data_4AQB # _entry.id 4AQB # _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 4AQB PDBE EBI-52057 WWPDB D_1290052057 # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4AQB _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2012-04-16 _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 'Skjoedt, M.O.' 1 'Roversi, P.' 2 'Hummelshoj, T.' 3 'Palarasah, Y.' 4 'Johnson, S.' 5 'Lea, S.M.' 6 'Garred, P.' 7 # _citation.id primary _citation.title ;Crystal Structure and Functional Characterization of the Complement Regulator Mannose-Binding Lectin (Mbl)/Ficolin-Associated Protein-1 (Map-1). ; _citation.journal_abbrev J.Biol.Chem. _citation.journal_volume 287 _citation.page_first 32913 _citation.page_last ? _citation.year 2012 _citation.journal_id_ASTM JBCHA3 _citation.country US _citation.journal_id_ISSN 0021-9258 _citation.journal_id_CSD 0071 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 22854970 _citation.pdbx_database_id_DOI 10.1074/JBC.M112.386680 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Skjoedt, M.O.' 1 primary 'Roversi, P.' 2 primary 'Hummelshoj, T.' 3 primary 'Palarasah, Y.' 4 primary 'Rosbjerg, A.' 5 primary 'Johnson, S.' 6 primary 'Lea, S.M.' 7 primary 'Garred, P.' 8 # _cell.entry_id 4AQB _cell.length_a 94.150 _cell.length_b 94.150 _cell.length_c 242.570 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 8 _cell.pdbx_unique_axis ? # _symmetry.entry_id 4AQB _symmetry.space_group_name_H-M 'P 43 2 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 95 # 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 'MANNAN-BINDING LECTIN SERINE PROTEASE 1' 41460.918 1 ? ? ? ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 4 ? ? ? ? 3 non-polymer man BETA-D-MANNOSE 180.156 2 ? ? ? ? 4 non-polymer man ALPHA-D-MANNOSE 180.156 3 ? ? ? ? 5 non-polymer syn 'CALCIUM ION' 40.078 6 ? ? ? ? 6 water nat water 18.015 5 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name ;MBL-FICOLIN ASSOCIATED PROTEIN-1, COMPLEMENT FACTOR MASP-3, COMPLEMENT-ACTIVATING COMPONENT OF RA-REACTIVE FACTOR, MANNOSE-BINDING LECTIN-ASSOCIATED SERINE PROTEASE 1, MASP-1, MANNOSE-BINDING PROTEIN-ASSOCIATED SERINE PROTEASE, RA-REACTIVE FACTOR SERINE PROTEASE P100, RARF, SERINE PROTEASE 5, MANNAN-BINDING LECTIN SERINE PROTEASE 1 HEAVY CHAIN ; # _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 ;HTVELNNMFGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKVETEDQVLATFCGRETTDTE QTPGQEVVLSPGSFMSITFRSDFSNEERFTGFDAHYMAVDVDECKEREDEELSCDHYCHNYIGGYYCSCRFGYILHTDNR TCRVECSDNLFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDIFDIEDHPEVPCPYDYIKIKVGPKVLGPF CGEKAPEPISTQSHSVLILFHSDNSGENRGWRLSYRAAGNECPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDN VEMDTFQIECLKDGTWSNKIPTCKKNEIDLESELKSEQVTE ; _entity_poly.pdbx_seq_one_letter_code_can ;HTVELNNMFGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKVETEDQVLATFCGRETTDTE QTPGQEVVLSPGSFMSITFRSDFSNEERFTGFDAHYMAVDVDECKEREDEELSCDHYCHNYIGGYYCSCRFGYILHTDNR TCRVECSDNLFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDIFDIEDHPEVPCPYDYIKIKVGPKVLGPF CGEKAPEPISTQSHSVLILFHSDNSGENRGWRLSYRAAGNECPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDN VEMDTFQIECLKDGTWSNKIPTCKKNEIDLESELKSEQVTE ; _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 HIS n 1 2 THR n 1 3 VAL n 1 4 GLU n 1 5 LEU n 1 6 ASN n 1 7 ASN n 1 8 MET n 1 9 PHE n 1 10 GLY n 1 11 GLN n 1 12 ILE n 1 13 GLN n 1 14 SER n 1 15 PRO n 1 16 GLY n 1 17 TYR n 1 18 PRO n 1 19 ASP n 1 20 SER n 1 21 TYR n 1 22 PRO n 1 23 SER n 1 24 ASP n 1 25 SER n 1 26 GLU n 1 27 VAL n 1 28 THR n 1 29 TRP n 1 30 ASN n 1 31 ILE n 1 32 THR n 1 33 VAL n 1 34 PRO n 1 35 ASP n 1 36 GLY n 1 37 PHE n 1 38 ARG n 1 39 ILE n 1 40 LYS n 1 41 LEU n 1 42 TYR n 1 43 PHE n 1 44 MET n 1 45 HIS n 1 46 PHE n 1 47 ASN n 1 48 LEU n 1 49 GLU n 1 50 SER n 1 51 SER n 1 52 TYR n 1 53 LEU n 1 54 CYS n 1 55 GLU n 1 56 TYR n 1 57 ASP n 1 58 TYR n 1 59 VAL n 1 60 LYS n 1 61 VAL n 1 62 GLU n 1 63 THR n 1 64 GLU n 1 65 ASP n 1 66 GLN n 1 67 VAL n 1 68 LEU n 1 69 ALA n 1 70 THR n 1 71 PHE n 1 72 CYS n 1 73 GLY n 1 74 ARG n 1 75 GLU n 1 76 THR n 1 77 THR n 1 78 ASP n 1 79 THR n 1 80 GLU n 1 81 GLN n 1 82 THR n 1 83 PRO n 1 84 GLY n 1 85 GLN n 1 86 GLU n 1 87 VAL n 1 88 VAL n 1 89 LEU n 1 90 SER n 1 91 PRO n 1 92 GLY n 1 93 SER n 1 94 PHE n 1 95 MET n 1 96 SER n 1 97 ILE n 1 98 THR n 1 99 PHE n 1 100 ARG n 1 101 SER n 1 102 ASP n 1 103 PHE n 1 104 SER n 1 105 ASN n 1 106 GLU n 1 107 GLU n 1 108 ARG n 1 109 PHE n 1 110 THR n 1 111 GLY n 1 112 PHE n 1 113 ASP n 1 114 ALA n 1 115 HIS n 1 116 TYR n 1 117 MET n 1 118 ALA n 1 119 VAL n 1 120 ASP n 1 121 VAL n 1 122 ASP n 1 123 GLU n 1 124 CYS n 1 125 LYS n 1 126 GLU n 1 127 ARG n 1 128 GLU n 1 129 ASP n 1 130 GLU n 1 131 GLU n 1 132 LEU n 1 133 SER n 1 134 CYS n 1 135 ASP n 1 136 HIS n 1 137 TYR n 1 138 CYS n 1 139 HIS n 1 140 ASN n 1 141 TYR n 1 142 ILE n 1 143 GLY n 1 144 GLY n 1 145 TYR n 1 146 TYR n 1 147 CYS n 1 148 SER n 1 149 CYS n 1 150 ARG n 1 151 PHE n 1 152 GLY n 1 153 TYR n 1 154 ILE n 1 155 LEU n 1 156 HIS n 1 157 THR n 1 158 ASP n 1 159 ASN n 1 160 ARG n 1 161 THR n 1 162 CYS n 1 163 ARG n 1 164 VAL n 1 165 GLU n 1 166 CYS n 1 167 SER n 1 168 ASP n 1 169 ASN n 1 170 LEU n 1 171 PHE n 1 172 THR n 1 173 GLN n 1 174 ARG n 1 175 THR n 1 176 GLY n 1 177 VAL n 1 178 ILE n 1 179 THR n 1 180 SER n 1 181 PRO n 1 182 ASP n 1 183 PHE n 1 184 PRO n 1 185 ASN n 1 186 PRO n 1 187 TYR n 1 188 PRO n 1 189 LYS n 1 190 SER n 1 191 SER n 1 192 GLU n 1 193 CYS n 1 194 LEU n 1 195 TYR n 1 196 THR n 1 197 ILE n 1 198 GLU n 1 199 LEU n 1 200 GLU n 1 201 GLU n 1 202 GLY n 1 203 PHE n 1 204 MET n 1 205 VAL n 1 206 ASN n 1 207 LEU n 1 208 GLN n 1 209 PHE n 1 210 GLU n 1 211 ASP n 1 212 ILE n 1 213 PHE n 1 214 ASP n 1 215 ILE n 1 216 GLU n 1 217 ASP n 1 218 HIS n 1 219 PRO n 1 220 GLU n 1 221 VAL n 1 222 PRO n 1 223 CYS n 1 224 PRO n 1 225 TYR n 1 226 ASP n 1 227 TYR n 1 228 ILE n 1 229 LYS n 1 230 ILE n 1 231 LYS n 1 232 VAL n 1 233 GLY n 1 234 PRO n 1 235 LYS n 1 236 VAL n 1 237 LEU n 1 238 GLY n 1 239 PRO n 1 240 PHE n 1 241 CYS n 1 242 GLY n 1 243 GLU n 1 244 LYS n 1 245 ALA n 1 246 PRO n 1 247 GLU n 1 248 PRO n 1 249 ILE n 1 250 SER n 1 251 THR n 1 252 GLN n 1 253 SER n 1 254 HIS n 1 255 SER n 1 256 VAL n 1 257 LEU n 1 258 ILE n 1 259 LEU n 1 260 PHE n 1 261 HIS n 1 262 SER n 1 263 ASP n 1 264 ASN n 1 265 SER n 1 266 GLY n 1 267 GLU n 1 268 ASN n 1 269 ARG n 1 270 GLY n 1 271 TRP n 1 272 ARG n 1 273 LEU n 1 274 SER n 1 275 TYR n 1 276 ARG n 1 277 ALA n 1 278 ALA n 1 279 GLY n 1 280 ASN n 1 281 GLU n 1 282 CYS n 1 283 PRO n 1 284 GLU n 1 285 LEU n 1 286 GLN n 1 287 PRO n 1 288 PRO n 1 289 VAL n 1 290 HIS n 1 291 GLY n 1 292 LYS n 1 293 ILE n 1 294 GLU n 1 295 PRO n 1 296 SER n 1 297 GLN n 1 298 ALA n 1 299 LYS n 1 300 TYR n 1 301 PHE n 1 302 PHE n 1 303 LYS n 1 304 ASP n 1 305 GLN n 1 306 VAL n 1 307 LEU n 1 308 VAL n 1 309 SER n 1 310 CYS n 1 311 ASP n 1 312 THR n 1 313 GLY n 1 314 TYR n 1 315 LYS n 1 316 VAL n 1 317 LEU n 1 318 LYS n 1 319 ASP n 1 320 ASN n 1 321 VAL n 1 322 GLU n 1 323 MET n 1 324 ASP n 1 325 THR n 1 326 PHE n 1 327 GLN n 1 328 ILE n 1 329 GLU n 1 330 CYS n 1 331 LEU n 1 332 LYS n 1 333 ASP n 1 334 GLY n 1 335 THR n 1 336 TRP n 1 337 SER n 1 338 ASN n 1 339 LYS n 1 340 ILE n 1 341 PRO n 1 342 THR n 1 343 CYS n 1 344 LYS n 1 345 LYS n 1 346 ASN n 1 347 GLU n 1 348 ILE n 1 349 ASP n 1 350 LEU n 1 351 GLU n 1 352 SER n 1 353 GLU n 1 354 LEU n 1 355 LYS n 1 356 SER n 1 357 GLU n 1 358 GLN n 1 359 VAL n 1 360 THR n 1 361 GLU 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 HUMAN _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 PLASMA _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 'HOMO SAPIENS' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 9606 _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 'CHINESE HAMSTER' _entity_src_gen.pdbx_host_org_scientific_name 'CRICETULUS GRISEUS' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 10029 _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 'CHO DG44' _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 PLASMID _entity_src_gen.pdbx_host_org_vector 'PPCR-SCRIPT AMP' _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name ? _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code MASP1_HUMAN _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_align_begin ? _struct_ref.pdbx_db_accession P48740 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 4AQB _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 361 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession P48740 _struct_ref_seq.db_align_beg 20 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 380 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 20 _struct_ref_seq.pdbx_auth_seq_align_end 380 # 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 BMA D-saccharide . BETA-D-MANNOSE ? 'C6 H12 O6' 180.156 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 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 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 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 4AQB _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 6.51 _exptl_crystal.density_percent_sol 81.1 _exptl_crystal.description ;DATA ANISOTROPICALLY TRUNCATED AND B-SHARPENED WITH A B=-5.85 AT THE UCLA SERVER HTTP SERVICES.MBI.UCLA.EDU ANISOSCALE ANISOSCALE_XDS ; _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 6.5 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '0.2 M CALCIUM ACETATE, 0.1 M SODIUM CACODYLATE PH 6.5, 40% W/V PEG 400' # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'ADSC QUANTUM 315r' _diffrn_detector.pdbx_collection_date 2011-04-11 _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 0.97930 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'ESRF BEAMLINE ID14-4' _diffrn_source.pdbx_synchrotron_site ESRF _diffrn_source.pdbx_synchrotron_beamline ID14-4 _diffrn_source.pdbx_wavelength 0.97930 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4AQB _reflns.observed_criterion_sigma_I 0.0 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 58.40 _reflns.d_resolution_high 4.20 _reflns.number_obs 7844 _reflns.number_all ? _reflns.percent_possible_obs 93.5 _reflns.pdbx_Rmerge_I_obs 0.28 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 8.70 _reflns.B_iso_Wilson_estimate 129.96 _reflns.pdbx_redundancy 3.64 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 4.20 _reflns_shell.d_res_low 4.36 _reflns_shell.percent_possible_all 95.2 _reflns_shell.Rmerge_I_obs 0.56 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 2.80 _reflns_shell.pdbx_redundancy 3.9 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4AQB _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 7843 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 0.0 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 58.36 _refine.ls_d_res_high 4.20 _refine.ls_percent_reflns_obs 91.80 _refine.ls_R_factor_obs 0.2797 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.2786 _refine.ls_R_factor_R_free 0.3006 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 4.59 _refine.ls_number_reflns_R_free 360 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.8191 _refine.correlation_coeff_Fo_to_Fc_free 0.8216 _refine.B_iso_mean 145.51 _refine.aniso_B[1][1] 8.7443 _refine.aniso_B[2][2] 8.7443 _refine.aniso_B[3][3] -17.4885 _refine.aniso_B[1][2] 0.0000 _refine.aniso_B[1][3] 0.0000 _refine.aniso_B[2][3] 0.0000 _refine.solvent_model_details ? _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details ;TLS REFINEMENT AND SECONDARY INITIAL COORDINATES FROM MOLECULAR REPLACEMENT. SECONDARY STRUCTURE RESTRAINTS TO THE INITIAL COORDINATES FROM MOLECULAR REPLACEMENT. ; _refine.pdbx_starting_model 'PDB ENTRIES 3DEM AND 3GOV' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ? _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML ? _refine.pdbx_overall_phase_error ? _refine.overall_SU_B ? _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 0.797 # _refine_analyze.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_analyze.entry_id 4AQB _refine_analyze.Luzzati_coordinate_error_obs 1.502 _refine_analyze.Luzzati_sigma_a_obs ? _refine_analyze.Luzzati_d_res_low_obs ? _refine_analyze.Luzzati_coordinate_error_free ? _refine_analyze.Luzzati_sigma_a_free ? _refine_analyze.Luzzati_d_res_low_free ? _refine_analyze.number_disordered_residues ? _refine_analyze.occupancy_sum_hydrogen ? _refine_analyze.occupancy_sum_non_hydrogen ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 2774 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 117 _refine_hist.number_atoms_solvent 5 _refine_hist.number_atoms_total 2896 _refine_hist.d_res_high 4.20 _refine_hist.d_res_low 58.36 # 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 t_bond_d 0.006 ? 2.00 2999 'X-RAY DIFFRACTION' HARMONIC t_angle_deg 1.02 ? 2.00 4073 'X-RAY DIFFRACTION' HARMONIC t_dihedral_angle_d ? ? 2.00 1049 'X-RAY DIFFRACTION' SINUSOIDAL t_incorr_chiral_ct ? ? ? ? 'X-RAY DIFFRACTION' ? t_pseud_angle ? ? ? ? 'X-RAY DIFFRACTION' ? t_trig_c_planes ? ? 2.00 86 'X-RAY DIFFRACTION' HARMONIC t_gen_planes ? ? 5.00 422 'X-RAY DIFFRACTION' HARMONIC t_it ? ? 20.00 2999 'X-RAY DIFFRACTION' HARMONIC t_nbd ? ? 5.00 3 'X-RAY DIFFRACTION' SEMIHARMONIC t_omega_torsion 3.21 ? ? ? 'X-RAY DIFFRACTION' ? t_other_torsion 17.28 ? ? ? 'X-RAY DIFFRACTION' ? t_improper_torsion ? ? ? ? 'X-RAY DIFFRACTION' ? t_chiral_improper_torsion ? ? 5.00 410 'X-RAY DIFFRACTION' SEMIHARMONIC t_sum_occupancies ? ? ? ? 'X-RAY DIFFRACTION' ? t_utility_distance ? ? 1.00 23 'X-RAY DIFFRACTION' HARMONIC t_utility_angle ? ? ? ? 'X-RAY DIFFRACTION' ? t_utility_torsion ? ? ? ? 'X-RAY DIFFRACTION' ? t_ideal_dist_contact ? ? 4.00 3182 'X-RAY DIFFRACTION' SEMIHARMONIC # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 5 _refine_ls_shell.d_res_high 4.20 _refine_ls_shell.d_res_low 4.70 _refine_ls_shell.number_reflns_R_work 1908 _refine_ls_shell.R_factor_R_work 0.2675 _refine_ls_shell.percent_reflns_obs 91.80 _refine_ls_shell.R_factor_R_free 0.2617 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free 4.46 _refine_ls_shell.number_reflns_R_free 89 _refine_ls_shell.number_reflns_all 1997 _refine_ls_shell.R_factor_all 0.2672 # _struct.entry_id 4AQB _struct.title 'MBL-Ficolin Associated Protein-1, MAP-1 aka MAP44' _struct.pdbx_descriptor 'MANNAN-BINDING LECTIN SERINE PROTEASE 1' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4AQB _struct_keywords.pdbx_keywords 'BLOOD CLOTTING' _struct_keywords.text ;BLOOD CLOTTING, MANNAN-BINDING PROTEIN, COMPLEMENT, FICOLINS, LECTIN COMPLEMENT PATHWAY, MANNOSE- BINDING LECTIN, MBL/FICOLIN ASSOCIATED PROTEIN-1, MBL/FICOLIN ASSOCIATED SERINE PROTEASES, MAP1, MAP44 ; # 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 2 ? D N N 3 ? E N N 4 ? F N N 4 ? G N N 2 ? H N N 2 ? I N N 3 ? J N N 4 ? K N N 5 ? L N N 5 ? M N N 5 ? N N N 5 ? O N N 5 ? P N N 5 ? Q N N 6 ? # 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 SER A 51 ? GLU A 55 ? SER A 70 GLU A 74 5 ? 5 HELX_P HELX_P2 2 ASP A 122 ? GLU A 126 ? ASP A 141 GLU A 145 5 ? 5 HELX_P HELX_P3 3 GLU A 126 ? GLU A 130 ? GLU A 145 GLU A 149 5 ? 5 # _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 54 SG ? ? ? 1_555 A CYS 72 SG ? ? A CYS 73 A CYS 91 1_555 ? ? ? ? ? ? ? 2.034 ? disulf2 disulf ? ? A CYS 124 SG ? ? ? 1_555 A CYS 138 SG ? ? A CYS 143 A CYS 157 1_555 ? ? ? ? ? ? ? 2.031 ? disulf3 disulf ? ? A CYS 134 SG ? ? ? 1_555 A CYS 147 SG ? ? A CYS 153 A CYS 166 1_555 ? ? ? ? ? ? ? 2.033 ? disulf4 disulf ? ? A CYS 149 SG ? ? ? 1_555 A CYS 162 SG ? ? A CYS 168 A CYS 181 1_555 ? ? ? ? ? ? ? 2.030 ? disulf5 disulf ? ? A CYS 166 SG ? ? ? 1_555 A CYS 193 SG ? ? A CYS 185 A CYS 212 1_555 ? ? ? ? ? ? ? 2.033 ? disulf6 disulf ? ? A CYS 223 SG ? ? ? 1_555 A CYS 241 SG ? ? A CYS 242 A CYS 260 1_555 ? ? ? ? ? ? ? 2.034 ? disulf7 disulf ? ? A CYS 282 SG ? ? ? 1_555 A CYS 330 SG ? ? A CYS 301 A CYS 349 1_555 ? ? ? ? ? ? ? 2.030 ? disulf8 disulf ? ? A CYS 310 SG ? ? ? 1_555 A CYS 343 SG ? ? A CYS 329 A CYS 362 1_555 ? ? ? ? ? ? ? 2.030 ? covale1 covale ? ? A ASN 30 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 49 A NAG 649 1_555 ? ? ? ? ? ? ? 1.423 ? covale2 covale ? ? A ASN 159 ND2 ? ? ? 1_555 G NAG . C1 ? ? A ASN 178 A NAG 678 1_555 ? ? ? ? ? ? ? 1.433 ? covale3 covale ? ? B NAG . O4 ? ? ? 1_555 C NAG . C1 ? ? A NAG 649 A NAG 650 1_555 ? ? ? ? ? ? ? 1.425 ? covale4 covale ? ? C NAG . O4 ? ? ? 1_555 D BMA . C1 ? ? A NAG 650 A BMA 651 1_555 ? ? ? ? ? ? ? 1.423 ? covale5 covale ? ? D BMA . O3 ? ? ? 1_555 E MAN . C1 ? ? A BMA 651 A MAN 652 1_555 ? ? ? ? ? ? ? 1.430 ? covale6 covale ? ? D BMA . O6 ? ? ? 1_555 F MAN . C1 ? ? A BMA 651 A MAN 653 1_555 ? ? ? ? ? ? ? 1.410 ? covale7 covale ? ? G NAG . O4 ? ? ? 1_555 H NAG . C1 ? ? A NAG 678 A NAG 679 1_555 ? ? ? ? ? ? ? 1.439 ? covale8 covale ? ? H NAG . O4 ? ? ? 1_555 I BMA . C1 ? ? A NAG 679 A BMA 680 1_555 ? ? ? ? ? ? ? 1.418 ? covale9 covale ? ? I BMA . O3 ? ? ? 1_555 J MAN . C1 ? ? A BMA 680 A MAN 681 1_555 ? ? ? ? ? ? ? 1.428 ? metalc1 metalc ? ? K CA . CA ? ? ? 1_555 A VAL 121 O ? ? A CA 701 A VAL 140 1_555 ? ? ? ? ? ? ? 2.424 ? metalc2 metalc ? ? K CA . CA ? ? ? 1_555 Q HOH . O ? ? A CA 701 A HOH 2001 1_555 ? ? ? ? ? ? ? 2.298 ? metalc3 metalc ? ? K CA . CA ? ? ? 1_555 A GLU 123 OE1 ? ? A CA 701 A GLU 142 1_555 ? ? ? ? ? ? ? 2.715 ? metalc4 metalc ? ? K CA . CA ? ? ? 1_555 A ASN 140 OD1 ? ? A CA 701 A ASN 159 1_555 ? ? ? ? ? ? ? 2.135 ? metalc5 metalc ? ? K CA . CA ? ? ? 1_555 A TYR 141 O ? ? A CA 701 A TYR 160 1_555 ? ? ? ? ? ? ? 2.361 ? metalc6 metalc ? ? K CA . CA ? ? ? 1_555 A GLY 144 O ? ? A CA 701 A GLY 163 1_555 ? ? ? ? ? ? ? 2.560 ? metalc7 metalc ? ? K CA . CA ? ? ? 1_555 A ASP 120 OD1 ? ? A CA 701 A ASP 139 1_555 ? ? ? ? ? ? ? 2.661 ? metalc8 metalc ? ? K CA . CA ? ? ? 1_555 A ASP 120 OD2 ? ? A CA 701 A ASP 139 1_555 ? ? ? ? ? ? ? 2.850 ? metalc9 metalc ? ? L CA . CA ? ? ? 1_555 A ASP 57 OD1 ? ? A CA 702 A ASP 76 1_555 ? ? ? ? ? ? ? 2.667 ? metalc10 metalc ? ? L CA . CA ? ? ? 1_555 A ASP 57 OD2 ? ? A CA 702 A ASP 76 1_555 ? ? ? ? ? ? ? 2.603 ? metalc11 metalc ? ? L CA . CA ? ? ? 1_555 A ASP 102 OD1 ? ? A CA 702 A ASP 121 1_555 ? ? ? ? ? ? ? 2.367 ? metalc12 metalc ? ? L CA . CA ? ? ? 1_555 Q HOH . O ? ? A CA 702 A HOH 2003 1_555 ? ? ? ? ? ? ? 2.645 ? metalc13 metalc ? ? L CA . CA ? ? ? 1_555 A GLU 49 OE1 ? ? A CA 702 A GLU 68 1_555 ? ? ? ? ? ? ? 2.487 ? metalc14 metalc ? ? L CA . CA ? ? ? 1_555 A GLU 49 OE2 ? ? A CA 702 A GLU 68 1_555 ? ? ? ? ? ? ? 2.655 ? metalc15 metalc ? ? L CA . CA ? ? ? 1_555 Q HOH . O ? ? A CA 702 A HOH 2002 1_555 ? ? ? ? ? ? ? 2.589 ? metalc16 metalc ? ? L CA . CA ? ? ? 1_555 A SER 104 O ? ? A CA 702 A SER 123 1_555 ? ? ? ? ? ? ? 2.553 ? metalc17 metalc ? ? M CA . CA ? ? ? 1_555 Q HOH . O ? ? A CA 703 A HOH 2005 1_555 ? ? ? ? ? ? ? 2.385 ? metalc18 metalc ? ? M CA . CA ? ? ? 1_555 A ASP 226 OD1 ? ? A CA 703 A ASP 245 1_555 ? ? ? ? ? ? ? 2.504 ? metalc19 metalc ? ? M CA . CA ? ? ? 1_555 Q HOH . O ? ? A CA 703 A HOH 2004 1_555 ? ? ? ? ? ? ? 2.217 ? metalc20 metalc ? ? M CA . CA ? ? ? 1_555 A ASP 226 OD2 ? ? A CA 703 A ASP 245 1_555 ? ? ? ? ? ? ? 2.449 ? metalc21 metalc ? ? M CA . CA ? ? ? 1_555 A ASP 263 OD1 ? ? A CA 703 A ASP 282 1_555 ? ? ? ? ? ? ? 2.099 ? metalc22 metalc ? ? M CA . CA ? ? ? 1_555 A GLU 216 OE1 ? ? A CA 703 A GLU 235 1_555 ? ? ? ? ? ? ? 2.101 ? metalc23 metalc ? ? M CA . CA ? ? ? 1_555 A SER 265 O ? ? A CA 703 A SER 284 1_555 ? ? ? ? ? ? ? 2.501 ? # 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 TYR 17 A . ? TYR 36 A PRO 18 A ? PRO 37 A 1 3.49 2 PHE 183 A . ? PHE 202 A PRO 184 A ? PRO 203 A 1 1.92 3 GLY 238 A . ? GLY 257 A PRO 239 A ? PRO 258 A 1 0.89 4 GLU 294 A . ? GLU 313 A PRO 295 A ? PRO 314 A 1 -1.11 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA ? 5 ? AB ? 4 ? AC ? 2 ? AD ? 2 ? AE ? 4 ? AF ? 4 ? AG ? 2 ? AH ? 3 ? AI ? 3 ? # 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 ? anti-parallel AA 3 4 ? anti-parallel AA 4 5 ? anti-parallel AB 1 2 ? anti-parallel AB 2 3 ? anti-parallel AB 3 4 ? anti-parallel AC 1 2 ? anti-parallel AD 1 2 ? anti-parallel AE 1 2 ? anti-parallel AE 2 3 ? anti-parallel AE 3 4 ? anti-parallel AF 1 2 ? anti-parallel AF 2 3 ? anti-parallel AF 3 4 ? anti-parallel AG 1 2 ? anti-parallel AH 1 2 ? anti-parallel AH 2 3 ? anti-parallel AI 1 2 ? anti-parallel AI 2 3 ? anti-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 GLU A 4 ? ASN A 6 ? GLU A 23 ASN A 25 AA 2 SER A 25 ? THR A 32 ? SER A 44 THR A 51 AA 3 PHE A 94 ? SER A 101 ? PHE A 113 SER A 120 AA 4 TYR A 58 ? GLU A 62 ? TYR A 77 GLU A 81 AA 5 VAL A 67 ? PHE A 71 ? VAL A 86 PHE A 90 AB 1 PHE A 9 ? GLN A 13 ? PHE A 28 GLN A 32 AB 2 GLY A 111 ? ASP A 120 ? GLY A 130 ASP A 139 AB 3 PHE A 37 ? ASN A 47 ? PHE A 56 ASN A 66 AB 4 VAL A 88 ? LEU A 89 ? VAL A 107 LEU A 108 AC 1 TYR A 137 ? TYR A 141 ? TYR A 156 TYR A 160 AC 2 GLY A 144 ? SER A 148 ? GLY A 163 SER A 167 AD 1 ILE A 154 ? LEU A 155 ? ILE A 173 LEU A 174 AD 2 CYS A 162 ? ARG A 163 ? CYS A 181 ARG A 182 AE 1 THR A 175 ? THR A 179 ? THR A 194 THR A 198 AE 2 ARG A 272 ? ALA A 278 ? ARG A 291 ALA A 297 AE 3 MET A 204 ? PHE A 209 ? MET A 223 PHE A 228 AE 4 ILE A 249 ? SER A 250 ? ILE A 268 SER A 269 AF 1 GLU A 192 ? GLU A 198 ? GLU A 211 GLU A 217 AF 2 SER A 255 ? HIS A 261 ? SER A 274 HIS A 280 AF 3 TYR A 227 ? VAL A 232 ? TYR A 246 VAL A 251 AF 4 LYS A 235 ? PHE A 240 ? LYS A 254 PHE A 259 AG 1 GLU A 281 ? CYS A 282 ? GLU A 300 CYS A 301 AG 2 TYR A 300 ? PHE A 301 ? TYR A 319 PHE A 320 AH 1 GLY A 291 ? GLU A 294 ? GLY A 310 GLU A 313 AH 2 GLN A 305 ? CYS A 310 ? GLN A 324 CYS A 329 AH 3 THR A 325 ? GLU A 329 ? THR A 344 GLU A 348 AI 1 VAL A 321 ? MET A 323 ? VAL A 340 MET A 342 AI 2 TYR A 314 ? LYS A 318 ? TYR A 333 LYS A 337 AI 3 THR A 342 ? LYS A 345 ? THR A 361 LYS A 364 # 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 N LEU A 5 ? N LEU A 24 O ASN A 30 ? O ASN A 49 AA 2 3 N ILE A 31 ? N ILE A 50 O MET A 95 ? O MET A 114 AA 3 4 N ARG A 100 ? N ARG A 119 O TYR A 58 ? O TYR A 77 AA 4 5 O VAL A 61 ? O VAL A 80 N LEU A 68 ? N LEU A 87 AB 1 2 N ILE A 12 ? N ILE A 31 O ALA A 114 ? O ALA A 133 AB 2 3 N VAL A 119 ? N VAL A 138 O ARG A 38 ? O ARG A 57 AB 3 4 N LEU A 41 ? N LEU A 60 O VAL A 88 ? O VAL A 107 AC 1 2 N TYR A 141 ? N TYR A 160 O GLY A 144 ? O GLY A 163 AD 1 2 N ILE A 154 ? N ILE A 173 O ARG A 163 ? O ARG A 182 AE 1 2 N ILE A 178 ? N ILE A 197 O LEU A 273 ? O LEU A 292 AE 2 3 N ALA A 278 ? N ALA A 297 O MET A 204 ? O MET A 223 AE 3 4 N LEU A 207 ? N LEU A 226 O ILE A 249 ? O ILE A 268 AF 1 2 N ILE A 197 ? N ILE A 216 O VAL A 256 ? O VAL A 275 AF 2 3 N HIS A 261 ? N HIS A 280 O TYR A 227 ? O TYR A 246 AF 3 4 N VAL A 232 ? N VAL A 251 O LYS A 235 ? O LYS A 254 AG 1 2 N CYS A 282 ? N CYS A 301 O TYR A 300 ? O TYR A 319 AH 1 2 N GLU A 294 ? N GLU A 313 O LEU A 307 ? O LEU A 326 AH 2 3 N VAL A 308 ? N VAL A 327 O PHE A 326 ? O PHE A 345 AI 1 2 N MET A 323 ? N MET A 342 O VAL A 316 ? O VAL A 335 AI 2 3 N LEU A 317 ? N LEU A 336 O THR A 342 ? O THR A 361 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE CA A 701' AC2 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE CA A 702' AC3 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE CA A 703' AC4 Software ? ? ? ? 5 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 49 RESIDUES 649 TO 653' AC5 Software ? ? ? ? 1 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 178 RESIDUES 678 TO 681' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 7 ASP A 120 ? ASP A 139 . ? 1_555 ? 2 AC1 7 VAL A 121 ? VAL A 140 . ? 1_555 ? 3 AC1 7 GLU A 123 ? GLU A 142 . ? 1_555 ? 4 AC1 7 ASN A 140 ? ASN A 159 . ? 1_555 ? 5 AC1 7 TYR A 141 ? TYR A 160 . ? 1_555 ? 6 AC1 7 GLY A 144 ? GLY A 163 . ? 1_555 ? 7 AC1 7 HOH Q . ? HOH A 2001 . ? 1_555 ? 8 AC2 6 GLU A 49 ? GLU A 68 . ? 1_555 ? 9 AC2 6 ASP A 57 ? ASP A 76 . ? 1_555 ? 10 AC2 6 ASP A 102 ? ASP A 121 . ? 1_555 ? 11 AC2 6 SER A 104 ? SER A 123 . ? 1_555 ? 12 AC2 6 HOH Q . ? HOH A 2002 . ? 1_555 ? 13 AC2 6 HOH Q . ? HOH A 2003 . ? 1_555 ? 14 AC3 6 GLU A 216 ? GLU A 235 . ? 1_555 ? 15 AC3 6 ASP A 226 ? ASP A 245 . ? 1_555 ? 16 AC3 6 ASP A 263 ? ASP A 282 . ? 1_555 ? 17 AC3 6 SER A 265 ? SER A 284 . ? 1_555 ? 18 AC3 6 HOH Q . ? HOH A 2004 . ? 1_555 ? 19 AC3 6 HOH Q . ? HOH A 2005 . ? 1_555 ? 20 AC4 5 GLU A 4 ? GLU A 23 . ? 1_555 ? 21 AC4 5 ASN A 30 ? ASN A 49 . ? 1_555 ? 22 AC4 5 GLU A 64 ? GLU A 83 . ? 1_555 ? 23 AC4 5 PHE A 94 ? PHE A 113 . ? 1_555 ? 24 AC4 5 SER A 96 ? SER A 115 . ? 1_555 ? 25 AC5 1 ASN A 159 ? ASN A 178 . ? 1_555 ? # _database_PDB_matrix.entry_id 4AQB _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 4AQB _atom_sites.fract_transf_matrix[1][1] 0.010621 _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] 0.010621 _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] 0.004123 _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 . VAL A 1 3 ? -21.412 -11.233 10.152 1.00 201.64 ? 22 VAL A N 1 ATOM 2 C CA . VAL A 1 3 ? -20.724 -11.101 8.867 1.00 196.96 ? 22 VAL A CA 1 ATOM 3 C C . VAL A 1 3 ? -19.248 -10.763 9.127 1.00 193.41 ? 22 VAL A C 1 ATOM 4 O O . VAL A 1 3 ? -18.958 -9.641 9.536 1.00 184.32 ? 22 VAL A O 1 ATOM 5 C CB . VAL A 1 3 ? -21.398 -10.032 7.953 1.00 176.90 ? 22 VAL A CB 1 ATOM 6 C CG1 . VAL A 1 3 ? -20.711 -9.955 6.594 1.00 173.60 ? 22 VAL A CG1 1 ATOM 7 C CG2 . VAL A 1 3 ? -22.894 -10.290 7.784 1.00 182.05 ? 22 VAL A CG2 1 ATOM 8 N N . GLU A 1 4 ? -18.320 -11.710 8.884 1.00 201.04 ? 23 GLU A N 1 ATOM 9 C CA . GLU A 1 4 ? -16.880 -11.475 9.087 1.00 197.90 ? 23 GLU A CA 1 ATOM 10 C C . GLU A 1 4 ? -16.159 -11.196 7.758 1.00 192.32 ? 23 GLU A C 1 ATOM 11 O O . GLU A 1 4 ? -16.390 -11.923 6.788 1.00 197.83 ? 23 GLU A O 1 ATOM 12 C CB . GLU A 1 4 ? -16.224 -12.653 9.823 1.00 201.31 ? 23 GLU A CB 1 ATOM 13 C CG . GLU A 1 4 ? -16.561 -12.742 11.303 1.00 208.02 ? 23 GLU A CG 1 ATOM 14 C CD . GLU A 1 4 ? -16.107 -14.030 11.962 1.00 224.55 ? 23 GLU A CD 1 ATOM 15 O OE1 . GLU A 1 4 ? -14.982 -14.490 11.662 1.00 229.84 ? 23 GLU A OE1 1 ATOM 16 O OE2 . GLU A 1 4 ? -16.869 -14.570 12.796 1.00 233.73 ? 23 GLU A OE2 1 ATOM 17 N N . LEU A 1 5 ? -15.284 -10.147 7.716 1.00 187.93 ? 24 LEU A N 1 ATOM 18 C CA . LEU A 1 5 ? -14.531 -9.721 6.515 1.00 183.15 ? 24 LEU A CA 1 ATOM 19 C C . LEU A 1 5 ? -13.059 -9.269 6.751 1.00 183.77 ? 24 LEU A C 1 ATOM 20 O O . LEU A 1 5 ? -12.842 -8.175 7.272 1.00 176.67 ? 24 LEU A O 1 ATOM 21 C CB . LEU A 1 5 ? -15.282 -8.572 5.789 1.00 160.07 ? 24 LEU A CB 1 ATOM 22 C CG . LEU A 1 5 ? -16.079 -8.873 4.507 1.00 161.47 ? 24 LEU A CG 1 ATOM 23 C CD1 . LEU A 1 5 ? -16.636 -7.590 3.915 1.00 150.80 ? 24 LEU A CD1 1 ATOM 24 C CD2 . LEU A 1 5 ? -15.230 -9.568 3.444 1.00 170.37 ? 24 LEU A CD2 1 ATOM 25 N N . ASN A 1 6 ? -12.059 -10.058 6.287 1.00 195.99 ? 25 ASN A N 1 ATOM 26 C CA . ASN A 1 6 ? -10.636 -9.689 6.375 1.00 198.38 ? 25 ASN A CA 1 ATOM 27 C C . ASN A 1 6 ? -10.047 -9.587 4.955 1.00 195.25 ? 25 ASN A C 1 ATOM 28 O O . ASN A 1 6 ? -10.047 -10.580 4.220 1.00 203.62 ? 25 ASN A O 1 ATOM 29 C CB . ASN A 1 6 ? -9.842 -10.655 7.285 1.00 203.72 ? 25 ASN A CB 1 ATOM 30 C CG . ASN A 1 6 ? -8.952 -11.637 6.563 1.00 216.17 ? 25 ASN A CG 1 ATOM 31 O OD1 . ASN A 1 6 ? -7.755 -11.404 6.371 1.00 219.72 ? 25 ASN A OD1 1 ATOM 32 N ND2 . ASN A 1 6 ? -9.545 -12.697 6.039 1.00 224.39 ? 25 ASN A ND2 1 ATOM 33 N N . ASN A 1 7 ? -9.607 -8.376 4.555 1.00 166.93 ? 26 ASN A N 1 ATOM 34 C CA . ASN A 1 7 ? -9.058 -8.073 3.222 1.00 161.38 ? 26 ASN A CA 1 ATOM 35 C C . ASN A 1 7 ? -8.549 -6.615 3.187 1.00 148.68 ? 26 ASN A C 1 ATOM 36 O O . ASN A 1 7 ? -8.469 -6.009 4.251 1.00 147.19 ? 26 ASN A O 1 ATOM 37 C CB . ASN A 1 7 ? -10.113 -8.286 2.132 1.00 162.20 ? 26 ASN A CB 1 ATOM 38 C CG . ASN A 1 7 ? -11.201 -7.262 2.195 1.00 160.71 ? 26 ASN A CG 1 ATOM 39 O OD1 . ASN A 1 7 ? -11.154 -6.263 1.497 1.00 162.68 ? 26 ASN A OD1 1 ATOM 40 N ND2 . ASN A 1 7 ? -12.146 -7.439 3.100 1.00 160.09 ? 26 ASN A ND2 1 ATOM 41 N N . MET A 1 8 ? -8.256 -6.048 1.968 1.00 102.87 ? 27 MET A N 1 ATOM 42 C CA . MET A 1 8 ? -7.640 -4.724 1.698 1.00 101.32 ? 27 MET A CA 1 ATOM 43 C C . MET A 1 8 ? -8.606 -3.601 1.290 1.00 96.65 ? 27 MET A C 1 ATOM 44 O O . MET A 1 8 ? -8.230 -2.424 1.312 1.00 96.04 ? 27 MET A O 1 ATOM 45 C CB . MET A 1 8 ? -6.572 -4.859 0.587 1.00 108.05 ? 27 MET A CB 1 ATOM 46 C CG . MET A 1 8 ? -5.414 -5.780 0.933 1.00 114.50 ? 27 MET A CG 1 ATOM 47 S SD . MET A 1 8 ? -4.214 -5.922 -0.404 1.00 118.33 ? 27 MET A SD 1 ATOM 48 C CE . MET A 1 8 ? -3.362 -4.420 -0.187 1.00 116.93 ? 27 MET A CE 1 ATOM 49 N N . PHE A 1 9 ? -9.818 -3.976 0.862 1.00 94.99 ? 28 PHE A N 1 ATOM 50 C CA . PHE A 1 9 ? -10.858 -3.064 0.390 1.00 92.62 ? 28 PHE A CA 1 ATOM 51 C C . PHE A 1 9 ? -12.232 -3.733 0.442 1.00 91.28 ? 28 PHE A C 1 ATOM 52 O O . PHE A 1 9 ? -12.321 -4.949 0.566 1.00 93.40 ? 28 PHE A O 1 ATOM 53 C CB . PHE A 1 9 ? -10.556 -2.641 -1.063 1.00 98.08 ? 28 PHE A CB 1 ATOM 54 C CG . PHE A 1 9 ? -10.770 -3.735 -2.085 1.00 103.54 ? 28 PHE A CG 1 ATOM 55 C CD1 . PHE A 1 9 ? -9.809 -4.720 -2.289 1.00 108.50 ? 28 PHE A CD1 1 ATOM 56 C CD2 . PHE A 1 9 ? -11.941 -3.791 -2.833 1.00 105.38 ? 28 PHE A CD2 1 ATOM 57 C CE1 . PHE A 1 9 ? -10.016 -5.739 -3.221 1.00 114.91 ? 28 PHE A CE1 1 ATOM 58 C CE2 . PHE A 1 9 ? -12.146 -4.810 -3.766 1.00 112.17 ? 28 PHE A CE2 1 ATOM 59 C CZ . PHE A 1 9 ? -11.182 -5.776 -3.955 1.00 117.00 ? 28 PHE A CZ 1 ATOM 60 N N . GLY A 1 10 ? -13.299 -2.958 0.254 1.00 89.49 ? 29 GLY A N 1 ATOM 61 C CA . GLY A 1 10 ? -14.638 -3.532 0.227 1.00 89.79 ? 29 GLY A CA 1 ATOM 62 C C . GLY A 1 10 ? -15.748 -2.499 0.235 1.00 88.58 ? 29 GLY A C 1 ATOM 63 O O . GLY A 1 10 ? -15.511 -1.314 0.484 1.00 86.88 ? 29 GLY A O 1 ATOM 64 N N . GLN A 1 11 ? -16.969 -2.970 -0.044 1.00 91.20 ? 30 GLN A N 1 ATOM 65 C CA . GLN A 1 11 ? -18.188 -2.173 -0.070 1.00 91.95 ? 30 GLN A CA 1 ATOM 66 C C . GLN A 1 11 ? -19.176 -2.768 0.915 1.00 90.73 ? 30 GLN A C 1 ATOM 67 O O . GLN A 1 11 ? -19.257 -3.991 1.052 1.00 92.59 ? 30 GLN A O 1 ATOM 68 C CB . GLN A 1 11 ? -18.796 -2.171 -1.479 1.00 99.14 ? 30 GLN A CB 1 ATOM 69 C CG . GLN A 1 11 ? -20.005 -1.249 -1.656 1.00 102.84 ? 30 GLN A CG 1 ATOM 70 C CD . GLN A 1 11 ? -20.482 -1.198 -3.087 1.00 111.98 ? 30 GLN A CD 1 ATOM 71 O OE1 . GLN A 1 11 ? -19.873 -1.762 -4.005 1.00 117.63 ? 30 GLN A OE1 1 ATOM 72 N NE2 . GLN A 1 11 ? -21.585 -0.504 -3.316 1.00 115.18 ? 30 GLN A NE2 1 ATOM 73 N N . ILE A 1 12 ? -19.923 -1.902 1.603 1.00 89.37 ? 31 ILE A N 1 ATOM 74 C CA . ILE A 1 12 ? -20.946 -2.310 2.557 1.00 89.59 ? 31 ILE A CA 1 ATOM 75 C C . ILE A 1 12 ? -22.204 -1.508 2.290 1.00 93.07 ? 31 ILE A C 1 ATOM 76 O O . ILE A 1 12 ? -22.140 -0.294 2.097 1.00 93.15 ? 31 ILE A O 1 ATOM 77 C CB . ILE A 1 12 ? -20.469 -2.193 4.031 1.00 85.26 ? 31 ILE A CB 1 ATOM 78 C CG1 . ILE A 1 12 ? -19.371 -3.227 4.345 1.00 83.98 ? 31 ILE A CG1 1 ATOM 79 C CG2 . ILE A 1 12 ? -21.638 -2.332 5.010 1.00 87.63 ? 31 ILE A CG2 1 ATOM 80 C CD1 . ILE A 1 12 ? -18.604 -2.970 5.618 1.00 81.52 ? 31 ILE A CD1 1 ATOM 81 N N . GLN A 1 13 ? -23.346 -2.193 2.278 1.00 97.66 ? 32 GLN A N 1 ATOM 82 C CA . GLN A 1 13 ? -24.646 -1.574 2.077 1.00 102.77 ? 32 GLN A CA 1 ATOM 83 C C . GLN A 1 13 ? -25.577 -2.029 3.183 1.00 104.35 ? 32 GLN A C 1 ATOM 84 O O . GLN A 1 13 ? -25.361 -3.086 3.784 1.00 103.69 ? 32 GLN A O 1 ATOM 85 C CB . GLN A 1 13 ? -25.249 -1.999 0.729 1.00 110.58 ? 32 GLN A CB 1 ATOM 86 C CG . GLN A 1 13 ? -24.376 -1.751 -0.499 1.00 111.71 ? 32 GLN A CG 1 ATOM 87 C CD . GLN A 1 13 ? -24.933 -2.403 -1.745 1.00 120.96 ? 32 GLN A CD 1 ATOM 88 O OE1 . GLN A 1 13 ? -25.913 -3.162 -1.717 1.00 126.94 ? 32 GLN A OE1 1 ATOM 89 N NE2 . GLN A 1 13 ? -24.311 -2.123 -2.879 1.00 124.59 ? 32 GLN A NE2 1 ATOM 90 N N . SER A 1 14 ? -26.636 -1.251 3.425 1.00 108.25 ? 33 SER A N 1 ATOM 91 C CA . SER A 1 14 ? -27.677 -1.603 4.382 1.00 112.02 ? 33 SER A CA 1 ATOM 92 C C . SER A 1 14 ? -28.548 -2.693 3.740 1.00 119.79 ? 33 SER A C 1 ATOM 93 O O . SER A 1 14 ? -28.634 -2.733 2.507 1.00 123.49 ? 33 SER A O 1 ATOM 94 C CB . SER A 1 14 ? -28.542 -0.389 4.699 1.00 115.67 ? 33 SER A CB 1 ATOM 95 O OG . SER A 1 14 ? -28.979 0.246 3.509 1.00 120.71 ? 33 SER A OG 1 ATOM 96 N N . PRO A 1 15 ? -29.194 -3.570 4.552 1.00 123.79 ? 34 PRO A N 1 ATOM 97 C CA . PRO A 1 15 ? -30.063 -4.610 3.989 1.00 133.32 ? 34 PRO A CA 1 ATOM 98 C C . PRO A 1 15 ? -31.147 -3.982 3.107 1.00 141.12 ? 34 PRO A C 1 ATOM 99 O O . PRO A 1 15 ? -31.769 -3.001 3.513 1.00 142.51 ? 34 PRO A O 1 ATOM 100 C CB . PRO A 1 15 ? -30.673 -5.274 5.227 1.00 137.63 ? 34 PRO A CB 1 ATOM 101 C CG . PRO A 1 15 ? -29.706 -5.033 6.301 1.00 129.57 ? 34 PRO A CG 1 ATOM 102 C CD . PRO A 1 15 ? -29.056 -3.721 6.016 1.00 121.65 ? 34 PRO A CD 1 ATOM 103 N N . GLY A 1 16 ? -31.323 -4.502 1.885 1.00 147.02 ? 35 GLY A N 1 ATOM 104 C CA . GLY A 1 16 ? -32.339 -4.002 0.958 1.00 156.89 ? 35 GLY A CA 1 ATOM 105 C C . GLY A 1 16 ? -31.853 -2.942 -0.028 1.00 155.29 ? 35 GLY A C 1 ATOM 106 O O . GLY A 1 16 ? -32.525 -2.738 -1.037 1.00 165.04 ? 35 GLY A O 1 ATOM 107 N N . TYR A 1 17 ? -30.702 -2.278 0.243 1.00 144.77 ? 36 TYR A N 1 ATOM 108 C CA . TYR A 1 17 ? -30.137 -1.239 -0.633 1.00 144.12 ? 36 TYR A CA 1 ATOM 109 C C . TYR A 1 17 ? -30.158 -1.674 -2.114 1.00 152.24 ? 36 TYR A C 1 ATOM 110 O O . TYR A 1 17 ? -29.827 -2.828 -2.395 1.00 152.66 ? 36 TYR A O 1 ATOM 111 C CB . TYR A 1 17 ? -28.711 -0.849 -0.198 1.00 132.64 ? 36 TYR A CB 1 ATOM 112 C CG . TYR A 1 17 ? -28.142 0.346 -0.939 1.00 133.16 ? 36 TYR A CG 1 ATOM 113 C CD1 . TYR A 1 17 ? -27.485 0.189 -2.157 1.00 135.84 ? 36 TYR A CD1 1 ATOM 114 C CD2 . TYR A 1 17 ? -28.261 1.633 -0.423 1.00 132.69 ? 36 TYR A CD2 1 ATOM 115 C CE1 . TYR A 1 17 ? -26.993 1.287 -2.860 1.00 138.49 ? 36 TYR A CE1 1 ATOM 116 C CE2 . TYR A 1 17 ? -27.750 2.737 -1.106 1.00 135.09 ? 36 TYR A CE2 1 ATOM 117 C CZ . TYR A 1 17 ? -27.117 2.558 -2.326 1.00 138.45 ? 36 TYR A CZ 1 ATOM 118 O OH . TYR A 1 17 ? -26.610 3.639 -3.006 1.00 142.47 ? 36 TYR A OH 1 ATOM 119 N N . PRO A 1 18 ? -30.579 -0.783 -3.053 1.00 160.68 ? 37 PRO A N 1 ATOM 120 C CA . PRO A 1 18 ? -30.978 0.621 -2.897 1.00 163.24 ? 37 PRO A CA 1 ATOM 121 C C . PRO A 1 18 ? -32.414 0.858 -2.419 1.00 171.83 ? 37 PRO A C 1 ATOM 122 O O . PRO A 1 18 ? -32.839 2.011 -2.323 1.00 176.63 ? 37 PRO A O 1 ATOM 123 C CB . PRO A 1 18 ? -30.673 1.207 -4.277 1.00 171.16 ? 37 PRO A CB 1 ATOM 124 C CG . PRO A 1 18 ? -30.968 0.078 -5.217 1.00 179.20 ? 37 PRO A CG 1 ATOM 125 C CD . PRO A 1 18 ? -30.627 -1.195 -4.470 1.00 170.66 ? 37 PRO A CD 1 ATOM 126 N N . ASP A 1 19 ? -33.150 -0.217 -2.102 1.00 175.11 ? 38 ASP A N 1 ATOM 127 C CA . ASP A 1 19 ? -34.516 -0.100 -1.596 1.00 184.01 ? 38 ASP A CA 1 ATOM 128 C C . ASP A 1 19 ? -34.490 0.184 -0.099 1.00 176.02 ? 38 ASP A C 1 ATOM 129 O O . ASP A 1 19 ? -33.441 0.036 0.536 1.00 163.88 ? 38 ASP A O 1 ATOM 130 C CB . ASP A 1 19 ? -35.325 -1.372 -1.897 1.00 206.09 ? 38 ASP A CB 1 ATOM 131 C CG . ASP A 1 19 ? -35.525 -1.635 -3.374 1.00 249.68 ? 38 ASP A CG 1 ATOM 132 O OD1 . ASP A 1 19 ? -36.145 -0.786 -4.050 1.00 264.63 ? 38 ASP A OD1 1 ATOM 133 O OD2 . ASP A 1 19 ? -35.083 -2.701 -3.850 1.00 251.82 ? 38 ASP A OD2 1 ATOM 134 N N . SER A 1 20 ? -35.640 0.599 0.463 1.00 184.15 ? 39 SER A N 1 ATOM 135 C CA . SER A 1 20 ? -35.775 0.900 1.888 1.00 179.51 ? 39 SER A CA 1 ATOM 136 C C . SER A 1 20 ? -35.414 -0.313 2.742 1.00 172.67 ? 39 SER A C 1 ATOM 137 O O . SER A 1 20 ? -35.764 -1.440 2.381 1.00 177.55 ? 39 SER A O 1 ATOM 138 C CB . SER A 1 20 ? -37.189 1.367 2.211 1.00 208.92 ? 39 SER A CB 1 ATOM 139 O OG . SER A 1 20 ? -38.133 0.323 2.039 1.00 244.18 ? 39 SER A OG 1 ATOM 140 N N . TYR A 1 21 ? -34.690 -0.085 3.849 1.00 162.99 ? 40 TYR A N 1 ATOM 141 C CA . TYR A 1 21 ? -34.276 -1.170 4.736 1.00 157.96 ? 40 TYR A CA 1 ATOM 142 C C . TYR A 1 21 ? -35.429 -1.746 5.562 1.00 167.39 ? 40 TYR A C 1 ATOM 143 O O . TYR A 1 21 ? -36.370 -1.010 5.868 1.00 174.82 ? 40 TYR A O 1 ATOM 144 C CB . TYR A 1 21 ? -33.091 -0.768 5.633 1.00 146.29 ? 40 TYR A CB 1 ATOM 145 C CG . TYR A 1 21 ? -33.312 0.464 6.480 1.00 146.78 ? 40 TYR A CG 1 ATOM 146 C CD1 . TYR A 1 21 ? -34.020 0.395 7.677 1.00 151.85 ? 40 TYR A CD1 1 ATOM 147 C CD2 . TYR A 1 21 ? -32.731 1.679 6.138 1.00 143.10 ? 40 TYR A CD2 1 ATOM 148 C CE1 . TYR A 1 21 ? -34.206 1.523 8.473 1.00 153.54 ? 40 TYR A CE1 1 ATOM 149 C CE2 . TYR A 1 21 ? -32.892 2.809 6.936 1.00 144.71 ? 40 TYR A CE2 1 ATOM 150 C CZ . TYR A 1 21 ? -33.635 2.728 8.101 1.00 149.99 ? 40 TYR A CZ 1 ATOM 151 O OH . TYR A 1 21 ? -33.803 3.843 8.885 1.00 153.38 ? 40 TYR A OH 1 ATOM 152 N N . PRO A 1 22 ? -35.359 -3.052 5.933 1.00 168.48 ? 41 PRO A N 1 ATOM 153 C CA . PRO A 1 22 ? -36.422 -3.648 6.744 1.00 178.97 ? 41 PRO A CA 1 ATOM 154 C C . PRO A 1 22 ? -36.324 -3.199 8.203 1.00 176.59 ? 41 PRO A C 1 ATOM 155 O O . PRO A 1 22 ? -35.262 -2.747 8.640 1.00 165.88 ? 41 PRO A O 1 ATOM 156 C CB . PRO A 1 22 ? -36.170 -5.151 6.605 1.00 180.98 ? 41 PRO A CB 1 ATOM 157 C CG . PRO A 1 22 ? -34.711 -5.261 6.375 1.00 168.28 ? 41 PRO A CG 1 ATOM 158 C CD . PRO A 1 22 ? -34.358 -4.069 5.540 1.00 161.98 ? 41 PRO A CD 1 ATOM 159 N N . SER A 1 23 ? -37.430 -3.327 8.950 1.00 190.00 ? 42 SER A N 1 ATOM 160 C CA . SER A 1 23 ? -37.468 -2.985 10.369 1.00 190.62 ? 42 SER A CA 1 ATOM 161 C C . SER A 1 23 ? -36.930 -4.162 11.185 1.00 187.92 ? 42 SER A C 1 ATOM 162 O O . SER A 1 23 ? -36.830 -5.276 10.660 1.00 193.41 ? 42 SER A O 1 ATOM 163 C CB . SER A 1 23 ? -38.887 -2.628 10.803 1.00 243.27 ? 42 SER A CB 1 ATOM 164 O OG . SER A 1 23 ? -39.771 -3.728 10.667 1.00 257.20 ? 42 SER A OG 1 ATOM 165 N N . ASP A 1 24 ? -36.579 -3.912 12.460 1.00 187.04 ? 43 ASP A N 1 ATOM 166 C CA . ASP A 1 24 ? -36.039 -4.907 13.389 1.00 188.53 ? 43 ASP A CA 1 ATOM 167 C C . ASP A 1 24 ? -34.867 -5.713 12.788 1.00 179.60 ? 43 ASP A C 1 ATOM 168 O O . ASP A 1 24 ? -34.862 -6.948 12.809 1.00 185.83 ? 43 ASP A O 1 ATOM 169 C CB . ASP A 1 24 ? -37.155 -5.799 13.975 1.00 242.53 ? 43 ASP A CB 1 ATOM 170 C CG . ASP A 1 24 ? -36.681 -6.799 15.013 1.00 249.19 ? 43 ASP A CG 1 ATOM 171 O OD1 . ASP A 1 24 ? -35.786 -6.447 15.814 1.00 232.61 ? 43 ASP A OD1 1 ATOM 172 O OD2 . ASP A 1 24 ? -37.161 -7.950 14.986 1.00 263.43 ? 43 ASP A OD2 1 ATOM 173 N N . SER A 1 25 ? -33.891 -5.001 12.215 1.00 166.64 ? 44 SER A N 1 ATOM 174 C CA . SER A 1 25 ? -32.713 -5.632 11.628 1.00 158.49 ? 44 SER A CA 1 ATOM 175 C C . SER A 1 25 ? -31.444 -5.108 12.287 1.00 148.72 ? 44 SER A C 1 ATOM 176 O O . SER A 1 25 ? -31.375 -3.930 12.643 1.00 145.21 ? 44 SER A O 1 ATOM 177 C CB . SER A 1 25 ? -32.675 -5.434 10.114 1.00 154.31 ? 44 SER A CB 1 ATOM 178 O OG . SER A 1 25 ? -32.369 -4.100 9.742 1.00 147.19 ? 44 SER A OG 1 ATOM 179 N N . GLU A 1 26 ? -30.458 -5.994 12.481 1.00 145.98 ? 45 GLU A N 1 ATOM 180 C CA . GLU A 1 26 ? -29.177 -5.650 13.089 1.00 138.42 ? 45 GLU A CA 1 ATOM 181 C C . GLU A 1 26 ? -28.067 -6.459 12.444 1.00 133.49 ? 45 GLU A C 1 ATOM 182 O O . GLU A 1 26 ? -28.039 -7.687 12.560 1.00 139.97 ? 45 GLU A O 1 ATOM 183 C CB . GLU A 1 26 ? -29.210 -5.846 14.610 1.00 145.35 ? 45 GLU A CB 1 ATOM 184 C CG . GLU A 1 26 ? -27.995 -5.272 15.321 1.00 139.27 ? 45 GLU A CG 1 ATOM 185 C CD . GLU A 1 26 ? -27.993 -5.401 16.832 1.00 147.74 ? 45 GLU A CD 1 ATOM 186 O OE1 . GLU A 1 26 ? -29.052 -5.728 17.415 1.00 158.34 ? 45 GLU A OE1 1 ATOM 187 O OE2 . GLU A 1 26 ? -26.924 -5.163 17.439 1.00 145.06 ? 45 GLU A OE2 1 ATOM 188 N N . VAL A 1 27 ? -27.175 -5.766 11.726 1.00 123.57 ? 46 VAL A N 1 ATOM 189 C CA . VAL A 1 27 ? -26.065 -6.398 11.017 1.00 119.02 ? 46 VAL A CA 1 ATOM 190 C C . VAL A 1 27 ? -24.745 -5.779 11.460 1.00 111.67 ? 46 VAL A C 1 ATOM 191 O O . VAL A 1 27 ? -24.631 -4.554 11.521 1.00 106.76 ? 46 VAL A O 1 ATOM 192 C CB . VAL A 1 27 ? -26.231 -6.337 9.468 1.00 116.38 ? 46 VAL A CB 1 ATOM 193 C CG1 . VAL A 1 27 ? -25.200 -7.220 8.765 1.00 114.62 ? 46 VAL A CG1 1 ATOM 194 C CG2 . VAL A 1 27 ? -27.645 -6.722 9.032 1.00 124.73 ? 46 VAL A CG2 1 ATOM 195 N N . THR A 1 28 ? -23.749 -6.631 11.749 1.00 112.52 ? 47 THR A N 1 ATOM 196 C CA . THR A 1 28 ? -22.408 -6.201 12.128 1.00 107.30 ? 47 THR A CA 1 ATOM 197 C C . THR A 1 28 ? -21.389 -6.673 11.099 1.00 103.68 ? 47 THR A C 1 ATOM 198 O O . THR A 1 28 ? -21.405 -7.840 10.701 1.00 108.62 ? 47 THR A O 1 ATOM 199 C CB . THR A 1 28 ? -22.046 -6.657 13.555 1.00 113.57 ? 47 THR A CB 1 ATOM 200 O OG1 . THR A 1 28 ? -22.965 -6.075 14.479 1.00 117.54 ? 47 THR A OG1 1 ATOM 201 C CG2 . THR A 1 28 ? -20.612 -6.280 13.955 1.00 109.89 ? 47 THR A CG2 1 ATOM 202 N N . TRP A 1 29 ? -20.495 -5.766 10.686 1.00 96.64 ? 48 TRP A N 1 ATOM 203 C CA . TRP A 1 29 ? -19.399 -6.080 9.782 1.00 94.00 ? 48 TRP A CA 1 ATOM 204 C C . TRP A 1 29 ? -18.095 -5.831 10.513 1.00 92.86 ? 48 TRP A C 1 ATOM 205 O O . TRP A 1 29 ? -17.852 -4.717 10.985 1.00 89.73 ? 48 TRP A O 1 ATOM 206 C CB . TRP A 1 29 ? -19.445 -5.229 8.511 1.00 88.72 ? 48 TRP A CB 1 ATOM 207 C CG . TRP A 1 29 ? -20.645 -5.464 7.652 1.00 91.14 ? 48 TRP A CG 1 ATOM 208 C CD1 . TRP A 1 29 ? -20.787 -6.407 6.680 1.00 94.62 ? 48 TRP A CD1 1 ATOM 209 C CD2 . TRP A 1 29 ? -21.854 -4.700 7.652 1.00 91.54 ? 48 TRP A CD2 1 ATOM 210 N NE1 . TRP A 1 29 ? -22.019 -6.291 6.083 1.00 97.50 ? 48 TRP A NE1 1 ATOM 211 C CE2 . TRP A 1 29 ? -22.698 -5.251 6.662 1.00 95.79 ? 48 TRP A CE2 1 ATOM 212 C CE3 . TRP A 1 29 ? -22.311 -3.599 8.396 1.00 90.40 ? 48 TRP A CE3 1 ATOM 213 C CZ2 . TRP A 1 29 ? -23.968 -4.730 6.386 1.00 98.69 ? 48 TRP A CZ2 1 ATOM 214 C CZ3 . TRP A 1 29 ? -23.573 -3.091 8.130 1.00 93.20 ? 48 TRP A CZ3 1 ATOM 215 C CH2 . TRP A 1 29 ? -24.387 -3.654 7.137 1.00 97.16 ? 48 TRP A CH2 1 ATOM 216 N N . ASN A 1 30 ? -17.264 -6.870 10.623 1.00 96.96 ? 49 ASN A N 1 ATOM 217 C CA . ASN A 1 30 ? -15.958 -6.764 11.256 1.00 97.69 ? 49 ASN A CA 1 ATOM 218 C C . ASN A 1 30 ? -14.896 -6.686 10.184 1.00 94.50 ? 49 ASN A C 1 ATOM 219 O O . ASN A 1 30 ? -14.809 -7.571 9.329 1.00 96.66 ? 49 ASN A O 1 ATOM 220 C CB . ASN A 1 30 ? -15.699 -7.925 12.199 1.00 106.84 ? 49 ASN A CB 1 ATOM 221 C CG . ASN A 1 30 ? -16.273 -7.724 13.562 1.00 111.71 ? 49 ASN A CG 1 ATOM 222 O OD1 . ASN A 1 30 ? -17.155 -6.875 13.804 1.00 108.34 ? 49 ASN A OD1 1 ATOM 223 N ND2 . ASN A 1 30 ? -15.782 -8.473 14.505 1.00 121.26 ? 49 ASN A ND2 1 ATOM 224 N N . ILE A 1 31 ? -14.116 -5.604 10.204 1.00 90.38 ? 50 ILE A N 1 ATOM 225 C CA . ILE A 1 31 ? -13.059 -5.385 9.226 1.00 88.51 ? 50 ILE A CA 1 ATOM 226 C C . ILE A 1 31 ? -11.695 -5.487 9.886 1.00 92.15 ? 50 ILE A C 1 ATOM 227 O O . ILE A 1 31 ? -11.370 -4.683 10.762 1.00 92.30 ? 50 ILE A O 1 ATOM 228 C CB . ILE A 1 31 ? -13.227 -4.052 8.446 1.00 82.95 ? 50 ILE A CB 1 ATOM 229 C CG1 . ILE A 1 31 ? -14.654 -3.892 7.878 1.00 80.94 ? 50 ILE A CG1 1 ATOM 230 C CG2 . ILE A 1 31 ? -12.171 -3.946 7.341 1.00 82.93 ? 50 ILE A CG2 1 ATOM 231 C CD1 . ILE A 1 31 ? -15.013 -2.482 7.480 1.00 77.84 ? 50 ILE A CD1 1 ATOM 232 N N . THR A 1 32 ? -10.896 -6.468 9.450 1.00 96.62 ? 51 THR A N 1 ATOM 233 C CA . THR A 1 32 ? -9.536 -6.656 9.938 1.00 101.86 ? 51 THR A CA 1 ATOM 234 C C . THR A 1 32 ? -8.564 -6.560 8.776 1.00 101.66 ? 51 THR A C 1 ATOM 235 O O . THR A 1 32 ? -8.765 -7.186 7.732 1.00 102.07 ? 51 THR A O 1 ATOM 236 C CB . THR A 1 32 ? -9.376 -7.974 10.715 1.00 110.90 ? 51 THR A CB 1 ATOM 237 O OG1 . THR A 1 32 ? -10.341 -8.026 11.763 1.00 112.57 ? 51 THR A OG1 1 ATOM 238 C CG2 . THR A 1 32 ? -7.974 -8.136 11.314 1.00 117.97 ? 51 THR A CG2 1 ATOM 239 N N . VAL A 1 33 ? -7.511 -5.771 8.969 1.00 102.51 ? 52 VAL A N 1 ATOM 240 C CA . VAL A 1 33 ? -6.434 -5.616 7.999 1.00 104.57 ? 52 VAL A CA 1 ATOM 241 C C . VAL A 1 33 ? -5.126 -6.108 8.633 1.00 113.12 ? 52 VAL A C 1 ATOM 242 O O . VAL A 1 33 ? -5.069 -6.216 9.863 1.00 116.47 ? 52 VAL A O 1 ATOM 243 C CB . VAL A 1 33 ? -6.315 -4.186 7.402 1.00 100.16 ? 52 VAL A CB 1 ATOM 244 C CG1 . VAL A 1 33 ? -7.510 -3.850 6.526 1.00 93.87 ? 52 VAL A CG1 1 ATOM 245 C CG2 . VAL A 1 33 ? -6.093 -3.127 8.473 1.00 100.00 ? 52 VAL A CG2 1 ATOM 246 N N . PRO A 1 34 ? -4.076 -6.405 7.818 1.00 118.09 ? 53 PRO A N 1 ATOM 247 C CA . PRO A 1 34 ? -2.795 -6.847 8.377 1.00 127.82 ? 53 PRO A CA 1 ATOM 248 C C . PRO A 1 34 ? -2.133 -5.749 9.206 1.00 129.40 ? 53 PRO A C 1 ATOM 249 O O . PRO A 1 34 ? -2.537 -4.583 9.139 1.00 123.03 ? 53 PRO A O 1 ATOM 250 C CB . PRO A 1 34 ? -1.951 -7.163 7.136 1.00 131.97 ? 53 PRO A CB 1 ATOM 251 C CG . PRO A 1 34 ? -2.921 -7.392 6.058 1.00 126.09 ? 53 PRO A CG 1 ATOM 252 C CD . PRO A 1 34 ? -4.055 -6.475 6.342 1.00 116.60 ? 53 PRO A CD 1 ATOM 253 N N . ASP A 1 35 ? -1.108 -6.129 9.981 1.00 139.54 ? 54 ASP A N 1 ATOM 254 C CA . ASP A 1 35 ? -0.349 -5.196 10.805 1.00 144.06 ? 54 ASP A CA 1 ATOM 255 C C . ASP A 1 35 ? 0.372 -4.198 9.912 1.00 143.51 ? 54 ASP A C 1 ATOM 256 O O . ASP A 1 35 ? 0.813 -4.551 8.815 1.00 144.95 ? 54 ASP A O 1 ATOM 257 C CB . ASP A 1 35 ? 0.636 -5.946 11.714 1.00 157.19 ? 54 ASP A CB 1 ATOM 258 C CG . ASP A 1 35 ? -0.019 -6.886 12.713 1.00 160.60 ? 54 ASP A CG 1 ATOM 259 O OD1 . ASP A 1 35 ? -1.220 -6.694 13.017 1.00 152.62 ? 54 ASP A OD1 1 ATOM 260 O OD2 . ASP A 1 35 ? 0.673 -7.801 13.206 1.00 172.82 ? 54 ASP A OD2 1 ATOM 261 N N . GLY A 1 36 ? 0.435 -2.941 10.356 1.00 142.59 ? 55 GLY A N 1 ATOM 262 C CA . GLY A 1 36 ? 1.060 -1.863 9.594 1.00 143.67 ? 55 GLY A CA 1 ATOM 263 C C . GLY A 1 36 ? 0.035 -1.120 8.738 1.00 133.73 ? 55 GLY A C 1 ATOM 264 O O . GLY A 1 36 ? 0.410 -0.241 7.961 1.00 135.10 ? 55 GLY A O 1 ATOM 265 N N . PHE A 1 37 ? -1.252 -1.466 8.885 1.00 125.22 ? 56 PHE A N 1 ATOM 266 C CA . PHE A 1 37 ? -2.331 -0.825 8.146 1.00 116.88 ? 56 PHE A CA 1 ATOM 267 C C . PHE A 1 37 ? -3.428 -0.325 9.064 1.00 111.69 ? 56 PHE A C 1 ATOM 268 O O . PHE A 1 37 ? -3.622 -0.862 10.155 1.00 113.03 ? 56 PHE A O 1 ATOM 269 C CB . PHE A 1 37 ? -2.947 -1.793 7.131 1.00 112.63 ? 56 PHE A CB 1 ATOM 270 C CG . PHE A 1 37 ? -2.035 -2.243 6.023 1.00 117.91 ? 56 PHE A CG 1 ATOM 271 C CD1 . PHE A 1 37 ? -1.892 -1.484 4.869 1.00 118.49 ? 56 PHE A CD1 1 ATOM 272 C CD2 . PHE A 1 37 ? -1.351 -3.448 6.113 1.00 123.83 ? 56 PHE A CD2 1 ATOM 273 C CE1 . PHE A 1 37 ? -1.059 -1.910 3.834 1.00 124.76 ? 56 PHE A CE1 1 ATOM 274 C CE2 . PHE A 1 37 ? -0.525 -3.878 5.074 1.00 129.90 ? 56 PHE A CE2 1 ATOM 275 C CZ . PHE A 1 37 ? -0.386 -3.108 3.940 1.00 130.22 ? 56 PHE A CZ 1 ATOM 276 N N . ARG A 1 38 ? -4.166 0.689 8.596 1.00 107.14 ? 57 ARG A N 1 ATOM 277 C CA . ARG A 1 38 ? -5.333 1.251 9.269 1.00 102.64 ? 57 ARG A CA 1 ATOM 278 C C . ARG A 1 38 ? -6.527 1.121 8.325 1.00 95.79 ? 57 ARG A C 1 ATOM 279 O O . ARG A 1 38 ? -6.355 0.710 7.175 1.00 95.40 ? 57 ARG A O 1 ATOM 280 C CB . ARG A 1 38 ? -5.102 2.715 9.670 1.00 106.31 ? 57 ARG A CB 1 ATOM 281 C CG . ARG A 1 38 ? -4.397 2.871 11.004 1.00 113.62 ? 57 ARG A CG 1 ATOM 282 C CD . ARG A 1 38 ? -4.163 4.332 11.316 1.00 119.18 ? 57 ARG A CD 1 ATOM 283 N NE . ARG A 1 38 ? -3.319 4.510 12.496 1.00 129.53 ? 