.1831 0.2053 0.2212 -0.0136 0.0054 0.0031 437 GLU A CG 2808 C CD . GLU A 351 ? 0.3031 0.3171 0.2785 -0.0085 0.0057 0.0079 437 GLU A CD 2809 O OE1 . GLU A 351 ? 0.3574 0.3661 0.3126 -0.0009 0.0162 -0.0091 437 GLU A OE1 2810 O OE2 . GLU A 351 ? 0.3949 0.3749 0.3951 0.0019 0.0113 0.0227 437 GLU A OE2 2811 N N . TYR A 352 ? 0.0998 0.1006 0.0982 -0.0028 -0.0085 0.0022 438 TYR A N 2812 C CA . TYR A 352 ? 0.0951 0.1013 0.0978 -0.0017 -0.0004 0.0038 438 TYR A CA 2813 C C . TYR A 352 ? 0.0837 0.0822 0.0822 -0.0015 0.0007 -0.0028 438 TYR A C 2814 O O . TYR A 352 ? 0.0728 0.0773 0.0699 -0.0035 0.0074 0.0042 438 TYR A O 2815 C CB . TYR A 352 ? 0.1028 0.0886 0.0911 -0.0066 -0.0090 0.0043 438 TYR A CB 2816 C CG . TYR A 352 ? 0.0748 0.0810 0.0810 -0.0037 -0.0059 0.0105 438 TYR A CG 2817 C CD1 . TYR A 352 ? 0.0660 0.0791 0.0729 0.0013 -0.0061 -0.0019 438 TYR A CD1 2818 C CD2 . TYR A 352 ? 0.0748 0.0788 0.0882 0.0118 0.0027 0.0098 438 TYR A CD2 2819 C CE1 . TYR A 352 ? 0.0812 0.0802 0.0754 0.0038 0.0127 0.0111 438 TYR A CE1 2820 C CE2 . TYR A 352 ? 0.0852 0.1103 0.0952 0.0007 0.0177 0.0123 438 TYR A CE2 2821 C CZ . TYR A 352 ? 0.0766 0.0836 0.0701 -0.0101 0.0124 -0.0002 438 TYR A CZ 2822 O OH . TYR A 352 ? 0.0779 0.0815 0.0563 -0.0018 0.0066 0.0021 438 TYR A OH 2823 N N . PHE A 353 ? 0.0906 0.0825 0.0936 -0.0027 -0.0100 0.0112 439 PHE A N 2824 C CA . PHE A 353 ? 0.0670 0.0792 0.0928 -0.0055 0.0029 0.0007 439 PHE A CA 2825 C C . PHE A 353 ? 0.0835 0.0942 0.0962 -0.0128 -0.0018 0.0075 439 PHE A C 2826 O O . PHE A 353 ? 0.1046 0.0988 0.0856 -0.0079 -0.0055 0.0072 439 PHE A O 2827 C CB . PHE A 353 ? 0.0673 0.0759 0.0787 -0.0094 -0.0040 0.0000 439 PHE A CB 2828 C CG . PHE A 353 ? 0.0587 0.0590 0.0844 -0.0051 -0.0023 -0.0073 439 PHE A CG 2829 C CD1 . PHE A 353 ? 0.0885 0.0816 0.0768 -0.0059 0.0088 -0.0028 439 PHE A CD1 2830 C CD2 . PHE A 353 ? 0.0978 0.1156 0.1006 -0.0106 -0.0134 0.0137 439 PHE A CD2 2831 C CE1 . PHE A 353 ? 0.1161 0.0974 0.0824 -0.0070 0.0065 0.0016 439 PHE A CE1 2832 C CE2 . PHE A 353 ? 0.1053 0.1210 0.1182 -0.0111 -0.0015 0.0286 439 PHE A CE2 2833 C CZ . PHE A 353 ? 0.0942 0.0981 0.0916 0.0075 0.0027 0.0163 439 PHE A CZ 2834 N N . ILE A 354 ? 0.0962 0.1074 0.0973 -0.0076 0.0034 0.0059 440 ILE A N 2835 C CA . ILE A 354 ? 0.0934 0.1122 0.1019 -0.0035 0.0046 0.0037 440 ILE A CA 2836 C C . ILE A 354 ? 0.0889 0.0993 0.0949 -0.0051 -0.0023 0.0111 440 ILE A C 2837 O O . ILE A 354 ? 0.0912 0.0901 0.0867 -0.0073 0.0064 0.0116 440 ILE A O 2838 C CB . ILE A 354 ? 0.0979 0.1299 0.1245 -0.0042 -0.0041 0.0092 440 ILE A CB 2839 C CG1 . ILE A 354 ? 0.1365 0.1414 0.1142 -0.0041 -0.0002 0.0063 440 ILE A CG1 2840 C CG2 . ILE A 354 ? 0.1422 0.1507 0.1514 -0.0033 0.0089 0.0095 440 ILE A CG2 2841 C CD1 . ILE A 354 ? 0.1855 0.1984 0.1909 -0.0084 -0.0016 0.0102 440 ILE A CD1 2842 N N . GLN A 355 ? 0.0826 0.0927 0.0904 -0.0056 -0.0004 0.0054 441 GLN A N 2843 C CA . GLN A 355 ? 0.0940 0.0979 0.0923 0.0004 0.0032 0.0061 441 GLN A CA 2844 C C . GLN A 355 ? 0.0886 0.0836 0.0775 0.0007 -0.0023 -0.0030 441 GLN A C 2845 O O . GLN A 355 ? 0.0968 0.0822 0.0785 -0.0073 0.0025 0.0168 441 GLN A O 2846 C CB . GLN A 355 ? 0.0869 0.0864 0.0796 -0.0100 0.0019 0.0046 441 GLN A CB 2847 C CG . GLN A 355 ? 0.1067 0.1023 0.0873 0.0036 0.0065 0.0013 441 GLN A CG 2848 C CD . GLN A 355 ? 0.0907 0.1085 0.0918 0.0038 0.0011 0.0109 441 GLN A CD 2849 O OE1 . GLN A 355 ? 0.1010 0.1076 0.1031 -0.0014 -0.0088 0.0142 441 GLN A OE1 2850 N NE2 . GLN A 355 ? 0.0825 0.0984 0.0753 -0.0140 -0.0003 0.0049 441 GLN A NE2 2851 N N . LEU A 356 ? 0.0808 0.0884 0.0703 0.0011 0.0018 0.0028 442 LEU A N 2852 C CA . LEU A 356 ? 0.0916 0.0977 0.0826 0.0030 0.0053 0.0006 442 LEU A CA 2853 C C . LEU A 356 ? 0.0808 0.0869 0.0916 0.0073 -0.0002 -0.0061 442 LEU A C 2854 O O . LEU A 356 ? 0.0844 0.0806 0.0843 -0.0076 0.0009 -0.0074 442 LEU A O 2855 C CB . LEU A 356 ? 0.0885 0.0836 0.0775 0.0011 -0.0003 -0.0012 442 LEU A CB 2856 C CG . LEU A 356 ? 0.0486 0.0690 0.0686 0.0026 0.0020 0.0045 442 LEU A CG 2857 C CD1 . LEU A 356 ? 0.0710 0.0677 0.0716 0.0043 -0.0027 -0.0018 442 LEU A CD1 2858 C CD2 . LEU A 356 ? 0.0764 0.0851 0.0824 0.0037 0.0035 -0.0011 442 LEU A CD2 2859 N N . LEU A 357 ? 0.1045 0.0994 0.0988 0.0001 0.0000 0.0063 443 LEU A N 2860 C CA . LEU A 357 ? 0.1022 0.1058 0.1081 -0.0028 -0.0007 0.0082 443 LEU A CA 2861 C C . LEU A 357 ? 0.1109 0.1112 0.1025 -0.0054 0.0000 0.0057 443 LEU A C 2862 O O . LEU A 357 ? 0.1099 0.1273 0.1224 -0.0035 -0.0039 0.0183 443 LEU A O 2863 C CB . LEU A 357 ? 0.1206 0.1146 0.1404 -0.0045 -0.0015 0.0021 443 LEU A CB 2864 C CG . LEU A 357 ? 0.1548 0.1587 0.1725 -0.0152 0.0097 -0.0112 443 LEU A CG 2865 C CD1 . LEU A 357 ? 0.1871 0.1588 0.2169 -0.0117 0.0092 0.0137 443 LEU A CD1 2866 C CD2 . LEU A 357 ? 0.1667 0.1615 0.1992 0.0074 0.0094 0.0048 443 LEU A CD2 2867 N N . ARG A 358 ? 0.1120 0.1042 0.0997 -0.0061 0.0009 0.0079 444 ARG A N 2868 C CA . ARG A 358 ? 0.1240 0.1174 0.0938 -0.0001 0.0022 0.0071 444 ARG A CA 2869 C C . ARG A 358 ? 0.1051 0.1223 0.0952 -0.0111 0.0031 0.0017 444 ARG A C 2870 O O . ARG A 358 ? 0.1475 0.1524 0.0961 -0.0114 0.0164 0.0042 444 ARG A O 2871 C CB . ARG A 358 ? 0.1306 0.1506 0.1174 -0.0021 0.0109 0.0003 444 ARG A CB 2872 C CG . ARG A 358 ? 0.1856 0.1736 0.1510 -0.0158 0.0064 -0.0068 444 ARG A CG 2873 C CD . ARG A 358 ? 0.2395 0.2521 0.2546 0.0027 0.0004 -0.0006 444 ARG A CD 2874 N NE . ARG A 358 ? 0.3040 0.3024 0.3021 -0.0153 0.0024 -0.0047 444 ARG A NE 2875 C CZ . ARG A 358 ? 0.3445 0.3500 0.3411 -0.0103 0.0097 0.0058 444 ARG A CZ 2876 N NH1 . ARG A 358 ? 0.3446 0.3654 0.3506 -0.0132 0.0016 0.0045 444 ARG A NH1 2877 N NH2 . ARG A 358 ? 0.3722 0.3679 0.3857 -0.0178 0.0000 -0.0126 444 ARG A NH2 2878 N N . ASN A 359 ? 0.1061 0.1115 0.0785 -0.0049 0.0026 0.0000 445 ASN A N 2879 C CA . ASN A 359 ? 0.1078 0.0989 0.0820 0.0021 0.0015 -0.0041 445 ASN A CA 2880 C C . ASN A 359 ? 0.1033 0.0929 0.0774 -0.0067 -0.0004 0.0052 445 ASN A C 2881 O O . ASN A 359 ? 0.1099 0.0945 0.0907 -0.0146 0.0014 0.0133 445 ASN A O 2882 C CB . ASN A 359 ? 0.0958 0.1039 0.0821 -0.0044 -0.0002 0.0058 445 ASN A CB 2883 C CG . ASN A 359 ? 0.1403 0.1532 0.1132 0.0229 0.0022 0.0002 445 ASN A CG 2884 O OD1 . ASN A 359 ? 0.1898 0.2001 0.1228 0.0337 0.0111 -0.0129 445 ASN A OD1 2885 N ND2 . ASN A 359 ? 0.1243 0.1590 0.1356 0.0176 -0.0021 -0.0109 445 ASN A ND2 2886 N N . ALA A 360 ? 0.0963 0.0995 0.0791 0.0057 0.0070 0.0026 446 ALA A N 2887 C CA . ALA A 360 ? 0.0960 0.0958 0.0821 0.0023 -0.0041 0.0025 446 ALA A CA 2888 C C . ALA A 360 ? 0.0976 0.1039 0.0955 0.0037 -0.0046 0.0031 446 ALA A C 2889 O O . ALA A 360 ? 0.1291 0.1148 0.0985 0.0063 0.0073 0.0142 446 ALA A O 2890 C CB . ALA A 360 ? 0.1092 0.1021 0.1043 -0.0034 -0.0018 0.0026 446 ALA A CB 2891 N N . ASN A 361 ? 0.0906 0.1045 0.0744 -0.0057 -0.0050 0.0112 447 ASN A N 2892 C CA . ASN A 361 ? 0.1164 0.1143 0.1055 -0.0013 -0.0033 0.0058 447 ASN A CA 2893 C C . ASN A 361 ? 0.1202 0.1251 0.1133 -0.0037 0.0000 0.0043 447 ASN A C 2894 O O . ASN A 361 ? 0.1277 0.1172 0.1029 -0.0012 0.0000 0.0071 447 ASN A O 2895 C CB . ASN A 361 ? 0.1357 0.1211 0.1170 -0.0093 -0.0018 0.0003 447 ASN A CB 2896 C CG . ASN A 361 ? 0.1731 0.1737 0.1722 -0.0090 -0.0116 0.0011 447 ASN A CG 2897 O OD1 . ASN A 361 ? 0.2120 0.1920 0.1710 -0.0153 -0.0405 -0.0110 447 ASN A OD1 2898 N ND2 . ASN A 361 ? 0.2616 0.2013 0.2643 -0.0011 0.0032 -0.0017 447 ASN A ND2 2899 N N . PRO A 362 ? 0.1224 0.1327 0.1172 0.0026 -0.0010 0.0073 448 PRO A N 2900 C CA . PRO A 362 ? 0.1319 0.1462 0.1295 -0.0044 -0.0003 0.0120 448 PRO A CA 2901 C C . PRO A 362 ? 0.1327 0.1331 0.1230 -0.0065 -0.0046 0.0030 448 PRO A C 2902 O O . PRO A 362 ? 0.1430 0.1289 0.1111 -0.0036 -0.0096 0.0133 448 PRO A O 2903 C CB . PRO A 362 ? 0.1436 0.1495 0.1533 -0.0056 -0.0061 0.0067 448 PRO A CB 2904 C CG . PRO A 362 ? 0.1724 0.2186 0.1644 0.0052 -0.0065 0.0120 448 PRO A CG 2905 C CD . PRO A 362 ? 0.1310 0.1653 0.1376 0.0005 -0.0039 0.0120 448 PRO A CD 2906 N N . PRO A 363 ? 0.1526 0.1515 0.1285 -0.0027 -0.0088 0.0060 449 PRO A N 2907 C CA . PRO A 363 ? 0.1473 0.1536 0.1298 0.0008 -0.0035 0.0066 449 PRO A CA 2908 C C . PRO A 363 ? 0.1519 0.1559 0.1365 0.0019 0.0030 0.0079 449 PRO A C 2909 O O . PRO A 363 ? 0.1568 0.1656 0.1289 -0.0025 -0.0054 0.0150 449 PRO A O 2910 C CB . PRO A 363 ? 0.1538 0.1704 0.1490 -0.0015 0.0062 0.0098 449 PRO A CB 2911 C CG . PRO A 363 ? 0.1972 0.1922 0.1700 -0.0069 0.0052 -0.0032 449 PRO A CG 2912 C CD . PRO A 363 ? 0.1554 0.1555 0.1395 0.0005 -0.0013 -0.0008 449 PRO A CD 2913 N N . PHE A 364 ? 0.1714 0.1812 0.1679 0.0026 -0.0035 0.0043 450 PHE A N 2914 C CA . PHE A 364 ? 0.1870 0.1837 0.1773 -0.0004 0.0047 0.0077 450 PHE A CA 2915 C C . PHE A 364 ? 0.2415 0.2281 0.2254 0.0066 0.0098 0.0146 450 PHE A C 2916 O O . PHE A 364 ? 0.2523 0.2653 0.2202 0.0058 0.0186 0.0221 450 PHE A O 2917 C CB . PHE A 364 ? 0.1792 0.1775 0.1908 -0.0069 0.0014 0.0044 450 PHE A CB 2918 C CG . PHE A 364 ? 0.1506 0.1374 0.1557 -0.0049 -0.0080 0.0033 450 PHE A CG 2919 C CD1 . PHE A 364 ? 0.1525 0.1294 0.1436 0.0005 -0.0086 -0.0003 450 PHE A CD1 2920 C CD2 . PHE A 364 ? 0.1530 0.1346 0.1583 0.0034 -0.0050 0.0028 450 PHE A CD2 2921 C CE1 . PHE A 364 ? 0.1742 0.1509 0.1558 0.0097 -0.0075 0.0008 450 PHE A CE1 2922 C CE2 . PHE A 364 ? 0.1585 0.1429 0.1235 0.0036 -0.0106 0.0014 450 PHE A CE2 2923 C CZ . PHE A 364 ? 0.1882 0.1595 0.1660 0.0029 -0.0037 0.0036 450 PHE A CZ 2924 O OXT . PHE A 364 ? 0.3053 0.2480 0.2934 0.0071 0.0105 0.0221 450 PHE A OXT 2925 C C1 . NAG B . ? 0.0630 0.0690 0.0620 0.0004 -0.0102 -0.0081 500 NAG A C1 2926 C C2 . NAG B . ? 0.0733 0.0850 0.0660 -0.0127 0.0004 -0.0013 500 NAG A C2 2927 C C3 . NAG B . ? 0.0670 0.0964 0.0842 -0.0007 -0.0036 -0.0013 500 NAG A C3 2928 C C4 . NAG B . ? 0.0827 0.0912 0.0870 -0.0027 0.0111 -0.0077 500 NAG A C4 2929 C C5 . NAG B . ? 0.0817 0.0840 0.0926 -0.0015 0.0040 -0.0014 500 NAG A C5 2930 C C6 . NAG B . ? 0.0947 0.0875 0.0783 0.0065 0.0032 0.0016 500 NAG A C6 2931 C C7 . NAG B . ? 0.0892 0.0838 0.0803 0.0063 0.0017 0.0064 500 NAG A C7 2932 C C8 . NAG B . ? 0.0945 0.0788 0.0722 -0.0097 -0.0061 -0.0141 500 NAG A C8 2933 N N2 . NAG B . ? 0.0716 0.0852 0.1007 -0.0044 0.0000 -0.0078 500 NAG A N2 2934 O O3 . NAG B . ? 0.1052 0.1172 0.0928 -0.0087 0.0014 -0.0280 500 NAG A O3 2935 O O4 . NAG B . ? 0.0965 0.0997 0.0996 0.0112 0.0157 -0.0137 500 NAG A O4 2936 O O5 . NAG B . ? 0.0896 0.0828 0.0854 0.0009 -0.0017 -0.0087 500 NAG A O5 2937 O O6 . NAG B . ? 0.0885 0.1042 0.0667 -0.0025 0.0060 -0.0040 500 NAG A O6 2938 O O7 . NAG B . ? 0.0951 0.1357 0.1320 -0.0117 -0.0126 -0.0034 500 NAG A O7 2939 CA CA . CA C . ? 