57 ARG A NE 1 ATOM 284 C CZ . ARG A 1 38 ? -2.373 5.438 12.606 1.00 138.90 ? 57 ARG A CZ 1 ATOM 285 N NH1 . ARG A 1 38 ? -2.144 6.284 11.609 1.00 140.84 ? 57 ARG A NH1 1 ATOM 286 N NH2 . ARG A 1 38 ? -1.648 5.526 13.713 1.00 147.81 ? 57 ARG A NH2 1 ATOM 287 N N . ILE A 1 39 ? -7.731 1.452 8.809 1.00 92.00 ? 58 ILE A N 1 ATOM 288 C CA . ILE A 1 39 ? -8.948 1.370 8.002 1.00 86.92 ? 58 ILE A CA 1 ATOM 289 C C . ILE A 1 39 ? -9.484 2.761 7.703 1.00 87.13 ? 58 ILE A C 1 ATOM 290 O O . ILE A 1 39 ? -9.652 3.567 8.620 1.00 88.91 ? 58 ILE A O 1 ATOM 291 C CB . ILE A 1 39 ? -10.050 0.493 8.665 1.00 84.06 ? 58 ILE A CB 1 ATOM 292 C CG1 . ILE A 1 39 ? -9.483 -0.755 9.400 1.00 86.88 ? 58 ILE A CG1 1 ATOM 293 C CG2 . ILE A 1 39 ? -11.197 0.169 7.677 1.00 80.16 ? 58 ILE A CG2 1 ATOM 294 C CD1 . ILE A 1 39 ? -9.395 -1.975 8.636 1.00 86.91 ? 58 ILE A CD1 1 ATOM 295 N N . LYS A 1 40 ? -9.796 3.018 6.425 1.00 86.63 ? 59 LYS A N 1 ATOM 296 C CA . LYS A 1 40 ? -10.389 4.269 5.962 1.00 88.47 ? 59 LYS A CA 1 ATOM 297 C C . LYS A 1 40 ? -11.819 3.958 5.531 1.00 85.04 ? 59 LYS A C 1 ATOM 298 O O . LYS A 1 40 ? -12.017 3.071 4.702 1.00 83.44 ? 59 LYS A O 1 ATOM 299 C CB . LYS A 1 40 ? -9.588 4.838 4.786 1.00 93.67 ? 59 LYS A CB 1 ATOM 300 C CG . LYS A 1 40 ? -9.970 6.260 4.417 1.00 98.93 ? 59 LYS A CG 1 ATOM 301 C CD . LYS A 1 40 ? -9.032 6.884 3.399 1.00 106.67 ? 59 LYS A CD 1 ATOM 302 C CE . LYS A 1 40 ? -9.508 6.685 1.981 1.00 107.89 ? 59 LYS A CE 1 ATOM 303 N NZ . LYS A 1 40 ? -8.486 7.111 0.989 1.00 116.79 ? 59 LYS A NZ 1 ATOM 304 N N . LEU A 1 41 ? -12.808 4.668 6.102 1.00 85.01 ? 60 LEU A N 1 ATOM 305 C CA . LEU A 1 41 ? -14.222 4.451 5.793 1.00 82.99 ? 60 LEU A CA 1 ATOM 306 C C . LEU A 1 41 ? -14.936 5.741 5.400 1.00 87.51 ? 60 LEU A C 1 ATOM 307 O O . LEU A 1 41 ? -14.792 6.755 6.078 1.00 91.03 ? 60 LEU A O 1 ATOM 308 C CB . LEU A 1 41 ? -14.934 3.777 6.987 1.00 80.16 ? 60 LEU A CB 1 ATOM 309 C CG . LEU A 1 41 ? -16.451 3.552 6.872 1.00 79.66 ? 60 LEU A CG 1 ATOM 310 C CD1 . LEU A 1 41 ? -16.777 2.395 5.938 1.00 78.13 ? 60 LEU A CD1 1 ATOM 311 C CD2 . LEU A 1 41 ? -17.071 3.327 8.230 1.00 79.28 ? 60 LEU A CD2 1 ATOM 312 N N . TYR A 1 42 ? -15.735 5.685 4.325 1.00 88.74 ? 61 TYR A N 1 ATOM 313 C CA . TYR A 1 42 ? -16.528 6.820 3.852 1.00 94.75 ? 61 TYR A CA 1 ATOM 314 C C . TYR A 1 42 ? -17.854 6.366 3.243 1.00 95.37 ? 61 TYR A C 1 ATOM 315 O O . TYR A 1 42 ? -18.019 5.186 2.925 1.00 91.82 ? 61 TYR A O 1 ATOM 316 C CB . TYR A 1 42 ? -15.728 7.735 2.908 1.00 101.58 ? 61 TYR A CB 1 ATOM 317 C CG . TYR A 1 42 ? -15.220 7.041 1.665 1.00 102.21 ? 61 TYR A CG 1 ATOM 318 C CD1 . TYR A 1 42 ? -13.983 6.407 1.654 1.00 100.03 ? 61 TYR A CD1 1 ATOM 319 C CD2 . TYR A 1 42 ? -15.964 7.042 0.489 1.00 107.07 ? 61 TYR A CD2 1 ATOM 320 C CE1 . TYR A 1 42 ? -13.508 5.770 0.511 1.00 101.66 ? 61 TYR A CE1 1 ATOM 321 C CE2 . TYR A 1 42 ? -15.499 6.407 -0.661 1.00 109.10 ? 61 TYR A CE2 1 ATOM 322 C CZ . TYR A 1 42 ? -14.268 5.773 -0.645 1.00 106.39 ? 61 TYR A CZ 1 ATOM 323 O OH . TYR A 1 42 ? -13.793 5.148 -1.772 1.00 109.57 ? 61 TYR A OH 1 ATOM 324 N N . PHE A 1 43 ? -18.798 7.302 3.091 1.00 101.31 ? 62 PHE A N 1 ATOM 325 C CA . PHE A 1 43 ? -20.136 7.004 2.592 1.00 103.88 ? 62 PHE A CA 1 ATOM 326 C C . PHE A 1 43 ? -20.484 7.761 1.319 1.00 113.17 ? 62 PHE A C 1 ATOM 327 O O . PHE A 1 43 ? -20.135 8.934 1.179 1.00 119.74 ? 62 PHE A O 1 ATOM 328 C CB . PHE A 1 43 ? -21.178 7.282 3.691 1.00 104.41 ? 62 PHE A CB 1 ATOM 329 C CG . PHE A 1 43 ? -21.014 6.459 4.951 1.00 97.67 ? 62 PHE A CG 1 ATOM 330 C CD1 . PHE A 1 43 ? -20.036 6.777 5.890 1.00 95.62 ? 62 PHE A CD1 1 ATOM 331 C CD2 . PHE A 1 43 ? -21.842 5.373 5.204 1.00 95.18 ? 62 PHE A CD2 1 ATOM 332 C CE1 . PHE A 1 43 ? -19.887 6.019 7.054 1.00 91.02 ? 62 PHE A CE1 1 ATOM 333 C CE2 . PHE A 1 43 ? -21.693 4.617 6.372 1.00 90.79 ? 62 PHE A CE2 1 ATOM 334 C CZ . PHE A 1 43 ? -20.716 4.945 7.288 1.00 88.66 ? 62 PHE A CZ 1 ATOM 335 N N . MET A 1 44 ? -21.188 7.084 0.399 1.00 115.47 ? 63 MET A N 1 ATOM 336 C CA . MET A 1 44 ? -21.633 7.665 -0.869 1.00 126.20 ? 63 MET A CA 1 ATOM 337 C C . MET A 1 44 ? -23.113 8.016 -0.826 1.00 132.65 ? 63 MET A C 1 ATOM 338 O O . MET A 1 44 ? -23.570 8.863 -1.596 1.00 143.88 ? 63 MET A O 1 ATOM 339 C CB . MET A 1 44 ? -21.326 6.733 -2.053 1.00 127.38 ? 63 MET A CB 1 ATOM 340 C CG . MET A 1 44 ? -19.840 6.448 -2.252 1.00 123.20 ? 63 MET A CG 1 ATOM 341 S SD . MET A 1 44 ? -18.716 7.867 -2.084 1.00 128.05 ? 63 MET A SD 1 ATOM 342 C CE . MET A 1 44 ? -19.209 8.853 -3.488 1.00 143.38 ? 63 MET A CE 1 ATOM 343 N N . HIS A 1 45 ? -23.857 7.361 0.078 1.00 127.14 ? 64 HIS A N 1 ATOM 344 C CA . HIS A 1 45 ? -25.285 7.572 0.290 1.00 133.35 ? 64 HIS A CA 1 ATOM 345 C C . HIS A 1 45 ? -25.617 7.272 1.745 1.00 126.95 ? 64 HIS A C 1 ATOM 346 O O . HIS A 1 45 ? -25.121 6.290 2.295 1.00 118.03 ? 64 HIS A O 1 ATOM 347 C CB . HIS A 1 45 ? -26.112 6.683 -0.652 1.00 137.68 ? 64 HIS A CB 1 ATOM 348 C CG . HIS A 1 45 ? -27.568 7.025 -0.674 1.00 147.33 ? 64 HIS A CG 1 ATOM 349 N ND1 . HIS A 1 45 ? -28.480 6.350 0.117 1.00 145.52 ? 64 HIS A ND1 1 ATOM 350 C CD2 . HIS A 1 45 ? -28.223 7.967 -1.391 1.00 160.13 ? 64 HIS A CD2 1 ATOM 351 C CE1 . HIS A 1 45 ? -29.654 6.899 -0.144 1.00 156.23 ? 64 HIS A CE1 1 ATOM 352 N NE2 . HIS A 1 45 ? -29.550 7.875 -1.046 1.00 165.56 ? 64 HIS A NE2 1 ATOM 353 N N . PHE A 1 46 ? -26.422 8.134 2.379 1.00 132.90 ? 65 PHE A N 1 ATOM 354 C CA . PHE A 1 46 ? -26.822 7.961 3.773 1.00 129.13 ? 65 PHE A CA 1 ATOM 355 C C . PHE A 1 46 ? -28.218 8.528 4.008 1.00 138.90 ? 65 PHE A C 1 ATOM 356 O O . PHE A 1 46 ? -28.422 9.742 3.949 1.00 147.32 ? 65 PHE A O 1 ATOM 357 C CB . PHE A 1 46 ? -25.782 8.561 4.734 1.00 124.69 ? 65 PHE A CB 1 ATOM 358 C CG . PHE A 1 46 ? -25.921 8.050 6.146 1.00 119.99 ? 65 PHE A CG 1 ATOM 359 C CD1 . PHE A 1 46 ? -26.805 8.650 7.035 1.00 126.18 ? 65 PHE A CD1 1 ATOM 360 C CD2 . PHE A 1 46 ? -25.171 6.967 6.588 1.00 110.82 ? 65 PHE A CD2 1 ATOM 361 C CE1 . PHE A 1 46 ? -26.942 8.172 8.337 1.00 123.42 ? 65 PHE A CE1 1 ATOM 362 C CE2 . PHE A 1 46 ? -25.300 6.496 7.897 1.00 108.55 ? 65 PHE A CE2 1 ATOM 363 C CZ . PHE A 1 46 ? -26.194 7.094 8.758 1.00 114.78 ? 65 PHE A CZ 1 ATOM 364 N N . ASN A 1 47 ? -29.177 7.636 4.271 1.00 139.24 ? 66 ASN A N 1 ATOM 365 C CA . ASN A 1 47 ? -30.577 7.987 4.458 1.00 149.78 ? 66 ASN A CA 1 ATOM 366 C C . ASN A 1 47 ? -31.187 7.170 5.591 1.00 147.56 ? 66 ASN A C 1 ATOM 367 O O . ASN A 1 47 ? -31.679 6.063 5.365 1.00 147.14 ? 66 ASN A O 1 ATOM 368 C CB . ASN A 1 47 ? -31.329 7.766 3.140 1.00 157.66 ? 66 ASN A CB 1 ATOM 369 C CG . ASN A 1 47 ? -32.659 8.459 3.066 1.00 171.82 ? 66 ASN A CG 1 ATOM 370 O OD1 . ASN A 1 47 ? -33.714 7.822 3.005 1.00 176.99 ? 66 ASN A OD1 1 ATOM 371 N ND2 . ASN A 1 47 ? -32.639 9.784 3.039 1.00 179.52 ? 66 ASN A ND2 1 ATOM 372 N N . LEU A 1 48 ? -31.128 7.706 6.817 1.00 147.54 ? 67 LEU A N 1 ATOM 373 C CA . LEU A 1 48 ? -31.648 7.027 8.002 1.00 147.10 ? 67 LEU A CA 1 ATOM 374 C C . LEU A 1 48 ? -32.626 7.890 8.787 1.00 157.79 ? 67 LEU A C 1 ATOM 375 O O . LEU A 1 48 ? -32.750 9.088 8.529 1.00 164.86 ? 67 LEU A O 1 ATOM 376 C CB . LEU A 1 48 ? -30.478 6.607 8.916 1.00 137.08 ? 67 LEU A CB 1 ATOM 377 C CG . LEU A 1 48 ? -29.989 5.162 8.808 1.00 129.07 ? 67 LEU A CG 1 ATOM 378 C CD1 . LEU A 1 48 ? -29.119 4.959 7.574 1.00 123.31 ? 67 LEU A CD1 1 ATOM 379 C CD2 . LEU A 1 48 ? -29.197 4.771 10.040 1.00 123.60 ? 67 LEU A CD2 1 ATOM 380 N N . GLU A 1 49 ? -33.321 7.273 9.752 1.00 160.42 ? 68 GLU A N 1 ATOM 381 C CA . GLU A 1 49 ? -34.233 7.958 10.661 1.00 171.15 ? 68 GLU A CA 1 ATOM 382 C C . GLU A 1 49 ? -33.361 8.732 11.655 1.00 168.73 ? 68 GLU A C 1 ATOM 383 O O . GLU A 1 49 ? -32.314 8.227 12.070 1.00 159.05 ? 68 GLU A O 1 ATOM 384 C CB . GLU A 1 49 ? -35.086 6.920 11.400 1.00 174.82 ? 68 GLU A CB 1 ATOM 385 C CG . GLU A 1 49 ? -36.143 7.471 12.342 1.00 187.83 ? 68 GLU A CG 1 ATOM 386 C CD . GLU A 1 49 ? -36.774 6.352 13.144 1.00 191.94 ? 68 GLU A CD 1 ATOM 387 O OE1 . GLU A 1 49 ? -36.037 5.704 13.918 1.00 183.93 ? 68 GLU A OE1 1 ATOM 388 O OE2 . GLU A 1 49 ? -37.934 5.988 12.849 1.00 237.44 ? 68 GLU A OE2 1 ATOM 389 N N . SER A 1 50 ? -33.768 9.955 12.010 1.00 178.68 ? 69 SER A N 1 ATOM 390 C CA . SER A 1 50 ? -33.014 10.767 12.963 1.00 178.99 ? 69 SER A CA 1 ATOM 391 C C . SER A 1 50 ? -33.572 10.586 14.369 1.00 184.98 ? 69 SER A C 1 ATOM 392 O O . SER A 1 50 ? -34.790 10.477 14.533 1.00 194.39 ? 69 SER A O 1 ATOM 393 C CB . SER A 1 50 ? -33.039 12.239 12.566 1.00 188.48 ? 69 SER A CB 1 ATOM 394 O OG . SER A 1 50 ? -32.150 12.999 13.368 1.00 189.35 ? 69 SER A OG 1 ATOM 395 N N . SER A 1 51 ? -32.679 10.540 15.380 1.00 180.58 ? 70 SER A N 1 ATOM 396 C CA . SER A 1 51 ? -33.049 10.395 16.792 1.00 187.91 ? 70 SER A CA 1 ATOM 397 C C . SER A 1 51 ? -31.962 10.862 17.749 1.00 193.35 ? 70 SER A C 1 ATOM 398 O O . SER A 1 51 ? -30.787 10.886 17.384 1.00 177.69 ? 70 SER A O 1 ATOM 399 C CB . SER A 1 51 ? -33.458 8.960 17.117 1.00 185.42 ? 70 SER A CB 1 ATOM 400 O OG . SER A 1 51 ? -32.368 8.056 17.172 1.00 173.58 ? 70 SER A OG 1 ATOM 401 N N . TYR A 1 52 ? -32.365 11.210 18.985 1.00 265.78 ? 71 TYR A N 1 ATOM 402 C CA . TYR A 1 52 ? -31.484 11.656 20.063 1.00 273.54 ? 71 TYR A CA 1 ATOM 403 C C . TYR A 1 52 ? -30.384 10.631 20.292 1.00 235.49 ? 71 TYR A C 1 ATOM 404 O O . TYR A 1 52 ? -30.678 9.469 20.568 1.00 211.09 ? 71 TYR A O 1 ATOM 405 C CB . TYR A 1 52 ? -32.296 11.888 21.349 1.00 286.51 ? 71 TYR A CB 1 ATOM 406 C CG . TYR A 1 52 ? -31.461 12.094 22.595 1.00 288.00 ? 71 TYR A CG 1 ATOM 407 C CD1 . TYR A 1 52 ? -30.813 13.302 22.832 1.00 289.63 ? 71 TYR A CD1 1 ATOM 408 C CD2 . TYR A 1 52 ? -31.354 11.095 23.558 1.00 287.36 ? 71 TYR A CD2 1 ATOM 409 C CE1 . TYR A 1 52 ? -30.056 13.503 23.985 1.00 289.70 ? 71 TYR A CE1 1 ATOM 410 C CE2 . TYR A 1 52 ? -30.610 11.288 24.720 1.00 288.22 ? 71 TYR A CE2 1 ATOM 411 C CZ . TYR A 1 52 ? -29.960 12.494 24.928 1.00 289.07 ? 71 TYR A CZ 1 ATOM 412 O OH . TYR A 1 52 ? -29.215 12.687 26.066 1.00 289.12 ? 71 TYR A OH 1 ATOM 413 N N . LEU A 1 53 ? -29.119 11.055 20.119 1.00 202.56 ? 72 LEU A N 1 ATOM 414 C CA . LEU A 1 53 ? -27.927 10.211 20.266 1.00 174.06 ? 72 LEU A CA 1 ATOM 415 C C . LEU A 1 53 ? -27.982 8.976 19.354 1.00 162.84 ? 72 LEU A C 1 ATOM 416 O O . LEU A 1 53 ? -27.334 7.964 19.641 1.00 157.06 ? 72 LEU A O 1 ATOM 417 C CB . LEU A 1 53 ? -27.711 9.804 21.742 1.00 198.70 ? 72 LEU A CB 1 ATOM 418 C CG . LEU A 1 53 ? -27.426 10.916 22.752 1.00 261.62 ? 72 LEU A CG 1 ATOM 419 C CD1 . LEU A 1 53 ? -27.210 10.334 24.128 1.00 269.84 ? 72 LEU A CD1 1 ATOM 420 C CD2 . LEU A 1 53 ? -26.197 11.725 22.361 1.00 247.38 ? 72 LEU A CD2 1 ATOM 421 N N . CYS A 1 54 ? -28.767 9.074 18.251 1.00 161.58 ? 73 CYS A N 1 ATOM 422 C CA . CYS A 1 54 ? -29.020 8.015 17.271 1.00 153.62 ? 73 CYS A CA 1 ATOM 423 C C . CYS A 1 54 ? -29.469 6.733 17.987 1.00 155.08 ? 73 CYS A C 1 ATOM 424 O O . CYS A 1 54 ? -28.917 5.658 17.755 1.00 147.42 ? 73 CYS A O 1 ATOM 425 C CB . CYS A 1 54 ? -27.805 7.784 16.374 1.00 142.30 ? 73 CYS A CB 1 ATOM 426 S SG . CYS A 1 54 ? -27.320 9.223 15.387 1.00 143.37 ? 73 CYS A SG 1 ATOM 427 N N . GLU A 1 55 ? -30.444 6.871 18.899 1.00 166.52 ? 74 GLU A N 1 ATOM 428 C CA . GLU A 1 55 ? -30.945 5.759 19.706 1.00 171.53 ? 74 GLU A CA 1 ATOM 429 C C . GLU A 1 55 ? -31.844 4.771 18.962 1.00 170.74 ? 74 GLU A C 1 ATOM 430 O O . GLU A 1 55 ? -31.859 3.588 19.310 1.00 170.99 ? 74 GLU A O 1 ATOM 431 C CB . GLU A 1 55 ? -31.583 6.251 21.018 1.00 195.71 ? 74 GLU A CB 1 ATOM 432 C CG . GLU A 1 55 ? -32.798 7.153 20.859 1.00 256.59 ? 74 GLU A CG 1 ATOM 433 C CD . GLU A 1 55 ? -33.353 7.748 22.140 1.00 279.28 ? 74 GLU A CD 1 ATOM 434 O OE1 . GLU A 1 55 ? -32.686 7.649 23.196 1.00 281.89 ? 74 GLU A OE1 1 ATOM 435 O OE2 . GLU A 1 55 ? -34.457 8.335 22.081 1.00 287.08 ? 74 GLU A OE2 1 ATOM 436 N N . TYR A 1 56 ? -32.584 5.244 17.947 1.00 171.31 ? 75 TYR A N 1 ATOM 437 C CA . TYR A 1 56 ? -33.492 4.387 17.186 1.00 172.53 ? 75 TYR A CA 1 ATOM 438 C C . TYR A 1 56 ? -32.750 3.656 16.072 1.00 160.75 ? 75 TYR A C 1 ATOM 439 O O . TYR A 1 56 ? -32.305 2.531 16.290 1.00 157.39 ? 75 TYR A O 1 ATOM 440 C CB . TYR A 1 56 ? -34.715 5.171 16.671 1.00 181.21 ? 75 TYR A CB 1 ATOM 441 C CG . TYR A 1 56 ? -35.521 5.894 17.732 1.00 195.63 ? 75 TYR A CG 1 ATOM 442 C CD1 . TYR A 1 56 ? -35.521 5.462 19.056 1.00 248.02 ? 75 TYR A CD1 1 ATOM 443 C CD2 . TYR A 1 56 ? -36.303 6.998 17.408 1.00 253.42 ? 75 TYR A CD2 1 ATOM 444 C CE1 . TYR A 1 56 ? -36.236 6.142 20.039 1.00 280.79 ? 75 TYR A CE1 1 ATOM 445 C CE2 . TYR A 1 56 ? -37.025 7.685 18.382 1.00 283.38 ? 75 TYR A CE2 1 ATOM 446 C CZ . TYR A 1 56 ? -36.990 7.252 19.696 1.00 286.72 ? 75 TYR A CZ 1 ATOM 447 O OH . TYR A 1 56 ? -37.681 7.939 20.661 1.00 288.21 ? 75 TYR A OH 1 ATOM 448 N N . ASP A 1 57 ? -32.591 4.289 14.899 1.00 156.07 ? 76 ASP A N 1 ATOM 449 C CA . ASP A 1 57 ? -31.852 3.709 13.780 1.00 145.95 ? 76 ASP A CA 1 ATOM 450 C C . ASP A 1 57 ? -30.467 4.325 13.757 1.00 137.69 ? 76 ASP A C 1 ATOM 451 O O . ASP A 1 57 ? -30.337 5.524 14.018 1.00 140.37 ? 76 ASP A O 1 ATOM 452 C CB . ASP A 1 57 ? -32.589 3.928 12.447 1.00 147.98 ? 76 ASP A CB 1 ATOM 453 C CG . ASP A 1 57 ? -33.959 3.264 12.361 1.00 157.23 ? 76 ASP A CG 1 ATOM 454 O OD1 . ASP A 1 57 ? -34.361 2.592 13.333 1.00 161.70 ? 76 ASP A OD1 1 ATOM 455 O OD2 . ASP A 1 57 ? -34.645 3.450 11.339 1.00 160.96 ? 76 ASP A OD2 1 ATOM 456 N N . TYR A 1 58 ? -29.424 3.510 13.501 1.00 128.90 ? 77 TYR A N 1 ATOM 457 C CA . TYR A 1 58 ? -28.048 4.011 13.509 1.00 122.08 ? 77 TYR A CA 1 ATOM 458 C C . TYR A 1 58 ? -27.026 3.161 12.770 1.00 113.41 ? 77 TYR A C 1 ATOM 459 O O . TYR A 1 58 ? -27.238 1.969 12.548 1.00 112.53 ? 77 TYR A O 1 ATOM 460 C CB . TYR A 1 58 ? -27.557 4.230 14.959 1.00 124.96 ? 77 TYR A CB 1 ATOM 461 C CG . TYR A 1 58 ? -27.515 2.973 15.804 1.00 126.30 ? 77 TYR A CG 1 ATOM 462 C CD1 . TYR A 1 58 ? -26.420 2.113 15.757 1.00 120.24 ? 77 TYR A CD1 1 ATOM 463 C CD2 . TYR A 1 58 ? -28.549 2.664 16.681 1.00 135.72 ? 77 TYR A CD2 1 ATOM 464 C CE1 . TYR A 1 58 ? -26.374 0.957 16.534 1.00 123.21 ? 77 TYR A CE1 1 ATOM 465 C CE2 . TYR A 1 58 ? -28.496 1.531 17.491 1.00 138.97 ? 77 TYR A CE2 1 ATOM 466 C CZ . TYR A 1 58 ? -27.410 0.676 17.409 1.00 133.09 ? 77 TYR A CZ 1 ATOM 467 O OH . TYR A 1 58 ? -27.368 -0.460 18.180 1.00 138.64 ? 77 TYR A OH 1 ATOM 468 N N . VAL A 1 59 ? -25.875 3.785 12.469 1.00 108.20 ? 78 VAL A N 1 ATOM 469 C CA . VAL A 1 59 ? -24.680 3.155 11.923 1.00 100.93 ? 78 VAL A CA 1 ATOM 470 C C . VAL A 1 59 ? -23.590 3.479 12.949 1.00 100.23 ? 78 VAL A C 1 ATOM 471 O O . VAL A 1 59 ? -23.203 4.642 13.097 1.00 101.90 ? 78 VAL A O 1 ATOM 472 C CB . VAL A 1 59 ? -24.301 3.587 10.483 1.00 97.63 ? 78 VAL A CB 1 ATOM 473 C CG1 . VAL A 1 59 ? -22.934 3.026 10.091 1.00 91.19 ? 78 VAL A CG1 1 ATOM 474 C CG2 . VAL A 1 59 ? -25.362 3.147 9.479 1.00 99.32 ? 78 VAL A CG2 1 ATOM 475 N N . LYS A 1 60 ? -23.154 2.459 13.698 1.00 99.66 ? 79 LYS A N 1 ATOM 476 C CA . LYS A 1 60 ? -22.149 2.597 14.749 1.00 100.96 ? 79 LYS A CA 1 ATOM 477 C C . LYS A 1 60 ? -20.794 2.093 14.256 1.00 95.65 ? 79 LYS A C 1 ATOM 478 O O . LYS A 1 60 ? -20.693 0.949 13.816 1.00 93.46 ? 79 LYS A O 1 ATOM 479 C CB . LYS A 1 60 ? -22.606 1.830 16.005 1.00 107.18 ? 79 LYS A CB 1 ATOM 480 C CG . LYS A 1 60 ? -21.778 2.081 17.259 1.00 111.53 ? 79 LYS A CG 1 ATOM 481 C CD . LYS A 1 60 ? -22.317 1.262 18.422 1.00 119.75 ? 79 LYS A CD 1 ATOM 482 C CE . LYS A 1 60 ? -21.672 1.622 19.736 1.00 127.42 ? 79 LYS A CE 1 ATOM 483 N NZ . LYS A 1 60 ? -22.284 0.882 20.872 1.00 137.40 ? 79 LYS A NZ 1 ATOM 484 N N . VAL A 1 61 ? -19.759 2.952 14.324 1.00 94.86 ? 80 VAL A N 1 ATOM 485 C CA . VAL A 1 61 ? -18.389 2.624 13.910 1.00 91.14 ? 80 VAL A CA 1 ATOM 486 C C . VAL A 1 61 ? -17.510 2.593 15.157 1.00 95.62 ? 80 VAL A C 1 ATOM 487 O O . VAL A 1 61 ? -17.399 3.602 15.857 1.00 100.22 ? 80 VAL A O 1 ATOM 488 C CB . VAL A 1 61 ? -17.833 3.589 12.830 1.00 88.62 ? 80 VAL A CB 1 ATOM 489 C CG1 . VAL A 1 61 ? -16.438 3.163 12.383 1.00 85.75 ? 80 VAL A CG1 1 ATOM 490 C CG2 . VAL A 1 61 ? -18.773 3.683 11.630 1.00 86.18 ? 80 VAL A CG2 1 ATOM 491 N N . GLU A 1 62 ? -16.890 1.438 15.438 1.00 95.96 ? 81 GLU A N 1 ATOM 492 C CA . GLU A 1 62 ? -16.075 1.280 16.640 1.00 102.27 ? 81 GLU A CA 1 ATOM 493 C C . GLU A 1 62 ? -14.909 0.308 16.489 1.00 102.21 ? 81 GLU A C 1 ATOM 494 O O . GLU A 1 62 ? -14.824 -0.419 15.500 1.00 97.56 ? 81 GLU A O 1 ATOM 495 C CB . GLU A 1 62 ? -16.975 0.828 17.810 1.00 108.98 ? 81 GLU A CB 1 ATOM 496 C CG . GLU A 1 62 ? -17.525 -0.585 17.669 1.00 109.33 ? 81 GLU A CG 1 ATOM 497 C CD . GLU A 1 62 ? -18.689 -0.931 18.575 1.00 116.58 ? 81 GLU A CD 1 ATOM 498 O OE1 . GLU A 1 62 ? -18.699 -0.482 19.745 1.00 124.26 ? 81 GLU A OE1 1 ATOM 499 O OE2 . GLU A 1 62 ? -19.583 -1.680 18.120 1.00 115.70 ? 81 GLU A OE2 1 ATOM 500 N N . THR A 1 63 ? -14.036 0.275 17.509 1.00 108.97 ? 82 THR A N 1 ATOM 501 C CA . THR A 1 63 ? -12.933 -0.674 17.616 1.00 112.11 ? 82 THR A CA 1 ATOM 502 C C . THR A 1 63 ? -13.326 -1.653 18.732 1.00 120.56 ? 82 THR A C 1 ATOM 503 O O . THR A 1 63 ? -14.476 -1.646 19.179 1.00 122.37 ? 82 THR A O 1 ATOM 504 C CB . THR A 1 63 ? -11.582 0.027 17.881 1.00 115.77 ? 82 THR A CB 1 ATOM 505 O OG1 . THR A 1 63 ? -11.539 0.543 19.212 1.00 125.02 ? 82 THR A OG1 1 ATOM 506 C CG2 . THR A 1 63 ? -11.250 1.097 16.859 1.00 110.06 ? 82 THR A CG2 1 ATOM 507 N N . GLU A 1 64 ? -12.376 -2.467 19.196 1.00 127.37 ? 83 GLU A N 1 ATOM 508 C CA . GLU A 1 64 ? -12.584 -3.447 20.263 1.00 138.00 ? 83 GLU A CA 1 ATOM 509 C C . GLU A 1 64 ? -12.739 -2.817 21.654 1.00 147.64 ? 83 GLU A C 1 ATOM 510 O O . GLU A 1 64 ? -13.156 -3.507 22.586 1.00 157.53 ? 83 GLU A O 1 ATOM 511 C CB . GLU A 1 64 ? -11.466 -4.512 20.262 1.00 144.42 ? 83 GLU A CB 1 ATOM 512 C CG . GLU A 1 64 ? -10.047 -3.965 20.195 1.00 145.93 ? 83 GLU A CG 1 ATOM 513 C CD . GLU A 1 64 ? -9.593 -3.592 18.798 1.00 135.31 ? 83 GLU A CD 1 ATOM 514 O OE1 . GLU A 1 64 ? -9.256 -4.509 18.015 1.00 134.02 ? 83 GLU A OE1 1 ATOM 515 O OE2 . GLU A 1 64 ? -9.617 -2.384 18.471 1.00 129.64 ? 83 GLU A OE2 1 ATOM 516 N N . ASP A 1 65 ? -12.412 -1.519 21.798 1.00 146.35 ? 84 ASP A N 1 ATOM 517 C CA . ASP A 1 65 ? -12.464 -0.826 23.086 1.00 156.98 ? 84 ASP A CA 1 ATOM 518 C C . ASP A 1 65 ? -12.816 0.661 22.970 1.00 153.40 ? 84 ASP A C 1 ATOM 519 O O . ASP A 1 65 ? -12.717 1.388 23.962 1.00 162.84 ? 84 ASP A O 1 ATOM 520 C CB . ASP A 1 65 ? -11.091 -0.971 23.777 1.00 167.65 ? 84 ASP A CB 1 ATOM 521 C CG . ASP A 1 65 ? -9.900 -0.433 22.985 1.00 162.52 ? 84 ASP A CG 1 ATOM 522 O OD1 . ASP A 1 65 ? -10.117 0.166 21.900 1.00 151.56 ? 84 ASP A OD1 1 ATOM 523 O OD2 . ASP A 1 65 ? -8.756 -0.611 23.447 1.00 171.45 ? 84 ASP A OD2 1 ATOM 524 N N . GLN A 1 66 ? -13.181 1.124 21.764 1.00 141.80 ? 85 GLN A N 1 ATOM 525 C CA . GLN A 1 66 ? -13.433 2.541 21.528 1.00 139.46 ? 85 GLN A CA 1 ATOM 526 C C . GLN A 1 66 ? -14.474 2.780 20.439 1.00 129.22 ? 85 GLN A C 1 ATOM 527 O O . GLN A 1 66 ? -14.342 2.242 19.341 1.00 121.06 ? 85 GLN A O 1 ATOM 528 C CB . GLN A 1 66 ? -12.089 3.203 21.160 1.00 139.41 ? 85 GLN A CB 1 ATOM 529 C CG . GLN A 1 66 ? -12.124 4.682 20.794 1.00 138.41 ? 85 GLN A CG 1 ATOM 530 C CD . GLN A 1 66 ? -10.771 5.170 20.319 1.00 139.75 ? 85 GLN A CD 1 ATOM 531 O OE1 . GLN A 1 66 ? -9.718 4.596 20.631 1.00 144.45 ? 85 GLN A OE1 1 ATOM 532 N NE2 . GLN A 1 66 ? -10.765 6.258 19.565 1.00 137.43 ? 85 GLN A NE2 1 ATOM 533 N N . VAL A 1 67 ? -15.486 3.615 20.733 1.00 131.28 ? 86 VAL A N 1 ATOM 534 C CA . VAL A 1 67 ? -16.513 3.981 19.757 1.00 123.91 ? 86 VAL A CA 1 ATOM 535 C C . VAL A 1 67 ? -15.984 5.182 18.981 1.00 121.16 ? 86 VAL A C 1 ATOM 536 O O . VAL A 1 67 ? -15.731 6.238 19.568 1.00 128.10 ? 86 VAL A O 1 ATOM 537 C CB . VAL A 1 67 ? -17.909 4.239 20.380 1.00 128.97 ? 86 VAL A CB 1 ATOM 538 C CG1 . VAL A 1 67 ? -18.904 4.737 19.329 1.00 122.88 ? 86 VAL A CG1 1 ATOM 539 C CG2 . VAL A 1 67 ? -18.441 2.991 21.078 1.00 132.83 ? 86 VAL A CG2 1 ATOM 540 N N . LEU A 1 68 ? -15.791 5.004 17.671 1.00 112.73 ? 87 LEU A N 1 ATOM 541 C CA . LEU A 1 68 ? -15.250 6.042 16.799 1.00 111.14 ? 87 LEU A CA 1 ATOM 542 C C . LEU A 1 68 ? -16.300 7.053 16.371 1.00 111.87 ? 87 LEU A C 1 ATOM 543 O O . LEU A 1 68 ? -16.037 8.256 16.429 1.00 116.96 ? 87 LEU A O 1 ATOM 544 C CB . LEU A 1 68 ? -14.542 5.426 15.576 1.00 103.72 ? 87 LEU A CB 1 ATOM 545 C CG . LEU A 1 68 ? -13.430 4.405 15.862 1.00 104.06 ? 87 LEU A CG 1 ATOM 546 C CD1 . LEU A 1 68 ? -12.935 3.769 14.582 1.00 97.71 ? 87 LEU A CD1 1 ATOM 547 C CD2 . LEU A 1 68 ? -12.267 5.036 16.616 1.00 111.45 ? 87 LEU A CD2 1 ATOM 548 N N . ALA A 1 69 ? -17.486 6.570 15.944 1.00 108.11 ? 88 ALA A N 1 ATOM 549 C CA . ALA A 1 69 ? -18.583 7.415 15.470 1.00 109.78 ? 88 ALA A CA 1 ATOM 550 C C . ALA A 1 69 ? -19.935 6.701 15.469 1.00 108.70 ? 88 ALA A C 1 ATOM 551 O O . ALA A 1 69 ? -19.991 5.474 15.380 1.00 104.61 ? 88 ALA A O 1 ATOM 552 C CB . ALA A 1 69 ? -18.273 7.915 14.064 1.00 106.12 ? 88 ALA A CB 1 ATOM 553 N N . THR A 1 70 ? -21.023 7.486 15.549 1.00 114.04 ? 89 THR A N 1 ATOM 554 C CA . THR A 1 70 ? -22.407 7.015 15.477 1.00 115.00 ? 89 THR A CA 1 ATOM 555 C C . THR A 1 70 ? -23.154 7.953 14.538 1.00 117.34 ? 89 THR A C 1 ATOM 556 O O . THR A 1 70 ? -23.153 9.170 14.748 1.00 123.82 ? 89 THR A O 1 ATOM 557 C CB . THR A 1 70 ? -23.063 6.915 16.862 1.00 122.84 ? 89 THR A CB 1 ATOM 558 O OG1 . THR A 1 70 ? -22.204 6.194 17.746 1.00 123.11 ? 89 THR A OG1 1 ATOM 559 C CG2 . THR A 1 70 ? -24.431 6.235 16.809 1.00 124.45 ? 89 THR A CG2 1 ATOM 560 N N . PHE A 1 71 ? -23.774 7.390 13.497 1.00 113.65 ? 90 PHE A N 1 ATOM 561 C CA . PHE A 1 71 ? -24.491 8.181 12.505 1.00 117.15 ? 90 PHE A CA 1 ATOM 562 C C . PHE A 1 71 ? -25.951 7.816 12.372 1.00 121.15 ? 90 PHE A C 1 ATOM 563 O O . PHE A 1 71 ? -26.320 6.657 12.547 1.00 118.55 ? 90 PHE A O 1 ATOM 564 C CB . PHE A 1 71 ? -23.817 8.066 11.131 1.00 111.51 ? 90 PHE A CB 1 ATOM 565 C CG . PHE A 1 71 ? -22.364 8.462 11.082 1.00 108.97 ? 90 PHE A CG 1 ATOM 566 C CD1 . PHE A 1 71 ? -21.980 9.786 11.263 1.00 115.35 ? 90 PHE A CD1 1 ATOM 567 C CD2 . PHE A 1 71 ? -21.379 7.517 10.822 1.00 101.45 ? 90 PHE A CD2 1 ATOM 568 C CE1 . PHE A 1 71 ? -20.634 10.152 11.219 1.00 114.52 ? 90 PHE A CE1 1 ATOM 569 C CE2 . PHE A 1 71 ? -20.033 7.887 10.764 1.00 100.47 ? 90 PHE A CE2 1 ATOM 570 C CZ . PHE A 1 71 ? -19.671 9.204 10.951 1.00 107.09 ? 90 PHE A CZ 1 ATOM 571 N N . CYS A 1 72 ? -26.776 8.818 12.035 1.00 129.05 ? 91 CYS A N 1 ATOM 572 C CA . CYS A 1 72 ? -28.208 8.706 11.753 1.00 134.86 ? 91 CYS A CA 1 ATOM 573 C C . CYS A 1 72 ? -28.692 9.965 11.029 1.00 143.43 ? 91 CYS A C 1 ATOM 574 O O . CYS A 1 72 ? -27.906 10.897 10.835 1.00 144.70 ? 91 CYS A O 1 ATOM 575 C CB . CYS A 1 72 ? -29.031 8.398 13.005 1.00 140.49 ? 91 CYS A CB 1 ATOM 576 S SG . CYS A 1 72 ? -28.969 9.676 14.286 1.00 149.46 ? 91 CYS A SG 1 ATOM 577 N N . GLY A 1 73 ? -29.956 9.975 10.581 1.00 150.51 ? 92 GLY A N 1 ATOM 578 C CA . GLY A 1 73 ? -30.528 11.112 9.862 1.00 160.92 ? 92 GLY A CA 1 ATOM 579 C C . GLY A 1 73 ? -30.326 10.995 8.351 1.00 159.38 ? 92 GLY A C 1 ATOM 580 O O . GLY A 1 73 ? -29.721 10.031 7.872 1.00 149.55 ? 92 GLY A O 1 ATOM 581 N N . ARG A 1 74 ? -30.845 11.979 7.604 1.00 170.58 ? 93 ARG A N 1 ATOM 582 C CA . ARG A 1 74 ? -30.743 12.016 6.147 1.00 172.65 ? 93 ARG A CA 1 ATOM 583 C C . ARG A 1 74 ? -29.803 13.125 5.683 1.00 176.49 ? 93 ARG A C 1 ATOM 584 O O . ARG A 1 74 ? -29.879 14.246 6.190 1.00 185.52 ? 93 ARG A O 1 ATOM 585 C CB . ARG A 1 74 ? -32.134 12.122 5.488 1.00 184.66 ? 93 ARG A CB 1 ATOM 586 C CG . ARG A 1 74 ? -32.891 13.424 5.760 1.00 200.20 ? 93 ARG A CG 1 ATOM 587 C CD . ARG A 1 74 ? -34.265 13.435 5.125 1.00 234.22 ? 93 ARG A CD 1 ATOM 588 N NE . ARG A 1 74 ? -35.240 12.677 5.914 1.00 242.57 ? 93 ARG A NE 1 ATOM 589 C CZ . ARG A 1 74 ? -36.043 13.207 6.832 1.00 262.29 ? 93 ARG A CZ 1 ATOM 590 N NH1 . ARG A 1 74 ? -36.002 14.509 7.090 1.00 272.51 ? 93 ARG A NH1 1 ATOM 591 N NH2 . ARG A 1 74 ? -36.895 12.440 7.499 1.00 263.28 ? 93 ARG A NH2 1 ATOM 592 N N . GLU A 1 75 ? -28.901 12.802 4.739 1.00 170.97 ? 94 GLU A N 1 ATOM 593 C CA . GLU A 1 75 ? -27.920 13.746 4.185 1.00 175.21 ? 94 GLU A CA 1 ATOM 594 C C . GLU A 1 75 ? -28.550 15.009 3.586 1.00 192.71 ? 94 GLU A C 1 ATOM 595 O O . GLU A 1 75 ? -27.916 16.067 3.596 1.00 199.82 ? 94 GLU A O 1 ATOM 596 C CB . GLU A 1 75 ? -26.960 13.057 3.198 1.00 167.59 ? 94 GLU A CB 1 ATOM 597 C CG . GLU A 1 75 ? -27.631 12.322 2.045 1.00 169.55 ? 94 GLU A CG 1 ATOM 598 C CD . GLU A 1 75 ? -26.775 11.276 1.354 1.00 159.96 ? 94 GLU A CD 1 ATOM 599 O OE1 . GLU A 1 75 ? -25.535 11.447 1.312 1.00 155.80 ? 94 GLU A OE1 1 ATOM 600 O OE2 . GLU A 1 75 ? -27.349 10.291 0.836 1.00 157.71 ? 94 GLU A OE2 1 ATOM 601 N N . THR A 1 76 ? -29.809 14.896 3.106 1.00 201.46 ? 95 THR A N 1 ATOM 602 C CA . THR A 1 76 ? -30.601 15.989 2.537 1.00 235.91 ? 95 THR A CA 1 ATOM 603 C C . THR A 1 76 ? -30.727 17.096 3.586 1.00 261.19 ? 95 THR A C 1 ATOM 604 O O . THR A 1 76 ? -30.128 18.160 3.416 1.00 276.00 ? 95 THR A O 1 ATOM 605 C CB . THR A 1 76 ? -31.985 15.481 2.086 1.00 264.36 ? 95 THR A CB 1 ATOM 606 O OG1 . THR A 1 76 ? -31.886 14.140 1.602 1.00 236.99 ? 95 THR A OG1 1 ATOM 607 C CG2 . THR A 1 76 ? -32.621 16.375 1.034 1.00 281.37 ? 95 THR A CG2 1 ATOM 608 N N . THR A 1 77 ? -31.452 16.818 4.691 1.00 259.14 ? 96 THR A N 1 ATOM 609 C CA . THR A 1 77 ? -31.636 17.751 5.804 1.00 286.38 ? 96 THR A CA 1 ATOM 610 C C . THR A 1 77 ? -30.279 18.004 6.459 1.00 264.32 ? 96 THR A C 1 ATOM 611 O O . THR A 1 77 ? -29.513 17.060 6.667 1.00 212.34 ? 96 THR A O 1 ATOM 612 C CB . THR A 1 77 ? -32.658 17.203 6.821 1.00 287.36 ? 96 THR A CB 1 ATOM 613 O OG1 . THR A 1 77 ? -33.807 16.704 6.135 1.00 288.09 ? 96 THR A OG1 1 ATOM 614 C CG2 . THR A 1 77 ? -33.086 18.249 7.849 1.00 300.00 ? 96 THR A CG2 1 ATOM 615 N N . ASP A 1 78 ? -29.969 19.277 6.738 1.00 300.00 ? 97 ASP A N 1 ATOM 616 C CA . ASP A 1 78 ? -28.709 19.636 7.375 1.00 299.82 ? 97 ASP A CA 1 ATOM 617 C C . ASP A 1 78 ? -28.879 20.009 8.844 1.00 299.86 ? 97 ASP A C 1 ATOM 618 O O . ASP A 1 78 ? -30.011 20.190 9.303 1.00 300.00 ? 97 ASP A O 1 ATOM 619 C CB . ASP A 1 78 ? -27.912 20.666 6.562 1.00 300.00 ? 97 ASP A CB 1 ATOM 620 C CG . ASP A 1 78 ? -26.410 20.430 6.595 1.00 299.79 ? 97 ASP A CG 1 ATOM 621 O OD1 . ASP A 1 78 ? -25.990 19.268 6.820 1.00 218.48 ? 97 ASP A OD1 1 ATOM 622 O OD2 . ASP A 1 78 ? -25.653 21.406 6.410 1.00 300.00 ? 97 ASP A OD2 1 ATOM 623 N N . THR A 1 79 ? -27.748 20.112 9.580 1.00 298.75 ? 98 THR A N 1 ATOM 624 C CA . THR A 1 79 ? -27.650 20.296 11.035 1.00 298.00 ? 98 THR A CA 1 ATOM 625 C C . THR A 1 79 ? -28.048 18.910 11.560 1.00 295.62 ? 98 THR A C 1 ATOM 626 O O . THR A 1 79 ? -28.947 18.759 12.393 1.00 296.56 ? 98 THR A O 1 ATOM 627 C CB . THR A 1 79 ? -28.493 21.488 11.561 1.00 298.64 ? 98 THR A CB 1 ATOM 628 O OG1 . THR A 1 79 ? -28.376 22.598 10.671 1.00 299.68 ? 98 THR A OG1 1 ATOM 629 C CG2 . THR A 1 79 ? -28.097 21.910 12.966 1.00 297.85 ? 98 THR A CG2 1 ATOM 630 N N . GLU A 1 80 ? -27.401 17.886 10.977 1.00 210.38 ? 99 GLU A N 1 ATOM 631 C CA . GLU A 1 80 ? -27.671 16.480 11.236 1.00 192.91 ? 99 GLU A CA 1 ATOM 632 C C . GLU A 1 80 ? -26.444 15.683 11.682 1.00 179.43 ? 99 GLU A C 1 ATOM 633 O O . GLU A 1 80 ? -25.324 16.200 11.695 1.00 179.77 ? 99 GLU A O 1 ATOM 634 C CB . GLU A 1 80 ? -28.341 15.846 10.004 1.00 189.89 ? 99 GLU A CB 1 ATOM 635 C CG . GLU A 1 80 ? -29.808 16.220 9.851 1.00 202.34 ? 99 GLU A CG 1 ATOM 636 C CD . GLU A 1 80 ? -30.782 15.448 10.721 1.00 201.02 ? 99 GLU A CD 1 ATOM 637 O OE1 . GLU A 1 80 ? -30.484 14.282 11.070 1.00 188.66 ? 99 GLU A OE1 1 ATOM 638 O OE2 . GLU A 1 80 ? -31.864 15.999 11.026 1.00 248.81 ? 99 GLU A OE2 1 ATOM 639 N N . GLN A 1 81 ? -26.676 14.416 12.050 1.00 168.90 ? 100 GLN A N 1 ATOM 640 C CA . GLN A 1 81 ? -25.674 13.476 12.552 1.00 157.28 ? 100 GLN A CA 1 ATOM 641 C C . GLN A 1 81 ? -25.204 12.519 11.453 1.00 145.89 ? 100 GLN A C 1 ATOM 642 O O . GLN A 1 81 ? -24.749 11.411 11.741 1.00 136.39 ? 100 GLN A O 1 ATOM 643 C CB . GLN A 1 81 ? -26.247 12.701 13.753 1.00 156.22 ? 100 GLN A CB 1 ATOM 644 C CG . GLN A 1 81 ? -27.398 13.426 14.453 1.00 169.05 ? 100 GLN A CG 1 ATOM 645 C CD . GLN A 1 81 ? -27.905 12.725 15.682 1.00 170.31 ? 100 GLN A CD 1 ATOM 646 O OE1 . GLN A 1 81 ? -29.112 12.538 15.855 1.00 175.77 ? 100 GLN A OE1 1 ATOM 647 N NE2 . GLN A 1 81 ? -27.005 12.354 16.583 1.00 167.06 ? 100 GLN A NE2 1 ATOM 648 N N . THR A 1 82 ? -25.315 12.957 10.192 1.00 148.29 ? 101 THR A N 1 ATOM 649 C CA . THR A 1 82 ? -24.905 12.180 9.026 1.00 140.05 ? 101 THR A CA 1 ATOM 650 C C . THR A 1 82 ? -23.384 12.243 8.850 1.00 135.09 ? 101 THR A C 1 ATOM 651 O O . THR A 1 82 ? -22.764 13.193 9.336 1.00 140.50 ? 101 THR A O 1 ATOM 652 C CB . THR A 1 82 ? -25.645 12.652 7.767 1.00 147.18 ? 101 THR A CB 1 ATOM 653 O OG1 . THR A 1 82 ? -25.355 14.029 7.526 1.00 157.65 ? 101 THR A OG1 1 ATOM 654 C CG2 . THR A 1 82 ? -27.136 12.420 7.848 1.00 152.32 ? 101 THR A CG2 1 ATOM 655 N N . PRO A 1 83 ? -22.780 11.249 8.153 1.00 126.01 ? 102 PRO A N 1 ATOM 656 C CA . PRO A 1 83 ? -21.331 11.240 7.937 1.00 122.07 ? 102 PRO A CA 1 ATOM 657 C C . PRO A 1 83 ? -20.853 12.304 6.951 1.00 129.67 ? 102 PRO A C 1 ATOM 658 O O . PRO A 1 83 ? -19.745 12.816 7.106 1.00 131.33 ? 102 PRO A O 1 ATOM 659 C CB . PRO A 1 83 ? -21.058 9.826 7.426 1.00 112.52 ? 102 PRO A CB 1 ATOM 660 C CG . PRO A 1 83 ? -22.336 9.397 6.807 1.00 113.65 ? 102 PRO A CG 1 ATOM 661 C CD . PRO A 1 83 ? -23.403 10.010 7.642 1.00 120.44 ? 102 PRO A CD 1 ATOM 662 N N . GLY A 1 84 ? -21.683 12.625 5.939 1.00 135.98 ? 103 GLY A N 1 ATOM 663 C CA . GLY A 1 84 ? -21.362 13.600 4.898 1.00 145.25 ? 103 GLY A CA 1 ATOM 664 C C . GLY A 1 84 ? -20.167 13.119 4.079 1.00 140.47 ? 103 GLY A C 1 ATOM 665 O O . GLY A 1 84 ? -20.097 11.941 3.724 1.00 131.70 ? 103 GLY A O 1 ATOM 666 N N . GLN A 1 85 ? -19.213 14.025 3.822 1.00 147.52 ? 104 GLN A N 1 ATOM 667 C CA . GLN A 1 85 ? -17.996 13.734 3.061 1.00 145.67 ? 104 GLN A CA 1 ATOM 668 C C . GLN A 1 85 ? -16.848 13.307 3.982 1.00 138.05 ? 104 GLN A C 1 ATOM 669 O O . GLN A 1 85 ? -15.738 13.053 3.508 1.00 136.72 ? 104 GLN A O 1 ATOM 670 C CB . GLN A 1 85 ? -17.590 14.952 2.203 1.00 159.98 ? 104 GLN A CB 1 ATOM 671 C CG . GLN A 1 85 ? -18.669 15.444 1.232 1.00 171.36 ? 104 GLN A CG 1 ATOM 672 C CD . GLN A 1 85 ? -18.769 14.620 -0.031 1.00 170.93 ? 104 GLN A CD 1 ATOM 673 O OE1 . GLN A 1 85 ? -18.329 15.037 -1.108 1.00 182.48 ? 104 GLN A OE1 1 ATOM 674 N NE2 . GLN A 1 85 ? -19.384 13.449 0.061 1.00 158.97 ? 104 GLN A NE2 1 ATOM 675 N N . GLU A 1 86 ? -17.125 13.204 5.293 1.00 134.24 ? 105 GLU A N 1 ATOM 676 C CA . GLU A 1 86 ? -16.135 12.838 6.301 1.00 129.35 ? 105 GLU A CA 1 ATOM 677 C C . GLU A 1 86 ? -15.656 11.400 6.240 1.00 118.19 ? 105 GLU A C 1 ATOM 678 O O . GLU A 1 86 ? -16.454 10.472 6.095 1.00 111.80 ? 105 GLU A O 1 ATOM 679 C CB . GLU A 1 86 ? -16.608 13.200 7.717 1.00 131.18 ? 105 GLU A CB 1 ATOM 680 C CG . GLU A 1 86 ? -16.692 14.697 7.980 1.00 144.57 ? 105 GLU A CG 1 ATOM 681 C CD . GLU A 1 86 ? -15.387 15.476 7.977 1.00 152.52 ? 105 GLU A CD 1 ATOM 682 O OE1 . GLU A 1 86 ? -14.309 14.857 8.134 1.00 147.64 ? 105 GLU A OE1 1 ATOM 683 O OE2 . GLU A 1 86 ? -15.448 16.719 7.837 1.00 165.25 ? 105 GLU A OE2 1 ATOM 684 N N . VAL A 1 87 ? -14.334 11.231 6.358 1.00 117.45 ? 106 VAL A N 1 ATOM 685 C CA . VAL A 1 87 ? -13.673 9.931 6.366 1.00 109.03 ? 106 VAL A CA 1 ATOM 686 C C . VAL A 1 87 ? -13.480 9.503 7.818 1.00 105.77 ? 106 VAL A C 1 ATOM 687 O O . VAL A 1 87 ? -13.022 10.301 8.640 1.00 111.60 ? 106 VAL A O 1 ATOM 688 C CB . VAL A 1 87 ? -12.326 9.956 5.590 1.00 111.81 ? 106 VAL A CB 1 ATOM 689 C CG1 . VAL A 1 87 ? -11.457 8.750 5.933 1.00 105.34 ? 106 VAL A CG1 1 ATOM 690 C CG2 . VAL A 1 87 ? -12.552 10.045 4.085 1.00 114.85 ? 106 VAL A CG2 1 ATOM 691 N N . VAL A 1 88 ? -13.817 8.243 8.122 1.00 98.25 ? 107 VAL A N 1 ATOM 692 C CA . VAL A 1 88 ? -13.623 7.670 9.448 1.00 96.39 ? 107 VAL A CA 1 ATOM 693 C C . VAL A 1 88 ? -12.367 6.802 9.386 1.00 94.22 ? 107 VAL A C 1 ATOM 694 O O . VAL A 1 88 ? -12.320 5.826 8.632 1.00 89.64 ? 107 VAL A O 1 ATOM 695 C CB . VAL A 1 88 ? -14.858 6.893 9.980 1.00 92.43 ? 107 VAL A CB 1 ATOM 696 C CG1 . VAL A 1 88 ? -14.603 6.362 11.390 1.00 92.85 ? 107 VAL A CG1 1 ATOM 697 C CG2 . VAL A 1 88 ? -16.113 7.763 9.959 1.00 95.80 ? 107 VAL A CG2 1 ATOM 698 N N . LEU A 1 89 ? -11.341 7.186 10.152 1.00 98.85 ? 108 LEU A N 1 ATOM 699 C CA . LEU A 1 89 ? -10.080 6.458 10.197 1.00 98.93 ? 108 LEU A CA 1 ATOM 700 C C . LEU A 1 89 ? -9.942 5.707 11.516 1.00 99.13 ? 108 LEU A C 1 ATOM 701 O O . LEU A 1 89 ? -10.097 6.304 12.584 1.00 103.65 ? 108 LEU A O 1 ATOM 702 C CB . LEU A 1 89 ? -8.889 7.412 9.967 1.00 106.20 ? 108 LEU A CB 1 ATOM 703 C CG . LEU A 1 89 ? -7.497 6.782 9.790 1.00 108.75 ? 108 LEU A CG 1 ATOM 704 C CD1 . LEU A 1 89 ? -7.372 6.064 8.449 1.00 104.62 ? 108 LEU A CD1 1 ATOM 705 C CD2 . LEU A 1 89 ? -6.413 7.836 9.901 1.00 118.27 ? 108 LEU A CD2 1 ATOM 706 N N . SER A 1 90 ? -9.667 4.394 11.439 1.00 95.68 ? 109 SER A N 1 ATOM 707 C CA . SER A 1 90 ? -9.472 3.571 12.631 1.00 97.94 ? 109 SER A CA 1 ATOM 708 C C . SER A 1 90 ? -8.066 3.823 13.187 1.00 105.21 ? 109 SER A C 1 ATOM 709 O O . SER A 1 90 ? -7.154 4.050 12.393 1.00 106.58 ? 109 SER A O 1 ATOM 710 C CB . SER A 1 90 ? -9.662 2.091 12.314 1.00 94.09 ? 109 SER A CB 1 ATOM 711 O OG . SER A 1 90 ? -8.597 1.580 11.531 1.00 94.44 ? 109 SER A OG 1 ATOM 712 N N . PRO A 1 91 ? -7.882 3.795 14.530 1.00 111.21 ? 110 PRO A N 1 ATOM 713 C CA . PRO A 1 91 ? -6.558 4.019 15.120 1.00 120.04 ? 110 PRO A CA 1 ATOM 714 C C . PRO A 1 91 ? -5.611 2.848 14.840 1.00 121.15 ? 110 PRO A C 1 ATOM 715 O O . PRO A 1 91 ? -4.406 3.060 14.693 1.00 127.12 ? 110 PRO A O 1 ATOM 716 C CB . PRO A 1 91 ? -6.845 4.164 16.623 1.00 126.88 ? 110 PRO A CB 1 ATOM 717 C CG . PRO A 1 91 ? -8.327 4.303 16.745 1.00 121.65 ? 110 PRO A CG 1 ATOM 718 C CD . PRO A 1 91 ? -8.895 3.581 15.580 1.00 111.77 ? 110 PRO A CD 1 ATOM 719 N N . GLY A 1 92 ? -6.162 1.622 14.759 1.00 116.86 ? 111 GLY A N 1 ATOM 720 C CA . GLY A 1 92 ? -5.400 0.401 14.509 1.00 118.92 ? 111 GLY A CA 1 ATOM 721 C C . GLY A 1 92 ? -5.861 -0.352 13.264 1.00 111.52 ? 111 GLY A C 1 ATOM 722 O O . GLY A 1 92 ? -6.406 0.248 12.335 1.00 105.23 ? 111 GLY A O 1 ATOM 723 N N . SER A 1 93 ? -5.632 -1.676 13.257 1.00 113.85 ? 112 SER A N 1 ATOM 724 C CA . SER A 1 93 ? -5.959 -2.563 12.141 1.00 109.27 ? 112 SER A CA 1 ATOM 725 C C . SER A 1 93 ? -7.334 -3.252 12.249 1.00 105.21 ? 112 SER A C 1 ATOM 726 O O . SER A 1 93 ? -7.574 -4.254 11.566 1.00 104.36 ? 112 SER A O 1 ATOM 727 C CB . SER A 1 93 ? -4.841 -3.583 11.937 1.00 116.07 ? 112 SER A CB 1 ATOM 728 O OG . SER A 1 93 ? -4.804 -4.534 12.988 1.00 123.13 ? 112 SER A OG 1 ATOM 729 N N . PHE A 1 94 ? -8.240 -2.705 13.079 1.00 103.94 ? 113 PHE A N 1 ATOM 730 C CA . PHE A 1 94 ? -9.576 -3.273 13.257 1.00 101.61 ? 113 PHE A CA 1 ATOM 731 C C . PHE A 1 94 ? -10.679 -2.223 13.291 1.00 96.54 ? 113 PHE A C 1 ATOM 732 O O . PHE A 1 94 ? -10.520 -1.174 13.917 1.00 98.07 ? 113 PHE A O 1 ATOM 733 C CB . PHE A 1 94 ? -9.634 -4.178 14.505 1.00 109.71 ? 113 PHE A CB 1 ATOM 734 C CG . PHE A 1 94 ? -11.013 -4.704 14.845 1.00 109.39 ? 113 PHE A CG 1 ATOM 735 C CD1 . PHE A 1 94 ? -11.555 -5.781 14.154 1.00 109.02 ? 113 PHE A CD1 1 ATOM 736 C CD2 . PHE A 1 94 ? -11.778 -4.107 15.842 1.00 111.00 ? 113 PHE A CD2 1 ATOM 737 C CE1 . PHE A 1 94 ? -12.836 -6.256 14.458 1.00 110.41 ? 113 PHE A CE1 1 ATOM 738 C CE2 . PHE A 1 94 ? -13.058 -4.581 16.143 1.00 112.11 ? 113 PHE A CE2 1 ATOM 739 C CZ . PHE A 1 94 ? -13.577 -5.651 15.448 1.00 111.78 ? 113 PHE A CZ 1 ATOM 740 N N . MET A 1 95 ? -11.820 -2.539 12.653 1.00 92.06 ? 114 MET A N 1 ATOM 741 C CA . MET A 1 95 ? -13.001 -1.681 12.625 1.00 88.66 ? 114 MET A CA 1 ATOM 742 C C . MET A 1 95 ? -14.273 -2.523 12.597 1.00 88.58 ? 114 MET A C 1 ATOM 743 O O . MET A 1 95 ? -14.404 -3.410 11.754 1.00 87.85 ? 114 MET A O 1 ATOM 744 C CB . MET A 1 95 ? -12.958 -0.715 11.426 1.00 83.91 ? 114 MET A CB 1 ATOM 745 C CG . MET A 1 95 ? -14.069 0.323 11.437 1.00 82.26 ? 114 MET A CG 1 ATOM 746 S SD . MET A 1 95 ? -14.104 1.343 9.941 1.00 79.25 ? 114 MET A SD 1 ATOM 747 C CE . MET A 1 95 ? -12.863 2.559 10.343 1.00 82.22 ? 114 MET A CE 1 ATOM 748 N N . SER A 1 96 ? -15.207 -2.236 13.515 1.00 90.84 ? 115 SER A N 1 ATOM 749 C CA . SER A 1 96 ? -16.499 -2.912 13.584 1.00 92.39 ? 115 SER A CA 1 ATOM 750 C C . SER A 1 96 ? -17.604 -1.920 13.250 1.00 89.54 ? 115 SER A C 1 ATOM 751 O O . SER A 1 96 ? -17.604 -0.794 13.756 1.00 90.12 ? 115 SER A O 1 ATOM 752 C CB . SER A 1 96 ? -16.728 -3.532 14.958 1.00 100.25 ? 115 SER A CB 1 ATOM 753 O OG . SER A 1 96 ? -17.901 -4.330 14.964 1.00 103.31 ? 115 SER A OG 1 ATOM 754 N N . ILE A 1 97 ? -18.523 -2.331 12.364 1.00 88.07 ? 116 ILE A N 1 ATOM 755 C CA . ILE A 1 97 ? -19.644 -1.505 11.917 1.00 86.81 ? 116 ILE A CA 1 ATOM 756 C C . ILE A 1 97 ? -20.961 -2.214 12.201 1.00 91.31 ? 116 ILE A C 1 ATOM 757 O O . ILE A 1 97 ? -21.142 -3.348 11.766 1.00 93.08 ? 116 ILE A O 1 ATOM 758 C CB . ILE A 1 97 ? -19.521 -1.122 10.410 1.00 82.68 ? 116 ILE A CB 1 ATOM 759 C CG1 . ILE A 1 97 ? -18.196 -0.386 10.111 1.00 79.78 ? 116 ILE A CG1 1 ATOM 760 C CG2 . ILE A 1 97 ? -20.737 -0.299 9.940 1.00 83.23 ? 116 ILE A CG2 1 ATOM 761 C CD1 . ILE A 1 97 ? -17.807 -0.357 8.650 1.00 77.46 ? 116 ILE A CD1 1 ATOM 762 N N . THR A 1 98 ? -21.889 -1.536 12.893 1.00 94.49 ? 117 THR A N 1 ATOM 763 C CA . THR A 1 98 ? -23.212 -2.083 13.174 1.00 100.17 ? 117 THR A CA 1 ATOM 764 C C . THR A 1 98 ? -24.305 -1.178 12.631 1.00 100.68 ? 117 THR A C 1 ATOM 765 O O . THR A 1 98 ? -24.354 0.004 12.978 1.00 100.79 ? 117 THR A O 1 ATOM 766 C CB . THR A 1 98 ? -23.413 -2.365 14.678 1.00 107.37 ? 117 THR A CB 1 ATOM 767 O OG1 . THR A 1 98 ? -22.452 -3.328 15.108 1.00 109.05 ? 117 THR A OG1 1 ATOM 768 C CG2 . THR A 1 98 ? -24.831 -2.871 15.007 1.00 114.77 ? 117 THR A CG2 1 ATOM 769 N N . PHE A 1 99 ? -25.195 -1.743 11.802 1.00 102.55 ? 118 PHE A N 1 ATOM 770 C CA . PHE A 1 99 ? -26.372 -1.035 11.321 1.00 105.92 ? 118 PHE A CA 1 ATOM 771 C C . PHE A 1 99 ? -27.547 -1.602 12.097 1.00 114.45 ? 118 PHE A C 1 ATOM 772 O O . PHE A 1 99 ? -27.773 -2.814 12.068 1.00 118.19 ? 118 PHE A O 1 ATOM 773 C CB . PHE A 1 99 ? -26.598 -1.187 9.800 1.00 104.71 ? 118 PHE A CB 1 ATOM 774 C CG . PHE A 1 99 ? -27.992 -0.784 9.354 1.00 110.91 ? 118 PHE A CG 1 ATOM 775 C CD1 . PHE A 1 99 ? -28.349 0.557 9.251 1.00 112.20 ? 118 PHE A CD1 1 ATOM 776 C CD2 . PHE A 1 99 ? -28.956 -1.747 9.072 1.00 117.55 ? 118 PHE A CD2 1 ATOM 777 C CE1 . PHE A 1 99 ? -29.643 0.926 8.863 1.00 119.86 ? 118 PHE A CE1 1 ATOM 778 C CE2 . PHE A 1 99 ? -30.250 -1.375 8.686 1.00 124.71 ? 118 PHE A CE2 1 ATOM 779 C CZ . PHE A 1 99 ? -30.582 -0.042 8.583 1.00 126.05 ? 118 PHE A CZ 1 ATOM 780 N N . ARG A 1 100 ? -28.291 -0.736 12.788 1.00 119.23 ? 119 ARG A N 1 ATOM 781 C CA . ARG A 1 100 ? -29.467 -1.167 13.531 1.00 128.80 ? 119 ARG A CA 1 ATOM 782 C C . ARG A 1 100 ? -30.703 -0.413 13.074 1.00 134.37 ? 119 ARG A C 1 ATOM 783 O O . ARG A 1 100 ? -30.659 0.801 12.880 1.00 132.93 ? 119 ARG A O 1 ATOM 784 C CB . ARG A 1 100 ? -29.261 -1.033 15.047 1.00 133.19 ? 119 ARG A CB 1 ATOM 785 C CG . ARG A 1 100 ? -30.379 -1.652 15.891 1.00 145.00 ? 119 ARG A CG 1 ATOM 786 C CD . ARG A 1 100 ? -31.130 -0.596 16.673 1.00 152.18 ? 119 ARG A CD 1 ATOM 787 N NE . ARG A 1 100 ? -32.301 -1.138 17.361 1.00 164.89 ? 119 ARG A NE 1 ATOM 788 C CZ . ARG A 1 100 ? -33.077 -0.440 18.185 1.00 174.00 ? 119 ARG A CZ 1 ATOM 789 N NH1 . ARG A 1 100 ? -32.812 0.837 18.438 1.00 172.06 ? 119 ARG A NH1 1 ATOM 790 N NH2 . ARG A 1 100 ? -34.123 -1.013 18.765 1.00 186.83 ? 119 ARG A NH2 1 ATOM 791 N N . SER A 1 101 ? -31.803 -1.150 12.908 1.00 142.35 ? 120 SER A N 1 ATOM 792 C CA . SER A 1 101 ? -33.107 -0.626 12.534 1.00 150.34 ? 120 SER A CA 1 ATOM 793 C C . SER A 1 101 ? -34.087 -1.107 13.597 1.00 161.88 ? 120 SER A C 1 ATOM 794 O O . SER A 1 101 ? -34.173 -2.311 13.845 1.00 165.60 ? 120 SER A O 1 ATOM 795 C CB . SER A 1 101 ? -33.510 -1.142 11.155 1.00 151.12 ? 120 SER A CB 1 ATOM 796 O OG . SER A 1 101 ? -34.773 -0.638 10.753 1.00 160.52 ? 120 SER A OG 1 ATOM 797 N N . ASP A 1 102 ? -34.797 -0.181 14.258 1.00 168.75 ? 121 ASP A N 1 ATOM 798 C CA . ASP A 1 102 ? -35.756 -0.575 15.288 1.00 181.46 ? 121 ASP A CA 1 ATOM 799 C C . ASP A 1 102 ? -37.065 -1.116 14.688 1.00 192.78 ? 121 ASP A C 1 ATOM 800 O O . ASP A 1 102 ? -37.123 -1.407 13.492 1.00 189.01 ? 121 ASP A O 1 ATOM 801 C CB . ASP A 1 102 ? -35.987 0.557 16.307 1.00 186.79 ? 121 ASP A CB 1 ATOM 802 C CG . ASP A 1 102 ? -36.585 1.849 15.775 1.00 189.01 ? 121 ASP A CG 1 ATOM 803 O OD1 . ASP A 1 102 ? -36.777 1.962 14.533 1.00 185.42 ? 121 ASP A OD1 1 ATOM 804 O OD2 . ASP A 1 102 ? -36.862 2.750 16.593 1.00 198.87 ? 121 ASP A OD2 1 ATOM 805 N N . PHE A 1 103 ? -38.104 -1.257 15.515 1.00 244.19 ? 122 PHE A N 1 ATOM 806 C CA . PHE A 1 103 ? -39.404 -1.784 15.104 1.00 259.29 ? 122 PHE A CA 1 ATOM 807 C C . PHE A 1 103 ? -40.234 -0.776 14.308 1.00 262.88 ? 122 PHE A C 1 ATOM 808 O O . PHE A 1 103 ? -41.151 -1.179 13.589 1.00 272.52 ? 122 PHE A O 1 ATOM 809 C CB . PHE A 1 103 ? -40.189 -2.254 16.340 1.00 273.47 ? 122 PHE A CB 1 ATOM 810 C CG . PHE A 1 103 ? -39.537 -3.379 17.109 1.00 274.10 ? 122 PHE A CG 1 ATOM 811 C CD1 . PHE A 1 103 ? -38.551 -3.119 18.055 1.00 269.06 ? 122 PHE A CD1 1 ATOM 812 C CD2 . PHE A 1 103 ? -39.928 -4.697 16.908 1.00 278.64 ? 122 PHE A CD2 1 ATOM 813 C CE1 . PHE A 1 103 ? -37.948 -4.160 18.765 1.00 272.32 ? 122 PHE A CE1 1 ATOM 814 C CE2 . PHE A 1 103 ? -39.330 -5.738 17.625 1.00 279.76 ? 122 PHE A CE2 1 ATOM 815 C CZ . PHE A 1 103 ? -38.345 -5.462 18.549 1.00 277.70 ? 122 PHE A CZ 1 ATOM 816 N N . SER A 1 104 ? -39.924 0.524 14.442 1.00 258.97 ? 123 SER A N 1 ATOM 817 C CA . SER A 1 104 ? -40.674 1.598 13.798 1.00 263.98 ? 123 SER A CA 1 ATOM 818 C C . SER A 1 104 ? -40.075 2.130 12.491 1.00 257.16 ? 123 SER A C 1 ATOM 819 O O . SER A 1 104 ? -39.253 3.052 12.514 1.00 249.17 ? 123 SER A O 1 ATOM 820 C CB . SER A 1 104 ? -40.935 2.728 14.790 1.00 269.49 ? 123 SER A CB 1 ATOM 821 O OG . SER A 1 104 ? -41.812 3.707 14.257 1.00 282.18 ? 123 SER A OG 1 ATOM 822 N N . ASN A 1 105 ? -40.511 1.565 11.349 1.00 258.89 ? 124 ASN A N 1 ATOM 823 C CA . ASN A 1 105 ? -40.080 2.039 10.035 1.00 254.66 ? 124 ASN A CA 1 ATOM 824 C C . ASN A 1 105 ? -41.251 2.569 9.209 1.00 265.22 ? 124 ASN A C 1 ATOM 825 O O . ASN A 1 105 ? -41.487 2.112 8.085 1.00 268.01 ? 124 ASN A O 1 ATOM 826 C CB . ASN A 1 105 ? -39.219 1.022 9.272 1.00 243.11 ? 124 ASN A CB 1 ATOM 827 C CG . ASN A 1 105 ? -38.195 1.670 8.355 1.00 208.71 ? 124 ASN A CG 1 ATOM 828 O OD1 . ASN A 1 105 ? -37.809 2.836 8.515 1.00 193.49 ? 124 ASN A OD1 1 ATOM 829 N ND2 . ASN A 1 105 ? -37.700 0.915 7.388 1.00 188.45 ? 124 ASN A ND2 1 ATOM 830 N N . GLU A 1 106 ? -41.985 3.547 9.785 1.00 275.14 ? 125 GLU A N 1 ATOM 831 C CA . GLU A 1 106 ? -43.132 4.213 9.156 1.00 282.58 ? 125 GLU A CA 1 ATOM 832 C C . GLU A 1 106 ? -42.665 4.829 7.843 1.00 281.62 ? 125 GLU A C 1 ATOM 833 O O . GLU A 1 106 ? -43.098 4.391 6.774 1.00 283.35 ? 125 GLU A O 1 ATOM 834 C CB . GLU A 1 106 ? -43.727 5.286 10.089 1.00 285.25 ? 125 GLU A CB 1 ATOM 835 C CG . GLU A 1 106 ? -44.328 4.732 11.372 1.00 286.75 ? 125 GLU A CG 1 ATOM 836 C CD . GLU A 1 106 ? -45.777 4.286 11.303 1.00 287.52 ? 125 GLU A CD 1 ATOM 837 O OE1 . GLU A 1 106 ? -46.140 3.542 10.363 1.00 287.00 ? 125 GLU A OE1 1 ATOM 838 O OE2 . GLU A 1 106 ? -46.544 4.648 12.224 1.00 288.10 ? 125 GLU A OE2 1 ATOM 839 N N . GLU A 1 107 ? -41.715 5.782 7.927 1.00 276.94 ? 126 GLU A N 1 ATOM 840 C CA . GLU A 1 107 ? -41.093 6.411 6.767 1.00 272.10 ? 126 GLU A CA 1 ATOM 841 C C . GLU A 1 107 ? -40.146 5.386 6.151 1.00 261.49 ? 126 GLU A C 1 ATOM 842 O O . GLU A 1 107 ? -39.577 4.560 6.871 1.00 254.05 ? 126 GLU A O 1 ATOM 843 C CB . GLU A 1 107 ? -40.305 7.659 7.170 1.00 267.61 ? 126 GLU A CB 1 ATOM 844 C CG . GLU A 1 107 ? -41.134 8.820 7.686 1.00 280.58 ? 126 GLU A CG 1 ATOM 845 C CD . GLU A 1 107 ? -40.315 10.061 7.986 1.00 278.23 ? 126 GLU A CD 1 ATOM 846 O OE1 . GLU A 1 107 ? -39.482 10.447 7.134 1.00 272.70 ? 126 GLU A OE1 1 ATOM 847 O OE2 . GLU A 1 107 ? -40.514 10.658 9.069 1.00 286.32 ? 126 GLU A OE2 1 ATOM 848 N N . ARG A 1 108 ? -39.995 5.426 4.824 1.00 262.21 ? 127 ARG A N 1 ATOM 849 C CA . ARG A 1 108 ? -39.168 4.471 4.096 1.00 255.04 ? 127 ARG A CA 1 ATOM 850 C C . ARG A 1 108 ? -37.785 4.999 3.741 1.00 237.81 ? 127 ARG A C 1 ATOM 851 O O . ARG A 1 108 ? -37.566 5.517 2.642 1.00 244.00 ? 127 ARG A O 1 ATOM 852 C CB . ARG A 1 108 ? -39.935 3.908 2.884 1.00 263.99 ? 127 ARG A CB 1 ATOM 853 C CG . ARG A 1 108 ? -40.619 2.553 3.119 1.00 269.38 ? 127 ARG A CG 1 ATOM 854 C CD . ARG A 1 108 ? -41.081 2.299 4.552 1.00 270.22 ? 127 ARG A CD 1 ATOM 855 N NE . ARG A 1 108 ? -41.635 0.957 4.733 1.00 275.61 ? 127 ARG A NE 1 ATOM 856 C CZ . ARG A 1 108 ? -40.911 -0.142 4.930 1.00 269.33 ? 127 ARG A CZ 1 ATOM 857 N NH1 . ARG A 1 108 ? -39.584 -0.077 4.958 1.00 254.77 ? 127 ARG A NH1 1 ATOM 858 N NH2 . ARG A 1 108 ? -41.506 -1.316 5.086 1.00 275.73 ? 127 ARG A NH2 1 ATOM 859 N N . PHE A 1 109 ? -36.848 4.862 4.690 1.00 188.81 ? 128 PHE A N 1 ATOM 860 C CA . PHE A 1 109 ? -35.468 5.305 4.527 1.00 177.44 ? 128 PHE A CA 1 ATOM 861 C C . PHE A 1 109 ? -34.673 4.270 3.741 1.00 169.20 ? 128 PHE A C 1 ATOM 862 O O . PHE A 1 109 ? -34.777 3.074 4.016 1.00 166.50 ? 128 PHE A O 1 ATOM 863 C CB . PHE A 1 109 ? -34.832 5.623 5.886 1.00 169.68 ? 128 PHE A CB 1 ATOM 864 C CG . PHE A 1 109 ? -35.561 6.687 6.671 1.00 178.90 ? 128 PHE A CG 1 ATOM 865 C CD1 . PHE A 1 109 ? -35.384 8.035 6.378 1.00 183.93 ? 128 PHE A CD1 1 ATOM 866 C CD2 . PHE A 1 109 ? -36.434 6.342 7.694 1.00 184.37 ? 128 PHE A CD2 1 ATOM 867 C CE1 . PHE A 1 109 ? -36.063 9.019 7.103 1.00 194.14 ? 128 PHE A CE1 1 ATOM 868 C CE2 . PHE A 1 109 ? -37.108 7.326 8.420 1.00 194.11 ? 128 PHE A CE2 1 ATOM 869 C CZ . PHE A 1 109 ? -36.917 8.658 8.122 1.00 205.59 ? 128 PHE A CZ 1 ATOM 870 N N . THR A 1 110 ? -33.906 4.736 2.741 1.00 166.88 ? 129 THR A N 1 ATOM 871 C CA . THR A 1 110 ? -33.135 3.896 1.816 1.00 161.61 ? 129 THR A CA 1 ATOM 872 C C . THR A 1 110 ? -31.793 3.363 2.329 1.00 147.94 ? 129 THR A C 1 ATOM 873 O O . THR A 1 110 ? -31.113 2.626 1.609 1.00 144.05 ? 129 THR A O 1 ATOM 874 C CB . THR A 1 110 ? -33.051 4.550 0.435 1.00 168.91 ? 129 THR A CB 1 ATOM 875 O OG1 . THR A 1 110 ? -32.468 5.844 0.574 1.00 167.94 ? 129 THR A OG1 1 ATOM 876 C CG2 . THR A 1 110 ? -34.410 4.653 -0.245 1.00 184.06 ? 129 THR A CG2 1 ATOM 877 N N . GLY A 1 111 ? -31.417 3.721 3.563 1.00 141.94 ? 130 GLY A N 1 ATOM 878 C CA . GLY A 1 111 ? -30.194 3.233 4.193 1.00 130.62 ? 130 GLY A CA 1 ATOM 879 C C . GLY A 1 111 ? -28.910 3.909 3.750 1.00 125.19 ? 130 GLY A C 1 ATOM 880 O O . GLY A 1 111 ? -28.871 5.127 3.577 1.00 129.02 ? 130 GLY A O 1 ATOM 881 N N . PHE A 1 112 ? -27.843 3.112 3.604 1.00 117.49 ? 131 PHE A N 1 ATOM 882 C CA . PHE A 1 112 ? -26.526 3.638 3.276 1.00 112.65 ? 131 PHE A CA 1 ATOM 883 C C . PHE A 1 112 ? -25.716 2.792 2.298 1.00 109.70 ? 131 PHE A C 1 ATOM 884 O O . PHE A 1 112 ? -25.998 1.609 2.096 1.00 109.74 ? 131 PHE A O 1 ATOM 885 C CB . PHE A 1 112 ? -25.724 3.846 4.579 1.00 106.10 ? 131 PHE A CB 1 ATOM 886 C CG . PHE A 1 112 ? -25.234 2.561 5.209 1.00 100.21 ? 131 PHE A CG 1 ATOM 887 C CD1 . PHE A 1 112 ? -26.057 1.820 6.049 1.00 101.74 ? 131 PHE A CD1 1 ATOM 888 C CD2 . PHE A 1 112 ? -23.955 2.084 4.950 1.00 94.60 ? 131 PHE A CD2 1 ATOM 889 C CE1 . PHE A 1 112 ? -25.612 0.621 6.612 1.00 98.28 ? 131 PHE A CE1 1 ATOM 890 C CE2 . PHE A 1 112 ? -23.512 0.884 5.511 1.00 90.77 ? 131 PHE A CE2 1 ATOM 891 C CZ . PHE A 1 112 ? -24.343 0.161 6.340 1.00 92.99 ? 131 PHE A CZ 1 ATOM 892 N N . ASP A 1 113 ? -24.656 3.407 1.754 1.00 108.24 ? 132 ASP A N 1 ATOM 893 C CA . ASP A 1 113 ? -23.675 2.789 0.873 1.00 106.17 ? 132 ASP A CA 1 ATOM 894 C C . ASP A 1 113 ? -22.302 3.253 1.352 1.00 100.52 ? 132 ASP A C 1 ATOM 895 O O . ASP A 1 113 ? -22.005 4.450 1.316 1.00 102.88 ? 132 ASP A O 1 ATOM 896 C CB . ASP A 1 113 ? -23.923 3.163 -0.599 1.00 114.78 ? 132 ASP A CB 1 ATOM 897 C CG . ASP A 1 113 ? -22.882 2.621 -1.563 1.00 114.80 ? 132 ASP A CG 1 ATOM 898 O OD1 . ASP A 1 113 ? -22.386 1.490 -1.334 1.00 110.05 ? 132 ASP A OD1 1 ATOM 899 O OD2 . ASP A 1 113 ? -22.573 3.317 -2.553 1.00 121.19 ? 132 ASP A OD2 1 ATOM 900 N N . ALA A 1 114 ? -21.489 2.310 1.845 1.00 94.31 ? 133 ALA A N 1 ATOM 901 C CA . ALA A 1 114 ? -20.169 2.613 2.389 1.00 89.83 ? 133 ALA A CA 1 ATOM 902 C C . ALA A 1 114 ? -19.035 1.879 1.695 1.00 88.46 ? 133 ALA A C 1 ATOM 903 O O . ALA A 1 114 ? -19.232 0.794 1.145 1.00 89.22 ? 133 ALA A O 1 ATOM 904 C CB . ALA A 1 114 ? -20.143 2.335 3.883 1.00 85.36 ? 133 ALA A CB 1 ATOM 905 N N . HIS A 1 115 ? -17.843 2.493 1.714 1.00 87.74 ? 134 HIS A N 1 ATOM 906 C CA . HIS A 1 115 ? -16.635 1.957 1.102 1.00 87.62 ? 134 HIS A CA 1 ATOM 907 C C . HIS A 1 115 ? -15.467 2.070 2.070 1.00 84.26 ? 134 HIS A C 1 ATOM 908 O O . HIS A 1 115 ? -15.316 3.092 2.745 1.00 84.52 ? 134 HIS A O 1 ATOM 909 C CB . HIS A 1 115 ? -16.323 2.698 -0.208 1.00 94.15 ? 134 HIS A CB 1 ATOM 910 C CG . HIS A 1 115 ? -17.391 2.559 -1.249 1.00 99.72 ? 134 HIS A CG 1 ATOM 911 N ND1 . HIS A 1 115 ? -18.566 3.283 -1.178 1.00 103.13 ? 134 HIS A ND1 1 ATOM 912 C CD2 . HIS A 1 115 ? -17.424 1.785 -2.356 1.00 103.55 ? 134 HIS A CD2 1 ATOM 913 C CE1 . HIS A 1 115 ? -19.274 2.919 -2.234 1.00 108.80 ? 134 HIS A CE1 1 ATOM 914 N NE2 . HIS A 1 115 ? -18.624 2.026 -2.975 1.00 109.89 ? 134 HIS A NE2 1 ATOM 915 N N . TYR A 1 116 ? -14.651 1.013 2.146 1.00 82.65 ? 135 TYR A N 1 ATOM 916 C CA . TYR A 1 116 ? -13.483 0.983 3.018 1.00 81.12 ? 135 TYR A CA 1 ATOM 917 C C . TYR A 1 116 ? -12.256 0.437 2.302 1.00 83.75 ? 135 TYR A C 1 ATOM 918 O O . TYR A 1 116 ? -12.387 -0.266 1.298 1.00 85.84 ? 135 TYR A O 1 ATOM 919 C CB . TYR A 1 116 ? -13.768 0.180 4.304 1.00 77.88 ? 135 TYR A CB 1 ATOM 920 C CG . TYR A 1 116 ? -13.872 -1.315 4.083 1.00 78.37 ? 135 TYR A CG 1 ATOM 921 C CD1 . TYR A 1 116 ? -12.739 -2.126 4.108 1.00 80.15 ? 135 TYR A CD1 1 ATOM 922 C CD2 . TYR A 1 116 ? -15.101 -1.922 3.853 1.00 78.94 ? 135 TYR A CD2 1 ATOM 923 C CE1 . TYR A 1 116 ? -12.825 -3.497 3.877 1.00 82.53 ? 135 TYR A CE1 1 ATOM 924 C CE2 . TYR A 1 116 ? -15.204 -3.299 3.663 1.00 80.72 ? 135 TYR A CE2 1 ATOM 925 C CZ . TYR A 1 116 ? -14.062 -4.081 3.668 1.00 82.96 ? 135 TYR A CZ 1 ATOM 926 O OH . TYR A 1 116 ? -14.157 -5.432 3.451 1.00 87.09 ? 135 TYR A OH 1 ATOM 927 N N . MET A 1 117 ? -11.068 0.721 2.853 1.00 84.73 ? 136 MET A N 1 ATOM 928 C CA . MET A 1 117 ? -9.796 0.223 2.338 1.00 88.99 ? 136 MET A CA 1 ATOM 929 C C . MET A 1 117 ? -8.715 0.282 3.394 1.00 89.26 ? 136 MET A C 1 ATOM 930 O O . MET A 1 117 ? -8.781 1.108 4.311 1.00 88.44 ? 136 MET A O 1 ATOM 931 C CB . MET A 1 117 ? -9.340 0.988 1.080 1.00 94.01 ? 136 MET A CB 1 ATOM 932 C CG . MET A 1 117 ? -8.703 2.340 1.382 1.00 97.71 ? 136 MET A CG 1 ATOM 933 S SD . MET A 1 117 ? -9.087 3.605 0.163 1.00 106.44 ? 136 MET A SD 1 ATOM 934 C CE . MET A 1 117 ? -10.861 3.543 0.189 1.00 99.30 ? 136 MET A CE 1 ATOM 935 N N . ALA A 1 118 ? -7.686 -0.556 3.223 1.00 92.49 ? 137 ALA A N 1 ATOM 936 C CA . ALA A 1 118 ? -6.520 -0.555 4.089 1.00 95.48 ? 137 ALA A CA 1 ATOM 937 C C . ALA A 1 118 ? -5.662 0.643 3.696 1.00 100.23 ? 137 ALA A C 1 ATOM 938 O O . ALA A 1 118 ? -5.543 0.954 2.507 1.00 103.20 ? 137 ALA A O 1 ATOM 939 C CB . ALA A 1 118 ? -5.728 -1.838 3.912 1.00 99.16 ? 137 ALA A CB 1 ATOM 940 N N . VAL A 1 119 ? -5.120 1.346 4.696 1.00 102.36 ? 138 VAL A N 1 ATOM 941 C CA . VAL A 1 119 ? -4.254 2.509 4.495 1.00 108.84 ? 138 VAL A CA 1 ATOM 942 C C . VAL A 1 119 ? -2.958 2.239 5.236 1.00 114.64 ? 138 VAL A C 1 ATOM 943 O O . VAL A 1 119 ? -2.993 1.888 6.416 1.00 113.62 ? 138 VAL A O 1 ATOM 944 C CB . VAL A 1 119 ? -4.916 3.843 4.945 1.00 108.28 ? 138 VAL A CB 1 ATOM 945 C CG1 . VAL A 1 119 ? -3.951 5.022 4.819 1.00 117.25 ? 138 VAL A CG1 1 ATOM 946 C CG2 . VAL A 1 119 ? -6.186 4.118 4.153 1.00 104.33 ? 138 VAL A CG2 1 ATOM 947 N N . ASP A 1 120 ? -1.819 2.403 4.550 1.00 93.87 ? 139 ASP A N 1 ATOM 948 C CA . ASP A 1 120 ? -0.517 2.181 5.160 1.00 92.30 ? 139 ASP A CA 1 ATOM 949 C C . ASP A 1 120 ? -0.228 3.168 6.274 1.00 94.88 ? 139 ASP A C 1 ATOM 950 O O . ASP A 1 120 ? -0.450 4.371 6.120 1.00 98.87 ? 139 ASP A O 1 ATOM 951 C CB . ASP A 1 120 ? 0.612 2.240 4.120 1.00 92.10 ? 139 ASP A CB 1 ATOM 952 C CG . ASP A 1 120 ? 1.987 2.070 4.738 1.00 91.02 ? 139 ASP A CG 1 ATOM 953 O OD1 . ASP A 1 120 ? 2.212 1.036 5.406 1.00 88.34 ? 139 ASP A OD1 1 ATOM 954 O OD2 . ASP A 1 120 ? 2.816 2.997 4.604 1.00 92.92 ? 139 ASP A OD2 1 ATOM 955 N N . VAL A 1 121 ? 0.297 2.648 7.385 1.00 93.50 ? 140 VAL A N 1 ATOM 956 C CA . VAL A 1 121 ? 0.727 3.449 8.523 1.00 96.33 ? 140 VAL A CA 1 ATOM 957 C C . VAL A 1 121 ? 2.142 3.931 8.182 1.00 96.14 ? 140 VAL A C 1 ATOM 958 O O . VAL A 1 121 ? 2.986 3.130 7.759 1.00 92.73 ? 140 VAL A O 1 ATOM 959 C CB . VAL A 1 121 ? 0.719 2.619 9.841 1.00 95.64 ? 140 VAL A CB 1 ATOM 960 C CG1 . VAL A 1 121 ? 1.437 3.345 10.979 1.00 98.50 ? 140 VAL A CG1 1 ATOM 961 C CG2 . VAL A 1 121 ? -0.698 2.237 10.252 1.00 96.99 ? 140 VAL A CG2 1 ATOM 962 N N . ASP A 1 122 ? 2.401 5.227 8.348 1.00 100.57 ? 141 ASP A N 1 ATOM 963 C CA . ASP A 1 122 ? 3.748 5.734 8.146 1.00 101.39 ? 141 ASP A CA 1 ATOM 964 C C . ASP A 1 122 ? 4.381 5.774 9.529 1.00 102.02 ? 141 ASP A C 1 ATOM 965 O O . ASP A 1 122 ? 4.276 6.784 10.228 1.00 106.91 ? 141 ASP A O 1 ATOM 966 C CB . ASP A 1 122 ? 3.766 7.118 7.467 1.00 106.86 ? 141 ASP A CB 1 ATOM 967 C CG . ASP A 1 122 ? 5.157 7.624 7.095 1.00 108.23 ? 141 ASP A CG 1 ATOM 968 O OD1 . ASP A 1 122 ? 6.155 7.127 7.676 1.00 105.27 ? 141 ASP A OD1 1 ATOM 969 O OD2 . ASP A 1 122 ? 5.247 8.531 6.244 1.00 112.96 ? 141 ASP A OD2 1 ATOM 970 N N . GLU A 1 123 ? 5.045 4.674 9.920 1.00 97.92 ? 142 GLU A N 1 ATOM 971 C CA . GLU A 1 123 ? 5.691 4.553 11.227 1.00 98.70 ? 142 GLU A CA 1 ATOM 972 C C . GLU A 1 123 ? 6.742 5.625 11.476 1.00 101.83 ? 142 GLU A C 1 ATOM 973 O O . GLU A 1 123 ? 6.954 5.978 12.623 1.00 104.76 ? 142 GLU A O 1 ATOM 974 C CB . GLU A 1 123 ? 6.250 3.145 11.468 1.00 94.46 ? 142 GLU A CB 1 ATOM 975 C CG . GLU A 1 123 ? 5.184 2.061 11.481 1.00 92.63 ? 142 GLU A CG 1 ATOM 976 C CD . GLU A 1 123 ? 4.921 1.379 10.151 1.00 89.64 ? 142 GLU A CD 1 ATOM 977 O OE1 . GLU A 1 123 ? 5.335 1.911 9.093 1.00 89.61 ? 142 GLU A OE1 1 ATOM 978 O OE2 . GLU A 1 123 ? 4.268 0.312 10.167 1.00 88.49 ? 142 GLU A OE2 1 ATOM 979 N N . CYS A 1 124 ? 7.346 6.190 10.416 1.00 102.19 ? 143 CYS A N 1 ATOM 980 C CA . CYS A 1 124 ? 8.354 7.250 10.529 1.00 105.97 ? 143 CYS A CA 1 ATOM 981 C C . CYS A 1 124 ? 7.905 8.638 11.120 1.00 113.06 ? 143 CYS A C 1 ATOM 982 O O . CYS A 1 124 ? 8.761 9.278 11.725 1.00 116.90 ? 143 CYS A O 1 ATOM 983 C CB . CYS A 1 124 ? 9.141 7.420 9.225 1.00 105.27 ? 143 CYS A CB 1 ATOM 984 S SG . CYS A 1 124 ? 9.958 5.921 8.613 1.00 100.35 ? 143 CYS A SG 1 ATOM 985 N N . LYS A 1 125 ? 6.608 9.110 10.944 1.00 151.67 ? 144 LYS A N 1 ATOM 986 C CA . LYS A 1 125 ? 6.033 10.436 11.364 1.00 178.33 ? 144 LYS A CA 1 ATOM 987 C C . LYS A 1 125 ? 5.258 10.443 12.718 1.00 192.99 ? 144 LYS A C 1 ATOM 988 O O . LYS A 1 125 ? 4.739 11.483 13.150 1.00 253.46 ? 144 LYS A O 1 ATOM 989 C CB . LYS A 1 125 ? 5.086 10.989 10.267 1.00 200.81 ? 144 LYS A CB 1 ATOM 990 C CG . LYS A 1 125 ? 5.739 11.314 8.927 1.00 214.33 ? 144 LYS A CG 1 ATOM 991 C CD . LYS A 1 125 ? 5.836 12.812 8.692 1.00 246.46 ? 144 LYS A CD 1 ATOM 992 C CE . LYS A 1 125 ? 6.436 13.142 7.346 1.00 254.43 ? 144 LYS A CE 1 ATOM 993 N NZ . LYS A 1 125 ? 5.479 12.910 6.230 1.00 272.72 ? 144 LYS A NZ 1 ATOM 994 N N . GLU A 1 126 ? 5.176 9.261 13.349 1.00 181.70 ? 145 GLU A N 1 ATOM 995 C CA . GLU A 1 126 ? 4.506 8.947 14.611 1.00 184.94 ? 145 GLU A CA 1 ATOM 996 C C . GLU A 1 126 ? 5.517 8.431 15.650 1.00 179.71 ? 145 GLU A C 1 ATOM 997 O O . GLU A 1 126 ? 5.329 8.649 16.849 1.00 183.06 ? 145 GLU A O 1 ATOM 998 C CB . GLU A 1 126 ? 3.438 7.866 14.365 1.00 182.76 ? 145 GLU A CB 1 ATOM 999 C CG . GLU A 1 126 ? 2.120 8.391 13.821 1.00 203.61 ? 145 GLU A CG 1 ATOM 1000 C CD . GLU A 1 126 ? 2.076 8.665 12.331 1.00 206.69 ? 145 GLU A CD 1 ATOM 1001 O OE1 . GLU A 1 126 ? 1.972 7.693 11.548 1.00 194.34 ? 145 GLU A OE1 1 ATOM 1002 O OE2 . GLU A 1 126 ? 2.100 9.856 11.947 1.00 228.87 ? 145 GLU A OE2 1 ATOM 1003 N N . ARG A 1 127 ? 6.580 7.738 15.176 1.00 173.02 ? 146 ARG A N 1 ATOM 1004 C CA . ARG A 1 127 ? 7.667 7.144 15.965 1.00 187.51 ? 146 ARG A CA 1 ATOM 1005 C C . ARG A 1 127 ? 8.346 8.081 16.968 1.00 202.84 ? 146 ARG A C 1 ATOM 1006 O O . ARG A 1 127 ? 8.765 7.625 18.035 1.00 215.81 ? 146 ARG A O 1 ATOM 1007 C CB . ARG A 1 127 ? 8.710 6.507 15.047 1.00 191.24 ? 146 ARG A CB 1 ATOM 1008 C CG . ARG A 1 127 ? 8.494 5.015 14.877 1.00 228.78 ? 146 ARG A CG 1 ATOM 1009 C CD . ARG A 1 127 ? 9.526 4.417 13.969 1.00 246.89 ? 146 ARG A CD 1 ATOM 1010 N NE . ARG A 1 127 ? 9.098 4.425 12.582 1.00 255.65 ? 146 ARG A NE 1 ATOM 1011 C CZ . ARG A 1 127 ? 9.907 4.181 11.573 1.00 239.56 ? 146 ARG A CZ 1 ATOM 1012 N NH1 . ARG A 1 127 ? 11.195 3.947 11.790 1.00 236.89 ? 146 ARG A NH1 1 ATOM 1013 N NH2 . ARG A 1 127 ? 9.445 4.171 10.331 1.00 229.95 ? 146 ARG A NH2 1 ATOM 1014 N N . GLU A 1 128 ? 8.447 9.382 16.630 1.00 229.30 ? 147 GLU A N 1 ATOM 1015 C CA . GLU A 1 128 ? 9.046 10.424 17.472 1.00 298.79 ? 147 GLU A CA 1 ATOM 1016 C C . GLU A 1 128 ? 8.184 10.783 18.691 1.00 300.00 ? 147 GLU A C 1 ATOM 1017 O O . GLU A 1 128 ? 8.664 11.445 19.614 1.00 300.00 ? 147 GLU A O 1 ATOM 1018 C CB . GLU A 1 128 ? 9.392 11.666 16.638 1.00 259.69 ? 147 GLU A CB 1 ATOM 1019 C CG . GLU A 1 128 ? 10.705 11.539 15.884 1.00 230.49 ? 147 GLU A CG 1 ATOM 1020 C CD . GLU A 1 128 ? 10.636 10.807 14.558 1.00 205.47 ? 147 GLU A CD 1 ATOM 1021 O OE1 . GLU A 1 128 ? 10.518 9.560 14.563 1.00 178.39 ? 147 GLU A OE1 1 ATOM 1022 O OE2 . GLU A 1 128 ? 10.724 11.484 13.508 1.00 227.59 ? 147 GLU A OE2 1 ATOM 1023 N N . ASP A 1 129 ? 6.915 10.338 18.685 1.00 300.00 ? 148 ASP A N 1 ATOM 1024 C CA . ASP A 1 129 ? 5.955 10.514 19.772 1.00 300.00 ? 148 ASP A CA 1 ATOM 1025 C C . ASP A 1 129 ? 5.863 9.189 20.569 1.00 300.00 ? 148 ASP A C 1 ATOM 1026 O O . ASP A 1 129 ? 5.077 9.097 21.519 1.00 300.00 ? 148 ASP A O 1 ATOM 1027 C CB . ASP A 1 129 ? 4.581 10.935 19.210 1.00 300.00 ? 148 ASP A CB 1 ATOM 1028 C CG . ASP A 1 129 ? 4.613 12.230 18.421 1.00 300.00 ? 148 ASP A CG 1 ATOM 1029 O OD1 . ASP A 1 129 ? 4.632 13.307 19.052 1.00 300.00 ? 148 ASP A OD1 1 ATOM 1030 O OD2 . ASP A 1 129 ? 4.612 12.164 17.172 1.00 282.28 ? 148 ASP A OD2 1 ATOM 1031 N N . GLU A 1 130 ? 6.698 8.172 20.171 1.00 300.00 ? 149 GLU A N 1 ATOM 1032 C CA . GLU A 1 130 ? 6.808 6.826 20.763 1.00 300.00 ? 149 GLU A CA 1 ATOM 1033 C C . GLU A 1 130 ? 8.080 6.571 21.607 1.00 300.00 ? 149 GLU A C 1 ATOM 1034 O O . GLU A 1 130 ? 8.265 7.286 22.594 1.00 300.00 ? 149 GLU A O 1 ATOM 1035 C CB . GLU A 1 130 ? 6.529 5.697 19.748 1.00 300.00 ? 149 GLU A CB 1 ATOM 1036 C CG . GLU A 1 130 ? 5.065 5.567 19.363 1.00 300.00 ? 149 GLU A CG 1 ATOM 1037 C CD . GLU A 1 130 ? 4.782 4.569 18.259 1.00 299.73 ? 149 GLU A CD 1 ATOM 1038 O OE1 . GLU A 1 130 ? 4.776 3.350 18.546 1.00 298.79 ? 149 GLU A OE1 1 ATOM 1039 O OE2 . GLU A 1 130 ? 4.546 5.006 17.110 1.00 291.30 ? 149 GLU A OE2 1 ATOM 1040 N N . GLU A 1 131 ? 8.911 5.523 21.296 1.00 145.03 ? 150 GLU A N 1 ATOM 1041 C CA . GLU A 1 131 ? 10.041 5.186 22.177 1.00 146.59 ? 150 GLU A CA 1 ATOM 1042 C C . GLU A 1 131 ? 11.524 5.130 21.638 1.00 137.14 ? 150 GLU A C 1 ATOM 1043 O O . GLU A 1 131 ? 12.180 6.135 21.893 1.00 141.86 ? 150 GLU A O 1 ATOM 1044 C CB . GLU A 1 131 ? 9.691 4.069 23.185 1.00 138.01 ? 150 GLU A CB 1 ATOM 1045 C CG . GLU A 1 131 ? 8.537 4.348 24.149 1.00 151.62 ? 150 GLU A CG 1 ATOM 1046 C CD . GLU A 1 131 ? 7.125 4.255 23.593 1.00 153.08 ? 150 GLU A CD 1 ATOM 1047 O OE1 . GLU A 1 131 ? 6.812 3.258 22.902 1.00 142.14 ? 150 GLU A OE1 1 ATOM 1048 O OE2 . GLU A 1 131 ? 6.332 5.193 23.838 1.00 166.05 ? 150 GLU A OE2 1 ATOM 1049 N N . LEU A 1 132 ? 12.187 4.008 21.200 1.00 194.92 ? 151 LEU A N 1 ATOM 1050 C CA . LEU A 1 132 ? 11.981 2.706 20.534 1.00 181.03 ? 151 LEU A CA 1 ATOM 1051 C C . LEU A 1 132 ? 11.791 2.918 19.037 1.00 171.62 ? 151 LEU A C 1 ATOM 1052 O O . LEU A 1 132 ? 11.060 2.197 18.355 1.00 165.10 ? 151 LEU A O 1 ATOM 1053 C CB . LEU A 1 132 ? 10.993 1.701 21.168 1.00 185.01 ? 151 LEU A CB 1 ATOM 1054 C CG . LEU A 1 132 ? 11.358 1.095 22.539 1.00 195.03 ? 151 LEU A CG 1 ATOM 1055 C CD1 . LEU A 1 132 ? 10.185 0.334 23.123 1.00 202.47 ? 151 LEU A CD1 1 ATOM 1056 C CD2 . LEU A 1 132 ? 12.557 0.165 22.457 1.00 186.88 ? 151 LEU A CD2 1 ATOM 1057 N N . SER A 1 133 ? 12.499 3.937 18.543 1.00 109.25 ? 152 SER A N 1 ATOM 1058 C CA . SER A 1 133 ? 12.489 4.401 17.167 1.00 106.25 ? 152 SER A CA 1 ATOM 1059 C C . SER A 1 133 ? 13.878 4.273 16.540 1.00 103.12 ? 152 SER A C 1 ATOM 1060 O O . SER A 1 133 ? 14.851 4.068 17.270 1.00 103.57 ? 152 SER A O 1 ATOM 1061 C CB . SER A 1 133 ? 12.021 5.852 17.129 1.00 111.19 ? 152 SER A CB 1 ATOM 1062 O OG . SER A 1 133 ? 12.887 6.704 17.863 1.00 115.76 ? 152 SER A OG 1 ATOM 1063 N N . CYS A 1 134 ? 13.970 4.403 15.192 1.00 100.34 ? 153 CYS A N 1 ATOM 1064 C CA . CYS A 1 134 ? 15.229 4.317 14.436 1.00 98.39 ? 153 CYS A CA 1 ATOM 1065 C C . CYS A 1 134 ? 16.267 5.283 14.979 1.00 101.52 ? 153 CYS A C 1 ATOM 1066 O O . CYS A 1 134 ? 15.964 6.463 15.177 1.00 105.74 ? 153 CYS A O 1 ATOM 1067 C CB . CYS A 1 134 ? 15.005 4.534 12.942 1.00 97.08 ? 153 CYS A CB 1 ATOM 1068 S SG . CYS A 1 134 ? 13.933 3.303 12.155 1.00 93.65 ? 153 CYS A SG 1 ATOM 1069 N N . ASP A 1 135 ? 17.482 4.777 15.236 1.00 100.22 ? 154 ASP A N 1 ATOM 1070 C CA . ASP A 1 135 ? 18.579 5.584 15.759 1.00 103.22 ? 154 ASP A CA 1 ATOM 1071 C C . ASP A 1 135 ? 18.985 6.668 14.760 1.00 105.87 ? 154 ASP A C 1 ATOM 1072 O O . ASP A 1 135 ? 19.076 7.837 15.138 1.00 110.41 ? 154 ASP A O 1 ATOM 1073 C CB . ASP A 1 135 ? 19.777 4.699 16.138 1.00 101.44 ? 154 ASP A CB 1 ATOM 1074 C CG . ASP A 1 135 ? 20.865 5.379 16.953 1.00 104.49 ? 154 ASP A CG 1 ATOM 1075 O OD1 . ASP A 1 135 ? 20.669 6.548 17.357 1.00 108.58 ? 154 ASP A OD1 1 ATOM 1076 O OD2 . ASP A 1 135 ? 21.903 4.737 17.204 1.00 103.34 ? 154 ASP A OD2 1 ATOM 1077 N N . HIS A 1 136 ? 19.190 6.286 13.487 1.00 103.67 ? 155 HIS A N 1 ATOM 1078 C CA . HIS A 1 136 ? 19.577 7.224 12.439 1.00 107.11 ? 155 HIS A CA 1 ATOM 1079 C C . HIS A 1 136 ? 18.465 7.479 11.430 1.00 107.53 ? 155 HIS A C 1 ATOM 1080 O O . HIS A 1 136 ? 17.721 8.448 11.583 1.00 111.00 ? 155 HIS A O 1 ATOM 1081 C CB . HIS A 1 136 ? 20.875 6.780 11.743 1.00 106.54 ? 155 HIS A CB 1 ATOM 1082 C CG . HIS A 1 136 ? 22.102 6.885 12.594 1.00 107.63 ? 155 HIS A CG 1 ATOM 1083 N ND1 . HIS A 1 136 ? 23.327 6.450 12.132 1.00 107.59 ? 155 HIS A ND1 1 ATOM 1084 C CD2 . HIS A 1 136 ? 22.256 7.376 13.848 1.00 109.61 ? 155 HIS A CD2 1 ATOM 1085 C CE1 . HIS A 1 136 ? 24.184 6.693 13.109 1.00 108.64 ? 155 HIS A CE1 1 ATOM 1086 N NE2 . HIS A 1 136 ? 23.583 7.240 14.165 1.00 110.29 ? 155 HIS A NE2 1 ATOM 1087 N N . TYR A 1 137 ? 18.354 6.620 10.404 1.00 104.65 ? 156 TYR A N 1 ATOM 1088 C CA . TYR A 1 137 ? 17.367 6.775 9.342 1.00 105.15 ? 156 TYR A CA 1 ATOM 1089 C C . TYR A 1 137 ? 16.191 5.837 9.475 1.00 101.17 ? 156 TYR A C 1 ATOM 1090 O O . TYR A 1 137 ? 16.360 4.666 9.812 1.00 97.78 ? 156 TYR A O 1 ATOM 1091 C CB . TYR A 1 137 ? 18.009 6.597 7.955 1.00 106.41 ? 156 TYR A CB 1 ATOM 1092 C CG . TYR A 1 137 ? 19.201 7.489 7.688 1.00 111.30 ? 156 TYR A CG 1 ATOM 1093 C CD1 . TYR A 1 137 ? 19.064 8.874 7.639 1.00 117.30 ? 156 TYR A CD1 1 ATOM 1094 C CD2 . TYR A 1 137 ? 20.455 6.948 7.421 1.00 111.50 ? 156 TYR A CD2 1 ATOM 1095 C CE1 . TYR A 1 137 ? 20.155 9.701 7.377 1.00 122.69 ? 156 TYR A CE1 1 ATOM 1096 C CE2 . TYR A 1 137 ? 21.552 7.764 7.148 1.00 116.54 ? 156 TYR A CE2 1 ATOM 1097 C CZ . TYR A 1 137 ? 21.398 9.141 7.129 1.00 122.04 ? 156 TYR A CZ 1 ATOM 1098 O OH . TYR A 1 137 ? 22.475 9.951 6.863 1.00 128.03 ? 156 TYR A OH 1 ATOM 1099 N N . CYS A 1 138 ? 15.002 6.357 9.163 1.00 102.36 ? 157 CYS A N 1 ATOM 1100 C CA . CYS A 1 138 ? 13.755 5.614 9.152 1.00 99.20 ? 157 CYS A CA 1 ATOM 1101 C C . CYS A 1 138 ? 13.253 5.536 7.723 1.00 99.65 ? 157 CYS A C 1 ATOM 1102 O O . CYS A 1 138 ? 13.197 6.564 7.042 1.00 103.51 ? 157 CYS A O 1 ATOM 1103 C CB . CYS A 1 138 ? 12.723 6.279 10.048 1.00 100.78 ? 157 CYS A CB 1 ATOM 1104 S SG . CYS A 1 138 ? 11.178 5.367 10.139 1.00 97.62 ? 157 CYS A SG 1 ATOM 1105 N N . HIS A 1 139 ? 12.846 4.339 7.278 1.00 96.48 ? 158 HIS A N 1 ATOM 1106 C CA . HIS A 1 139 ? 12.326 4.160 5.924 1.00 97.23 ? 158 HIS A CA 1 ATOM 1107 C C . HIS A 1 139 ? 10.949 3.528 5.977 1.00 94.90 ? 158 HIS A C 1 ATOM 1108 O O . HIS A 1 139 ? 10.803 2.420 6.491 1.00 91.81 ? 158 HIS A O 1 ATOM 1109 C CB . HIS A 1 139 ? 13.275 3.308 5.062 1.00 97.36 ? 158 HIS A CB 1 ATOM 1110 C CG . HIS A 1 139 ? 14.689 3.796 5.035 1.00 100.01 ? 158 HIS A CG 1 ATOM 1111 N ND1 . HIS A 1 139 ? 15.131 4.678 4.067 1.00 104.38 ? 158 HIS A ND1 1 ATOM 1112 C CD2 . HIS A 1 139 ? 15.720 3.497 5.857 1.00 98.63 ? 158 HIS A CD2 1 ATOM 1113 C CE1 . HIS A 1 139 ? 16.408 4.892 4.333 1.00 106.19 ? 158 HIS A CE1 1 ATOM 1114 N NE2 . HIS A 1 139 ? 16.806 4.205 5.402 1.00 102.51 ? 158 HIS A NE2 1 ATOM 1115 N N . ASN A 1 140 ? 9.940 4.228 5.450 1.00 96.87 ? 159 ASN A N 1 ATOM 1116 C CA . ASN A 1 140 ? 8.578 3.712 5.427 1.00 94.89 ? 159 ASN A CA 1 ATOM 1117 C C . ASN A 1 140 ? 8.278 2.986 4.128 1.00 94.62 ? 159 ASN A C 1 ATOM 1118 O O . ASN A 1 140 ? 8.725 3.415 3.065 1.00 97.76 ? 159 ASN A O 1 ATOM 1119 C CB . ASN A 1 140 ? 7.559 4.838 5.621 1.00 97.70 ? 159 ASN A CB 1 ATOM 1120 C CG . ASN A 1 140 ? 6.139 4.338 5.746 1.00 95.96 ? 159 ASN A CG 1 ATOM 1121 O OD1 . ASN A 1 140 ? 5.857 3.417 6.509 1.00 92.92 ? 159 ASN A OD1 1 ATOM 1122 N ND2 . ASN A 1 140 ? 5.220 4.912 4.981 1.00 98.17 ? 159 ASN A ND2 1 ATOM 1123 N N . TYR A 1 141 ? 7.493 1.906 4.214 1.00 91.72 ? 160 TYR A N 1 ATOM 1124 C CA . TYR A 1 141 ? 7.005 1.158 3.059 1.00 91.99 ? 160 TYR A CA 1 ATOM 1125 C C . TYR A 1 141 ? 5.594 0.647 3.322 1.00 90.02 ? 160 TYR A C 1 ATOM 1126 O O . TYR A 1 141 ? 5.110 0.750 4.444 1.00 88.44 ? 160 TYR A O 1 ATOM 1127 C CB . TYR A 1 141 ? 7.966 0.040 2.613 1.00 92.20 ? 160 TYR A CB 1 ATOM 1128 C CG . TYR A 1 141 ? 8.120 -1.105 3.588 1.00 89.73 ? 160 TYR A CG 1 ATOM 1129 C CD1 . TYR A 1 141 ? 7.227 -2.173 3.587 1.00 88.92 ? 160 TYR A CD1 1 ATOM 1130 C CD2 . TYR A 1 141 ? 9.208 -1.168 4.450 1.00 89.25 ? 160 TYR A CD2 1 ATOM 1131 C CE1 . TYR A 1 141 ? 7.379 -3.244 4.465 1.00 88.03 ? 160 TYR A CE1 1 ATOM 1132 C CE2 . TYR A 1 141 ? 9.389 -2.249 5.310 1.00 88.10 ? 160 TYR A CE2 1 ATOM 1133 C CZ . TYR A 1 141 ? 8.459 -3.274 5.331 1.00 87.81 ? 160 TYR A CZ 1 ATOM 1134 O OH . TYR A 1 141 ? 8.621 -4.327 6.198 1.00 88.00 ? 160 TYR A OH 1 ATOM 1135 N N . ILE A 1 142 ? 4.935 0.096 2.296 1.00 90.66 ? 161 ILE A N 1 ATOM 1136 C CA . ILE A 1 142 ? 3.577 -0.428 2.426 1.00 89.35 ? 161 ILE A CA 1 ATOM 1137 C C . ILE A 1 142 ? 3.564 -1.710 3.267 1.00 87.25 ? 161 ILE A C 1 ATOM 1138 O O . ILE A 1 142 ? 4.078 -2.740 2.833 1.00 87.85 ? 161 ILE A O 1 ATOM 1139 C CB . ILE A 1 142 ? 2.880 -0.589 1.043 1.00 91.41 ? 161 ILE A CB 1 ATOM 1140 C CG1 . ILE A 1 142 ? 2.795 0.769 0.304 1.00 94.47 ? 161 ILE A CG1 1 ATOM 1141 C CG2 . ILE A 1 142 ? 1.488 -1.227 1.197 1.00 89.94 ? 161 ILE A CG2 1 ATOM 1142 C CD1 . ILE A 1 142 ? 2.481 0.697 -1.191 1.00 97.75 ? 161 ILE A CD1 1 ATOM 1143 N N . GLY A 1 143 ? 2.993 -1.632 4.477 1.00 85.91 ? 162 GLY A N 1 ATOM 1144 C CA . GLY A 1 143 ? 2.882 -2.785 5.370 1.00 85.21 ? 162 GLY A CA 1 ATOM 1145 C C . GLY A 1 143 ? 3.909 -2.836 6.488 1.00 84.97 ? 162 GLY A C 1 ATOM 1146 O O . GLY A 1 143 ? 3.783 -3.680 7.377 1.00 85.32 ? 162 GLY A O 1 ATOM 1147 N N . GLY A 1 144 ? 4.921 -1.961 6.453 1.00 85.20 ? 163 GLY A N 1 ATOM 1148 C CA . GLY A 1 144 ? 5.934 -1.946 7.499 1.00 85.03 ? 163 GLY A CA 1 ATOM 1149 C C . GLY A 1 144 ? 6.898 -0.789 7.365 1.00 85.74 ? 163 GLY A C 1 ATOM 1150 O O . GLY A 1 144 ? 6.580 0.233 6.761 1.00 86.91 ? 163 GLY A O 1 ATOM 1151 N N . TYR A 1 145 ? 8.070 -0.947 7.975 1.00 85.82 ? 164 TYR A N 1 ATOM 1152 C CA . TYR A 1 145 ? 9.151 0.029 7.970 1.00 86.72 ? 164 TYR A CA 1 ATOM 1153 C C . TYR A 1 145 ? 10.444 -0.660 8.383 1.00 86.47 ? 164 TYR A C 1 ATOM 1154 O O . TYR A 1 145 ? 10.415 -1.790 8.877 1.00 86.03 ? 164 TYR A O 1 ATOM 1155 C CB . TYR A 1 145 ? 8.838 1.207 8.922 1.00 88.02 ? 164 TYR A CB 1 ATOM 1156 C CG . TYR A 1 145 ? 9.049 0.898 10.390 1.00 87.99 ? 164 TYR A CG 1 ATOM 1157 C CD1 . TYR A 1 145 ? 8.108 0.172 11.112 1.00 87.85 ? 164 TYR A CD1 1 ATOM 1158 C CD2 . TYR A 1 145 ? 10.233 1.244 11.032 1.00 88.89 ? 164 TYR A CD2 1 ATOM 1159 C CE1 . TYR A 1 145 ? 8.291 -0.104 12.466 1.00 88.98 ? 164 TYR A CE1 1 ATOM 1160 C CE2 . TYR A 1 145 ? 10.432 0.970 12.383 1.00 89.77 ? 164 TYR A CE2 1 ATOM 1161 C CZ . TYR A 1 145 ? 9.458 0.296 13.097 1.00 90.07 ? 164 TYR A CZ 1 ATOM 1162 O OH . TYR A 1 145 ? 9.660 0.015 14.426 1.00 91.70 ? 164 TYR A OH 1 ATOM 1163 N N . TYR A 1 146 ? 11.571 0.041 8.216 1.00 87.63 ? 165 TYR A N 1 ATOM 1164 C CA . TYR A 1 146 ? 12.889 -0.419 8.637 1.00 87.85 ? 165 TYR A CA 1 ATOM 1165 C C . TYR A 1 146 ? 13.816 0.759 8.892 1.00 89.30 ? 165 TYR A C 1 ATOM 1166 O O . TYR A 1 146 ? 13.553 1.883 8.449 1.00 90.95 ? 165 TYR A O 1 ATOM 1167 C CB . TYR A 1 146 ? 13.509 -1.434 7.651 1.00 88.79 ? 165 TYR A CB 1 ATOM 1168 C CG . TYR A 1 146 ? 13.852 -0.858 6.296 1.00 90.88 ? 165 TYR A CG 1 ATOM 1169 C CD1 . TYR A 1 146 ? 12.921 -0.858 5.263 1.00 91.93 ? 165 TYR A CD1 1 ATOM 1170 C CD2 . TYR A 1 146 ? 15.118 -0.341 6.035 1.00 92.95 ? 165 TYR A CD2 1 ATOM 1171 C CE1 . TYR A 1 146 ? 13.229 -0.333 4.012 1.00 94.76 ? 165 TYR A CE1 1 ATOM 1172 C CE2 . TYR A 1 146 ? 15.438 0.191 4.787 1.00 96.05 ? 165 TYR A CE2 1 ATOM 1173 C CZ . TYR A 1 146 ? 14.489 0.186 3.776 1.00 97.46 ? 165 TYR A CZ 1 ATOM 1174 O OH . TYR A 1 146 ? 14.765 0.699 2.534 1.00 101.08 ? 165 TYR A OH 1 ATOM 1175 N N . CYS A 1 147 ? 14.908 0.481 9.606 1.00 89.43 ? 166 CYS A N 1 ATOM 1176 C CA . CYS A 1 147 ? 15.935 1.454 9.936 1.00 91.02 ? 166 CYS A CA 1 ATOM 1177 C C . CYS A 1 147 ? 17.188 1.174 9.122 1.00 92.39 ? 166 CYS A C 1 ATOM 1178 O O . CYS A 1 147 ? 17.426 0.038 8.704 1.00 92.35 ? 166 CYS A O 1 ATOM 1179 C CB . CYS A 1 147 ? 16.246 1.436 11.432 1.00 90.87 ? 166 CYS A CB 1 ATOM 1180 S SG . CYS A 1 147 ? 14.792 1.495 12.513 1.00 90.35 ? 166 CYS A SG 1 ATOM 1181 N N . SER A 1 148 ? 17.999 2.214 8.922 1.00 94.59 ? 167 SER A N 1 ATOM 1182 C CA . SER A 1 148 ? 19.308 2.135 8.281 1.00 96.97 ? 167 SER A CA 1 ATOM 1183 C C . SER A 1 148 ? 20.235 3.122 8.989 1.00 98.84 ? 167 SER A C 1 ATOM 1184 O O . SER A 1 148 ? 19.765 3.937 9.791 1.00 98.91 ? 167 SER A O 1 ATOM 1185 C CB . SER A 1 148 ? 19.228 2.368 6.774 1.00 99.72 ? 167 SER A CB 1 ATOM 1186 O OG . SER A 1 148 ? 19.272 3.741 6.425 1.00 102.49 ? 167 SER A OG 1 ATOM 1187 N N . CYS A 1 149 ? 21.542 3.029 8.734 1.00 101.07 ? 168 CYS A N 1 ATOM 1188 C CA . CYS A 1 149 ? 22.517 3.859 9.428 1.00 103.09 ? 168 CYS A CA 1 ATOM 1189 C C . CYS A 1 149 ? 23.318 4.788 8.539 1.00 107.64 ? 168 CYS A C 1 ATOM 1190 O O . CYS A 1 149 ? 23.407 4.570 7.328 1.00 109.88 ? 168 CYS A O 1 ATOM 1191 C CB . CYS A 1 149 ? 23.429 2.981 10.277 1.00 101.77 ? 168 CYS A CB 1 ATOM 1192 S SG . CYS A 1 149 ? 22.553 1.974 11.498 1.00 99.18 ? 168 CYS A SG 1 ATOM 1193 N N . ARG A 1 150 ? 23.938 5.813 9.163 1.00 110.12 ? 169 ARG A N 1 ATOM 1194 C CA . ARG A 1 150 ? 24.823 6.764 8.492 1.00 115.65 ? 169 ARG A CA 1 ATOM 1195 C C . ARG A 1 150 ? 26.073 6.019 8.047 1.00 116.79 ? 169 ARG A C 1 ATOM 1196 O O . ARG A 1 150 ? 26.439 5.010 8.659 1.00 113.56 ? 169 ARG A O 1 ATOM 1197 C CB . ARG A 1 150 ? 25.243 7.897 9.441 1.00 118.68 ? 169 ARG A CB 1 ATOM 1198 C CG . ARG A 1 150 ? 24.138 8.869 9.816 1.00 120.20 ? 169 ARG A CG 1 ATOM 1199 C CD . ARG A 1 150 ? 24.710 10.052 10.568 1.00 125.57 ? 169 ARG A CD 1 ATOM 1200 N NE . ARG A 1 150 ? 23.879 10.432 11.711 1.00 125.83 ? 169 ARG A NE 1 ATOM 1201 C CZ . ARG A 1 150 ? 24.329 10.571 12.955 1.00 126.31 ? 169 ARG A CZ 1 ATOM 1202 N NH1 . ARG A 1 150 ? 25.612 10.368 13.231 1.00 125.52 ? 169 ARG A NH1 1 ATOM 1203 N NH2 . ARG A 1 150 ? 23.501 10.918 13.931 1.00 127.51 ? 169 ARG A NH2 1 ATOM 1204 N N . PHE A 1 151 ? 26.730 6.520 6.992 1.00 122.23 ? 170 PHE A N 1 ATOM 1205 C CA . PHE A 1 151 ? 27.957 5.934 6.463 1.00 125.08 ? 170 PHE A CA 1 ATOM 1206 C C . PHE A 1 151 ? 29.003 5.826 7.573 1.00 124.01 ? 170 PHE A C 1 ATOM 1207 O O . PHE A 1 151 ? 29.238 6.797 8.294 1.00 125.26 ? 170 PHE A O 1 ATOM 1208 C CB . PHE A 1 151 ? 28.485 6.768 5.286 1.00 132.37 ? 170 PHE A CB 1 ATOM 1209 C CG . PHE A 1 151 ? 29.694 6.175 4.604 1.00 136.54 ? 170 PHE A CG 1 ATOM 1210 C CD1 . PHE A 1 151 ? 29.552 5.188 3.637 1.00 138.18 ? 170 PHE A CD1 1 ATOM 1211 C CD2 . PHE A 1 151 ? 30.974 6.612 4.920 1.00 140.20 ? 170 PHE A CD2 1 ATOM 1212 C CE1 . PHE A 1 151 ? 30.671 4.642 3.004 1.00 143.84 ? 170 PHE A CE1 1 ATOM 1213 C CE2 . PHE A 1 151 ? 32.093 6.060 4.293 1.00 144.98 ? 170 PHE A CE2 1 ATOM 1214 C CZ . PHE A 1 151 ? 31.934 5.080 3.337 1.00 147.15 ? 170 PHE A CZ 1 ATOM 1215 N N . GLY A 1 152 ? 29.584 4.632 7.740 1.00 122.42 ? 171 GLY A N 1 ATOM 1216 C CA . GLY A 1 152 ? 30.580 4.375 8.778 1.00 121.57 ? 171 GLY A CA 1 ATOM 1217 C C . GLY A 1 152 ? 29.973 3.711 10.019 1.00 116.08 ? 171 GLY A C 1 ATOM 1218 O O . GLY A 1 152 ? 30.712 3.382 10.947 1.00 115.57 ? 171 GLY A O 1 ATOM 1219 N N . TYR A 1 153 ? 28.641 3.517 10.039 1.00 112.71 ? 172 TYR A N 1 ATOM 1220 C CA . TYR A 1 153 ? 27.935 2.871 11.148 1.00 108.39 ? 172 TYR A CA 1 ATOM 1221 C C . TYR A 1 153 ? 27.388 1.515 10.724 1.00 106.77 ? 172 TYR A C 1 ATOM 1222 O O . TYR A 1 153 ? 27.196 1.269 9.531 1.00 108.27 ? 172 TYR A O 1 ATOM 1223 C CB . TYR A 1 153 ? 26.789 3.749 11.663 1.00 106.76 ? 172 TYR A CB 1 ATOM 1224 C CG . TYR A 1 153 ? 27.219 4.958 12.460 1.00 109.11 ? 172 TYR A CG 1 ATOM 1225 C CD1 . TYR A 1 153 ? 27.646 6.121 11.824 1.00 113.27 ? 172 TYR A CD1 1 ATOM 1226 C CD2 . TYR A 1 153 ? 27.119 4.973 13.847 1.00 107.97 ? 172 TYR A CD2 1 ATOM 1227 C CE1 . TYR A 1 153 ? 28.011 7.252 12.552 1.00 116.18 ? 172 TYR A CE1 1 ATOM 1228 C CE2 . TYR A 1 153 ? 27.475 6.100 14.586 1.00 111.02 ? 172 TYR A CE2 1 ATOM 1229 C CZ . TYR A 1 153 ? 27.924 7.237 13.934 1.00 115.12 ? 172 TYR A CZ 1 ATOM 1230 O OH . TYR A 1 153 ? 28.280 8.349 14.659 1.00 119.19 ? 172 TYR A OH 1 ATOM 1231 N N . ILE A 1 154 ? 27.127 0.640 11.707 1.00 104.40 ? 173 ILE A N 1 ATOM 1232 C CA . ILE A 1 154 ? 26.602 -0.705 11.477 1.00 103.71 ? 173 ILE A CA 1 ATOM 1233 C C . ILE A 1 154 ? 25.279 -0.875 12.217 1.00 100.35 ? 173 ILE A C 1 ATOM 1234 O O . ILE A 1 154 ? 25.211 -0.595 13.417 1.00 99.21 ? 173 ILE A O 1 ATOM 1235 C CB . ILE A 1 154 ? 27.642 -1.792 11.888 1.00 105.91 ? 173 ILE A CB 1 ATOM 1236 C CG1 . ILE A 1 154 ? 28.987 -1.604 11.143 1.00 110.24 ? 173 ILE A CG1 1 ATOM 1237 C CG2 . ILE A 1 154 ? 27.083 -3.212 11.679 1.00 106.56 ? 173 ILE A CG2 1 ATOM 1238 C CD1 . ILE A 1 154 ? 30.214 -2.195 11.836 1.00 112.68 ? 173 ILE A CD1 1 ATOM 1239 N N . LEU A 1 155 ? 24.237 -1.353 11.511 1.00 99.30 ? 174 LEU A N 1 ATOM 1240 C CA . LEU A 1 155 ? 22.939 -1.609 12.127 1.00 96.69 ? 174 LEU A CA 1 ATOM 1241 C C . LEU A 1 155 ? 23.069 -2.799 13.069 1.00 97.36 ? 174 LEU A C 1 ATOM 1242 O O . LEU A 1 155 ? 23.546 -3.864 12.668 1.00 99.71 ? 174 LEU A O 1 ATOM 1243 C CB . LEU A 1 155 ? 21.840 -1.832 11.072 1.00 96.06 ? 174 LEU A CB 1 ATOM 1244 C CG . LEU A 1 155 ? 20.390 -1.850 11.579 1.00 93.72 ? 174 LEU A CG 1 ATOM 1245 C CD1 . LEU A 1 155 ? 19.943 -0.481 12.080 1.00 92.54 ? 174 LEU A CD1 1 ATOM 1246 C CD2 . LEU A 1 155 ? 19.450 -2.307 10.491 1.00 93.28 ? 174 LEU A CD2 1 ATOM 1247 N N . HIS A 1 156 ? 22.699 -2.587 14.337 1.00 96.35 ? 175 HIS A N 1 ATOM 1248 C CA . HIS A 1 156 ? 22.794 -3.585 15.399 1.00 97.85 ? 175 HIS A CA 1 ATOM 1249 C C . HIS A 1 156 ? 21.783 -4.729 15.237 1.00 98.44 ? 175 HIS A C 1 ATOM 1250 O O . HIS A 1 156 ? 20.887 -4.641 14.396 1.00 96.84 ? 175 HIS A O 1 ATOM 1251 C CB . HIS A 1 156 ? 22.676 -2.901 16.774 1.00 97.86 ? 175 HIS A CB 1 ATOM 1252 C CG . HIS A 1 156 ? 23.046 -3.776 17.933 1.00 100.51 ? 175 HIS A CG 1 ATOM 1253 N ND1 . HIS A 1 156 ? 24.247 -4.466 17.965 1.00 103.13 ? 175 HIS A ND1 1 ATOM 1254 C CD2 . HIS A 1 156 ? 22.356 -4.046 19.065 1.00 102.06 ? 175 HIS A CD2 1 ATOM 1255 C CE1 . HIS A 1 156 ? 24.248 -5.130 19.109 1.00 105.68 ? 175 HIS A CE1 1 ATOM 1256 N NE2 . HIS A 1 156 ? 23.133 -4.906 19.806 1.00 105.10 ? 175 HIS A NE2 1 ATOM 1257 N N . THR A 1 157 ? 21.940 -5.806 16.038 1.00 101.30 ? 176 THR A N 1 ATOM 1258 C CA . THR A 1 157 ? 21.075 -6.992 16.042 1.00 103.35 ? 176 THR A CA 1 ATOM 1259 C C . THR A 1 157 ? 19.617 -6.689 16.409 1.00 101.59 ? 176 THR A C 1 ATOM 1260 O O . THR A 1 157 ? 18.747 -7.529 16.176 1.00 102.84 ? 176 THR A O 1 ATOM 1261 C CB . THR A 1 157 ? 21.676 -8.116 16.897 1.00 108.21 ? 176 THR A CB 1 ATOM 1262 O OG1 . THR A 1 157 ? 22.007 -7.605 18.189 1.00 108.65 ? 176 THR A OG1 1 ATOM 1263 C CG2 . THR A 1 157 ? 22.896 -8.759 16.249 1.00 111.50 ? 176 THR A CG2 1 ATOM 1264 N N . ASP A 1 158 ? 19.347 -5.490 16.953 1.00 99.32 ? 177 ASP A N 1 ATOM 1265 C CA . ASP A 1 158 ? 17.999 -5.047 17.302 1.00 98.31 ? 177 ASP A CA 1 ATOM 1266 C C . ASP A 1 158 ? 17.290 -4.444 16.081 1.00 95.24 ? 177 ASP A C 1 ATOM 1267 O O . ASP A 1 158 ? 16.129 -4.041 16.188 1.00 94.44 ? 177 ASP A O 1 ATOM 1268 C CB . ASP A 1 158 ? 18.052 -4.023 18.455 1.00 99.08 ? 177 ASP A CB 1 ATOM 1269 C CG . ASP A 1 158 ? 18.879 -2.771 18.196 1.00 97.46 ? 177 ASP A CG 1 ATOM 1270 O OD1 . ASP A 1 158 ? 19.276 -2.542 17.029 1.00 95.06 ? 177 ASP A OD1 1 ATOM 1271 O OD2 . ASP A 1 158 ? 19.121 -2.016 19.155 1.00 98.93 ? 177 ASP A OD2 1 ATOM 1272 N N . ASN A 1 159 ? 18.021 -4.331 14.937 1.00 94.20 ? 178 ASN A N 1 ATOM 1273 C CA . ASN A 1 159 ? 17.568 -3.759 13.658 1.00 92.34 ? 178 ASN A CA 1 ATOM 1274 C C . ASN A 1 159 ? 17.124 -2.299 13.818 1.00 90.90 ? 178 ASN A C 1 ATOM 1275 O O . ASN A 1 159 ? 16.306 -1.809 13.034 1.00 89.67 ? 178 ASN A O 1 ATOM 1276 C CB . ASN A 1 159 ? 16.429 -4.603 13.051 1.00 92.25 ? 178 ASN A CB 1 ATOM 1277 C CG . ASN A 1 159 ? 16.796 -6.031 12.701 1.00 95.40 ? 178 ASN A CG 1 ATOM 1278 O OD1 . ASN A 1 159 ? 17.924 -6.336 12.329 1.00 97.48 ? 178 ASN A OD1 1 ATOM 1279 N ND2 . ASN A 1 159 ? 15.902 -6.986 12.764 1.00 97.62 ? 178 ASN A ND2 1 ATOM 1280 N N . ARG A 1 160 ? 17.670 -1.605 14.828 1.00 91.88 ? 179 ARG A N 1 ATOM 1281 C CA . ARG A 1 160 ? 17.251 -0.253 15.164 1.00 92.27 ? 179 ARG A CA 1 ATOM 1282 C C . ARG A 1 160 ? 18.407 0.706 15.455 1.00 93.70 ? 179 ARG A C 1 ATOM 1283 O O . ARG A 1 160 ? 18.452 1.798 14.880 1.00 94.34 ? 179 ARG A O 1 ATOM 1284 C CB . ARG A 1 160 ? 16.284 -0.346 16.355 1.00 93.80 ? 179 ARG A CB 1 ATOM 1285 C CG . ARG A 1 160 ? 15.570 0.942 16.721 1.00 95.72 ? 179 ARG A CG 1 ATOM 1286 C CD . ARG A 1 160 ? 14.524 0.731 17.808 1.00 98.29 ? 179 ARG A CD 1 ATOM 1287 N NE . ARG A 1 160 ? 15.056 0.025 18.978 1.00 100.32 ? 179 ARG A NE 1 ATOM 1288 C CZ . ARG A 1 160 ? 15.700 0.606 19.986 1.00 103.86 ? 179 ARG A CZ 1 ATOM 1289 N NH1 . ARG A 1 160 ? 15.909 1.918 19.983 1.00 105.41 ? 179 ARG A NH1 1 ATOM 1290 N NH2 . ARG A 1 160 ? 16.143 -0.120 21.003 1.00 105.78 ? 179 ARG A NH2 1 ATOM 1291 N N . THR A 1 161 ? 19.317 0.315 16.360 1.00 94.80 ? 180 THR A N 1 ATOM 1292 C CA . THR A 1 161 ? 20.451 1.151 16.751 1.00 96.24 ? 180 THR A CA 1 ATOM 1293 C C . THR A 1 161 ? 21.652 1.003 15.830 1.00 95.80 ? 180 THR A C 1 ATOM 1294 O O . THR A 1 161 ? 21.807 -0.026 15.168 1.00 94.74 ? 180 THR A O 1 ATOM 1295 C CB . THR A 1 161 ? 20.763 1.022 18.240 1.00 98.48 ? 180 THR A CB 1 ATOM 1296 O OG1 . THR A 1 161 ? 21.137 -0.324 18.525 1.00 98.38 ? 180 THR A OG1 1 ATOM 1297 C CG2 . THR A 1 161 ? 19.596 1.453 19.122 1.00 100.22 ? 180 THR A CG2 1 ATOM 1298 N N . CYS A 1 162 ? 22.490 2.050 15.779 1.00 97.43 ? 181 CYS A N 1 ATOM 1299 C CA . CYS A 1 162 ? 23.662 2.127 14.912 1.00 98.25 ? 181 CYS A CA 1 ATOM 1300 C C . CYS A 1 162 ? 24.970 2.153 15.691 1.00 100.00 ? 181 CYS A C 1 ATOM 1301 O O . CYS A 1 162 ? 25.314 3.169 16.300 1.00 102.04 ? 181 CYS A O 1 ATOM 1302 C CB . CYS A 1 162 ? 23.542 3.322 13.973 1.00 99.88 ? 181 CYS A CB 1 ATOM 1303 S SG . CYS A 1 162 ? 22.052 3.305 12.946 1.00 98.53 ? 181 CYS A SG 1 ATOM 1304 N N . ARG A 1 163 ? 25.696 1.029 15.668 1.00 99.87 ? 182 ARG A N 1 ATOM 1305 C CA . ARG A 1 163 ? 26.977 0.885 16.353 1.00 101.73 ? 182 ARG A CA 1 ATOM 1306 C C . ARG A 1 163 ? 28.147 1.163 15.406 1.00 103.60 ? 182 ARG A C 1 ATOM 1307 O O . ARG A 1 163 ? 27.940 1.386 14.212 1.00 103.86 ? 182 ARG A O 1 ATOM 1308 C CB . ARG A 1 163 ? 27.099 -0.511 16.997 1.00 101.71 ? 182 ARG A CB 1 ATOM 1309 C CG . ARG A 1 163 ? 27.230 -1.664 16.006 1.00 102.11 ? 182 ARG A CG 1 ATOM 1310 C CD . ARG A 1 163 ? 27.706 -2.929 16.688 1.00 104.47 ? 182 ARG A CD 1 ATOM 1311 N NE . ARG A 1 163 ? 28.095 -3.961 15.724 1.00 107.12 ? 182 ARG A NE 1 ATOM 1312 C CZ . ARG A 1 163 ? 29.311 -4.080 15.194 1.00 110.16 ? 182 ARG A CZ 1 ATOM 1313 N NH1 . ARG A 1 163 ? 30.272 -3.221 15.517 1.00 109.81 ? 182 ARG A NH1 1 ATOM 1314 N NH2 . ARG A 1 163 ? 29.572 -5.051 14.330 1.00 112.91 ? 182 ARG A NH2 1 ATOM 1315 N N . VAL A 1 164 ? 29.374 1.142 15.943 1.00 105.54 ? 183 VAL A N 1 ATOM 1316 C CA . VAL A 1 164 ? 30.603 1.347 15.176 1.00 108.12 ? 183 VAL A CA 1 ATOM 1317 C C . VAL A 1 164 ? 31.642 0.305 15.554 1.00 109.76 ? 183 VAL A C 1 ATOM 1318 O O . VAL A 1 164 ? 31.547 -0.321 16.614 1.00 109.16 ? 183 VAL A O 1 ATOM 1319 C CB . VAL A 1 164 ? 31.214 2.770 15.358 1.00 110.24 ? 183 VAL A CB 1 ATOM 1320 C CG1 . VAL A 1 164 ? 30.320 3.858 14.788 1.00 110.26 ? 183 VAL A CG1 1 ATOM 1321 C CG2 . VAL A 1 164 ? 31.585 3.058 16.814 1.00 110.49 ? 183 VAL A CG2 1 ATOM 1322 N N . GLU A 1 165 ? 32.673 0.176 14.713 1.00 139.57 ? 184 GLU A N 1 ATOM 1323 C CA . GLU A 1 165 ? 33.841 -0.626 15.018 1.00 138.85 ? 184 GLU A CA 1 ATOM 1324 C C . GLU A 1 165 ? 34.822 0.394 15.573 1.00 132.44 ? 184 GLU A C 1 ATOM 1325 O O . GLU A 1 165 ? 35.167 1.356 14.882 1.00 135.86 ? 184 GLU A O 1 ATOM 1326 C CB . GLU A 1 165 ? 34.390 -1.349 13.779 1.00 151.11 ? 184 GLU A CB 1 ATOM 1327 C CG . GLU A 1 165 ? 33.671 -2.653 13.466 1.00 158.24 ? 184 GLU A CG 1 ATOM 1328 C CD . GLU A 1 165 ? 33.524 -3.668 14.589 1.00 153.50 ? 184 GLU A CD 1 ATOM 1329 O OE1 . GLU A 1 165 ? 34.393 -3.713 15.490 1.00 147.70 ? 184 GLU A OE1 1 ATOM 1330 O OE2 . GLU A 1 165 ? 32.526 -4.423 14.563 1.00 157.29 ? 184 GLU A OE2 1 ATOM 1331 N N . CYS A 1 166 ? 35.176 0.253 16.855 1.00 124.28 ? 185 CYS A N 1 ATOM 1332 C CA . CYS A 1 166 ? 36.030 1.212 17.557 1.00 118.70 ? 185 CYS A CA 1 ATOM 1333 C C . CYS A 1 166 ? 37.153 0.531 18.342 1.00 116.18 ? 185 CYS A C 1 ATOM 1334 O O . CYS A 1 166 ? 37.586 1.045 19.378 1.00 109.97 ? 185 CYS A O 1 ATOM 1335 C CB . CYS A 1 166 ? 35.177 2.111 18.452 1.00 111.88 ? 185 CYS A CB 1 ATOM 1336 S SG . CYS A 1 166 ? 33.940 1.218 19.435 1.00 109.27 ? 185 CYS A SG 1 ATOM 1337 N N . SER A 1 167 ? 37.644 -0.611 17.831 1.00 122.57 ? 186 SER A N 1 ATOM 1338 C CA . SER A 1 167 ? 38.698 -1.385 18.483 1.00 122.56 ? 186 SER A CA 1 ATOM 1339 C C . SER A 1 167 ? 39.974 -1.534 17.648 1.00 130.47 ? 186 SER A C 1 ATOM 1340 O O . SER A 1 167 ? 40.985 -2.019 18.162 1.00 131.56 ? 186 SER A O 1 ATOM 1341 C CB . SER A 1 167 ? 38.158 -2.742 18.920 1.00 124.17 ? 186 SER A CB 1 ATOM 1342 O OG . SER A 1 167 ? 37.068 -2.570 19.810 1.00 117.88 ? 186 SER A OG 1 ATOM 1343 N N . ASP A 1 168 ? 39.938 -1.091 16.377 1.00 137.39 ? 187 ASP A N 1 ATOM 1344 C CA . ASP A 1 168 ? 41.078 -1.146 15.462 1.00 147.63 ? 187 ASP A CA 1 ATOM 1345 C C . ASP A 1 168 ? 42.038 0.008 15.739 1.00 144.42 ? 187 ASP A C 1 ATOM 1346 O O . ASP A 1 168 ? 42.158 0.944 14.943 1.00 149.18 ? 187 ASP A O 1 ATOM 1347 C CB . ASP A 1 168 ? 40.603 -1.162 13.997 1.00 158.72 ? 187 ASP A CB 1 ATOM 1348 C CG . ASP A 1 168 ? 39.834 -2.404 13.586 1.00 165.95 ? 187 ASP A CG 1 ATOM 1349 O OD1 . ASP A 1 168 ? 39.677 -3.317 14.429 1.00 162.79 ? 187 ASP A OD1 1 ATOM 1350 O OD2 . ASP A 1 168 ? 39.400 -2.470 12.417 1.00 177.19 ? 187 ASP A OD2 1 ATOM 1351 N N . ASN A 1 169 ? 42.711 -0.063 16.893 1.00 137.90 ? 188 ASN A N 1 ATOM 1352 C CA . ASN A 1 169 ? 43.658 0.951 17.345 1.00 135.19 ? 188 ASN A CA 1 ATOM 1353 C C . ASN A 1 169 ? 44.793 0.331 18.152 1.00 135.62 ? 188 ASN A C 1 ATOM 1354 O O . ASN A 1 169 ? 44.663 -0.787 18.657 1.00 135.86 ? 188 ASN A O 1 ATOM 1355 C CB . ASN A 1 169 ? 42.936 2.015 18.185 1.00 125.08 ? 188 ASN A CB 1 ATOM 1356 C CG . ASN A 1 169 ? 42.332 1.475 19.458 1.00 117.20 ? 188 ASN A CG 1 ATOM 1357 O OD1 . ASN A 1 169 ? 43.036 1.137 20.416 1.00 114.93 ? 188 ASN A OD1 1 ATOM 1358 N ND2 . ASN A 1 169 ? 41.015 1.363 19.487 1.00 113.78 ? 188 ASN A ND2 1 ATOM 1359 N N . LEU A 1 170 ? 45.887 1.087 18.303 1.00 136.62 ? 189 LEU A N 1 ATOM 1360 C CA . LEU A 1 170 ? 47.061 0.719 19.083 1.00 137.78 ? 189 LEU A CA 1 ATOM 1361 C C . LEU A 1 170 ? 47.915 1.955 19.275 1.00 137.29 ? 189 LEU A C 1 ATOM 1362 O O . LEU A 1 170 ? 48.493 2.469 18.315 1.00 145.06 ? 189 LEU A O 1 ATOM 1363 C CB . LEU A 1 170 ? 47.868 -0.424 18.430 1.00 149.16 ? 189 LEU A CB 1 ATOM 1364 C CG . LEU A 1 170 ? 49.035 -0.981 19.251 1.00 152.42 ? 189 LEU A CG 1 ATOM 1365 C CD1 . LEU A 1 170 ? 48.553 -1.633 20.537 1.00 145.20 ? 189 LEU A CD1 1 ATOM 1366 C CD2 . LEU A 1 170 ? 49.844 -1.964 18.441 1.00 165.91 ? 189 LEU A CD2 1 ATOM 1367 N N . PHE A 1 171 ? 47.968 2.445 20.514 1.00 129.69 ? 190 PHE A N 1 ATOM 1368 C CA . PHE A 1 171 ? 48.730 3.635 20.869 1.00 129.59 ? 190 PHE A CA 1 ATOM 1369 C C . PHE A 1 171 ? 50.092 3.208 21.394 1.00 134.29 ? 190 PHE A C 1 ATOM 1370 O O . PHE A 1 171 ? 50.182 2.553 22.433 1.00 131.40 ? 190 PHE A O 1 ATOM 1371 C CB . PHE A 1 171 ? 47.951 4.497 21.877 1.00 120.73 ? 190 PHE A CB 1 ATOM 1372 C CG . PHE A 1 171 ? 46.624 4.997 21.349 1.00 117.50 ? 190 PHE A CG 1 ATOM 1373 C CD1 . PHE A 1 171 ? 45.481 4.207 21.431 1.00 113.80 ? 190 PHE A CD1 1 ATOM 1374 C CD2 . PHE A 1 171 ? 46.518 6.254 20.766 1.00 120.02 ? 190 PHE A CD2 1 ATOM 1375 C CE1 . PHE A 1 171 ? 44.259 4.662 20.930 1.00 111.75 ? 190 PHE A CE1 1 ATOM 1376 C CE2 . PHE A 1 171 ? 45.291 6.714 20.276 1.00 118.00 ? 190 PHE A CE2 1 ATOM 1377 C CZ . PHE A 1 171 ? 44.171 5.915 20.362 1.00 113.82 ? 190 PHE A CZ 1 ATOM 1378 N N . THR A 1 172 ? 51.145 3.525 20.630 1.00 142.96 ? 191 THR A N 1 ATOM 1379 C CA . THR A 1 172 ? 52.524 3.142 20.944 1.00 149.89 ? 191 THR A CA 1 ATOM 1380 C C . THR A 1 172 ? 53.414 4.339 21.253 1.00 152.06 ? 191 THR A C 1 ATOM 1381 O O . THR A 1 172 ? 54.519 4.159 21.770 1.00 156.99 ? 191 THR A O 1 ATOM 1382 C CB . THR A 1 172 ? 53.109 2.291 19.809 1.00 161.53 ? 191 THR A CB 1 ATOM 1383 O OG1 . THR A 1 172 ? 53.124 3.064 18.607 1.00 167.78 ? 191 THR A OG1 1 ATOM 1384 C CG2 . THR A 1 172 ? 52.349 0.984 19.596 1.00 161.69 ? 191 THR A CG2 1 ATOM 1385 N N . GLN A 1 173 ? 52.945 5.554 20.925 1.00 149.57 ? 192 GLN A N 1 ATOM 1386 C CA . GLN A 1 173 ? 53.690 6.784 21.165 1.00 152.82 ? 192 GLN A CA 1 ATOM 1387 C C . GLN A 1 173 ? 53.757 7.118 22.650 1.00 146.27 ? 192 GLN A C 1 ATOM 1388 O O . GLN A 1 173 ? 52.882 6.697 23.405 1.00 137.64 ? 192 GLN A O 1 ATOM 1389 C CB . GLN A 1 173 ? 53.114 7.946 20.349 1.00 154.65 ? 192 GLN A CB 1 ATOM 1390 C CG . GLN A 1 173 ? 53.389 7.817 18.851 1.00 166.25 ? 192 GLN A CG 1 ATOM 1391 C CD . GLN A 1 173 ? 52.647 8.838 18.025 1.00 170.31 ? 192 GLN A CD 1 ATOM 1392 O OE1 . GLN A 1 173 ? 51.491 9.186 18.297 1.00 163.69 ? 192 GLN A OE1 1 ATOM 1393 N NE2 . GLN A 1 173 ? 53.283 9.310 16.964 1.00 183.15 ? 192 GLN A NE2 1 ATOM 1394 N N . ARG A 1 174 ? 54.808 7.851 23.070 1.00 151.39 ? 193 ARG A N 1 ATOM 1395 C CA . ARG A 1 174 ? 55.044 8.259 24.462 1.00 148.63 ? 193 ARG A CA 1 ATOM 1396 C C . ARG A 1 174 ? 53.872 9.025 25.067 1.00 140.87 ? 193 ARG A C 1 ATOM 1397 O O . ARG A 1 174 ? 53.612 8.910 26.266 1.00 137.05 ? 193 ARG A O 1 ATOM 1398 C CB . ARG A 1 174 ? 56.321 9.103 24.565 1.00 157.54 ? 193 ARG A CB 1 ATOM 1399 C CG . ARG A 1 174 ? 57.596 8.282 24.550 1.00 166.27 ? 193 ARG A CG 1 ATOM 1400 C CD . ARG A 1 174 ? 58.111 8.019 25.946 1.00 166.85 ? 193 ARG A CD 1 ATOM 1401 N NE . ARG A 1 174 ? 59.570 8.063 25.992 1.00 178.14 ? 193 ARG A NE 1 ATOM 1402 C CZ . ARG A 1 174 ? 60.274 8.560 27.004 1.00 182.33 ? 193 ARG A CZ 1 ATOM 1403 N NH1 . ARG A 1 174 ? 59.657 9.045 28.076 1.00 177.23 ? 193 ARG A NH1 1 ATOM 1404 N NH2 . ARG A 1 174 ? 61.598 8.553 26.964 1.00 192.79 ? 193 ARG A NH2 1 ATOM 1405 N N . THR A 1 175 ? 53.190 9.828 24.239 1.00 140.22 ? 194 THR A N 1 ATOM 1406 C CA . THR A 1 175 ? 52.035 10.632 24.630 1.00 135.05 ? 194 THR A CA 1 ATOM 1407 C C . THR A 1 175 ? 50.922 10.418 23.608 1.00 132.13 ? 194 THR A C 1 ATOM 1408 O O . THR A 1 175 ? 51.200 10.008 22.478 1.00 136.59 ? 194 THR A O 1 ATOM 1409 C CB . THR A 1 175 ? 52.406 12.129 24.723 1.00 140.90 ? 194 THR A CB 1 ATOM 1410 O OG1 . THR A 1 175 ? 52.662 12.642 23.413 1.00 147.48 ? 194 THR A OG1 1 ATOM 1411 C CG2 . THR A 1 175 ? 53.599 12.403 25.639 1.00 145.93 ? 194 THR A CG2 1 ATOM 1412 N N . GLY A 1 176 ? 49.675 10.721 23.984 1.00 126.32 ? 195 GLY A N 1 ATOM 1413 C CA . GLY A 1 176 ? 48.554 10.577 23.062 1.00 124.35 ? 195 GLY A CA 1 ATOM 1414 C C . GLY A 1 176 ? 47.219 10.991 23.655 1.00 119.22 ? 195 GLY A C 1 ATOM 1415 O O . GLY A 1 176 ? 47.110 11.238 24.857 1.00 116.90 ? 195 GLY A O 1 ATOM 1416 N N . VAL A 1 177 ? 46.204 11.078 22.786 1.00 118.85 ? 196 VAL A N 1 ATOM 1417 C CA . VAL A 1 177 ? 44.838 11.454 23.148 1.00 115.42 ? 196 VAL A CA 1 ATOM 1418 C C . VAL A 1 177 ? 43.890 10.336 22.725 1.00 111.09 ? 196 VAL A C 1 ATOM 1419 O O . VAL A 1 177 ? 43.988 9.821 21.607 1.00 113.74 ? 196 VAL A O 1 ATOM 1420 C CB . VAL A 1 177 ? 44.420 12.834 22.560 1.00 121.40 ? 196 VAL A CB 1 ATOM 1421 C CG1 . VAL A 1 177 ? 42.972 13.177 22.909 1.00 118.67 ? 196 VAL A CG1 1 ATOM 1422 C CG2 . VAL A 1 177 ? 45.354 13.947 23.029 1.00 127.19 ? 196 VAL A CG2 1 ATOM 1423 N N . ILE A 1 178 ? 42.992 9.949 23.636 1.00 105.71 ? 197 ILE A N 1 ATOM 1424 C CA . ILE A 1 178 ? 41.992 8.913 23.399 1.00 102.02 ? 197 ILE A CA 1 ATOM 1425 C C . ILE A 1 178 ? 40.624 9.483 23.756 1.00 100.90 ? 197 ILE A C 1 ATOM 1426 O O . ILE A 1 178 ? 40.487 10.149 24.784 1.00 101.08 ? 197 ILE A O 1 ATOM 1427 C CB . ILE A 1 178 ? 42.309 7.607 24.177 1.00 98.49 ? 197 ILE A CB 1 ATOM 1428 C CG1 . ILE A 1 178 ? 43.774 7.159 23.951 1.00 101.26 ? 197 ILE A CG1 1 ATOM 1429 C CG2 . ILE A 1 178 ? 41.319 6.498 23.807 1.00 96.34 ? 197 ILE A CG2 1 ATOM 1430 C CD1 . ILE A 1 178 ? 44.194 5.893 24.634 1.00 99.61 ? 197 ILE A CD1 1 ATOM 1431 N N . THR A 1 179 ? 39.625 9.261 22.887 1.00 101.16 ? 198 THR A N 1 ATOM 1432 C CA . THR A 1 179 ? 38.265 9.751 23.113 1.00 101.16 ? 198 THR A CA 1 ATOM 1433 C C . THR A 1 179 ? 37.229 8.698 22.749 1.00 99.13 ? 198 THR A C 1 ATOM 1434 O O . THR A 1 179 ? 37.532 7.738 22.032 1.00 99.17 ? 198 THR A O 1 ATOM 1435 C CB . THR A 1 179 ? 37.966 11.039 22.287 1.00 107.56 ? 198 THR A CB 1 ATOM 1436 O OG1 . THR A 1 179 ? 37.669 10.708 20.927 1.00 110.66 ? 198 THR A OG1 1 ATOM 1437 C CG2 . THR A 1 179 ? 39.059 12.101 22.367 1.00 111.37 ? 198 THR A CG2 1 ATOM 1438 N N . SER A 1 180 ? 35.978 8.930 23.188 1.00 98.78 ? 199 SER A N 1 ATOM 1439 C CA . SER A 1 180 ? 34.821 8.129 22.807 1.00 98.25 ? 199 SER A CA 1 ATOM 1440 C C . SER A 1 180 ? 34.568 8.472 21.323 1.00 103.27 ? 199 SER A C 1 ATOM 1441 O O . SER A 1 180 ? 34.946 9.573 20.904 1.00 107.31 ? 199 SER A O 1 ATOM 1442 C CB . SER A 1 180 ? 33.607 8.514 23.649 1.00 98.95 ? 199 SER A CB 1 ATOM 1443 O OG . SER A 1 180 ? 33.383 9.914 23.632 1.00 103.45 ? 199 SER A OG 1 ATOM 1444 N N . PRO A 1 181 ? 33.983 7.551 20.516 1.00 104.71 ? 200 PRO A N 1 ATOM 1445 C CA . PRO A 1 181 ? 33.779 7.857 19.095 1.00 111.50 ? 200 PRO A CA 1 ATOM 1446 C C . PRO A 1 181 ? 32.933 9.110 18.862 1.00 116.64 ? 200 PRO A C 1 ATOM 1447 O O . PRO A 1 181 ? 31.918 9.310 19.534 1.00 115.97 ? 200 PRO A O 1 ATOM 1448 C CB . PRO A 1 181 ? 33.122 6.592 18.535 1.00 112.37 ? 200 PRO A CB 1 ATOM 1449 C CG . PRO A 1 181 ? 33.401 5.531 19.528 1.00 106.16 ? 200 PRO A CG 1 ATOM 1450 C CD . PRO A 1 181 ? 33.445 6.217 20.849 1.00 101.67 ? 200 PRO A CD 1 ATOM 1451 N N . ASP A 1 182 ? 33.405 9.977 17.947 1.00 123.46 ? 201 ASP A N 1 ATOM 1452 C CA . ASP A 1 182 ? 32.769 11.235 17.551 1.00 131.12 ? 201 ASP A CA 1 ATOM 1453 C C . ASP A 1 182 ? 32.743 12.313 18.651 1.00 130.14 ? 201 ASP A C 1 ATOM 1454 O O . ASP A 1 182 ? 32.053 13.320 18.489 1.00 136.97 ? 201 ASP A O 1 ATOM 1455 C CB . ASP A 1 182 ? 31.368 10.984 16.945 1.00 135.44 ? 201 ASP A CB 1 ATOM 1456 C CG . ASP A 1 182 ? 30.914 11.983 15.899 1.00 147.61 ? 201 ASP A CG 1 ATOM 1457 O OD1 . ASP A 1 182 ? 31.766 12.752 15.397 1.00 153.42 ? 201 ASP A OD1 1 ATOM 1458 O OD2 . ASP A 1 182 ? 29.713 11.980 15.562 1.00 153.03 ? 201 ASP A OD2 1 ATOM 1459 N N . PHE A 1 183 ? 33.531 12.139 19.737 1.00 123.27 ? 202 PHE A N 1 ATOM 1460 C CA . PHE A 1 183 ? 33.614 13.113 20.833 1.00 123.76 ? 202 PHE A CA 1 ATOM 1461 C C . PHE A 1 183 ? 33.870 14.538 20.286 1.00 133.03 ? 202 PHE A C 1 ATOM 1462 O O . PHE A 1 183 ? 34.694 14.681 19.380 1.00 136.61 ? 202 PHE A O 1 ATOM 1463 C CB . PHE A 1 183 ? 34.710 12.716 21.839 1.00 117.37 ? 202 PHE A CB 1 ATOM 1464 C CG . PHE A 1 183 ? 34.925 13.705 22.962 1.00 119.47 ? 202 PHE A CG 1 ATOM 1465 C CD1 . PHE A 1 183 ? 34.184 13.622 24.134 1.00 117.94 ? 202 PHE A CD1 1 ATOM 1466 C CD2 . PHE A 1 183 ? 