0.3065 0.3349 0.3446 -0.0064 -0.0040 -0.0028 501 CA A CA 2940 C C1 . GOL D . ? 0.2412 0.2268 0.2585 -0.0024 -0.0012 -0.0127 510 GOL A C1 2941 O O1 . GOL D . ? 0.2694 0.1941 0.2044 -0.0148 0.0213 0.0107 510 GOL A O1 2942 C C2 . GOL D . ? 0.2560 0.2198 0.2105 -0.0122 -0.0054 0.0011 510 GOL A C2 2943 O O2 . GOL D . ? 0.2549 0.1794 0.1938 0.0022 -0.0195 0.0224 510 GOL A O2 2944 C C3 . GOL D . ? 0.2419 0.2465 0.2265 0.0118 -0.0059 -0.0081 510 GOL A C3 2945 O O3 . GOL D . ? 0.3127 0.2775 0.2625 0.0111 -0.0068 0.0208 510 GOL A O3 2946 C C1 A GOL E . ? 0.2203 0.2296 0.2457 -0.0035 0.0120 0.0022 511 GOL A C1 2947 C C1 B GOL E . ? 0.1939 0.1985 0.2033 0.0021 0.0028 -0.0013 511 GOL A C1 2948 O O1 A GOL E . ? 0.2281 0.2043 0.2442 0.0042 0.0183 -0.0093 511 GOL A O1 2949 O O1 B GOL E . ? 0.1585 0.2101 0.1751 -0.0204 0.0119 -0.0024 511 GOL A O1 2950 C C2 A GOL E . ? 0.2249 0.2278 0.2318 0.0014 0.0042 -0.0032 511 GOL A C2 2951 C C2 B GOL E . ? 0.1947 0.2148 0.2002 -0.0007 0.0008 0.0014 511 GOL A C2 2952 O O2 A GOL E . ? 0.1696 0.2238 0.1895 -0.0228 0.0111 0.0021 511 GOL A O2 2953 O O2 B GOL E . ? 0.1988 0.2283 0.2093 0.0099 0.0107 0.0021 511 GOL A O2 2954 C C3 A GOL E . ? 0.2278 0.2411 0.2347 -0.0047 -0.0017 0.0018 511 GOL A C3 2955 C C3 B GOL E . ? 0.2264 0.2176 0.2143 0.0067 -0.0032 0.0005 511 GOL A C3 2956 O O3 A GOL E . ? 0.2742 0.2518 0.2560 0.0013 0.0050 -0.0026 511 GOL A O3 2957 O O3 B GOL E . ? 0.1714 0.1638 0.2105 -0.0030 0.0033 0.0130 511 GOL A O3 2958 C C1 . GOL F . ? 0.2827 0.2828 0.2931 0.0056 -0.0011 0.0022 512 GOL A C1 2959 O O1 . GOL F . ? 0.3041 0.3247 0.3178 0.0052 -0.0023 -0.0146 512 GOL A O1 2960 C C2 . GOL F . ? 0.2531 0.2708 0.2668 -0.0021 0.0013 -0.0051 512 GOL A C2 2961 O O2 . GOL F . ? 0.2576 0.2791 0.2781 0.0138 0.0082 -0.0047 512 GOL A O2 2962 C C3 . GOL F . ? 0.2194 0.2179 0.2295 0.0063 0.0069 0.0051 512 GOL A C3 2963 O O3 . GOL F . ? 0.1813 0.2000 0.1824 0.0046 0.0107 0.0023 512 GOL A O3 2964 C C1 . GOL G . ? 0.2533 0.2596 0.2590 0.0005 0.0048 0.0036 514 GOL A C1 2965 O O1 . GOL G . ? 0.2870 0.2594 0.2533 0.0009 -0.0017 0.0009 514 GOL A O1 2966 C C2 . GOL G . ? 0.2800 0.2814 0.2740 0.0055 -0.0046 -0.0006 514 GOL A C2 2967 O O2 . GOL G . ? 0.2907 0.3024 0.3047 -0.0011 0.0095 -0.0056 514 GOL A O2 2968 C C3 . GOL G . ? 0.2693 0.2860 0.2768 -0.0140 0.0030 -0.0037 514 GOL A C3 2969 O O3 . GOL G . ? 0.2539 0.2993 0.2840 0.0139 -0.0021 -0.0155 514 GOL A O3 2970 C C1 . GOL H . ? 0.3120 0.2952 0.2990 0.0065 0.0120 0.0062 515 GOL A C1 2971 O O1 . GOL H . ? 0.2715 0.3042 0.3137 0.0254 0.0190 -0.0151 515 GOL A O1 2972 C C2 . GOL H . ? 0.2825 0.2885 0.2819 -0.0073 -0.0030 0.0026 515 GOL A C2 2973 O O2 . GOL H . ? 0.2663 0.2817 0.2718 -0.0016 0.0102 -0.0067 515 GOL A O2 2974 C C3 . GOL H . ? 0.2634 0.2842 0.2687 0.0006 0.0006 0.0252 515 GOL A C3 2975 O O3 . GOL H . ? 0.2006 0.2697 0.2280 0.0011 -0.0151 0.0158 515 GOL A O3 2976 C C1 . GOL I . ? 0.2527 0.2634 0.2545 0.0094 0.0004 0.0060 516 GOL A C1 2977 O O1 . GOL I . ? 0.2574 0.3013 0.2439 -0.0213 0.0016 0.0040 516 GOL A O1 2978 C C2 . GOL I . ? 0.2686 0.2795 0.2717 0.0023 -0.0066 -0.0011 516 GOL A C2 2979 O O2 . GOL I . ? 0.2906 0.2732 0.2895 0.0047 -0.0034 0.0012 516 GOL A O2 2980 C C3 . GOL I . ? 0.2671 0.2824 0.2815 0.0007 0.0000 0.0030 516 GOL A C3 2981 O O3 . GOL I . ? 0.2864 0.2844 0.3133 -0.0026 -0.0018 -0.0006 516 GOL A O3 2982 C C1 . GOL J . ? 0.3912 0.3892 0.3670 -0.0011 -0.0011 -0.0007 517 GOL A C1 2983 O O1 . GOL J . ? 0.4196 0.4091 0.3992 0.0037 0.0052 -0.0040 517 GOL A O1 2984 C C2 . GOL J . ? 0.4068 0.4098 0.4006 -0.0024 0.0076 -0.0001 517 GOL A C2 2985 O O2 . GOL J . ? 0.4238 0.4305 0.4184 0.0016 0.0108 -0.0091 517 GOL A O2 2986 C C3 . GOL J . ? 0.4182 0.4148 0.4158 -0.0015 0.0000 -0.0024 517 GOL A C3 2987 O O3 . GOL J . ? 0.4404 0.4556 0.4199 -0.0072 -0.0004 0.0001 517 GOL A O3 2988 O O . HOH K . ? 0.1391 0.1501 0.1458 0.0062 -0.0124 -0.0077 2001 HOH A O 2989 O O . HOH K . ? 0.1872 0.1608 0.2468 0.0044 0.0250 -0.0174 2002 HOH A O 2990 O O . HOH K . ? 0.3887 0.3529 0.3600 0.0192 0.0044 -0.0112 2003 HOH A O 2991 O O . HOH K . ? 0.2649 0.2510 0.2349 0.0138 -0.0181 -0.0149 2004 HOH A O 2992 O O . HOH K . ? 0.2272 0.3381 0.2766 -0.0191 -0.0043 -0.0219 2005 HOH A O 2993 O O . HOH K . ? 0.2417 0.2631 0.2970 0.0310 0.0199 0.0066 2006 HOH A O 2994 O O . HOH K . ? 0.1987 0.1917 0.2419 0.0140 0.0094 -0.0021 2007 HOH A O 2995 O O . HOH K . ? 0.2432 0.2418 0.2598 -0.0045 0.0028 0.0020 2008 HOH A O 2996 O O . HOH K . ? 0.2234 0.3354 0.3164 -0.0150 -0.0146 -0.0247 2009 HOH A O 2997 O O . HOH K . ? 0.5024 0.5191 0.5129 0.0123 -0.0005 0.0020 2010 HOH A O 2998 O O . HOH K . ? 0.4149 0.3522 0.3788 -0.0021 0.0085 -0.0135 2011 HOH A O 2999 O O . HOH K . ? 0.1813 0.2013 0.1099 0.0064 -0.0008 -0.0168 2012 HOH A O 3000 O O . HOH K . ? 0.3260 0.3133 0.2465 0.0032 -0.0050 0.0219 2013 HOH A O 3001 O O . HOH K . ? 0.1364 0.1161 0.1144 0.0137 -0.0003 -0.0014 2014 HOH A O 3002 O O . HOH K . ? 0.2707 0.2490 0.2313 0.0231 -0.0017 0.0209 2015 HOH A O 3003 O O . HOH K . ? 0.2984 0.2773 0.3441 -0.0171 -0.0007 0.0253 2016 HOH A O 3004 O O . HOH K . ? 0.3705 0.3867 0.3689 0.0106 0.0061 0.0221 2017 HOH A O 3005 O O . HOH K . ? 0.3904 0.3576 0.3898 0.0063 0.0030 -0.0077 2018 HOH A O 3006 O O . HOH K . ? 0.4033 0.3901 0.3625 0.0083 -0.0004 -0.0026 2019 HOH A O 3007 O O . HOH K . ? 0.2853 0.2615 0.2321 -0.0246 0.0169 0.0322 2020 HOH A O 3008 O O . HOH K . ? 0.3225 0.3077 0.2972 -0.0062 0.0222 0.0218 2021 HOH A O 3009 O O . HOH K . ? 0.3545 0.3321 0.2970 -0.0070 -0.0285 0.0015 2022 HOH A O 3010 O O . HOH K . ? 0.3660 0.3503 0.3435 -0.0213 0.0057 0.0107 2023 HOH A O 3011 O O . HOH K . ? 0.2521 0.2696 0.2828 -0.0158 0.0087 -0.0017 2024 HOH A O 3012 O O . HOH K . ? 0.3879 0.4198 0.4032 -0.0167 -0.0074 0.0089 2025 HOH A O 3013 O O . HOH K . ? 0.4104 0.4144 0.4245 -0.0002 -0.0163 0.0026 2026 HOH A O 3014 O O . HOH K . ? 0.1941 0.1888 0.2076 0.0141 -0.0201 -0.0120 2027 HOH A O 3015 O O . HOH K . ? 0.5126 0.4952 0.5004 0.0001 -0.0053 -0.0008 2028 HOH A O 3016 O O . HOH K . ? 0.3260 0.2966 0.2932 0.0008 0.0124 0.0124 2029 HOH A O 3017 O O . HOH K . ? 0.3539 0.3772 0.3711 -0.0090 0.0146 -0.0058 2030 HOH A O 3018 O O . HOH K . ? 0.4240 0.4339 0.4300 -0.0175 0.0247 0.0031 2031 HOH A O 3019 O O . HOH K . ? 0.2682 0.2630 0.2935 -0.0054 0.0110 0.0163 2032 HOH A O 3020 O O . HOH K . ? 0.4705 0.4786 0.4410 -0.0081 -0.0039 -0.0017 2033 HOH A O 3021 O O . HOH K . ? 0.4875 0.4703 0.4996 0.0016 0.0010 -0.0062 2034 HOH A O 3022 O O . HOH K . ? 0.4328 0.3890 0.4284 -0.0041 -0.0007 -0.0009 2035 HOH A O 3023 O O . HOH K . ? 0.3058 0.2658 0.2503 -0.0128 0.0162 0.0014 2036 HOH A O 3024 O O . HOH K . ? 0.3208 0.3428 0.3410 -0.0032 -0.0091 -0.0049 2037 HOH A O 3025 O O . HOH K . ? 0.3909 0.3810 0.3840 0.0001 0.0026 0.0009 2038 HOH A O 3026 O O . HOH K . ? 0.3122 0.2957 0.2901 -0.0051 -0.0066 0.0064 2039 HOH A O 3027 O O . HOH K . ? 0.2969 0.2962 0.2803 0.0131 0.0040 0.0081 2040 HOH A O 3028 O O . HOH K . ? 0.3547 0.3464 0.3530 0.0005 -0.0066 0.0086 2041 HOH A O 3029 O O . HOH K . ? 0.4068 0.3903 0.3939 -0.0125 0.0052 0.0221 2042 HOH A O 3030 O O . HOH K . ? 0.4536 0.4218 0.3771 0.0069 -0.0097 0.0171 2043 HOH A O 3031 O O . HOH K . ? 0.2986 0.2916 0.3046 -0.0059 0.0061 -0.0049 2044 HOH A O 3032 O O . HOH K . ? 0.5406 0.5462 0.5366 0.0097 0.0051 0.0007 2045 HOH A O 3033 O O . HOH K . ? 0.2458 0.3176 0.3029 -0.0209 -0.0251 -0.0080 2046 HOH A O 3034 O O . HOH K . ? 0.1203 0.1116 0.0888 0.0026 -0.0005 0.0013 2047 HOH A O 3035 O O . HOH K . ? 0.1555 0.1087 0.1639 0.0005 -0.0108 0.0082 2048 HOH A O 3036 O O . HOH K . ? 0.3179 0.3273 0.3047 0.0245 -0.0020 -0.0009 2049 HOH A O 3037 O O . HOH K . ? 0.3458 0.3116 0.3143 -0.0157 -0.0290 0.0076 2050 HOH A O 3038 O O . HOH K . ? 0.0972 0.0894 0.0942 0.0048 -0.0098 -0.0119 2051 HOH A O 3039 O O . HOH K . ? 0.0930 0.0944 0.0937 -0.0108 -0.0025 0.0100 2052 HOH A O 3040 O O . HOH K . ? 0.0925 0.0714 0.0993 -0.0054 0.0106 0.0045 2053 HOH A O 3041 O O . HOH K . ? 0.1211 0.0826 0.1042 -0.0195 -0.0094 -0.0048 2054 HOH A O 3042 O O . HOH K . ? 0.0942 0.0749 0.0898 -0.0045 0.0053 -0.0071 2055 HOH A O 3043 O O . HOH K . ? 0.1511 0.1522 0.1288 0.0107 0.0190 -0.0014 2056 HOH A O 3044 O O . HOH K . ? 0.2133 0.2153 0.2905 0.0471 0.0152 0.0455 2057 HOH A O 3045 O O . HOH K . ? 0.3906 0.4129 0.4184 0.0037 0.0205 -0.0042 2058 HOH A O 3046 O O . HOH K . ? 0.4385 0.4237 0.4577 -0.0162 0.0065 -0.0058 2059 HOH A O 3047 O O . HOH K . ? 0.5245 0.5319 0.5297 -0.0109 0.0040 -0.0070 2060 HOH A O 3048 O O . HOH K . ? 0.3797 0.3990 0.3075 -0.0109 -0.0080 -0.0045 2061 HOH A O 3049 O O . HOH K . ? 0.3873 0.4354 0.4523 -0.0016 0.0106 0.0077 2062 HOH A O 3050 O O . HOH K . ? 0.4274 0.4209 0.4166 -0.0138 -0.0048 0.0187 2063 HOH A O 3051 O O . HOH K . ? 0.0668 0.0632 0.0798 -0.0118 0.0012 -0.0138 2064 HOH A O 3052 O O . HOH K . ? 0.0678 0.1254 0.0829 -0.0130 -0.0008 -0.0284 2065 HOH A O 3053 O O . HOH K . ? 0.0804 0.0885 0.1037 -0.0083 -0.0104 -0.0043 2066 HOH A O 3054 O O . HOH K . ? 0.4426 0.4450 0.4409 -0.0013 0.0028 -0.0015 2067 HOH A O 3055 O O . HOH K . ? 0.1593 0.1472 0.1536 -0.0191 -0.0060 -0.0297 2068 HOH A O 3056 O O . HOH K . ? 0.2353 0.2490 0.3159 -0.0432 -0.0210 0.0247 2069 HOH A O 3057 O O . HOH K . ? 0.3826 0.3855 0.3801 0.0046 -0.0137 -0.0028 2070 HOH A O 3058 O O . HOH K . ? 0.4358 0.4147 0.4026 -0.0025 -0.0117 0.0100 2071 HOH A O 3059 O O . HOH K . ? 0.3131 0.3577 0.3516 0.0272 -0.0074 -0.0023 2072 HOH A O 3060 O O . HOH K . ? 0.4392 0.4274 0.4182 -0.0068 -0.0184 0.0019 2073 HOH A O 3061 O O . HOH K . ? 0.3853 0.4281 0.3714 -0.0229 -0.0083 -0.0105 2074 HOH A O 3062 O O . HOH K . ? 0.4378 0.4710 0.4525 0.0099 0.0032 -0.0020 2075 HOH A O 3063 O O . HOH K . ? 0.2210 0.1866 0.2100 -0.0068 -0.0067 -0.0014 2076 HOH A O 3064 O O . HOH K . ? 0.2866 0.3086 0.3393 -0.0109 -0.0091 0.0218 2077 HOH A O 3065 O O . HOH K . ? 0.3654 0.2853 0.3511 -0.0175 0.0213 -0.0003 2078 HOH A O 3066 O O . HOH K . ? 0.2759 0.2199 0.2100 -0.0210 0.0096 0.0248 2079 HOH A O 3067 O O . HOH K . ? 0.2247 0.1711 0.2082 0.0152 -0.0054 -0.0124 2080 HOH A O 3068 O O . HOH K . ? 0.1595 0.1990 0.2189 0.0056 -0.0168 -0.0039 2081 HOH A O 3069 O O . HOH K . ? 0.1079 0.1244 0.1456 -0.0119 0.0108 -0.0313 2082 HOH A O 3070 O O . HOH K . ? 0.1962 0.1974 0.1580 -0.0110 0.0091 0.0020 2083 HOH A O 3071 O O . HOH K . ? 0.3304 0.2892 0.3010 -0.0328 0.0066 0.0044 2084 HOH A O 3072 O O . HOH K . ? 0.2013 0.1908 0.1823 -0.0179 -0.0018 0.0251 2085 HOH A O 3073 O O . HOH K . ? 0.2255 0.1456 0.2238 0.0213 -0.0119 0.0142 2086 HOH A O 3074 O O . HOH K . ? 