35.852 14.735 22.838 1.00 124.89 ? 202 PHE A CD2 1 ATOM 1467 C CE1 . PHE A 1 183 ? 34.363 14.553 25.160 1.00 121.97 ? 202 PHE A CE1 1 ATOM 1468 C CE2 . PHE A 1 183 ? 36.024 15.670 23.861 1.00 128.91 ? 202 PHE A CE2 1 ATOM 1469 C CZ . PHE A 1 183 ? 35.287 15.565 25.021 1.00 127.82 ? 202 PHE A CZ 1 ATOM 1470 N N . PRO A 1 184 ? 33.169 15.581 20.807 1.00 138.81 ? 203 PRO A N 1 ATOM 1471 C CA . PRO A 1 184 ? 32.183 15.581 21.885 1.00 137.46 ? 203 PRO A CA 1 ATOM 1472 C C . PRO A 1 184 ? 30.730 15.441 21.425 1.00 141.65 ? 203 PRO A C 1 ATOM 1473 O O . PRO A 1 184 ? 29.819 15.856 22.141 1.00 145.43 ? 203 PRO A O 1 ATOM 1474 C CB . PRO A 1 184 ? 32.485 16.899 22.600 1.00 144.49 ? 203 PRO A CB 1 ATOM 1475 C CG . PRO A 1 184 ? 32.892 17.831 21.479 1.00 153.41 ? 203 PRO A CG 1 ATOM 1476 C CD . PRO A 1 184 ? 33.444 16.960 20.360 1.00 149.41 ? 203 PRO A CD 1 ATOM 1477 N N . ASN A 1 185 ? 30.508 14.850 20.244 1.00 142.19 ? 204 ASN A N 1 ATOM 1478 C CA . ASN A 1 185 ? 29.151 14.606 19.762 1.00 146.03 ? 204 ASN A CA 1 ATOM 1479 C C . ASN A 1 185 ? 28.650 13.317 20.440 1.00 137.50 ? 204 ASN A C 1 ATOM 1480 O O . ASN A 1 185 ? 29.488 12.560 20.943 1.00 129.29 ? 204 ASN A O 1 ATOM 1481 C CB . ASN A 1 185 ? 29.121 14.487 18.237 1.00 151.57 ? 204 ASN A CB 1 ATOM 1482 C CG . ASN A 1 185 ? 29.562 15.742 17.533 1.00 161.91 ? 204 ASN A CG 1 ATOM 1483 O OD1 . ASN A 1 185 ? 28.902 16.785 17.591 1.00 170.99 ? 204 ASN A OD1 1 ATOM 1484 N ND2 . ASN A 1 185 ? 30.696 15.668 16.854 1.00 162.29 ? 204 ASN A ND2 1 ATOM 1485 N N . PRO A 1 186 ? 27.308 13.069 20.493 1.00 140.45 ? 205 PRO A N 1 ATOM 1486 C CA . PRO A 1 186 ? 26.796 11.851 21.138 1.00 134.15 ? 205 PRO A CA 1 ATOM 1487 C C . PRO A 1 186 ? 27.507 10.583 20.651 1.00 127.12 ? 205 PRO A C 1 ATOM 1488 O O . PRO A 1 186 ? 27.632 10.383 19.439 1.00 130.20 ? 205 PRO A O 1 ATOM 1489 C CB . PRO A 1 186 ? 25.314 11.848 20.764 1.00 140.92 ? 205 PRO A CB 1 ATOM 1490 C CG . PRO A 1 186 ? 24.974 13.269 20.596 1.00 150.78 ? 205 PRO A CG 1 ATOM 1491 C CD . PRO A 1 186 ? 26.199 13.948 20.063 1.00 151.22 ? 205 PRO A CD 1 ATOM 1492 N N . TYR A 1 187 ? 28.027 9.764 21.590 1.00 119.62 ? 206 TYR A N 1 ATOM 1493 C CA . TYR A 1 187 ? 28.727 8.527 21.225 1.00 114.46 ? 206 TYR A CA 1 ATOM 1494 C C . TYR A 1 187 ? 27.767 7.467 20.673 1.00 116.21 ? 206 TYR A C 1 ATOM 1495 O O . TYR A 1 187 ? 26.610 7.435 21.102 1.00 118.83 ? 206 TYR A O 1 ATOM 1496 C CB . TYR A 1 187 ? 29.592 7.963 22.371 1.00 107.45 ? 206 TYR A CB 1 ATOM 1497 C CG . TYR A 1 187 ? 28.889 7.802 23.700 1.00 107.14 ? 206 TYR A CG 1 ATOM 1498 C CD1 . TYR A 1 187 ? 28.098 6.688 23.965 1.00 106.81 ? 206 TYR A CD1 1 ATOM 1499 C CD2 . TYR A 1 187 ? 29.092 8.714 24.728 1.00 108.41 ? 206 TYR A CD2 1 ATOM 1500 C CE1 . TYR A 1 187 ? 27.468 6.525 25.199 1.00 107.79 ? 206 TYR A CE1 1 ATOM 1501 C CE2 . TYR A 1 187 ? 28.481 8.555 25.970 1.00 109.70 ? 206 TYR A CE2 1 ATOM 1502 C CZ . TYR A 1 187 ? 27.665 7.462 26.201 1.00 109.60 ? 206 TYR A CZ 1 ATOM 1503 O OH . TYR A 1 187 ? 27.062 7.316 27.429 1.00 112.49 ? 206 TYR A OH 1 ATOM 1504 N N . PRO A 1 188 ? 28.234 6.609 19.720 1.00 116.33 ? 207 PRO A N 1 ATOM 1505 C CA . PRO A 1 188 ? 27.388 5.566 19.135 1.00 119.28 ? 207 PRO A CA 1 ATOM 1506 C C . PRO A 1 188 ? 26.867 4.588 20.179 1.00 115.87 ? 207 PRO A C 1 ATOM 1507 O O . PRO A 1 188 ? 27.602 4.185 21.084 1.00 110.57 ? 207 PRO A O 1 ATOM 1508 C CB . PRO A 1 188 ? 28.315 4.868 18.134 1.00 120.43 ? 207 PRO A CB 1 ATOM 1509 C CG . PRO A 1 188 ? 29.348 5.863 17.820 1.00 120.58 ? 207 PRO A CG 1 ATOM 1510 C CD . PRO A 1 188 ? 29.565 6.620 19.081 1.00 115.35 ? 207 PRO A CD 1 ATOM 1511 N N . LYS A 1 189 ? 25.589 4.219 20.050 1.00 120.30 ? 208 LYS A N 1 ATOM 1512 C CA . LYS A 1 189 ? 24.926 3.268 20.937 1.00 119.39 ? 208 LYS A CA 1 ATOM 1513 C C . LYS A 1 189 ? 25.375 1.856 20.581 1.00 118.96 ? 208 LYS A C 1 ATOM 1514 O O . LYS A 1 189 ? 25.964 1.647 19.516 1.00 120.70 ? 208 LYS A O 1 ATOM 1515 C CB . LYS A 1 189 ? 23.401 3.355 20.763 1.00 126.22 ? 208 LYS A CB 1 ATOM 1516 C CG . LYS A 1 189 ? 22.781 4.673 21.187 1.00 128.81 ? 208 LYS A CG 1 ATOM 1517 C CD . LYS A 1 189 ? 21.302 4.694 20.823 1.00 137.00 ? 208 LYS A CD 1 ATOM 1518 C CE . LYS A 1 189 ? 20.641 6.027 21.068 1.00 142.21 ? 208 LYS A CE 1 ATOM 1519 N NZ . LYS A 1 189 ? 21.205 7.102 20.207 1.00 143.29 ? 208 LYS A NZ 1 ATOM 1520 N N . SER A 1 190 ? 25.085 0.886 21.472 1.00 118.12 ? 209 SER A N 1 ATOM 1521 C CA . SER A 1 190 ? 25.333 -0.547 21.283 1.00 119.90 ? 209 SER A CA 1 ATOM 1522 C C . SER A 1 190 ? 26.750 -0.887 20.797 1.00 117.67 ? 209 SER A C 1 ATOM 1523 O O . SER A 1 190 ? 26.931 -1.812 20.000 1.00 122.43 ? 209 SER A O 1 ATOM 1524 C CB . SER A 1 190 ? 24.280 -1.132 20.343 1.00 127.33 ? 209 SER A CB 1 ATOM 1525 O OG . SER A 1 190 ? 22.970 -0.772 20.751 1.00 130.33 ? 209 SER A OG 1 ATOM 1526 N N . SER A 1 191 ? 27.748 -0.139 21.283 1.00 112.15 ? 210 SER A N 1 ATOM 1527 C CA . SER A 1 191 ? 29.136 -0.325 20.883 1.00 110.65 ? 210 SER A CA 1 ATOM 1528 C C . SER A 1 191 ? 30.016 -0.848 22.014 1.00 106.92 ? 210 SER A C 1 ATOM 1529 O O . SER A 1 191 ? 29.679 -0.705 23.192 1.00 104.60 ? 210 SER A O 1 ATOM 1530 C CB . SER A 1 191 ? 29.696 0.962 20.286 1.00 109.37 ? 210 SER A CB 1 ATOM 1531 O OG . SER A 1 191 ? 28.966 1.339 19.129 1.00 115.02 ? 210 SER A OG 1 ATOM 1532 N N . GLU A 1 192 ? 31.135 -1.480 21.638 1.00 107.86 ? 211 GLU A N 1 ATOM 1533 C CA . GLU A 1 192 ? 32.108 -2.067 22.549 1.00 106.16 ? 211 GLU A CA 1 ATOM 1534 C C . GLU A 1 192 ? 33.498 -1.686 22.041 1.00 105.54 ? 211 GLU A C 1 ATOM 1535 O O . GLU A 1 192 ? 34.040 -2.345 21.149 1.00 110.53 ? 211 GLU A O 1 ATOM 1536 C CB . GLU A 1 192 ? 31.906 -3.590 22.600 1.00 111.64 ? 211 GLU A CB 1 ATOM 1537 C CG . GLU A 1 192 ? 32.722 -4.301 23.661 1.00 112.15 ? 211 GLU A CG 1 ATOM 1538 C CD . GLU A 1 192 ? 32.412 -5.779 23.775 1.00 119.56 ? 211 GLU A CD 1 ATOM 1539 O OE1 . GLU A 1 192 ? 32.777 -6.539 22.848 1.00 125.13 ? 211 GLU A OE1 1 ATOM 1540 O OE2 . GLU A 1 192 ? 31.788 -6.177 24.785 1.00 121.16 ? 211 GLU A OE2 1 ATOM 1541 N N . CYS A 1 193 ? 34.047 -0.589 22.587 1.00 100.62 ? 212 CYS A N 1 ATOM 1542 C CA . CYS A 1 193 ? 35.338 -0.037 22.185 1.00 100.34 ? 212 CYS A CA 1 ATOM 1543 C C . CYS A 1 193 ? 36.492 -0.530 23.032 1.00 99.32 ? 212 CYS A C 1 ATOM 1544 O O . CYS A 1 193 ? 36.441 -0.451 24.260 1.00 96.71 ? 212 CYS A O 1 ATOM 1545 C CB . CYS A 1 193 ? 35.290 1.488 22.149 1.00 97.55 ? 212 CYS A CB 1 ATOM 1546 S SG . CYS A 1 193 ? 33.891 2.177 21.227 1.00 101.59 ? 212 CYS A SG 1 ATOM 1547 N N . LEU A 1 194 ? 37.547 -1.008 22.367 1.00 103.15 ? 213 LEU A N 1 ATOM 1548 C CA . LEU A 1 194 ? 38.758 -1.476 23.026 1.00 103.87 ? 213 LEU A CA 1 ATOM 1549 C C . LEU A 1 194 ? 39.916 -0.591 22.593 1.00 104.01 ? 213 LEU A C 1 ATOM 1550 O O . LEU A 1 194 ? 40.327 -0.634 21.430 1.00 108.63 ? 213 LEU A O 1 ATOM 1551 C CB . LEU A 1 194 ? 39.051 -2.959 22.709 1.00 110.65 ? 213 LEU A CB 1 ATOM 1552 C CG . LEU A 1 194 ? 37.989 -3.993 23.101 1.00 113.12 ? 213 LEU A CG 1 ATOM 1553 C CD1 . LEU A 1 194 ? 38.284 -5.337 22.468 1.00 122.23 ? 213 LEU A CD1 1 ATOM 1554 C CD2 . LEU A 1 194 ? 37.880 -4.145 24.612 1.00 110.85 ? 213 LEU A CD2 1 ATOM 1555 N N . TYR A 1 195 ? 40.404 0.249 23.517 1.00 99.92 ? 214 TYR A N 1 ATOM 1556 C CA . TYR A 1 195 ? 41.534 1.143 23.274 1.00 100.78 ? 214 TYR A CA 1 ATOM 1557 C C . TYR A 1 195 ? 42.755 0.550 23.950 1.00 103.35 ? 214 TYR A C 1 ATOM 1558 O O . TYR A 1 195 ? 42.726 0.292 25.158 1.00 101.51 ? 214 TYR A O 1 ATOM 1559 C CB . TYR A 1 195 ? 41.257 2.569 23.773 1.00 96.77 ? 214 TYR A CB 1 ATOM 1560 C CG . TYR A 1 195 ? 39.978 3.168 23.231 1.00 95.53 ? 214 TYR A CG 1 ATOM 1561 C CD1 . TYR A 1 195 ? 39.950 3.797 21.989 1.00 98.43 ? 214 TYR A CD1 1 ATOM 1562 C CD2 . TYR A 1 195 ? 38.798 3.117 23.964 1.00 92.63 ? 214 TYR A CD2 1 ATOM 1563 C CE1 . TYR A 1 195 ? 38.779 4.370 21.495 1.00 98.87 ? 214 TYR A CE1 1 ATOM 1564 C CE2 . TYR A 1 195 ? 37.621 3.683 23.480 1.00 92.09 ? 214 TYR A CE2 1 ATOM 1565 C CZ . TYR A 1 195 ? 37.613 4.303 22.240 1.00 95.64 ? 214 TYR A CZ 1 ATOM 1566 O OH . TYR A 1 195 ? 36.454 4.859 21.755 1.00 97.76 ? 214 TYR A OH 1 ATOM 1567 N N . THR A 1 196 ? 43.810 0.289 23.165 1.00 108.61 ? 215 THR A N 1 ATOM 1568 C CA . THR A 1 196 ? 45.019 -0.348 23.673 1.00 112.95 ? 215 THR A CA 1 ATOM 1569 C C . THR A 1 196 ? 46.244 0.548 23.635 1.00 114.98 ? 215 THR A C 1 ATOM 1570 O O . THR A 1 196 ? 46.646 1.014 22.566 1.00 118.78 ? 215 THR A O 1 ATOM 1571 C CB . THR A 1 196 ? 45.262 -1.692 22.957 1.00 120.76 ? 215 THR A CB 1 ATOM 1572 O OG1 . THR A 1 196 ? 44.035 -2.417 22.873 1.00 119.58 ? 215 THR A OG1 1 ATOM 1573 C CG2 . THR A 1 196 ? 46.310 -2.549 23.656 1.00 126.06 ? 215 THR A CG2 1 ATOM 1574 N N . ILE A 1 197 ? 46.853 0.754 24.810 1.00 113.83 ? 216 ILE A N 1 ATOM 1575 C CA . ILE A 1 197 ? 48.102 1.495 24.944 1.00 116.91 ? 216 ILE A CA 1 ATOM 1576 C C . ILE A 1 197 ? 49.171 0.436 25.176 1.00 124.42 ? 216 ILE A C 1 ATOM 1577 O O . ILE A 1 197 ? 49.067 -0.344 26.123 1.00 125.33 ? 216 ILE A O 1 ATOM 1578 C CB . ILE A 1 197 ? 48.091 2.580 26.060 1.00 112.81 ? 216 ILE A CB 1 ATOM 1579 C CG1 . ILE A 1 197 ? 46.913 3.564 25.886 1.00 106.97 ? 216 ILE A CG1 1 ATOM 1580 C CG2 . ILE A 1 197 ? 49.437 3.330 26.095 1.00 117.04 ? 216 ILE A CG2 1 ATOM 1581 C CD1 . ILE A 1 197 ? 46.650 4.490 27.089 1.00 103.96 ? 216 ILE A CD1 1 ATOM 1582 N N . GLU A 1 198 ? 50.160 0.374 24.280 1.00 131.50 ? 217 GLU A N 1 ATOM 1583 C CA . GLU A 1 198 ? 51.253 -0.586 24.371 1.00 140.85 ? 217 GLU A CA 1 ATOM 1584 C C . GLU A 1 198 ? 52.580 0.118 24.217 1.00 145.98 ? 217 GLU A C 1 ATOM 1585 O O . GLU A 1 198 ? 52.944 0.535 23.115 1.00 150.33 ? 217 GLU A O 1 ATOM 1586 C CB . GLU A 1 198 ? 51.108 -1.696 23.321 1.00 148.19 ? 217 GLU A CB 1 ATOM 1587 C CG . GLU A 1 198 ? 50.042 -2.721 23.662 1.00 147.79 ? 217 GLU A CG 1 ATOM 1588 C CD . GLU A 1 198 ? 50.534 -4.085 24.104 1.00 159.20 ? 217 GLU A CD 1 ATOM 1589 O OE1 . GLU A 1 198 ? 51.689 -4.190 24.577 1.00 165.60 ? 217 GLU A OE1 1 ATOM 1590 O OE2 . GLU A 1 198 ? 49.746 -5.051 23.997 1.00 160.72 ? 217 GLU A OE2 1 ATOM 1591 N N . LEU A 1 199 ? 53.290 0.277 25.329 1.00 146.91 ? 218 LEU A N 1 ATOM 1592 C CA . LEU A 1 199 ? 54.604 0.900 25.318 1.00 153.62 ? 218 LEU A CA 1 ATOM 1593 C C . LEU A 1 199 ? 55.630 -0.169 25.606 1.00 163.62 ? 218 LEU A C 1 ATOM 1594 O O . LEU A 1 199 ? 55.277 -1.281 26.013 1.00 165.06 ? 218 LEU A O 1 ATOM 1595 C CB . LEU A 1 199 ? 54.716 2.040 26.351 1.00 149.05 ? 218 LEU A CB 1 ATOM 1596 C CG . LEU A 1 199 ? 53.592 3.070 26.395 1.00 140.58 ? 218 LEU A CG 1 ATOM 1597 C CD1 . LEU A 1 199 ? 53.751 3.951 27.570 1.00 139.19 ? 218 LEU A CD1 1 ATOM 1598 C CD2 . LEU A 1 199 ? 53.530 3.902 25.124 1.00 141.01 ? 218 LEU A CD2 1 ATOM 1599 N N . GLU A 1 200 ? 56.901 0.165 25.394 1.00 172.18 ? 219 GLU A N 1 ATOM 1600 C CA . GLU A 1 200 ? 58.019 -0.728 25.645 1.00 183.90 ? 219 GLU A CA 1 ATOM 1601 C C . GLU A 1 200 ? 58.163 -0.984 27.143 1.00 183.38 ? 219 GLU A C 1 ATOM 1602 O O . GLU A 1 200 ? 57.756 -0.149 27.956 1.00 175.84 ? 219 GLU A O 1 ATOM 1603 C CB . GLU A 1 200 ? 59.293 -0.095 25.090 1.00 192.96 ? 219 GLU A CB 1 ATOM 1604 C CG . GLU A 1 200 ? 60.566 -0.885 25.336 1.00 206.39 ? 219 GLU A CG 1 ATOM 1605 C CD . GLU A 1 200 ? 61.812 -0.110 24.978 1.00 232.58 ? 219 GLU A CD 1 ATOM 1606 O OE1 . GLU A 1 200 ? 61.687 0.874 24.216 1.00 223.50 ? 219 GLU A OE1 1 ATOM 1607 O OE2 . GLU A 1 200 ? 62.916 -0.513 25.408 1.00 264.28 ? 219 GLU A OE2 1 ATOM 1608 N N . GLU A 1 201 ? 58.750 -2.141 27.494 1.00 193.30 ? 220 GLU A N 1 ATOM 1609 C CA . GLU A 1 201 ? 59.019 -2.548 28.865 1.00 196.56 ? 220 GLU A CA 1 ATOM 1610 C C . GLU A 1 201 ? 59.770 -1.447 29.599 1.00 196.66 ? 220 GLU A C 1 ATOM 1611 O O . GLU A 1 201 ? 60.756 -0.924 29.077 1.00 202.68 ? 220 GLU A O 1 ATOM 1612 C CB . GLU A 1 201 ? 59.821 -3.863 28.888 1.00 210.97 ? 220 GLU A CB 1 ATOM 1613 C CG . GLU A 1 201 ? 60.045 -4.444 30.278 1.00 220.77 ? 220 GLU A CG 1 ATOM 1614 C CD . GLU A 1 201 ? 58.838 -5.028 30.990 1.00 211.71 ? 220 GLU A CD 1 ATOM 1615 O OE1 . GLU A 1 201 ? 57.723 -4.477 30.851 1.00 199.78 ? 220 GLU A OE1 1 ATOM 1616 O OE2 . GLU A 1 201 ? 59.020 -6.021 31.729 1.00 231.78 ? 220 GLU A OE2 1 ATOM 1617 N N . GLY A 1 202 ? 59.271 -1.062 30.776 1.00 191.37 ? 221 GLY A N 1 ATOM 1618 C CA . GLY A 1 202 ? 59.915 -0.027 31.570 1.00 192.96 ? 221 GLY A CA 1 ATOM 1619 C C . GLY A 1 202 ? 59.211 1.307 31.621 1.00 182.74 ? 221 GLY A C 1 ATOM 1620 O O . GLY A 1 202 ? 59.575 2.143 32.447 1.00 184.54 ? 221 GLY A O 1 ATOM 1621 N N . PHE A 1 203 ? 58.240 1.529 30.728 1.00 173.62 ? 222 PHE A N 1 ATOM 1622 C CA . PHE A 1 203 ? 57.458 2.759 30.703 1.00 164.74 ? 222 PHE A CA 1 ATOM 1623 C C . PHE A 1 203 ? 56.233 2.595 31.588 1.00 157.90 ? 222 PHE A C 1 ATOM 1624 O O . PHE A 1 203 ? 55.724 1.485 31.717 1.00 157.10 ? 222 PHE A O 1 ATOM 1625 C CB . PHE A 1 203 ? 57.049 3.125 29.270 1.00 160.28 ? 222 PHE A CB 1 ATOM 1626 C CG . PHE A 1 203 ? 58.165 3.711 28.440 1.00 167.53 ? 222 PHE A CG 1 ATOM 1627 C CD1 . PHE A 1 203 ? 58.736 4.933 28.777 1.00 170.05 ? 222 PHE A CD1 1 ATOM 1628 C CD2 . PHE A 1 203 ? 58.632 3.052 27.308 1.00 173.89 ? 222 PHE A CD2 1 ATOM 1629 C CE1 . PHE A 1 203 ? 59.779 5.466 28.021 1.00 178.31 ? 222 PHE A CE1 1 ATOM 1630 C CE2 . PHE A 1 203 ? 59.658 3.602 26.534 1.00 182.10 ? 222 PHE A CE2 1 ATOM 1631 C CZ . PHE A 1 203 ? 60.220 4.809 26.893 1.00 183.66 ? 222 PHE A CZ 1 ATOM 1632 N N . MET A 1 204 ? 55.787 3.678 32.232 1.00 154.57 ? 223 MET A N 1 ATOM 1633 C CA . MET A 1 204 ? 54.612 3.645 33.104 1.00 149.99 ? 223 MET A CA 1 ATOM 1634 C C . MET A 1 204 ? 53.606 4.673 32.621 1.00 141.67 ? 223 MET A C 1 ATOM 1635 O O . MET A 1 204 ? 53.932 5.856 32.511 1.00 142.77 ? 223 MET A O 1 ATOM 1636 C CB . MET A 1 204 ? 54.993 3.882 34.566 1.00 156.76 ? 223 MET A CB 1 ATOM 1637 C CG . MET A 1 204 ? 55.733 2.725 35.200 1.00 165.84 ? 223 MET A CG 1 ATOM 1638 S SD . MET A 1 204 ? 56.376 3.063 36.865 1.00 178.36 ? 223 MET A SD 1 ATOM 1639 C CE . MET A 1 204 ? 55.392 4.493 37.344 1.00 174.27 ? 223 MET A CE 1 ATOM 1640 N N . VAL A 1 205 ? 52.392 4.218 32.306 1.00 134.75 ? 224 VAL A N 1 ATOM 1641 C CA . VAL A 1 205 ? 51.342 5.068 31.749 1.00 127.55 ? 224 VAL A CA 1 ATOM 1642 C C . VAL A 1 205 ? 50.579 5.872 32.791 1.00 126.78 ? 224 VAL A C 1 ATOM 1643 O O . VAL A 1 205 ? 50.008 5.305 33.719 1.00 127.51 ? 224 VAL A O 1 ATOM 1644 C CB . VAL A 1 205 ? 50.374 4.265 30.840 1.00 122.05 ? 224 VAL A CB 1 ATOM 1645 C CG1 . VAL A 1 205 ? 49.347 5.177 30.172 1.00 115.72 ? 224 VAL A CG1 1 ATOM 1646 C CG2 . VAL A 1 205 ? 51.129 3.455 29.793 1.00 124.76 ? 224 VAL A CG2 1 ATOM 1647 N N . ASN A 1 206 ? 50.514 7.190 32.593 1.00 126.61 ? 225 ASN A N 1 ATOM 1648 C CA . ASN A 1 206 ? 49.718 8.064 33.442 1.00 127.04 ? 225 ASN A CA 1 ATOM 1649 C C . ASN A 1 206 ? 48.525 8.540 32.623 1.00 120.44 ? 225 ASN A C 1 ATOM 1650 O O . ASN A 1 206 ? 48.697 8.958 31.478 1.00 117.91 ? 225 ASN A O 1 ATOM 1651 C CB . ASN A 1 206 ? 50.543 9.225 33.994 1.00 134.30 ? 225 ASN A CB 1 ATOM 1652 C CG . ASN A 1 206 ? 51.686 8.803 34.894 1.00 143.24 ? 225 ASN A CG 1 ATOM 1653 O OD1 . ASN A 1 206 ? 51.754 7.672 35.397 1.00 144.92 ? 225 ASN A OD1 1 ATOM 1654 N ND2 . ASN A 1 206 ? 52.613 9.718 35.124 1.00 150.15 ? 225 ASN A ND2 1 ATOM 1655 N N . LEU A 1 207 ? 47.313 8.407 33.183 1.00 118.71 ? 226 LEU A N 1 ATOM 1656 C CA . LEU A 1 207 ? 46.069 8.785 32.511 1.00 113.86 ? 226 LEU A CA 1 ATOM 1657 C C . LEU A 1 207 ? 45.475 10.039 33.122 1.00 117.89 ? 226 LEU A C 1 ATOM 1658 O O . LEU A 1 207 ? 45.521 10.212 34.342 1.00 123.74 ? 226 LEU A O 1 ATOM 1659 C CB . LEU A 1 207 ? 45.043 7.638 32.550 1.00 109.62 ? 226 LEU A CB 1 ATOM 1660 C CG . LEU A 1 207 ? 45.473 6.286 31.966 1.00 107.51 ? 226 LEU A CG 1 ATOM 1661 C CD1 . LEU A 1 207 ? 44.464 5.210 32.306 1.00 105.60 ? 226 LEU A CD1 1 ATOM 1662 C CD2 . LEU A 1 207 ? 45.675 6.361 30.454 1.00 104.04 ? 226 LEU A CD2 1 ATOM 1663 N N . GLN A 1 208 ? 44.912 10.911 32.273 1.00 116.35 ? 227 GLN A N 1 ATOM 1664 C CA . GLN A 1 208 ? 44.324 12.173 32.705 1.00 121.85 ? 227 GLN A CA 1 ATOM 1665 C C . GLN A 1 208 ? 43.139 12.580 31.830 1.00 119.06 ? 227 GLN A C 1 ATOM 1666 O O . GLN A 1 208 ? 43.320 12.900 30.653 1.00 117.47 ? 227 GLN A O 1 ATOM 1667 C CB . GLN A 1 208 ? 45.405 13.269 32.733 1.00 128.27 ? 227 GLN A CB 1 ATOM 1668 C CG . GLN A 1 208 ? 44.892 14.661 33.083 1.00 136.19 ? 227 GLN A CG 1 ATOM 1669 C CD . GLN A 1 208 ? 45.989 15.575 33.561 1.00 145.91 ? 227 GLN A CD 1 ATOM 1670 O OE1 . GLN A 1 208 ? 47.112 15.586 33.040 1.00 146.21 ? 227 GLN A OE1 1 ATOM 1671 N NE2 . GLN A 1 208 ? 45.679 16.387 34.557 1.00 154.65 ? 227 GLN A NE2 1 ATOM 1672 N N . PHE A 1 209 ? 41.933 12.588 32.415 1.00 120.03 ? 228 PHE A N 1 ATOM 1673 C CA . PHE A 1 209 ? 40.725 12.998 31.704 1.00 118.81 ? 228 PHE A CA 1 ATOM 1674 C C . PHE A 1 209 ? 40.667 14.512 31.576 1.00 126.45 ? 228 PHE A C 1 ATOM 1675 O O . PHE A 1 209 ? 41.155 15.228 32.454 1.00 133.71 ? 228 PHE A O 1 ATOM 1676 C CB . PHE A 1 209 ? 39.467 12.459 32.393 1.00 118.88 ? 228 PHE A CB 1 ATOM 1677 C CG . PHE A 1 209 ? 39.236 10.986 32.168 1.00 111.99 ? 228 PHE A CG 1 ATOM 1678 C CD1 . PHE A 1 209 ? 39.786 10.041 33.026 1.00 111.96 ? 228 PHE A CD1 1 ATOM 1679 C CD2 . PHE A 1 209 ? 38.474 10.540 31.094 1.00 106.93 ? 228 PHE A CD2 1 ATOM 1680 C CE1 . PHE A 1 209 ? 39.586 8.675 32.807 1.00 107.29 ? 228 PHE A CE1 1 ATOM 1681 C CE2 . PHE A 1 209 ? 38.268 9.174 30.880 1.00 102.04 ? 228 PHE A CE2 1 ATOM 1682 C CZ . PHE A 1 209 ? 38.822 8.252 31.741 1.00 102.16 ? 228 PHE A CZ 1 ATOM 1683 N N . GLU A 1 210 ? 40.088 14.996 30.470 1.00 125.76 ? 229 GLU A N 1 ATOM 1684 C CA . GLU A 1 210 ? 39.965 16.427 30.189 1.00 134.51 ? 229 GLU A CA 1 ATOM 1685 C C . GLU A 1 210 ? 38.703 16.764 29.404 1.00 135.42 ? 229 GLU A C 1 ATOM 1686 O O . GLU A 1 210 ? 38.092 15.876 28.802 1.00 128.79 ? 229 GLU A O 1 ATOM 1687 C CB . GLU A 1 210 ? 41.230 16.974 29.500 1.00 136.79 ? 229 GLU A CB 1 ATOM 1688 C CG . GLU A 1 210 ? 41.667 16.190 28.272 1.00 130.11 ? 229 GLU A CG 1 ATOM 1689 C CD . GLU A 1 210 ? 43.118 16.354 27.865 1.00 132.67 ? 229 GLU A CD 1 ATOM 1690 O OE1 . GLU A 1 210 ? 43.962 16.660 28.739 1.00 136.36 ? 229 GLU A OE1 1 ATOM 1691 O OE2 . GLU A 1 210 ? 43.419 16.136 26.670 1.00 131.43 ? 229 GLU A OE2 1 ATOM 1692 N N . ASP A 1 211 ? 38.315 18.057 29.425 1.00 145.51 ? 230 ASP A N 1 ATOM 1693 C CA . ASP A 1 211 ? 37.130 18.611 28.762 1.00 149.77 ? 230 ASP A CA 1 ATOM 1694 C C . ASP A 1 211 ? 35.836 17.954 29.263 1.00 147.35 ? 230 ASP A C 1 ATOM 1695 O O . ASP A 1 211 ? 35.767 17.572 30.434 1.00 147.25 ? 230 ASP A O 1 ATOM 1696 C CB . ASP A 1 211 ? 37.267 18.569 27.222 1.00 147.07 ? 230 ASP A CB 1 ATOM 1697 C CG . ASP A 1 211 ? 38.498 19.270 26.677 1.00 151.90 ? 230 ASP A CG 1 ATOM 1698 O OD1 . ASP A 1 211 ? 38.959 20.246 27.310 1.00 158.68 ? 230 ASP A OD1 1 ATOM 1699 O OD2 . ASP A 1 211 ? 38.983 18.861 25.604 1.00 150.25 ? 230 ASP A OD2 1 ATOM 1700 N N . ILE A 1 212 ? 34.821 17.828 28.388 1.00 146.71 ? 231 ILE A N 1 ATOM 1701 C CA . ILE A 1 212 ? 33.526 17.230 28.712 1.00 145.59 ? 231 ILE A CA 1 ATOM 1702 C C . ILE A 1 212 ? 33.655 15.759 29.104 1.00 135.18 ? 231 ILE A C 1 ATOM 1703 O O . ILE A 1 212 ? 34.344 14.991 28.432 1.00 126.92 ? 231 ILE A O 1 ATOM 1704 C CB . ILE A 1 212 ? 32.503 17.421 27.548 1.00 147.53 ? 231 ILE A CB 1 ATOM 1705 C CG1 . ILE A 1 212 ? 32.118 18.908 27.368 1.00 160.71 ? 231 ILE A CG1 1 ATOM 1706 C CG2 . ILE A 1 212 ? 31.247 16.537 27.731 1.00 144.93 ? 231 ILE A CG2 1 ATOM 1707 C CD1 . ILE A 1 212 ? 31.563 19.277 25.970 1.00 164.15 ? 231 ILE A CD1 1 ATOM 1708 N N . PHE A 1 213 ? 32.974 15.383 30.191 1.00 137.29 ? 232 PHE A N 1 ATOM 1709 C CA . PHE A 1 213 ? 32.853 14.009 30.650 1.00 130.37 ? 232 PHE A CA 1 ATOM 1710 C C . PHE A 1 213 ? 31.363 13.779 30.860 1.00 133.92 ? 232 PHE A C 1 ATOM 1711 O O . PHE A 1 213 ? 30.761 14.374 31.758 1.00 142.75 ? 232 PHE A O 1 ATOM 1712 C CB . PHE A 1 213 ? 33.664 13.736 31.925 1.00 131.45 ? 232 PHE A CB 1 ATOM 1713 C CG . PHE A 1 213 ? 33.713 12.267 32.276 1.00 124.91 ? 232 PHE A CG 1 ATOM 1714 C CD1 . PHE A 1 213 ? 34.713 11.446 31.766 1.00 116.82 ? 232 PHE A CD1 1 ATOM 1715 C CD2 . PHE A 1 213 ? 32.750 11.699 33.103 1.00 128.26 ? 232 PHE A CD2 1 ATOM 1716 C CE1 . PHE A 1 213 ? 34.758 10.087 32.091 1.00 112.69 ? 232 PHE A CE1 1 ATOM 1717 C CE2 . PHE A 1 213 ? 32.790 10.339 33.420 1.00 123.99 ? 232 PHE A CE2 1 ATOM 1718 C CZ . PHE A 1 213 ? 33.799 9.545 32.920 1.00 116.45 ? 232 PHE A CZ 1 ATOM 1719 N N . ASP A 1 214 ? 30.759 12.969 29.984 1.00 128.19 ? 233 ASP A N 1 ATOM 1720 C CA . ASP A 1 214 ? 29.328 12.703 29.999 1.00 131.85 ? 233 ASP A CA 1 ATOM 1721 C C . ASP A 1 214 ? 29.011 11.272 29.579 1.00 124.53 ? 233 ASP A C 1 ATOM 1722 O O . ASP A 1 214 ? 28.886 10.973 28.389 1.00 120.63 ? 233 ASP A O 1 ATOM 1723 C CB . ASP A 1 214 ? 28.591 13.743 29.124 1.00 137.84 ? 233 ASP A CB 1 ATOM 1724 C CG . ASP A 1 214 ? 27.084 13.587 29.006 1.00 143.14 ? 233 ASP A CG 1 ATOM 1725 O OD1 . ASP A 1 214 ? 26.484 12.893 29.859 1.00 143.89 ? 233 ASP A OD1 1 ATOM 1726 O OD2 . ASP A 1 214 ? 26.500 14.185 28.079 1.00 147.70 ? 233 ASP A OD2 1 ATOM 1727 N N . ILE A 1 215 ? 28.881 10.391 30.576 1.00 124.22 ? 234 ILE A N 1 ATOM 1728 C CA . ILE A 1 215 ? 28.533 8.986 30.385 1.00 119.49 ? 234 ILE A CA 1 ATOM 1729 C C . ILE A 1 215 ? 27.257 8.737 31.173 1.00 126.62 ? 234 ILE A C 1 ATOM 1730 O O . ILE A 1 215 ? 27.199 9.075 32.357 1.00 133.40 ? 234 ILE A O 1 ATOM 1731 C CB . ILE A 1 215 ? 29.678 8.023 30.813 1.00 113.99 ? 234 ILE A CB 1 ATOM 1732 C CG1 . ILE A 1 215 ? 31.012 8.382 30.119 1.00 108.85 ? 234 ILE A CG1 1 ATOM 1733 C CG2 . ILE A 1 215 ? 29.287 6.557 30.560 1.00 110.77 ? 234 ILE A CG2 1 ATOM 1734 C CD1 . ILE A 1 215 ? 32.170 7.460 30.428 1.00 104.16 ? 234 ILE A CD1 1 ATOM 1735 N N . GLU A 1 216 ? 26.236 8.153 30.521 1.00 126.55 ? 235 GLU A N 1 ATOM 1736 C CA . GLU A 1 216 ? 24.953 7.838 31.150 1.00 133.98 ? 235 GLU A CA 1 ATOM 1737 C C . GLU A 1 216 ? 25.163 7.060 32.450 1.00 136.78 ? 235 GLU A C 1 ATOM 1738 O O . GLU A 1 216 ? 25.952 6.112 32.484 1.00 131.06 ? 235 GLU A O 1 ATOM 1739 C CB . GLU A 1 216 ? 24.078 7.031 30.190 1.00 132.33 ? 235 GLU A CB 1 ATOM 1740 C CG . GLU A 1 216 ? 22.615 6.949 30.593 1.00 141.48 ? 235 GLU A CG 1 ATOM 1741 C CD . GLU A 1 216 ? 21.792 5.977 29.771 1.00 140.82 ? 235 GLU A CD 1 ATOM 1742 O OE1 . GLU A 1 216 ? 22.354 5.355 28.845 1.00 133.24 ? 235 GLU A OE1 1 ATOM 1743 O OE2 . GLU A 1 216 ? 20.581 5.837 30.048 1.00 148.95 ? 235 GLU A OE2 1 ATOM 1744 N N . ASP A 1 217 ? 24.486 7.487 33.519 1.00 147.07 ? 236 ASP A N 1 ATOM 1745 C CA . ASP A 1 217 ? 24.598 6.849 34.825 1.00 152.68 ? 236 ASP A CA 1 ATOM 1746 C C . ASP A 1 217 ? 23.240 6.689 35.501 1.00 164.46 ? 236 ASP A C 1 ATOM 1747 O O . ASP A 1 217 ? 22.213 7.088 34.948 1.00 167.71 ? 236 ASP A O 1 ATOM 1748 C CB . ASP A 1 217 ? 25.571 7.644 35.724 1.00 156.22 ? 236 ASP A CB 1 ATOM 1749 C CG . ASP A 1 217 ? 25.086 9.000 36.223 1.00 167.79 ? 236 ASP A CG 1 ATOM 1750 O OD1 . ASP A 1 217 ? 24.040 9.485 35.728 1.00 172.55 ? 236 ASP A OD1 1 ATOM 1751 O OD2 . ASP A 1 217 ? 25.756 9.580 37.100 1.00 173.87 ? 236 ASP A OD2 1 ATOM 1752 N N . HIS A 1 218 ? 23.255 6.136 36.718 1.00 172.32 ? 237 HIS A N 1 ATOM 1753 C CA . HIS A 1 218 ? 22.080 5.947 37.556 1.00 185.57 ? 237 HIS A CA 1 ATOM 1754 C C . HIS A 1 218 ? 22.386 6.526 38.944 1.00 197.93 ? 237 HIS A C 1 ATOM 1755 O O . HIS A 1 218 ? 23.516 6.371 39.413 1.00 195.32 ? 237 HIS A O 1 ATOM 1756 C CB . HIS A 1 218 ? 21.727 4.462 37.649 1.00 185.42 ? 237 HIS A CB 1 ATOM 1757 C CG . HIS A 1 218 ? 20.372 4.200 38.221 1.00 199.23 ? 237 HIS A CG 1 ATOM 1758 N ND1 . HIS A 1 218 ? 20.177 4.078 39.584 1.00 215.12 ? 237 HIS A ND1 1 ATOM 1759 C CD2 . HIS A 1 218 ? 19.182 4.062 37.594 1.00 201.94 ? 237 HIS A CD2 1 ATOM 1760 C CE1 . HIS A 1 218 ? 18.882 3.860 39.742 1.00 284.64 ? 237 HIS A CE1 1 ATOM 1761 N NE2 . HIS A 1 218 ? 18.242 3.844 38.573 1.00 217.55 ? 237 HIS A NE2 1 ATOM 1762 N N . PRO A 1 219 ? 21.404 7.197 39.601 1.00 212.81 ? 238 PRO A N 1 ATOM 1763 C CA . PRO A 1 219 ? 21.651 7.796 40.918 1.00 295.83 ? 238 PRO A CA 1 ATOM 1764 C C . PRO A 1 219 ? 21.867 6.800 42.062 1.00 300.00 ? 238 PRO A C 1 ATOM 1765 O O . PRO A 1 219 ? 22.465 7.169 43.074 1.00 300.00 ? 238 PRO A O 1 ATOM 1766 C CB . PRO A 1 219 ? 20.396 8.639 41.160 1.00 300.00 ? 238 PRO A CB 1 ATOM 1767 C CG . PRO A 1 219 ? 19.339 7.973 40.362 1.00 300.00 ? 238 PRO A CG 1 ATOM 1768 C CD . PRO A 1 219 ? 20.044 7.526 39.122 1.00 218.54 ? 238 PRO A CD 1 ATOM 1769 N N . GLU A 1 220 ? 21.370 5.562 41.914 1.00 300.00 ? 239 GLU A N 1 ATOM 1770 C CA . GLU A 1 220 ? 21.431 4.540 42.961 1.00 300.00 ? 239 GLU A CA 1 ATOM 1771 C C . GLU A 1 220 ? 22.366 3.383 42.637 1.00 298.26 ? 239 GLU A C 1 ATOM 1772 O O . GLU A 1 220 ? 23.056 2.887 43.528 1.00 297.34 ? 239 GLU A O 1 ATOM 1773 C CB . GLU A 1 220 ? 20.021 3.988 43.252 1.00 300.00 ? 239 GLU A CB 1 ATOM 1774 C CG . GLU A 1 220 ? 18.879 4.982 43.071 1.00 300.00 ? 239 GLU A CG 1 ATOM 1775 C CD . GLU A 1 220 ? 18.759 6.107 44.082 1.00 300.00 ? 239 GLU A CD 1 ATOM 1776 O OE1 . GLU A 1 220 ? 19.256 5.954 45.222 1.00 300.00 ? 239 GLU A OE1 1 ATOM 1777 O OE2 . GLU A 1 220 ? 18.136 7.138 43.740 1.00 300.00 ? 239 GLU A OE2 1 ATOM 1778 N N . VAL A 1 221 ? 22.358 2.933 41.375 1.00 296.22 ? 240 VAL A N 1 ATOM 1779 C CA . VAL A 1 221 ? 23.135 1.788 40.903 1.00 283.69 ? 240 VAL A CA 1 ATOM 1780 C C . VAL A 1 221 ? 24.424 2.221 40.194 1.00 198.39 ? 240 VAL A C 1 ATOM 1781 O O . VAL A 1 221 ? 24.360 3.073 39.306 1.00 184.32 ? 240 VAL A O 1 ATOM 1782 C CB . VAL A 1 221 ? 22.260 0.863 40.018 1.00 230.31 ? 240 VAL A CB 1 ATOM 1783 C CG1 . VAL A 1 221 ? 23.049 -0.340 39.505 1.00 211.66 ? 240 VAL A CG1 1 ATOM 1784 C CG2 . VAL A 1 221 ? 21.011 0.409 40.769 1.00 295.32 ? 240 VAL A CG2 1 ATOM 1785 N N . PRO A 1 222 ? 25.585 1.614 40.555 1.00 206.58 ? 241 PRO A N 1 ATOM 1786 C CA . PRO A 1 222 ? 26.845 1.961 39.899 1.00 177.47 ? 241 PRO A CA 1 ATOM 1787 C C . PRO A 1 222 ? 26.908 1.482 38.445 1.00 163.79 ? 241 PRO A C 1 ATOM 1788 O O . PRO A 1 222 ? 26.874 0.278 38.176 1.00 162.32 ? 241 PRO A O 1 ATOM 1789 C CB . PRO A 1 222 ? 27.910 1.302 40.784 1.00 192.11 ? 241 PRO A CB 1 ATOM 1790 C CG . PRO A 1 222 ? 27.192 0.229 41.516 1.00 262.99 ? 241 PRO A CG 1 ATOM 1791 C CD . PRO A 1 222 ? 25.822 0.774 41.747 1.00 288.55 ? 241 PRO A CD 1 ATOM 1792 N N . CYS A 1 223 ? 26.971 2.453 37.517 1.00 155.85 ? 242 CYS A N 1 ATOM 1793 C CA . CYS A 1 223 ? 27.094 2.296 36.062 1.00 144.34 ? 242 CYS A CA 1 ATOM 1794 C C . CYS A 1 223 ? 26.356 1.078 35.460 1.00 143.36 ? 242 CYS A C 1 ATOM 1795 O O . CYS A 1 223 ? 27.008 0.139 34.995 1.00 138.45 ? 242 CYS A O 1 ATOM 1796 C CB . CYS A 1 223 ? 28.563 2.332 35.650 1.00 136.10 ? 242 CYS A CB 1 ATOM 1797 S SG . CYS A 1 223 ? 29.517 3.678 36.401 1.00 139.44 ? 242 CYS A SG 1 ATOM 1798 N N . PRO A 1 224 ? 25.008 1.083 35.470 1.00 149.42 ? 243 PRO A N 1 ATOM 1799 C CA . PRO A 1 224 ? 24.276 -0.062 34.928 1.00 150.12 ? 243 PRO A CA 1 ATOM 1800 C C . PRO A 1 224 ? 24.055 -0.021 33.407 1.00 141.66 ? 243 PRO A C 1 ATOM 1801 O O . PRO A 1 224 ? 23.627 -1.026 32.835 1.00 141.90 ? 243 PRO A O 1 ATOM 1802 C CB . PRO A 1 224 ? 22.951 0.000 35.680 1.00 161.66 ? 243 PRO A CB 1 ATOM 1803 C CG . PRO A 1 224 ? 22.729 1.441 35.915 1.00 163.80 ? 243 PRO A CG 1 ATOM 1804 C CD . PRO A 1 224 ? 24.080 2.091 36.029 1.00 157.57 ? 243 PRO A CD 1 ATOM 1805 N N . TYR A 1 225 ? 24.325 1.131 32.763 1.00 135.93 ? 244 TYR A N 1 ATOM 1806 C CA . TYR A 1 225 ? 24.078 1.340 31.334 1.00 130.34 ? 244 TYR A CA 1 ATOM 1807 C C . TYR A 1 225 ? 25.342 1.384 30.488 1.00 121.49 ? 244 TYR A C 1 ATOM 1808 O O . TYR A 1 225 ? 25.597 0.465 29.707 1.00 118.52 ? 244 TYR A O 1 ATOM 1809 C CB . TYR A 1 225 ? 23.229 2.614 31.119 1.00 133.61 ? 244 TYR A CB 1 ATOM 1810 C CG . TYR A 1 225 ? 22.025 2.714 32.031 1.00 144.22 ? 244 TYR A CG 1 ATOM 1811 C CD1 . TYR A 1 225 ? 21.060 1.714 32.056 1.00 149.45 ? 244 TYR A CD1 1 ATOM 1812 C CD2 . TYR A 1 225 ? 21.848 3.811 32.869 1.00 150.60 ? 244 TYR A CD2 1 ATOM 1813 C CE1 . TYR A 1 225 ? 19.965 1.786 32.913 1.00 160.60 ? 244 TYR A CE1 1 ATOM 1814 C CE2 . TYR A 1 225 ? 20.744 3.904 33.717 1.00 162.35 ? 244 TYR A CE2 1 ATOM 1815 C CZ . TYR A 1 225 ? 19.806 2.885 33.737 1.00 167.07 ? 244 TYR A CZ 1 ATOM 1816 O OH . TYR A 1 225 ? 18.707 2.963 34.557 1.00 179.98 ? 244 TYR A OH 1 ATOM 1817 N N . ASP A 1 226 ? 26.105 2.475 30.619 1.00 118.46 ? 245 ASP A N 1 ATOM 1818 C CA . ASP A 1 226 ? 27.351 2.713 29.898 1.00 111.17 ? 245 ASP A CA 1 ATOM 1819 C C . ASP A 1 226 ? 28.476 2.855 30.901 1.00 110.66 ? 245 ASP A C 1 ATOM 1820 O O . ASP A 1 226 ? 28.214 3.202 32.056 1.00 116.00 ? 245 ASP A O 1 ATOM 1821 C CB . ASP A 1 226 ? 27.238 3.975 29.028 1.00 109.64 ? 245 ASP A CB 1 ATOM 1822 C CG . ASP A 1 226 ? 26.003 4.021 28.154 1.00 112.71 ? 245 ASP A CG 1 ATOM 1823 O OD1 . ASP A 1 226 ? 25.505 2.941 27.776 1.00 113.05 ? 245 ASP A OD1 1 ATOM 1824 O OD2 . ASP A 1 226 ? 25.543 5.135 27.842 1.00 114.74 ? 245 ASP A OD2 1 ATOM 1825 N N . TYR A 1 227 ? 29.725 2.570 30.481 1.00 105.33 ? 246 TYR A N 1 ATOM 1826 C CA . TYR A 1 227 ? 30.868 2.634 31.391 1.00 105.54 ? 246 TYR A CA 1 ATOM 1827 C C . TYR A 1 227 ? 32.224 2.492 30.735 1.00 100.47 ? 246 TYR A C 1 ATOM 1828 O O . TYR A 1 227 ? 32.345 1.967 29.626 1.00 97.27 ? 246 TYR A O 1 ATOM 1829 C CB . TYR A 1 227 ? 30.747 1.547 32.485 1.00 110.87 ? 246 TYR A CB 1 ATOM 1830 C CG . TYR A 1 227 ? 30.588 0.143 31.940 1.00 110.86 ? 246 TYR A CG 1 ATOM 1831 C CD1 . TYR A 1 227 ? 31.699 -0.630 31.612 1.00 108.34 ? 246 TYR A CD1 1 ATOM 1832 C CD2 . TYR A 1 227 ? 29.327 -0.422 31.770 1.00 114.10 ? 246 TYR A CD2 1 ATOM 1833 C CE1 . TYR A 1 227 ? 31.559 -1.920 31.105 1.00 109.93 ? 246 TYR A CE1 1 ATOM 1834 C CE2 . TYR A 1 227 ? 29.174 -1.712 31.264 1.00 115.51 ? 246 TYR A CE2 1 ATOM 1835 C CZ . TYR A 1 227 ? 30.294 -2.463 30.945 1.00 113.80 ? 246 TYR A CZ 1 ATOM 1836 O OH . TYR A 1 227 ? 30.152 -3.736 30.449 1.00 117.23 ? 246 TYR A OH 1 ATOM 1837 N N . ILE A 1 228 ? 33.254 2.889 31.493 1.00 100.90 ? 247 ILE A N 1 ATOM 1838 C CA . ILE A 1 228 ? 34.659 2.718 31.165 1.00 97.86 ? 247 ILE A CA 1 ATOM 1839 C C . ILE A 1 228 ? 35.233 1.766 32.205 1.00 101.83 ? 247 ILE A C 1 ATOM 1840 O O . ILE A 1 228 ? 35.022 1.955 33.405 1.00 107.16 ? 247 ILE A O 1 ATOM 1841 C CB . ILE A 1 228 ? 35.477 4.044 31.156 1.00 97.21 ? 247 ILE A CB 1 ATOM 1842 C CG1 . ILE A 1 228 ? 35.024 5.003 30.042 1.00 94.61 ? 247 ILE A CG1 1 ATOM 1843 C CG2 . ILE A 1 228 ? 36.994 3.760 31.060 1.00 95.73 ? 247 ILE A CG2 1 ATOM 1844 C CD1 . ILE A 1 228 ? 35.702 6.393 30.097 1.00 95.49 ? 247 ILE A CD1 1 ATOM 1845 N N . LYS A 1 229 ? 35.975 0.765 31.740 1.00 100.80 ? 248 LYS A N 1 ATOM 1846 C CA . LYS A 1 229 ? 36.742 -0.146 32.576 1.00 105.21 ? 248 LYS A CA 1 ATOM 1847 C C . LYS A 1 229 ? 38.175 0.009 32.093 1.00 103.00 ? 248 LYS A C 1 ATOM 1848 O O . LYS A 1 229 ? 38.406 0.137 30.886 1.00 98.76 ? 248 LYS A O 1 ATOM 1849 C CB . LYS A 1 229 ? 36.288 -1.600 32.416 1.00 108.73 ? 248 LYS A CB 1 ATOM 1850 C CG . LYS A 1 229 ? 35.063 -1.974 33.234 1.00 114.18 ? 248 LYS A CG 1 ATOM 1851 C CD . LYS A 1 229 ? 34.603 -3.380 32.860 1.00 117.41 ? 248 LYS A CD 1 ATOM 1852 C CE . LYS A 1 229 ? 33.458 -3.880 33.706 1.00 125.10 ? 248 LYS A CE 1 ATOM 1853 N NZ . LYS A 1 229 ? 33.110 -5.289 33.385 1.00 129.86 ? 248 LYS A NZ 1 ATOM 1854 N N . ILE A 1 230 ? 39.128 0.056 33.026 1.00 106.62 ? 249 ILE A N 1 ATOM 1855 C CA . ILE A 1 230 ? 40.539 0.199 32.683 1.00 106.01 ? 249 ILE A CA 1 ATOM 1856 C C . ILE A 1 230 ? 41.320 -0.973 33.258 1.00 112.33 ? 249 ILE A C 1 ATOM 1857 O O . ILE A 1 230 ? 41.462 -1.075 34.478 1.00 117.98 ? 249 ILE A O 1 ATOM 1858 C CB . ILE A 1 230 ? 41.133 1.575 33.102 1.00 105.73 ? 249 ILE A CB 1 ATOM 1859 C CG1 . ILE A 1 230 ? 40.368 2.748 32.448 1.00 101.13 ? 249 ILE A CG1 1 ATOM 1860 C CG2 . ILE A 1 230 ? 42.629 1.639 32.777 1.00 106.20 ? 249 ILE A CG2 1 ATOM 1861 C CD1 . ILE A 1 230 ? 40.686 4.141 32.995 1.00 102.77 ? 249 ILE A CD1 1 ATOM 1862 N N . LYS A 1 231 ? 41.824 -1.855 32.382 1.00 112.74 ? 250 LYS A N 1 ATOM 1863 C CA . LYS A 1 231 ? 42.615 -2.993 32.826 1.00 120.27 ? 250 LYS A CA 1 ATOM 1864 C C . LYS A 1 231 ? 44.101 -2.681 32.751 1.00 122.04 ? 250 LYS A C 1 ATOM 1865 O O . LYS A 1 231 ? 44.625 -2.365 31.683 1.00 118.82 ? 250 LYS A O 1 ATOM 1866 C CB . LYS A 1 231 ? 42.267 -4.287 32.070 1.00 122.95 ? 250 LYS A CB 1 ATOM 1867 C CG . LYS A 1 231 ? 43.012 -5.506 32.618 1.00 132.77 ? 250 LYS A CG 1 ATOM 1868 C CD . LYS A 1 231 ? 42.515 -6.814 32.040 1.00 138.04 ? 250 LYS A CD 1 ATOM 1869 C CE . LYS A 1 231 ? 43.194 -7.992 32.695 1.00 149.25 ? 250 LYS A CE 1 ATOM 1870 N NZ . LYS A 1 231 ? 42.758 -9.281 32.100 1.00 156.16 ? 250 LYS A NZ 1 ATOM 1871 N N . VAL A 1 232 ? 44.765 -2.766 33.903 1.00 128.31 ? 251 VAL A N 1 ATOM 1872 C CA . VAL A 1 232 ? 46.199 -2.555 34.070 1.00 132.47 ? 251 VAL A CA 1 ATOM 1873 C C . VAL A 1 232 ? 46.713 -3.746 34.871 1.00 142.96 ? 251 VAL A C 1 ATOM 1874 O O . VAL A 1 232 ? 46.273 -3.969 36.004 1.00 148.23 ? 251 VAL A O 1 ATOM 1875 C CB . VAL A 1 232 ? 46.568 -1.156 34.654 1.00 130.68 ? 251 VAL A CB 1 ATOM 1876 C CG1 . VAL A 1 232 ? 45.504 -0.635 35.617 1.00 130.65 ? 251 VAL A CG1 1 ATOM 1877 C CG2 . VAL A 1 232 ? 47.947 -1.151 35.306 1.00 138.56 ? 251 VAL A CG2 1 ATOM 1878 N N . GLY A 1 233 ? 47.574 -4.561 34.236 1.00 147.71 ? 252 GLY A N 1 ATOM 1879 C CA . GLY A 1 233 ? 48.085 -5.799 34.819 1.00 159.54 ? 252 GLY A CA 1 ATOM 1880 C C . GLY A 1 233 ? 46.896 -6.769 34.973 1.00 161.76 ? 252 GLY A C 1 ATOM 1881 O O . GLY A 1 233 ? 46.018 -6.773 34.107 1.00 154.90 ? 252 GLY A O 1 ATOM 1882 N N . PRO A 1 234 ? 46.817 -7.531 36.087 1.00 172.16 ? 253 PRO A N 1 ATOM 1883 C CA . PRO A 1 234 ? 45.680 -8.434 36.287 1.00 176.12 ? 253 PRO A CA 1 ATOM 1884 C C . PRO A 1 234 ? 44.567 -7.747 37.105 1.00 172.38 ? 253 PRO A C 1 ATOM 1885 O O . PRO A 1 234 ? 43.844 -8.415 37.849 1.00 224.92 ? 253 PRO A O 1 ATOM 1886 C CB . PRO A 1 234 ? 46.312 -9.609 37.036 1.00 266.17 ? 253 PRO A CB 1 ATOM 1887 C CG . PRO A 1 234 ? 47.440 -8.995 37.815 1.00 267.59 ? 253 PRO A CG 1 ATOM 1888 C CD . PRO A 1 234 ? 47.807 -7.678 37.175 1.00 184.72 ? 253 PRO A CD 1 ATOM 1889 N N . LYS A 1 235 ? 44.433 -6.418 36.961 1.00 162.20 ? 254 LYS A N 1 ATOM 1890 C CA . LYS A 1 235 ? 43.478 -5.624 37.725 1.00 160.48 ? 254 LYS A CA 1 ATOM 1891 C C . LYS A 1 235 ? 42.635 -4.698 36.849 1.00 148.13 ? 254 LYS A C 1 ATOM 1892 O O . LYS A 1 235 ? 43.159 -4.060 35.937 1.00 140.53 ? 254 LYS A O 1 ATOM 1893 C CB . LYS A 1 235 ? 44.242 -4.823 38.792 1.00 165.61 ? 254 LYS A CB 1 ATOM 1894 C CG . LYS A 1 235 ? 43.373 -4.115 39.826 1.00 169.11 ? 254 LYS A CG 1 ATOM 1895 C CD . LYS A 1 235 ? 44.183 -3.085 40.596 1.00 174.64 ? 254 LYS A CD 1 ATOM 1896 C CE . LYS A 1 235 ? 43.346 -2.305 41.578 1.00 198.87 ? 254 LYS A CE 1 ATOM 1897 N NZ . LYS A 1 235 ? 44.146 -1.260 42.271 1.00 204.13 ? 254 LYS A NZ 1 ATOM 1898 N N . VAL A 1 236 ? 41.333 -4.602 37.161 1.00 147.56 ? 255 VAL A N 1 ATOM 1899 C CA . VAL A 1 236 ? 40.398 -3.738 36.441 1.00 137.69 ? 255 VAL A CA 1 ATOM 1900 C C . VAL A 1 236 ? 39.971 -2.578 37.335 1.00 138.42 ? 255 VAL A C 1 ATOM 1901 O O . VAL A 1 236 ? 39.528 -2.792 38.466 1.00 147.05 ? 255 VAL A O 1 ATOM 1902 C CB . VAL A 1 236 ? 39.172 -4.508 35.870 1.00 136.90 ? 255 VAL A CB 1 ATOM 1903 C CG1 . VAL A 1 236 ? 38.239 -3.579 35.092 1.00 127.52 ? 255 VAL A CG1 1 ATOM 1904 C CG2 . VAL A 1 236 ? 39.611 -5.677 34.994 1.00 138.34 ? 255 VAL A CG2 1 ATOM 1905 N N . LEU A 1 237 ? 40.097 -1.355 36.813 1.00 130.94 ? 256 LEU A N 1 ATOM 1906 C CA . LEU A 1 237 ? 39.672 -0.144 37.501 1.00 132.21 ? 256 LEU A CA 1 ATOM 1907 C C . LEU A 1 237 ? 38.325 0.271 36.945 1.00 127.22 ? 256 LEU A C 1 ATOM 1908 O O . LEU A 1 237 ? 38.073 0.124 35.745 1.00 119.80 ? 256 LEU A O 1 ATOM 1909 C CB . LEU A 1 237 ? 40.689 0.996 37.336 1.00 129.20 ? 256 LEU A CB 1 ATOM 1910 C CG . LEU A 1 237 ? 42.109 0.738 37.842 1.00 134.56 ? 256 LEU A CG 1 ATOM 1911 C CD1 . LEU A 1 237 ? 43.047 1.821 37.369 1.00 130.54 ? 256 LEU A CD1 1 ATOM 1912 C CD2 . LEU A 1 237 ? 42.156 0.627 39.364 1.00 146.49 ? 256 LEU A CD2 1 ATOM 1913 N N . GLY A 1 238 ? 37.459 0.777 37.823 1.00 132.71 ? 257 GLY A N 1 ATOM 1914 C CA . GLY A 1 238 ? 36.118 1.210 37.460 1.00 130.20 ? 257 GLY A CA 1 ATOM 1915 C C . GLY A 1 238 ? 35.057 0.232 37.965 1.00 137.14 ? 257 GLY A C 1 ATOM 1916 O O . GLY A 1 238 ? 35.309 -0.471 38.947 1.00 145.94 ? 257 GLY A O 1 ATOM 1917 N N . PRO A 1 239 ? 33.870 0.187 37.311 1.00 134.52 ? 258 PRO A N 1 ATOM 1918 C CA . PRO A 1 239 ? 33.457 0.964 36.133 1.00 125.70 ? 258 PRO A CA 1 ATOM 1919 C C . PRO A 1 239 ? 33.290 2.460 36.413 1.00 126.75 ? 258 PRO A C 1 ATOM 1920 O O . PRO A 1 239 ? 32.988 2.848 37.543 1.00 135.22 ? 258 PRO A O 1 ATOM 1921 C CB . PRO A 1 239 ? 32.143 0.293 35.716 1.00 126.44 ? 258 PRO A CB 1 ATOM 1922 C CG . PRO A 1 239 ? 31.597 -0.281 36.983 1.00 138.12 ? 258 PRO A CG 1 ATOM 1923 C CD . PRO A 1 239 ? 32.805 -0.737 37.749 1.00 141.77 ? 258 PRO A CD 1 ATOM 1924 N N . PHE A 1 240 ? 33.514 3.291 35.384 1.00 119.51 ? 259 PHE A N 1 ATOM 1925 C CA . PHE A 1 240 ? 33.384 4.744 35.488 1.00 121.24 ? 259 PHE A CA 1 ATOM 1926 C C . PHE A 1 240 ? 32.283 5.270 34.584 1.00 118.94 ? 259 PHE A C 1 ATOM 1927 O O . PHE A 1 240 ? 32.194 4.871 33.423 1.00 112.48 ? 259 PHE A O 1 ATOM 1928 C CB . PHE A 1 240 ? 34.710 5.450 35.169 1.00 117.19 ? 259 PHE A CB 1 ATOM 1929 C CG . PHE A 1 240 ? 35.887 5.019 36.009 1.00 120.22 ? 259 PHE A CG 1 ATOM 1930 C CD1 . PHE A 1 240 ? 35.922 5.280 37.374 1.00 129.59 ? 259 PHE A CD1 1 ATOM 1931 C CD2 . PHE A 1 240 ? 36.967 4.362 35.434 1.00 115.03 ? 259 PHE A CD2 1 ATOM 1932 C CE1 . PHE A 1 240 ? 37.015 4.884 38.151 1.00 133.89 ? 259 PHE A CE1 1 ATOM 1933 C CE2 . PHE A 1 240 ? 38.067 3.980 36.208 1.00 119.34 ? 259 PHE A CE2 1 ATOM 1934 C CZ . PHE A 1 240 ? 38.082 4.241 37.562 1.00 128.31 ? 259 PHE A CZ 1 ATOM 1935 N N . CYS A 1 241 ? 31.448 6.171 35.122 1.00 125.63 ? 260 CYS A N 1 ATOM 1936 C CA . CYS A 1 241 ? 30.331 6.811 34.419 1.00 125.77 ? 260 CYS A CA 1 ATOM 1937 C C . CYS A 1 241 ? 29.965 8.129 35.108 1.00 134.53 ? 260 CYS A C 1 ATOM 1938 O O . CYS A 1 241 ? 30.603 8.504 36.094 1.00 140.00 ? 260 CYS A O 1 ATOM 1939 C CB . CYS A 1 241 ? 29.129 5.870 34.339 1.00 127.49 ? 260 CYS A CB 1 ATOM 1940 S SG . CYS A 1 241 ? 28.473 5.364 35.950 1.00 139.47 ? 260 CYS A SG 1 ATOM 1941 N N . GLY A 1 242 ? 28.942 8.831 34.592 1.00 137.25 ? 261 GLY A N 1 ATOM 1942 C CA . GLY A 1 242 ? 28.466 10.078 35.186 1.00 147.82 ? 261 GLY A CA 1 ATOM 1943 C C . GLY A 1 242 ? 28.959 11.346 34.501 1.00 147.31 ? 261 GLY A C 1 ATOM 1944 O O . GLY A 1 242 ? 29.450 11.308 33.371 1.00 138.52 ? 261 GLY A O 1 ATOM 1945 N N . GLU A 1 243 ? 28.808 12.474 35.208 1.00 158.54 ? 262 GLU A N 1 ATOM 1946 C CA . GLU A 1 243 ? 29.182 13.811 34.746 1.00 161.86 ? 262 GLU A CA 1 ATOM 1947 C C . GLU A 1 243 ? 30.531 14.271 35.311 1.00 162.90 ? 262 GLU A C 1 ATOM 1948 O O . GLU A 1 243 ? 31.038 15.320 34.907 1.00 165.62 ? 262 GLU A O 1 ATOM 1949 C CB . GLU A 1 243 ? 28.074 14.817 35.096 1.00 175.89 ? 262 GLU A CB 1 ATOM 1950 C CG . GLU A 1 243 ? 26.766 14.561 34.364 1.00 176.49 ? 262 GLU A CG 1 ATOM 1951 C CD . GLU A 1 243 ? 25.541 15.208 34.980 1.00 192.74 ? 262 GLU A CD 1 ATOM 1952 O OE1 . GLU A 1 243 ? 25.546 16.447 35.163 1.00 203.49 ? 262 GLU A OE1 1 ATOM 1953 O OE2 . GLU A 1 243 ? 24.559 14.478 35.247 1.00 196.12 ? 262 GLU A OE2 1 ATOM 1954 N N . LYS A 1 244 ? 31.110 13.485 36.236 1.00 162.10 ? 263 LYS A N 1 ATOM 1955 C CA . LYS A 1 244 ? 32.393 13.785 36.864 1.00 164.29 ? 263 LYS A CA 1 ATOM 1956 C C . LYS A 1 244 ? 33.417 12.705 36.525 1.00 152.54 ? 263 LYS A C 1 ATOM 1957 O O . LYS A 1 244 ? 33.222 11.533 36.858 1.00 149.67 ? 263 LYS A O 1 ATOM 1958 C CB . LYS A 1 244 ? 32.227 13.955 38.388 1.00 178.12 ? 263 LYS A CB 1 ATOM 1959 C CG . LYS A 1 244 ? 33.480 14.433 39.127 1.00 183.94 ? 263 LYS A CG 1 ATOM 1960 C CD . LYS A 1 244 ? 33.552 15.960 39.259 1.00 196.72 ? 263 LYS A CD 1 ATOM 1961 C CE . LYS A 1 244 ? 34.649 16.420 40.195 1.00 206.15 ? 263 LYS A CE 1 ATOM 1962 N NZ . LYS A 1 244 ? 36.010 16.163 39.646 1.00 195.68 ? 263 LYS A NZ 1 ATOM 1963 N N . ALA A 1 245 ? 34.502 13.112 35.850 1.00 147.22 ? 264 ALA A N 1 ATOM 1964 C CA . ALA A 1 245 ? 35.593 12.234 35.438 1.00 137.70 ? 264 ALA A CA 1 ATOM 1965 C C . ALA A 1 245 ? 36.383 11.731 36.643 1.00 141.96 ? 264 ALA A C 1 ATOM 1966 O O . ALA A 1 245 ? 36.533 12.480 37.613 1.00 152.26 ? 264 ALA A O 1 ATOM 1967 C CB . ALA A 1 245 ? 36.522 12.976 34.494 1.00 133.59 ? 264 ALA A CB 1 ATOM 1968 N N . PRO A 1 246 ? 36.913 10.479 36.586 1.00 135.58 ? 265 PRO A N 1 ATOM 1969 C CA . PRO A 1 246 ? 37.725 9.982 37.700 1.00 140.72 ? 265 PRO A CA 1 ATOM 1970 C C . PRO A 1 246 ? 39.018 10.785 37.798 1.00 143.48 ? 265 PRO A C 1 ATOM 1971 O O . PRO A 1 246 ? 39.449 11.388 36.809 1.00 138.48 ? 265 PRO A O 1 ATOM 1972 C CB . PRO A 1 246 ? 38.004 8.521 37.329 1.00 133.08 ? 265 PRO A CB 1 ATOM 1973 C CG . PRO A 1 246 ? 37.756 8.428 35.877 1.00 123.15 ? 265 PRO A CG 1 ATOM 1974 C CD . PRO A 1 246 ? 36.683 9.420 35.582 1.00 125.13 ? 265 PRO A CD 1 ATOM 1975 N N . GLU A 1 247 ? 39.629 10.794 38.989 1.00 152.52 ? 266 GLU A N 1 ATOM 1976 C CA . GLU A 1 247 ? 40.881 11.504 39.244 1.00 156.69 ? 266 GLU A CA 1 ATOM 1977 C C . GLU A 1 247 ? 42.023 10.894 38.416 1.00 147.28 ? 266 GLU A C 1 ATOM 1978 O O . GLU A 1 247 ? 41.907 9.724 38.036 1.00 140.14 ? 266 GLU A O 1 ATOM 1979 C CB . GLU A 1 247 ? 41.215 11.495 40.746 1.00 169.77 ? 266 GLU A CB 1 ATOM 1980 C CG . GLU A 1 247 ? 40.228 12.275 41.606 1.00 182.38 ? 266 GLU A CG 1 ATOM 1981 C CD . GLU A 1 247 ? 40.021 13.737 41.251 1.00 187.96 ? 266 GLU A CD 1 ATOM 1982 O OE1 . GLU A 1 247 ? 41.022 14.486 41.187 1.00 191.01 ? 266 GLU A OE1 1 ATOM 1983 O OE2 . GLU A 1 247 ? 38.851 14.136 41.051 1.00 190.66 ? 266 GLU A OE2 1 ATOM 1984 N N . PRO A 1 248 ? 43.104 11.674 38.104 1.00 148.48 ? 267 PRO A N 1 ATOM 1985 C CA . PRO A 1 248 ? 44.224 11.152 37.308 1.00 141.68 ? 267 PRO A CA 1 ATOM 1986 C C . PRO A 1 248 ? 44.739 9.807 37.819 1.00 141.53 ? 267 PRO A C 1 ATOM 1987 O O . PRO A 1 248 ? 44.826 9.599 39.032 1.00 149.95 ? 267 PRO A O 1 ATOM 1988 C CB . PRO A 1 248 ? 45.283 12.247 37.421 1.00 148.24 ? 267 PRO A CB 1 ATOM 1989 C CG . PRO A 1 248 ? 44.510 13.484 37.603 1.00 154.62 ? 267 PRO A CG 1 ATOM 1990 C CD . PRO A 1 248 ? 43.262 13.125 38.350 1.00 157.85 ? 267 PRO A CD 1 ATOM 1991 N N . ILE A 1 249 ? 45.032 8.885 36.889 1.00 133.42 ? 268 ILE A N 1 ATOM 1992 C CA . ILE A 1 249 ? 45.494 7.537 37.219 1.00 133.97 ? 268 ILE A CA 1 ATOM 1993 C C . ILE A 1 249 ? 46.962 7.333 36.868 1.00 134.59 ? 268 ILE A C 1 ATOM 1994 O O . ILE A 1 249 ? 47.332 7.390 35.696 1.00 128.75 ? 268 ILE A O 1 ATOM 1995 C CB . ILE A 1 249 ? 44.582 6.448 36.583 1.00 126.79 ? 268 ILE A CB 1 ATOM 1996 C CG1 . ILE A 1 249 ? 43.125 6.566 37.090 1.00 128.16 ? 268 ILE A CG1 1 ATOM 1997 C CG2 . ILE A 1 249 ? 45.149 5.033 36.824 1.00 128.15 ? 268 ILE A CG2 1 ATOM 1998 C CD1 . ILE A 1 249 ? 42.071 5.894 36.197 1.00 121.14 ? 268 ILE A CD1 1 ATOM 1999 N N . SER A 1 250 ? 47.786 7.050 37.885 1.00 142.91 ? 269 SER A N 1 ATOM 2000 C CA . SER A 1 250 ? 49.202 6.767 37.695 1.00 145.63 ? 269 SER A CA 1 ATOM 2001 C C . SER A 1 250 ? 49.405 5.254 37.760 1.00 146.09 ? 269 SER A C 1 ATOM 2002 O O . SER A 1 250 ? 49.350 4.671 38.847 1.00 153.49 ? 269 SER A O 1 ATOM 2003 C CB . SER A 1 250 ? 50.046 7.476 38.752 1.00 156.41 ? 269 SER A CB 1 ATOM 2004 O OG . SER A 1 250 ? 49.906 8.885 38.676 1.00 158.27 ? 269 SER A OG 1 ATOM 2005 N N . THR A 1 251 ? 49.582 4.611 36.593 1.00 139.79 ? 270 THR A N 1 ATOM 2006 C CA . THR A 1 251 ? 49.814 3.165 36.541 1.00 141.65 ? 270 THR A CA 1 ATOM 2007 C C . THR A 1 251 ? 51.307 2.906 36.690 1.00 149.07 ? 270 THR A C 1 ATOM 2008 O O . THR A 1 251 ? 52.116 3.830 36.568 1.00 151.23 ? 270 THR A O 1 ATOM 2009 C CB . THR A 1 251 ? 49.262 2.515 35.243 1.00 133.99 ? 270 THR A CB 1 ATOM 2010 O OG1 . THR A 1 251 ? 50.161 2.742 34.153 1.00 132.53 ? 270 THR A OG1 1 ATOM 2011 C CG2 . THR A 1 251 ? 47.851 2.972 34.889 1.00 125.81 ? 270 THR A CG2 1 ATOM 2012 N N . GLN A 1 252 ? 51.666 1.650 36.947 1.00 154.47 ? 271 GLN A N 1 ATOM 2013 C CA . GLN A 1 252 ? 53.052 1.209 37.042 1.00 162.31 ? 271 GLN A CA 1 ATOM 2014 C C . GLN A 1 252 ? 53.258 0.254 35.864 1.00 159.79 ? 271 GLN A C 1 ATOM 2015 O O . GLN A 1 252 ? 54.100 -0.644 35.919 1.00 167.80 ? 271 GLN A O 1 ATOM 2016 C CB . GLN A 1 252 ? 53.308 0.495 38.387 1.00 173.83 ? 271 GLN A CB 1 ATOM 2017 C CG . GLN A 1 252 ? 52.905 1.285 39.637 1.00 178.56 ? 271 GLN A CG 1 ATOM 2018 C CD . GLN A 1 252 ? 53.664 2.577 39.807 1.00 180.98 ? 271 GLN A CD 1 ATOM 2019 O OE1 . GLN A 1 252 ? 53.107 3.671 39.665 1.00 175.95 ? 271 GLN A OE1 1 ATOM 2020 N NE2 . GLN A 1 252 ? 54.950 2.483 40.110 1.00 188.83 ? 271 GLN A NE2 1 ATOM 2021 N N . SER A 1 253 ? 52.480 0.470 34.786 1.00 150.25 ? 272 SER A N 1 ATOM 2022 C CA . SER A 1 253 ? 52.441 -0.397 33.618 1.00 148.73 ? 272 SER A CA 1 ATOM 2023 C C . SER A 1 253 ? 52.713 0.295 32.293 1.00 143.91 ? 272 SER A C 1 ATOM 2024 O O . SER A 1 253 ? 52.321 1.444 32.101 1.00 137.92 ? 272 SER A O 1 ATOM 2025 C CB . SER A 1 253 ? 51.084 -1.089 33.559 1.00 144.19 ? 272 SER A CB 1 ATOM 2026 O OG . SER A 1 253 ? 51.017 -2.102 32.570 1.00 145.94 ? 272 SER A OG 1 ATOM 2027 N N . HIS A 1 254 ? 53.342 -0.441 31.361 1.00 147.83 ? 273 HIS A N 1 ATOM 2028 C CA . HIS A 1 254 ? 53.636 0.016 30.002 1.00 146.16 ? 273 HIS A CA 1 ATOM 2029 C C . HIS A 1 254 ? 52.469 -0.287 29.074 1.00 139.96 ? 273 HIS A C 1 ATOM 2030 O O . HIS A 1 254 ? 52.461 0.167 27.931 1.00 138.70 ? 273 HIS A O 1 ATOM 2031 C CB . HIS A 1 254 ? 54.924 -0.634 29.468 1.00 155.93 ? 273 HIS A CB 1 ATOM 2032 C CG . HIS A 1 254 ? 54.883 -2.127 29.430 1.00 162.34 ? 273 HIS A CG 1 ATOM 2033 N ND1 . HIS A 1 254 ? 54.305 -2.808 28.373 1.00 161.90 ? 273 HIS A ND1 1 ATOM 2034 C CD2 . HIS A 1 254 ? 55.341 -3.024 30.330 1.00 170.79 ? 273 HIS A CD2 1 ATOM 2035 C CE1 . HIS A 1 254 ? 54.434 -4.092 28.663 1.00 169.81 ? 273 HIS A CE1 1 ATOM 2036 N NE2 . HIS A 1 254 ? 55.059 -4.271 29.826 1.00 175.63 ? 273 HIS A NE2 1 ATOM 2037 N N . SER A 1 255 ? 51.507 -1.089 29.550 1.00 137.68 ? 274 SER A N 1 ATOM 2038 C CA . SER A 1 255 ? 50.343 -1.467 28.765 1.00 133.09 ? 274 SER A CA 1 ATOM 2039 C C . SER A 1 255 ? 49.059 -1.260 29.536 1.00 126.72 ? 274 SER A C 1 ATOM 2040 O O . SER A 1 255 ? 48.963 -1.645 30.705 1.00 129.34 ? 274 SER A O 1 ATOM 2041 C CB . SER A 1 255 ? 50.459 -2.903 28.271 1.00 140.10 ? 274 SER A CB 1 ATOM 2042 O OG . SER A 1 255 ? 50.472 -3.813 29.358 1.00 145.54 ? 274 SER A OG 1 ATOM 2043 N N . VAL A 1 256 ? 48.083 -0.620 28.884 1.00 119.81 ? 275 VAL A N 1 ATOM 2044 C CA . VAL A 1 256 ? 46.784 -0.302 29.471 1.00 114.39 ? 275 VAL A CA 1 ATOM 2045 C C . VAL A 1 256 ? 45.676 -0.626 28.476 1.00 111.05 ? 275 VAL A C 1 ATOM 2046 O O . VAL A 1 256 ? 