0.3147 0.3273 0.2874 -0.0486 -0.0201 -0.0013 2087 HOH A O 3075 O O . HOH K . ? 0.2978 0.3210 0.2608 0.0066 -0.0170 0.0209 2088 HOH A O 3076 O O . HOH K . ? 0.5255 0.5338 0.5296 -0.0101 0.0032 -0.0013 2089 HOH A O 3077 O O . HOH K . ? 0.1902 0.2015 0.1591 0.0186 0.0367 0.0366 2090 HOH A O 3078 O O . HOH K . ? 0.4233 0.4617 0.4406 0.0079 0.0042 0.0035 2091 HOH A O 3079 O O . HOH K . ? 0.3675 0.3339 0.3308 0.0093 0.0029 -0.0122 2092 HOH A O 3080 O O . HOH K . ? 0.3797 0.4097 0.3721 0.0126 -0.0205 0.0226 2093 HOH A O 3081 O O . HOH K . ? 0.4036 0.3575 0.4067 0.0114 -0.0047 -0.0047 2094 HOH A O 3082 O O . HOH K . ? 0.4264 0.4143 0.4488 0.0048 0.0088 0.0022 2095 HOH A O 3083 O O . HOH K . ? 0.4339 0.4335 0.4406 -0.0053 0.0121 0.0192 2096 HOH A O 3084 O O . HOH K . ? 0.3188 0.3726 0.3788 -0.0320 -0.0095 0.0066 2097 HOH A O 3085 O O . HOH K . ? 0.4060 0.4526 0.4107 0.0054 0.0149 0.0056 2098 HOH A O 3086 O O . HOH K . ? 0.1594 0.1496 0.1292 0.0087 0.0092 0.0115 2099 HOH A O 3087 O O . HOH K . ? 0.4103 0.4019 0.4230 -0.0076 -0.0106 0.0153 2100 HOH A O 3088 O O . HOH K . ? 0.4660 0.4092 0.4082 0.0011 -0.0004 0.0003 2101 HOH A O 3089 O O . HOH K . ? 0.1100 0.0783 0.1108 0.0022 0.0106 0.0093 2102 HOH A O 3090 O O . HOH K . ? 0.2778 0.3181 0.2826 0.0079 0.0150 -0.0006 2103 HOH A O 3091 O O . HOH K . ? 0.4694 0.4352 0.4624 -0.0172 -0.0063 0.0158 2104 HOH A O 3092 O O . HOH K . ? 0.2608 0.2531 0.2593 -0.0042 0.0052 -0.0065 2105 HOH A O 3093 O O . HOH K . ? 0.3690 0.3792 0.4044 0.0029 0.0041 -0.0064 2106 HOH A O 3094 O O . HOH K . ? 0.3426 0.3762 0.3993 -0.0016 0.0065 0.0038 2107 HOH A O 3095 O O . HOH K . ? 0.0895 0.0928 0.1244 -0.0009 -0.0128 0.0095 2108 HOH A O 3096 O O . HOH K . ? 0.1675 0.1849 0.1510 0.0160 -0.0188 -0.0174 2109 HOH A O 3097 O O . HOH K . ? 0.2741 0.3098 0.2990 -0.0145 0.0104 -0.0064 2110 HOH A O 3098 O O . HOH K . ? 0.3055 0.3080 0.2835 0.0049 -0.0284 -0.0162 2111 HOH A O 3099 O O . HOH K . ? 0.1540 0.1212 0.1701 0.0064 0.0007 -0.0058 2112 HOH A O 3100 O O . HOH K . ? 0.2541 0.2580 0.2902 -0.0412 -0.0508 0.0294 2113 HOH A O 3101 O O . HOH K . ? 0.1396 0.1494 0.1798 -0.0134 -0.0116 0.0158 2114 HOH A O 3102 O O . HOH K . ? 0.0677 0.0857 0.1050 -0.0065 0.0129 0.0048 2115 HOH A O 3103 O O . HOH K . ? 0.1634 0.2181 0.1787 -0.0034 0.0037 -0.0026 2116 HOH A O 3104 O O . HOH K . ? 0.1560 0.1872 0.1852 0.0105 -0.0026 0.0230 2117 HOH A O 3105 O O . HOH K . ? 0.1486 0.1752 0.1508 0.0196 -0.0141 0.0052 2118 HOH A O 3106 O O . HOH K . ? 0.5316 0.5412 0.5444 -0.0049 0.0089 -0.0039 2119 HOH A O 3107 O O . HOH K . ? 0.3421 0.3442 0.3498 0.0035 -0.0071 -0.0092 2120 HOH A O 3108 O O . HOH K . ? 0.4110 0.4018 0.3776 -0.0016 -0.0077 0.0006 2121 HOH A O 3109 O O . HOH K . ? 0.2920 0.2968 0.3392 -0.0060 0.0126 0.0076 2122 HOH A O 3110 O O . HOH K . ? 0.3568 0.3684 0.3675 0.0349 -0.0183 -0.0194 2123 HOH A O 3111 O O . HOH K . ? 0.4497 0.4397 0.4358 -0.0008 -0.0155 -0.0062 2124 HOH A O 3112 O O . HOH K . ? 0.3420 0.3448 0.3688 0.0279 -0.0064 0.0141 2125 HOH A O 3113 O O . HOH K . ? 0.4070 0.4162 0.3709 -0.0150 0.0291 0.0113 2126 HOH A O 3114 O O . HOH K . ? 0.2874 0.2867 0.2848 -0.0097 0.0086 -0.0360 2127 HOH A O 3115 O O . HOH K . ? 0.2500 0.2682 0.2813 -0.0214 -0.0072 -0.0046 2128 HOH A O 3116 O O . HOH K . ? 0.1105 0.1124 0.1554 0.0027 -0.0199 -0.0045 2129 HOH A O 3117 O O . HOH K . ? 0.1664 0.1273 0.1474 0.0129 -0.0256 -0.0027 2130 HOH A O 3118 O O . HOH K . ? 0.3658 0.3753 0.3845 -0.0142 0.0082 0.0018 2131 HOH A O 3119 O O . HOH K . ? 0.4356 0.4563 0.4439 0.0011 -0.0184 0.0042 2132 HOH A O 3120 O O . HOH K . ? 0.2159 0.1800 0.2603 -0.0185 -0.0045 -0.0046 2133 HOH A O 3121 O O . HOH K . ? 0.1799 0.1726 0.1557 -0.0230 0.0181 -0.0176 2134 HOH A O 3122 O O . HOH K . ? 0.1384 0.1317 0.1104 0.0002 -0.0057 0.0132 2135 HOH A O 3123 O O . HOH K . ? 0.1986 0.1289 0.1369 0.0002 0.0135 -0.0100 2136 HOH A O 3124 O O . HOH K . ? 0.4322 0.4843 0.4587 0.0004 -0.0009 0.0097 2137 HOH A O 3125 O O . HOH K . ? 0.4249 0.4118 0.4252 -0.0212 0.0050 -0.0009 2138 HOH A O 3126 O O . HOH K . ? 0.3937 0.4145 0.3847 -0.0124 -0.0027 0.0152 2139 HOH A O 3127 O O . HOH K . ? 0.3374 0.2943 0.3507 -0.0037 -0.0050 0.0227 2140 HOH A O 3128 O O . HOH K . ? 0.3781 0.4336 0.3994 -0.0050 0.0085 0.0022 2141 HOH A O 3129 O O . HOH K . ? 0.3802 0.4052 0.4084 -0.0064 0.0107 -0.0031 2142 HOH A O 3130 O O . HOH K . ? 0.3351 0.3313 0.3414 0.0048 -0.0054 0.0329 2143 HOH A O 3131 O O . HOH K . ? 0.1288 0.1462 0.1255 -0.0121 0.0091 0.0070 2144 HOH A O 3132 O O . HOH K . ? 0.4368 0.4551 0.4280 0.0029 0.0073 -0.0083 2145 HOH A O 3133 O O . HOH K . ? 0.3801 0.4141 0.3773 0.0016 -0.0084 0.0111 2146 HOH A O 3134 O O . HOH K . ? 0.3416 0.3834 0.3613 -0.0130 0.0002 0.0009 2147 HOH A O 3135 O O . HOH K . ? 0.4454 0.4589 0.4230 -0.0072 0.0067 -0.0027 2148 HOH A O 3136 O O . HOH K . ? 0.2854 0.2517 0.2493 0.0181 0.0159 0.0042 2149 HOH A O 3137 O O . HOH K . ? 0.4748 0.4524 0.4550 -0.0034 0.0077 -0.0002 2150 HOH A O 3138 O O . HOH K . ? 0.4256 0.3246 0.3671 0.0055 -0.0024 -0.0175 2151 HOH A O 3139 O O . HOH K . ? 0.5188 0.5024 0.5172 -0.0015 -0.0031 -0.0101 2152 HOH A O 3140 O O . HOH K . ? 0.0817 0.0829 0.0905 -0.0060 0.0006 -0.0120 2153 HOH A O 3141 O O . HOH K . ? 0.1857 0.1864 0.1793 0.0120 0.0003 0.0255 2154 HOH A O 3142 O O . HOH K . ? 0.1898 0.2271 0.2030 -0.0335 0.0028 -0.0022 2155 HOH A O 3143 O O . HOH K . ? 0.4298 0.4068 0.4196 -0.0228 0.0047 0.0007 2156 HOH A O 3144 O O . HOH K . ? 0.2141 0.1916 0.1930 -0.0020 0.0053 -0.0038 2157 HOH A O 3145 O O . HOH K . ? 0.0901 0.0936 0.0960 -0.0197 0.0079 0.0098 2158 HOH A O 3146 O O . HOH K . ? 0.1811 0.1987 0.2138 -0.0068 0.0056 0.0003 2159 HOH A O 3147 O O . HOH K . ? 0.3725 0.3701 0.3094 -0.0124 0.0080 -0.0011 2160 HOH A O 3148 O O . HOH K . ? 0.2029 0.1809 0.2006 -0.0068 0.0237 -0.0102 2161 HOH A O 3149 O O . HOH K . ? 0.3674 0.3823 0.3991 -0.0127 -0.0124 -0.0072 2162 HOH A O 3150 O O . HOH K . ? 0.4162 0.3947 0.4198 0.0111 0.0045 -0.0046 2163 HOH A O 3151 O O . HOH K . ? 0.2758 0.2764 0.2702 -0.0115 0.0149 0.0070 2164 HOH A O 3152 O O . HOH K . ? 0.3776 0.3681 0.3947 -0.0193 -0.0101 0.0070 2165 HOH A O 3153 O O . HOH K . ? 0.2180 0.2361 0.2444 0.0070 -0.0090 -0.0147 2166 HOH A O 3154 O O . HOH K . ? 0.3349 0.3092 0.3139 0.0071 -0.0178 -0.0082 2167 HOH A O 3155 O O . HOH K . ? 0.4236 0.3858 0.3852 -0.0009 -0.0008 -0.0098 2168 HOH A O 3156 O O . HOH K . ? 0.3325 0.3222 0.2601 -0.0310 -0.0123 -0.0247 2169 HOH A O 3157 O O . HOH K . ? 0.5046 0.5064 0.5101 0.0066 0.0056 -0.0020 2170 HOH A O 3158 O O . HOH K . ? 0.4094 0.4568 0.4157 -0.0026 -0.0034 -0.0219 2171 HOH A O 3159 O O . HOH K . ? 0.1611 0.1850 0.1559 0.0049 0.0284 -0.0290 2172 HOH A O 3160 O O . HOH K . ? 0.2441 0.2123 0.2359 0.0162 -0.0151 -0.0168 2173 HOH A O 3161 O O . HOH K . ? 0.4570 0.3972 0.4250 -0.0013 0.0092 -0.0056 2174 HOH A O 3162 O O . HOH K . ? 0.2394 0.2713 0.2746 0.0209 -0.0072 -0.0187 2175 HOH A O 3163 O O . HOH K . ? 0.5413 0.5603 0.5639 0.0095 -0.0089 -0.0096 2176 HOH A O 3164 O O . HOH K . ? 0.3094 0.2268 0.2123 0.0100 -0.0080 0.0116 2177 HOH A O 3165 O O . HOH K . ? 0.0563 0.0804 0.0697 0.0159 0.0142 0.0022 2178 HOH A O 3166 O O . HOH K . ? 0.1837 0.1871 0.1999 0.0157 -0.0027 -0.0149 2179 HOH A O 3167 O O . HOH K . ? 0.2251 0.2505 0.2413 -0.0035 -0.0150 -0.0170 2180 HOH A O 3168 O O . HOH K . ? 0.3504 0.3333 0.3324 0.0280 -0.0321 0.0174 2181 HOH A O 3169 O O . HOH K . ? 0.2543 0.2405 0.2252 -0.0061 0.0113 -0.0177 2182 HOH A O 3170 O O . HOH K . ? 0.4098 0.4446 0.4012 0.0195 -0.0152 -0.0054 2183 HOH A O 3171 O O . HOH K . ? 0.2516 0.2912 0.3080 -0.0235 0.0259 0.0023 2184 HOH A O 3172 O O . HOH K . ? 0.4141 0.4196 0.4235 -0.0157 -0.0096 0.0146 2185 HOH A O 3173 O O . HOH K . ? 0.1686 0.1516 0.1222 -0.0205 -0.0081 0.0027 2186 HOH A O 3174 O O . HOH K . ? 0.2449 0.2284 0.2089 0.0148 -0.0049 -0.0143 2187 HOH A O 3175 O O . HOH K . ? 0.2418 0.2454 0.2448 0.0144 0.0206 -0.0052 2188 HOH A O 3176 O O . HOH K . ? 0.5718 0.5696 0.5541 -0.0087 0.0009 -0.0085 2189 HOH A O 3177 O O . HOH K . ? 0.2515 0.2649 0.2865 0.0099 -0.0170 -0.0189 2190 HOH A O 3178 O O . HOH K . ? 0.0860 0.0847 0.1228 0.0038 0.0179 -0.0004 2191 HOH A O 3179 O O . HOH K . ? 0.0628 0.0747 0.0931 0.0012 -0.0046 -0.0001 2192 HOH A O 3180 O O . HOH K . ? 0.3018 0.3553 0.3543 0.0128 0.0174 -0.0024 2193 HOH A O 3181 O O . HOH K . ? 0.2913 0.3149 0.2863 0.0073 -0.0054 0.0131 2194 HOH A O 3182 O O . HOH K . ? 0.3964 0.3875 0.4009 0.0123 0.0033 0.0088 2195 HOH A O 3183 O O . HOH K . ? 0.2979 0.2646 0.2939 0.0170 0.0221 0.0158 2196 HOH A O 3184 O O . HOH K . ? 0.4325 0.4506 0.4397 0.0046 0.0030 0.0130 2197 HOH A O 3185 O O . HOH K . ? 0.4175 0.4113 0.4213 0.0116 -0.0054 0.0120 2198 HOH A O 3186 O O . HOH K . ? 0.3811 0.3951 0.4098 -0.0091 -0.0121 0.0051 2199 HOH A O 3187 O O . HOH K . ? 0.4757 0.4678 0.4700 -0.0088 0.0036 0.0062 2200 HOH A O 3188 O O . HOH K . ? 0.4121 0.4220 0.3835 0.0111 -0.0081 0.0012 2201 HOH A O 3189 O O . HOH K . ? 0.4364 0.4303 0.4492 -0.0115 -0.0017 -0.0019 2202 HOH A O 3190 O O . HOH K . ? 0.1444 0.1123 0.1000 -0.0079 -0.0151 -0.0006 2203 HOH A O 3191 O O . HOH K . ? 0.2181 0.1853 0.1506 -0.0336 -0.0160 0.0125 2204 HOH A O 3192 O O . HOH K . ? 0.1391 0.1446 0.1368 0.0123 -0.0170 0.0009 2205 HOH A O 3193 O O . HOH K . ? 0.3148 0.3662 0.3394 0.0179 0.0033 0.0172 2206 HOH A O 3194 O O . HOH K . ? 0.1248 0.1643 0.1055 0.0098 -0.0128 0.0039 2207 HOH A O 3195 O O . HOH K . ? 0.4781 0.5008 0.4998 -0.0005 -0.0044 -0.0004 2208 HOH A O 3196 O O . HOH K . ? 0.4056 0.3973 0.4481 -0.0151 -0.0196 0.0044 2209 HOH A O 3197 O O . HOH K . ? 0.1393 0.1568 0.1787 0.0289 0.0122 0.0155 2210 HOH A O 3198 O O . HOH K . ? 0.4038 0.3670 0.3615 0.0085 -0.0258 -0.0054 2211 HOH A O 3199 O O . HOH K . ? 0.4735 0.4821 0.4628 0.0008 -0.0030 0.0023 2212 HOH A O 3200 O O . HOH K . ? 0.4496 0.4263 0.4061 -0.0072 -0.0113 0.0076 2213 HOH A O 3201 O O . HOH K . ? 0.4741 0.4665 0.4598 0.0018 0.0099 -0.0087 2214 HOH A O 3202 O O . HOH K . ? 0.1534 0.1447 0.1265 0.0464 -0.0183 0.0296 2215 HOH A O 3203 O O . HOH K . ? 0.3598 0.3330 0.3754 0.0077 -0.0096 0.0101 2216 HOH A O 3204 O O . HOH K . ? 0.1368 0.1342 0.1486 0.0130 0.0006 0.0066 2217 HOH A O 3205 O O . HOH K . ? 0.4021 0.4075 0.3381 0.0074 -0.0127 -0.0072 2218 HOH A O 3206 O O . HOH K . ? 0.2582 0.2376 0.2531 0.0018 -0.0030 -0.0240 2219 HOH A O 3207 O O . HOH K . ? 0.3023 0.3145 0.2987 -0.0040 0.0018 -0.0101 2220 HOH A O 3208 O O . HOH K . ? 0.3080 0.2781 0.2793 0.0098 0.0092 -0.0130 2221 HOH A O 3209 O O . HOH K . ? 0.3670 0.3475 0.3778 -0.0087 0.0172 0.0173 2222 HOH A O 3210 O O . HOH K . ? 0.5614 0.5642 0.5526 0.0068 -0.0013 0.0006 2223 HOH A O 3211 O O . HOH K . ? 0.2917 0.2567 0.2945 -0.0042 0.0209 0.0292 2224 HOH A O 3212 O O . HOH K . ? 0.5091 0.5455 0.5257 -0.0097 0.0092 0.0062 2225 HOH A O 3213 O O . HOH K . ? 0.4994 0.4840 0.4500 0.0009 -0.0017 0.0015 2226 HOH A O 3214 O O . HOH K . ? 0.2059 0.2871 0.1852 0.0047 0.0330 -0.0037 2227 HOH A O 3215 O O . HOH K . ? 0.0904 0.1240 0.1157 0.0004 -0.0066 0.0157 2228 HOH A O 3216 O O . HOH K . ? 0.4646 0.4790 0.4642 0.0102 0.0000 0.0025 2229 HOH A O 3217 O O . HOH K . ? 0.5205 0.5399 0.5030 -0.0010 0.0117 -0.0009 2230 HOH A O 3218 O O . HOH K . ? 0.3828 0.3856 0.3868 -0.0026 -0.0152 -0.0326 2231 HOH A O 3219 O O . HOH K . ? 0.3616 0.3834 0.3565 0.0190 0.0017 0.0018 2232 HOH A O 3220 O O . HOH K . ? 0.4482 0.4685 0.4686 -0.0094 -0.0051 -0.0084 2233 HOH A O 3221 O O . HOH K . ? 0.1384 0.1511 0.1874 -0.0045 -0.0060 0.0176 2234 HOH A O 3222 O O . HOH K . ? 0.1298 0.1349 0.1367 -0.0142 0.0070 -0.0059 2235 HOH A O 3223 O O . HOH K . ? 0.2301 0.2410 0.2068 -0.0162 -0.0040 0.0220 2236 HOH A O 3224 O O . HOH K . ? 0.3906 0.4136 0.4111 0.0214 -0.0068 0.0056 2237 HOH A O 3225 O O . HOH K . ? 0.3519 0.3545 0.3695 -0.0006 -0.0012 -0.0040 2238 HOH A O 3226 O O . HOH K . ? 0.1334 0.1386 0.2187 0.0239 0.0002 -0.0012 2239 HOH A O 3227 O O . HOH K . ? 0.1524 0.1749 0.1906 -0.0090 -0.0172 -0.0004 2240 HOH A O 3228 O O . HOH K . ? 0.0926 0.0997 0.1055 -0.0011 0.0063 0.0125 2241 HOH A O 3229 O O . HOH K . ? 0.0708 0.0861 0.0811 -0.0081 -0.0098 0.0131 2242 HOH A O 3230 O O . HOH K . ? 0.1246 0.1861 0.1892 0.0226 0.0059 -0.0042 2243 HOH A O 3231 O O . HOH K . ? 0.0650 0.0631 0.0786 0.0065 -0.0124 -0.0063 2244 HOH A O 3232 O O . HOH K . ? 0.1210 0.0908 0.0627 -0.0208 0.0195 0.0051 2245 HOH A O 3233 O O . HOH K . ? 0.2371 0.3492 0.3227 -0.0139 0.0238 0.0145 2246 HOH A O 3234 O O . HOH K . ? 0.4198 0.4009 0.4048 -0.0179 -0.0077 -0.0059 2247 HOH A O 3235 O O . HOH K . ? 0.2329 0.1375 0.1948 0.0131 0.0628 0.0010 2248 HOH A O 3236 O O . HOH K . ? 0.1880 0.1727 0.1896 0.0131 0.0264 0.0081 2249 HOH A O 3237 O O . HOH K . ? 0.2992 0.2139 0.2704 0.0358 0.0055 0.0095 2250 HOH A O 3238 O O . HOH K . ? 0.5067 0.5242 0.4939 0.0050 -0.0072 0.0065 2251 HOH A O 3239 O O . HOH K . ? 0.3470 0.3379 0.3752 -0.0201 0.0094 0.0014 2252 HOH A O 3240 O O . HOH K . ? 0.2867 0.3287 0.3525 0.0100 -0.0224 0.0042 2253 HOH A O 3241 O O . HOH K . ? 0.4177 0.3918 0.4073 -0.0101 -0.0073 -0.0149 2254 HOH A O 3242 O O . HOH K . ? 0.5759 0.5845 0.5778 0.0000 -0.0010 0.0009 2255 HOH A O 3243 O O . HOH K . ? 0.3401 0.3076 0.3231 0.0098 -0.0105 0.0083 2256 HOH A O 3244 O O . HOH K . ? 0.5682 0.5438 0.5498 0.0047 -0.0097 0.0099 2257 HOH A O 3245 O O . HOH K . ? 0.1533 0.1422 0.2120 -0.0181 0.0520 0.0171 2258 HOH A O 3246 O O . HOH K . ? 0.4039 0.3935 0.4193 -0.0098 -0.0214 0.0209 2259 HOH A O 3247 O O . HOH K . ? 0.1846 0.2777 0.2249 0.0080 -0.0036 0.0233 2260 HOH A O 3248 O O . HOH K . ? 0.0645 0.0773 0.0870 -0.0043 -0.0046 0.0096 2261 HOH A O 3249 O O . HOH K . ? 0.2236 0.2304 0.2769 0.0043 -0.0112 0.0117 2262 HOH A O 3250 O O . HOH K . ? 0.3500 0.2939 0.2688 0.0085 -0.0144 -0.0055 2263 HOH A O 3251 O O . HOH K . ? 0.1733 0.1838 0.1609 -0.0158 0.0140 0.0127 2264 HOH A O 3252 O O . HOH K . ? 0.4653 0.4608 0.4608 -0.0006 0.0100 0.0085 2265 HOH A O 3253 O O . HOH K . ? 0.1943 0.2280 0.2599 -0.0079 0.0340 0.0203 2266 HOH A O 3254 O O . HOH K . ? 0.3264 0.2889 0.3283 0.0187 0.0188 -0.0074 2267 HOH A O 3255 O O . HOH K . ? 0.1946 0.2538 0.2445 0.0197 0.0210 0.0128 2268 HOH A O 3256 O O . HOH K . ? 0.4099 0.4228 0.4014 0.0220 0.0093 -0.0039 2269 HOH A O 3257 O O . HOH K . ? 0.3271 0.3969 0.3748 0.0006 -0.0239 -0.0048 2270 HOH A O 3258 O O . HOH K . ? 0.3302 0.3487 0.3457 -0.0099 0.0004 -0.0026 2271 HOH A O 3259 O O . HOH K . ? 0.3089 0.3383 0.3146 -0.0084 -0.0037 0.0003 2272 HOH A O 3260 O O . HOH K . ? 0.2656 0.2623 0.2653 -0.0063 0.0056 0.0217 2273 HOH A O 3261 O O . HOH K . ? 0.2238 0.2328 0.1952 -0.0206 0.0060 0.0037 2274 HOH A O 3262 O O . HOH K . ? 0.1125 0.0948 0.1279 -0.0022 -0.0142 -0.0037 2275 HOH A O 3263 O O . HOH K . ? 0.3416 0.3729 0.4042 -0.0180 -0.0229 0.0061 2276 HOH A O 3264 O O . HOH K . ? 0.1557 0.1372 0.1488 0.0109 0.0023 -0.0081 2277 HOH A O 3265 O O . HOH K . ? 0.1011 0.1456 0.0915 0.0171 -0.0184 -0.0171 2278 HOH A O 3266 O O . HOH K . ? 0.0823 0.0880 0.0761 0.0212 0.0125 -0.0031 2279 HOH A O 3267 O O . HOH K . ? 0.0881 0.0801 0.0975 0.0133 -0.0021 -0.0078 2280 HOH A O 3268 O O . HOH K . ? 0.2194 0.2500 0.2126 0.0222 -0.0259 -0.0091 2281 HOH A O 3269 O O . HOH K . ? 0.3719 0.4066 0.3302 -0.0005 -0.0101 0.0000 2282 HOH A O 3270 O O . HOH K . ? 0.4260 0.4326 0.3980 -0.0057 -0.0060 0.0017 2283 HOH A O 3271 O O . HOH K . ? 0.4046 0.4114 0.4289 -0.0144 0.0053 -0.0220 2284 HOH A O 3272 O O . HOH K . ? 0.5322 0.5724 0.5588 0.0073 0.0083 0.0000 2285 HOH A O 3273 O O . HOH K . ? 0.3589 0.3660 0.2950 -0.0035 0.0075 0.0146 2286 HOH A O 3274 O O . HOH K . ? 0.4317 0.4222 0.4152 -0.0035 0.0270 -0.0035 2287 HOH A O 3275 O O . HOH K . ? 0.2588 0.3005 0.2414 -0.0277 0.0123 -0.0176 2288 HOH A O 3276 O O . HOH K . ? 0.3117 0.3571 0.3529 -0.0093 0.0076 0.0049 2289 HOH A O 3277 O O . HOH K . ? 0.0852 0.0778 0.0778 -0.0009 0.0020 -0.0056 2290 HOH A O 3278 O O . HOH K . ? 0.1430 0.1066 0.1862 0.0206 0.0157 0.0206 2291 HOH A O 3279 O O . HOH K . ? 0.2851 0.3047 0.2854 -0.0163 0.0051 0.0380 2292 HOH A O 3280 O O . HOH K . ? 0.2962 0.3423 0.3328 -0.0139 -0.0042 0.0205 2293 HOH A O 3281 O O . HOH K . ? 0.1490 0.1345 0.1399 0.0119 0.0038 -0.0140 2294 HOH A O 3282 O O . HOH K . ? 0.2674 0.2390 0.2492 -0.0203 -0.0012 -0.0217 2295 HOH A O 3283 O O . HOH K . ? 0.2964 0.2967 0.3545 -0.0172 -0.0184 -0.0177 2296 HOH A O 3284 O O . HOH K . ? 0.1965 0.2170 0.2698 -0.0231 0.0102 0.0258 2297 HOH A O 3285 O O . HOH K . ? 0.1396 0.1216 0.1336 -0.0148 -0.0092 -0.0011 2298 HOH A O 3286 O O . HOH K . ? 0.3863 0.3662 0.3460 -0.0151 0.0100 -0.0180 2299 HOH A O 3287 O O . HOH K . ? 0.2824 0.2877 0.3098 -0.0032 -0.0230 -0.0183 2300 HOH A O 3288 O O . HOH K . ? 0.2370 0.2090 0.3507 -0.0153 0.0071 0.0120 2301 HOH A O 3289 O O . HOH K . ? 0.4022 0.3933 0.3819 -0.0136 0.0064 -0.0301 2302 HOH A O 3290 O O . HOH K . ? 0.1707 0.1660 0.1691 -0.0211 -0.0087 -0.0170 2303 HOH A O 3291 O O . HOH K . ? 0.1116 0.1664 0.2146 -0.0076 -0.0212 -0.0102 2304 HOH A O 3292 O O . HOH K . ? 0.2594 0.2978 0.2347 0.0241 -0.0431 -0.0223 2305 HOH A O 3293 O O . HOH K . ? 0.2101 0.2670 0.2519 -0.0048 -0.0327 -0.0052 2306 HOH A O 3294 O O . HOH K . ? 0.3073 0.1741 0.2524 -0.0153 0.0225 -0.0298 2307 HOH A O 3295 O O . HOH K . ? 0.2572 0.3136 0.2627 -0.0303 -0.0209 0.0016 2308 HOH A O 3296 O O . HOH K . ? 0.3229 0.3144 0.3088 -0.0007 -0.0106 0.0071 2309 HOH A O 3297 O O . HOH K . ? 0.3589 0.3620 0.3823 0.0032 -0.0178 -0.0067 2310 HOH A O 3298 O O . HOH K . ? 0.2684 0.2913 0.2787 -0.0026 -0.0119 0.0140 2311 HOH A O 3299 O O . HOH K . ? 0.2321 0.2311 0.2387 -0.0022 -0.0026 0.0119 2312 HOH A O 3300 O O . HOH K . ? 0.4726 0.4301 0.4549 -0.0109 0.0130 -0.0104 2313 HOH A O 3301 O O . HOH K . ? 0.4081 0.4276 0.4181 0.0076 0.0028 -0.0001 2314 HOH A O 3302 O O . HOH K . ? 0.2717 0.2447 0.2787 -0.0088 -0.0131 -0.0160 2315 HOH A O 3303 O O . HOH K . ? 0.0419 0.0887 0.0905 -0.0029 0.0257 0.0227 2316 HOH A O 3304 O O . HOH K . ? 0.2966 0.3465 0.3195 0.0205 -0.0033 0.0325 2317 HOH A O 3305 O O . HOH K . ? 0.3163 0.3286 0.3750 -0.0005 -0.0110 0.0056 2318 HOH A O 3306 O O . HOH K . ? 0.0629 0.0706 0.0534 0.0046 0.0002 -0.0059 2319 HOH A O 3307 O O . HOH K . ? 0.1141 0.1026 0.0826 -0.0049 -0.0045 -0.0124 2320 HOH A O 3308 O O . HOH K . ? 0.0859 0.0799 0.1111 -0.0044 0.0034 -0.0061 2321 HOH A O 3309 O O . HOH K . ? 0.0602 0.0667 0.0520 -0.0031 0.0015 0.0033 2322 HOH A O 3310 O O . HOH K . ? 0.0662 0.0690 0.0602 0.0118 0.0040 0.0078 2323 HOH A O 3311 O O . HOH K . ? 0.1617 0.1628 0.2044 -0.0068 0.0165 -0.0004 2324 HOH A O 3312 O O . HOH K . ? 0.0459 0.0646 0.0563 0.0073 -0.0104 -0.0021 2325 HOH A O 3313 O O . HOH K . ? 0.2967 0.2361 0.2541 0.0089 -0.0263 0.0276 2326 HOH A O 3314 O O . HOH K . ? 0.3986 0.3690 0.3981 0.0072 0.0110 -0.0008 2327 HOH A O 3315 O O . HOH K . ? 0.2430 0.2236 0.2331 0.0059 0.0233 -0.0073 2328 HOH A O 3316 O O . HOH K . ? 0.2373 0.2847 0.2406 0.0050 0.0426 -0.0010 2329 HOH A O 3317 O O . HOH K . ? 0.0943 0.0938 0.0795 0.0004 0.0054 -0.0111 2330 HOH A O 3318 O O . HOH K . ? 0.2357 0.2659 0.2209 -0.0018 0.0147 -0.0186 2331 HOH A O 3319 O O . HOH K . ? 0.1084 0.1216 0.1046 0.0105 -0.0219 0.0087 2332 HOH A O 3320 O O . HOH K . ? 0.1403 0.1541 0.1261 0.0058 0.0029 0.0050 2333 HOH A O 3321 O O . HOH K . ? 0.4624 0.4519 0.4418 0.0036 0.0132 -0.0062 2334 HOH A O 3322 O O . HOH K . ? 0.1206 0.1105 0.1366 0.0373 -0.0208 -0.0149 2335 HOH A O 3323 O O . HOH K . ? 0.1808 0.2075 0.1910 0.0107 -0.0195 -0.0248 2336 HOH A O 3324 O O . HOH K . ? 0.3613 0.3619 0.3713 0.0072 0.0096 0.0034 2337 HOH A O 3325 O O . HOH K . ? 0.2054 0.1645 0.1493 0.0387 0.0308 0.0394 2338 HOH A O 3326 O O . HOH K . ? 0.3223 0.2698 0.2679 -0.0202 -0.0059 0.0114 2339 HOH A O 3327 O O . HOH K . ? 0.4195 0.4143 0.4093 0.0087 -0.0048 0.0046 2340 HOH A O 3328 O O . HOH K . ? 0.2600 0.2650 0.2729 0.0278 0.0189 0.0379 2341 HOH A O 3329 O O . HOH K . ? 0.2521 0.2668 0.2062 0.0055 0.0076 -0.0035 2342 HOH A O 3330 O O . HOH K . ? 0.1667 0.2094 0.1411 0.0205 -0.0056 0.0217 2343 HOH A O 3331 O O . HOH K . ? 0.2139 0.2009 0.1789 -0.0275 0.0028 0.0044 2344 HOH A O 3332 O O . HOH K . ? 0.1264 0.1886 0.0996 0.0056 -0.0184 -0.0252 2345 HOH A O 3333 O O . HOH K . ? 0.3027 0.3446 0.3373 0.0011 -0.0151 -0.0108 2346 HOH A O 3334 O O . HOH K . ? 0.2712 0.2479 0.2734 -0.0130 -0.0085 0.0139 2347 HOH A O 3335 O O . HOH K . ? 0.0936 0.0813 0.0981 -0.0049 -0.0038 -0.0158 2348 HOH A O 3336 O O . HOH K . ? 0.1427 0.2037 0.1327 -0.0080 -0.0273 -0.0300 2349 HOH A O 3337 O O . HOH K . ? 0.4702 0.4620 0.4366 -0.0170 -0.0200 0.0083 2350 HOH A O 3338 O O . HOH K . ? 0.2377 0.2369 0.2599 -0.0072 -0.0026 0.0135 2351 HOH A O 3339 O O . HOH K . ? 0.4397 0.4328 0.4116 0.0083 -0.0075 0.0127 2352 HOH A O 3340 O O . HOH K . ? 0.2554 0.2362 0.2839 -0.0043 -0.0161 -0.0108 2353 HOH A O 3341 O O . HOH K . ? 0.2432 0.2143 0.3130 0.0266 0.0001 0.0210 2354 HOH A O 3342 O O . HOH K . ? 0.4385 0.4571 0.4136 -0.0069 -0.0086 0.0032 2355 HOH A O 3343 O O . HOH K . ? 0.4154 0.3871 0.4271 0.0175 -0.0243 -0.0060 2356 HOH A O 3344 O O . HOH K . ? 0.3008 0.3164 0.2950 0.0057 -0.0015 0.0035 2357 HOH A O 3345 O O . HOH K . ? 