45.808 -0.343 27.282 1.00 110.66 ? 275 VAL A O 1 ATOM 2047 C CB . VAL A 1 256 ? 46.714 1.192 29.915 1.00 110.56 ? 275 VAL A CB 1 ATOM 2048 C CG1 . VAL A 1 256 ? 45.324 1.572 30.414 1.00 106.05 ? 275 VAL A CG1 1 ATOM 2049 C CG2 . VAL A 1 256 ? 47.759 1.519 30.976 1.00 114.81 ? 275 VAL A CG2 1 ATOM 2050 N N . LEU A 1 257 ? 44.574 -1.189 28.978 1.00 109.73 ? 276 LEU A N 1 ATOM 2051 C CA . LEU A 1 257 ? 43.401 -1.441 28.163 1.00 106.89 ? 276 LEU A CA 1 ATOM 2052 C C . LEU A 1 257 ? 42.248 -0.612 28.691 1.00 101.93 ? 276 LEU A C 1 ATOM 2053 O O . LEU A 1 257 ? 41.937 -0.666 29.881 1.00 103.06 ? 276 LEU A O 1 ATOM 2054 C CB . LEU A 1 257 ? 43.016 -2.930 28.104 1.00 111.77 ? 276 LEU A CB 1 ATOM 2055 C CG . LEU A 1 257 ? 41.661 -3.226 27.431 1.00 109.99 ? 276 LEU A CG 1 ATOM 2056 C CD1 . LEU A 1 257 ? 41.729 -3.048 25.918 1.00 109.82 ? 276 LEU A CD1 1 ATOM 2057 C CD2 . LEU A 1 257 ? 41.152 -4.592 27.797 1.00 115.22 ? 276 LEU A CD2 1 ATOM 2058 N N . ILE A 1 258 ? 41.620 0.152 27.800 1.00 98.16 ? 277 ILE A N 1 ATOM 2059 C CA . ILE A 1 258 ? 40.448 0.948 28.128 1.00 94.72 ? 277 ILE A CA 1 ATOM 2060 C C . ILE A 1 258 ? 39.281 0.323 27.389 1.00 94.55 ? 277 ILE A C 1 ATOM 2061 O O . ILE A 1 258 ? 39.306 0.220 26.160 1.00 95.09 ? 277 ILE A O 1 ATOM 2062 C CB . ILE A 1 258 ? 40.616 2.453 27.783 1.00 92.49 ? 277 ILE A CB 1 ATOM 2063 C CG1 . ILE A 1 258 ? 41.819 3.068 28.520 1.00 94.32 ? 277 ILE A CG1 1 ATOM 2064 C CG2 . ILE A 1 258 ? 39.325 3.237 28.082 1.00 90.89 ? 277 ILE A CG2 1 ATOM 2065 C CD1 . ILE A 1 258 ? 42.544 4.125 27.724 1.00 94.16 ? 277 ILE A CD1 1 ATOM 2066 N N . LEU A 1 259 ? 38.273 -0.113 28.141 1.00 94.95 ? 278 LEU A N 1 ATOM 2067 C CA . LEU A 1 259 ? 37.063 -0.682 27.572 1.00 95.32 ? 278 LEU A CA 1 ATOM 2068 C C . LEU A 1 259 ? 35.942 0.327 27.761 1.00 93.04 ? 278 LEU A C 1 ATOM 2069 O O . LEU A 1 259 ? 35.688 0.760 28.885 1.00 93.52 ? 278 LEU A O 1 ATOM 2070 C CB . LEU A 1 259 ? 36.709 -2.030 28.235 1.00 99.60 ? 278 LEU A CB 1 ATOM 2071 C CG . LEU A 1 259 ? 35.464 -2.763 27.703 1.00 102.50 ? 278 LEU A CG 1 ATOM 2072 C CD1 . LEU A 1 259 ? 35.650 -4.261 27.778 1.00 108.53 ? 278 LEU A CD1 1 ATOM 2073 C CD2 . LEU A 1 259 ? 34.195 -2.354 28.461 1.00 102.55 ? 278 LEU A CD2 1 ATOM 2074 N N . PHE A 1 260 ? 35.264 0.682 26.664 1.00 91.89 ? 279 PHE A N 1 ATOM 2075 C CA . PHE A 1 260 ? 34.125 1.587 26.704 1.00 91.50 ? 279 PHE A CA 1 ATOM 2076 C C . PHE A 1 260 ? 32.895 0.872 26.171 1.00 93.62 ? 279 PHE A C 1 ATOM 2077 O O . PHE A 1 260 ? 32.854 0.483 25.002 1.00 94.85 ? 279 PHE A O 1 ATOM 2078 C CB . PHE A 1 260 ? 34.391 2.910 25.958 1.00 90.19 ? 279 PHE A CB 1 ATOM 2079 C CG . PHE A 1 260 ? 33.219 3.870 25.970 1.00 91.32 ? 279 PHE A CG 1 ATOM 2080 C CD1 . PHE A 1 260 ? 32.579 4.202 27.161 1.00 92.70 ? 279 PHE A CD1 1 ATOM 2081 C CD2 . PHE A 1 260 ? 32.759 4.447 24.792 1.00 92.70 ? 279 PHE A CD2 1 ATOM 2082 C CE1 . PHE A 1 260 ? 31.489 5.076 27.170 1.00 95.30 ? 279 PHE A CE1 1 ATOM 2083 C CE2 . PHE A 1 260 ? 31.675 5.332 24.803 1.00 95.01 ? 279 PHE A CE2 1 ATOM 2084 C CZ . PHE A 1 260 ? 31.049 5.641 25.992 1.00 96.43 ? 279 PHE A CZ 1 ATOM 2085 N N . HIS A 1 261 ? 31.905 0.678 27.045 1.00 95.55 ? 280 HIS A N 1 ATOM 2086 C CA . HIS A 1 261 ? 30.662 0.006 26.694 1.00 98.86 ? 280 HIS A CA 1 ATOM 2087 C C . HIS A 1 261 ? 29.516 1.006 26.637 1.00 99.82 ? 280 HIS A C 1 ATOM 2088 O O . HIS A 1 261 ? 29.380 1.827 27.541 1.00 100.36 ? 280 HIS A O 1 ATOM 2089 C CB . HIS A 1 261 ? 30.358 -1.106 27.712 1.00 102.65 ? 280 HIS A CB 1 ATOM 2090 C CG . HIS A 1 261 ? 29.097 -1.864 27.436 1.00 107.16 ? 280 HIS A CG 1 ATOM 2091 N ND1 . HIS A 1 261 ? 27.883 -1.462 27.965 1.00 110.12 ? 280 HIS A ND1 1 ATOM 2092 C CD2 . HIS A 1 261 ? 28.905 -2.982 26.700 1.00 110.42 ? 280 HIS A CD2 1 ATOM 2093 C CE1 . HIS A 1 261 ? 26.995 -2.340 27.528 1.00 114.54 ? 280 HIS A CE1 1 ATOM 2094 N NE2 . HIS A 1 261 ? 27.563 -3.273 26.765 1.00 114.94 ? 280 HIS A NE2 1 ATOM 2095 N N . SER A 1 262 ? 28.691 0.930 25.580 1.00 101.58 ? 281 SER A N 1 ATOM 2096 C CA . SER A 1 262 ? 27.503 1.773 25.434 1.00 104.32 ? 281 SER A CA 1 ATOM 2097 C C . SER A 1 262 ? 26.295 0.899 25.117 1.00 108.98 ? 281 SER A C 1 ATOM 2098 O O . SER A 1 262 ? 26.401 -0.004 24.288 1.00 110.21 ? 281 SER A O 1 ATOM 2099 C CB . SER A 1 262 ? 27.706 2.861 24.382 1.00 103.59 ? 281 SER A CB 1 ATOM 2100 O OG . SER A 1 262 ? 27.756 2.344 23.063 1.00 105.08 ? 281 SER A OG 1 ATOM 2101 N N . ASP A 1 263 ? 25.166 1.132 25.804 1.00 112.82 ? 282 ASP A N 1 ATOM 2102 C CA . ASP A 1 263 ? 23.949 0.347 25.597 1.00 118.56 ? 282 ASP A CA 1 ATOM 2103 C C . ASP A 1 263 ? 23.116 0.889 24.413 1.00 121.77 ? 282 ASP A C 1 ATOM 2104 O O . ASP A 1 263 ? 23.589 1.761 23.686 1.00 119.60 ? 282 ASP A O 1 ATOM 2105 C CB . ASP A 1 263 ? 23.142 0.222 26.911 1.00 123.44 ? 282 ASP A CB 1 ATOM 2106 C CG . ASP A 1 263 ? 22.436 1.479 27.374 1.00 126.59 ? 282 ASP A CG 1 ATOM 2107 O OD1 . ASP A 1 263 ? 22.418 2.444 26.627 1.00 124.81 ? 282 ASP A OD1 1 ATOM 2108 O OD2 . ASP A 1 263 ? 21.791 1.440 28.433 1.00 132.29 ? 282 ASP A OD2 1 ATOM 2109 N N . ASN A 1 264 ? 21.879 0.410 24.247 1.00 128.22 ? 283 ASN A N 1 ATOM 2110 C CA . ASN A 1 264 ? 20.997 0.792 23.143 1.00 133.19 ? 283 ASN A CA 1 ATOM 2111 C C . ASN A 1 264 ? 20.236 2.121 23.319 1.00 136.71 ? 283 ASN A C 1 ATOM 2112 O O . ASN A 1 264 ? 19.310 2.385 22.546 1.00 142.65 ? 283 ASN A O 1 ATOM 2113 C CB . ASN A 1 264 ? 20.008 -0.352 22.873 1.00 139.75 ? 283 ASN A CB 1 ATOM 2114 C CG . ASN A 1 264 ? 18.962 -0.580 23.952 1.00 145.58 ? 283 ASN A CG 1 ATOM 2115 O OD1 . ASN A 1 264 ? 18.907 0.095 24.992 1.00 145.20 ? 283 ASN A OD1 1 ATOM 2116 N ND2 . ASN A 1 264 ? 18.088 -1.544 23.714 1.00 152.25 ? 283 ASN A ND2 1 ATOM 2117 N N . SER A 1 265 ? 20.586 2.935 24.330 1.00 134.31 ? 284 SER A N 1 ATOM 2118 C CA . SER A 1 265 ? 19.845 4.166 24.601 1.00 139.99 ? 284 SER A CA 1 ATOM 2119 C C . SER A 1 265 ? 20.700 5.326 25.111 1.00 137.01 ? 284 SER A C 1 ATOM 2120 O O . SER A 1 265 ? 21.706 5.098 25.795 1.00 131.36 ? 284 SER A O 1 ATOM 2121 C CB . SER A 1 265 ? 18.725 3.874 25.597 1.00 146.75 ? 284 SER A CB 1 ATOM 2122 O OG . SER A 1 265 ? 17.950 5.025 25.892 1.00 154.25 ? 284 SER A OG 1 ATOM 2123 N N . GLY A 1 266 ? 20.262 6.575 24.814 1.00 142.37 ? 285 GLY A N 1 ATOM 2124 C CA . GLY A 1 266 ? 20.915 7.801 25.281 1.00 142.26 ? 285 GLY A CA 1 ATOM 2125 C C . GLY A 1 266 ? 21.623 8.620 24.208 1.00 140.79 ? 285 GLY A C 1 ATOM 2126 O O . GLY A 1 266 ? 21.931 8.113 23.130 1.00 138.00 ? 285 GLY A O 1 ATOM 2127 N N . GLU A 1 267 ? 21.897 9.896 24.529 1.00 144.14 ? 286 GLU A N 1 ATOM 2128 C CA . GLU A 1 267 ? 22.567 10.842 23.632 1.00 144.71 ? 286 GLU A CA 1 ATOM 2129 C C . GLU A 1 267 ? 23.762 11.542 24.299 1.00 141.52 ? 286 GLU A C 1 ATOM 2130 O O . GLU A 1 267 ? 24.158 12.631 23.872 1.00 145.45 ? 286 GLU A O 1 ATOM 2131 C CB . GLU A 1 267 ? 21.558 11.873 23.077 1.00 155.89 ? 286 GLU A CB 1 ATOM 2132 C CG . GLU A 1 267 ? 20.393 11.287 22.289 1.00 161.21 ? 286 GLU A CG 1 ATOM 2133 C CD . GLU A 1 267 ? 20.724 10.442 21.072 1.00 157.74 ? 286 GLU A CD 1 ATOM 2134 O OE1 . GLU A 1 267 ? 21.771 10.687 20.429 1.00 154.18 ? 286 GLU A OE1 1 ATOM 2135 O OE2 . GLU A 1 267 ? 19.908 9.553 20.739 1.00 159.60 ? 286 GLU A OE2 1 ATOM 2136 N N . ASN A 1 268 ? 24.353 10.897 25.323 1.00 135.47 ? 287 ASN A N 1 ATOM 2137 C CA . ASN A 1 268 ? 25.488 11.414 26.094 1.00 133.16 ? 287 ASN A CA 1 ATOM 2138 C C . ASN A 1 268 ? 26.715 11.700 25.221 1.00 128.75 ? 287 ASN A C 1 ATOM 2139 O O . ASN A 1 268 ? 26.967 10.984 24.252 1.00 124.48 ? 287 ASN A O 1 ATOM 2140 C CB . ASN A 1 268 ? 25.792 10.519 27.295 1.00 129.07 ? 287 ASN A CB 1 ATOM 2141 C CG . ASN A 1 268 ? 24.582 10.271 28.167 1.00 135.61 ? 287 ASN A CG 1 ATOM 2142 O OD1 . ASN A 1 268 ? 24.335 10.972 29.151 1.00 143.02 ? 287 ASN A OD1 1 ATOM 2143 N ND2 . ASN A 1 268 ? 23.764 9.301 27.789 1.00 133.84 ? 287 ASN A ND2 1 ATOM 2144 N N . ARG A 1 269 ? 27.422 12.797 25.531 1.00 131.52 ? 288 ARG A N 1 ATOM 2145 C CA . ARG A 1 269 ? 28.554 13.322 24.760 1.00 130.16 ? 288 ARG A CA 1 ATOM 2146 C C . ARG A 1 269 ? 29.869 12.543 24.828 1.00 121.72 ? 288 ARG A C 1 ATOM 2147 O O . ARG A 1 269 ? 30.697 12.665 23.921 1.00 120.69 ? 288 ARG A O 1 ATOM 2148 C CB . ARG A 1 269 ? 28.748 14.821 25.027 1.00 138.65 ? 288 ARG A CB 1 ATOM 2149 C CG . ARG A 1 269 ? 27.499 15.644 24.714 1.00 149.17 ? 288 ARG A CG 1 ATOM 2150 C CD . ARG A 1 269 ? 27.710 17.131 24.913 1.00 159.71 ? 288 ARG A CD 1 ATOM 2151 N NE . ARG A 1 269 ? 28.426 17.738 23.789 1.00 162.84 ? 288 ARG A NE 1 ATOM 2152 C CZ . ARG A 1 269 ? 28.606 19.045 23.627 1.00 173.59 ? 288 ARG A CZ 1 ATOM 2153 N NH1 . ARG A 1 269 ? 28.117 19.905 24.513 1.00 182.47 ? 288 ARG A NH1 1 ATOM 2154 N NH2 . ARG A 1 269 ? 29.270 19.504 22.575 1.00 176.65 ? 288 ARG A NH2 1 ATOM 2155 N N . GLY A 1 270 ? 30.071 11.754 25.888 1.00 117.23 ? 289 GLY A N 1 ATOM 2156 C CA . GLY A 1 270 ? 31.274 10.939 25.992 1.00 110.27 ? 289 GLY A CA 1 ATOM 2157 C C . GLY A 1 270 ? 32.378 11.474 26.867 1.00 110.67 ? 289 GLY A C 1 ATOM 2158 O O . GLY A 1 270 ? 32.127 12.121 27.882 1.00 115.73 ? 289 GLY A O 1 ATOM 2159 N N . TRP A 1 271 ? 33.619 11.171 26.470 1.00 106.68 ? 290 TRP A N 1 ATOM 2160 C CA . TRP A 1 271 ? 34.812 11.478 27.247 1.00 106.52 ? 290 TRP A CA 1 ATOM 2161 C C . TRP A 1 271 ? 36.063 11.646 26.395 1.00 105.09 ? 290 TRP A C 1 ATOM 2162 O O . TRP A 1 271 ? 36.110 11.200 25.247 1.00 103.29 ? 290 TRP A O 1 ATOM 2163 C CB . TRP A 1 271 ? 35.043 10.332 28.249 1.00 102.64 ? 290 TRP A CB 1 ATOM 2164 C CG . TRP A 1 271 ? 35.071 8.975 27.601 1.00 97.47 ? 290 TRP A CG 1 ATOM 2165 C CD1 . TRP A 1 271 ? 34.005 8.158 27.361 1.00 96.35 ? 290 TRP A CD1 1 ATOM 2166 C CD2 . TRP A 1 271 ? 36.218 8.307 27.059 1.00 94.26 ? 290 TRP A CD2 1 ATOM 2167 N NE1 . TRP A 1 271 ? 34.419 7.013 26.722 1.00 93.24 ? 290 TRP A NE1 1 ATOM 2168 C CE2 . TRP A 1 271 ? 35.774 7.077 26.525 1.00 91.85 ? 290 TRP A CE2 1 ATOM 2169 C CE3 . TRP A 1 271 ? 37.587 8.619 26.991 1.00 94.60 ? 290 TRP A CE3 1 ATOM 2170 C CZ2 . TRP A 1 271 ? 36.648 6.159 25.932 1.00 89.79 ? 290 TRP A CZ2 1 ATOM 2171 C CZ3 . TRP A 1 271 ? 38.451 7.711 26.399 1.00 92.46 ? 290 TRP A CZ3 1 ATOM 2172 C CH2 . TRP A 1 271 ? 37.981 6.497 25.879 1.00 90.49 ? 290 TRP A CH2 1 ATOM 2173 N N . ARG A 1 272 ? 37.101 12.229 27.004 1.00 107.07 ? 291 ARG A N 1 ATOM 2174 C CA . ARG A 1 272 ? 38.411 12.436 26.404 1.00 107.29 ? 291 ARG A CA 1 ATOM 2175 C C . ARG A 1 272 ? 39.475 12.294 27.480 1.00 107.09 ? 291 ARG A C 1 ATOM 2176 O O . ARG A 1 272 ? 39.301 12.791 28.595 1.00 110.47 ? 291 ARG A O 1 ATOM 2177 C CB . ARG A 1 272 ? 38.499 13.829 25.750 1.00 114.36 ? 291 ARG A CB 1 ATOM 2178 C CG . ARG A 1 272 ? 39.915 14.262 25.357 1.00 116.99 ? 291 ARG A CG 1 ATOM 2179 C CD . ARG A 1 272 ? 39.971 15.693 24.877 1.00 125.66 ? 291 ARG A CD 1 ATOM 2180 N NE . ARG A 1 272 ? 41.348 16.186 24.820 1.00 130.05 ? 291 ARG A NE 1 ATOM 2181 C CZ . ARG A 1 272 ? 41.940 16.651 23.724 1.00 135.85 ? 291 ARG A CZ 1 ATOM 2182 N NH1 . ARG A 1 272 ? 41.281 16.699 22.573 1.00 138.06 ? 291 ARG A NH1 1 ATOM 2183 N NH2 . ARG A 1 272 ? 43.195 17.078 23.772 1.00 139.66 ? 291 ARG A NH2 1 ATOM 2184 N N . LEU A 1 273 ? 40.582 11.640 27.137 1.00 104.70 ? 292 LEU A N 1 ATOM 2185 C CA . LEU A 1 273 ? 41.717 11.522 28.035 1.00 105.84 ? 292 LEU A CA 1 ATOM 2186 C C . LEU A 1 273 ? 43.014 11.704 27.278 1.00 107.94 ? 292 LEU A C 1 ATOM 2187 O O . LEU A 1 273 ? 43.072 11.478 26.068 1.00 107.50 ? 292 LEU A O 1 ATOM 2188 C CB . LEU A 1 273 ? 41.713 10.200 28.848 1.00 102.14 ? 292 LEU A CB 1 ATOM 2189 C CG . LEU A 1 273 ? 41.978 8.863 28.122 1.00 98.28 ? 292 LEU A CG 1 ATOM 2190 C CD1 . LEU A 1 273 ? 43.480 8.596 27.940 1.00 99.64 ? 292 LEU A CD1 1 ATOM 2191 C CD2 . LEU A 1 273 ? 41.391 7.708 28.908 1.00 95.59 ? 292 LEU A CD2 1 ATOM 2192 N N . SER A 1 274 ? 44.060 12.081 28.005 1.00 111.23 ? 293 SER A N 1 ATOM 2193 C CA . SER A 1 274 ? 45.405 12.175 27.471 1.00 114.00 ? 293 SER A CA 1 ATOM 2194 C C . SER A 1 274 ? 46.273 11.272 28.328 1.00 113.07 ? 293 SER A C 1 ATOM 2195 O O . SER A 1 274 ? 46.047 11.164 29.539 1.00 113.44 ? 293 SER A O 1 ATOM 2196 C CB . SER A 1 274 ? 45.919 13.611 27.486 1.00 121.18 ? 293 SER A CB 1 ATOM 2197 O OG . SER A 1 274 ? 46.064 14.117 28.803 1.00 125.10 ? 293 SER A OG 1 ATOM 2198 N N . TYR A 1 275 ? 47.225 10.585 27.700 1.00 113.47 ? 294 TYR A N 1 ATOM 2199 C CA . TYR A 1 275 ? 48.129 9.710 28.426 1.00 114.33 ? 294 TYR A CA 1 ATOM 2200 C C . TYR A 1 275 ? 49.565 10.147 28.211 1.00 120.45 ? 294 TYR A C 1 ATOM 2201 O O . TYR A 1 275 ? 49.881 10.757 27.186 1.00 123.30 ? 294 TYR A O 1 ATOM 2202 C CB . TYR A 1 275 ? 47.924 8.229 28.050 1.00 110.56 ? 294 TYR A CB 1 ATOM 2203 C CG . TYR A 1 275 ? 48.523 7.839 26.716 1.00 112.30 ? 294 TYR A CG 1 ATOM 2204 C CD1 . TYR A 1 275 ? 49.873 7.516 26.603 1.00 117.92 ? 294 TYR A CD1 1 ATOM 2205 C CD2 . TYR A 1 275 ? 47.738 7.772 25.571 1.00 110.42 ? 294 TYR A CD2 1 ATOM 2206 C CE1 . TYR A 1 275 ? 50.436 7.184 25.374 1.00 121.37 ? 294 TYR A CE1 1 ATOM 2207 C CE2 . TYR A 1 275 ? 48.282 7.401 24.343 1.00 114.53 ? 294 TYR A CE2 1 ATOM 2208 C CZ . TYR A 1 275 ? 49.635 7.121 24.246 1.00 120.26 ? 294 TYR A CZ 1 ATOM 2209 O OH . TYR A 1 275 ? 50.182 6.770 23.036 1.00 126.10 ? 294 TYR A OH 1 ATOM 2210 N N . ARG A 1 276 ? 50.435 9.800 29.164 1.00 124.01 ? 295 ARG A N 1 ATOM 2211 C CA . ARG A 1 276 ? 51.862 10.099 29.128 1.00 131.26 ? 295 ARG A CA 1 ATOM 2212 C C . ARG A 1 276 ? 52.627 8.928 29.729 1.00 133.46 ? 295 ARG A C 1 ATOM 2213 O O . ARG A 1 276 ? 52.288 8.466 30.823 1.00 132.60 ? 295 ARG A O 1 ATOM 2214 C CB . ARG A 1 276 ? 52.171 11.395 29.899 1.00 136.67 ? 295 ARG A CB 1 ATOM 2215 C CG . ARG A 1 276 ? 51.791 12.668 29.155 1.00 138.70 ? 295 ARG A CG 1 ATOM 2216 C CD . ARG A 1 276 ? 51.520 13.824 30.100 1.00 143.43 ? 295 ARG A CD 1 ATOM 2217 N NE . ARG A 1 276 ? 50.921 14.964 29.403 1.00 145.01 ? 295 ARG A NE 1 ATOM 2218 C CZ . ARG A 1 276 ? 49.618 15.109 29.175 1.00 140.53 ? 295 ARG A CZ 1 ATOM 2219 N NH1 . ARG A 1 276 ? 48.757 14.187 29.589 1.00 132.36 ? 295 ARG A NH1 1 ATOM 2220 N NH2 . ARG A 1 276 ? 49.167 16.176 28.529 1.00 144.62 ? 295 ARG A NH2 1 ATOM 2221 N N . ALA A 1 277 ? 53.650 8.441 29.012 1.00 138.19 ? 296 ALA A N 1 ATOM 2222 C CA . ALA A 1 277 ? 54.493 7.341 29.473 1.00 142.91 ? 296 ALA A CA 1 ATOM 2223 C C . ALA A 1 277 ? 55.687 7.901 30.229 1.00 151.25 ? 296 ALA A C 1 ATOM 2224 O O . ALA A 1 277 ? 56.560 8.539 29.631 1.00 157.02 ? 296 ALA A O 1 ATOM 2225 C CB . ALA A 1 277 ? 54.973 6.522 28.297 1.00 145.24 ? 296 ALA A CB 1 ATOM 2226 N N . ALA A 1 278 ? 55.711 7.675 31.548 1.00 153.97 ? 297 ALA A N 1 ATOM 2227 C CA . ALA A 1 278 ? 56.775 8.130 32.437 1.00 163.34 ? 297 ALA A CA 1 ATOM 2228 C C . ALA A 1 278 ? 57.766 7.012 32.735 1.00 169.80 ? 297 ALA A C 1 ATOM 2229 O O . ALA A 1 278 ? 57.724 5.941 32.119 1.00 168.39 ? 297 ALA A O 1 ATOM 2230 C CB . ALA A 1 278 ? 56.174 8.636 33.742 1.00 164.99 ? 297 ALA A CB 1 ATOM 2231 N N . GLY A 1 279 ? 58.625 7.258 33.735 1.00 199.79 ? 298 GLY A N 1 ATOM 2232 C CA . GLY A 1 279 ? 59.621 6.314 34.213 1.00 203.49 ? 298 GLY A CA 1 ATOM 2233 C C . GLY A 1 279 ? 60.285 6.769 35.505 1.00 239.94 ? 298 GLY A C 1 ATOM 2234 O O . GLY A 1 279 ? 59.876 7.754 36.129 1.00 242.52 ? 298 GLY A O 1 ATOM 2235 N N . ASN A 1 280 ? 61.313 6.021 35.906 1.00 178.90 ? 299 ASN A N 1 ATOM 2236 C CA . ASN A 1 280 ? 62.109 6.314 37.085 1.00 179.51 ? 299 ASN A CA 1 ATOM 2237 C C . ASN A 1 280 ? 63.070 7.441 36.740 1.00 170.54 ? 299 ASN A C 1 ATOM 2238 O O . ASN A 1 280 ? 63.581 7.498 35.617 1.00 163.51 ? 299 ASN A O 1 ATOM 2239 C CB . ASN A 1 280 ? 62.879 5.071 37.532 1.00 182.42 ? 299 ASN A CB 1 ATOM 2240 C CG . ASN A 1 280 ? 62.078 4.058 38.322 1.00 196.09 ? 299 ASN A CG 1 ATOM 2241 O OD1 . ASN A 1 280 ? 60.930 4.288 38.720 1.00 202.58 ? 299 ASN A OD1 1 ATOM 2242 N ND2 . ASN A 1 280 ? 62.688 2.914 38.594 1.00 202.58 ? 299 ASN A ND2 1 ATOM 2243 N N . GLU A 1 281 ? 63.286 8.354 37.693 1.00 171.75 ? 300 GLU A N 1 ATOM 2244 C CA . GLU A 1 281 ? 64.190 9.481 37.507 1.00 164.93 ? 300 GLU A CA 1 ATOM 2245 C C . GLU A 1 281 ? 65.616 9.070 37.859 1.00 160.51 ? 300 GLU A C 1 ATOM 2246 O O . GLU A 1 281 ? 65.855 8.516 38.936 1.00 168.74 ? 300 GLU A O 1 ATOM 2247 C CB . GLU A 1 281 ? 63.746 10.687 38.353 1.00 170.36 ? 300 GLU A CB 1 ATOM 2248 C CG . GLU A 1 281 ? 64.557 11.951 38.102 1.00 165.44 ? 300 GLU A CG 1 ATOM 2249 C CD . GLU A 1 281 ? 64.569 12.956 39.237 1.00 172.32 ? 300 GLU A CD 1 ATOM 2250 O OE1 . GLU A 1 281 ? 63.479 13.291 39.753 1.00 181.26 ? 300 GLU A OE1 1 ATOM 2251 O OE2 . GLU A 1 281 ? 65.671 13.437 39.587 1.00 171.84 ? 300 GLU A OE2 1 ATOM 2252 N N . CYS A 1 282 ? 66.555 9.342 36.944 1.00 151.37 ? 301 CYS A N 1 ATOM 2253 C CA . CYS A 1 282 ? 67.973 9.067 37.146 1.00 147.79 ? 301 CYS A CA 1 ATOM 2254 C C . CYS A 1 282 ? 68.615 10.250 37.878 1.00 148.66 ? 301 CYS A C 1 ATOM 2255 O O . CYS A 1 282 ? 68.178 11.386 37.664 1.00 146.54 ? 301 CYS A O 1 ATOM 2256 C CB . CYS A 1 282 ? 68.669 8.774 35.821 1.00 139.85 ? 301 CYS A CB 1 ATOM 2257 S SG . CYS A 1 282 ? 68.474 7.067 35.251 1.00 141.48 ? 301 CYS A SG 1 ATOM 2258 N N . PRO A 1 283 ? 69.637 9.999 38.746 1.00 152.59 ? 302 PRO A N 1 ATOM 2259 C CA . PRO A 1 283 ? 70.272 11.081 39.506 1.00 154.83 ? 302 PRO A CA 1 ATOM 2260 C C . PRO A 1 283 ? 70.996 12.116 38.651 1.00 145.95 ? 302 PRO A C 1 ATOM 2261 O O . PRO A 1 283 ? 71.364 11.837 37.504 1.00 138.33 ? 302 PRO A O 1 ATOM 2262 C CB . PRO A 1 283 ? 71.245 10.343 40.428 1.00 161.95 ? 302 PRO A CB 1 ATOM 2263 C CG . PRO A 1 283 ? 71.555 9.086 39.713 1.00 158.97 ? 302 PRO A CG 1 ATOM 2264 C CD . PRO A 1 283 ? 70.258 8.698 39.076 1.00 157.11 ? 302 PRO A CD 1 ATOM 2265 N N . GLU A 1 284 ? 71.205 13.311 39.235 1.00 148.58 ? 303 GLU A N 1 ATOM 2266 C CA . GLU A 1 284 ? 71.907 14.436 38.621 1.00 142.03 ? 303 GLU A CA 1 ATOM 2267 C C . GLU A 1 284 ? 73.308 13.983 38.217 1.00 136.66 ? 303 GLU A C 1 ATOM 2268 O O . GLU A 1 284 ? 73.992 13.324 39.005 1.00 140.81 ? 303 GLU A O 1 ATOM 2269 C CB . GLU A 1 284 ? 71.986 15.615 39.613 1.00 150.48 ? 303 GLU A CB 1 ATOM 2270 C CG . GLU A 1 284 ? 72.596 16.888 39.046 1.00 148.46 ? 303 GLU A CG 1 ATOM 2271 C CD . GLU A 1 284 ? 72.814 17.983 40.071 1.00 161.73 ? 303 GLU A CD 1 ATOM 2272 N N . LEU A 1 285 ? 73.702 14.285 36.974 1.00 128.62 ? 304 LEU A N 1 ATOM 2273 C CA . LEU A 1 285 ? 75.025 13.933 36.474 1.00 125.31 ? 304 LEU A CA 1 ATOM 2274 C C . LEU A 1 285 ? 75.932 15.143 36.517 1.00 126.27 ? 304 LEU A C 1 ATOM 2275 O O . LEU A 1 285 ? 75.523 16.240 36.128 1.00 127.39 ? 304 LEU A O 1 ATOM 2276 C CB . LEU A 1 285 ? 74.979 13.385 35.036 1.00 118.65 ? 304 LEU A CB 1 ATOM 2277 C CG . LEU A 1 285 ? 74.360 12.011 34.778 1.00 118.50 ? 304 LEU A CG 1 ATOM 2278 C CD1 . LEU A 1 285 ? 74.484 11.653 33.314 1.00 113.22 ? 304 LEU A CD1 1 ATOM 2279 C CD2 . LEU A 1 285 ? 75.018 10.926 35.599 1.00 122.19 ? 304 LEU A CD2 1 ATOM 2280 N N . GLN A 1 286 ? 77.164 14.942 36.985 1.00 128.26 ? 305 GLN A N 1 ATOM 2281 C CA . GLN A 1 286 ? 78.164 15.998 37.032 1.00 131.61 ? 305 GLN A CA 1 ATOM 2282 C C . GLN A 1 286 ? 79.172 15.781 35.906 1.00 123.37 ? 305 GLN A C 1 ATOM 2283 O O . GLN A 1 286 ? 79.712 14.674 35.791 1.00 121.89 ? 305 GLN A O 1 ATOM 2284 C CB . GLN A 1 286 ? 78.849 16.072 38.401 1.00 143.99 ? 305 GLN A CB 1 ATOM 2285 C CG . GLN A 1 286 ? 78.081 16.931 39.401 1.00 155.78 ? 305 GLN A CG 1 ATOM 2286 C CD . GLN A 1 286 ? 78.984 17.857 40.181 1.00 168.28 ? 305 GLN A CD 1 ATOM 2287 O OE1 . GLN A 1 286 ? 79.725 18.674 39.619 1.00 168.11 ? 305 GLN A OE1 1 ATOM 2288 N NE2 . GLN A 1 286 ? 78.908 17.782 41.501 1.00 182.22 ? 305 GLN A NE2 1 ATOM 2289 N N . PRO A 1 287 ? 79.407 16.816 35.053 1.00 119.62 ? 306 PRO A N 1 ATOM 2290 C CA . PRO A 1 287 ? 80.359 16.681 33.949 1.00 115.34 ? 306 PRO A CA 1 ATOM 2291 C C . PRO A 1 287 ? 81.769 16.395 34.459 1.00 116.70 ? 306 PRO A C 1 ATOM 2292 O O . PRO A 1 287 ? 82.128 16.881 35.536 1.00 123.77 ? 306 PRO A O 1 ATOM 2293 C CB . PRO A 1 287 ? 80.280 18.033 33.234 1.00 116.61 ? 306 PRO A CB 1 ATOM 2294 C CG . PRO A 1 287 ? 79.761 18.972 34.247 1.00 122.41 ? 306 PRO A CG 1 ATOM 2295 C CD . PRO A 1 287 ? 78.802 18.163 35.060 1.00 123.22 ? 306 PRO A CD 1 ATOM 2296 N N . PRO A 1 288 ? 82.563 15.602 33.704 1.00 113.20 ? 307 PRO A N 1 ATOM 2297 C CA . PRO A 1 288 ? 83.926 15.296 34.134 1.00 117.86 ? 307 PRO A CA 1 ATOM 2298 C C . PRO A 1 288 ? 84.806 16.540 34.083 1.00 121.60 ? 307 PRO A C 1 ATOM 2299 O O . PRO A 1 288 ? 84.539 17.451 33.290 1.00 118.93 ? 307 PRO A O 1 ATOM 2300 C CB . PRO A 1 288 ? 84.391 14.253 33.117 1.00 114.07 ? 307 PRO A CB 1 ATOM 2301 C CG . PRO A 1 288 ? 83.596 14.534 31.898 1.00 110.83 ? 307 PRO A CG 1 ATOM 2302 C CD . PRO A 1 288 ? 82.259 14.978 32.398 1.00 109.96 ? 307 PRO A CD 1 ATOM 2303 N N . VAL A 1 289 ? 85.853 16.577 34.931 1.00 128.69 ? 308 VAL A N 1 ATOM 2304 C CA . VAL A 1 289 ? 86.824 17.675 34.956 1.00 132.79 ? 308 VAL A CA 1 ATOM 2305 C C . VAL A 1 289 ? 87.461 17.681 33.570 1.00 129.64 ? 308 VAL A C 1 ATOM 2306 O O . VAL A 1 289 ? 87.842 16.616 33.079 1.00 125.54 ? 308 VAL A O 1 ATOM 2307 C CB . VAL A 1 289 ? 87.883 17.512 36.081 1.00 140.93 ? 308 VAL A CB 1 ATOM 2308 C CG1 . VAL A 1 289 ? 88.955 18.598 35.999 1.00 145.82 ? 308 VAL A CG1 1 ATOM 2309 C CG2 . VAL A 1 289 ? 87.229 17.510 37.460 1.00 146.59 ? 308 VAL A CG2 1 ATOM 2310 N N . HIS A 1 290 ? 87.505 18.861 32.920 1.00 132.04 ? 309 HIS A N 1 ATOM 2311 C CA . HIS A 1 290 ? 88.020 19.058 31.560 1.00 131.39 ? 309 HIS A CA 1 ATOM 2312 C C . HIS A 1 290 ? 87.088 18.435 30.504 1.00 122.85 ? 309 HIS A C 1 ATOM 2313 O O . HIS A 1 290 ? 87.540 18.091 29.410 1.00 122.34 ? 309 HIS A O 1 ATOM 2314 C CB . HIS A 1 290 ? 89.459 18.522 31.402 1.00 136.15 ? 309 HIS A CB 1 ATOM 2315 C CG . HIS A 1 290 ? 90.478 19.235 32.227 1.00 144.64 ? 309 HIS A CG 1 ATOM 2316 N ND1 . HIS A 1 290 ? 90.862 20.527 31.933 1.00 151.12 ? 309 HIS A ND1 1 ATOM 2317 C CD2 . HIS A 1 290 ? 91.208 18.788 33.275 1.00 149.76 ? 309 HIS A CD2 1 ATOM 2318 C CE1 . HIS A 1 290 ? 91.783 20.839 32.828 1.00 158.88 ? 309 HIS A CE1 1 ATOM 2319 N NE2 . HIS A 1 290 ? 92.024 19.824 33.658 1.00 158.39 ? 309 HIS A NE2 1 ATOM 2320 N N . GLY A 1 291 ? 85.790 18.295 30.823 1.00 118.13 ? 310 GLY A N 1 ATOM 2321 C CA . GLY A 1 291 ? 84.846 17.690 29.890 1.00 114.63 ? 310 GLY A CA 1 ATOM 2322 C C . GLY A 1 291 ? 83.424 18.221 29.972 1.00 113.40 ? 310 GLY A C 1 ATOM 2323 O O . GLY A 1 291 ? 83.173 19.258 30.591 1.00 116.02 ? 310 GLY A O 1 ATOM 2324 N N . LYS A 1 292 ? 82.493 17.495 29.326 1.00 110.83 ? 311 LYS A N 1 ATOM 2325 C CA . LYS A 1 292 ? 81.074 17.847 29.260 1.00 111.64 ? 311 LYS A CA 1 ATOM 2326 C C . LYS A 1 292 ? 80.154 16.638 29.056 1.00 108.91 ? 311 LYS A C 1 ATOM 2327 O O . LYS A 1 292 ? 80.602 15.557 28.664 1.00 108.03 ? 311 LYS A O 1 ATOM 2328 C CB . LYS A 1 292 ? 80.822 18.896 28.154 1.00 115.20 ? 311 LYS A CB 1 ATOM 2329 C CG . LYS A 1 292 ? 81.117 18.396 26.742 1.00 116.26 ? 311 LYS A CG 1 ATOM 2330 C CD . LYS A 1 292 ? 80.523 19.296 25.686 1.00 120.86 ? 311 LYS A CD 1 ATOM 2331 C CE . LYS A 1 292 ? 80.818 18.773 24.303 1.00 124.85 ? 311 LYS A CE 1 ATOM 2332 N NZ . LYS A 1 292 ? 80.000 19.459 23.270 1.00 129.02 ? 311 LYS A NZ 1 ATOM 2333 N N . ILE A 1 293 ? 78.855 16.852 29.306 1.00 107.63 ? 312 ILE A N 1 ATOM 2334 C CA . ILE A 1 293 ? 77.791 15.870 29.125 1.00 105.77 ? 312 ILE A CA 1 ATOM 2335 C C . ILE A 1 293 ? 76.698 16.541 28.301 1.00 106.61 ? 312 ILE A C 1 ATOM 2336 O O . ILE A 1 293 ? 76.271 17.648 28.631 1.00 108.65 ? 312 ILE A O 1 ATOM 2337 C CB . ILE A 1 293 ? 77.235 15.334 30.479 1.00 105.85 ? 312 ILE A CB 1 ATOM 2338 C CG1 . ILE A 1 293 ? 78.326 14.609 31.307 1.00 106.98 ? 312 ILE A CG1 1 ATOM 2339 C CG2 . ILE A 1 293 ? 76.008 14.430 30.258 1.00 104.75 ? 312 ILE A CG2 1 ATOM 2340 C CD1 . ILE A 1 293 ? 77.899 14.163 32.726 1.00 110.05 ? 312 ILE A CD1 1 ATOM 2341 N N . GLU A 1 294 ? 76.253 15.872 27.231 1.00 107.42 ? 313 GLU A N 1 ATOM 2342 C CA . GLU A 1 294 ? 75.172 16.348 26.373 1.00 111.10 ? 313 GLU A CA 1 ATOM 2343 C C . GLU A 1 294 ? 74.154 15.227 26.161 1.00 112.14 ? 313 GLU A C 1 ATOM 2344 O O . GLU A 1 294 ? 74.571 14.078 26.009 1.00 112.41 ? 313 GLU A O 1 ATOM 2345 C CB . GLU A 1 294 ? 75.700 16.839 25.022 1.00 113.46 ? 313 GLU A CB 1 ATOM 2346 C CG . GLU A 1 294 ? 76.509 18.122 25.103 1.00 116.29 ? 313 GLU A CG 1 ATOM 2347 C CD . GLU A 1 294 ? 76.771 18.822 23.783 1.00 122.53 ? 313 GLU A CD 1 ATOM 2348 O OE1 . GLU A 1 294 ? 76.478 18.237 22.714 1.00 124.79 ? 313 GLU A OE1 1 ATOM 2349 O OE2 . GLU A 1 294 ? 77.276 19.967 23.820 1.00 127.32 ? 313 GLU A OE2 1 ATOM 2350 N N . PRO A 1 295 ? 72.833 15.539 26.136 1.00 114.51 ? 314 PRO A N 1 ATOM 2351 C CA . PRO A 1 295 ? 72.216 16.857 26.313 1.00 116.82 ? 314 PRO A CA 1 ATOM 2352 C C . PRO A 1 295 ? 72.069 17.218 27.787 1.00 116.45 ? 314 PRO A C 1 ATOM 2353 O O . PRO A 1 295 ? 71.823 16.342 28.620 1.00 115.35 ? 314 PRO A O 1 ATOM 2354 C CB . PRO A 1 295 ? 70.869 16.703 25.603 1.00 120.20 ? 314 PRO A CB 1 ATOM 2355 C CG . PRO A 1 295 ? 70.512 15.259 25.790 1.00 119.25 ? 314 PRO A CG 1 ATOM 2356 C CD . PRO A 1 295 ? 71.825 14.507 25.813 1.00 116.18 ? 314 PRO A CD 1 ATOM 2357 N N . SER A 1 296 ? 72.231 18.507 28.107 1.00 118.97 ? 315 SER A N 1 ATOM 2358 C CA . SER A 1 296 ? 72.091 18.992 29.477 1.00 121.17 ? 315 SER A CA 1 ATOM 2359 C C . SER A 1 296 ? 70.611 19.113 29.824 1.00 125.81 ? 315 SER A C 1 ATOM 2360 O O . SER A 1 296 ? 69.906 19.948 29.253 1.00 130.14 ? 315 SER A O 1 ATOM 2361 C CB . SER A 1 296 ? 72.796 20.333 29.653 1.00 124.98 ? 315 SER A CB 1 ATOM 2362 O OG . SER A 1 296 ? 74.181 20.232 29.367 1.00 124.76 ? 315 SER A OG 1 ATOM 2363 N N . GLN A 1 297 ? 70.137 18.250 30.729 1.00 126.65 ? 316 GLN A N 1 ATOM 2364 C CA . GLN A 1 297 ? 68.745 18.245 31.177 1.00 131.83 ? 316 GLN A CA 1 ATOM 2365 C C . GLN A 1 297 ? 68.692 18.493 32.675 1.00 135.54 ? 316 GLN A C 1 ATOM 2366 O O . GLN A 1 297 ? 69.675 18.235 33.375 1.00 133.63 ? 316 GLN A O 1 ATOM 2367 C CB . GLN A 1 297 ? 68.070 16.900 30.857 1.00 131.54 ? 316 GLN A CB 1 ATOM 2368 C CG . GLN A 1 297 ? 67.956 16.579 29.364 1.00 130.36 ? 316 GLN A CG 1 ATOM 2369 C CD . GLN A 1 297 ? 67.446 15.180 29.070 1.00 130.88 ? 316 GLN A CD 1 ATOM 2370 O OE1 . GLN A 1 297 ? 67.551 14.689 27.941 1.00 131.24 ? 316 GLN A OE1 1 ATOM 2371 N NE2 . GLN A 1 297 ? 66.867 14.505 30.061 1.00 132.91 ? 316 GLN A NE2 1 ATOM 2372 N N . ALA A 1 298 ? 67.542 18.983 33.170 1.00 141.48 ? 317 ALA A N 1 ATOM 2373 C CA . ALA A 1 298 ? 67.328 19.201 34.598 1.00 146.75 ? 317 ALA A CA 1 ATOM 2374 C C . ALA A 1 298 ? 67.235 17.820 35.254 1.00 146.76 ? 317 ALA A C 1 ATOM 2375 O O . ALA A 1 298 ? 67.972 17.546 36.203 1.00 147.22 ? 317 ALA A O 1 ATOM 2376 C CB . ALA A 1 298 ? 66.046 19.990 34.824 1.00 153.91 ? 317 ALA A CB 1 ATOM 2377 N N . LYS A 1 299 ? 66.347 16.951 34.707 1.00 146.80 ? 318 LYS A N 1 ATOM 2378 C CA A LYS A 1 299 ? 66.140 15.579 35.175 0.50 146.61 ? 318 LYS A CA 1 ATOM 2379 C CA B LYS A 1 299 ? 66.120 15.580 35.178 0.50 146.88 ? 318 LYS A CA 1 ATOM 2380 C C . LYS A 1 299 ? 66.238 14.609 33.999 1.00 142.33 ? 318 LYS A C 1 ATOM 2381 O O . LYS A 1 299 ? 65.994 15.003 32.855 1.00 140.30 ? 318 LYS A O 1 ATOM 2382 C CB A LYS A 1 299 ? 64.782 15.435 35.887 0.50 154.47 ? 318 LYS A CB 1 ATOM 2383 C CB B LYS A 1 299 ? 64.730 15.424 35.847 0.50 155.02 ? 318 LYS A CB 1 ATOM 2384 C CG A LYS A 1 299 ? 64.736 16.058 37.280 0.50 161.69 ? 318 LYS A CG 1 ATOM 2385 C CG B LYS A 1 299 ? 64.181 16.643 36.607 0.50 162.38 ? 318 LYS A CG 1 ATOM 2386 C CD A LYS A 1 299 ? 64.049 17.418 37.276 0.50 167.11 ? 318 LYS A CD 1 ATOM 2387 C CD B LYS A 1 299 ? 64.864 16.900 37.949 0.50 166.40 ? 318 LYS A CD 1 ATOM 2388 C CE A LYS A 1 299 ? 64.010 18.038 38.650 0.50 175.84 ? 318 LYS A CE 1 ATOM 2389 C CE B LYS A 1 299 ? 64.358 18.173 38.582 0.50 173.30 ? 318 LYS A CE 1 ATOM 2390 N NZ A LYS A 1 299 ? 63.284 19.334 38.645 0.50 182.94 ? 318 LYS A NZ 1 ATOM 2391 N NZ B LYS A 1 299 ? 65.051 18.467 39.863 0.50 183.85 ? 318 LYS A NZ 1 ATOM 2392 N N . TYR A 1 300 ? 66.605 13.344 34.275 1.00 141.21 ? 319 TYR A N 1 ATOM 2393 C CA . TYR A 1 300 ? 66.749 12.300 33.255 1.00 137.37 ? 319 TYR A CA 1 ATOM 2394 C C . TYR A 1 300 ? 65.813 11.132 33.545 1.00 141.68 ? 319 TYR A C 1 ATOM 2395 O O . TYR A 1 300 ? 65.668 10.738 34.703 1.00 146.25 ? 319 TYR A O 1 ATOM 2396 C CB . TYR A 1 300 ? 68.202 11.814 33.172 1.00 132.56 ? 319 TYR A CB 1 ATOM 2397 C CG . TYR A 1 300 ? 69.181 12.872 32.711 1.00 128.36 ? 319 TYR A CG 1 ATOM 2398 C CD1 . TYR A 1 300 ? 69.477 13.037 31.361 1.00 125.22 ? 319 TYR A CD1 1 ATOM 2399 C CD2 . TYR A 1 300 ? 69.838 13.690 33.626 1.00 128.37 ? 319 TYR A CD2 1 ATOM 2400 C CE1 . TYR A 1 300 ? 70.370 14.016 30.928 1.00 122.12 ? 319 TYR A CE1 1 ATOM 2401 C CE2 . TYR A 1 300 ? 70.744 14.664 33.206 1.00 125.09 ? 319 TYR A CE2 1 ATOM 2402 C CZ . TYR A 1 300 ? 71.011 14.820 31.856 1.00 122.07 ? 319 TYR A CZ 1 ATOM 2403 O OH . TYR A 1 300 ? 71.906 15.773 31.429 1.00 120.19 ? 319 TYR A OH 1 ATOM 2404 N N . PHE A 1 301 ? 65.186 10.575 32.495 1.00 141.31 ? 320 PHE A N 1 ATOM 2405 C CA . PHE A 1 301 ? 64.237 9.468 32.631 1.00 146.54 ? 320 PHE A CA 1 ATOM 2406 C C . PHE A 1 301 ? 64.599 8.255 31.780 1.00 145.12 ? 320 PHE A C 1 ATOM 2407 O O . PHE A 1 301 ? 65.496 8.345 30.944 1.00 141.47 ? 320 PHE A O 1 ATOM 2408 C CB . PHE A 1 301 ? 62.808 9.949 32.338 1.00 150.70 ? 320 PHE A CB 1 ATOM 2409 C CG . PHE A 1 301 ? 62.334 11.048 33.258 1.00 153.97 ? 320 PHE A CG 1 ATOM 2410 C CD1 . PHE A 1 301 ? 61.909 10.761 34.551 1.00 160.10 ? 320 PHE A CD1 1 ATOM 2411 C CD2 . PHE A 1 301 ? 62.321 12.372 32.837 1.00 152.38 ? 320 PHE A CD2 1 ATOM 2412 C CE1 . PHE A 1 301 ? 61.474 11.780 35.403 1.00 164.83 ? 320 PHE A CE1 1 ATOM 2413 C CE2 . PHE A 1 301 ? 61.885 13.391 33.689 1.00 156.77 ? 320 PHE A CE2 1 ATOM 2414 C CZ . PHE A 1 301 ? 61.465 13.088 34.966 1.00 163.01 ? 320 PHE A CZ 1 ATOM 2415 N N . PHE A 1 302 ? 63.919 7.112 32.015 1.00 149.50 ? 321 PHE A N 1 ATOM 2416 C CA . PHE A 1 302 ? 64.148 5.846 31.314 1.00 150.08 ? 321 PHE A CA 1 ATOM 2417 C C . PHE A 1 302 ? 64.397 6.014 29.815 1.00 146.40 ? 321 PHE A C 1 ATOM 2418 O O . PHE A 1 302 ? 63.638 6.713 29.137 1.00 146.43 ? 321 PHE A O 1 ATOM 2419 C CB . PHE A 1 302 ? 63.033 4.825 31.616 1.00 156.91 ? 321 PHE A CB 1 ATOM 2420 C CG . PHE A 1 302 ? 63.146 3.490 30.914 1.00 159.37 ? 321 PHE A CG 1 ATOM 2421 C CD1 . PHE A 1 302 ? 64.341 2.781 30.917 1.00 158.50 ? 321 PHE A CD1 1 ATOM 2422 C CD2 . PHE A 1 302 ? 62.054 2.934 30.264 1.00 163.81 ? 321 PHE A CD2 1 ATOM 2423 C CE1 . PHE A 1 302 ? 64.445 1.548 30.274 1.00 162.73 ? 321 PHE A CE1 1 ATOM 2424 C CE2 . PHE A 1 302 ? 62.165 1.710 29.605 1.00 167.97 ? 321 PHE A CE2 1 ATOM 2425 C CZ . PHE A 1 302 ? 63.353 1.015 29.631 1.00 167.55 ? 321 PHE A CZ 1 ATOM 2426 N N . LYS A 1 303 ? 65.507 5.379 29.343 1.00 144.48 ? 322 LYS A N 1 ATOM 2427 C CA A LYS A 1 303 ? 66.005 5.363 27.960 0.50 140.89 ? 322 LYS A CA 1 ATOM 2428 C CA B LYS A 1 303 ? 66.015 5.365 27.965 0.50 140.86 ? 322 LYS A CA 1 ATOM 2429 C C . LYS A 1 303 ? 66.684 6.657 27.489 1.00 137.31 ? 322 LYS A C 1 ATOM 2430 O O . LYS A 1 303 ? 67.094 6.736 26.325 1.00 137.35 ? 322 LYS A O 1 ATOM 2431 C CB A LYS A 1 303 ? 64.947 4.871 26.957 0.50 145.26 ? 322 LYS A CB 1 ATOM 2432 C CB B LYS A 1 303 ? 64.982 4.854 26.952 0.50 145.27 ? 322 LYS A CB 1 ATOM 2433 C CG A LYS A 1 303 ? 65.397 3.667 26.134 0.50 149.30 ? 322 LYS A CG 1 ATOM 2434 C CG B LYS A 1 303 ? 64.855 3.337 26.897 0.50 150.46 ? 322 LYS A CG 1 ATOM 2435 C CD A LYS A 1 303 ? 65.005 3.753 24.641 0.50 152.72 ? 322 LYS A CD 1 ATOM 2436 C CD B LYS A 1 303 ? 64.404 2.867 25.514 0.50 154.86 ? 322 LYS A CD 1 ATOM 2437 C CE A LYS A 1 303 ? 63.541 4.023 24.333 0.50 158.16 ? 322 LYS A CE 1 ATOM 2438 C CE B LYS A 1 303 ? 63.088 3.473 25.080 0.50 156.26 ? 322 LYS A CE 1 ATOM 2439 N NZ A LYS A 1 303 ? 62.622 3.133 25.090 0.50 160.14 ? 322 LYS A NZ 1 ATOM 2440 N NZ B LYS A 1 303 ? 63.125 3.923 23.666 0.50 155.63 ? 322 LYS A NZ 1 ATOM 2441 N N . ASP A 1 304 ? 66.833 7.667 28.379 1.00 133.11 ? 323 ASP A N 1 ATOM 2442 C CA . ASP A 1 304 ? 67.511 8.909 27.984 1.00 128.01 ? 323 ASP A CA 1 ATOM 2443 C C . ASP A 1 304 ? 68.977 8.583 27.732 1.00 124.91 ? 323 ASP A C 1 ATOM 2444 O O . ASP A 1 304 ? 69.575 7.835 28.505 1.00 123.65 ? 323 ASP A O 1 ATOM 2445 C CB . ASP A 1 304 ? 67.381 10.011 29.052 1.00 126.51 ? 323 ASP A CB 1 ATOM 2446 C CG . ASP A 1 304 ? 66.135 10.875 28.945 1.00 128.38 ? 323 ASP A CG 1 ATOM 2447 O OD1 . ASP A 1 304 ? 65.423 10.775 27.920 1.00 129.98 ? 323 ASP A OD1 1 ATOM 2448 O OD2 . ASP A 1 304 ? 65.887 11.674 29.874 1.00 128.84 ? 323 ASP A OD2 1 ATOM 2449 N N . GLN A 1 305 ? 69.526 9.077 26.614 1.00 123.74 ? 324 GLN A N 1 ATOM 2450 C CA . GLN A 1 305 ? 70.914 8.822 26.226 1.00 122.29 ? 324 GLN A CA 1 ATOM 2451 C C . GLN A 1 305 ? 71.741 10.079 26.370 1.00 117.43 ? 324 GLN A C 1 ATOM 2452 O O . GLN A 1 305 ? 71.272 11.164 26.015 1.00 116.26 ? 324 GLN A O 1 ATOM 2453 C CB . GLN A 1 305 ? 71.007 8.338 24.766 1.00 126.35 ? 324 GLN A CB 1 ATOM 2454 C CG . GLN A 1 305 ? 70.079 7.187 24.380 1.00 132.21 ? 324 GLN A CG 1 ATOM 2455 C CD . GLN A 1 305 ? 70.414 5.882 25.054 1.00 135.05 ? 324 GLN A CD 1 ATOM 2456 O OE1 . GLN A 1 305 ? 71.558 5.410 25.042 1.00 135.87 ? 324 GLN A OE1 1 ATOM 2457 N NE2 . GLN A 1 305 ? 69.401 5.253 25.625 1.00 138.11 ? 324 GLN A NE2 1 ATOM 2458 N N . VAL A 1 306 ? 72.976 9.937 26.883 1.00 115.38 ? 325 VAL A N 1 ATOM 2459 C CA . VAL A 1 306 ? 73.914 11.051 27.042 1.00 112.43 ? 325 VAL A CA 1 ATOM 2460 C C . VAL A 1 306 ? 75.321 10.657 26.565 1.00 111.99 ? 325 VAL A C 1 ATOM 2461 O O . VAL A 1 306 ? 75.758 9.528 26.806 1.00 113.12 ? 325 VAL A O 1 ATOM 2462 C CB . VAL A 1 306 ? 73.925 11.724 28.455 1.00 109.84 ? 325 VAL A CB 1 ATOM 2463 C CG1 . VAL A 1 306 ? 72.521 12.026 28.969 1.00 111.65 ? 325 VAL A CG1 1 ATOM 2464 C CG2 . VAL A 1 306 ? 74.696 10.906 29.476 1.00 108.55 ? 325 VAL A CG2 1 ATOM 2465 N N . LEU A 1 307 ? 76.018 11.584 25.886 1.00 111.63 ? 326 LEU A N 1 ATOM 2466 C CA . LEU A 1 307 ? 77.389 11.370 25.421 1.00 111.74 ? 326 LEU A CA 1 ATOM 2467 C C . LEU A 1 307 ? 78.340 12.176 26.285 1.00 109.61 ? 326 LEU A C 1 ATOM 2468 O O . LEU A 1 307 ? 78.129 13.377 26.480 1.00 107.37 ? 326 LEU A O 1 ATOM 2469 C CB . LEU A 1 307 ? 77.583 11.779 23.947 1.00 114.80 ? 326 LEU A CB 1 ATOM 2470 C CG . LEU A 1 307 ? 76.987 10.895 22.857 1.00 119.82 ? 326 LEU A CG 1 ATOM 2471 C CD1 . LEU A 1 307 ? 77.142 11.555 21.505 1.00 123.96 ? 326 LEU A CD1 1 ATOM 2472 C CD2 . LEU A 1 307 ? 77.647 9.526 22.818 1.00 122.61 ? 326 LEU A CD2 1 ATOM 2473 N N . VAL A 1 308 ? 79.389 11.519 26.794 1.00 112.12 ? 327 VAL A N 1 ATOM 2474 C CA . VAL A 1 308 ? 80.424 12.156 27.607 1.00 113.07 ? 327 VAL A CA 1 ATOM 2475 C C . VAL A 1 308 ? 81.582 12.533 26.670 1.00 116.25 ? 327 VAL A C 1 ATOM 2476 O O . VAL A 1 308 ? 82.064 11.685 25.917 1.00 120.50 ? 327 VAL A O 1 ATOM 2477 C CB . VAL A 1 308 ? 80.873 11.268 28.806 1.00 113.91 ? 327 VAL A CB 1 ATOM 2478 C CG1 . VAL A 1 308 ? 82.076 11.870 29.530 1.00 114.48 ? 327 VAL A CG1 1 ATOM 2479 C CG2 . VAL A 1 308 ? 79.725 11.040 29.789 1.00 113.21 ? 327 VAL A CG2 1 ATOM 2480 N N . SER A 1 309 ? 81.994 13.812 26.701 1.00 116.44 ? 328 SER A N 1 ATOM 2481 C CA . SER A 1 309 ? 83.076 14.348 25.874 1.00 120.27 ? 328 SER A CA 1 ATOM 2482 C C . SER A 1 309 ? 84.095 15.108 26.707 1.00 120.63 ? 328 SER A C 1 ATOM 2483 O O . SER A 1 309 ? 83.790 15.531 27.821 1.00 117.60 ? 328 SER A O 1 ATOM 2484 C CB . SER A 1 309 ? 82.516 15.267 24.795 1.00 123.21 ? 328 SER A CB 1 ATOM 2485 O OG . SER A 1 309 ? 81.892 14.519 23.766 1.00 127.28 ? 328 SER A OG 1 ATOM 2486 N N . CYS A 1 310 ? 85.297 15.301 26.151 1.00 124.68 ? 329 CYS A N 1 ATOM 2487 C CA . CYS A 1 310 ? 86.378 16.028 26.804 1.00 126.48 ? 329 CYS A CA 1 ATOM 2488 C C . CYS A 1 310 ? 86.747 17.274 26.023 1.00 130.50 ? 329 CYS A C 1 ATOM 2489 O O . CYS A 1 310 ? 86.461 17.359 24.825 1.00 133.86 ? 329 CYS A O 1 ATOM 2490 C CB . CYS A 1 310 ? 87.586 15.120 27.006 1.00 128.42 ? 329 CYS A CB 1 ATOM 2491 S SG . CYS A 1 310 ? 87.278 13.727 28.117 1.00 125.14 ? 329 CYS A SG 1 ATOM 2492 N N . ASP A 1 311 ? 87.411 18.232 26.697 1.00 132.05 ? 330 ASP A N 1 ATOM 2493 C CA . ASP A 1 311 ? 87.901 19.469 26.091 1.00 139.02 ? 330 ASP A CA 1 ATOM 2494 C C . ASP A 1 311 ? 88.980 19.144 25.067 1.00 144.58 ? 330 ASP A C 1 ATOM 2495 O O . ASP A 1 311 ? 89.516 18.031 25.069 1.00 143.43 ? 330 ASP A O 1 ATOM 2496 C CB . ASP A 1 311 ? 88.493 20.400 27.163 1.00 144.59 ? 330 ASP A CB 1 ATOM 2497 C CG . ASP A 1 311 ? 87.497 20.970 28.152 1.00 142.60 ? 330 ASP A CG 1 ATOM 2498 O OD1 . ASP A 1 311 ? 86.292 21.030 27.819 1.00 140.01 ? 330 ASP A OD1 1 ATOM 2499 O OD2 . ASP A 1 311 ? 87.924 21.382 29.249 1.00 146.98 ? 330 ASP A OD2 1 ATOM 2500 N N . THR A 1 312 ? 89.302 20.112 24.194 1.00 151.97 ? 331 THR A N 1 ATOM 2501 C CA . THR A 1 312 ? 90.344 19.924 23.188 1.00 161.06 ? 331 THR A CA 1 ATOM 2502 C C . THR A 1 312 ? 91.683 19.766 23.912 1.00 164.94 ? 331 THR A C 1 ATOM 2503 O O . THR A 1 312 ? 92.010 20.575 24.781 1.00 165.73 ? 331 THR A O 1 ATOM 2504 C CB . THR A 1 312 ? 90.333 21.041 22.137 1.00 170.86 ? 331 THR A CB 1 ATOM 2505 O OG1 . THR A 1 312 ? 88.992 21.470 21.883 1.00 167.10 ? 331 THR A OG1 1 ATOM 2506 C CG2 . THR A 1 312 ? 90.967 20.599 20.838 1.00 183.38 ? 331 THR A CG2 1 ATOM 2507 N N . GLY A 1 313 ? 92.401 18.674 23.617 1.00 167.62 ? 332 GLY A N 1 ATOM 2508 C CA . GLY A 1 313 ? 93.676 18.338 24.256 1.00 172.14 ? 332 GLY A CA 1 ATOM 2509 C C . GLY A 1 313 ? 93.495 17.237 25.310 1.00 165.32 ? 332 GLY A C 1 ATOM 2510 O O . GLY A 1 313 ? 94.454 16.881 26.001 1.00 169.68 ? 332 GLY A O 1 ATOM 2511 N N . TYR A 1 314 ? 92.262 16.706 25.427 1.00 156.59 ? 333 TYR A N 1 ATOM 2512 C CA . TYR A 1 314 ? 91.885 15.649 26.363 1.00 149.90 ? 333 TYR A CA 1 ATOM 2513 C C . TYR A 1 314 ? 90.983 14.621 25.685 1.00 144.55 ? 333 TYR A C 1 ATOM 2514 O O . TYR A 1 314 ? 90.285 14.945 24.721 1.00 142.83 ? 333 TYR A O 1 ATOM 2515 C CB . TYR A 1 314 ? 91.142 16.235 27.576 1.00 145.08 ? 333 TYR A CB 1 ATOM 2516 C CG . TYR A 1 314 ? 91.985 17.106 28.478 1.00 149.84 ? 333 TYR A CG 1 ATOM 2517 C CD1 . TYR A 1 314 ? 92.221 18.441 28.168 1.00 154.27 ? 333 TYR A CD1 1 ATOM 2518 C CD2 . TYR A 1 314 ? 92.456 16.628 29.696 1.00 151.73 ? 333 TYR A CD2 1 ATOM 2519 C CE1 . TYR A 1 314 ? 92.968 19.257 29.011 1.00 160.40 ? 333 TYR A CE1 1 ATOM 2520 C CE2 . TYR A 1 314 ? 93.217 17.432 30.544 1.00 157.18 ? 333 TYR A CE2 1 ATOM 2521 C CZ . TYR A 1 314 ? 93.481 18.744 30.191 1.00 161.25 ? 333 TYR A CZ 1 ATOM 2522 O OH . TYR A 1 314 ? 94.224 19.543 31.027 1.00 168.51 ? 333 TYR A OH 1 ATOM 2523 N N . LYS A 1 315 ? 90.986 13.384 26.207 1.00 142.83 ? 334 LYS A N 1 ATOM 2524 C CA . LYS A 1 315 ? 90.151 12.283 25.716 1.00 139.73 ? 334 LYS A CA 1 ATOM 2525 C C . LYS A 1 315 ? 89.533 11.523 26.891 1.00 134.80 ? 334 LYS A C 1 ATOM 2526 O O . LYS A 1 315 ? 90.069 11.575 28.001 1.00 138.05 ? 334 LYS A O 1 ATOM 2527 C CB . LYS A 1 315 ? 90.954 11.326 24.807 1.00 148.10 ? 334 LYS A CB 1 ATOM 2528 C CG . LYS A 1 315 ? 91.466 11.942 23.497 1.00 155.61 ? 334 LYS A CG 1 ATOM 2529 C CD . LYS A 1 315 ? 90.341 12.317 22.534 1.00 151.74 ? 334 LYS A CD 1 ATOM 2530 C CE . LYS A 1 315 ? 90.840 13.049 21.315 1.00 161.29 ? 334 LYS A CE 1 ATOM 2531 N NZ . LYS A 1 315 ? 89.723 13.425 20.410 1.00 159.37 ? 334 LYS A NZ 1 ATOM 2532 N N . VAL A 1 316 ? 88.387 10.851 26.657 1.00 129.94 ? 335 VAL A N 1 ATOM 2533 C CA . VAL A 1 316 ? 87.675 10.065 27.674 1.00 127.21 ? 335 VAL A CA 1 ATOM 2534 C C . VAL A 1 316 ? 88.512 8.850 28.048 1.00 134.10 ? 335 VAL A C 1 ATOM 2535 O O . VAL A 1 316 ? 89.019 8.160 27.164 1.00 140.03 ? 335 VAL A O 1 ATOM 2536 C CB . VAL A 1 316 ? 86.256 9.634 27.217 1.00 124.90 ? 335 VAL A CB 1 ATOM 2537 C CG1 . VAL A 1 316 ? 85.585 8.750 28.261 1.00 124.05 ? 335 VAL A CG1 1 ATOM 2538 C CG2 . VAL A 1 316 ? 85.378 10.836 26.894 1.00 120.22 ? 335 VAL A CG2 1 ATOM 2539 N N . LEU A 1 317 ? 88.621 8.577 29.353 1.00 137.84 ? 336 LEU A N 1 ATOM 2540 C CA . LEU A 1 317 ? 89.381 7.450 29.862 1.00 148.13 ? 336 LEU A CA 1 ATOM 2541 C C . LEU A 1 317 ? 88.496 6.369 30.484 1.00 150.71 ? 336 LEU A C 1 ATOM 2542 O O . LEU A 1 317 ? 87.888 6.587 31.533 1.00 149.43 ? 336 LEU A O 1 ATOM 2543 C CB . LEU A 1 317 ? 90.443 7.944 30.863 1.00 153.16 ? 336 LEU A CB 1 ATOM 2544 C CG . LEU A 1 317 ? 91.506 6.948 31.308 1.00 163.87 ? 336 LEU A CG 1 ATOM 2545 C CD1 . LEU A 1 317 ? 92.471 6.639 30.179 1.00 168.97 ? 336 LEU A CD1 1 ATOM 2546 C CD2 . LEU A 1 317 ? 92.272 7.479 32.502 1.00 167.48 ? 336 LEU A CD2 1 ATOM 2547 N N . LYS A 1 318 ? 88.436 5.202 29.824 1.00 157.36 ? 337 LYS A N 1 ATOM 2548 C CA . LYS A 1 318 ? 87.727 4.009 30.292 1.00 163.29 ? 337 LYS A CA 1 ATOM 2549 C C . LYS A 1 318 ? 88.792 2.982 30.615 1.00 174.85 ? 337 LYS A C 1 ATOM 2550 O O . LYS A 1 318 ? 89.612 2.677 29.745 1.00 179.70 ? 337 LYS A O 1 ATOM 2551 C CB . LYS A 1 318 ? 86.751 3.477 29.233 1.00 163.03 ? 337 LYS A CB 1 ATOM 2552 C CG . LYS A 1 318 ? 85.462 4.293 29.112 1.00 154.07 ? 337 LYS A CG 1 ATOM 2553 C CD . LYS A 1 318 ? 84.577 4.268 30.374 1.00 152.57 ? 337 LYS A CD 1 ATOM 2554 C CE . LYS A 1 318 ? 83.947 2.923 30.650 1.00 159.38 ? 337 LYS A CE 1 ATOM 2555 N NZ . LYS A 1 318 ? 83.752 2.705 32.105 1.00 162.16 ? 337 LYS A NZ 1 ATOM 2556 N N . ASP A 1 319 ? 88.804 2.474 31.873 1.00 180.65 ? 338 ASP A N 1 ATOM 2557 C CA . ASP A 1 319 ? 89.835 1.574 32.407 1.00 193.72 ? 338 ASP A CA 1 ATOM 2558 C C . ASP A 1 319 ? 91.135 2.364 32.207 1.00 196.29 ? 338 ASP A C 1 ATOM 2559 O O . ASP A 1 319 ? 91.257 3.443 32.788 1.00 192.69 ? 338 ASP A O 1 ATOM 2560 C CB . ASP A 1 319 ? 89.833 0.202 31.698 1.00 201.62 ? 338 ASP A CB 1 ATOM 2561 C CG . ASP A 1 319 ? 90.149 -0.953 32.622 1.00 242.39 ? 338 ASP A CG 1 ATOM 2562 O OD1 . ASP A 1 319 ? 89.215 -1.456 33.280 1.00 243.50 ? 338 ASP A OD1 1 ATOM 2563 O OD2 . ASP A 1 319 ? 91.329 -1.355 32.686 1.00 265.70 ? 338 ASP A OD2 1 ATOM 2564 N N . ASN A 1 320 ? 92.030 1.927 31.312 1.00 204.19 ? 339 ASN A N 1 ATOM 2565 C CA . ASN A 1 320 ? 93.225 2.704 30.992 1.00 205.03 ? 339 ASN A CA 1 ATOM 2566 C C . ASN A 1 320 ? 93.332 2.879 29.459 1.00 203.21 ? 339 ASN A C 1 ATOM 2567 O O . ASN A 1 320 ? 94.426 2.975 28.901 1.00 209.19 ? 339 ASN A O 1 ATOM 2568 C CB . ASN A 1 320 ? 94.479 2.104 31.638 1.00 238.07 ? 339 ASN A CB 1 ATOM 2569 C CG . ASN A 1 320 ? 94.391 1.838 33.126 1.00 254.89 ? 339 ASN A CG 1 ATOM 2570 O OD1 . ASN A 1 320 ? 93.757 2.569 33.895 1.00 238.85 ? 339 ASN A OD1 1 ATOM 2571 N ND2 . ASN A 1 320 ? 95.070 0.797 33.573 1.00 292.75 ? 339 ASN A ND2 1 ATOM 2572 N N . VAL A 1 321 ? 92.153 2.974 28.800 1.00 193.22 ? 340 VAL A N 1 ATOM 2573 C CA . VAL A 1 321 ? 91.959 3.104 27.349 1.00 191.69 ? 340 VAL A CA 1 ATOM 2574 C C . VAL A 1 321 ? 91.332 4.468 26.992 1.00 179.06 ? 340 VAL A C 1 ATOM 2575 O O . VAL A 1 321 ? 90.313 4.840 27.583 1.00 169.01 ? 340 VAL A O 1 ATOM 2576 C CB . VAL A 1 321 ? 91.083 1.937 26.806 1.00 194.26 ? 340 VAL A CB 1 ATOM 2577 C CG1 . VAL A 1 321 ? 91.086 1.905 25.280 1.00 196.15 ? 340 VAL A CG1 1 ATOM 2578 C CG2 . VAL A 1 321 ? 91.517 0.587 27.373 1.00 207.54 ? 340 VAL A CG2 1 ATOM 2579 N N . GLU A 1 322 ? 91.936 5.185 26.008 1.00 181.27 ? 341 GLU A N 1 ATOM 2580 C CA A GLU A 1 322 ? 91.480 6.500 25.539 0.50 172.65 ? 341 GLU A CA 1 ATOM 2581 C CA B GLU A 1 322 ? 91.467 6.496 25.547 0.50 173.14 ? 341 GLU A CA 1 ATOM 2582 C C . GLU A 1 322 ? 90.449 6.406 24.407 1.00 170.38 ? 341 GLU A C 1 ATOM 2583 O O . GLU A 1 322 ? 90.564 5.531 23.547 1.00 179.00 ? 341 GLU A O 1 ATOM 2584 C CB A GLU A 1 322 ? 92.674 7.363 25.100 0.50 177.63 ? 341 GLU A CB 1 ATOM 2585 C CB B GLU A 1 322 ? 92.639 7.444 25.208 0.50 177.96 ? 341 GLU A CB 1 ATOM 2586 C CG A GLU A 1 322 ? 93.455 7.966 26.255 0.50 177.77 ? 341 GLU A CG 1 ATOM 2587 C CG B GLU A 1 322 ? 93.655 6.914 24.204 0.50 190.23 ? 341 GLU A CG 1 ATOM 2588 C CD A GLU A 1 322 ? 94.749 8.655 25.866 0.50 184.87 ? 341 GLU A CD 1 ATOM 2589 C CD B GLU A 1 322 ? 93.309 7.129 22.744 0.50 199.56 ? 341 GLU A CD 1 ATOM 2590 O OE1 A GLU A 1 322 ? 94.694 9.645 25.101 0.50 184.13 ? 341 GLU A OE1 1 ATOM 2591 O OE1 B GLU A 1 322 ? 93.260 8.302 22.307 0.50 196.58 ? 341 GLU A OE1 1 ATOM 2592 O OE2 A GLU A 1 322 ? 95.820 8.208 26.335 0.50 192.97 ? 341 GLU A OE2 1 ATOM 2593 O OE2 B GLU A 1 322 ? 93.116 6.121 22.027 0.50 210.52 ? 341 GLU A OE2 1 ATOM 2594 N N . MET A 1 323 ? 89.447 7.323 24.403 1.00 161.01 ? 342 MET A N 1 ATOM 2595 C CA . MET A 1 323 ? 88.374 7.404 23.393 1.00 159.16 ? 342 MET A CA 1 ATOM 2596 C C . MET A 1 323 ? 87.767 8.817 23.259 1.00 151.54 ? 342 MET A C 1 ATOM 2597 O O . MET A 1 323 ? 87.895 9.621 24.181 1.00 147.16 ? 342 MET A O 1 ATOM 2598 C CB . MET A 1 323 ? 87.286 6.342 23.637 1.00 158.54 ? 342 MET A CB 1 ATOM 2599 C CG . MET A 1 323 ? 86.467 6.560 24.897 1.00 151.77 ? 342 MET A CG 1 ATOM 2600 S SD . MET A 1 323 ? 85.662 5.047 25.472 1.00 156.05 ? 342 MET A SD 1 ATOM 2601 C CE . MET A 1 323 ? 84.607 4.666 24.071 1.00 158.73 ? 342 MET A CE 1 ATOM 2602 N N . ASP A 1 324 ? 87.093 9.104 22.123 1.00 153.10 ? 343 ASP A N 1 ATOM 2603 C CA . ASP A 1 324 ? 86.490 10.414 21.839 1.00 148.51 ? 343 ASP A CA 1 ATOM 2604 C C . ASP A 1 324 ? 85.205 10.705 22.616 1.00 139.26 ? 343 ASP A C 1 ATOM 2605 O O . ASP A 1 324 ? 85.061 11.798 23.172 1.00 134.51 ? 343 ASP A O 1 ATOM 2606 C CB . ASP A 1 324 ? 86.288 10.616 20.327 1.00 156.03 ? 343 ASP A CB 1 ATOM 2607 C CG . ASP A 1 324 ? 87.564 10.581 19.502 1.00 166.11 ? 343 ASP A CG 1 ATOM 2608 O OD1 . ASP A 1 324 ? 88.648 10.850 20.066 1.00 165.59 ? 343 ASP A OD1 1 ATOM 2609 O OD2 . ASP A 1 324 ? 87.476 10.308 18.289 1.00 175.44 ? 343 ASP A OD2 1 ATOM 2610 N N . THR A 1 325 ? 84.260 9.749 22.620 1.00 138.06 ? 344 THR A N 1 ATOM 2611 C CA . THR A 1 325 ? 82.992 9.872 23.344 1.00 131.91 ? 344 THR A CA 1 ATOM 2612 C C . THR A 1 325 ? 82.611 8.551 23.985 1.00 132.29 ? 344 THR A C 1 ATOM 2613 O O . THR A 1 325 ? 82.960 7.487 23.471 1.00 139.13 ? 344 THR A O 1 ATOM 2614 C CB . THR A 1 325 ? 81.819 10.342 22.444 1.00 131.32 ? 344 THR A CB 1 ATOM 2615 O OG1 . THR A 1 325 ? 81.559 9.378 21.425 1.00 138.36 ? 344 THR A OG1 1 ATOM 2616 C CG2 . THR A 1 325 ? 82.019 11.727 21.843 1.00 131.65 ? 344 THR A CG2 1 ATOM 2617 N N . PHE A 1 326 ? 81.860 8.627 25.088 1.00 127.16 ? 345 PHE A N 1 ATOM 2618 C CA . PHE A 1 326 ? 81.312 7.470 25.781 1.00 127.29 ? 345 PHE A CA 1 ATOM 2619 C C . PHE A 1 326 ? 79.830 7.707 26.004 1.00 122.51 ? 345 PHE A C 1 ATOM 2620 O O . PHE A 1 326 ? 79.438 8.795 26.433 1.00 117.12 ? 345 PHE A O 1 ATOM 2621 C CB . PHE A 1 326 ? 82.041 7.172 27.100 1.00 128.59 ? 345 PHE A CB 1 ATOM 2622 C CG . PHE A 1 326 ? 81.541 5.923 27.796 1.00 132.44 ? 345 PHE A CG 1 ATOM 2623 C CD1 . PHE A 1 326 ? 81.553 4.691 27.148 1.00 138.95 ? 345 PHE A CD1 1 ATOM 2624 C CD2 . PHE A 1 326 ? 81.065 5.977 29.100 1.00 131.09 ? 345 PHE A CD2 1 ATOM 2625 C CE1 . PHE A 1 326 ? 81.082 3.540 27.788 1.00 143.63 ? 345 PHE A CE1 1 ATOM 2626 C CE2 . PHE A 1 326 ? 80.617 4.820 29.746 1.00 136.29 ? 345 PHE A CE2 1 ATOM 2627 C CZ . PHE A 1 326 ? 80.615 3.613 29.082 1.00 142.12 ? 345 PHE A CZ 1 ATOM 2628 N N . GLN A 1 327 ? 79.006 6.699 25.683 1.00 123.93 ? 346 GLN A N 1 ATOM 2629 C CA . GLN A 1 327 ? 77.557 6.795 25.807 1.00 119.59 ? 346 GLN A CA 1 ATOM 2630 C C . GLN A 1 327 ? 77.006 6.011 26.988 1.00 119.71 ? 346 GLN A C 1 ATOM 2631 O O . GLN A 1 327 ? 77.279 4.817 27.127 1.00 123.62 ? 346 GLN A O 1 ATOM 2632 C CB . GLN A 1 327 ? 76.867 6.361 24.502 1.00 124.86 ? 346 GLN A CB 1 ATOM 2633 C CG . GLN A 1 327 ? 75.385 6.732 24.442 1.00 124.53 ? 346 GLN A CG 1 ATOM 2634 C CD . GLN A 1 327 ? 74.748 6.443 23.108 1.00 129.81 ? 346 GLN A CD 1 ATOM 2635 O OE1 . GLN A 1 327 ? 75.205 6.901 22.055 1.00 132.38 ? 346 GLN A OE1 1 ATOM 2636 N NE2 . GLN A 1 327 ? 73.621 5.745 23.134 1.00 132.66 ? 346 GLN A NE2 1 ATOM 2637 N N . ILE A 1 328 ? 76.215 6.695 27.826 1.00 116.51 ? 347 ILE A N 1 ATOM 2638 C CA . ILE A 1 328 ? 75.517 6.109 28.971 1.00 118.64 ? 347 ILE A CA 1 ATOM 2639 C C . ILE A 1 328 ? 74.022 6.369 28.836 1.00 119.76 ? 347 ILE A C 1 ATOM 2640 O O . ILE A 1 328 ? 73.620 7.356 28.210 1.00 118.23 ? 347 ILE A O 1 ATOM 2641 C CB . ILE A 1 328 ? 76.087 6.499 30.367 1.00 119.26 ? 347 ILE A CB 1 ATOM 2642 C CG1 . ILE A 1 328 ? 75.988 8.014 30.639 1.00 114.75 ? 347 ILE A CG1 1 ATOM 2643 C CG2 . ILE A 1 328 ? 77.504 5.980 30.539 1.00 122.47 ? 347 ILE A CG2 1 ATOM 2644 C CD1 . ILE A 1 328 ? 76.388 8.504 32.065 1.00 115.29 ? 347 ILE A CD1 1 ATOM 2645 N N . GLU A 1 329 ? 73.203 5.472 29.400 1.00 123.11 ? 348 GLU A N 1 ATOM 2646 C CA . GLU A 1 329 ? 71.753 5.588 29.341 1.00 125.16 ? 348 GLU A CA 1 ATOM 2647 C C . GLU A 1 329 ? 71.080 5.425 30.694 1.00 127.55 ? 348 GLU A C 1 ATOM 2648 O O . GLU A 1 329 ? 71.592 4.719 31.567 1.00 130.02 ? 348 GLU A O 1 ATOM 2649 C CB . GLU A 1 329 ? 71.160 4.615 28.312 1.00 129.61 ? 348 GLU A CB 1 ATOM 2650 C CG . GLU A 1 329 ? 71.142 3.150 28.724 1.00 135.40 ? 348 GLU A CG 1 ATOM 2651 C CD . GLU A 1 329 ? 70.451 2.205 27.760 1.00 141.32 ? 348 GLU A CD 1 ATOM 2652 O OE1 . GLU A 1 329 ? 69.543 2.651 27.021 1.00 142.59 ? 348 GLU A OE1 1 ATOM 2653 O OE2 . GLU A 1 329 ? 70.805 1.004 27.763 1.00 145.84 ? 348 GLU A OE2 1 ATOM 2654 N N . CYS A 1 330 ? 69.923 6.078 30.857 1.00 128.78 ? 349 CYS A N 1 ATOM 2655 C CA . CYS A 1 330 ? 69.125 5.994 32.071 1.00 132.48 ? 349 CYS A CA 1 ATOM 2656 C C . CYS A 1 330 ? 68.285 4.718 31.979 1.00 138.00 ? 349 CYS A C 1 ATOM 2657 O O . CYS A 1 330 ? 67.422 4.610 31.105 1.00 138.79 ? 349 CYS A O 1 ATOM 2658 C CB . CYS A 1 330 ? 68.259 7.242 32.234 1.00 132.21 ? 349 CYS A CB 1 ATOM 2659 S SG . CYS A 1 330 ? 67.183 7.221 33.692 1.00 139.24 ? 349 CYS A SG 1 ATOM 2660 N N . LEU A 1 331 ? 68.582 3.734 32.845 1.00 142.36 ? 350 LEU A N 1 ATOM 2661 C CA . LEU A 1 331 ? 67.902 2.436 32.865 1.00 149.22 ? 350 LEU A CA 1 ATOM 2662 C C . LEU A 1 331 ? 66.552 2.474 33.575 1.00 154.89 ? 350 LEU A C 1 ATOM 2663 O O . LEU A 1 331 ? 66.232 3.449 34.257 1.00 153.22 ? 350 LEU A O 1 ATOM 2664 C CB . LEU A 1 331 ? 68.803 1.338 33.465 1.00 154.56 ? 350 LEU A CB 1 ATOM 2665 C CG . LEU A 1 331 ? 70.175 1.135 32.817 1.00 151.95 ? 350 LEU A CG 1 ATOM 2666 C CD1 . LEU A 1 331 ? 71.090 0.362 33.737 1.00 160.27 ? 350 LEU A CD1 1 ATOM 2667 C CD2 . LEU A 1 331 ? 70.062 0.442 31.463 1.00 151.70 ? 350 LEU A CD2 1 ATOM 2668 N N . LYS A 1 332 ? 65.764 1.400 33.406 1.00 161.85 ? 351 LYS A N 1 ATOM 2669 C CA . LYS A 1 332 ? 64.426 1.228 33.966 1.00 168.53 ? 351 LYS A CA 1 ATOM 2670 C C . LYS A 1 332 ? 64.386 1.376 35.486 1.00 174.21 ? 351 LYS A C 1 ATOM 2671 O O . LYS A 1 332 ? 63.482 2.030 36.007 1.00 175.99 ? 351 LYS A O 1 ATOM 2672 C CB . LYS A 1 332 ? 63.858 -0.124 33.519 1.00 176.28 ? 351 LYS A CB 1 ATOM 2673 C CG . LYS A 1 332 ? 62.399 -0.336 33.859 1.00 182.73 ? 351 LYS A CG 1 ATOM 2674 C CD . LYS A 1 332 ? 61.959 -1.748 33.489 1.00 191.17 ? 351 LYS A CD 1 ATOM 2675 C CE . LYS A 1 332 ? 60.948 -2.347 34.447 1.00 198.35 ? 351 LYS A CE 1 ATOM 2676 N NZ . LYS A 1 332 ? 59.664 -1.593 34.508 1.00 197.15 ? 351 LYS A NZ 1 ATOM 2677 N N . ASP A 1 333 ? 65.375 0.799 36.188 1.00 180.66 ? 352 ASP A N 1 ATOM 2678 C CA . ASP A 1 333 ? 65.468 0.832 37.649 1.00 190.57 ? 352 ASP A CA 1 ATOM 2679 C C . ASP A 1 333 ? 65.856 2.203 38.237 1.00 185.07 ? 352 ASP A C 1 ATOM 2680 O O . ASP A 1 333 ? 65.931 2.341 39.459 1.00 194.11 ? 352 ASP A O 1 ATOM 2681 C CB . ASP A 1 333 ? 66.406 -0.280 38.149 1.00 201.16 ? 352 ASP A CB 1 ATOM 2682 C CG . ASP A 1 333 ? 67.868 -0.129 37.762 1.00 195.19 ? 352 ASP A CG 1 ATOM 2683 O OD1 . ASP A 1 333 ? 68.186 0.781 36.961 1.00 183.02 ? 352 ASP A OD1 1 ATOM 2684 O OD2 . ASP A 1 333 ? 68.693 -0.924 38.255 1.00 204.52 ? 352 ASP A OD2 1 ATOM 2685 N N . GLY A 1 334 ? 66.106 3.204 37.375 1.00 171.78 ? 353 GLY A N 1 ATOM 2686 C CA . GLY A 1 334 ? 66.466 4.559 37.796 1.00 167.47 ? 353 GLY A CA 1 ATOM 2687 C C . GLY A 1 334 ? 67.963 4.755 37.971 1.00 164.74 ? 353 GLY A C 1 ATOM 2688 O O . GLY A 1 334 ? 68.379 5.748 38.567 1.00 164.16 ? 353 GLY A O 1 ATOM 2689 N N . THR A 1 335 ? 68.767 3.819 37.449 1.00 163.08 ? 354 THR A N 1 ATOM 2690 C CA . THR A 1 335 ? 70.225 3.883 37.526 1.00 159.88 ? 354 THR A CA 1 ATOM 2691 C C . THR A 1 335 ? 70.802 4.113 36.136 1.00 148.91 ? 354 THR A C 1 ATOM 2692 O O . THR A 1 335 ? 70.142 3.823 35.137 1.00 144.85 ? 354 THR A O 1 ATOM 2693 C CB . THR A 1 335 ? 70.807 2.600 38.154 1.00 170.34 ? 354 THR A CB 1 ATOM 2694 O OG1 . THR A 1 335 ? 70.729 1.527 37.215 1.00 170.54 ? 354 THR A OG1 1 ATOM 2695 C CG2 . THR A 1 335 ? 70.133 2.217 39.471 1.00 182.62 ? 354 THR A CG2 1 ATOM 2696 N N . TRP A 1 336 ? 72.035 4.617 36.072 1.00 144.93 ? 355 TRP A N 1 ATOM 2697 C CA . TRP A 1 336 ? 72.732 4.831 34.811 1.00 137.13 ? 355 TRP A CA 1 ATOM 2698 C C . TRP A 1 336 ? 73.418 3.532 34.395 1.00 141.65 ? 355 TRP A C 1 ATOM 2699 O O . TRP A 1 336 ? 73.756 2.719 35.260 1.00 150.60 ? 355 TRP A O 1 ATOM 2700 C CB . TRP A 1 336 ? 73.738 5.982 34.945 1.00 131.97 ? 355 TRP A CB 1 ATOM 2701 C CG . TRP A 1 336 ? 73.072 7.324 35.014 1.00 127.21 ? 355 TRP A CG 1 ATOM 2702 C CD1 . TRP A 1 336 ? 72.786 8.045 36.136 1.00 130.07 ? 355 TRP A CD1 1 ATOM 2703 C CD2 . TRP A 1 336 ? 72.544 8.069 33.911 1.00 119.88 ? 355 TRP A CD2 1 ATOM 2704 N NE1 . TRP A 1 336 ? 72.133 9.208 35.798 1.00 125.44 ? 355 TRP A NE1 1 ATOM 2705 C CE2 . TRP A 1 336 ? 71.973 9.250 34.437 1.00 119.93 ? 355 TRP A CE2 1 ATOM 2706 C CE3 . TRP A 1 336 ? 72.516 7.865 32.522 1.00 118.09 ? 355 TRP A CE3 1 ATOM 2707 C CZ2 . TRP A 1 336 ? 71.361 10.211 33.623 1.00 118.16 ? 355 TRP A CZ2 1 ATOM 2708 C CZ3 . TRP A 1 336 ? 71.921 8.822 31.715 1.00 116.47 ? 355 TRP A CZ3 1 ATOM 2709 C CH2 . TRP A 1 336 ? 71.360 9.983 32.264 1.00 116.37 ? 355 TRP A CH2 1 ATOM 2710 N N . SER A 1 337 ? 73.608 3.326 33.076 1.00 137.48 ? 356 SER A N 1 ATOM 2711 C CA . SER A 1 337 ? 74.259 2.129 32.529 1.00 142.79 ? 356 SER A CA 1 ATOM 2712 C C . SER A 1 337 ? 75.712 2.023 32.992 1.00 144.99 ? 356 SER A C 1 ATOM 2713 O O . SER A 1 337 ? 76.232 0.916 33.143 1.00 152.61 ? 356 SER A O 1 ATOM 2714 C CB . SER A 1 337 ? 74.191 2.126 31.006 1.00 139.16 ? 356 SER A CB 1 ATOM 2715 O OG . SER A 1 337 ? 74.959 3.182 30.455 1.00 131.71 ? 356 SER A OG 1 ATOM 2716 N N . ASN A 1 338 ? 76.354 3.182 33.222 1.00 139.35 ? 357 ASN A N 1 ATOM 2717 C CA . ASN A 1 338 ? 77.732 3.296 33.689 1.00 142.06 ? 357 ASN A CA 1 ATOM 2718 C C . ASN A 1 338 ? 77.953 4.585 34.469 1.00 138.45 ? 357 ASN A C 1 ATOM 2719 O O . ASN A 1 338 ? 77.109 5.485 34.448 1.00 135.04 ? 357 ASN A O 1 ATOM 2720 C CB . ASN A 1 338 ? 78.694 3.249 32.507 1.00 140.08 ? 357 ASN A CB 1 ATOM 2721 C CG . ASN A 1 338 ? 79.407 1.941 32.374 1.00 149.15 ? 357 ASN A CG 1 ATOM 2722 O OD1 . ASN A 1 338 ? 80.340 1.640 33.124 1.00 153.88 ? 357 ASN A OD1 1 ATOM 2723 N ND2 . ASN A 1 338 ? 78.987 1.139 31.410 1.00 152.49 ? 357 ASN A ND2 1 ATOM 2724 N N . LYS A 1 339 ? 79.104 4.679 35.145 1.00 140.65 ? 358 LYS A N 1 ATOM 2725 C CA . LYS A 1 339 ? 79.493 5.878 35.877 1.00 137.25 ? 358 LYS A CA 1 ATOM 2726 C C . LYS A 1 339 ? 80.109 6.858 34.872 1.00 129.24 ? 358 LYS A C 1 ATOM 2727 O O . LYS A 1 339 ? 80.418 6.460 33.744 1.00 127.23 ? 358 LYS A O 1 ATOM 2728 C CB . LYS A 1 339 ? 80.499 5.531 36.988 1.00 144.10 ? 358 LYS A CB 1 ATOM 2729 C CG . LYS A 1 339 ? 79.869 4.835 38.189 1.00 155.37 ? 358 LYS A CG 1 ATOM 2730 N N . ILE A 1 340 ? 80.269 8.135 35.267 1.00 125.72 ? 359 ILE A N 1 ATOM 2731 C CA . ILE A 1 340 ? 80.874 9.156 34.407 1.00 119.56 ? 359 ILE A CA 1 ATOM 2732 C C . ILE A 1 340 ? 82.381 8.950 34.434 1.00 121.91 ? 359 ILE A C 1 ATOM 2733 O O . ILE A 1 340 ? 82.981 9.020 35.511 1.00 127.02 ? 359 ILE A O 1 ATOM 2734 C CB . ILE A 1 340 ? 80.477 10.621 34.778 1.00 116.57 ? 359 ILE A CB 1 ATOM 2735 C CG1 . ILE A 1 340 ? 78.974 10.866 34.608 1.00 114.29 ? 359 ILE A CG1 1 ATOM 2736 C CG2 . ILE A 1 340 ? 81.288 11.659 33.984 1.00 113.13 ? 359 ILE A CG2 1 ATOM 2737 C CD1 . ILE A 1 340 ? 78.201 10.524 35.820 1.00 119.01 ? 359 ILE A CD1 1 ATOM 2738 N N . PRO A 1 341 ? 82.998 8.698 33.263 1.00 120.69 ? 360 PRO A N 1 ATOM 2739 C CA . PRO A 1 341 ? 84.446 8.520 33.226 1.00 123.91 ? 360 PRO A CA 1 ATOM 2740 C C . PRO A 1 341 ? 85.167 9.872 33.307 1.00 122.51 ? 360 PRO A C 1 ATOM 2741 O O . PRO A 1 341 ? 84.528 10.922 33.214 1.00 118.07 ? 360 PRO A O 1 ATOM 2742 C CB . PRO A 1 341 ? 84.679 7.801 31.900 1.00 124.66 ? 360 PRO A CB 1 ATOM 2743 C CG . PRO A 1 341 ? 83.561 8.227 31.043 1.00 119.88 ? 360 PRO A CG 1 ATOM 2744 C CD . PRO A 1 341 ? 82.400 8.565 31.917 1.00 117.83 ? 360 PRO A CD 1 ATOM 2745 N N . THR A 1 342 ? 86.492 9.839 33.492 1.00 129.14 ? 361 THR A N 1 ATOM 2746 C CA . THR A 1 342 ? 87.318 11.043 33.601 1.00 131.49 ? 361 THR A CA 1 ATOM 2747 C C . THR A 1 342 ? 87.979 11.410 32.271 1.00 130.88 ? 361 THR A C 1 ATOM 2748 O O . THR A 1 342 ? 88.018 10.596 31.343 1.00 129.60 ? 361 THR A O 1 ATOM 2749 C CB . THR A 1 342 ? 88.372 10.879 34.710 1.00 139.82 ? 361 THR A CB 1 ATOM 2750 O OG1 . THR A 1 342 ? 89.180 9.736 34.424 1.00 144.10 ? 361 THR A OG1 1 ATOM 2751 C CG2 . THR A 1 342 ? 87.757 10.765 36.101 1.00 142.85 ? 361 THR A CG2 1 ATOM 2752 N N . CYS A 1 343 ? 88.502 12.641 32.189 1.00 133.03 ? 362 CYS A N 1 ATOM 2753 C CA . CYS A 1 343 ? 89.212 13.121 31.013 1.00 135.15 ? 362 CYS A CA 1 ATOM 2754 C C . CYS A 1 343 ? 90.707 13.053 31.259 1.00 143.45 ? 362 CYS A C 1 ATOM 2755 O O . CYS A 1 343 ? 91.179 13.394 32.347 1.00 146.52 ? 362 CYS A O 1 ATOM 2756 C CB . CYS A 1 343 ? 88.759 14.523 30.625 1.00 131.91 ? 362 CYS A CB 1 ATOM 2757 S SG . CYS A 1 343 ? 87.083 14.589 29.945 1.00 122.65 ? 362 CYS A SG 1 ATOM 2758 N N . LYS A 1 344 ? 91.439 12.562 30.258 1.00 148.54 ? 363 LYS A N 1 ATOM 2759 C CA . LYS A 1 344 ? 92.880 12.383 30.306 1.00 157.82 ? 363 LYS A CA 1 ATOM 2760 C C . LYS A 1 344 ? 93.504 13.222 29.213 1.00 159.78 ? 363 LYS A C 1 ATOM 2761 O O . LYS A 1 344 ? 93.099 13.145 28.055 1.00 159.78 ? 363 LYS A O 1 ATOM 2762 C CB . LYS A 1 344 ? 93.227 10.896 30.132 1.00 165.28 ? 363 LYS A CB 1 ATOM 2763 C CG . LYS A 1 344 ? 94.611 10.509 30.630 1.00 177.17 ? 363 LYS A CG 1 ATOM 2764 C CD . LYS A 1 344 ? 95.515 10.115 29.472 1.00 186.95 ? 363 LYS A CD 1 ATOM 2765 C CE . LYS A 1 344 ? 96.939 9.860 29.901 1.00 197.08 ? 363 LYS A CE 1 ATOM 2766 N NZ . LYS A 1 344 ? 97.701 11.125 30.081 1.00 197.11 ? 363 LYS A NZ 1 ATOM 2767 N N . LYS A 1 345 ? 94.474 14.042 29.592 1.00 198.35 ? 364 LYS A N 1 ATOM 2768 C CA . LYS A 1 345 ? 95.215 14.918 28.696 1.00 207.93 ? 364 LYS A CA 1 ATOM 2769 C C . LYS A 1 345 ? 95.960 14.111 27.631 1.00 221.74 ? 364 LYS A C 1 ATOM 2770 O O . LYS A 1 345 ? 96.182 12.913 27.803 1.00 227.55 ? 364 LYS A O 1 ATOM 2771 C CB . LYS A 1 345 ? 96.204 15.727 29.541 1.00 177.96 ? 364 LYS A CB 1 ATOM 2772 C CG . LYS A 1 345 ? 97.015 16.755 28.786 1.00 180.87 ? 364 LYS A CG 1 ATOM 2773 C CD . LYS A 1 345 ? 98.152 17.280 29.635 1.00 182.13 ? 364 LYS A CD 1 ATOM 2774 C CE . LYS A 1 345 ? 99.263 17.856 28.795 1.00 187.36 ? 364 LYS A CE 1 ATOM 2775 N NZ . LYS A 1 345 ? 100.490 18.118 29.591 1.00 189.78 ? 364 LYS A NZ 1 ATOM 2776 N N . ASN A 1 346 ? 96.379 14.774 26.554 1.00 198.02 ? 365 ASN A N 1 ATOM 2777 C CA . ASN A 1 346 ? 97.151 14.134 25.497 1.00 207.10 ? 365 ASN A CA 1 ATOM 2778 C C . ASN A 1 346 ? 98.648 14.072 25.839 1.00 208.08 ? 365 ASN A C 1 ATOM 2779 O O . ASN A 1 346 ? 99.392 13.353 25.168 1.00 216.05 ? 365 ASN A O 1 ATOM 2780 C CB . ASN A 1 346 ? 96.890 14.824 24.162 1.00 213.73 ? 365 ASN A CB 1 ATOM 2781 C CG . ASN A 1 346 ? 95.426 14.857 23.785 1.00 213.77 ? 365 ASN A CG 1 ATOM 2782 O OD1 . ASN A 1 346 ? 94.542 14.416 24.536 1.00 209.60 ? 365 ASN A OD1 1 ATOM 2783 N ND2 . ASN A 1 346 ? 95.132 15.422 22.628 1.00 219.13 ? 365 ASN A ND2 1 ATOM 2784 N N . GLU A 1 347 ? 99.070 14.792 26.907 1.00 203.05 ? 366 GLU A N 1 ATOM 2785 C CA . GLU A 1 347 ? 100.440 14.888 27.432 1.00 203.42 ? 366 GLU A CA 1 ATOM 2786 C C . GLU A 1 347 ? 101.564 15.065 26.401 1.00 213.82 ? 366 GLU A C 1 ATOM 2787 O O . GLU A 1 347 ? 102.255 14.112 26.037 1.00 219.34 ? 366 GLU A O 1 ATOM 2788 C CB . GLU A 1 347 ? 100.746 13.819 28.498 1.00 198.77 ? 366 GLU A CB 1 ATOM 2789 C CG . GLU A 1 347 ? 100.430 14.281 29.913 1.00 189.43 ? 366 GLU A CG 1 ATOM 2790 C CD . GLU A 1 347 ? 101.265 13.704 31.043 1.00 186.23 ? 366 GLU A CD 1 ATOM 2791 O OE1 . GLU A 1 347 ? 102.226 12.949 30.767 1.00 190.81 ? 366 GLU A OE1 1 ATOM 2792 O OE2 . GLU A 1 347 ? 100.967 14.031 32.215 1.00 179.98 ? 366 GLU A OE2 1 HETATM 2793 C C1 . NAG B 2 . ? -16.275 -8.391 15.837 1.00 208.51 ? 649 NAG A C1 1 HETATM 2794 C C2 . NAG B 2 . ? -15.917 -9.573 16.722 1.00 189.18 ? 649 NAG A C2 1 HETATM 2795 C C3 . NAG B 2 . ? -17.116 -9.423 17.659 1.00 194.66 ? 649 NAG A C3 1 HETATM 2796 C C4 . NAG B 2 . ? -17.093 -8.072 18.389 1.00 233.88 ? 649 NAG A C4 1 HETATM 2797 C C5 . NAG B 2 . ? -16.964 -6.889 17.424 1.00 243.60 ? 649 NAG A C5 1 HETATM 2798 C C6 . NAG B 2 . ? -16.621 -5.570 18.080 1.00 280.05 ? 649 NAG A C6 1 HETATM 2799 C C7 . NAG B 2 . ? -15.243 -11.876 16.179 1.00 184.23 ? 649 NAG A C7 1 HETATM 2800 C C8 . NAG B 2 . ? -15.389 -13.002 15.202 1.00 168.54 ? 649 NAG A C8 1 HETATM 2801 N N2 . NAG B 2 . ? -16.015 -10.805 15.955 1.00 169.77 ? 649 NAG A N2 1 HETATM 2802 O O3 . NAG B 2 . ? -17.127 -10.495 18.595 1.00 202.61 ? 649 NAG A O3 1 HETATM 2803 O O4 . NAG B 2 . ? -18.331 -7.917 19.078 1.00 257.85 ? 649 NAG A O4 1 HETATM 2804 O O5 . NAG B 2 . ? -15.952 -7.159 16.448 1.00 238.23 ? 649 NAG A O5 1 HETATM 2805 O O6 . NAG B 2 . ? -15.392 -5.615 18.793 1.00 286.11 ? 649 NAG A O6 1 HETATM 2806 O O7 . NAG B 2 . ? -14.458 -11.932 17.122 1.00 198.71 ? 649 NAG A O7 1 HETATM 2807 C C1 . NAG C 2 . ? -18.352 -7.821 20.500 1.00 252.59 ? 650 NAG A C1 1 HETATM 2808 C C2 . NAG C 2 . ? -19.807 -7.628 20.924 1.00 231.39 ? 650 NAG A C2 1 HETATM 2809 C C3 . NAG C 2 . ? -19.918 -7.545 22.446 1.00 271.78 ? 650 NAG A C3 1 HETATM 2810 C C4 . NAG C 2 . ? -18.541 -7.427 23.101 1.00 279.07 ? 650 NAG A C4 1 HETATM 2811 C C5 . NAG C 2 . ? -17.663 -6.407 22.370 1.00 233.83 ? 650 NAG A C5 1 HETATM 2812 C C6 . NAG C 2 . ? -16.236 -6.341 22.870 1.00 207.90 ? 650 NAG A C6 1 HETATM 2813 C C7 . NAG C 2 . ? -21.677 -6.316 19.976 1.00 180.48 ? 650 NAG A C7 1 HETATM 2814 C C8 . NAG C 2 . ? -22.069 -5.006 19.360 1.00 144.86 ? 650 NAG A C8 1 HETATM 2815 N N2 . NAG C 2 . ? -20.379 -6.442 20.304 1.00 213.66 ? 650 NAG A N2 1 HETATM 2816 O O3 . NAG C 2 . ? -20.595 -8.698 22.931 1.00 288.96 ? 650 NAG A O3 1 HETATM 2817 O O4 . NAG C 2 . ? -18.733 -7.010 24.451 1.00 290.13 ? 650 NAG A O4 1 HETATM 2818 O O5 . NAG C 2 . ? -17.591 -6.699 20.962 1.00 271.06 ? 650 NAG A O5 1 HETATM 2819 O O6 . NAG C 2 . ? -15.513 -7.536 22.599 1.00 187.15 ? 650 NAG A O6 1 HETATM 2820 O O7 . NAG C 2 . ? -22.493 -7.213 20.169 1.00 176.45 ? 650 NAG A O7 1 HETATM 2821 C C1 . BMA D 3 . ? -18.133 -7.748 25.509 1.00 290.83 ? 651 BMA A C1 1 HETATM 2822 C C2 . BMA D 3 . ? -17.631 -6.737 26.548 1.00 290.85 ? 651 BMA A C2 1 HETATM 2823 C C3 . BMA D 3 . ? -17.066 -7.447 27.777 1.00 291.44 ? 651 BMA A C3 1 HETATM 2824 C C4 . BMA D 3 . ? -18.050 -8.481 28.322 1.00 291.27 ? 651 BMA A C4 1 HETATM 2825 C C5 . BMA D 3 . ? -18.496 -9.419 27.202 1.00 291.28 ? 651 BMA A C5 1 HETATM 2826 C C6 . BMA D 3 . ? -19.541 -10.424 27.634 1.00 291.23 ? 651 BMA A C6 1 HETATM 2827 O O2 . BMA D 3 . ? -18.684 -5.853 26.919 1.00 290.17 ? 651 BMA A O2 1 HETATM 2828 O O3 . BMA D 3 . ? -16.730 -6.486 28.775 1.00 291.45 ? 651 BMA A O3 1 HETATM 2829 O O4 . BMA D 3 . ? -17.432 -9.238 29.358 1.00 291.92 ? 651 BMA A O4 1 HETATM 2830 O O5 . BMA D 3 . ? -19.057 -8.659 26.117 1.00 290.71 ? 651 BMA A O5 1 HETATM 2831 O O6 . BMA D 3 . ? -19.286 -11.733 27.118 1.00 291.90 ? 651 BMA A O6 1 HETATM 2832 C C1 . MAN E 4 . ? -15.420 -6.502 29.349 1.00 292.08 ? 652 MAN A C1 1 HETATM 2833 C C2 . MAN E 4 . ? -15.381 -5.526 30.534 1.00 291.81 ? 652 MAN A C2 1 HETATM 2834 C C3 . MAN E 4 . ? -15.316 -4.075 30.061 1.00 291.41 ? 652 MAN A C3 1 HETATM 2835 C C4 . MAN E 4 . ? -14.195 -3.865 29.046 1.00 291.65 ? 652 MAN A C4 1 HETATM 2836 C C5 . MAN E 4 . ? -14.334 -4.860 27.895 1.00 291.72 ? 652 MAN A C5 1 HETATM 2837 C C6 . MAN E 4 . ? -13.184 -4.810 26.914 1.00 287.48 ? 652 MAN A C6 1 HETATM 2838 O O2 . MAN E 4 . ? -14.281 -5.833 31.384 1.00 292.20 ? 652 MAN A O2 1 HETATM 2839 O O3 . MAN E 4 . ? -15.143 -3.200 31.170 1.00 291.37 ? 652 MAN A O3 1 HETATM 2840 O O4 . MAN E 4 . ? -14.250 -2.535 28.541 1.00 290.71 ? 652 MAN A O4 1 HETATM 2841 O O5 . MAN E 4 . ? -14.373 -6.204 28.409 1.00 292.42 ? 652 MAN A O5 1 HETATM 2842 O O6 . MAN E 4 . ? -13.199 -3.618 26.139 1.00 255.32 ? 652 MAN A O6 1 HETATM 2843 C C1 . MAN F 4 . ? -18.183 -12.402 27.687 1.00 292.85 ? 653 MAN A C1 1 HETATM 2844 C C2 . MAN F 4 . ? -17.817 -13.599 26.798 1.00 293.73 ? 653 MAN A C2 1 HETATM 2845 C C3 . MAN F 4 . ? -18.784 -14.765 26.997 1.00 293.98 ? 653 MAN A C3 1 HETATM 2846 C C4 . MAN F 4 . ? -18.959 -15.105 28.475 1.00 293.86 ? 653 MAN A C4 1 HETATM 2847 C C5 . MAN F 4 . ? -19.354 -13.855 29.259 1.00 292.99 ? 653 MAN A C5 1 HETATM 2848 C C6 . MAN F 4 . ? -19.428 -14.081 30.752 1.00 292.85 ? 653 MAN A C6 1 HETATM 2849 O O2 . MAN F 4 . ? -16.476 -14.004 27.058 1.00 294.74 ? 653 MAN A O2 1 HETATM 2850 O O3 . MAN F 4 . ? -18.331 -15.910 26.283 1.00 294.85 ? 653 MAN A O3 1 HETATM 2851 O O4 . MAN F 4 . ? -19.963 -16.103 28.621 1.00 294.04 ? 653 MAN A O4 1 HETATM 2852 O O5 . MAN F 4 . ? -18.380 -12.817 29.048 1.00 292.95 ? 653 MAN A O5 1 HETATM 2853 O O6 . MAN F 4 . ? -19.826 -12.902 31.439 1.00 292.14 ? 653 MAN A O6 1 HETATM 2854 C C1 . NAG G 2 . ? 14.535 -6.797 13.150 1.00 183.76 ? 678 NAG A C1 1 HETATM 2855 C C2 . NAG G 2 . ? 13.602 -7.139 11.993 1.00 210.74 ? 678 NAG A C2 1 HETATM 2856 C C3 . NAG G 2 . ? 14.068 -8.486 11.445 1.00 205.06 ? 678 NAG A C3 1 HETATM 2857 C C4 . NAG G 2 . ? 14.234 -9.535 12.552 1.00 157.49 ? 678 NAG A C4 1 HETATM 2858 C C5 . NAG G 2 . ? 13.860 -9.038 13.957 1.00 133.32 ? 678 NAG A C5 1 HETATM 2859 C C6 . NAG G 2 . ? 14.435 -9.892 15.066 1.00 115.51 ? 678 NAG A C6 1 HETATM 2860 C C7 . NAG G 2 . ? 11.352 -6.115 11.883 1.00 186.60 ? 678 NAG A C7 1 HETATM 2861 C C8 . NAG G 2 . ? 9.888 -6.341 12.114 1.00 149.16 ? 678 NAG A C8 1 HETATM 2862 N N2 . NAG G 2 . ? 12.163 -7.135 12.218 1.00 211.76 ? 678 NAG A N2 1 HETATM 2863 O O3 . NAG G 2 . ? 15.292 -8.314 10.737 1.00 236.87 ? 678 NAG A O3 1 HETATM 2864 O O4 . NAG G 2 . ? 13.418 -10.644 12.166 1.00 167.27 ? 678 NAG A O4 1 HETATM 2865 O O5 . NAG G 2 . ? 14.318 -7.698 14.232 1.00 150.58 ? 678 NAG A O5 1 HETATM 2866 O O6 . NAG G 2 . ? 15.858 -9.836 15.095 1.00 98.14 ? 678 NAG A O6 1 HETATM 2867 O O7 . NAG G 2 . ? 11.781 -5.063 11.415 1.00 158.70 ? 678 NAG A O7 1 HETATM 2868 C C1 . NAG H 2 . ? 13.725 -12.000 12.536 1.00 174.94 ? 679 NAG A C1 1 HETATM 2869 C C2 . NAG H 2 . ? 14.560 -12.697 11.456 1.00 170.01 ? 679 NAG A C2 1 HETATM 2870 C C3 . NAG H 2 . ? 13.759 -13.779 10.732 1.00 167.51 ? 679 NAG A C3 1 HETATM 2871 C C4 . NAG H 2 . ? 13.209 -14.803 11.721 1.00 189.93 ? 679 NAG A C4 1 HETATM 2872 C C5 . NAG H 2 . ? 12.531 -14.138 12.920 1.00 206.88 ? 679 NAG A C5 1 HETATM 2873 C C6 . NAG H 2 . ? 13.151 -14.479 14.258 1.00 217.84 ? 679 NAG A C6 1 HETATM 2874 C C7 . NAG H 2 . ? 14.910 -11.256 9.446 1.00 168.32 ? 679 NAG A C7 1 HETATM 2875 C C8 . NAG H 2 . ? 15.955 -10.731 8.508 1.00 154.26 ? 679 NAG A C8 1 HETATM 2876 N N2 . NAG H 2 . ? 15.375 -11.928 10.524 1.00 173.19 ? 679 NAG A N2 1 HETATM 2877 O O3 . NAG H 2 . ? 14.584 -14.440 9.778 1.00 161.89 ? 679 NAG A O3 1 HETATM 2878 O O4 . NAG H 2 . ? 12.237 -15.598 11.049 1.00 214.36 ? 679 NAG A O4 1 HETATM 2879 O O5 . NAG H 2 . ? 12.494 -12.703 12.785 1.00 207.67 ? 679 NAG A O5 1 HETATM 2880 O O6 . NAG H 2 . ? 12.376 -13.966 15.333 1.00 278.06 ? 679 NAG A O6 1 HETATM 2881 O O7 . NAG H 2 . ? 13.711 -11.070 9.249 1.00 185.73 ? 679 NAG A O7 1 HETATM 2882 C C1 . BMA I 3 . ? 12.481 -16.980 10.848 1.00 232.49 ? 680 BMA A C1 1 HETATM 2883 C C2 . BMA I 3 . ? 11.144 -17.630 10.488 1.00 225.33 ? 680 BMA A C2 1 HETATM 2884 C C3 . BMA I 3 . ? 11.334 -19.109 10.158 1.00 233.57 ? 680 BMA A C3 1 HETATM 2885 C C4 . BMA I 3 . ? 12.428 -19.313 9.112 1.00 245.02 ? 680 BMA A C4 1 HETATM 2886 C C5 . BMA I 3 . ? 13.708 -18.585 9.525 1.00 234.11 ? 680 BMA A C5 1 HETATM 2887 C C6 . BMA I 3 . ? 14.793 -18.616 8.471 1.00 217.51 ? 680 BMA A C6 1 HETATM 2888 O O2 . BMA I 3 . ? 10.542 -16.944 9.394 1.00 196.99 ? 680 BMA A O2 1 HETATM 2889 O O3 . BMA I 3 . ? 10.105 -19.670 9.704 1.00 229.17 ? 680 BMA A O3 1 HETATM 2890 O O4 . BMA I 3 . ? 12.692 -20.704 8.966 1.00 286.47 ? 680 BMA A O4 1 HETATM 2891 O O5 . BMA I 3 . ? 13.426 -17.200 9.794 1.00 238.84 ? 680 BMA A O5 1 HETATM 2892 O O6 . BMA I 3 . ? 14.448 -17.854 7.320 1.00 204.72 ? 680 BMA A O6 1 HETATM 2893 C C1 . MAN J 4 . ? 9.398 -20.587 10.539 1.00 257.12 ? 681 MAN A C1 1 HETATM 2894 C C2 . MAN J 4 . ? 7.915 -20.518 10.152 1.00 260.80 ? 681 MAN A C2 1 HETATM 2895 C C3 . MAN J 4 . ? 7.020 -20.544 11.389 1.00 255.23 ? 681 MAN A C3 1 HETATM 2896 C C4 . MAN J 4 . ? 7.528 -21.551 12.416 1.00 254.92 ? 681 MAN A C4 1 HETATM 2897 C C5 . MAN J 4 . ? 8.938 -21.184 12.877 1.00 233.54 ? 681 MAN A C5 1 HETATM 2898 C C6 . MAN J 4 . ? 9.848 -22.378 13.066 1.00 233.26 ? 681 MAN A C6 1 HETATM 2899 O O2 . MAN J 4 . ? 7.596 -21.595 9.277 1.00 275.95 ? 681 MAN A O2 1 HETATM 2900 O O3 . MAN J 4 . ? 5.676 -20.841 11.027 1.00 218.50 ? 681 MAN A O3 1 HETATM 2901 O O4 . MAN J 4 . ? 6.661 -21.575 13.544 1.00 251.73 ? 681 MAN A O4 1 HETATM 2902 O O5 . MAN J 4 . ? 9.569 -20.292 11.937 1.00 231.34 ? 681 MAN A O5 1 HETATM 2903 O O6 . MAN J 4 . ? 11.119 -21.989 13.568 1.00 218.91 ? 681 MAN A O6 1 HETATM 2904 CA CA . CA K 5 . ? 4.530 1.744 6.505 1.00 56.42 2 701 CA A CA 1 HETATM 2905 CA CA . CA L 5 . ? -36.778 3.598 12.823 1.00 271.82 2 702 CA A CA 1 HETATM 2906 CA CA . CA M 5 . ? 23.339 4.149 27.434 1.00 167.08 2 703 CA A CA 1 HETATM 2907 CA CA . CA N 5 . ? 33.528 7.092 11.810 1.00 149.98 2 706 CA A CA 1 HETATM 2908 CA CA . CA O 5 . ? -17.699 12.844 14.373 1.00 161.26 2 707 CA A CA 1 HETATM 2909 CA CA . CA P 5 . ? 22.051 13.052 31.694 1.00 195.91 2 708 CA A CA 1 HETATM 2910 O O . HOH Q 6 . ? 2.931 1.028 7.992 1.00 99.32 ? 2001 HOH A O 1 HETATM 2911 O O . HOH Q 6 . ? -37.953 4.444 10.677 1.00 163.75 ? 2002 HOH A O 1 HETATM 2912 O O . HOH Q 6 . ? -36.812 1.385 11.375 1.00 124.65 ? 2003 HOH A O 1 HETATM 2913 O O . HOH Q 6 . ? 24.017 5.986 26.395 1.00 57.78 ? 2004 HOH A O 1 HETATM 2914 O O . HOH Q 6 . ? 24.065 3.591 25.232 1.00 43.66 ? 2005 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 . VAL A 3 ? 2.4837 2.6818 2.4959 -0.2501 0.1833 -0.0108 22 VAL A N 2 C CA . VAL A 3 ? 2.4393 2.6103 2.4340 -0.2309 0.1647 -0.0298 22 VAL A CA 3 C C . VAL A 3 ? 2.3993 2.5813 2.3681 -0.1874 0.1642 -0.0037 22 VAL A C 4 O O . VAL A 3 ? 2.2581 2.5078 2.2374 -0.1765 0.1501 -0.0026 22 VAL A O 5 C CB . VAL A 3 ? 2.1616 2.3811 2.1788 -0.2409 0.1330 -0.0690 22 VAL A CB 6 C CG1 . VAL A 3 ? 2.1432 2.3245 2.1283 -0.2211 0.1190 -0.0859 22 VAL A CG1 7 C CG2 . VAL A 3 ? 2.2085 2.4424 2.2662 -0.2820 0.1281 -0.0981 22 VAL A CG2 8 N N . GLU A 4 ? 2.5269 2.6452 2.4665 -0.1628 0.1797 0.0142 23 GLU A N 9 C CA . GLU A 4 ? 2.4840 2.6240 2.4113 -0.1198 0.1790 0.0364 23 GLU A CA 10 C C . GLU A 4 ? 2.4206 2.5467 2.3400 -0.1033 0.1721 0.0150 23 GLU A C 11 O O . GLU A 4 ? 2.5200 2.5767 2.4200 -0.1095 0.1791 -0.0027 23 GLU A O 12 C CB . GLU A 4 ? 2.5524 2.6421 2.4544 -0.0921 0.2019 0.0756 23 GLU A CB 13 C CG . GLU A 4 ? 2.6311 2.7459 2.5268 -0.0949 0.2099 0.1070 23 GLU A CG 14 C CD . GLU A 4 ? 2.8768 2.9203 2.7347 -0.0673 0.2353 0.1493 23 GLU A CD 15 O OE1 . GLU A 4 ? 2.9562 2.9758 2.8009 -0.0242 0.2373 0.1633 23 GLU A OE1 16 O OE2 . GLU A 4 ? 3.0097 3.0206 2.8505 -0.0864 0.2559 0.1703 23 GLU A OE2 17 N N . LEU A 5 ? 2.3397 2.5292 2.2716 -0.0847 0.1611 0.0149 24 LEU A N 18 C CA . LEU A 5 ? 2.2837 2.4674 2.2078 -0.0701 0.1611 -0.0020 24 LEU A CA 19 C C . LEU A 5 ? 2.2672 2.5049 2.2104 -0.0389 0.1661 0.0130 24 LEU A C 20 O O . LEU A 5 ? 2.1455 2.4536 2.1136 -0.0451 0.1538 0.0117 24 LEU A O 21 C CB . LEU A 5 ? 1.9847 2.1887 1.9086 -0.0935 0.1425 -0.0308 24 LEU A CB 22 C CG . LEU A 5 ? 2.0321 2.1773 1.9258 -0.1074 0.1364 -0.0598 24 LEU A CG 23 C CD1 . LEU A 5 ? 1.8883 2.0632 1.7782 -0.1177 0.1154 -0.0802 24 LEU A CD1 24 C CD2 . LEU A 5 ? 2.1768 2.2615 2.0350 -0.0848 0.1543 -0.0647 24 LEU A CD2 25 N N . ASN A 6 ? 2.4348 2.6415 2.3704 -0.0068 0.1849 0.0219 25 ASN A N 26 C CA . ASN A 6 ? 2.4344 2.7024 2.4007 0.0229 0.1915 0.0314 25 ASN A CA 27 C C . ASN A 6 ? 2.4088 2.6474 2.3624 0.0322 0.2108 0.0129 25 ASN A C 28 O O . ASN A 6 ? 2.5510 2.7139 2.4718 0.0471 0.2281 0.0087 25 ASN A O 29 C CB . ASN A 6 ? 2.4948 2.7735 2.4721 0.0625 0.1975 0.0627 25 ASN A CB 30 C CG . ASN A 6 ? 2.6705 2.9028 2.6402 0.1026 0.2225 0.0680 25 ASN A CG 31 O OD1 . ASN A 6 ? 2.6848 2.9738 2.6897 0.1306 0.2306 0.0693 25 ASN A OD1 32 N ND2 . ASN A 6 ? 2.8238 2.9517 2.7503 0.1026 0.2375 0.0651 25 ASN A ND2 33 N N . ASN A 7 ? 2.0267 2.3164 1.9995 0.0211 0.2110 0.0006 26 ASN A N 34 C CA . ASN A 7 ? 1.9706 2.2360 1.9252 0.0264 0.2342 -0.0147 26 ASN A CA 35 C C . ASN A 7 ? 1.7770 2.1087 1.7634 0.0085 0.2357 -0.0209 26 ASN A C 36 O O . ASN A 7 ? 1.7216 2.1213 1.7497 -0.0028 0.2180 -0.0154 26 ASN A O 37 C CB . ASN A 7 ? 2.0317 2.2097 1.9214 0.0114 0.2320 -0.0348 26 ASN A CB 38 C CG . ASN A 7 ? 2.0131 2.2008 1.8924 -0.0212 0.2062 -0.0460 26 ASN A CG 39 O OD1 . ASN A 7 ? 2.0432 2.2325 1.9054 -0.0298 0.2095 -0.0554 26 ASN A OD1 40 N ND2 . ASN A 7 ? 1.9978 2.1951 1.8897 -0.0375 0.1836 -0.0427 26 ASN A ND2 41 N N . MET A 8 ? 1.2152 1.5189 1.1745 0.0043 0.2586 -0.0332 27 MET A N 42 C CA . MET A 8 ? 1.1739 1.5195 1.1563 -0.0133 0.2734 -0.0380 27 MET A CA 43 C C . MET A 8 ? 1.1412 1.4502 1.0809 -0.0410 0.2607 -0.0476 27 MET A C 44 O O . MET A 8 ? 1.1173 1.4545 1.0773 -0.0600 0.2703 -0.0498 27 MET A O 45 C CB . MET A 8 ? 1.2658 1.5984 1.2413 0.0039 0.3176 -0.0402 27 MET A CB 46 C CG . MET A 8 ? 1.3118 1.6956 1.3431 0.0371 0.3353 -0.0317 27 MET A CG 47 S SD . MET A 8 ? 1.3657 1.7383 1.3919 0.0584 0.3941 -0.0372 27 MET A SD 48 C CE . MET A 8 ? 1.2944 1.7567 1.3918 0.0246 0.4117 -0.0398 27 MET A CE 49 N N . PHE A 9 ? 1.1611 1.4054 1.0427 -0.0420 0.2407 -0.0547 28 PHE A N 50 C CA . PHE A 9 ? 1.1586 1.3659 0.9946 -0.0579 0.2234 -0.0638 28 PHE A CA 51 C C . PHE A 9 ? 1.1622 1.3360 0.9700 -0.0602 0.1906 -0.0735 28 PHE A C 52 O O . PHE A 9 ? 1.1945 1.3514 1.0029 -0.0517 0.1894 -0.0743 28 PHE A O 53 C CB . PHE A 9 ? 1.2692 1.4175 1.0400 -0.0502 0.2500 -0.0670 28 PHE A CB 54 C CG . PHE A 9 ? 1.3810 1.4642 1.0889 -0.0307 0.2552 -0.0767 28 PHE A CG 55 C CD1 . PHE A 9 ? 1.4407 1.5219 1.1599 -0.0111 0.2845 -0.0748 28 PHE A CD1 56 C CD2 . PHE A 9 ? 1.4464 1.4726 1.0850 -0.0300 0.2290 -0.0912 28 PHE A CD2 57 C CE1 . PHE A 9 ? 1.5658 1.5782 1.2221 0.0066 0.2909 -0.0886 28 PHE A CE1 58 C CE2 . PHE A 9 ? 1.5727 1.5385 1.1507 -0.0153 0.2309 -0.1069 28 PHE A CE2 59 C CZ . PHE A 9 ? 1.6359 1.5895 1.2200 0.0018 0.2636 -0.1063 28 PHE A CZ 60 N N . GLY A 10 ? 1.1527 1.3125 0.9350 -0.0708 0.1666 -0.0823 29 GLY A N 61 C CA . GLY A 10 ? 1.1682 1.3089 0.9345 -0.0760 0.1353 -0.0963 29 GLY A CA 62 C C . GLY A 10 ? 1.1528 1.3020 0.9108 -0.0833 0.1074 -0.1047 29 GLY A C 63 O O . GLY A 10 ? 1.1225 1.2889 0.8897 -0.0855 0.1123 -0.0976 29 GLY A O 64 N N . GLN A 11 ? 1.1947 1.3319 0.9386 -0.0868 0.0784 -0.1222 30 GLN A N 65 C CA . GLN A 11 ? 1.1990 1.3527 0.9420 -0.0880 0.0468 -0.1337 30 GLN A CA 66 C C . GLN A 11 ? 1.1488 1.3486 0.9500 -0.1070 0.0285 -0.1430 30 GLN A C 67 O O . GLN A 11 ? 1.1716 1.3616 0.9848 -0.1184 0.0323 -0.1481 30 GLN A O 68 C CB . GLN A 11 ? 1.3293 1.4358 1.0018 -0.0726 0.0257 -0.1507 30 GLN A CB 69 C CG . GLN A 11 ? 1.3717 1.4973 1.0385 -0.0629 -0.0103 -0.1612 30 GLN A CG 70 C CD . GLN A 11 ? 1.5295 1.6100 1.1153 -0.0407 -0.0344 -0.1756 30 GLN A CD 71 O OE1 . GLN A 11 ? 1.6390 1.6671 1.1633 -0.0334 -0.0207 -0.1783 30 GLN A OE1 72 N NE2 . GLN A 11 ? 1.5649 1.6664 1.1450 -0.0253 -0.0718 -0.1860 30 GLN A NE2 73 N N . ILE A 12 ? 1.1052 1.3498 0.9407 -0.1103 0.0134 -0.1451 31 ILE A N 74 C CA . ILE A 12 ? 1.0721 1.3672 0.9647 -0.1286 0.0010 -0.1540 31 ILE A CA 75 C C . ILE A 12 ? 1.1039 1.4272 1.0051 -0.1205 -0.0298 -0.1721 31 ILE A C 76 O O . ILE A 12 ? 1.1134 1.4314 0.9945 -0.1011 -0.0340 -0.1675 31 ILE A O 77 C CB . ILE A 12 ? 0.9887 1.3251 0.9257 -0.1392 0.0211 -0.1365 31 ILE A CB 78 C CG1 . ILE A 12 ? 0.9797 1.2968 0.9144 -0.1423 0.0456 -0.1189 31 ILE A CG1 79 C CG2 . ILE A 12 ? 0.9839 1.3734 0.9722 -0.1555 0.0126 -0.1450 31 ILE A CG2 80 C CD1 . ILE A 12 ? 0.9261 1.2826 0.8887 -0.1436 0.0612 -0.1002 31 ILE A CD1 81 N N . GLN A 13 ? 1.1410 1.4941 1.0756 -0.1349 -0.0501 -0.1933 32 GLN A N 82 C CA . GLN A 13 ? 1.1822 1.5809 1.1417 -0.1257 -0.0827 -0.2143 32 GLN A CA 83 C C . GLN A 13 ? 1.1531 1.6192 1.1925 -0.1523 -0.0792 -0.2239 32 GLN A C 84 O O . GLN A 13 ? 1.1391 1.6003 1.2003 -0.1801 -0.0570 -0.2178 32 GLN A O 85 C CB . GLN A 13 ? 1.2987 1.6792 1.2236 -0.1182 -0.1168 -0.2397 32 GLN A CB 86 C CG . GLN A 13 ? 1.3689 1.6747 1.2009 -0.0927 -0.1167 -0.2314 32 GLN A CG 87 C CD . GLN A 13 ? 1.5063 1.7928 1.2968 -0.0890 -0.1498 -0.2605 32 GLN A CD 88 O OE1 . GLN A 13 ? 1.5522 1.8808 1.3902 -0.1114 -0.1732 -0.2902 32 GLN A OE1 89 N NE2 . GLN A 13 ? 1.6043 1.8265 1.3031 -0.0626 -0.1510 -0.2546 32 GLN A NE2 90 N N . SER A 14 ? 1.1687 1.6946 1.2497 -0.1416 -0.0986 -0.2381 33 SER A N 91 C CA . SER A 14 ? 1.1648 1.7646 1.3268 -0.1658 -0.0935 -0.2511 33 SER A CA 92 C C . SER A 14 ? 1.2458 1.8657 1.4399 -0.1914 -0.1142 -0.2804 33 SER A C 93 O O . SER A 14 ? 1.3142 1.9093 1.4686 -0.1768 -0.1462 -0.2969 33 SER A O 94 C CB . SER A 14 ? 1.1790 1.8388 1.3771 -0.1399 -0.1081 -0.2611 33 SER A CB 95 O OG . SER A 14 ? 1.2541 1.9089 1.4234 -0.1054 -0.1482 -0.2754 33 SER A OG 96 N N . PRO A 15 ? 1.2600 1.9216 1.5218 -0.2311 -0.0949 -0.2884 34 PRO A N 97 C CA . PRO A 15 ? 1.3600 2.0425 1.6631 -0.2644 -0.1119 -0.3217 34 PRO A CA 98 C C . PRO A 15 ? 1.4267 2.1761 1.7591 -0.2431 -0.1634 -0.3574 34 PRO A C 99 O O . PRO A 15 ? 1.4084 2.2248 1.7815 -0.2192 -0.1721 -0.3596 34 PRO A O 100 C CB . PRO A 15 ? 1.3740 2.1019 1.7534 -0.3068 -0.0750 -0.3194 34 PRO A CB 101 C CG . PRO A 15 ? 1.2949 1.9883 1.6398 -0.2977 -0.0357 -0.2782 34 PRO A CG 102 C CD . PRO A 15 ? 1.2158 1.8966 1.5097 -0.2502 -0.0526 -0.2661 34 PRO A CD 103 N N . GLY A 16 ? 1.5178 2.2461 1.8221 -0.2458 -0.1990 -0.3854 35 GLY A N 104 C CA . GLY A 16 ? 1.6140 2.4084 1.9387 -0.2219 -0.2560 -0.4214 35 GLY A CA 105 C C . GLY A 16 ? 1.6399 2.3904 1.8699 -0.1616 -0.2875 -0.4090 35 GLY A C 106 O O . GLY A 16 ? 1.7565 2.5393 1.9749 -0.1384 -0.3396 -0.4377 35 GLY A O 107 N N . TYR A 17 ? 1.5537 2.2317 1.7152 -0.1370 -0.2566 -0.3675 36 TYR A N 108 C CA . TYR A 17 ? 1.5960 2.2173 1.6627 -0.0841 -0.2742 -0.3496 36 TYR A CA 109 C C . TYR A 17 ? 1.7364 2.3191 1.7290 -0.0716 -0.3134 -0.3717 36 TYR A C 110 O O . TYR A 17 ? 1.7583 2.3050 1.7371 -0.1060 -0.3042 -0.3854 36 TYR A O 111 C CB . TYR A 17 ? 1.4970 2.0373 1.5055 -0.0786 -0.2274 -0.3077 36 TYR A CB 112 C CG . TYR A 17 ? 1.5529 2.0333 1.4732 -0.0300 -0.2341 -0.2860 36 TYR A CG 113 C CD1 . TYR A 17 ? 1.6446 2.0493 1.4674 -0.0139 -0.2413 -0.2817 36 TYR A CD1 114 C CD2 . TYR A 17 ? 1.5402 2.0318 1.4696 -0.0006 -0.2285 -0.2697 36 TYR A CD2 115 C CE1 . TYR A 17 ? 1.7277 2.0703 1.4640 0.0292 -0.2415 -0.2585 36 TYR A CE1 116 C CE2 . TYR A 17 ? 1.6214 2.0446 1.4668 0.0414 -0.2292 -0.2477 36 TYR A CE2 117 C CZ . TYR A 17 ? 1.7212 2.0697 1.4696 0.0553 -0.2345 -0.2402 36 TYR A CZ 118 O OH . TYR A 17 ? 1.8267 2.0999 1.4866 0.0945 -0.2284 -0.2148 36 TYR A OH 119 N N . PRO A 18 ? 1.8592 2.4462 1.7996 -0.0205 -0.3572 -0.3763 37 PRO A N 120 C CA . PRO A 18 ? 1.8828 2.4952 1.8244 0.0299 -0.3707 -0.3597 37 PRO A CA 121 C C . PRO A 18 ? 1.9133 2.6496 1.9659 0.0358 -0.4029 -0.3882 37 PRO A C 122 O O . PRO A 18 ? 1.9652 2.7245 2.0214 0.0840 -0.4167 -0.3776 37 PRO A O 123 C CB . PRO A 18 ? 2.0484 2.5900 1.8649 0.0813 -0.4005 -0.3499 37 PRO A CB 124 C CG . PRO A 18 ? 2.1556 2.7042 1.9490 0.0614 -0.4354 -0.3876 37 PRO A CG 125 C CD . PRO A 18 ? 2.0250 2.5767 1.8826 -0.0056 -0.3974 -0.3991 37 PRO A CD 126 N N . ASP A 19 ? 1.8979 2.7117 2.0438 -0.0132 -0.4106 -0.4243 38 ASP A N 127 C CA . ASP A 19 ? 1.9259 2.8710 2.1947 -0.0157 -0.4342 -0.4547 38 ASP A CA 128 C C . ASP A 19 ? 1.7901 2.7647 2.1332 -0.0348 -0.3809 -0.4350 38 ASP A C 129 O O . ASP A 19 ? 1.6741 2.5733 1.9793 -0.0561 -0.3309 -0.4036 38 ASP A O 130 C CB . ASP A 19 ? 2.1572 3.1733 2.4998 -0.0673 -0.4603 -0.5048 38 ASP A CB 131 C CG . ASP A 19 ? 2.8541 3.5960 3.0366 -0.1035 -0.4872 -0.3670 38 ASP A CG 132 O OD1 . ASP A 19 ? 3.1320 3.6959 3.2268 -0.1258 -0.4909 -0.2226 38 ASP A OD1 133 O OD2 . ASP A 19 ? 2.9205 3.5930 3.0544 -0.1396 -0.4848 -0.3738 38 ASP A OD2 134 N N . SER A 20 ? 1.8200 2.9089 2.2679 -0.0245 -0.3923 -0.4549 39 SER A N 135 C CA . SER A 20 ? 1.7246 2.8524 2.2436 -0.0392 -0.3427 -0.4418 39 SER A CA 136 C C . SER A 20 ? 1.6307 2.7451 2.1849 -0.1112 -0.2927 -0.4382 39 SER A C 137 O O . SER A 20 ? 1.6731 2.8098 2.2632 -0.1562 -0.3032 -0.4650 39 SER A O 138 C CB . SER A 20 ? 2.0126 3.2780 2.6475 -0.0184 -0.3645 -0.4717 39 SER A CB 139 O OG . SER A 20 ? 2.5192 3.6028 3.1558 -0.0926 -0.3675 -0.3464 39 SER A OG 140 N N . TYR A 21 ? 1.5282 2.5994 2.0653 -0.1208 -0.2394 -0.4056 40 TYR A N 141 C CA . TYR A 21 ? 1.4657 2.5145 2.0216 -0.1797 -0.1901 -0.3940 40 TYR A CA 142 C C . TYR A 21 ? 1.5100 2.6639 2.1861 -0.2210 -0.1692 -0.4177 40 TYR A C 143 O O . TYR A 21 ? 1.5495 2.7967 2.2962 -0.1970 -0.1780 -0.4344 40 TYR A O 144 C CB . TYR A 21 ? 1.3640 2.3378 1.8566 -0.1738 -0.1454 -0.3527 40 TYR A CB 145 C CG . TYR A 21 ? 1.3526 2.3617 1.8626 -0.1400 -0.1308 -0.3450 40 TYR A CG 146 C CD1 . TYR A 21 ? 1.3665 2.4501 1.9530 -0.1598 -0.0970 -0.3512 40 TYR A CD1 147 C CD2 . TYR A 21 ? 1.3462 2.3024 1.7886 -0.0909 -0.1434 -0.3304 40 TYR A CD2 148 C CE1 . TYR A 21 ? 1.3758 2.4861 1.9719 -0.1272 -0.0809 -0.3480 40 TYR A CE1 149 C CE2 . TYR A 21 ? 1.3567 2.3318 1.8098 -0.0613 -0.1270 -0.3264 40 TYR A CE2 150 C CZ . TYR A 21 ? 1.3721 2.4255 1.9013 -0.0780 -0.0972 -0.3370 40 TYR A CZ 151 O OH . TYR A 21 ? 1.4082 2.4765 1.9430 -0.0468 -0.0796 -0.3375 40 TYR A OH 152 N N . PRO A 22 ? 1.5218 2.6578 2.2218 -0.2819 -0.1374 -0.4183 41 PRO A N 153 C CA . PRO A 22 ? 1.5866 2.8142 2.3993 -0.3284 -0.1075 -0.4378 41 PRO A CA 154 C C . PRO A 22 ? 1.5480 2.7902 2.3714 -0.3260 -0.0525 -0.4096 41 PRO A C 155 O O . PRO A 22 ? 1.4664 2.6318 2.2045 -0.3024 -0.0344 -0.3742 41 PRO A O 156 C CB . PRO A 22 ? 1.6333 2.8020 2.4411 -0.3905 -0.0871 -0.4403 41 PRO A CB 157 C CG . PRO A 22 ? 1.5562 2.5954 2.2423 -0.3728 -0.0804 -0.4039 41 PRO A CG 158 C CD . PRO A 22 ? 1.4997 2.5284 2.1264 -0.3097 -0.1264 -0.4031 41 PRO A CD 159 N N . SER A 23 ? 1.6484 2.9934 2.5774 -0.3516 -0.0255 -0.4282 42 SER A N 160 C CA . SER A 23 ? 1.6458 3.0114 2.5853 -0.3525 0.0311 -0.4059 42 SER A CA 161 C C . SER A 23 ? 1.6456 2.9414 2.5531 -0.4063 0.0876 -0.3756 42 SER A C 162 O O . SER A 23 ? 1.7296 2.9818 2.6375 -0.4483 0.0854 -0.3804 42 SER A O 163 C CB . SER A 23 ? 2.3409 3.5787 3.3235 -0.2965 0.0079 -0.2749 42 SER A CB 164 O OG . SER A 23 ? 2.5664 3.6414 3.5645 -0.2962 -0.0203 -0.1478 42 SER A OG 165 N N . ASP A 24 ? 1.6513 2.9311 2.5243 -0.4019 0.1374 -0.3448 43 ASP A N 166 C CA . ASP A 24 ? 1.7081 2.9193 2.5359 -0.4410 0.1932 -0.3083 43 ASP A CA 167 C C . ASP A 24 ? 1.6640 2.7547 2.4053 -0.4488 0.1794 -0.2847 43 ASP A C 168 O O . ASP A 24 ? 1.7577 2.8009 2.5021 -0.4949 0.2053 -0.2760 43 ASP A O 169 C CB . ASP A 24 ? 2.4058 3.5152 3.2942 -0.4256 0.2002 -0.2101 43 ASP A CB 170 C CG . ASP A 24 ? 2.5480 3.5372 3.3831 -0.4218 0.2412 -0.1296 43 ASP A CG 171 O OD1 . ASP A 24 ? 2.3095 3.4451 3.0834 -0.5039 0.3228 -0.2356 43 ASP A OD1 172 O OD2 . ASP A 24 ? 2.7721 3.6123 3.6249 -0.3761 0.2042 -0.0068 43 ASP A OD2 173 N N . SER A 25 ? 1.5417 2.5813 2.2085 -0.4031 0.1412 -0.2758 44 SER A N 174 C CA . SER A 25 ? 1.5008 2.4342 2.0869 -0.4020 0.1292 -0.2546 44 SER A CA 175 C C . SER A 25 ? 1.4253 2.3030 1.9224 -0.3682 0.1398 -0.2175 44 SER A C 176 O O . SER A 25 ? 1.3724 2.2847 1.8602 -0.3344 0.1318 -0.2199 44 SER A O 177 C CB . SER A 25 ? 1.4530 2.3755 2.0346 -0.3849 0.0729 -0.2823 44 SER A CB 178 O OG . SER A 25 ? 1.3688 2.3040 1.9198 -0.3329 0.0397 -0.2854 44 SER A OG 179 N N . GLU A 26 ? 1.4393 2.2328 1.8744 -0.3774 0.1584 -0.1856 45 GLU A N 180 C CA . GLU A 26 ? 1.3851 2.1327 1.7416 -0.3476 0.1652 -0.1520 45 GLU A CA 181 C C . GLU A 26 ? 1.3707 2.0298 1.6715 -0.3438 0.1574 -0.1332 45 GLU A C 182 O O . GLU A 26 ? 1.4719 2.0804 1.7658 -0.3699 0.1821 -0.1180 45 GLU A O 183 C CB . GLU A 26 ? 1.4745 2.2341 1.8140 -0.3559 0.2108 -0.1243 45 GLU A CB 184 C CG . GLU A 26 ? 1.4296 2.1666 1.6954 -0.3221 0.2095 -0.0985 45 GLU A CG 185 C CD . GLU A 26 ? 1.5435 2.2933 1.7767 -0.3242 0.2494 -0.0723 45 GLU A CD 186 O OE1 . GLU A 26 ? 1.6532 2.4380 1.9250 -0.3505 0.2842 -0.0750 45 GLU A OE1 187 O OE2 . GLU A 26 ? 1.5382 2.2669 1.7066 -0.2992 0.2460 -0.0502 45 GLU A OE2 188 N N . VAL A 27 ? 1.2652 1.9023 1.5276 -0.3112 0.1263 -0.1353 46 VAL A N 189 C CA . VAL A 27 ? 1.2495 1.8107 1.4620 -0.3013 0.1191 -0.1211 46 VAL A CA 190 C C . VAL A 27 ? 1.1775 1.7263 1.3392 -0.2689 0.1179 -0.0973 46 VAL A C 191 O O . VAL A 27 ? 1.1031 1.6885 1.2647 -0.2499 0.1024 -0.1075 46 VAL A O 192 C CB . VAL A 27 ? 1.2213 1.7636 1.4370 -0.2978 0.0847 -0.1507 46 VAL A CB 193 C CG1 . VAL A 27 ? 1.2431 1.7027 1.4093 -0.2920 0.0867 -0.1383 46 VAL A CG1 194 C CG2 . VAL A 27 ? 1.2936 1.8737 1.5719 -0.3291 0.0758 -0.1842 46 VAL A CG2 195 N N . THR A 28 ? 1.2188 1.7159 1.3406 -0.2623 0.1337 -0.0676 47 THR A N 196 C CA . THR A 28 ? 1.1668 1.6606 1.2495 -0.2327 0.1301 -0.0471 47 THR A CA 197 C C . THR A 28 ? 1.1480 1.5865 1.2049 -0.2170 0.1220 -0.0427 47 THR A C 198 O O . THR A 28 ? 1.2323 1.6146 1.2802 -0.2252 0.1338 -0.0359 47 THR A O 199 C CB . THR A 28 ? 1.2529 1.7523 1.3100 -0.2281 0.1541 -0.0140 47 THR A CB 200 O OG1 . THR A 28 ? 1.2789 1.8327 1.3544 -0.2403 0.1643 -0.0216 47 THR A OG1 201 C CG2 . THR A 28 ? 1.2145 1.7230 1.2378 -0.1969 0.1443 0.0034 47 THR A CG2 202 N N . TRP A 29 ? 1.0586 1.5097 1.1036 -0.1955 0.1062 -0.0475 48 TRP A N 203 C CA . TRP A 29 ? 1.0469 1.4559 1.0688 -0.1775 0.1040 -0.0426 48 TRP A CA 204 C C . TRP A 29 ? 1.0274 1.4620 1.0389 -0.1553 0.1077 -0.0216 48 TRP A C 205 O O . TRP A 29 ? 0.9686 1.4519 0.9888 -0.1526 0.0985 -0.0287 48 TRP A O 206 C CB . TRP A 29 ? 0.9838 1.3854 1.0018 -0.1734 0.0861 -0.0674 48 TRP A CB 207 C CG . TRP A 29 ? 1.0178 1.4016 1.0435 -0.1894 0.0738 -0.0918 48 TRP A CG 208 C CD1 . TRP A 29 ? 1.0850 1.4155 1.0946 -0.1949 0.0730 -0.1019 48 TRP A CD1 209 C CD2 . TRP A 29 ? 0.9999 1.4251 1.0531 -0.1996 0.0573 -0.1135 48 TRP A CD2 210 N NE1 . TRP A 29 ? 1.1119 1.4539 1.1387 -0.2109 0.0533 -0.1304 48 TRP A NE1 211 C CE2 . TRP A 29 ? 1.0595 1.4632 1.1169 -0.2118 0.0432 -0.1365 48 TRP A CE2 212 C CE3 . TRP A 29 ? 0.9597 1.4396 1.0354 -0.1973 0.0527 -0.1184 48 TRP A CE3 213 C CZ2 . TRP A 29 ? 1.0714 1.5173 1.1611 -0.2192 0.0213 -0.1626 48 TRP A CZ2 214 C CZ3 . TRP A 29 ? 0.9741 1.4875 1.0796 -0.2023 0.0359 -0.1424 48 TRP A CZ3 215 C CH2 . TRP A 29 ? 1.0247 1.5266 1.1404 -0.2120 0.0189 -0.1634 48 TRP A CH2 216 N N . ASN A 30 ? 1.0953 1.4982 1.0905 -0.1383 0.1201 0.0021 49 ASN A N 217 C CA . ASN A 30 ? 1.0945 1.5311 1.0863 -0.1122 0.1193 0.0211 49 ASN A CA 218 C C . ASN A 30 ? 1.0577 1.4805 1.0524 -0.0950 0.1197 0.0151 49 ASN A C 219 O O . ASN A 30 ? 1.1098 1.4728 1.0900 -0.0880 0.1307 0.0166 49 ASN A O 220 C CB . ASN A 30 ? 1.2236 1.6414 1.1944 -0.0956 0.1327 0.0554 49 ASN A CB 221 C CG . ASN A 30 ? 1.2762 1.7309 1.2374 -0.1038 0.1339 0.0670 49 ASN A CG 222 O OD1 . ASN A 30 ? 1.2181 1.7056 1.1927 -0.1269 0.1289 0.0468 49 ASN A OD1 223 N ND2 . ASN A 30 ? 1.4079 1.8582 1.3411 -0.0807 0.1415 0.1005 49 ASN A ND2 224 N N . ILE A 31 ? 0.9820 1.4571 0.9950 -0.0911 0.1108 0.0053 50 ILE A N 225 C CA . ILE A 31 ? 0.9566 1.4282 0.9781 -0.0784 0.1174 -0.0008 50 ILE A CA 226 C C . ILE A 31 ? 0.9753 1.5045 1.0215 -0.0546 0.1172 0.0135 50 ILE A C 227 O O . ILE A 31 ? 0.9482 1.5439 1.0149 -0.0602 0.1038 0.0085 50 ILE A O 228 C CB . ILE A 31 ? 0.8836 1.3591 0.9090 -0.0962 0.1136 -0.0255 50 ILE A CB 229 C CG1 . ILE A 31 ? 0.8797 1.3122 0.8834 -0.1133 0.1060 -0.0404 50 ILE A CG1 230 C CG2 . ILE A 31 ? 0.8878 1.3486 0.9146 -0.0849 0.1296 -0.0287 50 ILE A CG2 231 C CD1 . ILE A 31 ? 0.8384 1.2779 0.8413 -0.1252 0.0981 -0.0595 50 ILE A CD1 232 N N . THR A 32 ? 1.0397 1.5460 1.0854 -0.0266 0.1307 0.0280 51 THR A N 233 C CA . THR A 32 ? 1.0747 1.6433 1.1522 0.0036 0.1294 0.0409 51 THR A CA 234 C C . THR A 32 ? 1.0646 1.6331 1.1649 0.0144 0.1485 0.0307 51 THR A C 235 O O . THR A 32 ? 1.1034 1.5986 1.1762 0.0206 0.1673 0.0290 51 THR A O 236 C CB . THR A 32 ? 1.2015 1.7522 1.2600 0.0385 0.1300 0.0734 51 THR A CB 237 O OG1 . THR A 32 ? 1.2337 1.7791 1.2643 0.0245 0.1193 0.0840 51 THR A OG1 238 C CG2 . THR A 32 ? 1.2524 1.8829 1.3471 0.0775 0.1211 0.0871 51 THR A CG2 239 N N . VAL A 33 ? 1.0306 1.6829 1.1813 0.0144 0.1454 0.0213 52 VAL A N 240 C CA . VAL A 33 ? 1.0393 1.7101 1.2238 0.0236 0.1692 0.0124 52 VAL A CA 241 C C . VAL A 33 ? 1.1003 1.8579 1.3398 0.0610 0.1646 0.0244 52 VAL A C 242 O O . VAL A 33 ? 1.1217 1.9334 1.3702 0.0722 0.1369 0.0350 52 VAL A O 243 C CB . VAL A 33 ? 0.9714 1.6597 1.1745 -0.0146 0.1788 -0.0126 52 VAL A CB 244 C CG1 . VAL A 33 ? 0.9425 1.5385 1.0856 -0.0372 0.1848 -0.0210 52 VAL A CG1 245 C CG2 . VAL A 33 ? 0.9278 1.7000 1.1718 -0.0385 0.1559 -0.0260 52 VAL A CG2 246 N N . PRO A 34 ? 1.1453 1.9212 1.4204 0.0838 0.1911 0.0224 53 PRO A N 247 C CA . PRO A 34 ? 1.2147 2.0876 1.5543 0.1244 0.1852 0.0314 53 PRO A CA 248 C C . PRO A 34 ? 1.1698 2.1682 1.5785 0.1011 0.1613 0.0128 53 PRO A C 249 O O . PRO A 34 ? 1.0887 2.0881 1.4977 0.0516 0.1596 -0.0092 53 PRO A O 250 C CB . PRO A 34 ? 1.2621 2.1249 1.6272 0.1437 0.2268 0.0256 53 PRO A CB 251 C CG . PRO A 34 ? 1.2566 1.9904 1.5439 0.1283 0.2495 0.0227 53 PRO A CG 252 C CD . PRO A 34 ? 1.1577 1.8634 1.4091 0.0800 0.2285 0.0129 53 PRO A CD 253 N N . ASP A 35 ? 1.2440 2.3471 1.7108 0.1387 0.1415 0.0198 54 ASP A N 254 C CA . ASP A 35 ? 1.2319 2.4691 1.7727 0.1193 0.1138 -0.0032 54 ASP A CA 255 C C . ASP A 35 ? 1.1866 2.4688 1.7973 0.0791 0.1454 -0.0343 54 ASP A C 256 O O . ASP A 35 ? 1.2093 2.4635 1.8347 0.0922 0.1863 -0.0316 54 ASP A O 257 C CB . ASP A 35 ? 1.3466 2.6910 1.9349 0.1775 0.0836 0.0117 54 ASP A CB 258 C CG . ASP A 35 ? 1.4311 2.7286 1.9424 0.2184 0.0543 0.0472 54 ASP A CG 259 O OD1 . ASP A 35 ? 1.3823 2.5976 1.8190 0.1892 0.0490 0.0520 54 ASP A OD1 260 O OD2 . ASP A 35 ? 1.5653 2.9096 2.0915 0.2811 0.0385 0.0712 54 ASP A OD2 261 N N . GLY A 36 ? 1.1440 2.4838 1.7899 0.0277 0.1311 -0.0643 55 GLY A N 262 C CA . GLY A 36 ? 1.1257 2.4984 1.8347 -0.0204 0.1647 -0.0941 55 GLY A CA 263 C C . GLY A 36 ? 1.0666 2.3108 1.7037 -0.0637 0.1935 -0.0976 55 GLY A C 264 O O . GLY A 36 ? 1.0759 2.3145 1.7428 -0.1028 0.2297 -0.1154 55 GLY A O 265 N N . PHE A 37 ? 1.0235 2.1668 1.5675 -0.0558 0.1783 -0.0801 56 PHE A N 266 C CA . PHE A 37 ? 0.9797 2.0079 1.4533 -0.0879 0.1966 -0.0825 56 PHE A CA 267 C C . PHE A 37 ? 0.9377 1.9402 1.3658 -0.1071 0.1626 -0.0879 56 PHE A C 268 O O . PHE A 37 ? 0.9444 1.9849 1.3653 -0.0858 0.1284 -0.0793 56 PHE A O 269 C CB . PHE A 37 ? 0.9848 1.9062 1.3884 -0.0590 0.2183 -0.0597 56 PHE A CB 270 C CG . PHE A 37 ? 1.0438 1.9645 1.4718 -0.0399 0.2606 -0.0561 56 PHE A CG 271 C CD1 . PHE A 37 ? 1.0704 1.9453 1.4864 -0.0675 0.3021 -0.0655 56 PHE A CD1 272 C CD2 . PHE A 37 ? 1.0978 2.0549 1.5523 0.0097 0.2623 -0.0413 56 PHE A CD2 273 C CE1 . PHE A 37 ? 1.1452 2.0180 1.5771 -0.0489 0.3470 -0.0624 56 PHE A CE1 274 C CE2 . PHE A 37 ? 1.1681 2.1234 1.6440 0.0309 0.3057 -0.0402 56 PHE A CE2 275 C CZ . PHE A 37 ? 1.1893 2.1048 1.6536 0.0002 0.3489 -0.0517 56 PHE A CZ 276 N N . ARG A 38 ? 0.9155 1.8481 1.3072 -0.1432 0.1749 -0.1002 57 ARG A N 277 C CA . ARG A 38 ? 0.8867 1.7814 1.2318 -0.1601 0.1506 -0.1072 57 ARG A CA 278 C C . ARG A 38 ? 0.8633 1.6427 1.1336 -0.1561 0.1637 -0.0943 57 ARG A C 279 O O . ARG A 38 ? 0.8807 1.6115 1.1326 -0.1445 0.1905 -0.0836 57 ARG A O 280 C CB . ARG A 38 ? 0.9130 1.8365 1.2898 -0.2048 0.1497 -0.1391 57 ARG A CB 281 C CG . ARG A 38 ? 0.9492 1.9866 1.3812 -0.2106 0.1176 -0.1589 57 ARG A CG 282 C CD . ARG A 38 ? 1.0036 2.0585 1.4662 -0.2604 0.1200 -0.1969 57 ARG A CD 283 N NE . ARG A 38 ? 1.0742 2.2501 1.5972 -0.2697 0.0878 -0.2236 57 ARG A NE 284 C CZ . ARG A 38 ? 1.1476 2.3871 1.7429 -0.3118 0.0942 -0.2600 57 ARG A CZ 285 N NH1 . ARG A 38 ? 1.1848 2.3687 1.7978 -0.3492 0.1381 -0.2695 57 ARG A NH1 286 N NH2 . ARG A 38 ? 1.2031 2.5614 1.8516 -0.3177 0.0572 -0.2877 57 ARG A NH2 287 N N . ILE A 39 ? 0.8419 1.5837 1.0700 -0.1638 0.1442 -0.0976 58 ILE A N 288 C CA . ILE A 39 ? 0.8295 1.4780 0.9951 -0.1594 0.1489 -0.0897 58 ILE A CA 289 C C . ILE A 39 ? 0.8534 1.4576 0.9995 -0.1848 0.1549 -0.1063 58 ILE A C 290 O O . ILE A 39 ? 0.8611 1.4946 1.0224 -0.2025 0.1414 -0.1235 58 ILE A O 291 C CB . ILE A 39 ? 0.8077 1.4438 0.9424 -0.1431 0.1256 -0.0780 58 ILE A CB 292 C CG1 . ILE A 39 ? 0.8213 1.5053 0.9744 -0.1177 0.1166 -0.0599 58 ILE A CG1 293 C CG2 . ILE A 39 ? 0.8034 1.3560 0.8862 -0.1371 0.1291 -0.0726 58 ILE A CG2 294 C CD1 . ILE A 39 ? 0.8424 1.4829 0.9769 -0.0929 0.1298 -0.0415 58 ILE A CD1 295 N N . LYS A 40 ? 0.8867 1.4140 0.9908 -0.1828 0.1748 -0.1007 59 LYS A N 296 C CA . LYS A 40 ? 0.9419 1.4072 1.0124 -0.1970 0.1823 -0.1095 59 LYS A CA 297 C C . LYS A 40 ? 0.9359 1.3445 0.9508 -0.1770 0.1640 -0.1028 59 LYS A C 298 O O . LYS A 40 ? 0.9362 1.3137 0.9204 -0.1588 0.1660 -0.0912 59 LYS A O 299 C CB . LYS A 40 ? 1.0270 1.4470 1.0850 -0.2066 0.2210 -0.1051 59 LYS A CB 300 C CG . LYS A 40 ? 