0.2889 0.2984 0.2931 -0.0128 -0.0182 0.0092 2358 HOH A O 3346 O O . HOH K . ? 0.3183 0.3054 0.2792 0.0093 -0.0091 0.0028 2359 HOH A O 3347 O O . HOH K . ? 0.3806 0.3641 0.3244 0.0421 -0.0041 -0.0184 2360 HOH A O 3348 O O . HOH K . ? 0.2216 0.2250 0.3532 -0.0165 0.0067 -0.0214 2361 HOH A O 3349 O O . HOH K . ? 0.4284 0.4530 0.4270 0.0043 0.0209 -0.0145 2362 HOH A O 3350 O O . HOH K . ? 0.3547 0.3930 0.4268 0.0029 -0.0084 -0.0225 2363 HOH A O 3351 O O . HOH K . ? 0.4136 0.4352 0.3985 -0.0120 0.0095 0.0031 2364 HOH A O 3352 O O . HOH K . ? 0.2927 0.2990 0.3510 -0.0158 0.0212 -0.0207 2365 HOH A O 3353 O O . HOH K . ? 0.3079 0.2480 0.2103 0.0138 -0.0035 0.0188 2366 HOH A O 3354 O O . HOH K . ? 0.2717 0.2441 0.2210 0.0017 -0.0209 -0.0165 2367 HOH A O 3355 O O . HOH K . ? 0.4159 0.4204 0.4025 0.0147 -0.0169 0.0108 2368 HOH A O 3356 O O . HOH K . ? 0.3268 0.3194 0.2924 -0.0009 0.0029 -0.0081 2369 HOH A O 3357 O O . HOH K . ? 0.1854 0.2817 0.2665 -0.0057 0.0384 -0.0028 2370 HOH A O 3358 O O . HOH K . ? 0.2137 0.1788 0.1930 0.0079 -0.0019 0.0009 2371 HOH A O 3359 O O . HOH K . ? 0.3743 0.3973 0.3902 0.0047 0.0031 0.0049 2372 HOH A O 3360 O O . HOH K . ? 0.0913 0.0611 0.1215 -0.0129 -0.0027 0.0224 2373 HOH A O 3361 O O . HOH K . ? 0.3130 0.3747 0.3012 0.0047 0.0055 0.0083 2374 HOH A O 3362 O O . HOH K . ? 0.0402 0.0472 0.0626 -0.0055 0.0100 -0.0010 2375 HOH A O 3363 O O . HOH K . ? 0.2749 0.3069 0.2634 0.0119 -0.0114 0.0143 2376 HOH A O 3364 O O . HOH K . ? 0.4466 0.4831 0.4716 -0.0060 0.0009 0.0018 2377 HOH A O 3365 O O . HOH K . ? 0.2373 0.2784 0.1986 0.0165 -0.0213 0.0086 2378 HOH A O 3366 O O . HOH K . ? 0.3569 0.3314 0.3966 -0.0002 -0.0044 -0.0102 2379 HOH A O 3367 O O . HOH K . ? 0.1329 0.0995 0.1129 0.0114 -0.0072 0.0194 2380 HOH A O 3368 O O . HOH K . ? 0.2640 0.3141 0.3206 -0.0006 -0.0258 -0.0026 2381 HOH A O 3369 O O . HOH K . ? 0.2332 0.2900 0.2887 -0.0073 0.0167 0.0283 2382 HOH A O 3370 O O . HOH K . ? 0.1982 0.2351 0.2153 -0.0003 -0.0010 0.0032 2383 HOH A O 3371 O O . HOH K . ? 0.4466 0.4511 0.4662 -0.0042 -0.0097 -0.0122 2384 HOH A O 3372 O O . HOH K . ? 0.4659 0.4358 0.4673 0.0053 -0.0091 -0.0073 2385 HOH A O 3373 O O . HOH K . ? 0.4098 0.4045 0.4272 -0.0009 -0.0147 -0.0027 2386 HOH A O 3374 O O . HOH K . ? 0.3566 0.3581 0.3333 -0.0078 0.0078 -0.0135 2387 HOH A O 3375 O O . HOH K . ? 0.2905 0.3109 0.2924 0.0053 -0.0154 0.0069 2388 HOH A O 3376 O O . HOH K . ? 0.4164 0.4230 0.4258 -0.0120 -0.0020 -0.0087 2389 HOH A O 3377 O O . HOH K . ? 0.5263 0.5186 0.5165 -0.0102 0.0002 0.0003 2390 HOH A O 3378 O O . HOH K . ? 0.2927 0.2637 0.3437 0.0013 -0.0204 -0.0119 2391 HOH A O 3379 O O . HOH K . ? 0.4079 0.4197 0.4022 -0.0171 -0.0040 -0.0166 2392 HOH A O 3380 O O . HOH K . ? 0.3108 0.3109 0.2730 0.0185 -0.0003 0.0111 2393 HOH A O 3381 O O . HOH K . ? 0.2611 0.2850 0.2592 -0.0145 -0.0063 0.0060 2394 HOH A O 3382 O O . HOH K . ? 0.2374 0.2054 0.2039 0.0152 -0.0484 -0.0124 2395 HOH A O 3383 O O . HOH K . ? 0.4755 0.4205 0.4325 -0.0003 0.0108 0.0011 2396 HOH A O 3384 O O . HOH K . ? 0.1668 0.1394 0.1147 -0.0038 -0.0219 -0.0084 2397 HOH A O 3385 O O . HOH K . ? 0.2698 0.2499 0.2509 -0.0155 -0.0065 -0.0030 2398 HOH A O 3386 O O . HOH K . ? 0.2207 0.1799 0.2322 0.0258 -0.0118 -0.0348 2399 HOH A O 3387 O O . HOH K . ? 0.1234 0.1427 0.1102 -0.0306 0.0168 -0.0025 2400 HOH A O 3388 O O . HOH K . ? 0.1959 0.2402 0.1680 0.0366 -0.0055 -0.0118 2401 HOH A O 3389 O O . HOH K . ? 0.1264 0.1287 0.1688 0.0193 0.0037 -0.0065 2402 HOH A O 3390 O O . HOH K . ? 0.1867 0.2138 0.1972 -0.0037 0.0168 -0.0211 2403 HOH A O 3391 O O . HOH K . ? 0.1487 0.1407 0.1765 0.0068 0.0195 -0.0148 2404 HOH A O 3392 O O . HOH K . ? 0.0712 0.0895 0.0757 0.0256 0.0039 0.0110 2405 HOH A O 3393 O O . HOH K . ? 0.2325 0.2281 0.2468 -0.0121 -0.0143 -0.0050 2406 HOH A O 3394 O O . HOH K . ? 0.0898 0.0995 0.1044 0.0097 0.0198 0.0039 2407 HOH A O 3395 O O . HOH K . ? 0.3165 0.3620 0.3978 -0.0028 0.0063 -0.0098 2408 HOH A O 3396 O O . HOH K . ? 0.4566 0.4280 0.4313 0.0079 0.0011 -0.0052 2409 HOH A O 3397 O O . HOH K . ? 0.3221 0.3335 0.3521 0.0020 0.0155 0.0168 2410 HOH A O 3398 O O . HOH K . ? 0.2205 0.2258 0.2158 0.0072 0.0121 -0.0126 2411 HOH A O 3399 O O . HOH K . ? 0.1832 0.1611 0.1920 0.0005 0.0117 0.0080 2412 HOH A O 3400 O O . HOH K . ? 0.1018 0.1138 0.0775 0.0017 -0.0060 0.0052 2413 HOH A O 3401 O O . HOH K . ? 0.2454 0.3190 0.2738 0.0174 0.0045 -0.0280 2414 HOH A O 3402 O O . HOH K . ? 0.1956 0.2131 0.2115 0.0042 0.0030 0.0240 2415 HOH A O 3403 O O . HOH K . ? 0.3503 0.3677 0.3726 -0.0083 -0.0044 -0.0077 2416 HOH A O 3404 O O . HOH K . ? 0.1912 0.2697 0.2045 -0.0120 -0.0058 0.0305 2417 HOH A O 3405 O O . HOH K . ? 0.3272 0.3731 0.3623 -0.0214 -0.0064 0.0000 2418 HOH A O 3406 O O . HOH K . ? 0.4607 0.4825 0.4628 0.0007 -0.0085 -0.0101 2419 HOH A O 3407 O O . HOH K . ? 0.3447 0.2989 0.3090 -0.0344 -0.0322 -0.0083 2420 HOH A O 3408 O O . HOH K . ? 0.2486 0.2211 0.1760 0.0151 -0.0366 0.0226 2421 HOH A O 3409 O O . HOH K . ? 0.2346 0.1859 0.3044 -0.0174 -0.0149 0.0034 2422 HOH A O 3410 O O . HOH K . ? 0.5306 0.5205 0.5312 -0.0027 -0.0028 -0.0020 2423 HOH A O 3411 O O . HOH K . ? 0.4902 0.4709 0.4814 -0.0006 -0.0003 -0.0074 2424 HOH A O 3412 O O . HOH K . ? 0.3426 0.3619 0.3252 -0.0179 -0.0062 -0.0002 2425 HOH A O 3413 O O . HOH K . ? 0.2282 0.2152 0.2425 -0.0469 0.0019 -0.0098 2426 HOH A O 3414 O O . HOH K . ? 0.2993 0.3845 0.3373 0.0050 -0.0017 0.0143 2427 HOH A O 3415 O O . HOH K . ? 0.2895 0.3199 0.2853 -0.0012 0.0227 -0.0057 2428 HOH A O 3416 O O . HOH K . ? 0.1284 0.1957 0.2212 -0.0291 -0.0417 0.0174 2429 HOH A O 3417 O O . HOH K . ? 0.1639 0.2052 0.1495 -0.0091 0.0220 -0.0130 2430 HOH A O 3418 O O . HOH K . ? 0.1256 0.1853 0.1424 -0.0046 -0.0137 0.0425 2431 HOH A O 3419 O O . HOH K . ? 0.4201 0.3839 0.3539 -0.0045 0.0169 -0.0033 2432 HOH A O 3420 O O . HOH K . ? 0.3291 0.3206 0.3024 0.0265 -0.0041 -0.0201 2433 HOH A O 3421 O O . HOH K . ? 0.2460 0.2354 0.2300 0.0053 0.0074 -0.0090 2434 HOH A O 3422 O O . HOH K . ? 0.1264 0.1567 0.1421 0.0043 0.0084 -0.0087 2435 HOH A O 3423 O O . HOH K . ? 0.1448 0.1250 0.1376 0.0113 0.0257 0.0006 2436 HOH A O 3424 O O . HOH K . ? 0.4643 0.4631 0.4400 -0.0040 -0.0066 0.0008 2437 HOH A O 3425 O O . HOH K . ? 0.2037 0.2996 0.1565 -0.0123 0.0085 0.0202 2438 HOH A O 3426 O O . HOH K . ? 0.2516 0.2998 0.3134 0.0035 -0.0288 0.0169 2439 HOH A O 3427 O O . HOH K . ? 0.4322 0.4173 0.4346 0.0000 -0.0058 -0.0038 2440 HOH A O 3428 O O . HOH K . ? 0.3695 0.3303 0.3159 0.0146 0.0000 0.0039 2441 HOH A O 3429 O O . HOH K . ? 0.3082 0.3092 0.2909 -0.0096 0.0055 0.0081 2442 HOH A O 3430 O O . HOH K . ? 0.2342 0.2383 0.2464 0.0039 -0.0168 0.0070 2443 HOH A O 3431 O O . HOH K . ? 0.2113 0.2095 0.2209 0.0017 -0.0055 -0.0002 2444 HOH A O 3432 O O . HOH K . ? 0.2356 0.2980 0.2834 0.0117 0.0166 0.0053 2445 HOH A O 3433 O O . HOH K . ? 0.2727 0.2428 0.2586 0.0200 0.0195 -0.0298 2446 HOH A O 3434 O O . HOH K . ? 0.2095 0.2363 0.1957 0.0418 0.0061 -0.0118 2447 HOH A O 3435 O O . HOH K . ? 0.2529 0.1965 0.2139 -0.0063 0.0057 -0.0082 2448 HOH A O 3436 O O . HOH K . ? 0.1620 0.1764 0.1856 -0.0166 0.0081 -0.0131 2449 HOH A O 3437 O O . HOH K . ? 0.4093 0.4383 0.3857 0.0007 0.0156 0.0003 2450 HOH A O 3438 O O . HOH K . ? 0.1656 0.1376 0.1307 -0.0061 0.0259 0.0000 2451 HOH A O 3439 O O . HOH K . ? 0.3314 0.3858 0.3619 0.0054 0.0141 0.0192 2452 HOH A O 3440 O O . HOH K . ? 0.1137 0.1065 0.1478 0.0118 -0.0126 -0.0269 2453 HOH A O 3441 O O . HOH K . ? 0.2210 0.2700 0.2629 0.0099 -0.0094 -0.0067 2454 HOH A O 3442 O O . HOH K . ? 0.4531 0.4780 0.4560 0.0166 0.0097 -0.0196 2455 HOH A O 3443 O O . HOH K . ? 0.4278 0.4394 0.4503 0.0060 0.0083 0.0013 2456 HOH A O 3444 O O . HOH K . ? 0.2517 0.2498 0.2414 0.0032 0.0033 -0.0203 2457 HOH A O 3445 O O . HOH K . ? 0.4303 0.4366 0.4488 -0.0014 -0.0099 -0.0005 2458 HOH A O 3446 O O . HOH K . ? 0.2935 0.3366 0.3119 0.0126 0.0070 0.0052 2459 HOH A O 3447 O O . HOH K . ? 0.2872 0.2863 0.2966 -0.0035 0.0201 0.0066 2460 HOH A O 3448 O O . HOH K . ? 0.2691 0.2943 0.2763 0.0015 -0.0175 -0.0030 2461 HOH A O 3449 O O . HOH K . ? 0.2812 0.2922 0.3119 0.0062 -0.0119 0.0101 2462 HOH A O 3450 O O . HOH K . ? 0.1526 0.2469 0.2030 -0.0009 -0.0012 0.0091 2463 HOH A O 3451 O O . HOH K . ? 0.2740 0.2151 0.1886 0.0104 0.0057 -0.0146 2464 HOH A O 3452 O O . HOH K . ? 0.1727 0.1568 0.1477 -0.0052 0.0159 0.0105 2465 HOH A O # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ALA 1 87 87 ALA ALA A . n A 1 2 PRO 2 88 88 PRO PRO A . n A 1 3 TYR 3 89 89 TYR TYR A . n A 1 4 ASN 4 90 90 ASN ASN A . n A 1 5 GLY 5 91 91 GLY GLY A . n A 1 6 ASN 6 92 92 ASN ASN A . n A 1 7 PRO 7 93 93 PRO PRO A . n A 1 8 PHE 8 94 94 PHE PHE A . n A 1 9 GLU 9 95 95 GLU GLU A . n A 1 10 GLY 10 96 96 GLY GLY A . n A 1 11 VAL 11 97 97 VAL VAL A . n A 1 12 GLN 12 98 98 GLN GLN A . n A 1 13 LEU 13 99 99 LEU LEU A . n A 1 14 TRP 14 100 100 TRP TRP A . n A 1 15 ALA 15 101 101 ALA ALA A . n A 1 16 ASN 16 102 102 ASN ASN A . n A 1 17 ASN 17 103 103 ASN ASN A . n A 1 18 TYR 18 104 104 TYR TYR A . n A 1 19 TYR 19 105 105 TYR TYR A . n A 1 20 ARG 20 106 106 ARG ARG A . n A 1 21 SER 21 107 107 SER SER A . n A 1 22 GLU 22 108 108 GLU GLU A . n A 1 23 VAL 23 109 109 VAL VAL A . n A 1 24 HIS 24 110 110 HIS HIS A . n A 1 25 THR 25 111 111 THR THR A . n A 1 26 LEU 26 112 112 LEU LEU A . n A 1 27 ALA 27 113 113 ALA ALA A . n A 1 28 ILE 28 114 114 ILE ILE A . n A 1 29 PRO 29 115 115 PRO PRO A . n A 1 30 GLN 30 116 116 GLN GLN A . n A 1 31 ILE 31 117 117 ILE ILE A . n A 1 32 THR 32 118 118 THR THR A . n A 1 33 ASP 33 119 119 ASP ASP A . n A 1 34 PRO 34 120 120 PRO PRO A . n A 1 35 ALA 35 121 121 ALA ALA A . n A 1 36 LEU 36 122 122 LEU LEU A . n A 1 37 ARG 37 123 123 ARG ARG A . n A 1 38 ALA 38 124 124 ALA ALA A . n A 1 39 ALA 39 125 125 ALA ALA A . n A 1 40 ALA 40 126 126 ALA ALA A . n A 1 41 SER 41 127 127 SER SER A . n A 1 42 ALA 42 128 128 ALA ALA A . n A 1 43 VAL 43 129 129 VAL VAL A . n A 1 44 ALA 44 130 130 ALA ALA A . n A 1 45 GLU 45 131 131 GLU GLU A . n A 1 46 VAL 46 132 132 VAL VAL A . n A 1 47 PRO 47 133 133 PRO PRO A . n A 1 48 SER 48 134 134 SER SER A . n A 1 49 PHE 49 135 135 PHE PHE A . n A 1 50 GLN 50 136 136 GLN GLN A . n A 1 51 TRP 51 137 137 TRP TRP A . n A 1 52 LEU 52 138 138 LEU LEU A . n A 1 53 ASP 53 139 139 ASP ASP A . n A 1 54 ARG 54 140 140 ARG ARG A . n A 1 55 ASN 55 141 141 ASN ASN A . n A 1 56 VAL 56 142 142 VAL VAL A . n A 1 57 THR 57 143 143 THR THR A . n A 1 58 VAL 58 144 144 VAL VAL A . n A 1 59 ASP 59 145 145 ASP ASP A . n A 1 60 THR 60 146 146 THR THR A . n A 1 61 LEU 61 147 