1.1276 1.4789 1.1524 -0.2225 0.2346 -0.1114 59 LYS A CG 301 C CD . LYS A 40 ? 1.2434 1.5509 1.2587 -0.2384 0.2811 -0.1050 59 LYS A CD 302 C CE . LYS A 40 ? 1.3168 1.5346 1.2479 -0.2128 0.2958 -0.0841 59 LYS A CE 303 N NZ . LYS A 40 ? 1.4467 1.6261 1.3648 -0.2267 0.3485 -0.0741 59 LYS A NZ 304 N N . LEU A 41 ? 0.9413 1.3415 0.9472 -0.1802 0.1461 -0.1138 60 LEU A N 305 C CA . LEU A 41 ? 0.9397 1.3050 0.9086 -0.1620 0.1258 -0.1121 60 LEU A CA 306 C C . LEU A 41 ? 1.0264 1.3360 0.9625 -0.1582 0.1256 -0.1192 60 LEU A C 307 O O . LEU A 41 ? 1.0636 1.3785 1.0166 -0.1723 0.1306 -0.1323 60 LEU A O 308 C CB . LEU A 41 ? 0.8764 1.2974 0.8719 -0.1608 0.1031 -0.1162 60 LEU A CB 309 C CG . LEU A 41 ? 0.8806 1.2872 0.8589 -0.1480 0.0830 -0.1196 60 LEU A CG 310 C CD1 . LEU A 41 ? 0.8773 1.2579 0.8334 -0.1366 0.0780 -0.1103 60 LEU A CD1 311 C CD2 . LEU A 41 ? 0.8476 1.3095 0.8552 -0.1536 0.0716 -0.1262 60 LEU A CD2 312 N N . TYR A 42 ? 1.0768 1.3318 0.9631 -0.1363 0.1177 -0.1121 61 TYR A N 313 C CA . TYR A 42 ? 1.1854 1.3828 1.0319 -0.1207 0.1131 -0.1142 61 TYR A CA 314 C C . TYR A 42 ? 1.2063 1.3935 1.0238 -0.0925 0.0828 -0.1144 61 TYR A C 315 O O . TYR A 42 ? 1.1545 1.3617 0.9725 -0.0900 0.0713 -0.1128 61 TYR A O 316 C CB . TYR A 42 ? 1.3120 1.4336 1.1139 -0.1232 0.1451 -0.1026 61 TYR A CB 317 C CG . TYR A 42 ? 1.3465 1.4332 1.1038 -0.1139 0.1592 -0.0863 61 TYR A CG 318 C CD1 . TYR A 42 ? 1.2994 1.4158 1.0855 -0.1325 0.1845 -0.0823 61 TYR A CD1 319 C CD2 . TYR A 42 ? 1.4528 1.4789 1.1365 -0.0832 0.1471 -0.0767 61 TYR A CD2 320 C CE1 . TYR A 42 ? 1.3461 1.4282 1.0883 -0.1214 0.2023 -0.0698 61 TYR A CE1 321 C CE2 . TYR A 42 ? 1.5079 1.4978 1.1395 -0.0735 0.1613 -0.0650 61 TYR A CE2 322 C CZ . TYR A 42 ? 1.4554 1.4708 1.1161 -0.0932 0.1917 -0.0618 61 TYR A CZ 323 O OH . TYR A 42 ? 1.5258 1.5039 1.1334 -0.0815 0.2106 -0.0525 61 TYR A OH 324 N N . PHE A 43 ? 1.2987 1.4564 1.0943 -0.0708 0.0692 -0.1189 62 PHE A N 325 C CA . PHE A 43 ? 1.3337 1.4988 1.1144 -0.0421 0.0348 -0.1241 62 PHE A CA 326 C C . PHE A 43 ? 1.5025 1.5901 1.2073 -0.0075 0.0284 -0.1126 62 PHE A C 327 O O . PHE A 43 ? 1.6176 1.6425 1.2895 -0.0004 0.0490 -0.1032 62 PHE A O 328 C CB . PHE A 43 ? 1.3034 1.5263 1.1374 -0.0384 0.0175 -0.1418 62 PHE A CB 329 C CG . PHE A 43 ? 1.1725 1.4700 1.0685 -0.0675 0.0219 -0.1504 62 PHE A CG 330 C CD1 . PHE A 43 ? 1.1352 1.4455 1.0524 -0.0917 0.0446 -0.1515 62 PHE A CD1 331 C CD2 . PHE A 43 ? 1.1107 1.4645 1.0412 -0.0711 0.0035 -0.1576 62 PHE A CD2 332 C CE1 . PHE A 43 ? 1.0402 1.4166 1.0015 -0.1120 0.0461 -0.1560 62 PHE A CE1 333 C CE2 . PHE A 43 ? 1.0212 1.4317 0.9967 -0.0952 0.0121 -0.1597 62 PHE A CE2 334 C CZ . PHE A 43 ? 0.9876 1.4082 0.9729 -0.1120 0.0320 -0.1571 62 PHE A CZ 335 N N . MET A 44 ? 1.5420 1.6305 1.2148 0.0143 -0.0007 -0.1142 63 MET A N 336 C CA . MET A 44 ? 1.7280 1.7495 1.3175 0.0548 -0.0158 -0.1032 63 MET A CA 337 C C . MET A 44 ? 1.7926 1.8496 1.3979 0.0904 -0.0588 -0.1168 63 MET A C 338 O O . MET A 44 ? 1.9741 1.9764 1.5163 0.1330 -0.0725 -0.1058 63 MET A O 339 C CB . MET A 44 ? 1.7716 1.7669 1.3014 0.0589 -0.0208 -0.0988 63 MET A CB 340 C CG . MET A 44 ? 1.7374 1.6957 1.2480 0.0317 0.0258 -0.0842 63 MET A CG 341 S SD . MET A 44 ? 1.8289 1.7172 1.3193 0.0201 0.0787 -0.0619 63 MET A SD 342 C CE . MET A 44 ? 2.0997 1.8810 1.4671 0.0697 0.0735 -0.0394 63 MET A CE 343 N N . HIS A 45 ? 1.6637 1.8133 1.3537 0.0749 -0.0781 -0.1393 64 HIS A N 344 C CA . HIS A 45 ? 1.7085 1.9180 1.4401 0.1028 -0.1156 -0.1576 64 HIS A CA 345 C C . HIS A 45 ? 1.5680 1.8602 1.3954 0.0736 -0.1064 -0.1749 64 HIS A C 346 O O . HIS A 45 ? 1.4326 1.7572 1.2948 0.0339 -0.0913 -0.1776 64 HIS A O 347 C CB . HIS A 45 ? 1.7549 2.0000 1.4763 0.1168 -0.1595 -0.1724 64 HIS A CB 348 C CG . HIS A 45 ? 1.8425 2.1519 1.6035 0.1531 -0.2025 -0.1915 64 HIS A CG 349 N ND1 . HIS A 45 ? 1.7508 2.1660 1.6123 0.1324 -0.2173 -0.2186 64 HIS A ND1 350 C CD2 . HIS A 45 ? 2.0289 2.3121 1.7432 0.2103 -0.2311 -0.1858 64 HIS A CD2 351 C CE1 . HIS A 45 ? 1.8640 2.3251 1.7470 0.1760 -0.2550 -0.2320 64 HIS A CE1 352 N NE2 . HIS A 45 ? 2.0371 2.4215 1.8319 0.2272 -0.2673 -0.2125 64 HIS A NE2 353 N N . PHE A 46 ? 1.6220 1.9423 1.4853 0.0966 -0.1122 -0.1847 65 PHE A N 354 C CA . PHE A 46 ? 1.5214 1.9183 1.4666 0.0739 -0.1000 -0.2016 65 PHE A CA 355 C C . PHE A 46 ? 1.6105 2.0647 1.6024 0.1111 -0.1232 -0.2201 65 PHE A C 356 O O . PHE A 46 ? 1.7401 2.1512 1.7063 0.1498 -0.1219 -0.2168 65 PHE A O 357 C CB . PHE A 46 ? 1.4786 1.8403 1.4188 0.0502 -0.0603 -0.1949 65 PHE A CB 358 C CG . PHE A 46 ? 1.3717 1.8088 1.3785 0.0189 -0.0453 -0.2087 65 PHE A CG 359 C CD1 . PHE A 46 ? 1.4204 1.9031 1.4707 0.0338 -0.0431 -0.2268 65 PHE A CD1 360 C CD2 . PHE A 46 ? 1.2438 1.7030 1.2639 -0.0211 -0.0313 -0.2023 65 PHE A CD2 361 C CE1 . PHE A 46 ? 1.3469 1.8955 1.4470 0.0062 -0.0254 -0.2377 65 PHE A CE1 362 C CE2 . PHE A 46 ? 1.1785 1.6997 1.2462 -0.0457 -0.0164 -0.2102 65 PHE A CE2 363 C CZ . PHE A 46 ? 1.2304 1.7958 1.3350 -0.0334 -0.0128 -0.2277 65 PHE A CZ 364 N N . ASN A 47 ? 1.5587 2.1093 1.6225 0.0992 -0.1417 -0.2401 66 ASN A N 365 C CA . ASN A 47 ? 1.6446 2.2744 1.7719 0.1319 -0.1650 -0.2619 66 ASN A CA 366 C C . ASN A 47 ? 1.5514 2.2825 1.7727 0.0944 -0.1496 -0.2813 66 ASN A C 367 O O . ASN A 47 ? 1.5113 2.3023 1.7771 0.0684 -0.1648 -0.2937 66 ASN A O 368 C CB . ASN A 47 ? 1.7426 2.3912 1.8566 0.1651 -0.2153 -0.2691 66 ASN A CB 369 C CG . ASN A 47 ? 1.8827 2.5992 2.0465 0.2180 -0.2461 -0.2873 66 ASN A CG 370 O OD1 . ASN A 47 ? 1.8864 2.7092 2.1291 0.2149 -0.2742 -0.3135 66 ASN A OD1 371 N ND2 . ASN A 47 ? 2.0145 2.6706 2.1359 0.2686 -0.2411 -0.2751 66 ASN A ND2 372 N N . LEU A 48 ? 1.5388 2.2825 1.7845 0.0890 -0.1162 -0.2846 67 LEU A N 373 C CA . LEU A 48 ? 1.4792 2.3094 1.8005 0.0551 -0.0924 -0.2987 67 LEU A CA 374 C C . LEU A 48 ? 1.5772 2.4659 1.9523 0.0864 -0.0821 -0.3188 67 LEU A C 375 O O . LEU A 48 ? 1.6894 2.5378 2.0368 0.1346 -0.0901 -0.3202 67 LEU A O 376 C CB . LEU A 48 ? 1.3754 2.1678 1.6652 0.0117 -0.0552 -0.2828 67 LEU A CB 377 C CG . LEU A 48 ? 1.2731 2.0679 1.5631 -0.0341 -0.0510 -0.2712 67 LEU A CG 378 C CD1 . LEU A 48 ? 1.2471 1.9658 1.4723 -0.0312 -0.0701 -0.2557 67 LEU A CD1 379 C CD2 . LEU A 48 ? 1.2090 1.9987 1.4886 -0.0675 -0.0141 -0.2589 67 LEU A CD2 380 N N . GLU A 49 ? 1.5556 2.5344 2.0052 0.0599 -0.0599 -0.3334 68 GLU A N 381 C CA . GLU A 49 ? 1.6509 2.6952 2.1569 0.0842 -0.0398 -0.3544 68 GLU A CA 382 C C . GLU A 49 ? 1.6619 2.6400 2.1090 0.0826 -0.0042 -0.3485 68 GLU A C 383 O O . GLU A 49 ? 1.5693 2.5035 1.9704 0.0430 0.0134 -0.3319 68 GLU A O 384 C CB . GLU A 49 ? 1.6315 2.7844 2.2265 0.0456 -0.0179 -0.3681 68 GLU A CB 385 C CG . GLU A 49 ? 1.7439 2.9828 2.4099 0.0674 0.0089 -0.3922 68 GLU A CG 386 C CD . GLU A 49 ? 1.7405 3.0709 2.4814 0.0176 0.0428 -0.3992 68 GLU A CD 387 O OE1 . GLU A 49 ? 1.6653 2.9594 2.3638 -0.0258 0.0761 -0.3805 68 GLU A OE1 388 O OE2 . GLU A 49 ? 2.3004 3.6138 3.1076 0.0178 0.0318 -0.3585 68 GLU A OE2 389 N N . SER A 50 ? 1.7906 2.7603 2.2381 0.1273 0.0042 -0.3640 69 SER A N 390 C CA . SER A 50 ? 1.8336 2.7407 2.2265 0.1253 0.0363 -0.3672 69 SER A CA 391 C C . SER A 50 ? 1.8700 2.8529 2.3055 0.1107 0.0757 -0.3859 69 SER A C 392 O O . SER A 50 ? 1.9324 3.0076 2.4459 0.1288 0.0802 -0.4032 69 SER A O 393 C CB . SER A 50 ? 1.9915 2.8233 2.3465 0.1806 0.0286 -0.3744 69 SER A CB 394 O OG . SER A 50 ? 2.0472 2.8041 2.3431 0.1696 0.0570 -0.3804 69 SER A OG 395 N N . SER A 51 ? 1.8425 2.7918 2.2269 0.0785 0.1043 -0.3832 70 SER A N 396 C CA . SER A 51 ? 1.9111 2.9179 2.3108 0.0645 0.1452 -0.3985 70 SER A CA 397 C C . SER A 51 ? 2.0265 2.9722 2.3477 0.0477 0.1653 -0.4029 70 SER A C 398 O O . SER A 51 ? 1.8698 2.7450 2.1366 0.0295 0.1492 -0.3882 70 SER A O 399 C CB . SER A 51 ? 1.8377 2.9235 2.2839 0.0233 0.1594 -0.3850 70 SER A CB 400 O OG . SER A 51 ? 1.7175 2.7636 2.1142 -0.0194 0.1572 -0.3577 70 SER A OG 401 N N . TYR A 52 ? 3.0948 3.6866 3.3170 0.0683 0.1932 -0.2325 71 TYR A N 402 C CA . TYR A 52 ? 3.2809 3.7115 3.4008 0.0695 0.2043 -0.1856 71 TYR A CA 403 C C . TYR A 52 ? 2.6059 3.5343 2.8074 -0.0082 0.2133 -0.4105 71 TYR A C 404 O O . TYR A 52 ? 2.2711 3.2549 2.4945 -0.0315 0.2252 -0.3896 71 TYR A O 405 C CB . TYR A 52 ? 3.5288 3.7632 3.5941 0.0993 0.2358 -0.0865 71 TYR A CB 406 C CG . TYR A 52 ? 3.5933 3.7650 3.5845 0.0844 0.2106 -0.0862 71 TYR A CG 407 C CD1 . TYR A 52 ? 3.6506 3.7599 3.5940 0.0769 0.1750 -0.0903 71 TYR A CD1 408 C CD2 . TYR A 52 ? 3.5803 3.7714 3.5666 0.0786 0.2260 -0.0810 71 TYR A CD2 409 C CE1 . TYR A 52 ? 3.6750 3.7585 3.5736 0.0715 0.1677 -0.0963 71 TYR A CE1 410 C CE2 . TYR A 52 ? 3.6252 3.7713 3.5548 0.0702 0.2066 -0.0832 71 TYR A CE2 411 C CZ . TYR A 52 ? 3.6648 3.7643 3.5544 0.0689 0.1817 -0.0929 71 TYR A CZ 412 O OH . TYR A 52 ? 3.6882 3.7627 3.5342 0.0641 0.1719 -0.0989 71 TYR A OH 413 N N . LEU A 53 ? 2.2313 3.0882 2.3769 -0.0207 0.1949 -0.4093 72 LEU A N 414 C CA . LEU A 53 ? 1.8865 2.7333 1.9937 -0.0573 0.1837 -0.3844 72 LEU A CA 415 C C . LEU A 53 ? 1.7265 2.5913 1.8694 -0.0722 0.1685 -0.3477 72 LEU A C 416 O O . LEU A 53 ? 1.6566 2.5321 1.7789 -0.0982 0.1683 -0.3230 72 LEU A O 417 C CB . LEU A 53 ? 2.2001 3.0860 2.2635 -0.0739 0.2072 -0.3886 72 LEU A CB 418 C CG . LEU A 53 ? 3.1559 3.6772 3.1075 -0.0123 0.1955 -0.2742 72 LEU A CG 419 C CD1 . LEU A 53 ? 3.3275 3.7152 3.2101 0.0062 0.2025 -0.2085 72 LEU A CD1 420 C CD2 . LEU A 53 ? 2.9153 3.6086 2.8755 -0.0591 0.1860 -0.3943 72 LEU A CD2 421 N N . CYS A 54 ? 1.6935 2.5594 1.8864 -0.0523 0.1545 -0.3461 73 CYS A N 422 C CA . CYS A 54 ? 1.5744 2.4572 1.8052 -0.0634 0.1377 -0.3211 73 CYS A CA 423 C C . CYS A 54 ? 1.5648 2.5094 1.8182 -0.0905 0.1607 -0.3059 73 CYS A C 424 O O . CYS A 54 ? 1.4748 2.4089 1.7176 -0.1160 0.1555 -0.2794 73 CYS A O 425 C CB . CYS A 54 ? 1.4638 2.2837 1.6593 -0.0764 0.1132 -0.3003 73 CYS A CB 426 S SG . CYS A 54 ? 1.5149 2.2506 1.6819 -0.0490 0.0938 -0.3118 73 CYS A SG 427 N N . GLU A 55 ? 1.6812 2.6842 1.9616 -0.0840 0.1912 -0.3224 74 GLU A N 428 C CA . GLU A 55 ? 1.7210 2.7781 2.0183 -0.1107 0.2240 -0.3078 74 GLU A CA 429 C C . GLU A 55 ? 1.6710 2.7721 2.0443 -0.1273 0.2220 -0.2987 74 GLU A C 430 O O . GLU A 55 ? 1.6698 2.7826 2.0445 -0.1601 0.2426 -0.2757 74 GLU A O 431 C CB . GLU A 55 ? 2.0148 3.1164 2.3049 -0.1005 0.2648 -0.3284 74 GLU A CB 432 C CG . GLU A 55 ? 2.8713 3.7019 3.1760 -0.0221 0.2537 -0.2260 74 GLU A CG 433 C CD . GLU A 55 ? 3.3069 3.7738 3.5308 0.0484 0.2734 -0.0764 74 GLU A CD 434 O OE1 . GLU A 55 ? 3.3876 3.7827 3.5403 0.0542 0.2873 -0.0616 74 GLU A OE1 435 O OE2 . GLU A 55 ? 3.4606 3.7899 3.6573 0.0573 0.2196 -0.0371 74 GLU A OE2 436 N N . TYR A 56 ? 1.6509 2.7737 2.0844 -0.1046 0.1966 -0.3172 75 TYR A N 437 C CA . TYR A 56 ? 1.6224 2.7976 2.1353 -0.1207 0.1877 -0.3178 75 TYR A CA 438 C C . TYR A 56 ? 1.4996 2.6184 1.9898 -0.1375 0.1534 -0.2980 75 TYR A C 439 O O . TYR A 56 ? 1.4702 2.5689 1.9411 -0.1732 0.1674 -0.2746 75 TYR A O 440 C CB . TYR A 56 ? 1.6839 2.9252 2.2760 -0.0844 0.1733 -0.3494 75 TYR A CB 441 C CG . TYR A 56 ? 1.8365 3.1381 2.4585 -0.0628 0.2111 -0.3724 75 TYR A CG 442 C CD1 . TYR A 56 ? 2.5947 3.6774 3.1515 -0.0552 0.2473 -0.2560 75 TYR A CD1 443 C CD2 . TYR A 56 ? 2.6764 3.6840 3.2685 0.0109 0.1865 -0.2421 75 TYR A CD2 444 C CE1 . TYR A 56 ? 3.2038 3.7931 3.6719 0.0374 0.2536 -0.0249 75 TYR A CE1 445 C CE2 . TYR A 56 ? 3.2479 3.7925 3.7267 0.0622 0.2005 -0.0226 75 TYR A CE2 446 C CZ . TYR A 56 ? 3.3749 3.7949 3.7242 0.0444 0.1789 -0.0187 75 TYR A CZ 447 O OH . TYR A 56 ? 3.4359 3.7931 3.7217 0.0484 0.1683 -0.0224 75 TYR A OH 448 N N . ASP A 57 ? 1.4531 2.5394 1.9375 -0.1092 0.1117 -0.3057 76 ASP A N 449 C CA . ASP A 57 ? 1.3547 2.3829 1.8078 -0.1199 0.0808 -0.2895 76 ASP A CA 450 C C . ASP A 57 ? 1.3059 2.2501 1.6756 -0.1090 0.0746 -0.2747 76 ASP A C 451 O O . ASP A 57 ? 1.3532 2.2794 1.7009 -0.0809 0.0753 -0.2864 76 ASP A O 452 C CB . ASP A 57 ? 1.3601 2.4085 1.8540 -0.0963 0.0396 -0.3065 76 ASP A CB 453 C CG . ASP A 57 ? 1.4124 2.5580 2.0037 -0.1118 0.0396 -0.3272 76 ASP A CG 454 O OD1 . ASP A 57 ? 1.4410 2.6330 2.0699 -0.1450 0.0786 -0.3259 76 ASP A OD1 455 O OD2 . ASP A 57 ? 1.4357 2.6141 2.0660 -0.0900 0.0013 -0.3455 76 ASP A OD2 456 N N . TYR A 58 ? 1.2255 2.1194 1.5527 -0.1322 0.0720 -0.2511 77 TYR A N 457 C CA . TYR A 58 ? 1.1834 2.0112 1.4439 -0.1269 0.0684 -0.2386 77 TYR A CA 458 C C . TYR A 58 ? 1.1015 1.8787 1.3289 -0.1424 0.0577 -0.2163 77 TYR A C 459 O O . TYR A 58 ? 1.0821 1.8668 1.3267 -0.1633 0.0599 -0.2064 77 TYR A O 460 C CB . TYR A 58 ? 1.2256 2.0643 1.4580 -0.1352 0.0958 -0.2363 77 TYR A CB 461 C CG . TYR A 58 ? 1.2350 2.0977 1.4661 -0.1634 0.1197 -0.2161 77 TYR A CG 462 C CD1 . TYR A 58 ? 1.1833 2.0085 1.3768 -0.1781 0.1181 -0.1896 77 TYR A CD1 463 C CD2 . TYR A 58 ? 1.3241 2.2438 1.5889 -0.1725 0.1480 -0.2217 77 TYR A CD2 464 C CE1 . TYR A 58 ? 1.2214 2.0557 1.4044 -0.1982 0.1415 -0.1663 77 TYR A CE1 465 C CE2 . TYR A 58 ? 1.3665 2.2950 1.6187 -0.1979 0.1760 -0.1982 77 TYR A CE2 466 C CZ . TYR A 58 ? 1.3226 2.2037 1.5305 -0.2091 0.1714 -0.1691 77 TYR A CZ 467 O OH . TYR A 58 ? 1.4006 2.2783 1.5887 -0.2288 0.1999 -0.1414 77 TYR A OH 468 N N . VAL A 59 ? 1.0688 1.7928 1.2495 -0.1338 0.0508 -0.2100 78 VAL A N 469 C CA . VAL A 59 ? 1.0030 1.6818 1.1501 -0.1444 0.0468 -0.1898 78 VAL A CA 470 C C . VAL A 59 ? 1.0037 1.6814 1.1232 -0.1511 0.0605 -0.1840 78 VAL A C 471 O O . VAL A 59 ? 1.0353 1.6971 1.1394 -0.1422 0.0597 -0.1973 78 VAL A O 472 C CB . VAL A 59 ? 0.9878 1.6117 1.1099 -0.1289 0.0275 -0.1893 78 VAL A CB 473 C CG1 . VAL A 59 ? 0.9306 1.5142 1.0200 -0.1392 0.0319 -0.1700 78 VAL A CG1 474 C CG2 . VAL A 59 ? 0.9992 1.6316 1.1429 -0.1213 0.0072 -0.1975 78 VAL A CG2 475 N N . LYS A 60 ? 0.9932 1.6877 1.1057 -0.1662 0.0725 -0.1658 79 LYS A N 476 C CA . LYS A 60 ? 1.0143 1.7216 1.1001 -0.1700 0.0797 -0.1601 79 LYS A CA 477 C C . LYS A 60 ? 0.9616 1.6425 1.0302 -0.1718 0.0731 -0.1419 79 LYS A C 478 O O . LYS A 60 ? 0.9390 1.6039 1.0082 -0.1744 0.0750 -0.1219 79 LYS A O 479 C CB . LYS A 60 ? 1.0818 1.8275 1.1631 -0.1779 0.0982 -0.1486 79 LYS A CB 480 C CG . LYS A 60 ? 1.1409 1.9104 1.1863 -0.1766 0.1018 -0.1473 79 LYS A CG 481 C CD . LYS A 60 ? 1.2416 2.0392 1.2691 -0.1810 0.1238 -0.1304 79 LYS A CD 482 C CE . LYS A 60 ? 1.3445 2.1710 1.3259 -0.1752 0.1245 -0.1336 79 LYS A CE 483 N NZ . LYS A 60 ? 1.4740 2.3212 1.4254 -0.1767 0.1511 -0.1146 79 LYS A NZ 484 N N . VAL A 61 ? 0.9566 1.6335 1.0142 -0.1712 0.0676 -0.1516 80 VAL A N 485 C CA . VAL A 61 ? 0.9145 1.5811 0.9672 -0.1724 0.0638 -0.1388 80 VAL A CA 486 C C . VAL A 61 ? 0.9586 1.6723 1.0022 -0.1747 0.0610 -0.1381 80 VAL A C 487 O O . VAL A 61 ? 1.0114 1.7457 1.0508 -0.1805 0.0581 -0.1622 80 VAL A O 488 C CB . VAL A 61 ? 0.8952 1.5224 0.9496 -0.1735 0.0621 -0.1507 80 VAL A CB 489 C CG1 . VAL A 61 ? 0.8577 1.4841 0.9164 -0.1757 0.0642 -0.1377 80 VAL A CG1 490 C CG2 . VAL A 61 ? 0.8806 1.4625 0.9313 -0.1645 0.0597 -0.1513 80 VAL A CG2 491 N N . GLU A 62 ? 0.9603 1.6886 0.9971 -0.1676 0.0606 -0.1120 81 GLU A N 492 C CA . GLU A 62 ? 1.0282 1.8072 1.0504 -0.1623 0.0524 -0.1076 81 GLU A CA 493 C C . GLU A 62 ? 1.0222 1.8130 1.0483 -0.1476 0.0468 -0.0822 81 GLU A C 494 O O . GLU A 62 ? 0.9732 1.7250 1.0086 -0.1418 0.0545 -0.0655 81 GLU A O 495 C CB . GLU A 62 ? 1.1177 1.9139 1.1092 -0.1586 0.0608 -0.0979 81 GLU A CB 496 C CG . GLU A 62 ? 1.1353 1.9018 1.1169 -0.1525 0.0759 -0.0632 81 GLU A CG 497 C CD . GLU A 62 ? 1.2324 2.0046 1.1925 -0.1569 0.0952 -0.0554 81 GLU A CD 498 O OE1 . GLU A 62 ? 1.3274 2.1366 1.2573 -0.1537 0.0953 -0.0632 81 GLU A OE1 499 O OE2 . GLU A 62 ? 1.2275 1.9682 1.2004 -0.1654 0.1120 -0.0430 81 GLU A OE2 500 N N . THR A 63 ? 1.0924 1.9392 1.1088 -0.1382 0.0322 -0.0810 82 THR A N 501 C CA . THR A 63 ? 1.1226 1.9949 1.1421 -0.1149 0.0234 -0.0553 82 THR A CA 502 C C . THR A 63 ? 1.2451 2.1211 1.2146 -0.0944 0.0251 -0.0243 82 THR A C 503 O O . THR A 63 ? 1.2849 2.1382 1.2264 -0.1040 0.0392 -0.0230 82 THR A O 504 C CB . THR A 63 ? 1.1348 2.0775 1.1864 -0.1165 0.0018 -0.0779 82 THR A CB 505 O OG1 . THR A 63 ? 1.2423 2.2400 1.2678 -0.1180 -0.0169 -0.0953 82 THR A OG1 506 C CG2 . THR A 63 ? 1.0520 1.9820 1.1478 -0.1428 0.0084 -0.1080 82 THR A CG2 507 N N . GLU A 64 ? 1.3254 2.2309 1.2832 -0.0644 0.0128 0.0015 83 GLU A N 508 C CA . GLU A 64 ? 1.4813 2.3821 1.3800 -0.0381 0.0152 0.0383 83 GLU A CA 509 C C . GLU A 64 ? 1.6006 2.5545 1.4546 -0.0384 0.0007 0.0244 83 GLU A C 510 O O . GLU A 64 ? 1.7512 2.6917 1.5425 -0.0206 0.0097 0.0548 83 GLU A O 511 C CB . GLU A 64 ? 1.5597 2.4709 1.4566 0.0034 0.0048 0.0727 83 GLU A CB 512 C CG . GLU A 64 ? 1.5341 2.5306 1.4799 0.0147 -0.0263 0.0508 83 GLU A CG 513 C CD . GLU A 64 ? 1.3801 2.3666 1.3945 -0.0029 -0.0174 0.0300 83 GLU A CD 514 O OE1 . GLU A 64 ? 1.3724 2.3199 1.3999 0.0183 -0.0036 0.0539 83 GLU A OE1 515 O OE2 . GLU A 64 ? 1.2897 2.2977 1.3383 -0.0375 -0.0202 -0.0098 83 GLU A OE2 516 N N . ASP A 65 ? 1.5580 2.5648 1.4378 -0.0591 -0.0185 -0.0218 84 ASP A N 517 C CA . ASP A 65 ? 1.6900 2.7488 1.5258 -0.0606 -0.0351 -0.0448 84 ASP A CA 518 C C . ASP A 65 ? 1.6329 2.7009 1.4946 -0.0966 -0.0358 -0.0994 84 ASP A C 519 O O . ASP A 65 ? 1.7481 2.8605 1.5786 -0.1012 -0.0520 -0.1295 84 ASP A O 520 C CB . ASP A 65 ? 1.7996 2.9402 1.6302 -0.0333 -0.0747 -0.0446 84 ASP A CB 521 C CG . ASP A 65 ? 1.6904 2.8808 1.6037 -0.0443 -0.0954 -0.0730 84 ASP A CG 522 O OD1 . ASP A 65 ? 1.5466 2.6999 1.5121 -0.0748 -0.0771 -0.0934 84 ASP A OD1 523 O OD2 . ASP A 65 ? 1.7733 3.0420 1.6990 -0.0213 -0.1287 -0.0741 84 ASP A OD2 524 N N . GLN A 66 ? 1.4843 2.5066 1.3969 -0.1194 -0.0192 -0.1130 85 GLN A N 525 C CA . GLN A 66 ? 1.4483 2.4653 1.3852 -0.1490 -0.0178 -0.1607 85 GLN A CA 526 C C . GLN A 66 ? 1.3342 2.2816 1.2940 -0.1620 0.0082 -0.1605 85 GLN A C 527 O O . GLN A 66 ? 1.2325 2.1462 1.2210 -0.1595 0.0157 -0.1401 85 GLN A O 528 C CB . GLN A 66 ? 1.4163 2.4764 1.4042 -0.1627 -0.0392 -0.1884 85 GLN A CB 529 C CG . GLN A 66 ? 1.4001 2.4421 1.4167 -0.1965 -0.0347 -0.2366 85 GLN A CG 530 C CD . GLN A 66 ? 1.3843 2.4656 1.4599 -0.2152 -0.0476 -0.2585 85 GLN A CD 531 O OE1 . GLN A 66 ? 1.4140 2.5651 1.5094 -0.2025 -0.0697 -0.2501 85 GLN A OE1 532 N NE2 . GLN A 66 ? 1.3588 2.3974 1.4655 -0.2450 -0.0323 -0.2869 85 GLN A NE2 533 N N . VAL A 67 ? 1.3712 2.2999 1.3170 -0.1727 0.0204 -0.1859 86 VAL A N 534 C CA . VAL A 67 ? 1.2887 2.1618 1.2575 -0.1798 0.0393 -0.1902 86 VAL A CA 535 C C . VAL A 67 ? 1.2510 2.1014 1.2511 -0.1963 0.0347 -0.2213 86 VAL A C 536 O O . VAL A 67 ? 1.3366 2.2001 1.3305 -0.2086 0.0290 -0.2578 86 VAL A O 537 C CB . VAL A 67 ? 1.3622 2.2292 1.3089 -0.1772 0.0576 -0.1999 86 VAL A CB 538 C CG1 . VAL A 67 ? 1.2896 2.1110 1.2683 -0.1794 0.0698 -0.2088 86 VAL A CG1 539 C CG2 . VAL A 67 ? 1.4166 2.2975 1.3328 -0.1660 0.0709 -0.1648 86 VAL A CG2 540 N N . LEU A 68 ? 1.1479 1.9590 1.1763 -0.1976 0.0395 -0.2070 87 LEU A N 541 C CA . LEU A 68 ? 1.1311 1.9085 1.1832 -0.2130 0.0423 -0.2279 87 LEU A CA 542 C C . LEU A 68 ? 1.1612 1.8828 1.2066 -0.2129 0.0541 -0.2463 87 LEU A C 543 O O . LEU A 68 ? 1.2326 1.9319 1.2794 -0.2268 0.0574 -0.2766 87 LEU A O 544 C CB . LEU A 68 ? 1.0364 1.7933 1.1112 -0.2110 0.0462 -0.2035 87 LEU A CB 545 C CG . LEU A 68 ? 1.0184 1.8287 1.1067 -0.2037 0.0359 -0.1837 87 LEU A CG 546 C CD1 . LEU A 68 ? 0.9420 1.7223 1.0483 -0.1972 0.0462 -0.1610 87 LEU A CD1 547 C CD2 . LEU A 68 ? 1.0843 1.9564 1.1939 -0.2191 0.0216 -0.2105 87 LEU A CD2 548 N N . ALA A 69 ? 1.1227 1.8218 1.1633 -0.1966 0.0602 -0.2295 88 ALA A N 549 C CA . ALA A 69 ? 1.1591 1.8140 1.1980 -0.1868 0.0675 -0.2435 88 ALA A CA 550 C C . ALA A 69 ? 1.1393 1.8073 1.1835 -0.1710 0.0703 -0.2305 88 ALA A C 551 O O . ALA A 69 ? 1.0796 1.7665 1.1286 -0.1710 0.0692 -0.2053 88 ALA A O 552 C CB . ALA A 69 ? 1.1328 1.7247 1.1745 -0.1860 0.0704 -0.2383 88 ALA A CB 553 N N . THR A 70 ? 1.2095 1.8665 1.2570 -0.1577 0.0757 -0.2496 89 THR A N 554 C CA . THR A 70 ? 1.2077 1.8864 1.2754 -0.1436 0.0792 -0.2449 89 THR A CA 555 C C . THR A 70 ? 1.2480 1.8857 1.3247 -0.1216 0.0744 -0.2570 89 THR A C 556 O O . THR A 70 ? 1.3442 1.9519 1.4084 -0.1126 0.0795 -0.2797 89 THR A O 557 C CB . THR A 70 ? 1.2902 2.0211 1.3560 -0.1438 0.0940 -0.2562 89 THR A CB 558 O OG1 . THR A 70 ? 1.2923 2.0515 1.3338 -0.1588 0.0954 -0.2432 89 THR A OG1 559 C CG2 . THR A 70 ? 1.2877 2.0536 1.3873 -0.1367 0.1029 -0.2494 89 THR A CG2 560 N N . PHE A 71 ? 1.1973 1.8296 1.2913 -0.1112 0.0635 -0.2430 90 PHE A N 561 C CA . PHE A 71 ? 1.2529 1.8491 1.3491 -0.0831 0.0526 -0.2501 90 PHE A CA 562 C C . PHE A 71 ? 1.2728 1.9191 1.4112 -0.0656 0.0450 -0.2561 90 PHE A C 563 O O . PHE A 71 ? 1.2148 1.9088 1.3807 -0.0823 0.0459 -0.2475 90 PHE A O 564 C CB . PHE A 71 ? 1.2098 1.7476 1.2795 -0.0813 0.0407 -0.2318 90 PHE A CB 565 C CG . PHE A 71 ? 1.2029 1.6953 1.2421 -0.0999 0.0512 -0.2266 90 PHE A CG 566 C CD1 . PHE A 71 ? 1.3062 1.7509 1.3257 -0.0974 0.0621 -0.2421 90 PHE A CD1 567 C CD2 . PHE A 71 ? 1.1077 1.6045 1.1424 -0.1201 0.0522 -0.2082 90 PHE A CD2 568 C CE1 . PHE A 71 ? 1.3122 1.7235 1.3155 -0.1216 0.0738 -0.2414 90 PHE A CE1 569 C CE2 . PHE A 71 ? 1.1093 1.5788 1.1293 -0.1377 0.0628 -0.2060 90 PHE A CE2 570 C CZ . PHE A 71 ? 1.2104 1.6405 1.2180 -0.1412 0.0735 -0.2234 90 PHE A CZ 571 N N . CYS A 72 ? 1.3743 2.0084 1.5205 -0.0314 0.0384 -0.2713 91 CYS A N 572 C CA . CYS A 72 ? 1.4133 2.1018 1.6089 -0.0062 0.0260 -0.2819 91 CYS A CA 573 C C . CYS A 72 ? 1.5415 2.1851 1.7231 0.0413 0.0121 -0.2905 91 CYS A C 574 O O . CYS A 72 ? 1.6019 2.1639 1.7322 0.0488 0.0186 -0.2874 91 CYS A O 575 C CB . CYS A 72 ? 1.4414 2.2115 1.6851 -0.0148 0.0476 -0.2973 91 CYS A CB 576 S SG . CYS A 72 ? 1.5658 2.3238 1.7892 -0.0007 0.0753 -0.3221 91 CYS A SG 577 N N . GLY A 73 ? 1.5989 2.2938 1.8260 0.0736 -0.0072 -0.3004 92 GLY A N 578 C CA . GLY A 73 ? 1.7481 2.4047 1.9614 0.1293 -0.0246 -0.3055 92 GLY A CA 579 C C . GLY A 73 ? 1.7599 2.3652 1.9307 0.1470 -0.0571 -0.2858 92 GLY A C 580 O O . GLY A 73 ? 1.6426 2.2424 1.7972 0.1138 -0.0639 -0.2717 92 GLY A O 581 N N . ARG A 74 ? 1.9235 2.4877 2.0701 0.2036 -0.0762 -0.2845 93 ARG A N 582 C CA . ARG A 74 ? 1.9867 2.4958 2.0775 0.2310 -0.1079 -0.2648 93 ARG A CA 583 C C . ARG A 74 ? 2.1117 2.4836 2.1105 0.2478 -0.0907 -0.2437 93 ARG A C 584 O O . ARG A 74 ? 2.2456 2.5700 2.2333 0.2727 -0.0711 -0.2502 93 ARG A O 585 C CB . ARG A 74 ? 2.1036 2.6790 2.2336 0.2868 -0.1503 -0.2761 93 ARG A CB 586 C CG . ARG A 74 ? 2.3018 2.8643 2.4406 0.3500 -0.1487 -0.2853 93 ARG A CG 587 C CD . ARG A 74 ? 2.6869 3.3356 2.8768 0.4078 -0.1953 -0.2979 93 ARG A CD 588 N NE . ARG A 74 ? 2.7133 3.4831 3.0200 0.3719 -0.1884 -0.3113 93 ARG A NE 589 C CZ . ARG A 74 ? 3.0113 3.5947 3.3597 0.2726 -0.1066 -0.1800 93 ARG A CZ 590 N NH1 . ARG A 74 ? 3.2046 3.6262 3.5233 0.2486 -0.0523 -0.1156 93 ARG A NH1 591 N NH2 . ARG A 74 ? 2.9749 3.6243 3.4044 0.2438 -0.0984 -0.1697 93 ARG A NH2 592 N N . GLU A 75 ? 2.0860 2.3909 2.0192 0.2315 -0.0932 -0.2199 94 GLU A N 593 C CA . GLU A 75 ? 2.2135 2.3853 2.0584 0.2388 -0.0706 -0.1965 94 GLU A CA 594 C C . GLU A 75 ? 2.4766 2.5732 2.2723 0.3082 -0.0807 -0.1866 94 GLU A C 595 O O . GLU A 75 ? 2.6226 2.6071 2.3625 0.3136 -0.0497 -0.1749 94 GLU A O 596 C CB . GLU A 75 ? 2.1509 2.2780 1.9387 0.2126 -0.0701 -0.1732 94 GLU A CB 597 C CG . GLU A 75 ? 2.1708 2.3308 1.9406 0.2400 -0.1138 -0.1678 94 GLU A CG 598 C CD . GLU A 75 ? 2.0647 2.2126 1.8005 0.2037 -0.1117 -0.1559 94 GLU A CD 599 O OE1 . GLU A 75 ? 2.0492 2.1266 1.7439 0.1739 -0.0750 -0.1397 94 GLU A OE1 600 O OE2 . GLU A 75 ? 2.0098 2.2197 1.7627 0.2049 -0.1458 -0.1657 94 GLU A OE2 601 N N . THR A 76 ? 2.5577 2.7182 2.3787 0.3611 -0.1237 -0.1928 95 THR A N 602 C CA . THR A 76 ? 3.0241 3.1330 2.8065 0.4402 -0.1428 -0.1835 95 THR A CA 603 C C . THR A 76 ? 3.3377 3.3929 3.1935 0.3818 -0.0802 -0.1660 95 THR A C 604 O O . THR A 76 ? 3.5406 3.4894 3.4567 0.2637 -0.0083 -0.1110 95 THR A O 605 C CB . THR A 76 ? 3.3176 3.4800 3.2469 0.3336 -0.1356 -0.1198 95 THR A CB 606 O OG1 . THR A 76 ? 2.9500 3.2486 2.8062 0.4461 -0.2238 -0.2027 95 THR A OG1 607 C CG2 . THR A 76 ? 3.5258 3.6073 3.5576 0.2088 -0.0886 -0.0163 95 THR A CG2 608 N N . THR A 77 ? 3.2527 3.4097 3.1838 0.3900 -0.0831 -0.2003 96 THR A N 609 C CA . THR A 77 ? 3.5955 3.6181 3.6675 0.1796 0.0482 -0.0955 96 THR A CA 610 C C . THR A 77 ? 3.3565 3.4181 3.2685 0.3503 -0.0081 -0.2291 96 THR A C 611 O O . THR A 77 ? 2.6825 2.8024 2.5831 0.3310 -0.0213 -0.2523 96 THR A O 612 C CB . THR A 77 ? 3.5744 3.6460 3.6982 0.1735 0.0549 -0.0841 96 THR A CB 613 O OG1 . THR A 77 ? 3.5497 3.6658 3.7306 0.1725 0.0276 -0.0502 96 THR A OG1 616 C CA . ASP A 78 ? 3.7980 3.7964 3.7976 0.0022 0.0017 -0.0025 97 ASP A CA 617 C C . ASP A 78 ? 3.7984 3.7971 3.7978 0.0017 0.0014 -0.0020 97 ASP A C 620 C CG . ASP A 78 ? 3.7983 3.7954 3.7969 0.0023 0.0018 -0.0033 97 ASP A CG 621 O OD1 . ASP A 78 ? 2.9318 2.7039 2.6656 0.2352 0.0874 -0.2340 97 ASP A OD1 623 N N . THR A 79 ? 3.7910 3.7784 3.7818 0.0134 0.0123 -0.0194 98 THR A N 624 C CA . THR A 79 ? 3.7867 3.7673 3.7689 0.0204 0.0199 -0.0314 98 THR A CA 625 C C . THR A 79 ? 3.7677 3.7375 3.7270 0.0444 0.0480 -0.0671 98 THR A C 626 O O . THR A 79 ? 3.7702 3.7534 3.7443 0.0368 0.0403 -0.0505 98 THR A O 627 C CB . THR A 79 ? 3.7900 3.7763 3.7807 0.0149 0.0134 -0.0209 98 THR A CB 628 O OG1 . THR A 79 ? 3.7974 3.7935 3.7957 0.0036 0.0029 -0.0048 98 THR A OG1 629 C CG2 . THR A 79 ? 3.7862 3.7637 3.7672 0.0219 0.0208 -0.0341 98 THR A CG2 630 N N . GLU A 80 ? 2.6442 2.7620 2.5872 0.1816 0.0909 -0.3402 99 GLU A N 631 C CA . GLU A 80 ? 2.3636 2.6068 2.3594 0.1573 0.0738 -0.3361 99 GLU A CA 632 C C . GLU A 80 ? 2.1866 2.4523 2.1787 0.0921 0.0822 -0.3322 99 GLU A C 633 O O . GLU A 80 ? 2.2274 2.4208 2.1823 0.0627 0.0984 -0.3333 99 GLU A O 634 C CB . GLU A 80 ? 2.3120 2.5847 2.3183 0.1882 0.0400 -0.3101 99 GLU A CB 635 C CG . GLU A 80 ? 2.4429 2.7588 2.4863 0.2518 0.0229 -0.3202 99 GLU A CG 636 C CD . GLU A 80 ? 2.3528 2.8056 2.4794 0.2470 0.0214 -0.3418 99 GLU A CD 637 O OE1 . GLU A 80 ? 2.1646 2.6854 2.3183 0.1980 0.0220 -0.3383 99 GLU A OE1 638 O OE2 . GLU A 80 ? 2.9325 3.4232 3.0978 0.2944 0.0220 -0.3609 99 GLU A OE2 639 N N . GLN A 81 ? 2.0051 2.3729 2.0394 0.0705 0.0721 -0.3280 100 GLN A N 640 C CA . GLN A 81 ? 1.8448 2.2500 1.8811 0.0184 0.0767 -0.3215 100 GLN A CA 641 C C . GLN A 81 ? 1.7034 2.1063 1.7334 0.0055 0.0596 -0.2903 100 GLN A C 642 O O . GLN A 81 ? 1.5611 2.0150 1.6062 -0.0258 0.0578 -0.2805 100 GLN A O 643 C CB . GLN A 81 ? 1.7845 2.2902 1.8610 0.0058 0.0832 -0.3346 100 GLN A CB 644 C CG . GLN A 81 ? 1.9311 2.4623 2.0297 0.0399 0.0953 -0.3622 100 GLN A CG 645 C CD . GLN A 81 ? 1.9061 2.5296 2.0353 0.0251 0.1106 -0.3742 100 GLN A CD 646 O OE1 . GLN A 81 ? 1.9385 2.6256 2.1143 0.0484 0.1145 -0.3819 100 GLN A OE1 647 N NE2 . GLN A 81 ? 1.8696 2.5049 1.9730 -0.0122 0.1212 -0.3766 100 GLN A NE2 648 N N . THR A 82 ? 1.7657 2.1028 1.7659 0.0333 0.0483 -0.2743 101 THR A N 649 C CA . THR A 82 ? 1.6728 1.9947 1.6537 0.0272 0.0335 -0.2475 101 THR A CA 650 C C . THR A 82 ? 1.6391 1.9069 1.5868 -0.0094 0.0521 -0.2363 101 THR A C 651 O O . THR A 82 ? 1.7284 1.9489 1.6611 -0.0223 0.0730 -0.2490 101 THR A O 652 C CB . THR A 82 ? 1.7889 2.0632 1.7401 0.0758 0.0131 -0.2351 101 THR A CB 653 O OG1 . THR A 82 ? 1.9716 2.1441 1.8743 0.0969 0.0296 -0.2336 101 THR A OG1 654 C CG2 . THR A 82 ? 1.8121 2.1633 1.8120 0.1110 -0.0109 -0.2479 101 THR A CG2 655 N N . PRO A 83 ? 1.5240 1.7998 1.4640 -0.0268 0.0462 -0.2160 102 PRO A N 656 C CA . PRO A 83 ? 1.4935 1.7316 1.4130 -0.0593 0.0658 -0.2057 102 PRO A CA 657 C C . PRO A 83 ? 1.6431 1.7753 1.5084 -0.0487 0.0821 -0.1937 102 PRO A C 658 O O . PRO A 83 ? 1.6784 1.7743 1.5373 -0.0788 0.1075 -0.1964 102 PRO A O 659 C CB . PRO A 83 ? 1.3570 1.6344 1.2839 -0.0703 0.0551 -0.1885 102 PRO A CB 660 C CG . PRO A 83 ? 1.3650 1.6604 1.2928 -0.0390 0.0287 -0.1861 102 PRO A CG 661 C CD . PRO A 83 ? 1.4297 1.7586 1.3879 -0.0206 0.0232 -0.2062 102 PRO A CD 662 N N . GLY A 84 ? 1.7520 1.8364 1.5782 -0.0061 0.0680 -0.1805 103 GLY A N 663 C CA . GLY A 84 ? 1.9297 1.9011 1.6881 0.0125 0.0843 -0.1617 103 GLY A CA 664 C C . GLY A 84 ? 1.8892 1.8297 1.6184 -0.0144 0.1036 -0.1408 103 GLY A C 665 O O . GLY A 84 ? 1.7577 1.7497 1.4966 -0.0197 0.0889 -0.1337 103 GLY A O 666 N N . GLN A 85 ? 2.0170 1.8735 1.7145 -0.0339 0.1407 -0.1334 104 GLN A N 667 C CA . GLN A 85 ? 2.0119 1.8368 1.6861 -0.0615 0.1693 -0.1148 104 GLN A CA 668 C C . GLN A 85 ? 1.8688 1.7649 1.6116 -0.1151 0.1856 -0.1326 104 GLN A C 669 O O . GLN A 85 ? 1.8546 1.7430 1.5971 -0.1417 0.2123 -0.1220 104 GLN A O 670 C CB . GLN A 85 ? 2.2612 1.9536 1.8638 -0.0551 0.2065 -0.0945 104 GLN A CB 671 C CG . GLN A 85 ? 2.4588 2.0720 1.9801 0.0068 0.1888 -0.0719 104 GLN A CG 672 C CD . GLN A 85 ? 2.4750 2.0815 1.9380 0.0321 0.1747 -0.0466 104 GLN A CD 673 O OE1 . GLN A 85 ? 2.6810 2.1905 2.0619 0.0429 0.2021 -0.0179 104 GLN A OE1 674 N NE2 . GLN A 85 ? 2.2798 1.9828 1.7775 0.0422 0.1335 -0.0576 104 GLN A NE2 675 N N . GLU A 86 ? 1.7766 1.7472 1.5767 -0.1276 0.1692 -0.1597 105 GLU A N 676 C CA . GLU A 86 ? 1.6690 1.7155 1.5302 -0.1715 0.1760 -0.1789 105 GLU A CA 677 C C . GLU A 86 ? 1.4917 1.6173 1.3817 -0.1790 0.1649 -0.1682 105 GLU A C 678 O O . GLU A 86 ? 1.4006 1.5602 1.2871 -0.1548 0.1397 -0.1596 105 GLU A O 679 C CB . GLU A 86 ? 1.6643 1.7587 1.5612 -0.1777 0.1621 -0.2106 105 GLU A CB 680 C CG . GLU A 86 ? 1.8669 1.8814 1.7448 -0.1824 0.1819 -0.2300 105 GLU A CG 681 C CD . GLU A 86 ? 1.9782 1.9507 1.8662 -0.2293 0.2164 -0.2418 105 GLU A CD 682 O OE1 . GLU A 86 ? 1.8808 1.9184 1.8104 -0.2636 0.2211 -0.2441 105 GLU A OE1 683 O OE2 . GLU A 86 ? 2.1819 2.0567 2.0402 -0.2320 0.2401 -0.2503 105 GLU A OE2 684 N N . VAL A 87 ? 1.4617 1.6163 1.3846 -0.2133 0.1853 -0.1707 106 VAL A N 685 C CA . VAL A 87 ? 1.3203 1.5475 1.2749 -0.2189 0.1796 -0.1613 106 VAL A CA 686 C C . VAL A 87 ? 1.2290 1.5518 1.2380 -0.2337 0.1598 -0.1813 106 VAL A C 687 O O . VAL A 87 ? 1.2882 1.6283 1.3238 -0.2594 0.1647 -0.2059 106 VAL A O 688 C CB . VAL A 87 ? 1.3578 1.5700 1.3205 -0.2410 0.2148 -0.1513 106 VAL A CB 689 C CG1 . VAL A 87 ? 1.2285 1.5318 1.2421 -0.2478 0.2096 -0.1491 106 VAL A CG1 690 C CG2 . VAL A 87 ? 1.4496 1.5714 1.3429 -0.2190 0.2335 -0.1253 106 VAL A CG2 691 N N . VAL A 88 ? 1.1115 1.4905 1.1310 -0.2178 0.1384 -0.1711 107 VAL A N 692 C CA . VAL A 88 ? 1.0468 1.5116 1.1040 -0.2253 0.1206 -0.1818 107 VAL A CA 693 C C . VAL A 88 ? 0.9907 1.5080 1.0813 -0.2326 0.1261 -0.1714 107 VAL A C 694 O O . VAL A 88 ? 0.9398 1.4468 1.0193 -0.2158 0.1292 -0.1497 107 VAL A O 695 C CB . VAL A 88 ? 0.9923 1.4807 1.0389 -0.2038 0.0985 -0.1761 107 VAL A CB 696 C CG1 . VAL A 88 ? 0.9631 1.5304 1.0344 -0.2101 0.0851 -0.1830 107 VAL A CG1 697 C CG2 . VAL A 88 ? 1.0569 1.5029 1.0801 -0.1913 0.0942 -0.1876 107 VAL A CG2 698 N N . LEU A 89 ? 1.0162 1.5905 1.1491 -0.2564 0.1270 -0.1901 108 LEU A N 699 C CA . LEU A 89 ? 0.9804 1.6212 1.1573 -0.2600 0.1298 -0.1839 108 LEU A CA 700 C C . LEU A 89 ? 0.9477 1.6746 1.1442 -0.2502 0.1010 -0.1862 108 LEU A C 701 O O . LEU A 89 ? 0.9931 1.7522 1.1929 -0.2628 0.0854 -0.2099 108 LEU A O 702 C CB . LEU A 89 ? 1.0541 1.7070 1.2740 -0.2949 0.1527 -0.2039 108 LEU A CB 703 C CG . LEU A 89 ? 1.0421 1.7691 1.3209 -0.2988 0.1620 -0.1996 108 LEU A CG 704 C CD1 . LEU A 89 ? 1.0126 1.6924 1.2701 -0.2779 0.1878 -0.1702 108 LEU A CD1 705 C CD2 . LEU A 89 ? 1.1322 1.8925 1.4690 -0.3427 0.1802 -0.2295 108 LEU A CD2 706 N N . SER A 90 ? 0.8925 1.6491 1.0938 -0.2250 0.0954 -0.1610 109 SER A N 707 C CA . SER A 90 ? 0.8941 1.7234 1.1037 -0.2085 0.0704 -0.1548 109 SER A CA 708 C C . SER A 90 ? 0.9365 1.8572 1.2038 -0.2202 0.0612 -0.1727 109 SER A C 709 O O . SER A 90 ? 0.9373 1.8665 1.2457 -0.2320 0.0808 -0.1769 109 SER A O 710 C CB . SER A 90 ? 0.8564 1.6708 1.0477 -0.1757 0.0711 -0.1203 109 SER A CB 711 O OG . SER A 90 ? 0.8458 1.6740 1.0685 -0.1656 0.0858 -0.1097 109 SER A OG 712 N N . PRO A 91 ? 0.9871 1.9803 1.2580 -0.2172 0.0321 -0.1850 110 PRO A N 713 C CA . PRO A 91 ? 1.0450 2.1408 1.3751 -0.2270 0.0149 -0.2070 110 PRO A CA 714 C C . PRO A 91 ? 1.0294 2.1786 1.3952 -0.1938 0.0130 -0.1802 110 PRO A C 715 O O . PRO A 91 ? 1.0570 2.2805 1.4925 -0.2039 0.0133 -0.1963 110 PRO A O 716 C CB . PRO A 91 ? 1.1242 2.2714 1.4252 -0.2236 -0.0192 -0.2233 110 PRO A CB 717 C CG . PRO A 91 ? 1.1076 2.1725 1.3421 -0.2214 -0.0106 -0.2158 110 PRO A CG 718 C CD . PRO A 91 ? 1.0132 2.0017 1.2319 -0.2048 0.0140 -0.1812 110 PRO A CD 719 N N . GLY A 92 ? 1.0026 2.1129 1.3247 -0.1548 0.0135 -0.1412 111 GLY A N 720 C CA . GLY A 92 ? 1.0113 2.1525 1.3547 -0.1147 0.0141 -0.1122 111 GLY A CA 721 C C . GLY A 92 ? 0.9575 2.0051 1.2746 -0.0998 0.0456 -0.0853 111 GLY A C 722 O O . GLY A 92 ? 0.9064 1.8834 1.2085 -0.1246 0.0687 -0.0939 111 GLY A O 723 N N . SER A 93 ? 0.9920 2.0356 1.2982 -0.0566 0.0452 -0.0533 112 SER A N 724 C CA . SER A 93 ? 0.9716 1.9290 1.2512 -0.0386 0.0730 -0.0309 112 SER A CA 725 C C . SER A 93 ? 0.9733 1.8416 1.1826 -0.0330 0.0739 -0.0107 112 SER A C 726 O O . SER A 93 ? 0.9931 1.7949 1.1773 -0.0131 0.0908 0.0088 112 SER A O 727 C CB . SER A 93 ? 1.0331 2.0294 1.3476 0.0047 0.0787 -0.0123 112 SER A CB 728 O OG . SER A 93 ? 1.1225 2.1415 1.4144 0.0445 0.0556 0.0142 112 SER A OG 729 N N . PHE A 94 ? 0.9672 1.8342 1.1479 -0.0531 0.0586 -0.0188 113 PHE A N 730 C CA . PHE A 94 ? 0.9791 1.7760 1.1057 -0.0538 0.0623 -0.0033 113 PHE A CA 731 C C . PHE A 94 ? 0.9275 1.7019 1.0387 -0.0879 0.0611 -0.0263 113 PHE A C 732 O O . PHE A 94 ? 0.9261 1.7490 1.0512 -0.1052 0.0486 -0.0490 113 PHE A O 733 C CB . PHE A 94 ? 1.0852 1.9016 1.1817 -0.0263 0.0494 0.0245 113 PHE A CB 734 C CG . PHE A 94 ? 1.1190 1.8715 1.1659 -0.0341 0.0587 0.0394 113 PHE A CG 735 C CD1 . PHE A 94 ? 1.1484 1.8196 1.1743 -0.0275 0.0788 0.0585 113 PHE A CD1 736 C CD2 . PHE A 94 ? 1.1394 1.9143 1.1638 -0.0509 0.0500 0.0306 113 PHE A CD2 737 C CE1 . PHE A 94 ? 1.1945 1.8138 1.1868 -0.0419 0.0901 0.0685 113 PHE A CE1 738 C CE2 . PHE A 94 ? 1.1821 1.9067 1.1709 -0.0610 0.0642 0.0430 113 PHE A CE2 739 C CZ . PHE A 94 ? 1.2065 1.8566 1.1839 -0.0586 0.0841 0.0618 113 PHE A CZ 740 N N . MET A 95 ? 0.9039 1.6064 0.9876 -0.0957 0.0729 -0.0223 114 MET A N 741 C CA . MET A 95 ? 0.8722 1.5529 0.9436 -0.1198 0.0715 -0.0415 114 MET A CA 742 C C . MET A 95 ? 0.8959 1.5284 0.9414 -0.1209 0.0779 -0.0291 114 MET A C 743 O O . MET A 95 ? 0.9063 1.4883 0.9433 -0.1144 0.0876 -0.0185 114 MET A O 744 C CB . MET A 95 ? 0.8190 1.4692 0.9000 -0.1343 0.0787 -0.0619 114 MET A CB 745 C CG . MET A 95 ? 0.8076 1.4397 0.8782 -0.1513 0.0747 -0.0821 114 MET A CG 746 S SD . MET A 95 ? 0.7907 1.3667 0.8538 -0.1593 0.0846 -0.0967 114 MET A SD 747 C CE . MET A 95 ? 0.8047 1.4214 0.8979 -0.1762 0.0893 -0.1146 114 MET A CE 748 N N . SER A 96 ? 0.9222 1.5718 0.9575 -0.1312 0.0748 -0.0337 115 SER A N 749 C CA . SER A 96 ? 0.9568 1.5737 0.9799 -0.1394 0.0844 -0.0264 115 SER A CA 750 C C . SER A 96 ? 0.9169 1.5332 0.9520 -0.1561 0.0809 -0.0533 115 SER A C 751 O O . SER A 96 ? 0.9120 1.5609 0.9512 -0.1600 0.0745 -0.0717 115 SER A O 752 C CB . SER A 96 ? 1.0567 1.6949 1.0574 -0.1344 0.0909 -0.0053 115 SER A CB 753 O OG . SER A 96 ? 1.1090 1.7118 1.1045 -0.1472 0.1076 0.0039 115 SER A OG 754 N N . ILE A 97 ? 0.9090 1.4875 0.9497 -0.1638 0.0835 -0.0581 116 ILE A N 755 C CA . ILE A 97 ? 0.8873 1.4682 0.9429 -0.1722 0.0763 -0.0824 116 ILE A CA 756 C C . ILE A 97 ? 0.9371 1.5234 1.0088 -0.1861 0.0842 -0.0827 116 ILE A C 757 O O . ILE A 97 ? 0.9707 1.5242 1.0418 -0.1933 0.0905 -0.0729 116 ILE A O 758 C CB . ILE A 97 ? 0.8503 1.3910 0.9002 -0.1666 0.0661 -0.0942 116 ILE A CB 759 C CG1 . ILE A 97 ? 0.8190 1.3540 0.8582 -0.1584 0.0667 -0.0935 116 ILE A CG1 760 C CG2 . ILE A 97 ? 0.8521 1.3965 0.9137 -0.1668 0.0538 -0.1166 116 ILE A CG2 761 C CD1 . ILE A 97 ? 0.8122 1.2981 0.8328 -0.1512 0.0666 -0.0952 116 ILE A CD1 762 N N . THR A 98 ? 0.9581 1.5846 1.0475 -0.1913 0.0865 -0.0970 117 THR A N 763 C CA . THR A 98 ? 1.0141 1.6597 1.1322 -0.2077 0.0980 -0.1016 117 THR A CA 764 C C . THR A 98 ? 1.0002 1.6724 1.1528 -0.2050 0.0841 -0.1311 117 THR A C 765 O O . THR A 98 ? 0.9943 1.6891 1.1462 -0.1917 0.0796 -0.1449 117 THR A O 766 C CB . THR A 98 ? 1.0978 1.7747 1.2070 -0.2144 0.1223 -0.0868 117 THR A CB 767 O OG1 . THR A 98 ? 1.1409 1.7885 1.2140 -0.2106 0.1322 -0.0553 117 THR A OG1 768 C CG2 . THR A 98 ? 1.1704 1.8730 1.3174 -0.2362 0.1427 -0.0925 117 THR A CG2 769 N N . PHE A 99 ? 1.0144 1.6845 1.1975 -0.2161 0.0762 -0.1428 118 PHE A N 770 C CA . PHE A 99 ? 1.0305 1.7394 1.2546 -0.2099 0.0597 -0.1708 118 PHE A CA 771 C C . PHE A 99 ? 1.1033 1.8657 1.3795 -0.2332 0.0808 -0.1770 118 PHE A C 772 O O . PHE A 99 ? 1.1506 1.8998 1.4403 -0.2604 0.0942 -0.1692 118 PHE A O 773 C CB . PHE A 99 ? 1.0240 1.7064 1.2482 -0.2041 0.0301 -0.1852 118 PHE A CB 774 C CG . PHE A 99 ? 1.0668 1.8035 1.3438 -0.1989 0.0097 -0.2142 118 PHE A CG 775 C CD1 . PHE A 99 ? 1.0744 1.8333 1.3553 -0.1672 -0.0055 -0.2271 118 PHE A CD1 776 C CD2 . PHE A 99 ? 1.1239 1.8914 1.4511 -0.2254 0.0063 -0.2300 118 PHE A CD2 777 C CE1 . PHE A 99 ? 1.1340 1.9518 1.4684 -0.1545 -0.0269 -0.2533 118 PHE A CE1 778 C CE2 . PHE A 99 ? 1.1716 2.0071 1.5597 -0.2194 -0.0161 -0.2601 118 PHE A CE2 779 C CZ . PHE A 99 ? 1.1781 2.0416 1.5696 -0.1804 -0.0340 -0.2705 118 PHE A CZ 780 N N . ARG A 100 ? 1.1353 1.9538 1.4411 -0.2237 0.0882 -0.1917 119 ARG A N 781 C CA . ARG A 100 ? 1.2172 2.0968 1.5798 -0.2455 0.1141 -0.1998 119 ARG A CA 782 C C . ARG A 100 ? 1.2437 2.1896 1.6721 -0.2311 0.0961 -0.2333 119 ARG A C 783 O O . ARG A 100 ? 1.2279 2.1776 1.6453 -0.1963 0.0780 -0.2454 119 ARG A O 784 C CB . ARG A 100 ? 1.2760 2.1714 1.6132 -0.2477 0.1509 -0.1841 119 ARG A CB 785 C CG . ARG A 100 ? 1.3911 2.3406 1.7776 -0.2752 0.1899 -0.1855 119 ARG A CG 786 C CD . ARG A 100 ? 1.4512 2.4666 1.8643 -0.2574 0.2050 -0.2064 119 ARG A CD 787 N NE . ARG A 100 ? 1.5716 2.6493 2.0442 -0.2842 0.2459 -0.2115 119 ARG A NE 788 C CZ . ARG A 100 ? 1.6559 2.7981 2.1573 -0.2731 0.2720 -0.2285 119 ARG A CZ 789 N NH1 . ARG A 100 ? 1.6401 2.7853 2.1121 -0.2347 0.2593 -0.2436 119 ARG A NH1 790 N NH2 . ARG A 100 ? 1.7790 2.9802 2.3396 -0.3017 0.3149 -0.2319 119 ARG A NH2 791 N N . SER A 101 ? 1.3039 2.3014 1.8034 -0.2579 0.1020 -0.2488 120 SER A N 792 C CA . SER A 101 ? 1.3498 2.4318 1.9306 -0.2466 0.0851 -0.2829 120 SER A CA 793 C C . SER A 101 ? 1.4490 2.6041 2.0977 -0.2777 0.1304 -0.2883 120 SER A C 794 O O . SER A 101 ? 1.4959 2.6384 2.1578 -0.3224 0.1574 -0.2767 120 SER A O 795 C CB . SER A 101 ? 1.3480 2.4341 1.9598 -0.2545 0.0442 -0.3030 120 SER A CB 796 O OG . SER A 101 ? 1.4082 2.5876 2.1032 -0.2388 0.0205 -0.3377 120 SER A OG 797 N N . ASP A 102 ? 1.5002 2.7241 2.1874 -0.2541 0.1445 -0.3044 121 ASP A N 798 C CA . ASP A 102 ? 1.6143 2.9133 2.3670 -0.2822 0.1945 -0.3102 121 ASP A CA 799 C C . ASP A 102 ? 1.6873 3.0784 2.5589 -0.3087 0.1863 -0.3421 121 ASP A C 800 O O . ASP A 102 ? 1.6357 3.0200 2.5258 -0.3113 0.1405 -0.3569 121 ASP A O 801 C CB . ASP A 102 ? 1.6717 3.0085 2.4170 -0.2478 0.2198 -0.3172 121 ASP A CB 802 C CG . ASP A 102 ? 1.6695 3.0561 2.4559 -0.1954 0.1862 -0.3487 121 ASP A CG 803 O OD1 . ASP A 102 ? 1.6135 3.0050 2.4266 -0.1796 0.1361 -0.3630 121 ASP A OD1 804 O OD2 . ASP A 102 ? 1.7849 3.2009 2.5704 -0.1667 0.2099 -0.3590 121 ASP A OD2 805 N N . PHE A 103 ? 2.3806 3.6179 3.2797 -0.2625 0.1964 -0.2197 122 PHE A N 806 C CA . PHE A 103 ? 2.6033 3.6903 3.5584 -0.2234 0.1543 -0.0934 122 PHE A CA 807 C C . PHE A 103 ? 2.6407 3.7196 3.6279 -0.1817 0.1058 -0.0747 122 PHE A C 808 O O . PHE A 103 ? 2.7871 3.7714 3.7961 -0.1688 0.0590 0.0098 122 PHE A O 809 C CB . PHE A 103 ? 2.8559 3.7671 3.7677 -0.1749 0.1733 0.0321 122 PHE A CB 810 C CG . PHE A 103 ? 2.9031 3.7586 3.7530 -0.1916 0.2044 0.0437 122 PHE A CG 811 C CD1 . PHE A 103 ? 2.8129 3.7404 3.6697 -0.2068 0.2682 0.0262 122 PHE A CD1 812 C CD2 . PHE A 103 ? 3.0691 3.7544 3.7637 -0.1816 0.1619 0.0403 122 PHE A CD2 813 C CE1 . PHE A 103 ? 2.8932 3.7512 3.7024 -0.2092 0.2968 0.0685 122 PHE A CE1 814 C CE2 . PHE A 103 ? 3.1288 3.7487 3.7521 -0.1846 0.1783 0.0491 122 PHE A CE2 815 C CZ . PHE A 103 ? 3.0771 3.7483 3.7259 -0.1923 0.2307 0.0614 122 PHE A CZ 816 N N . SER A 104 ? 2.5867 3.7074 3.5455 -0.1513 0.1104 -0.1199 123 SER A N 817 C CA . SER A 104 ? 2.6597 3.7391 3.6312 -0.1050 0.0724 -0.0845 123 SER A CA 818 C C . SER A 104 ? 2.5622 3.7021 3.5066 -0.0990 0.0233 -0.1599 123 SER A C 819 O O . SER A 104 ? 2.4484 3.6658 3.3533 -0.0787 0.0273 -0.2384 123 SER A O 820 C CB . SER A 104 ? 2.7615 3.7714 3.7064 -0.0587 0.1063 -0.0392 123 SER A CB 821 O OG . SER A 104 ? 3.1278 3.7992 3.7947 -0.0158 0.0573 0.0014 123 SER A OG 822 N N . ASN A 105 ? 2.5804 3.7081 3.5481 -0.1128 -0.0249 -0.1449 124 ASN A N 823 C CA . ASN A 105 ? 2.5297 3.6851 3.4612 -0.0961 -0.0763 -0.1949 124 ASN A CA 824 C C . ASN A 105 ? 2.6982 3.7438 3.6353 -0.0710 -0.1188 -0.0957 124 ASN A C 825 O O . ASN A 105 ? 2.7512 3.7578 3.6740 -0.0860 -0.1658 -0.0723 124 ASN A O 826 C CB . ASN A 105 ? 2.3424 3.6201 3.2744 -0.1402 -0.0925 -0.3025 124 ASN A CB 827 C CG . ASN A 105 ? 1.8579 3.3106 2.7616 -0.1126 -0.1226 -0.4444 124 ASN A CG 828 O OD1 . ASN A 105 ? 1.6973 3.1080 2.5466 -0.0611 -0.1231 -0.4301 124 ASN A OD1 829 N ND2 . ASN A 105 ? 1.6359 3.0313 2.4931 -0.1338 -0.1515 -0.4430 124 ASN A ND2 830 N N . GLU A 106 ? 2.8662 3.7979 3.7899 -0.0396 -0.0951 -0.0040 125 GLU A N 831 C CA . GLU A 106 ? 3.1474 3.7993 3.7900 -0.0118 -0.0789 -0.0014 125 GLU A CA 832 C C . GLU A 106 ? 3.1219 3.7995 3.7787 -0.0023 -0.1189 -0.0004 125 GLU A C 833 O O . GLU A 106 ? 3.1958 3.7994 3.7709 -0.0105 -0.1316 -0.0023 125 GLU A O 834 C CB . GLU A 106 ? 3.2426 3.7993 3.7962 0.0108 -0.0431 0.0008 125 GLU A CB 835 C CG . GLU A 106 ? 3.2965 3.7995 3.7991 0.0035 -0.0146 0.0001 125 GLU A CG 836 C CD . GLU A 106 ? 3.3258 3.7995 3.7991 -0.0010 -0.0152 0.0000 125 GLU A CD 837 O OE1 . GLU A 106 ? 3.3081 3.7993 3.7973 -0.0118 -0.0331 -0.0008 125 GLU A OE1 838 O OE2 . GLU A 106 ? 3.3475 3.7995 3.7995 0.0053 0.0008 0.0000 125 GLU A OE2 839 N N . GLU A 107 ? 2.9494 3.7991 3.7738 0.0203 -0.1478 0.0035 126 GLU A N 840 C CA . GLU A 107 ? 2.9005 3.7680 3.6701 0.0470 -0.1865 -0.0416 126 GLU A CA 841 C C . GLU A 107 ? 2.7358 3.7129 3.4866 0.0373 -0.2213 -0.1431 126 GLU A C 842 O O . GLU A 107 ? 2.5968 3.6770 3.3791 0.0162 -0.2000 -0.2149 126 GLU A O 843 C CB . GLU A 107 ? 2.8575 3.7311 3.5795 0.0956 -0.1639 -0.0894 126 GLU A CB 844 C CG . GLU A 107 ? 3.0924 3.7872 3.7812 0.0933 -0.1138 0.0150 126 GLU A CG 845 C CD . GLU A 107 ? 3.0748 3.7602 3.7364 0.1327 -0.0939 -0.0106 126 GLU A CD 846 O OE1 . GLU A 107 ? 3.0200 3.7206 3.6207 0.1603 -0.1233 -0.0602 126 GLU A OE1 847 O OE2 . GLU A 107 ? 3.3033 3.7783 3.7972 0.1028 -0.0340 0.0070 126 GLU A OE2 848 N N . ARG A 108 ? 2.7769 3.7144 3.4713 0.0423 -0.2658 -0.1359 127 ARG A N 849 C CA . ARG A 108 ? 2.6771 3.6753 3.3380 0.0308 -0.2967 -0.2093 127 ARG A CA 850 C C . ARG A 108 ? 2.4209 3.5804 3.0345 0.1050 -0.3182 -0.3579 127 ARG A C 851 O O . ARG A 108 ? 2.5765 3.6020 3.0925 0.1233 -0.3437 -0.3015 127 ARG A O 852 C CB . ARG A 108 ? 2.8339 3.7275 3.4692 -0.0091 -0.3371 -0.1269 127 ARG A CB 853 C CG . ARG A 108 ? 2.8940 3.7610 3.5804 -0.0703 -0.3380 -0.0817 127 ARG A CG 854 C CD . ARG A 108 ? 2.8636 3.7671 3.6364 -0.0814 -0.2938 -0.0680 127 ARG A CD 855 N NE . ARG A 108 ? 2.9759 3.7831 3.7129 -0.1162 -0.2671 -0.0377 127 ARG A NE 856 C CZ . ARG A 108 ? 2.8343 3.7489 3.6500 -0.1597 -0.2870 -0.0869 127 ARG A CZ 857 N NH1 . ARG A 108 ? 2.6062 3.6634 3.4106 -0.1480 -0.2707 -0.2300 127 ARG A NH1 858 N NH2 . ARG A 108 ? 2.9888 3.7635 3.7241 -0.1711 -0.2472 -0.0522 127 ARG A NH2 859 N N . PHE A 109 ? 1.7772 3.0030 2.3937 0.0964 -0.2775 -0.4116 128 PHE A N 860 C CA . PHE A 109 ? 1.7200 2.8068 2.2151 0.1037 -0.2593 -0.3757 128 PHE A CA 861 C C . PHE A 109 ? 1.6567 2.6807 2.0915 0.0659 -0.2686 -0.3676 128 PHE A C 862 O O . PHE A 109 ? 1.5949 2.6545 2.0768 0.0107 -0.2562 -0.3795 128 PHE A O 863 C CB . PHE A 109 ? 1.6343 2.6886 2.1241 0.0830 -0.2011 -0.3588 128 PHE A CB 864 C CG . PHE A 109 ? 1.7184 2.8225 2.2565 0.1227 -0.1875 -0.3696 128 PHE A CG 865 C CD1 . PHE A 109 ? 1.8231 2.8623 2.3031 0.1831 -0.1964 -0.3590 128 PHE A CD1 866 C CD2 . PHE A 109 ? 1.7186 2.9288 2.3579 0.1006 -0.1613 -0.3905 128 PHE A CD2 867 C CE1 . PHE A 109 ? 1.9256 3.0029 2.4479 0.2235 -0.1815 -0.3716 128 PHE A CE1 868 C CE2 . PHE A 109 ? 1.8121 3.0685 2.4947 0.1407 -0.1449 -0.4030 128 PHE A CE2 869 C CZ . PHE A 109 ? 1.9996 3.1883 2.6235 0.2034 -0.1562 -0.3948 128 PHE A CZ 870 N N . THR A 110 ? 1.6953 2.6215 2.0239 0.0972 -0.2873 -0.3476 129 THR A N 871 C CA . THR A 110 ? 1.6748 2.5336 1.9321 0.0737 -0.2976 -0.3408 129 THR A CA 872 C C . THR A 110 ? 1.5430 2.3225 1.7555 0.0304 -0.2497 -0.3155 129 THR A C 873 O O . THR A 110 ? 1.5311 2.2544 1.6878 0.0122 -0.2526 -0.3105 129 THR A O 874 C CB . THR A 110 ? 1.8176 2.6184 1.9819 0.1286 -0.3398 -0.3333 129 THR A CB 875 O OG1 . THR A 110 ? 1.8526 2.5749 1.9534 0.1690 -0.3192 -0.3033 129 THR A OG1 876 C CG2 . THR A 110 ? 1.9620 2.8574 2.1740 0.1657 -0.4000 -0.3647 129 THR A CG2 877 N N . GLY A 111 ? 1.4596 2.2381 1.6954 0.0169 -0.2071 -0.3019 130 GLY A N 878 C CA . GLY A 111 ? 1.3456 2.0673 1.5500 -0.0203 -0.1653 -0.2795 130 GLY A CA 879 C C . GLY A 111 ? 1.3414 1.9618 1.4534 -0.0033 -0.1524 -0.2528 130 GLY A C 880 O O . GLY A 111 ? 1.4124 1.9991 1.4907 0.0345 -0.1556 -0.2454 130 GLY A O 881 N N . PHE A 112 ? 1.2730 1.8436 1.3475 -0.0319 -0.1336 -0.2384 131 PHE A N 882 C CA . PHE A 112 ? 1.2644 1.7504 1.2654 -0.0243 -0.1135 -0.2143 131 PHE A CA 883 C C . PHE A 112 ? 1.2640 1.6948 1.2093 -0.0347 -0.1128 -0.2063 131 PHE A C 884 O O . PHE A 112 ? 1.2511 1.7024 1.2161 -0.0565 -0.1216 -0.2186 131 PHE A O 885 C CB . PHE A 112 ? 1.1739 1.6625 1.1949 -0.0466 -0.0758 -0.2022 131 PHE A CB 886 C CG . PHE A 112 ? 1.0849 1.5921 1.1305 -0.0846 -0.0567 -0.1967 131 PHE A CG 887 C CD1 . PHE A 112 ? 1.0621 1.6338 1.1698 -0.1063 -0.0535 -0.2074 131 PHE A CD1 888 C CD2 . PHE A 112 ? 1.0434 1.5013 1.0497 -0.0961 -0.0389 -0.1794 131 PHE A CD2 889 C CE1 . PHE A 112 ? 1.0134 1.5874 1.1334 -0.1376 -0.0332 -0.1974 131 PHE A CE1 890 C CE2 . PHE A 112 ? 0.9851 1.4538 1.0099 -0.1228 -0.0223 -0.1716 131 PHE A CE2 891 C CZ . PHE A 112 ? 0.9787 1.4992 1.0553 -0.1427 -0.0196 -0.1790 131 PHE A CZ 892 N N . ASP A 113 ? 1.2926 1.6498 1.1702 -0.0216 -0.0962 -0.1863 132 ASP A N 893 C CA . ASP A 113 ? 1.3056 1.6041 1.1243 -0.0276 -0.0845 -0.1757 132 ASP A CA 894 C C . ASP A 113 ? 1.2500 1.5132 1.0562 -0.0391 -0.0441 -0.1542 132 ASP A C 895 O O . ASP A 113 ? 1.3000 1.5285 1.0805 -0.0243 -0.0329 -0.1440 132 ASP A O 896 C CB . ASP A 113 ? 1.4587 1.7050 1.1974 0.0068 -0.1086 -0.1759 132 ASP A CB 897 C CG . ASP A 113 ? 1.5049 1.6848 1.1722 0.0043 -0.0904 -0.1653 132 ASP A CG 898 O OD1 . ASP A 113 ? 1.4345 1.6230 1.1239 -0.0229 -0.0757 -0.1694 132 ASP A OD1 899 O OD2 . ASP A 113 ? 