147 LEU LEU A . n A 1 62 LEU 62 148 148 LEU LEU A . n A 1 63 VAL 63 149 149 VAL VAL A . n A 1 64 GLN 64 150 150 GLN GLN A . n A 1 65 THR 65 151 151 THR THR A . n A 1 66 LEU 66 152 152 LEU LEU A . n A 1 67 SER 67 153 153 SER SER A . n A 1 68 GLU 68 154 154 GLU GLU A . n A 1 69 ILE 69 155 155 ILE ILE A . n A 1 70 ARG 70 156 156 ARG ARG A . n A 1 71 GLU 71 157 157 GLU GLU A . n A 1 72 ALA 72 158 158 ALA ALA A . n A 1 73 ASN 73 159 159 ASN ASN A . n A 1 74 GLN 74 160 160 GLN GLN A . n A 1 75 ALA 75 161 161 ALA ALA A . n A 1 76 GLY 76 162 162 GLY GLY A . n A 1 77 ALA 77 163 163 ALA ALA A . n A 1 78 ASN 78 164 164 ASN ASN A . n A 1 79 PRO 79 165 165 PRO PRO A . n A 1 80 GLN 80 166 166 GLN GLN A . n A 1 81 TYR 81 167 167 TYR TYR A . n A 1 82 ALA 82 168 168 ALA ALA A . n A 1 83 ALA 83 169 169 ALA ALA A . n A 1 84 GLN 84 170 170 GLN GLN A . n A 1 85 ILE 85 171 171 ILE ILE A . n A 1 86 VAL 86 172 172 VAL VAL A . n A 1 87 VAL 87 173 173 VAL VAL A . n A 1 88 TYR 88 174 174 TYR TYR A . n A 1 89 ASP 89 175 175 ASP ASP A . n A 1 90 LEU 90 176 176 LEU LEU A . n A 1 91 PRO 91 177 177 PRO PRO A . n A 1 92 ASP 92 178 178 ASP ASP A . n A 1 93 ARG 93 179 179 ARG ARG A . n A 1 94 ASP 94 180 180 ASP ASP A . n A 1 95 CYS 95 181 181 CYS CYS A . n A 1 96 ALA 96 182 182 ALA ALA A . n A 1 97 ALA 97 183 183 ALA ALA A . n A 1 98 ALA 98 184 184 ALA ALA A . n A 1 99 ALA 99 185 185 ALA ALA A . n A 1 100 SER 100 186 186 SER SER A . n A 1 101 ASN 101 187 187 ASN ASN A . n A 1 102 GLY 102 188 188 GLY GLY A . n A 1 103 GLU 103 189 189 GLU GLU A . n A 1 104 TRP 104 190 190 TRP TRP A . n A 1 105 ALA 105 191 191 ALA ALA A . n A 1 106 ILE 106 192 192 ILE ILE A . n A 1 107 ALA 107 193 193 ALA ALA A . n A 1 108 ASN 108 194 194 ASN ASN A . n A 1 109 ASN 109 195 195 ASN ASN A . n A 1 110 GLY 110 196 196 GLY GLY A . n A 1 111 VAL 111 197 197 VAL VAL A . n A 1 112 ASN 112 198 198 ASN ASN A . n A 1 113 ASN 113 199 199 ASN ASN A . n A 1 114 TYR 114 200 200 TYR TYR A . n A 1 115 LYS 115 201 201 LYS LYS A . n A 1 116 ALA 116 202 202 ALA ALA A . n A 1 117 TYR 117 203 203 TYR TYR A . n A 1 118 ILE 118 204 204 ILE ILE A . n A 1 119 ASN 119 205 205 ASN ASN A . n A 1 120 ARG 120 206 206 ARG ARG A . n A 1 121 ILE 121 207 207 ILE ILE A . n A 1 122 ARG 122 208 208 ARG ARG A . n A 1 123 GLU 123 209 209 GLU GLU A . n A 1 124 ILE 124 210 210 ILE ILE A . n A 1 125 LEU 125 211 211 LEU LEU A . n A 1 126 ILE 126 212 212 ILE ILE A . n A 1 127 SER 127 213 213 SER SER A . n A 1 128 PHE 128 214 214 PHE PHE A . n A 1 129 SER 129 215 215 SER SER A . n A 1 130 ASP 130 216 216 ASP ASP A . n A 1 131 VAL 131 217 217 VAL VAL A . n A 1 132 ARG 132 218 218 ARG ARG A . n A 1 133 THR 133 219 219 THR THR A . n A 1 134 ILE 134 220 220 ILE ILE A . n A 1 135 LEU 135 221 221 LEU LEU A . n A 1 136 VAL 136 222 222 VAL VAL A . n A 1 137 ILE 137 223 223 ILE ILE A . n A 1 138 GLU 138 224 224 GLU GLU A . n A 1 139 PRO 139 225 225 PRO PRO A . n A 1 140 ASP 140 226 226 ASP ASP A . n A 1 141 SER 141 227 227 SER SER A . n A 1 142 LEU 142 228 228 LEU LEU A . n A 1 143 ALA 143 229 229 ALA ALA A . n A 1 144 ASN 144 230 230 ASN ASN A . n A 1 145 MET 145 231 231 MET MET A . n A 1 146 VAL 146 232 232 VAL VAL A . n A 1 147 THR 147 233 233 THR THR A . n A 1 148 ASN 148 234 234 ASN ASN A . n A 1 149 MET 149 235 235 MET MET A . n A 1 150 ASN 150 236 236 ASN ASN A . n A 1 151 VAL 151 237 237 VAL VAL A . n A 1 152 PRO 152 238 238 PRO PRO A . n A 1 153 LYS 153 239 239 LYS LYS A . n A 1 154 CYS 154 240 240 CYS CYS A . n A 1 155 SER 155 241 241 SER SER A . n A 1 156 GLY 156 242 242 GLY GLY A . n A 1 157 ALA 157 243 243 ALA ALA A . n A 1 158 ALA 158 244 244 ALA ALA A . n A 1 159 SER 159 245 245 SER SER A . n A 1 160 THR 160 246 246 THR THR A . n A 1 161 TYR 161 247 247 TYR TYR A . n A 1 162 ARG 162 248 248 ARG ARG A . n A 1 163 GLU 163 249 249 GLU GLU A . n A 1 164 LEU 164 250 250 LEU LEU A . n A 1 165 THR 165 251 251 THR THR A . n A 1 166 ILE 166 252 252 ILE ILE A . n A 1 167 TYR 167 253 253 TYR TYR A . n A 1 168 ALA 168 254 254 ALA ALA A . n A 1 169 LEU 169 255 255 LEU LEU A . n A 1 170 LYS 170 256 256 LYS LYS A . n A 1 171 GLN 171 257 257 GLN GLN A . n A 1 172 LEU 172 258 258 LEU LEU A . n A 1 173 ASP 173 259 259 ASP ASP A . n A 1 174 LEU 174 260 260 LEU LEU A . n A 1 175 PRO 175 261 261 PRO PRO A . n A 1 176 HIS 176 262 262 HIS HIS A . n A 1 177 VAL 177 263 263 VAL VAL A . n A 1 178 ALA 178 264 264 ALA ALA A . n A 1 179 MET 179 265 265 MET MET A . n A 1 180 TYR 180 266 266 TYR TYR A . n A 1 181 MET 181 267 267 MET MET A . n A 1 182 ASP 182 268 268 ASP ASP A . n A 1 183 ALA 183 269 269 ALA ALA A . n A 1 184 GLY 184 270 270 GLY GLY A . n A 1 185 HIS 185 271 271 HIS HIS A . n A 1 186 ALA 186 272 272 ALA ALA A . n A 1 187 GLY 187 273 273 GLY GLY A . n A 1 188 TRP 188 274 274 TRP TRP A . n A 1 189 LEU 189 275 275 LEU LEU A . n A 1 190 GLY 190 276 276 GLY GLY A . n A 1 191 TRP 191 277 277 TRP TRP A . n A 1 192 PRO 192 278 278 PRO PRO A . n A 1 193 ALA 193 279 279 ALA ALA A . n A 1 194 ASN 194 280 280 ASN ASN A . n A 1 195 ILE 195 281 281 ILE ILE A . n A 1 196 GLN 196 282 282 GLN GLN A . n A 1 197 PRO 197 283 283 PRO PRO A . n A 1 198 ALA 198 284 284 ALA ALA A . n A 1 199 ALA 199 285 285 ALA ALA A . n A 1 200 GLU 200 286 286 GLU GLU A . n A 1 201 LEU 201 287 287 LEU LEU A . n A 1 202 PHE 202 288 288 PHE PHE A . n A 1 203 ALA 203 289 289 ALA ALA A . n A 1 204 LYS 204 290 290 LYS LYS A . n A 1 205 ILE 205 291 291 ILE ILE A . n A 1 206 TYR 206 292 292 TYR TYR A . n A 1 207 GLU 207 293 293 GLU GLU A . n A 1 208 ASP 208 294 294 ASP ASP A . n A 1 209 ALA 209 295 295 ALA ALA A . n A 1 210 GLY 210 296 296 GLY GLY A . n A 1 211 LYS 211 297 297 LYS LYS A . n A 1 212 PRO 212 298 298 PRO PRO A . n A 1 213 ARG 213 299 299 ARG ARG A . n A 1 214 ALA 214 300 300 ALA ALA A . n A 1 215 VAL 215 301 301 VAL VAL A . n A 1 216 ARG 216 302 302 ARG ARG A . n A 1 217 GLY 217 303 303 GLY GLY A . n A 1 218 LEU 218 304 304 LEU LEU A . n A 1 219 ALA 219 305 305 ALA ALA A . n A 1 220 THR 220 306 306 THR THR A . n A 1 221 ASN 221 307 307 ASN ASN A . n A 1 222 VAL 222 308 308 VAL VAL A . n A 1 223 ALA 223 309 309 ALA ALA A . n A 1 224 ASN 224 310 310 ASN ASN A . n A 1 225 TYR 225 311 311 TYR TYR A . n A 1 226 ASN 226 312 312 ASN ASN A . n A 1 227 ALA 227 313 313 ALA ALA A . n A 1 228 TRP 228 314 314 TRP TRP A . n A 1 229 SER 229 315 315 SER SER A . n A 1 230 VAL 230 316 316 VAL VAL A . n A 1 231 SER 231 317 317 SER SER A . n A 1 232 SER 232 318 318 SER SER A . n A 1 233 PRO 233 319 319 PRO PRO A . n A 1 234 PRO 234 320 320 PRO PRO A . n A 1 235 PRO 235 321 321 PRO PRO A . n A 1 236 TYR 236 322 322 TYR TYR A . n A 1 237 THR 237 323 323 THR THR A . n A 1 238 SER 238 324 324 SER SER A . n A 1 239 PRO 239 325 325 PRO PRO A . n A 1 240 ASN 240 326 326 ASN ASN A . n A 1 241 PRO 241 327 327 PRO PRO A . n A 1 242 ASN 242 328 328 ASN ASN A . n A 1 243 TYR 243 329 329 TYR TYR A . n A 1 244 ASP 244 330 330 ASP ASP A . n A 1 245 GLU 245 331 331 GLU GLU A . n A 1 246 LYS 246 332 332 LYS LYS A . n A 1 247 HIS 247 333 333 HIS HIS A . n A 1 248 TYR 248 334 334 TYR TYR A . n A 1 249 ILE 249 335 335 ILE ILE A . n A 1 250 GLU 250 336 336 GLU GLU A . n A 1 251 ALA 251 337 337 ALA ALA A . n A 1 252 PHE 252 338 338 PHE PHE A . n A 1 253 ARG 253 339 339 ARG ARG A . n A 1 254 PRO 254 340 340 PRO PRO A . n A 1 255 LEU 255 341 341 LEU LEU A . n A 1 256 LEU 256 342 342 LEU LEU A . n A 1 257 GLU 257 343 343 GLU GLU A . n A 1 258 ALA 258 344 344 ALA ALA A . n A 1 259 ARG 259 345 345 ARG ARG A . n A 1 260 GLY 260 346 346 GLY GLY A . n A 1 261 PHE 261 347 347 PHE PHE A . n A 1 262 PRO 262 348 348 PRO PRO A . n A 1 263 ALA 263 349 349 ALA ALA A . n A 1 264 GLN 264 350 350 GLN GLN A . n A 1 265 PHE 265 351 351 PHE PHE A . n A 1 266 ILE 266 352 352 ILE ILE A . n A 1 267 VAL 267 353 353 VAL VAL A . n A 1 268 ASP 268 354 354 ASP ASP A . n A 1 269 GLN 269 355 355 GLN GLN A . n A 1 270 GLY 270 356 356 GLY GLY A . n A 1 271 ARG 271 357 357 ARG ARG A . n A 1 272 SER 272 358 358 SER SER A . n A 1 273 GLY 273 359 359 GLY GLY A . n A 1 274 LYS 274 360 360 LYS LYS A . n A 1 275 GLN 275 361 361 GLN GLN A . n A 1 276 PRO 276 362 362 PRO PRO A . n A 1 277 THR 277 363 363 THR THR A . n A 1 278 GLY 278 364 364 GLY GLY A . n A 1 279 GLN 279 365 365 GLN GLN A . n A 1 280 LYS 280 366 366 LYS LYS A . n A 1 281 GLU 281 367 367 GLU GLU A . n A 1 282 TRP 282 368 368 TRP TRP A . n A 1 283 GLY 283 369 369 GLY GLY A . n A 1 284 HIS 284 370 370 HIS HIS A . n A 1 285 TRP 285 371 371 TRP TRP A . n A 1 286 CYS 286 372 372 CYS CYS A . n A 1 287 ASN 287 373 373 ASN ASN A . n A 1 288 ALA 288 374 374 ALA ALA A . n A 1 289 ILE 289 375 375 ILE ILE A . n A 1 290 GLY 290 376 376 GLY GLY A . n A 1 291 THR 291 377 377 THR THR A . n A 1 292 GLY 292 378 378 GLY GLY A . n A 1 293 PHE 293 379 379 PHE PHE A . n A 1 294 GLY 294 380 380 GLY GLY A . n A 1 295 MET 295 381 381 MET MET A . n A 1 296 ARG 296 382 382 ARG ARG A . n A 1 297 PRO 297 383 383 PRO PRO A . n A 1 298 THR 298 384 384 THR THR A . n A 1 299 ALA 299 385 385 ALA ALA A . n A 1 300 ASN 300 386 386 ASN ASN A . n A 1 301 THR 301 387 387 THR THR A . n A 1 302 GLY 302 388 388 GLY GLY A . n A 1 303 HIS 303 389 389 HIS HIS A . n A 1 304 GLN 304 390 390 GLN GLN A . n A 1 305 TYR 305 391 391 TYR TYR A . n A 1 306 VAL 306 392 392 VAL VAL A . n A 1 307 ASP 307 393 393 ASP ASP A . n A 1 308 ALA 308 394 394 ALA ALA A . n A 1 309 PHE 309 395 395 PHE PHE A . n A 1 310 VAL 310 396 396 VAL VAL A . n A 1 311 TRP 311 397 397 TRP TRP A . n A 1 312 VAL 312 398 398 VAL VAL A . n A 1 313 LYS 313 399 399 LYS LYS A . n A 1 314 PRO 314 400 400 PRO PRO A . n A 1 315 GLY 315 401 401 GLY GLY A . n A 1 316 GLY 316 402 402 GLY GLY A . n A 1 317 GLU 317 403 403 GLU GLU A . n A 1 318 CYS 318 404 404 CYS CYS A . n A 1 319 ASN 319 405 405 ASN ASN A . n A 1 320 GLY 320 406 406 GLY GLY A . n A 1 321 THR 321 407 407 THR THR A . n A 1 322 SER 322 408 408 SER SER A . n A 1 323 ASP 323 409 409 ASP ASP A . n A 1 324 THR 324 410 410 THR THR A . n A 1 325 THR 325 411 411 THR THR A . n A 1 326 ALA 326 412 412 ALA ALA A . n A 1 327 ALA 327 413 413 ALA ALA A . n A 1 328 ARG 328 414 414 ARG ARG A . n A 1 329 TYR 329 415 415 TYR TYR A . n A 1 330 ASP 330 416 416 ASP ASP A . n A 1 331 TYR 331 417 417 TYR TYR A . n A 1 332 HIS 332 418 418 HIS HIS A . n A 1 333 CYS 333 419 419 CYS CYS A . n A 1 334 GLY 334 420 420 GLY GLY A . n A 1 335 LEU 335 421 421 LEU LEU A . n A 1 336 GLU 336 422 422 GLU GLU A . n A 1 337 ASP 337 423 423 ASP ASP A . n A 1 338 ALA 338 424 424 ALA ALA A . n A 1 339 LEU 339 425 425 LEU LEU A . n A 1 340 LYS 340 426 426 LYS LYS A . n A 1 341 PRO 341 427 427 PRO PRO A . n A 1 342 ALA 342 428 428 ALA ALA A . n A 1 343 PRO 343 429 429 PRO PRO A . n A 1 344 GLU 344 430 430 GLU GLU A . n A 1 345 ALA 345 431 431 ALA ALA A . n A 1 346 GLY 346 432 432 GLY GLY A . n A 1 347 GLN 347 433 433 GLN GLN A . n A 1 348 TRP 348 434 434 TRP TRP A . n A 1 349 PHE 349 435 435 PHE PHE A . n A 1 350 ASN 350 436 436 ASN ASN A . n A 1 351 GLU 351 437 437 GLU GLU A . n A 1 352 TYR 352 438 438 TYR TYR A . n A 1 353 PHE 353 439 439 PHE PHE A . n A 1 354 ILE 354 440 440 ILE ILE A . n A 1 355 GLN 355 441 441 GLN GLN A . n A 1 356 LEU 356 442 442 LEU LEU A . n A 1 357 LEU 357 443 443 LEU LEU A . n A 1 358 ARG 358 444 444 ARG ARG A . n A 1 359 ASN 359 445 445 ASN ASN A . n A 1 360 ALA 360 446 446 ALA ALA A . n A 1 361 ASN 361 447 447 ASN ASN A . n A 1 362 PRO 362 448 448 PRO PRO A . n A 1 363 PRO 363 449 449 PRO PRO A . n A 1 364 PHE 364 450 450 PHE PHE A . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 NAG 1 500 500 NAG NAG A . C 3 CA 1 501 501 CA CA A . D 4 GOL 1 510 510 GOL GOL A . E 4 GOL 1 511 511 GOL GOL A . F 4 GOL 1 512 512 GOL GOL A . G 4 GOL 1 514 514 GOL GOL A . H 4 GOL 1 515 515 GOL GOL A . I 4 GOL 1 516 516 GOL GOL A . J 4 GOL 1 517 517 GOL GOL A . K 5 HOH 1 2001 2001 HOH HOH A . K 5 HOH 2 2002 2002 HOH HOH A . K 5 HOH 3 2003 2003 HOH HOH A . K 5 HOH 4 2004 2004 HOH HOH A . K 5 HOH 5 2005 2005 HOH HOH A . K 5 HOH 6 2006 2006 HOH HOH A . K 5 HOH 7 2007 2007 HOH HOH A . K 5 HOH 8 2008 2008 HOH HOH A . K 5 HOH 9 2009 2009 HOH HOH A . K 5 HOH 10 2010 2010 HOH HOH A . K 5 HOH 11 2011 2011 HOH HOH A . K 5 HOH 12 2012 2012 HOH HOH A . K 5 HOH 13 2013 2013 HOH HOH A . K 5 HOH 14 2014 2014 HOH HOH A . K 5 HOH 15 2015 2015 HOH HOH A . K 5 HOH 16 2016 2016 HOH HOH A . K 5 HOH 17 2017 2017 HOH HOH A . K 5 HOH 18 2018 2018 HOH HOH A . K 5 HOH 19 2019 2019 HOH HOH A . K 5 HOH 20 2020 2020 HOH HOH A . K 5 HOH 21 2021 2021 HOH HOH A . K 5 HOH 22 2022 2022 HOH HOH A . K 5 HOH 23 2023 2023 HOH HOH A . K 5 HOH 24 2024 2024 HOH HOH A . K 5 HOH 25 2025 2025 HOH HOH A . K 5 HOH 26 2026 2026 HOH HOH A . K 5 HOH 27 2027 2027 HOH HOH A . K 5 HOH 28 2028 2028 HOH HOH A . K 5 HOH 29 2029 2029 HOH HOH A . K 5 HOH 30 2030 2030 HOH HOH A . K 5 HOH 31 2031 2031 HOH HOH A . K 5 HOH 32 2032 2032 HOH HOH A . K 5 HOH 33 2033 2033 HOH HOH A . K 5 HOH 34 2034 2034 HOH HOH A . K 5 HOH 35 2035 2035 HOH HOH A . K 5 HOH 36 2036 2036 HOH HOH A . K 5 HOH 37 2037 2037 HOH HOH A . K 5 HOH 38 2038 2038 HOH HOH A . K 5 HOH 39 2039 2039 HOH HOH A . K 5 HOH 40 2040 2040 HOH HOH A . K 5 HOH 41 2041 2041 HOH HOH A . K 5 HOH 42 2042 2042 HOH HOH A . K 5 HOH 43 2043 2043 HOH HOH A . K 5 HOH 44 2044 2044 HOH HOH A . K 5 HOH 45 2045 2045 HOH HOH A . K 5 HOH 46 2046 2046 HOH HOH A . K 5 HOH 47 2047 2047 HOH HOH A . K 5 HOH 48 2048 2048 HOH HOH A . K 5 HOH 49 2049 2049 HOH HOH A . K 5 HOH 50 2050 2050 HOH HOH A . K 5 HOH 51 2051 2051 HOH HOH A . K 5 HOH 52 2052 2052 HOH HOH A . K 5 HOH 53 2053 2053 HOH HOH A . K 5 HOH 54 2054 2054 HOH HOH A . K 5 HOH 55 2055 2055 HOH HOH A . K 5 HOH 56 2056 2056 HOH HOH A . K 5 HOH 57 2057 2057 HOH HOH A . K 5 HOH 58 2058 2058 HOH HOH A . K 5 HOH 59 2059 2059 HOH HOH A . K 5 HOH 60 2060 2060 HOH HOH A . K 5 HOH 61 2061 2061 HOH HOH A . K 5 HOH 62 2062 2062 HOH HOH A . K 5 HOH 63 2063 2063 HOH HOH A . K 5 HOH 64 2064 2064 HOH HOH A . K 5 HOH 65 2065 2065 HOH HOH A . K 5 HOH 66 2066 2066 HOH HOH A . K 5 HOH 67 2067 2067 HOH HOH A . K 5 HOH 68 2068 2068 HOH HOH A . K 5 HOH 69 2069 2069 HOH HOH A . K 5 HOH 70 2070 2070 HOH HOH A . K 5 HOH 71 2071 2071 HOH HOH A . K 5 HOH 72 2072 2072 HOH HOH A . K 5 HOH 73 2073 2073 HOH HOH A . K 5 HOH 74 2074 2074 HOH HOH A . K 5 HOH 75 2075 2075 HOH HOH A . K 5 HOH 76 2076 2076 HOH HOH A . K 5 HOH 77 2077 2077 HOH HOH A . K 5 HOH 78 2078 2078 HOH HOH A . K 5 HOH 79 2079 2079 HOH HOH A . K 5 HOH 80 2080 2080 HOH HOH A . K 5 HOH 81 2081 2081 HOH HOH A . K 5 HOH 82 2082 2082 HOH HOH A . K 5 HOH 83 2083 2083 HOH HOH A . K 5 HOH 84 2084 2084 HOH HOH A . K 5 HOH 85 2085 2085 HOH HOH A . K 5 HOH 86 2086 2086 HOH HOH A . K 5 HOH 87 2087 2087 HOH HOH A . K 5 HOH 88 2088 2088 HOH HOH A . K 5 HOH 89 2089 2089 HOH HOH A . K 5 HOH 90 2090 2090 HOH HOH A . K 5 HOH 91 2091 2091 HOH HOH A . K 5 HOH 92 2092 2092 HOH HOH A . K 5 HOH 93 2093 2093 HOH HOH A . K 5 HOH 94 2094 2094 HOH HOH A . K 5 HOH 95 2095 2095 HOH HOH A . K 5 HOH 96 2096 2096 HOH HOH A . K 5 HOH 97 2097 2097 HOH HOH A . K 5 HOH 98 2098 2098 HOH HOH A . K 5 HOH 99 2099 2099 HOH HOH A . K 5 HOH 100 2100 2100 HOH HOH A . K 5 HOH 101 2101 2101 HOH HOH A . K 5 HOH 102 2102 2102 HOH HOH A . K 5 HOH 103 2103 2103 HOH HOH A . K 5 HOH 104 2104 2104 HOH HOH A . K 5 HOH 105 2105 2105 HOH HOH A . K 5 HOH 106 2106 2106 HOH HOH A . K 5 HOH 107 2107 2107 HOH HOH A . K 5 HOH 108 2108 2108 HOH HOH A . K 5 HOH 109 2109 2109 HOH HOH A . K 5 HOH 110 2110 2110 HOH HOH A . K 5 HOH 111 2111 2111 HOH HOH A . K 5 HOH 112 2112 2112 HOH HOH A . K 5 HOH 113 2113 2113 HOH HOH A . K 5 HOH 114 2114 2114 HOH HOH A . K 5 HOH 115 2115 2115 HOH HOH A . K 5 HOH 116 2116 2116 HOH HOH A . K 5 HOH 117 2117 2117 HOH HOH A . K 5 HOH 118 2118 2118 HOH HOH A . K 5 HOH 119 2119 2119 HOH HOH A . K 5 HOH 120 2120 2120 HOH HOH A . K 5 HOH 121 2121 2121 HOH HOH A . K 5 HOH 122 2122 2122 HOH HOH A . K 5 HOH 123 2123 2123 HOH HOH A . K 5 HOH 124 2124 2124 HOH HOH A . K 5 HOH 125 2125 2125 HOH HOH A . K 5 HOH 126 2126 2126 HOH HOH A . K 5 HOH 127 2127 2127 HOH HOH A . K 5 HOH 128 2128 2128 HOH HOH A . K 5 HOH 129 2129 2129 HOH HOH A . K 5 HOH 130 2130 2130 HOH HOH A . K 5 HOH 131 2131 2131 HOH HOH A . K 5 HOH 132 2132 2132 HOH HOH A . K 5 HOH 133 2133 2133 HOH HOH A . K 5 HOH 134 2134 2134 HOH HOH A . K 5 HOH 135 2135 2135 HOH HOH A . K 5 HOH 136 2136 2136 HOH HOH A . K 5 HOH 137 2137 2137 HOH HOH A . K 5 HOH 138 2138 2138 HOH HOH A . K 5 HOH 139 2139 2139 HOH HOH A . K 5 HOH 140 2140 2140 HOH HOH A . K 5 HOH 141 2141 2141 HOH HOH A . K 5 HOH 142 2142 2142 HOH HOH A . K 5 HOH 143 2143 2143 HOH HOH A . K 5 HOH 144 2144 2144 HOH HOH A . K 5 HOH 145 2145 2145 HOH HOH A . K 5 HOH 146 2146 2146 HOH HOH A . K 5 HOH 147 2147 2147 HOH HOH A . K 5 HOH 148 2148 2148 HOH HOH A . K 5 HOH 149 2149 2149 HOH HOH A . K 5 HOH 150 2150 2150 HOH HOH A . K 5 HOH 151 2151 2151 HOH HOH A . K 5 HOH 152 2152 2152 HOH HOH A . K 5 HOH 153 2153 2153 HOH HOH A . K 5 HOH 154 2154 2154 HOH HOH A . K 5 HOH 155 2155 2155 HOH HOH A . K 5 HOH 156 2156 2156 HOH HOH A . K 5 HOH 157 2157 2157 HOH HOH A . K 5 HOH 158 2158 2158 HOH HOH A . K 5 HOH 159 2159 2159 HOH HOH A . K 5 HOH 160 2160 2160 HOH HOH A . K 5 HOH 161 2161 2161 HOH HOH A . K 5 HOH 162 2162 2162 HOH HOH A . K 5 HOH 163 2163 2163 HOH HOH A . K 5 HOH 164 2164 2164 HOH HOH A . K 5 HOH 165 2165 2165 HOH HOH A . K 5 HOH 166 2166 2166 HOH HOH A . K 5 HOH 167 2167 2167 HOH HOH A . K 5 HOH 168 2168 2168 HOH HOH A . K 5 HOH 169 2169 2169 HOH HOH A . K 5 HOH 170 2170 2170 HOH HOH A . K 5 HOH 171 2171 2171 HOH HOH A . K 5 HOH 172 2172 2172 HOH HOH A . K 5 HOH 173 2173 2173 HOH HOH A . K 5 HOH 174 2174 2174 HOH HOH A . K 5 HOH 175 2175 2175 HOH HOH A . K 5 HOH 176 2176 2176 HOH HOH A . K 5 HOH 177 2177 2177 HOH HOH A . K 5 HOH 178 2178 2178 HOH HOH A . K 5 HOH 179 2179 2179 HOH HOH A . K 5 HOH 180 2180 2180 HOH HOH A . K 5 HOH 181 2181 2181 HOH HOH A . K 5 HOH 182 2182 2182 HOH HOH A . K 5 HOH 183 2183 2183 HOH HOH A . K 5 HOH 184 2184 2184 HOH HOH A . K 5 HOH 185 2185 2185 HOH HOH A . K 5 HOH 186 2186 2186 HOH HOH A . K 5 HOH 187 2187 2187 HOH HOH A . K 5 HOH 188 2188 2188 HOH HOH A . K 5 HOH 189 2189 2189 HOH HOH A . K 5 HOH 190 2190 2190 HOH HOH A . K 5 HOH 191 2191 2191 HOH HOH A . K 5 HOH 192 2192 2192 HOH HOH A . K 5 HOH 193 2193 2193 HOH HOH A . K 5 HOH 194 2194 2194 HOH HOH A . K 5 HOH 195 2195 2195 HOH HOH A . K 5 HOH 196 2196 2196 HOH HOH A . K 5 HOH 197 2197 2197 HOH HOH A . K 5 HOH 198 2198 2198 HOH HOH A . K 5 HOH 199 2199 2199 HOH HOH A . K 5 HOH 200 2200 2200 HOH HOH A . K 5 HOH 201 2201 2201 HOH HOH A . K 5 HOH 202 2202 2202 HOH HOH A . K 5 HOH 203 2203 2203 HOH HOH A . K 5 HOH 204 2204 2204 HOH HOH A . K 5 HOH 205 2205 2205 HOH HOH A . K 5 HOH 206 2206 2206 HOH HOH A . K 5 HOH 207 2207 2207 HOH HOH A . K 5 HOH 208 2208 2208 HOH HOH A . K 5 HOH 209 2209 2209 HOH HOH A . K 5 HOH 210 2210 2210 HOH HOH A . K 5 HOH 211 2211 2211 HOH HOH A . K 5 HOH 212 2212 2212 HOH HOH A . K 5 HOH 213 2213 2213 HOH HOH A . K 5 HOH 214 2214 2214 HOH HOH A . K 5 HOH 215 2215 2215 HOH HOH A . K 5 HOH 216 2216 2216 HOH HOH A . K 5 HOH 217 2217 2217 HOH HOH A . K 5 HOH 218 2218 2218 HOH HOH A . K 5 HOH 219 2219 2219 HOH HOH A . K 5 HOH 220 2220 2220 HOH HOH A . K 5 HOH 221 2221 2221 HOH HOH A . K 5 HOH 222 2222 2222 HOH HOH A . K 5 HOH 223 2223 2223 HOH HOH A . K 5 HOH 224 2224 2224 HOH HOH A . K 5 HOH 225 2225 2225 HOH HOH A . K 5 HOH 226 2226 2226 HOH HOH A . K 5 HOH 227 2227 2227 HOH HOH A . K 5 HOH 228 2228 2228 HOH HOH A . K 5 HOH 229 2229 2229 HOH HOH A . K 5 HOH 230 2230 2230 HOH HOH A . K 5 HOH 231 2231 2231 HOH HOH A . K 5 HOH 232 2232 2232 HOH HOH A . K 5 HOH 233 2233 2233 HOH HOH A . K 5 HOH 234 2234 2234 HOH HOH A . K 5 HOH 235 2235 2235 HOH HOH A . K 5 HOH 236 2236 2236 HOH HOH A . K 5 HOH 237 2237 2237 HOH HOH A . K 5 HOH 238 2238 2238 HOH HOH A . K 5 HOH 239 2239 2239 HOH HOH A . K 5 HOH 240 2240 2240 HOH HOH A . K 5 HOH 241 2241 2241 HOH HOH A . K 5 HOH 242 2242 2242 HOH HOH A . K 5 HOH 243 2243 2243 HOH HOH A . K 5 HOH 244 2244 2244 HOH HOH A . K 5 HOH 245 2245 2245 HOH HOH A . K 5 HOH 246 2246 2246 HOH HOH A . K 5 HOH 247 2247 2247 HOH HOH A . K 5 HOH 248 2248 2248 HOH HOH A . K 5 HOH 249 2249 2249 HOH HOH A . K 5 HOH 250 2250 2250 HOH HOH A . K 5 HOH 251 2251 2251 HOH HOH A . K 5 HOH 252 2252 2252 HOH HOH A . K 5 HOH 253 2253 2253 HOH HOH A . K 5 HOH 254 2254 2254 HOH HOH A . K 5 HOH 255 2255 2255 HOH HOH A . K 5 HOH 256 2256 2256 HOH HOH A . K 5 HOH 257 2257 2257 HOH HOH A . K 5 HOH 258 2258 2258 HOH HOH A . K 5 HOH 259 2259 2259 HOH HOH A . K 5 HOH 260 2260 2260 HOH HOH A . K 5 HOH 261 2261 2261 HOH HOH A . K 5 HOH 262 2262 2262 HOH HOH A . K 5 HOH 263 2263 2263 HOH HOH A . K 5 HOH 264 2264 2264 HOH HOH A . K 5 HOH 265 2265 2265 HOH HOH A . K 5 HOH 266 2266 2266 HOH HOH A . K 5 HOH 267 2267 2267 HOH HOH A . K 5 HOH 268 2268 2268 HOH HOH A . K 5 HOH 269 2269 2269 HOH HOH A . K 5 HOH 270 2270 2270 HOH HOH A . K 5 HOH 271 2271 2271 HOH HOH A . K 5 HOH 272 2272 2272 HOH HOH A . K 5 HOH 273 2273 2273 HOH HOH A . K 5 HOH 274 2274 2274 HOH HOH A . K 5 HOH 275 2275 2275 HOH HOH A . K 5 HOH 276 2276 2276 HOH HOH A . K 5 HOH 277 2277 2277 HOH HOH A . K 5 HOH 278 2278 2278 HOH HOH A . K 5 HOH 279 2279 2279 HOH HOH A . K 5 HOH 280 2280 2280 HOH HOH A . K 5 HOH 281 2281 2281 HOH HOH A . K 5 HOH 282 2282 2282 HOH HOH A . K 5 HOH 283 2283 2283 HOH HOH A . K 5 HOH 284 2284 2284 HOH HOH A . K 5 HOH 285 2285 2285 HOH HOH A . K 5 HOH 286 2286 2286 HOH HOH A . K 5 HOH 287 2287 2287 HOH HOH A . K 5 HOH 288 2288 2288 HOH HOH A . K 5 HOH 289 2289 2289 HOH HOH A . K 5 HOH 290 2290 2290 HOH HOH A . K 5 HOH 291 2291 2291 HOH HOH A . K 5 HOH 292 2292 2292 HOH HOH A . K 5 HOH 293 2293 2293 HOH HOH A . K 5 HOH 294 2294 2294 HOH HOH A . K 5 HOH 295 2295 2295 HOH HOH A . K 5 HOH 296 2296 2296 HOH HOH A . K 5 HOH 297 2297 2297 HOH HOH A . K 5 HOH 298 2298 2298 HOH HOH A . K 5 HOH 299 2299 2299 HOH HOH A . K 5 HOH 300 2300 2300 HOH HOH A . K 5 HOH 301 2301 2301 HOH HOH A . K 5 HOH 302 2302 2302 HOH HOH A . K 5 HOH 303 2303 2303 HOH HOH A . K 5 HOH 304 2304 2304 HOH HOH A . K 5 HOH 305 2305 2305 HOH HOH A . K 5 HOH 306 2306 2306 HOH HOH A . K 5 HOH 307 2307 2307 HOH HOH A . K 5 HOH 308 2308 2308 HOH HOH A . K 5 HOH 309 2309 2309 HOH HOH A . K 5 HOH 310 2310 2310 HOH HOH A . K 5 HOH 311 2311 2311 HOH HOH A . K 5 HOH 312 2312 2312 HOH HOH A . K 5 HOH 313 2313 2313 HOH HOH A . K 5 HOH 314 2314 2314 HOH HOH A . K 5 HOH 315 2315 2315 HOH HOH A . K 5 HOH 316 2316 2316 HOH HOH A . K 5 HOH 317 2317 2317 HOH HOH A . K 5 HOH 318 2318 2318 HOH HOH A . K 5 HOH 319 2319 2319 HOH HOH A . K 5 HOH 320 2320 2320 HOH HOH A . K 5 HOH 321 2321 2321 HOH HOH A . K 5 HOH 322 2322 2322 HOH HOH A . K 5 HOH 323 2323 2323 HOH HOH A . K 5 HOH 324 2324 2324 HOH HOH A . K 5 HOH 325 2325 2325 HOH HOH A . K 5 HOH 326 2326 2326 HOH HOH A . K 5 HOH 327 2327 2327 HOH HOH A . K 5 HOH 328 2328 2328 HOH HOH A . K 5 HOH 329 2329 2329 HOH HOH A . K 5 HOH 330 2330 2330 HOH HOH A . K 5 HOH 331 2331 2331 HOH HOH A . K 5 HOH 332 2332 2332 HOH HOH A . K 5 HOH 333 2333 2333 HOH HOH A . K 5 HOH 334 2334 2334 HOH HOH A . K 5 HOH 335 2335 2335 HOH HOH A . K 5 HOH 336 2336 2336 HOH HOH A . K 5 HOH 337 2337 2337 HOH HOH A . K 5 HOH 338 2338 2338 HOH HOH A . K 5 HOH 339 2339 2339 HOH HOH A . K 5 HOH 340 2340 2340 HOH HOH A . K 5 HOH 341 2341 2341 HOH HOH A . K 5 HOH 342 2342 2342 HOH HOH A . K 5 HOH 343 2343 2343 HOH HOH A . K 5 HOH 344 2344 2344 HOH HOH A . K 5 HOH 345 2345 2345 HOH HOH A . K 5 HOH 346 2346 2346 HOH HOH A . K 5 HOH 347 2347 2347 HOH HOH A . K 5 HOH 348 2348 2348 HOH HOH A . K 5 HOH 349 2349 2349 HOH HOH A . K 5 HOH 350 2350 2350 HOH HOH A . K 5 HOH 351 2351 2351 HOH HOH A . K 5 HOH 352 2352 2352 HOH HOH A . K 5 HOH 353 2353 2353 HOH HOH A . K 5 HOH 354 2354 2354 HOH HOH A . K 5 HOH 355 2355 2355 HOH HOH A . K 5 HOH 356 2356 2356 HOH HOH A . K 5 HOH 357 2357 2357 HOH HOH A . K 5 HOH 358 2358 2358 HOH HOH A . K 5 HOH 359 2359 2359 HOH HOH A . K 5 HOH 360 2360 2360 HOH HOH A . K 5 HOH 361 2361 2361 HOH HOH A . K 5 HOH 362 2362 2362 HOH HOH A . K 5 HOH 363 2363 2363 HOH HOH A . K 5 HOH 364 2364 2364 HOH HOH A . K 5 HOH 365 2365 2365 HOH HOH A . K 5 HOH 366 2366 2366 HOH HOH A . K 5 HOH 367 2367 2367 HOH HOH A . K 5 HOH 368 2368 2368 HOH HOH A . K 5 HOH 369 2369 2369 HOH HOH A . K 5 HOH 370 2370 2370 HOH HOH A . K 5 HOH 371 2371 2371 HOH HOH A . K 5 HOH 372 2372 2372 HOH HOH A . K 5 HOH 373 2373 2373 HOH HOH A . K 5 HOH 374 2374 2374 HOH HOH A . K 5 HOH 375 2375 2375 HOH HOH A . K 5 HOH 376 2376 2376 HOH HOH A . K 5 HOH 377 2377 2377 HOH HOH A . K 5 HOH 378 2378 2378 HOH HOH A . K 5 HOH 379 2379 2379 HOH HOH A . K 5 HOH 380 2380 2380 HOH HOH A . K 5 HOH 381 2381 2381 HOH HOH A . K 5 HOH 382 2382 2382 HOH HOH A . K 5 HOH 383 2383 2383 HOH HOH A . K 5 HOH 384 2384 2384 HOH HOH A . K 5 HOH 385 2385 2385 HOH HOH A . K 5 HOH 386 2386 2386 HOH HOH A . K 5 HOH 387 2387 2387 HOH HOH A . K 5 HOH 388 2388 2388 HOH HOH A . K 5 HOH 389 2389 2389 HOH HOH A . K 5 HOH 390 2390 2390 HOH HOH A . K 5 HOH 391 2391 2391 HOH HOH A . K 5 HOH 392 2392 2392 HOH HOH A . K 5 HOH 393 2393 2393 HOH HOH A . K 5 HOH 394 2394 2394 HOH HOH A . K 5 HOH 395 2395 2395 HOH HOH A . K 5 HOH 396 2396 2396 HOH HOH A . K 5 HOH 397 2397 2397 HOH HOH A . K 5 HOH 398 2398 2398 HOH HOH A . K 5 HOH 399 2399 2399 HOH HOH A . K 5 HOH 400 2400 2400 HOH HOH A . K 5 HOH 401 2401 2401 HOH HOH A . K 5 HOH 402 2402 2402 HOH HOH A . K 5 HOH 403 2403 2403 HOH HOH A . K 5 HOH 404 2404 2404 HOH HOH A . K 5 HOH 405 2405 2405 HOH HOH A . K 5 HOH 406 2406 2406 HOH HOH A . K 5 HOH 407 2407 2407 HOH HOH A . K 5 HOH 408 2408 2408 HOH HOH A . K 5 HOH 409 2409 2409 HOH HOH A . K 5 HOH 410 2410 2410 HOH HOH A . K 5 HOH 411 2411 2411 HOH HOH A . K 5 HOH 412 2412 2412 HOH HOH A . K 5 HOH 413 2413 2413 HOH HOH A . K 5 HOH 414 2414 2414 HOH HOH A . K 5 HOH 415 2415 2415 HOH HOH A . K 5 HOH 416 2416 2416 HOH HOH A . K 5 HOH 417 2417 2417 HOH HOH A . K 5 HOH 418 2418 2418 HOH HOH A . K 5 HOH 419 2419 2419 HOH HOH A . K 5 HOH 420 2420 2420 HOH HOH A . K 5 HOH 421 2421 2421 HOH HOH A . K 5 HOH 422 2422 2422 HOH HOH A . K 5 HOH 423 2423 2423 HOH HOH A . K 5 HOH 424 2424 2424 HOH HOH A . K 5 HOH 425 2425 2425 HOH HOH A . K 5 HOH 426 2426 2426 HOH HOH A . K 5 HOH 427 2427 2427 HOH HOH A . K 5 HOH 428 2428 2428 HOH HOH A . K 5 HOH 429 2429 2429 HOH HOH A . K 5 HOH 430 2430 2430 HOH HOH A . K 5 HOH 431 2431 2431 HOH HOH A . K 5 HOH 432 2432 2432 HOH HOH A . K 5 HOH 433 2433 2433 HOH HOH A . K 5 HOH 434 2434 2434 HOH HOH A . K 5 HOH 435 2435 2435 HOH HOH A . K 5 HOH 436 2436 2436 HOH HOH A . K 5 HOH 437 2437 2437 HOH HOH A . K 5 HOH 438 2438 2438 HOH HOH A . K 5 HOH 439 2439 2439 HOH HOH A . K 5 HOH 440 2440 2440 HOH HOH A . K 5 HOH 441 2441 2441 HOH HOH A . K 5 HOH 442 2442 2442 HOH HOH A . K 5 HOH 443 2443 2443 HOH HOH A . K 5 HOH 444 2444 2444 HOH HOH A . K 5 HOH 445 2445 2445 HOH HOH A . K 5 HOH 446 2446 2446 HOH HOH A . K 5 HOH 447 2447 2447 HOH HOH A . K 5 HOH 448 2448 2448 HOH HOH A . K 5 HOH 449 2449 2449 HOH HOH A . K 5 HOH 450 2450 2450 HOH HOH A . K 5 HOH 451 2451 2451 HOH HOH A . K 5 HOH 452 2452 2452 HOH HOH A . K 5 HOH 453 2453 2453 HOH HOH A . K 5 HOH 454 2454 2454 HOH HOH A . K 5 HOH 455 2455 2455 HOH HOH A . K 5 HOH 456 2456 2456 HOH HOH A . K 5 HOH 457 2457 2457 HOH HOH A . K 5 HOH 458 2458 2458 HOH HOH A . K 5 HOH 459 2459 2459 HOH HOH A . K 5 HOH 460 2460 2460 HOH HOH A . K 5 HOH 461 2461 2461 HOH HOH A . K 5 HOH 462 2462 2462 HOH HOH A . K 5 HOH 463 2463 2463 HOH HOH A . K 5 HOH 464 2464 2464 HOH HOH A . K 5 HOH 465 2465 2465 HOH HOH A . # _pdbx_struct_mod_residue.id 1 _pdbx_struct_mod_residue.label_asym_id A _pdbx_struct_mod_residue.label_comp_id ASN _pdbx_struct_mod_residue.label_seq_id 55 _pdbx_struct_mod_residue.auth_asym_id A _pdbx_struct_mod_residue.auth_comp_id ASN _pdbx_struct_mod_residue.auth_seq_id 141 _pdbx_struct_mod_residue.PDB_ins_code ? _pdbx_struct_mod_residue.parent_comp_id ASN _pdbx_struct_mod_residue.details 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PQS _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 O ? K HOH . ? A HOH 2332 ? 1_555 CA ? C CA . ? A CA 501 ? 1_555 O ? K HOH . ? A HOH 2173 ? 1_555 81.0 ? 2 O ? K HOH . ? A HOH 2332 ? 1_555 CA ? C CA . ? A CA 501 ? 1_555 O ? K HOH . ? A HOH 2335 ? 1_555 103.1 ? 3 O ? K HOH . ? A HOH 2173 ? 1_555 CA ? C CA . ? A CA 501 ? 1_555 O ? K HOH . ? A HOH 2335 ? 1_555 80.1 ? 4 O ? K HOH . ? A HOH 2332 ? 1_555 CA ? C CA . ? A CA 501 ? 1_555 OE1 ? A GLU 281 ? A GLU 367 ? 1_555 88.4 ? 5 O ? K HOH . ? A HOH 2173 ? 1_555 CA ? C CA . ? A CA 501 ? 1_555 OE1 ? A GLU 281 ? A GLU 367 ? 1_555 147.3 ? 6 O ? K HOH . ? A HOH 2335 ? 1_555 CA ? C CA . ? A CA 501 ? 1_555 OE1 ? A GLU 281 ? A GLU 367 ? 1_555 72.3 ? 7 O ? K HOH . ? A HOH 2332 ? 1_555 CA ? C CA . ? A CA 501 ? 1_555 O ? K HOH . ? A HOH 2154 ? 3_645 78.5 ? 8 O ? K HOH . ? A HOH 2173 ? 1_555 CA ? C CA . ? A CA 501 ? 1_555 O ? K HOH . ? A HOH 2154 ? 3_645 83.7 ? 9 O ? K HOH . ? A HOH 2335 ? 1_555 CA ? C CA . ? A CA 501 ? 1_555 O ? K HOH . ? A HOH 2154 ? 3_645 163.3 ? 10 OE1 ? A GLU 281 ? A GLU 367 ? 1_555 CA ? C CA . ? A CA 501 ? 1_555 O ? K HOH . ? A HOH 2154 ? 3_645 124.4 ? 11 O ? K HOH . ? A HOH 2332 ? 1_555 CA ? C CA . ? A CA 501 ? 1_555 O ? K HOH . ? A HOH 2293 ? 1_555 149.1 ? 12 O ? K HOH . ? A HOH 2173 ? 1_555 CA ? C CA . ? A CA 501 ? 1_555 O ? K HOH . ? A HOH 2293 ? 1_555 71.0 ? 13 O ? K HOH . ? A HOH 2335 ? 1_555 CA ? C CA . ? A CA 501 ? 1_555 O ? K HOH . ? A HOH 2293 ? 1_555 85.1 ? 14 OE1 ? A GLU 281 ? A GLU 367 ? 1_555 CA ? C CA . ? A CA 501 ? 1_555 O ? K HOH . ? A HOH 2293 ? 1_555 122.3 ? 15 O ? K HOH . ? A HOH 2154 ? 3_645 CA ? C CA . ? A CA 501 ? 1_555 O ? K HOH . ? A HOH 2293 ? 1_555 85.6 ? # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2003-07-10 2 'Structure model' 1 1 2011-05-08 3 'Structure model' 1 2 2011-07-13 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Version format compliance' 2 3 'Structure model' 'Version format compliance' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.1.06 ? 1 DENZO 'data reduction' . ? 2 SCALEPACK 'data scaling' . ? 3 # _pdbx_database_remark.id 700 _pdbx_database_remark.text ; SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. ; # _pdbx_entry_details.entry_id 1OC6 _pdbx_entry_details.compound_details 'ENGINEERED MUTATION ASP 405 ASN CHAIN A' _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ? _pdbx_entry_details.sequence_details ;THIS MUTANT HAS BEEN PRODUCED BY SITE DIRECTED MUTAGENESIS. THE CLONING WAS PERFORMED SUCH AS ONLY THE SIGNAL PEPTIDE AND THE CATALYTIC DOMAIN WERE EXPRESSED. THE CATALYTIC DOMAIN SHOULD BEGIN AT PHE 89. OUR NUMBERING BEGIN AT THE FIRST RESIDUE OF THE MATURE PROTEIN WHICH EXPLAIN A DIFFERENCE WITH THE DATABASE SEQUENCE WHICH INCLUDE THE PROSEQUENCE. HERE,DUE TO THE INCORRECT PROCESSING OF THE SIGNAL PEPTIDE ALA 87 AND PRO 88 ARE ALSO PRESENT IN THE MATURE PROTEIN. THIS PROTEIN IS CLOSELY RELATED TO AVICELASE 2 (SWISS-PROT ACCESSION ID:Q9C1S9) WITH WHICH IT HAS 96% SEQUENCE IDENTITY. ; # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 NE A ARG 123 ? ? CZ A ARG 123 ? ? NH1 A ARG 123 ? ? 123.40 120.30 3.10 0.50 N 2 1 CB A ASP 139 ? ? CG A ASP 139 ? ? OD1 A ASP 139 ? ? 123.74 118.30 5.44 0.90 N 3 1 NE A ARG 140 ? ? CZ A ARG 140 ? ? NH1 A ARG 140 ? ? 124.17 120.30 3.87 0.50 N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 THR A 146 ? ? -111.71 -84.38 2 1 TYR A 174 ? ? -150.25 69.84 3 1 ASP A 175 ? ? -152.06 33.42 4 1 PHE A 214 ? ? -103.74 40.57 5 1 GLU A 224 ? ? 51.12 74.94 6 1 SER A 227 ? ? -111.40 -93.44 7 1 TRP A 274 ? ? -116.37 -79.86 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 'CALCIUM ION' CA 4 GLYCEROL GOL 5 water HOH #