1.6347 1.7498 1.2202 0.0319 -0.0882 -0.1520 132 ASP A OD2 900 N N . ALA A 114 ? 1.1600 1.4343 0.9890 -0.0655 -0.0224 -0.1487 133 ALA A N 901 C CA . ALA A 114 ? 1.1057 1.3685 0.9390 -0.0784 0.0115 -0.1328 133 ALA A CA 902 C C . ALA A 114 ? 1.1114 1.3373 0.9124 -0.0823 0.0329 -0.1221 133 ALA A C 903 O O . ALA A 114 ? 1.1290 1.3451 0.9159 -0.0824 0.0246 -0.1282 133 ALA A O 904 C CB . ALA A 114 ? 1.0074 1.3313 0.9046 -0.0994 0.0189 -0.1343 133 ALA A CB 905 N N . HIS A 115 ? 1.1118 1.3178 0.9041 -0.0867 0.0626 -0.1091 134 HIS A N 906 C CA . HIS A 115 ? 1.1263 1.3059 0.8970 -0.0884 0.0903 -0.0987 134 HIS A CA 907 C C . HIS A 115 ? 1.0521 1.2738 0.8757 -0.1064 0.1148 -0.0917 134 HIS A C 908 O O . HIS A 115 ? 1.0415 1.2805 0.8893 -0.1169 0.1193 -0.0937 134 HIS A O 909 C CB . HIS A 115 ? 1.2573 1.3658 0.9542 -0.0726 0.1055 -0.0905 134 HIS A CB 910 C CG . HIS A 115 ? 1.3617 1.4314 0.9959 -0.0492 0.0763 -0.0980 134 HIS A CG 911 N ND1 . HIS A 115 ? 1.4052 1.4790 1.0343 -0.0348 0.0451 -0.1048 134 HIS A ND1 912 C CD2 . HIS A 115 ? 1.4425 1.4739 1.0180 -0.0361 0.0723 -0.1025 134 HIS A CD2 913 C CE1 . HIS A 115 ? 1.5053 1.5514 1.0772 -0.0136 0.0190 -0.1130 134 HIS A CE1 914 N NE2 . HIS A 115 ? 1.5416 1.5583 1.0754 -0.0152 0.0340 -0.1132 134 HIS A NE2 915 N N . TYR A 116 ? 1.0198 1.2589 0.8616 -0.1080 0.1288 -0.0861 135 TYR A N 916 C CA . TYR A 116 ? 0.9651 1.2565 0.8606 -0.1192 0.1468 -0.0803 135 TYR A CA 917 C C . TYR A 116 ? 1.0034 1.2844 0.8943 -0.1116 0.1772 -0.0721 135 TYR A C 918 O O . TYR A 116 ? 1.0613 1.2942 0.9061 -0.0968 0.1827 -0.0713 135 TYR A O 919 C CB . TYR A 116 ? 0.8906 1.2379 0.8305 -0.1228 0.1293 -0.0796 135 TYR A CB 920 C CG . TYR A 116 ? 0.9050 1.2370 0.8357 -0.1111 0.1281 -0.0735 135 TYR A CG 921 C CD1 . TYR A 116 ? 0.9177 1.2625 0.8651 -0.1001 0.1470 -0.0627 135 TYR A CD1 922 C CD2 . TYR A 116 ? 0.9282 1.2332 0.8380 -0.1112 0.1092 -0.0809 135 TYR A CD2 923 C CE1 . TYR A 116 ? 0.9624 1.2776 0.8958 -0.0868 0.1495 -0.0576 135 TYR A CE1 924 C CE2 . TYR A 116 ? 0.9619 1.2420 0.8631 -0.1057 0.1113 -0.0786 135 TYR A CE2 925 C CZ . TYR A 116 ? 0.9887 1.2665 0.8969 -0.0923 0.1326 -0.0660 135 TYR A CZ 926 O OH . TYR A 116 ? 1.0588 1.2973 0.9529 -0.0844 0.1379 -0.0642 135 TYR A OH 927 N N . MET A 117 ? 0.9815 1.3139 0.9239 -0.1214 0.1963 -0.0694 136 MET A N 928 C CA . MET A 117 ? 1.0262 1.3704 0.9846 -0.1131 0.2281 -0.0630 136 MET A CA 929 C C . MET A 117 ? 0.9733 1.4071 1.0111 -0.1217 0.2319 -0.0638 136 MET A C 930 O O . MET A 117 ? 0.9382 1.4131 1.0090 -0.1417 0.2178 -0.0725 136 MET A O 931 C CB . MET A 117 ? 1.1217 1.4119 1.0384 -0.1168 0.2633 -0.0611 136 MET A CB 932 C CG . MET A 117 ? 1.1490 1.4620 1.1016 -0.1448 0.2826 -0.0651 136 MET A CG 933 S SD . MET A 117 ? 1.3204 1.5322 1.1916 -0.1509 0.3072 -0.0591 136 MET A SD 934 C CE . MET A 117 ? 1.2647 1.4311 1.0771 -0.1322 0.2578 -0.0618 136 MET A CE 935 N N . ALA A 118 ? 0.9937 1.4592 1.0613 -0.1044 0.2510 -0.0574 137 ALA A N 936 C CA . ALA A 118 ? 0.9724 1.5348 1.1207 -0.1063 0.2535 -0.0592 137 ALA A CA 937 C C . ALA A 118 ? 1.0141 1.5981 1.1961 -0.1350 0.2843 -0.0701 137 ALA A C 938 O O . ALA A 118 ? 1.0852 1.6083 1.2276 -0.1380 0.3186 -0.0673 137 ALA A O 939 C CB . ALA A 118 ? 1.0044 1.5898 1.1734 -0.0716 0.2663 -0.0483 137 ALA A CB 940 N N . VAL A 119 ? 0.9919 1.6565 1.2408 -0.1584 0.2729 -0.0838 138 VAL A N 941 C CA . VAL A 119 ? 1.0488 1.7419 1.3447 -0.1948 0.3025 -0.0990 138 VAL A CA 942 C C . VAL A 119 ? 1.0463 1.8663 1.4431 -0.1951 0.2996 -0.1097 138 VAL A C 943 O O . VAL A 119 ? 1.0009 1.8890 1.4272 -0.1849 0.2594 -0.1139 138 VAL A O 944 C CB . VAL A 119 ? 1.0577 1.7192 1.3373 -0.2305 0.2907 -0.1144 138 VAL A CB 945 C CG1 . VAL A 119 ? 1.1443 1.8317 1.4789 -0.2744 0.3244 -0.1329 138 VAL A CG1 946 C CG2 . VAL A 119 ? 1.0789 1.6225 1.2627 -0.2224 0.2914 -0.1029 138 VAL A CG2 947 N N . ASP A 120 ? 0.9298 1.6178 1.0190 -0.0429 0.1432 0.3083 139 ASP A N 948 C CA . ASP A 120 ? 0.9215 1.5757 1.0097 -0.0456 0.1258 0.2889 139 ASP A CA 949 C C . ASP A 120 ? 0.9666 1.5949 1.0435 -0.0287 0.1218 0.2717 139 ASP A C 950 O O . ASP A 120 ? 1.0156 1.6381 1.1029 -0.0148 0.1282 0.2690 139 ASP A O 951 C CB . ASP A 120 ? 0.9111 1.5561 1.0322 -0.0545 0.1202 0.2842 139 ASP A CB 952 C CG . ASP A 120 ? 0.9078 1.5215 1.0290 -0.0566 0.1025 0.2659 139 ASP A CG 953 O OD1 . ASP A 120 ? 0.8835 1.4887 0.9843 -0.0627 0.0910 0.2610 139 ASP A OD1 954 O OD2 . ASP A 120 ? 0.9307 1.5281 1.0718 -0.0531 0.0983 0.2581 139 ASP A OD2 955 N N . VAL A 121 ? 0.9624 1.5723 1.0179 -0.0301 0.1086 0.2597 140 VAL A N 956 C CA . VAL A 121 ? 1.0125 1.5935 1.0541 -0.0155 0.1013 0.2411 140 VAL A CA 957 C C . VAL A 121 ? 1.0136 1.5594 1.0799 -0.0205 0.0891 0.2293 140 VAL A C 958 O O . VAL A 121 ? 0.9672 1.5102 1.0459 -0.0360 0.0807 0.2297 140 VAL A O 959 C CB . VAL A 121 ? 1.0143 1.5954 1.0241 -0.0182 0.0916 0.2356 140 VAL A CB 960 C CG1 . VAL A 121 ? 1.0667 1.6123 1.0636 -0.0059 0.0810 0.2138 140 VAL A CG1 961 C CG2 . VAL A 121 ? 1.0251 1.6500 1.0101 -0.0137 0.1018 0.2507 140 VAL A CG2 962 N N . ASP A 122 ? 1.0761 1.5964 1.1487 -0.0072 0.0857 0.2199 141 ASP A N 963 C CA . ASP A 122 ? 1.0900 1.5787 1.1836 -0.0140 0.0707 0.2124 141 ASP A CA 964 C C . ASP A 122 ? 1.1179 1.5718 1.1865 -0.0089 0.0563 0.1947 141 ASP A C 965 O O . ASP A 122 ? 1.1934 1.6203 1.2484 0.0076 0.0504 0.1833 141 ASP A O 966 C CB . ASP A 122 ? 1.1554 1.6323 1.2725 -0.0071 0.0689 0.2159 141 ASP A CB 967 C CG . ASP A 122 ? 1.1719 1.6256 1.3148 -0.0191 0.0511 0.2153 141 ASP A CG 968 O OD1 . ASP A 122 ? 1.1423 1.5788 1.2786 -0.0270 0.0391 0.2070 141 ASP A OD1 969 O OD2 . ASP A 122 ? 1.2223 1.6773 1.3924 -0.0216 0.0478 0.2251 141 ASP A OD2 970 N N . GLU A 123 ? 1.0686 1.5214 1.1305 -0.0224 0.0489 0.1916 142 GLU A N 971 C CA . GLU A 123 ? 1.0959 1.5189 1.1353 -0.0213 0.0353 0.1765 142 GLU A CA 972 C C . GLU A 123 ? 1.1470 1.5275 1.1945 -0.0186 0.0199 0.1666 142 GLU A C 973 O O . GLU A 123 ? 1.2016 1.5531 1.2257 -0.0104 0.0104 0.1528 142 GLU A O 974 C CB . GLU A 123 ? 1.0415 1.4709 1.0767 -0.0382 0.0279 0.1770 142 GLU A CB 975 C CG . GLU A 123 ? 1.0116 1.4762 1.0317 -0.0427 0.0361 0.1878 142 GLU A CG 976 C CD . GLU A 123 ? 0.9579 1.4497 0.9982 -0.0525 0.0426 0.2024 142 GLU A CD 977 O OE1 . GLU A 123 ? 0.9477 1.4412 1.0159 -0.0528 0.0463 0.2053 142 GLU A OE1 978 O OE2 . GLU A 123 ? 0.9405 1.4538 0.9679 -0.0608 0.0423 0.2121 142 GLU A OE2 979 N N . CYS A 124 ? 1.1414 1.5203 1.2211 -0.0258 0.0161 0.1753 143 CYS A N 980 C CA . CYS A 124 ? 1.1983 1.5394 1.2886 -0.0272 -0.0025 0.1719 143 CYS A CA 981 C C . CYS A 124 ? 1.3059 1.6097 1.3802 -0.0077 -0.0111 0.1623 143 CYS A C 982 O O . CYS A 124 ? 1.3706 1.6321 1.4389 -0.0085 -0.0314 0.1548 143 CYS A O 983 C CB . CYS A 124 ? 1.1700 1.5295 1.3003 -0.0429 -0.0067 0.1877 143 CYS A CB 984 S SG . CYS A 124 ? 1.0900 1.4862 1.2367 -0.0602 -0.0036 0.1931 143 CYS A SG 985 N N . LYS A 125 ? 1.7929 2.1105 1.8595 0.0105 0.0019 0.1625 144 LYS A N 986 C CA . LYS A 125 ? 2.1462 2.4316 2.1979 0.0345 -0.0067 0.1518 144 LYS A CA 987 C C . LYS A 125 ? 2.3489 2.6272 2.3566 0.0599 -0.0032 0.1317 144 LYS A C 988 O O . LYS A 125 ? 3.1289 3.3822 3.1193 0.0852 -0.0109 0.1188 144 LYS A O 989 C CB . LYS A 125 ? 2.4158 2.7258 2.4883 0.0412 0.0049 0.1647 144 LYS A CB 990 C CG . LYS A 125 ? 2.5696 2.8880 2.6859 0.0198 -0.0014 0.1846 144 LYS A CG 991 C CD . LYS A 125 ? 2.9858 3.2652 3.1133 0.0273 -0.0232 0.1856 144 LYS A CD 992 C CE . LYS A 125 ? 3.0655 3.3631 3.2386 0.0034 -0.0305 0.2094 144 LYS A CE 993 N NZ . LYS A 125 ? 3.2733 3.6207 3.4683 0.0015 -0.0075 0.2245 144 LYS A NZ 994 N N . GLU A 126 ? 2.2030 2.5071 2.1936 0.0531 0.0068 0.1298 145 GLU A N 995 C CA . GLU A 126 ? 2.2532 2.5687 2.2049 0.0702 0.0118 0.1159 145 GLU A CA 996 C C . GLU A 126 ? 2.2004 2.4910 2.1368 0.0586 -0.0021 0.1052 145 GLU A C 997 O O . GLU A 126 ? 2.2574 2.5369 2.1612 0.0750 -0.0075 0.0883 145 GLU A O 998 C CB . GLU A 126 ? 2.2062 2.5836 2.1543 0.0661 0.0341 0.1301 145 GLU A CB 999 C CG . GLU A 126 ? 2.4598 2.8685 2.4079 0.0857 0.0499 0.1369 145 GLU A CG 1000 C CD . GLU A 126 ? 2.4844 2.8993 2.4696 0.0751 0.0562 0.1539 145 GLU A CD 1001 O OE1 . GLU A 126 ? 2.3112 2.7594 2.3134 0.0546 0.0672 0.1717 145 GLU A OE1 1002 O OE2 . GLU A 126 ? 2.7708 3.1579 2.7672 0.0877 0.0484 0.1496 145 GLU A OE2 1003 N N . ARG A 127 ? 2.1095 2.3950 2.0694 0.0314 -0.0078 0.1151 146 ARG A N 1004 C CA . ARG A 127 ? 2.3027 2.5666 2.2553 0.0159 -0.0210 0.1088 146 ARG A CA 1005 C C . ARG A 127 ? 2.5214 2.7315 2.4542 0.0256 -0.0412 0.0913 146 ARG A C 1006 O O . ARG A 127 ? 2.6961 2.8955 2.6083 0.0213 -0.0481 0.0816 146 ARG A O 1007 C CB . ARG A 127 ? 2.3376 2.6054 2.3233 -0.0095 -0.0249 0.1223 146 ARG A CB 1008 C CG . ARG A 127 ? 2.7993 3.1060 2.7873 -0.0238 -0.0151 0.1307 146 ARG A CG 1009 C CD . ARG A 127 ? 3.0169 3.3286 3.0352 -0.0430 -0.0203 0.1402 146 ARG A CD 1010 N NE . ARG A 127 ? 3.1090 3.4514 3.1531 -0.0443 -0.0086 0.1539 146 ARG A NE 1011 C CZ . ARG A 127 ? 2.8914 3.2457 2.9651 -0.0562 -0.0117 0.1625 146 ARG A CZ 1012 N NH1 . ARG A 127 ? 2.8602 3.1988 2.9417 -0.0668 -0.0262 0.1595 146 ARG A NH1 1013 N NH2 . ARG A 127 ? 2.7517 3.1380 2.8474 -0.0569 -0.0004 0.1746 146 ARG A NH2 1014 N N . GLU A 128 ? 2.8664 3.0411 2.8049 0.0376 -0.0530 0.0880 147 GLU A N 1015 C CA . GLU A 128 ? 3.7881 3.7953 3.7691 0.0070 -0.0186 0.0114 147 GLU A CA 1018 C CB . GLU A 128 ? 3.2827 3.3618 3.2225 0.0491 -0.0951 0.0790 147 GLU A CB 1019 C CG . GLU A 128 ? 2.9041 2.9752 2.8783 0.0183 -0.1076 0.0983 147 GLU A CG 1020 C CD . GLU A 128 ? 2.5568 2.6817 2.5684 0.0010 -0.0892 0.1196 147 GLU A CD 1021 O OE1 . GLU A 128 ? 2.2006 2.3645 2.2130 -0.0074 -0.0715 0.1218 147 GLU A OE1 1022 O OE2 . GLU A 128 ? 2.8267 2.9541 2.8667 -0.0047 -0.0952 0.1344 147 GLU A OE2 1030 O OD2 . ASP A 129 ? 3.5585 3.7256 3.4413 0.1315 -0.0393 0.0489 148 ASP A OD2 1037 C CD . GLU A 130 ? 3.7995 3.7991 3.7898 -0.0001 0.0003 0.0020 149 GLU A CD 1038 O OE1 . GLU A 130 ? 3.7995 3.7975 3.7558 -0.0004 0.0017 0.0094 149 GLU A OE1 1039 O OE2 . GLU A 130 ? 3.6986 3.7876 3.5820 0.0051 0.0119 0.0496 149 GLU A OE2 1040 N N . GLU A 131 ? 1.8125 2.0390 1.6590 0.0072 -0.0542 0.0618 150 GLU A N 1041 C CA . GLU A 131 ? 1.8446 2.0405 1.6847 -0.0092 -0.0701 0.0555 150 GLU A CA 1042 C C . GLU A 131 ? 1.7285 1.8862 1.5960 -0.0311 -0.0837 0.0622 150 GLU A C 1043 O O . GLU A 131 ? 1.8056 1.9166 1.6679 -0.0256 -0.0978 0.0538 150 GLU A O 1044 C CB . GLU A 131 ? 1.7299 1.9625 1.5514 -0.0194 -0.0684 0.0566 150 GLU A CB 1045 C CG . GLU A 131 ? 1.9025 2.1689 1.6894 0.0034 -0.0613 0.0465 150 GLU A CG 1046 C CD . GLU A 131 ? 1.9032 2.2247 1.6885 0.0177 -0.0430 0.0565 150 GLU A CD 1047 O OE1 . GLU A 131 ? 1.7474 2.1028 1.5505 -0.0004 -0.0362 0.0762 150 GLU A OE1 1048 O OE2 . GLU A 131 ? 2.0715 2.4010 1.8366 0.0483 -0.0370 0.0444 150 GLU A OE2 1049 N N . LEU A 132 ? 2.4482 2.6198 2.3381 -0.0550 -0.0849 0.0744 151 LEU A N 1050 C CA . LEU A 132 ? 2.2534 2.4640 2.1609 -0.0697 -0.0776 0.0879 151 LEU A CA 1051 C C . LEU A 132 ? 2.1199 2.3455 2.0554 -0.0669 -0.0681 0.0990 151 LEU A C 1052 O O . LEU A 132 ? 2.0224 2.2846 1.9660 -0.0688 -0.0574 0.1088 151 LEU A O 1053 C CB . LEU A 132 ? 2.2965 2.5477 2.1853 -0.0728 -0.0719 0.0911 151 LEU A CB 1054 C CG . LEU A 132 ? 2.4317 2.6781 2.3005 -0.0847 -0.0840 0.0852 151 LEU A CG 1055 C CD1 . LEU A 132 ? 2.5160 2.8113 2.3657 -0.0862 -0.0790 0.0920 151 LEU A CD1 1056 C CD2 . LEU A 132 ? 2.3279 2.5576 2.2151 -0.1081 -0.0981 0.0896 151 LEU A CD2 1057 N N . SER A 133 ? 1.3347 1.5314 1.2849 -0.0640 -0.0745 0.0990 152 SER A N 1058 C CA . SER A 133 ? 1.2834 1.4915 1.2621 -0.0624 -0.0688 0.1101 152 SER A CA 1059 C C . SER A 133 ? 1.2369 1.4376 1.2436 -0.0786 -0.0803 0.1185 152 SER A C 1060 O O . SER A 133 ? 1.2522 1.4296 1.2534 -0.0887 -0.0937 0.1145 152 SER A O 1061 C CB . SER A 133 ? 1.3559 1.5411 1.3277 -0.0445 -0.0701 0.1055 152 SER A CB 1062 O OG . SER A 133 ? 1.4338 1.5697 1.3949 -0.0446 -0.0897 0.0975 152 SER A OG 1063 N N . CYS A 134 ? 1.1834 1.4088 1.2203 -0.0809 -0.0749 0.1312 153 CYS A N 1064 C CA . CYS A 134 ? 1.1462 1.3799 1.2123 -0.0941 -0.0844 0.1417 153 CYS A CA 1065 C C . CYS A 134 ? 1.1996 1.3935 1.2642 -0.1002 -0.1039 0.1430 153 CYS A C 1066 O O . CYS A 134 ? 1.2656 1.4303 1.3217 -0.0927 -0.1104 0.1419 153 CYS A O 1067 C CB . CYS A 134 ? 1.1070 1.3781 1.2036 -0.0934 -0.0753 0.1555 153 CYS A CB 1068 S SG . CYS A 134 ? 1.0470 1.3644 1.1469 -0.0890 -0.0556 0.1566 153 CYS A SG 1069 N N . ASP A 135 ? 1.1819 1.3726 1.2534 -0.1134 -0.1155 0.1455 154 ASP A N 1070 C CA . ASP A 135 ? 1.2324 1.3870 1.3025 -0.1230 -0.1362 0.1502 154 ASP A CA 1071 C C . ASP A 135 ? 1.2549 1.4166 1.3511 -0.1280 -0.1458 0.1688 154 ASP A C 1072 O O . ASP A 135 ? 1.3294 1.4498 1.4159 -0.1280 -0.1619 0.1710 154 ASP A O 1073 C CB . ASP A 135 ? 1.2067 1.3658 1.2817 -0.1365 -0.1449 0.1515 154 ASP A CB 1074 C CG . ASP A 135 ? 1.2619 1.3797 1.3286 -0.1481 -0.1665 0.1557 154 ASP A CG 1075 O OD1 . ASP A 135 ? 1.3320 1.4093 1.3842 -0.1451 -0.1775 0.1551 154 ASP A OD1 1076 O OD2 . ASP A 135 ? 1.2432 1.3670 1.3163 -0.1595 -0.1740 0.1592 154 ASP A OD2 1077 N N . HIS A 136 ? 1.1987 1.4133 1.3270 -0.1319 -0.1380 0.1823 155 HIS A N 1078 C CA . HIS A 136 ? 1.2258 1.4606 1.3833 -0.1396 -0.1471 0.2038 155 HIS A CA 1079 C C . HIS A 136 ? 1.2172 1.4802 1.3882 -0.1303 -0.1315 0.2073 155 HIS A C 1080 O O . HIS A 136 ? 1.2748 1.5069 1.4358 -0.1231 -0.1348 0.2055 155 HIS A O 1081 C CB . HIS A 136 ? 1.1933 1.4747 1.3800 -0.1531 -0.1541 0.2207 155 HIS A CB 1082 C CG . HIS A 136 ? 1.2187 1.4730 1.3977 -0.1659 -0.1742 0.2252 155 HIS A CG 1083 N ND1 . HIS A 136 ? 1.1961 1.4938 1.3980 -0.1765 -0.1812 0.2399 155 HIS A ND1 1084 C CD2 . HIS A 136 ? 1.2742 1.4658 1.4247 -0.1687 -0.1884 0.2172 155 HIS A CD2 1085 C CE1 . HIS A 136 ? 1.2270 1.4861 1.4147 -0.1874 -0.1991 0.2424 155 HIS A CE1 1086 N NE2 . HIS A 136 ? 1.2804 1.4734 1.4367 -0.1837 -0.2043 0.2285 155 HIS A NE2 1087 N N . TYR A 137 ? 1.1544 1.4747 1.3470 -0.1293 -0.1158 0.2116 156 TYR A N 1088 C CA . TYR A 137 ? 1.1446 1.4978 1.3528 -0.1228 -0.1003 0.2172 156 TYR A CA 1089 C C . TYR A 137 ? 1.0983 1.4576 1.2881 -0.1096 -0.0791 0.2015 156 TYR A C 1090 O O . TYR A 137 ? 1.0564 1.4230 1.2358 -0.1084 -0.0749 0.1911 156 TYR A O 1091 C CB . TYR A 137 ? 1.1259 1.5446 1.3726 -0.1312 -0.0991 0.2357 156 TYR A CB 1092 C CG . TYR A 137 ? 1.1772 1.6051 1.4466 -0.1477 -0.1217 0.2579 156 TYR A CG 1093 C CD1 . TYR A 137 ? 1.2604 1.6608 1.5356 -0.1552 -0.1378 0.2722 156 TYR A CD1 1094 C CD2 . TYR A 137 ? 1.1609 1.6289 1.4467 -0.1559 -0.1292 0.2667 156 TYR A CD2 1095 C CE1 . TYR A 137 ? 1.3186 1.7283 1.6148 -0.1741 -0.1631 0.2973 156 TYR A CE1 1096 C CE2 . TYR A 137 ? 1.2118 1.6970 1.5193 -0.1733 -0.1511 0.2920 156 TYR A CE2 1097 C CZ . TYR A 137 ? 1.2896 1.7450 1.6024 -0.1842 -0.1690 0.3087 156 TYR A CZ 1098 O OH . TYR A 137 ? 1.3527 1.8251 1.6867 -0.2049 -0.1951 0.3379 156 TYR A OH 1099 N N . CYS A 138 ? 1.1147 1.4729 1.3016 -0.1008 -0.0678 0.2020 157 CYS A N 1100 C CA . CYS A 138 ? 1.0757 1.4463 1.2472 -0.0899 -0.0481 0.1931 157 CYS A CA 1101 C C . CYS A 138 ? 1.0562 1.4753 1.2547 -0.0905 -0.0346 0.2059 157 CYS A C 1102 O O . CYS A 138 ? 1.0956 1.5222 1.3151 -0.0933 -0.0376 0.2190 157 CYS A O 1103 C CB . CYS A 138 ? 1.1175 1.4511 1.2605 -0.0769 -0.0451 0.1831 157 CYS A CB 1104 S SG . CYS A 138 ? 1.0770 1.4331 1.1991 -0.0656 -0.0225 0.1769 157 CYS A SG 1105 N N . HIS A 139 ? 1.0061 1.4562 1.2035 -0.0884 -0.0221 0.2028 158 HIS A N 1106 C CA . HIS A 139 ? 0.9925 1.4891 1.2126 -0.0885 -0.0090 0.2137 158 HIS A CA 1107 C C . HIS A 139 ? 0.9685 1.4686 1.1687 -0.0809 0.0069 0.2100 158 HIS A C 1108 O O . HIS A 139 ? 0.9380 1.4327 1.1176 -0.0799 0.0062 0.2008 158 HIS A O 1109 C CB . HIS A 139 ? 0.9730 1.5119 1.2143 -0.0930 -0.0125 0.2161 158 HIS A CB 1110 C CG . HIS A 139 ? 0.9980 1.5436 1.2584 -0.1012 -0.0286 0.2225 158 HIS A CG 1111 N ND1 . HIS A 139 ? 1.0306 1.6114 1.3239 -0.1092 -0.0323 0.2411 158 HIS A ND1 1112 C CD2 . HIS A 139 ? 0.9904 1.5155 1.2416 -0.1040 -0.0427 0.2152 158 HIS A CD2 1113 C CE1 . HIS A 139 ? 1.0500 1.6324 1.3523 -0.1169 -0.0489 0.2459 158 HIS A CE1 1114 N NE2 . HIS A 139 ? 1.0231 1.5713 1.3005 -0.1135 -0.0549 0.2302 158 HIS A NE2 1115 N N . ASN A 140 ? 0.9880 1.4982 1.1945 -0.0770 0.0190 0.2192 159 ASN A N 1116 C CA . ASN A 140 ? 0.9655 1.4854 1.1545 -0.0709 0.0345 0.2201 159 ASN A CA 1117 C C . ASN A 140 ? 0.9415 1.5053 1.1483 -0.0753 0.0444 0.2296 159 ASN A C 1118 O O . ASN A 140 ? 0.9615 1.5538 1.1991 -0.0801 0.0452 0.2391 159 ASN A O 1119 C CB . ASN A 140 ? 1.0070 1.5149 1.1903 -0.0616 0.0428 0.2242 159 ASN A CB 1120 C CG . ASN A 140 ? 0.9873 1.5093 1.1495 -0.0548 0.0585 0.2271 159 ASN A CG 1121 O OD1 . ASN A 140 ? 0.9589 1.4766 1.0950 -0.0544 0.0577 0.2211 159 ASN A OD1 1122 N ND2 . ASN A 140 ? 1.0044 1.5468 1.1787 -0.0510 0.0718 0.2389 159 ASN A ND2 1123 N N . TYR A 141 ? 0.9093 1.4799 1.0958 -0.0744 0.0500 0.2285 160 TYR A N 1124 C CA . TYR A 141 ? 0.8977 1.5036 1.0939 -0.0775 0.0580 0.2370 160 TYR A CA 1125 C C . TYR A 141 ? 0.8808 1.4878 1.0518 -0.0765 0.0674 0.2438 160 TYR A C 1126 O O . TYR A 141 ? 0.8762 1.4619 1.0222 -0.0729 0.0668 0.2406 160 TYR A O 1127 C CB . TYR A 141 ? 0.8945 1.5125 1.0962 -0.0797 0.0457 0.2287 160 TYR A CB 1128 C CG . TYR A 141 ? 0.8820 1.4727 1.0547 -0.0801 0.0314 0.2169 160 TYR A CG 1129 C CD1 . TYR A 141 ? 0.8789 1.4696 1.0300 -0.0826 0.0292 0.2201 160 TYR A CD1 1130 C CD2 . TYR A 141 ? 0.8854 1.4519 1.0538 -0.0802 0.0170 0.2046 160 TYR A CD2 1131 C CE1 . TYR A 141 ? 0.8842 1.4501 1.0104 -0.0859 0.0116 0.2119 160 TYR A CE1 1132 C CE2 . TYR A 141 ? 0.8867 1.4294 1.0313 -0.0823 0.0019 0.1948 160 TYR A CE2 1133 C CZ . TYR A 141 ? 0.8902 1.4322 1.0139 -0.0855 -0.0016 0.1986 160 TYR A CZ 1134 O OH . TYR A 141 ? 0.9081 1.4261 1.0094 -0.0903 -0.0206 0.1915 160 TYR A OH 1135 N N . ILE A 142 ? 0.8775 1.5129 1.0543 -0.0800 0.0753 0.2545 161 ILE A N 1136 C CA . ILE A 142 ? 0.8662 1.5084 1.0203 -0.0819 0.0828 0.2661 161 ILE A CA 1137 C C . ILE A 142 ? 0.8558 1.4796 0.9796 -0.0867 0.0661 0.2608 161 ILE A C 1138 O O . ILE A 142 ? 0.8638 1.4867 0.9874 -0.0906 0.0522 0.2554 161 ILE A O 1139 C CB . ILE A 142 ? 0.8759 1.5521 1.0452 -0.0862 0.0947 0.2812 161 ILE A CB 1140 C CG1 . ILE A 142 ? 0.8980 1.5931 1.0983 -0.0837 0.1100 0.2894 161 ILE A CG1 1141 C CG2 . ILE A 142 ? 0.8633 1.5472 1.0069 -0.0908 0.0997 0.2967 161 ILE A CG2 1142 C CD1 . ILE A 142 ? 0.9190 1.6519 1.1431 -0.0894 0.1201 0.3023 161 ILE A CD1 1143 N N . GLY A 143 ? 0.8517 1.4624 0.9501 -0.0856 0.0655 0.2619 162 GLY A N 1144 C CA . GLY A 143 ? 0.8567 1.4540 0.9269 -0.0933 0.0479 0.2611 162 GLY A CA 1145 C C . GLY A 143 ? 0.8661 1.4337 0.9287 -0.0924 0.0333 0.2438 162 GLY A C 1146 O O . GLY A 143 ? 0.8817 1.4390 0.9211 -0.0999 0.0182 0.2442 162 GLY A O 1147 N N . GLY A 144 ? 0.8667 1.4218 0.9488 -0.0854 0.0356 0.2311 163 GLY A N 1148 C CA . GLY A 144 ? 0.8764 1.4025 0.9518 -0.0854 0.0219 0.2160 163 GLY A CA 1149 C C . GLY A 144 ? 0.8817 1.3970 0.9791 -0.0791 0.0249 0.2077 163 GLY A C 1150 O O . GLY A 144 ? 0.8873 1.4141 1.0008 -0.0736 0.0381 0.2139 163 GLY A O 1151 N N . TYR A 145 ? 0.8902 1.3826 0.9879 -0.0814 0.0103 0.1953 164 TYR A N 1152 C CA . TYR A 145 ? 0.8996 1.3794 1.0159 -0.0791 0.0071 0.1897 164 TYR A CA 1153 C C . TYR A 145 ? 0.9012 1.3659 1.0184 -0.0842 -0.0106 0.1789 164 TYR A C 1154 O O . TYR A 145 ? 0.9038 1.3608 1.0041 -0.0885 -0.0211 0.1740 164 TYR A O 1155 C CB . TYR A 145 ? 0.9286 1.3839 1.0319 -0.0725 0.0105 0.1866 164 TYR A CB 1156 C CG . TYR A 145 ? 0.9469 1.3737 1.0226 -0.0735 -0.0002 0.1757 164 TYR A CG 1157 C CD1 . TYR A 145 ? 0.9519 1.3851 1.0009 -0.0744 0.0012 0.1770 164 TYR A CD1 1158 C CD2 . TYR A 145 ? 0.9674 1.3654 1.0447 -0.0763 -0.0136 0.1664 164 TYR A CD2 1159 C CE1 . TYR A 145 ? 0.9807 1.3943 1.0058 -0.0769 -0.0091 0.1684 164 TYR A CE1 1160 C CE2 . TYR A 145 ? 0.9951 1.3681 1.0476 -0.0784 -0.0233 0.1566 164 TYR A CE2 1161 C CZ . TYR A 145 ? 1.0043 1.3866 1.0314 -0.0785 -0.0207 0.1571 164 TYR A CZ 1162 O OH . TYR A 145 ? 1.0388 1.4026 1.0428 -0.0822 -0.0309 0.1488 164 TYR A OH 1163 N N . TYR A 146 ? 0.9106 1.3714 1.0475 -0.0847 -0.0161 0.1772 165 TYR A N 1164 C CA . TYR A 146 ? 0.9165 1.3652 1.0562 -0.0888 -0.0323 0.1687 165 TYR A CA 1165 C C . TYR A 146 ? 0.9354 1.3700 1.0877 -0.0913 -0.0379 0.1710 165 TYR A C 1166 O O . TYR A 146 ? 0.9505 1.3897 1.1155 -0.0900 -0.0315 0.1801 165 TYR A O 1167 C CB . TYR A 146 ? 0.9129 1.3920 1.0687 -0.0872 -0.0382 0.1665 165 TYR A CB 1168 C CG . TYR A 146 ? 0.9150 1.4354 1.1026 -0.0845 -0.0308 0.1759 165 TYR A CG 1169 C CD1 . TYR A 146 ? 0.9159 1.4651 1.1119 -0.0815 -0.0174 0.1839 165 TYR A CD1 1170 C CD2 . TYR A 146 ? 0.9286 1.4646 1.1385 -0.0865 -0.0384 0.1791 165 TYR A CD2 1171 C CE1 . TYR A 146 ? 0.9271 1.5197 1.1537 -0.0807 -0.0110 0.1939 165 TYR A CE1 1172 C CE2 . TYR A 146 ? 0.9418 1.5252 1.1825 -0.0861 -0.0332 0.1910 165 TYR A CE2 1173 C CZ . TYR A 146 ? 0.9472 1.5592 1.1966 -0.0832 -0.0193 0.1976 165 TYR A CZ 1174 O OH . TYR A 146 ? 0.9654 1.6289 1.2463 -0.0843 -0.0142 0.2104 165 TYR A OH 1175 N N . CYS A 147 ? 0.9445 1.3604 1.0931 -0.0960 -0.0524 0.1642 166 CYS A N 1176 C CA . CYS A 147 ? 0.9668 1.3666 1.1249 -0.1014 -0.0626 0.1682 166 CYS A CA 1177 C C . CYS A 147 ? 0.9636 1.3981 1.1487 -0.1044 -0.0705 0.1738 166 CYS A C 1178 O O . CYS A 147 ? 0.9541 1.4122 1.1426 -0.1002 -0.0719 0.1675 166 CYS A O 1179 C CB . CYS A 147 ? 0.9887 1.3430 1.1210 -0.1053 -0.0733 0.1581 166 CYS A CB 1180 S SG . CYS A 147 ? 1.0032 1.3300 1.0997 -0.0991 -0.0647 0.1494 166 CYS A SG 1181 N N . SER A 148 ? 0.9840 1.4227 1.1872 -0.1112 -0.0783 0.1863 167 SER A N 1182 C CA . SER A 148 ? 0.9926 1.4702 1.2216 -0.1156 -0.0879 0.1957 167 SER A CA 1183 C C . SER A 148 ? 1.0255 1.4749 1.2550 -0.1277 -0.1043 0.2057 167 SER A C 1184 O O . SER A 148 ? 1.0486 1.4493 1.2602 -0.1304 -0.1076 0.2042 167 SER A O 1185 C CB . SER A 148 ? 0.9970 1.5351 1.2568 -0.1136 -0.0800 0.2093 167 SER A CB 1186 O OG . SER A 148 ? 1.0252 1.5666 1.3024 -0.1234 -0.0841 0.2286 167 SER A OG 1187 N N . CYS A 149 ? 1.0376 1.5173 1.2853 -0.1338 -0.1161 0.2156 168 CYS A N 1188 C CA . CYS A 149 ? 1.0722 1.5256 1.3192 -0.1478 -0.1347 0.2277 168 CYS A CA 1189 C C . CYS A 149 ? 1.1045 1.6020 1.3833 -0.1599 -0.1460 0.2557 168 CYS A C 1190 O O . CYS A 149 ? 1.1020 1.6657 1.4072 -0.1563 -0.1390 0.2649 168 CYS A O 1191 C CB . CYS A 149 ? 1.0638 1.5042 1.2988 -0.1487 -0.1432 0.2177 168 CYS A CB 1192 S SG . CYS A 149 ? 1.0615 1.4477 1.2592 -0.1407 -0.1362 0.1896 168 CYS A SG 1193 N N . ARG A 150 ? 1.1489 1.6110 1.4242 -0.1754 -0.1661 0.2705 169 ARG A N 1194 C CA . ARG A 150 ? 1.1971 1.6962 1.5008 -0.1925 -0.1843 0.3026 169 ARG A CA 1195 C C . ARG A 150 ? 1.1825 1.7489 1.5061 -0.1939 -0.1874 0.3123 169 ARG A C 1196 O O . ARG A 150 ? 1.1496 1.7067 1.4584 -0.1853 -0.1834 0.2942 169 ARG A O 1197 C CB . ARG A 150 ? 1.2620 1.6965 1.5508 -0.2090 -0.2099 0.3146 169 ARG A CB 1198 C CG . ARG A 150 ? 1.3085 1.6794 1.5792 -0.2061 -0.2131 0.3076 169 ARG A CG 1199 C CD . ARG A 150 ? 1.4000 1.7122 1.6589 -0.2225 -0.2449 0.3224 169 ARG A CD 1200 N NE . ARG A 150 ? 1.4438 1.6728 1.6643 -0.2112 -0.2467 0.2981 169 ARG A NE 1201 C CZ . ARG A 150 ? 1.4794 1.6488 1.6710 -0.2148 -0.2616 0.2894 169 ARG A CZ 1202 N NH1 . ARG A 150 ? 1.4640 1.6440 1.6613 -0.2313 -0.2762 0.3047 169 ARG A NH1 1203 N NH2 . ARG A 150 ? 1.5285 1.6312 1.6851 -0.2012 -0.2620 0.2658 169 ARG A NH2 1204 N N . PHE A 151 ? 1.2166 1.8538 1.5738 -0.2045 -0.1960 0.3415 170 PHE A N 1205 C CA . PHE A 151 ? 1.2193 1.9352 1.5980 -0.2042 -0.2000 0.3542 170 PHE A CA 1206 C C . PHE A 151 ? 1.2222 1.9042 1.5854 -0.2134 -0.2163 0.3568 170 PHE A C 1207 O O . PHE A 151 ? 1.2593 1.8875 1.6124 -0.2326 -0.2361 0.3719 170 PHE A O 1208 C CB . PHE A 151 ? 1.2721 2.0685 1.6888 -0.2198 -0.2115 0.3919 170 PHE A CB 1209 C CG . PHE A 151 ? 1.2839 2.1793 1.7247 -0.2161 -0.2139 0.4061 170 PHE A CG 1210 C CD1 . PHE A 151 ? 1.2759 2.2446 1.7297 -0.1927 -0.1946 0.3909 170 PHE A CD1 1211 C CD2 . PHE A 151 ? 1.3198 2.2378 1.7693 -0.2349 -0.2368 0.4351 170 PHE A CD2 1212 C CE1 . PHE A 151 ? 1.3084 2.3739 1.7829 -0.1844 -0.1974 0.4015 170 PHE A CE1 1213 C CE2 . PHE A 151 ? 1.3396 2.3578 1.8111 -0.2289 -0.2385 0.4488 170 PHE A CE2 1214 C CZ . PHE A 151 ? 1.3381 2.4311 1.8219 -0.2020 -0.2184 0.4306 170 PHE A CZ 1215 N N . GLY A 152 ? 1.1948 1.9025 1.5541 -0.1988 -0.2094 0.3404 171 GLY A N 1216 C CA . GLY A 152 ? 1.1980 1.8776 1.5435 -0.2060 -0.2228 0.3413 171 GLY A CA 1217 C C . GLY A 152 ? 1.1685 1.7635 1.4785 -0.1978 -0.2158 0.3082 171 GLY A C 1218 O O . GLY A 152 ? 1.1757 1.7429 1.4726 -0.2031 -0.2252 0.3054 171 GLY A O 1219 N N . TYR A 153 ? 1.1429 1.7015 1.4381 -0.1864 -0.2001 0.2857 172 TYR A N 1220 C CA . TYR A 153 ? 1.1221 1.6113 1.3849 -0.1793 -0.1933 0.2568 172 TYR A CA 1221 C C . TYR A 153 ? 1.0942 1.6075 1.3551 -0.1579 -0.1778 0.2322 172 TYR A C 1222 O O . TYR A 153 ? 1.0869 1.6592 1.3677 -0.1466 -0.1687 0.2342 172 TYR A O 1223 C CB . TYR A 153 ? 1.1294 1.5549 1.3721 -0.1835 -0.1907 0.2518 172 TYR A CB 1224 C CG . TYR A 153 ? 1.1798 1.5541 1.4118 -0.2021 -0.2108 0.2674 172 TYR A CG 1225 C CD1 . TYR A 153 ? 1.2189 1.6135 1.4713 -0.2165 -0.2260 0.2969 172 TYR A CD1 1226 C CD2 . TYR A 153 ? 1.1995 1.5032 1.3997 -0.2056 -0.2169 0.2529 172 TYR A CD2 1227 C CE1 . TYR A 153 ? 1.2782 1.6180 1.5181 -0.2339 -0.2496 0.3115 172 TYR A CE1 1228 C CE2 . TYR A 153 ? 1.2602 1.5112 1.4468 -0.2208 -0.2377 0.2651 172 TYR A CE2 1229 C CZ . TYR A 153 ? 1.3009 1.5666 1.5066 -0.2347 -0.2553 0.2942 172 TYR A CZ 1230 O OH . TYR A 153 ? 1.3771 1.5844 1.5672 -0.2501 -0.2810 0.3066 172 TYR A OH 1231 N N . ILE A 154 ? 1.0879 1.5548 1.3240 -0.1534 -0.1771 0.2099 173 ILE A N 1232 C CA . ILE A 154 ? 1.0780 1.5547 1.3078 -0.1358 -0.1691 0.1869 173 ILE A CA 1233 C C . ILE A 154 ? 1.0634 1.4837 1.2658 -0.1360 -0.1613 0.1710 173 ILE A C 1234 O O . ILE A 154 ? 1.0736 1.4407 1.2552 -0.1467 -0.1668 0.1679 173 ILE A O 1235 C CB . ILE A 154 ? 1.1034 1.5884 1.3324 -0.1305 -0.1807 0.1775 173 ILE A CB 1236 C CG1 . ILE A 154 ? 1.1267 1.6790 1.3829 -0.1284 -0.1879 0.1952 173 ILE A CG1 1237 C CG2 . ILE A 154 ? 1.1141 1.6005 1.3342 -0.1125 -0.1788 0.1531 173 ILE A CG2 1238 C CD1 . ILE A 154 ? 1.1583 1.7099 1.4132 -0.1299 -0.2021 0.1940 173 ILE A CD1 1239 N N . LEU A 155 ? 1.0451 1.4809 1.2470 -0.1240 -0.1493 0.1619 174 LEU A N 1240 C CA . LEU A 155 ? 1.0342 1.4286 1.2110 -0.1237 -0.1421 0.1497 174 LEU A CA 1241 C C . LEU A 155 ? 1.0585 1.4241 1.2166 -0.1245 -0.1527 0.1343 174 LEU A C 1242 O O . LEU A 155 ? 1.0786 1.4663 1.2436 -0.1152 -0.1604 0.1259 174 LEU A O 1243 C CB . LEU A 155 ? 1.0152 1.4373 1.1973 -0.1127 -0.1281 0.1477 174 LEU A CB 1244 C CG . LEU A 155 ? 1.0043 1.3938 1.1628 -0.1134 -0.1187 0.1416 174 LEU A CG 1245 C CD1 . LEU A 155 ? 1.0010 1.3630 1.1521 -0.1200 -0.1131 0.1496 174 LEU A CD1 1246 C CD2 . LEU A 155 ? 0.9865 1.4069 1.1508 -0.1033 -0.1076 0.1406 174 LEU A CD2 1247 N N . HIS A 156 ? 1.0695 1.3871 1.2043 -0.1351 -0.1553 0.1306 175 HIS A N 1248 C CA . HIS A 156 ? 1.1044 1.3924 1.2211 -0.1409 -0.1672 0.1192 175 HIS A CA 1249 C C . HIS A 156 ? 1.1147 1.4050 1.2206 -0.1353 -0.1676 0.1094 175 HIS A C 1250 O O . HIS A 156 ? 1.0868 1.3971 1.1956 -0.1272 -0.1560 0.1113 175 HIS A O 1251 C CB . HIS A 156 ? 1.1267 1.3696 1.2219 -0.1542 -0.1694 0.1196 175 HIS A CB 1252 C CG . HIS A 156 ? 1.1740 1.3901 1.2548 -0.1643 -0.1836 0.1116 175 HIS A CG 1253 N ND1 . HIS A 156 ? 1.2012 1.4233 1.2940 -0.1663 -0.1975 0.1103 175 HIS A ND1 1254 C CD2 . HIS A 156 ? 1.2109 1.3992 1.2676 -0.1730 -0.1863 0.1058 175 HIS A CD2 1255 C CE1 . HIS A 156 ? 1.2486 1.4416 1.3251 -0.1775 -0.2089 0.1039 175 HIS A CE1 1256 N NE2 . HIS A 156 ? 1.2548 1.4289 1.3096 -0.1828 -0.2028 0.1017 175 HIS A NE2 1257 N N . THR A 157 ? 1.1621 1.4312 1.2557 -0.1414 -0.1835 0.1008 176 THR A N 1258 C CA . THR A 157 ? 1.1934 1.4586 1.2748 -0.1407 -0.1922 0.0943 176 THR A CA 1259 C C . THR A 157 ? 1.1800 1.4378 1.2421 -0.1463 -0.1810 0.0992 176 THR A C 1260 O O . THR A 157 ? 1.1971 1.4597 1.2506 -0.1461 -0.1863 0.0989 176 THR A O 1261 C CB . THR A 157 ? 1.2650 1.5070 1.3394 -0.1491 -0.2162 0.0869 176 THR A CB 1262 O OG1 . THR A 157 ? 1.2832 1.4980 1.3470 -0.1648 -0.2176 0.0897 176 THR A OG1 1263 C CG2 . THR A 157 ? 1.2952 1.5533 1.3880 -0.1366 -0.2295 0.0793 176 THR A CG2 1264 N N . ASP A 158 ? 1.1572 1.4048 1.2118 -0.1501 -0.1673 0.1041 177 ASP A N 1265 C CA . ASP A 158 ? 1.1507 1.3977 1.1869 -0.1510 -0.1548 0.1079 177 ASP A CA 1266 C C . ASP A 158 ? 1.0994 1.3726 1.1467 -0.1385 -0.1369 0.1136 177 ASP A C 1267 O O . ASP A 158 ? 1.0919 1.3703 1.1261 -0.1362 -0.1249 0.1176 177 ASP A O 1268 C CB . ASP A 158 ? 1.1739 1.3962 1.1946 -0.1563 -0.1509 0.1071 177 ASP A CB 1269 C CG . ASP A 158 ? 1.1523 1.3654 1.1854 -0.1522 -0.1459 0.1094 177 ASP A CG 1270 O OD1 . ASP A 158 ? 1.1071 1.3417 1.1630 -0.1452 -0.1416 0.1143 177 ASP A OD1 1271 O OD2 . ASP A 158 ? 1.1846 1.3703 1.2040 -0.1568 -0.1484 0.1073 177 ASP A OD2 1272 N N . ASN A 159 ? 1.0711 1.3651 1.1430 -0.1303 -0.1352 0.1148 178 ASN A N 1273 C CA . ASN A 159 ? 1.0322 1.3561 1.1202 -0.1200 -0.1198 0.1214 178 ASN A CA 1274 C C . ASN A 159 ? 1.0173 1.3333 1.1032 -0.1191 -0.1059 0.1279 178 ASN A C 1275 O O . ASN A 159 ? 0.9934 1.3283 1.0854 -0.1125 -0.0920 0.1341 178 ASN A O 1276 C CB . ASN A 159 ? 1.0276 1.3683 1.1092 -0.1161 -0.1165 0.1223 178 ASN A CB 1277 C CG . ASN A 159 ? 1.0655 1.4107 1.1486 -0.1141 -0.1344 0.1150 178 ASN A CG 1278 O OD1 . ASN A 159 ? 1.0841 1.4375 1.1822 -0.1085 -0.1439 0.1088 178 ASN A OD1 1279 N ND2 . ASN A 159 ? 1.1001 1.4414 1.1676 -0.1175 -0.1426 0.1157 178 ASN A ND2 1280 N N . ARG A 160 ? 1.0428 1.3287 1.1195 -0.1251 -0.1117 0.1262 179 ARG A N 1281 C CA . ARG A 160 ? 1.0564 1.3243 1.1251 -0.1223 -0.1044 0.1290 179 ARG A CA 1282 C C . ARG A 160 ? 1.0793 1.3253 1.1556 -0.1280 -0.1149 0.1328 179 ARG A C 1283 O O . ARG A 160 ? 1.0827 1.3305 1.1712 -0.1254 -0.1127 0.1414 179 ARG A O 1284 C CB . ARG A 160 ? 1.0928 1.3411 1.1301 -0.1220 -0.1022 0.1217 179 ARG A CB 1285 C CG . ARG A 160 ? 1.1272 1.3594 1.1504 -0.1127 -0.0944 0.1204 179 ARG A CG 1286 C CD . ARG A 160 ? 1.1713 1.4000 1.1634 -0.1090 -0.0905 0.1133 179 ARG A CD 1287 N NE . ARG A 160 ? 1.2074 1.4199 1.1844 -0.1206 -0.1034 0.1070 179 ARG A NE 1288 C CZ . ARG A 160 ? 1.2677 1.4471 1.2314 -0.1233 -0.1130 0.0998 179 ARG A CZ 1289 N NH1 . ARG A 160 ? 1.2964 1.4505 1.2582 -0.1147 -0.1140 0.0975 179 ARG A NH1 1290 N NH2 . ARG A 160 ? 1.2994 1.4684 1.2513 -0.1357 -0.1242 0.0956 179 ARG A NH2 1291 N N . THR A 161 ? 1.1030 1.3273 1.1717 -0.1373 -0.1283 0.1284 180 THR A N 1292 C CA . THR A 161 ? 1.1277 1.3285 1.2005 -0.1455 -0.1410 0.1341 180 THR A CA 1293 C C . THR A 161 ? 1.1018 1.3337 1.2045 -0.1496 -0.1475 0.1456 180 THR A C 1294 O O . THR A 161 ? 1.0727 1.3384 1.1887 -0.1452 -0.1452 0.1434 180 THR A O 1295 C CB . THR A 161 ? 1.1777 1.3386 1.2255 -0.1538 -0.1515 0.1253 180 THR A CB 1296 O OG1 . THR A 161 ? 1.1729 1.3436 1.2215 -0.1597 -0.1568 0.1201 180 THR A OG1 1297 C CG2 . THR A 161 ? 1.2174 1.3552 1.2353 -0.1470 -0.1452 0.1151 180 THR A CG2 1298 N N . CYS A 162 ? 1.1224 1.3448 1.2347 -0.1572 -0.1578 0.1586 181 CYS A N 1299 C CA . CYS A 162 ? 1.1103 1.3708 1.2519 -0.1624 -0.1653 0.1747 181 CYS A CA 1300 C C . CYS A 162 ? 1.1393 1.3814 1.2788 -0.1756 -0.1824 0.1808 181 CYS A C 1301 O O . CYS A 162 ? 1.1807 1.3857 1.3106 -0.1860 -0.1946 0.1892 181 CYS A O 1302 C CB . CYS A 162 ? 1.1189 1.3970 1.2791 -0.1636 -0.1653 0.1922 181 CYS A CB 1303 S SG . CYS A 162 ? 1.0907 1.3958 1.2571 -0.1491 -0.1444 0.1878 181 CYS A SG 1304 N N . ARG A 163 ? 1.1270 1.3932 1.2744 -0.1746 -0.1851 0.1765 182 ARG A N 1305 C CA . ARG A 163 ? 1.1539 1.4098 1.3016 -0.1865 -0.2004 0.1827 182 ARG A CA 1306 C C . ARG A 163 ? 1.1497 1.4592 1.3274 -0.1895 -0.2076 0.2044 182 ARG A C 1307 O O . ARG A 163 ? 1.1301 1.4873 1.3288 -0.1820 -0.2005 0.2128 182 ARG A O 1308 C CB . ARG A 163 ? 1.1594 1.4079 1.2972 -0.1835 -0.2021 0.1653 182 ARG A CB 1309 C CG . ARG A 163 ? 1.1414 1.4409 1.2974 -0.1683 -0.1984 0.1586 182 ARG A CG 1310 C CD . ARG A 163 ? 1.1775 1.4655 1.3264 -0.1681 -0.2088 0.1453 182 ARG A CD 1311 N NE . ARG A 163 ? 1.1893 1.5250 1.3558 -0.1508 -0.2110 0.1386 182 ARG A NE 1312 C CZ . ARG A 163 ? 1.2065 1.5856 1.3934 -0.1451 -0.2178 0.1467 182 ARG A CZ 1313 N NH1 . ARG A 163 ? 1.1991 1.5804 1.3928 -0.1591 -0.2236 0.1659 182 ARG A NH1 1314 N NH2 . ARG A 163 ? 1.2227 1.6452 1.4221 -0.1246 -0.2205 0.1363 182 ARG A NH2 1315 N N . VAL A 164 ? 1.1744 1.4811 1.3545 -0.2012 -0.2220 0.2149 183 VAL A N 1316 C CA . VAL A 164 ? 1.1786 1.5434 1.3860 -0.2054 -0.2309 0.2384 183 VAL A CA 1317 C C . VAL A 164 ? 1.1925 1.5746 1.4033 -0.2032 -0.2377 0.2339 183 VAL A C 1318 O O . VAL A 164 ? 1.2072 1.5427 1.3977 -0.2058 -0.2401 0.2173 183 VAL A O 1319 C CB . VAL A 164 ? 1.2100 1.5587 1.4200 -0.2269 -0.2477 0.2673 183 VAL A CB 1320 C CG1 . VAL A 164 ? 1.2124 1.5522 1.4247 -0.2280 -0.2452 0.2750 183 VAL A CG1 1321 C CG2 . VAL A 164 ? 1.2454 1.5238 1.4289 -0.2430 -0.2614 0.2659 183 VAL A CG2 1322 N N . GLU A 165 ? 2.2213 1.9076 1.1741 -0.2909 -0.2999 0.1098 184 GLU A N 1323 C CA . GLU A 165 ? 2.2291 1.8860 1.1606 -0.2657 -0.2666 0.0654 184 GLU A CA 1324 C C . GLU A 165 ? 2.1175 1.8106 1.1040 -0.2444 -0.2296 0.0871 184 GLU A C 1325 O O . GLU A 165 ? 2.1509 1.8844 1.1267 -0.2460 -0.2186 0.1143 184 GLU A O 1326 C CB . GLU A 165 ? 2.4264 2.0631 1.2519 -0.2650 -0.2589 0.0256 184 GLU A CB 1327 C CG . GLU A 165 ? 2.5517 2.1328 1.3279 -0.2804 -0.2939 -0.0136 184 GLU A CG 1328 C CD . GLU A 165 ? 2.4871 2.0234 1.3218 -0.2724 -0.3018 -0.0354 184 GLU A CD 1329 O OE1 . GLU A 165 ? 2.3959 1.9329 1.2831 -0.2476 -0.2692 -0.0402 184 GLU A OE1 1330 O OE2 . GLU A 165 ? 2.5474 2.0500 1.3789 -0.2933 -0.3440 -0.0433 184 GLU A OE2 1331 N N . CYS A 166 ? 1.9964 1.6781 1.0476 -0.2282 -0.2160 0.0812 185 CYS A N 1332 C CA . CYS A 166 ? 1.8963 1.6064 1.0073 -0.2110 -0.1889 0.1004 185 CYS A CA 1333 C C . CYS A 166 ? 1.8658 1.5540 0.9945 -0.1887 -0.1633 0.0734 185 CYS A C 1334 O O . CYS A 166 ? 1.7636 1.4623 0.9525 -0.1787 -0.1532 0.0850 185 CYS A O 1335 C CB . CYS A 166 ? 1.7789 1.5079 0.9641 -0.2180 -0.2037 0.1317 185 CYS A CB 1336 S SG . CYS A 166 ? 1.7461 1.4474 0.9583 -0.2281 -0.2295 0.1234 185 CYS A SG 1337 N N . SER A 167 ? 1.9741 1.6313 1.0518 -0.1810 -0.1541 0.0368 186 SER A N 1338 C CA . SER A 167 ? 1.9733 1.6082 1.0752 -0.1600 -0.1318 0.0129 186 SER A CA 1339 C C . SER A 167 ? 2.0820 1.7239 1.1513 -0.1402 -0.0947 -0.0040 186 SER A C 1340 O O . SER A 167 ? 2.0878 1.7190 1.1919 -0.1206 -0.0727 -0.0163 186 SER A O 1341 C CB . SER A 167 ? 2.0100 1.5973 1.1106 -0.1647 -0.1529 -0.0150 186 SER A CB 1342 O OG . SER A 167 ? 1.9157 1.5062 1.0569 -0.1806 -0.1808 0.0071 186 SER A OG 1343 N N . ASP A 168 ? 2.1827 1.8480 1.1894 -0.1454 -0.0869 0.0001 187 ASP A N 1344 C CA . ASP A 168 ? 2.3194 2.0025 1.2874 -0.1266 -0.0465 -0.0121 187 ASP A CA 1345 C C . ASP A 168 ? 2.2417 1.9747 1.2708 -0.1155 -0.0214 0.0295 187 ASP A C 1346 O O . ASP A 168 ? 2.2929 2.0717 1.3036 -0.1210 -0.0122 0.0605 187 ASP A O 1347 C CB . ASP A 168 ? 2.4905 2.1831 1.3570 -0.1397 -0.0500 -0.0224 187 ASP A CB 1348 C CG . ASP A 168 ? 2.6232 2.2600 1.4222 -0.1496 -0.0747 -0.0715 187 ASP A CG 1349 O OD1 . ASP A 168 ? 2.5856 2.1758 1.4240 -0.1451 -0.0878 -0.0961 187 ASP A OD1 1350 O OD2 . ASP A 168 ? 2.7950 2.4350 1.5024 -0.1636 -0.0835 -0.0838 187 ASP A OD2 1351 N N . ASN A 169 ? 2.1362 1.8611 1.2423 -0.1023 -0.0145 0.0336 188 ASN A N 1352 C CA . ASN A 169 ? 2.0656 1.8293 1.2417 -0.0934 0.0020 0.0709 188 ASN A CA 1353 C C . ASN A 169 ? 2.0569 1.8060 1.2900 -0.0727 0.0212 0.0603 188 ASN A C 1354 O O . ASN A 169 ? 2.0737 1.7810 1.3073 -0.0684 0.0140 0.0294 188 ASN A O 1355 C CB . ASN A 169 ? 1.9167 1.6917 1.1441 -0.1105 -0.0291 0.1024 188 ASN A CB 1356 C CG . ASN A 169 ? 1.8195 1.5580 1.0755 -0.1158 -0.0539 0.0867 188 ASN A CG 1357 O OD1 . ASN A 169 ? 1.7794 1.5061 1.0813 -0.1057 -0.0493 0.0822 188 ASN A OD1 1358 N ND2 . ASN A 169 ? 1.7891 1.5134 1.0206 -0.1329 -0.0813 0.0823 188 ASN A ND2 1359 N N . LEU A 170 ? 2.0381 1.8235 1.3293 -0.0622 0.0412 0.0917 189 LEU A N 1360 C CA . LEU A 170 ? 2.0308 1.8123 1.3918 -0.0452 0.0560 0.0946 189 LEU A CA 1361 C C . LEU A 170 ? 1.9872 1.8134 1.4158 -0.0445 0.0620 0.1410 189 LEU A C 1362 O O . LEU A 170 ? 2.0732 1.9410 1.4974 -0.0369 0.0900 0.1630 189 LEU A O 1363 C CB . LEU A 170 ? 2.1847 1.9549 1.5278 -0.0206 0.0945 0.0645 189 LEU A CB 1364 C CG . LEU A 170 ? 2.2006 1.9637 1.6270 -0.0027 0.1074 0.0687 189 LEU A CG 1365 C CD1 . LEU A 170 ? 2.1133 1.8343 1.5694 -0.0137 0.0707 0.0576 189 LEU A CD1 1366 C CD2 . LEU A 170 ? 2.3766 2.1345 1.7927 0.0255 0.1527 0.0402 189 LEU A CD2 1367 N N . PHE A 171 ? 1.8731 1.6918 1.3627 -0.0539 0.0341 0.1566 190 PHE A N 1368 C CA . PHE A 171 ? 1.8368 1.6882 1.3989 -0.0567 0.0292 0.1978 190 PHE A CA 1369 C C . PHE A 171 ? 1.8721 1.7279 1.5024 -0.0421 0.0433 0.2085 190 PHE A C 1370 O O . PHE A 171 ? 1.8381 1.6641 1.4904 -0.0435 0.0260 0.1947 190 PHE A O 1371 C CB . PHE A 171 ? 1.7220 1.5600 1.3052 -0.0763 -0.0112 0.2035 190 PHE A CB 1372 C CG . PHE A 171 ? 1.6970 1.5357 1.2318 -0.0899 -0.0245 0.2001 190 PHE A CG 1373 C CD1 . PHE A 171 ? 1.6796 1.4878 1.1564 -0.0962 -0.0359 0.1690 190 PHE A CD1 1374 C CD2 . PHE A 171 ? 1.7102 1.5821 1.2680 -0.0976 -0.0283 0.2336 190 PHE A CD2 1375 C CE1 . PHE A 171 ? 1.6641 1.4759 1.1060 -0.1098 -0.0503 0.1714 190 PHE A CE1 1376 C CE2 . PHE A 171 ? 1.6948 1.5697 1.2190 -0.1110 -0.0430 0.2362 190 PHE A CE2 1377 C CZ . PHE A 171 ? 1.6710 1.5163 1.1373 -0.1169 -0.0537 0.2050 190 PHE A CZ 1378 N N . THR A 172 ? 1.9564 1.8537 1.6218 -0.0281 0.0758 0.2369 191 THR A N 1379 C CA . THR A 172 ? 2.0141 1.9247 1.7563 -0.0117 0.0949 0.2545 191 THR A CA 1380 C C . THR A 172 ? 1.9993 1.9472 1.8311 -0.0184 0.0837 0.3066 191 THR A C 1381 O O . THR A 172 ? 2.0323 1.9894 1.9431 -0.0110 0.0863 0.3282 191 THR A O 1382 C CB . THR A 172 ? 2.1638 2.0919 1.8817 0.0151 0.1492 0.2414 191 THR A CB 1383 O OG1 . THR A 172 ? 2.2370 2.2132 1.9248 0.0167 0.1752 0.2646 191 THR A OG1 1384 C CG2 . THR A 172 ? 2.2071 2.0883 1.8481 0.0220 0.1553 0.1850 191 THR A CG2 1385 N N . GLN A 173 ? 1.9619 1.9308 1.7903 -0.0333 0.0685 0.3298 192 GLN A N 1386 C CA . GLN A 173 ? 1.9626 1.9632 1.8807 -0.0425 0.0519 0.3798 192 GLN A CA 1387 C C . GLN A 173 ? 1.8750 1.8408 1.8418 -0.0589 0.0029 0.3763 192 GLN A C 1388 O O . GLN A 173 ? 1.7966 1.7195 1.7135 -0.0674 -0.0203 0.3378 192 GLN A O 1389 C CB . GLN A 173 ? 1.9794 2.0106 1.8860 -0.0541 0.0478 0.4063 192 GLN A CB 1390 C CG . GLN A 173 ? 2.1202 2.2037 1.9928 -0.0400 0.0969 0.4266 192 GLN A CG 1391 C CD . GLN A 173 ? 2.1693 2.2827 2.0190 -0.0549 0.0887 0.4537 192 GLN A CD 1392 O OE1 . GLN A 173 ? 2.1068 2.1904 1.9223 -0.0711 0.0561 0.4351 192 GLN A OE1 1393 N NE2 . GLN A 173 ? 2.3034 2.4813 2.1742 -0.0495 0.1201 0.5018 192 GLN A NE2 1394 N N . ARG A 174 ? 1.9009 1.8871 1.9642 -0.0644 -0.0134 0.4177 193 ARG A N 1395 C CA . ARG A 174 ? 1.8601 1.8160 1.9711 -0.0823 -0.0634 0.4170 193 ARG A CA 1396 C C . ARG A 174 ? 1.7867 1.7080 1.8577 -0.1009 -0.1012 0.3892 193 ARG A C 1397 O O . ARG A 174 ? 1.7551 1.6392 1.8130 -0.1128 -0.1347 0.3630 193 ARG A O 1398 C CB . ARG A 174 ? 1.9244 1.9123 2.1491 -0.0876 -0.0770 0.4716 193 ARG A CB 1399 C CG . ARG A 174 ? 2.0061 2.0182 2.2932 -0.0725 -0.0533 0.4977 193 ARG A CG 1400 C CD . ARG A 174 ? 2.0098 1.9912 2.3385 -0.0869 -0.0976 0.4952 193 ARG A CD 1401 N NE . ARG A 174 ? 2.1027 2.1193 2.5466 -0.0834 -0.0963 0.5490 193 ARG A NE 1402 C CZ . ARG A 174 ? 2.1344 2.1412 2.6521 -0.1047 -0.1478 0.5735 193 ARG A CZ 1403 N NH1 . ARG A 174 ? 2.0981 2.0591 2.5767 -0.1296 -0.2020 0.5431 193 ARG A NH1 1404 N NH2 . ARG A 174 ? 2.2170 2.2604 2.8478 -0.1013 -0.1454 0.6280 193 ARG A NH2 1405 N N . THR A 175 ? 1.7782 1.7156 1.8340 -0.1033 -0.0949 0.3979 194 THR A N 1406 C CA . THR A 175 ? 1.7301 1.6402 1.7609 -0.1173 -0.1243 0.3754 194 THR A CA 1407 C C . THR A 175 ? 1.7140 1.6337 1.6727 -0.1123 -0.1000 0.3638 194 THR A C 1408 O O . THR A 175 ? 1.7654 1.7198 1.7045 -0.1011 -0.0643 0.3822 194 THR A O 1409 C CB . THR A 175 ? 1.7715 1.6916 1.8905 -0.1301 -0.1544 0.4094 194 THR A CB 1410 O OG1 . THR A 175 ? 1.8270 1.7977 1.9788 -0.1257 -0.1303 0.4567 194 THR A OG1 1411 C CG2 . THR A 175 ? 1.8117 1.7242 2.0087 -0.1383 -0.1839 0.4265 194 THR A CG2 1412 N N . GLY A 176 ? 1.6625 1.5541 1.5830 -0.1210 -0.1192 0.3347 195 GLY A N 1413 C CA . GLY A 176 ? 1.6550 1.5552 1.5146 -0.1203 -0.1041 0.3280 195 GLY A CA 1414 C C . GLY A 176 ? 1.6070 1.4770 1.4457 -0.1296 -0.1277 0.2998 195 GLY A C 1415 O O . GLY A 176 ? 1.5825 1.4216 1.4375 -0.1343 -0.1511 0.2759 195 GLY A O 1416 N N . VAL A 177 ? 1.6102 1.4925 1.4130 -0.1325 -0.1209 0.3041 196 VAL A N 1417 C CA . VAL A 177 ? 1.5776 1.4394 1.3684 -0.1395 -0.1382 0.2843 196 VAL A CA 1418 C C . VAL A 177 ? 1.5530 1.4081 1.2598 -0.1388 -0.1256 0.2623 196 VAL A C 1419 O O . VAL A 177 ? 1.5932 1.4703 1.2581 -0.1372 -0.1074 0.2754 196 VAL A O 1420 C CB . VAL A 177 ? 1.6254 1.5083 1.4789 -0.1477 -0.1524 0.3193 196 VAL A CB 1421 C CG1 . VAL A 177 ? 1.5982 1.4619 1.4489 -0.1523 -0.1667 0.2998 196 VAL A CG1 1422 C CG2 . VAL A 177 ? 1.6677 1.5510 1.6140 -0.1499 -0.1707 0.3397 196 VAL A CG2 1423 N N . ILE A 178 ? 1.5031 1.3284 1.1850 -0.1404 -0.1357 0.2287 197 ILE A N 1424 C CA . ILE A 178 ? 1.4821 1.2972 1.0970 -0.1423 -0.1308 0.2091 197 ILE A CA 1425 C C . ILE A 178 ? 1.4651 1.2738 1.0949 -0.1489 -0.1457 0.2037 197 ILE A C 1426 O O . ILE A 178 ? 1.4586 1.2540 1.1280 -0.1473 -0.1555 0.1908 197 ILE A O 1427 C CB . ILE A 178 ? 1.4586 1.2493 1.0343 -0.1369 -0.1250 0.1793 197 ILE A CB 1428 C CG1 . ILE A 178 ? 1.4886 1.2864 1.0724 -0.1277 -0.1095 0.1871 197 ILE A CG1 1429 C CG2 . ILE A 178 ? 1.4556 1.2348 0.9701 -0.1403 -0.1230 0.1628 197 ILE A CG2 1430 C CD1 . ILE A 178 ? 1.4824 1.2586 1.0437 -0.1223 -0.1052 0.1650 197 ILE A CD1 1431 N N . THR A 179 ? 1.4746 1.2937 1.0753 -0.1562 -0.1476 0.2137 198 THR A N 1432 C CA . THR A 179 ? 1.4669 1.2851 1.0916 -0.1621 -0.1603 0.2151 198 THR A CA 1433 C C . THR A 179 ? 1.4614 1.2746 1.0305 -0.1696 -0.1634 0.2074 198 THR A C 1434 O O . THR A 179 ? 1.4823 1.2934 0.9923 -0.1720 -0.1581 0.2034 198 THR A O 1435 C CB . THR A 179 ? 1.5196 1.3643 1.2029 -0.1688 -0.1707 0.2539 198 THR A CB 1436 O OG1 . THR A 179 ? 1.5648 1.4330 1.2068 -0.1799 -0.1727 0.2803 198 THR A OG1 1437 C CG2 . THR A 179 ? 1.5439 1.3971 1.2905 -0.1646 -0.1719 0.2713 198 THR A CG2 1438 N N . SER A 180 ? 1.4490 1.2610 1.0432 -0.1733 -0.1725 0.2066 199 SER A N 1439 C CA . SER A 180 ? 1.4533 1.2649 1.0148 -0.1838 -0.1820 0.2090 199 SER A CA 1440 C C . SER A 180 ? 1.5123 1.3469 1.0646 -0.1974 -0.1943 0.2431 199 SER A C 1441 O O . SER A 180 ? 1.5417 1.3965 1.1391 -0.1974 -0.1954 0.2689 199 SER A O 1442 C CB . SER A 180 ? 1.4453 1.2590 1.0554 -0.1825 -0.1854 0.2076 199 SER A CB 1443 O OG . SER A 180 ? 1.4727 1.3006 1.1574 -0.1791 -0.1879 0.2256 199 SER A OG 1444 N N . PRO A 181 ? 1.5507 1.3829 1.0450 -0.2108 -0.2062 0.2451 200 PRO A N 1445 C CA . PRO A 181 ? 1.6360 1.4927 1.1078 -0.2268 -0.2203 0.2775 200 PRO A CA 1446 C C . PRO A 181 ? 1.6656 1.5505 1.2156 -0.2357 -0.2369 0.3194 200 PRO A C 1447 O O . PRO A 181 ? 1.6404 1.5223 1.2436 -0.2355 -0.2445 0.3214 200 PRO A O 1448 C CB . PRO A 181 ? 1.6771 1.5169 1.0755 -0.2408 -0.2358 0.2638 200 PRO A CB 1449 C CG . PRO A 181 ? 1.6164 1.4224 0.9948 -0.2287 -0.2239 0.2236 200 PRO A CG 1450 C CD . PRO A 181 ? 1.5355 1.3430 0.9845 -0.2146 -0.2116 0.2204 200 PRO A CD 1451 N N . ASP A 182 ? 1.7366 1.6521 1.3023 -0.2422 -0.2402 0.3556 201 ASP A N 1452 C CA . ASP A 182 ? 1.7953 1.7418 1.4448 -0.2522 -0.2585 0.4043 201 ASP A CA 1453 C C . ASP A 182 ? 1.7494 1.6889 1.5065 -0.2356 -0.2512 0.4012 201 ASP A C 1454 O O . ASP A 182 ? 1.8006 1.7592 1.6444 -0.2410 -0.2663 0.4367 201 ASP A O 1455 C CB . ASP A 182 ? 1.8475 1.8053 1.4933 -0.2740 -0.2879 0.4300 201 ASP A CB 1456 C CG . ASP A 182 ? 1.9711 1.9715 1.6659 -0.2940 -0.3132 0.4930 201 ASP A CG 1457 O OD1 . ASP A 182 ? 2.0302 2.0560 1.7431 -0.2938 -0.3078 0.5201 201 ASP A OD1 1458 O OD2 . ASP A 182 ? 2.0276 2.0396 1.7472 -0.3116 -0.3406 0.5206 201 ASP A OD2 1459 N N . PHE A 183 ? 1.6725 1.5846 1.4266 -0.2163 -0.2299 0.3593 202 PHE A N 1460 C CA . PHE A 183 ? 1.6543 1.5534 1.4946 -0.2005 -0.2234 0.3457 202 PHE A CA 1461 C C . PHE A 183 ? 1.7336 1.6562 1.6648 -0.2041 -0.2355 0.3890 202 PHE A C 1462 O O . PHE A 183 ? 1.7776 1.7231 1.6898 -0.2124 -0.2377 0.4185 202 PHE A O 1463 C CB . PHE A 183 ? 1.5931 1.4646 1.4018 -0.1851 -0.2047 0.3019 202 PHE A CB 1464 C CG . PHE A 183 ? 1.6010 1.4547 1.4836 -0.1709 -0.2012 0.2815 202 PHE A CG 1465 C CD1 . PHE A 183 ? 1.5840 1.4186 1.4785 -0.1603 -0.1929 0.2465 202 PHE A CD1 1466 C CD2 . PHE A 183 ? 1.6490 1.5062 1.5900 -0.1688 -0.2068 0.2974 202 PHE A CD2 1467 C CE1 . PHE A 183 ? 1.6220 1.4373 1.5751 -0.1469 -0.1892 0.2204 202 PHE A CE1 1468 C CE2 . PHE A 183 ? 1.6850 1.5189 1.6940 -0.1571 -0.2085 0.2733 202 PHE A CE2 1469 C CZ . PHE A 183 ? 1.6789 1.4900 1.6877 -0.1457 -0.1991 0.2310 202 PHE A CZ 1470 N N . PRO A 184 ? 1.7736 1.6928 1.8077 -0.1975 -0.2422 0.3948 203 PRO A N 1471 C CA . PRO A 184 ? 1.7519 1.6507 1.8202 -0.1846 -0.2337 0.3621 203 PRO A CA 1472 C C . PRO A 184 ? 1.7891 1.7083 1.8846 -0.1950 -0.2457 0.3910 203 PRO A C 1473 O O . PRO A 184 ? 1.8158 1.7296 1.9804 -0.1834 -0.2391 0.3803 203 PRO A O 1474 C CB . PRO A 184 ? 1.8125 1.6954 1.9820 -0.1697 -0.2325 0.3507 203 PRO A CB 1475 C CG . PRO A 184 ? 1.8949 1.8055 2.1286 -0.1829 -0.2536 0.4088 203 PRO A CG 1476 C CD . PRO A 184 ? 1.8677 1.8047 2.0045 -0.2006 -0.2569 0.4365 203 PRO A CD 1477 N N . ASN A 185 ? 1.8061 1.7491 1.8474 -0.2169 -0.2632 0.4269 204 ASN A N 1478 C CA . ASN A 185 ? 1.8418 1.8038 1.9028 -0.2316 -0.2814 0.4576 204 ASN A CA 1479 C C . ASN A 185 ? 1.7635 1.7057 1.7552 -0.2280 -0.2702 0.4189 204 ASN A C 1480 O O . ASN A 185 ? 1.6929 1.6118 1.6077 -0.2194 -0.2532 0.3777 204 ASN A O 1481 C CB . ASN A 185 ? 1.9143 1.9085 1.9361 -0.2599 -0.3096 0.5099 204 ASN A CB 1482 C CG . ASN A 185 ? 2.0109 2.0337 2.1073 -0.2665 -0.3227 0.5593 204 ASN A CG 1483 O OD1 . ASN A 185 ? 2.0813 2.1176 2.2979 -0.2655 -0.3347 0.5921 204 ASN A OD1 1484 N ND2 . ASN A 185 ? 2.0324 2.0671 2.0668 -0.2728 -0.3198 0.5685 204 ASN A ND2 1485 N N . PRO A 186 ? 1.7848 1.7383 1.8134 -0.2346 -0.2803 0.4361 205 PRO A N 1486 C CA . PRO A 186 ? 1.7277 1.6669 1.7025 -0.2331 -0.2720 0.4073 205 PRO A CA 1487 C C . PRO A 186 ? 1.6857 1.6076 1.5366 -0.2453 -0.2785 0.3877 205 PRO A C 1488 O O . PRO A 186 ? 1.7369 1.6688 1.5413 -0.2661 -0.3020 0.4130 205 PRO A O 1489 C CB . PRO A 186 ? 1.7842 1.7482 1.8219 -0.2476 -0.2938 0.4495 205 PRO A CB 1490 C CG . PRO A 186 ? 1.8626 1.8476 2.0188 -0.2421 -0.2972 0.4834 205 PRO A CG 1491 C CD . PRO A 186 ? 1.8749 1.8570 2.0138 -0.2425 -0.2994 0.4864 205 PRO A CD 1492 N N . TYR A 187 ? 1.6168 1.5133 1.4149 -0.2319 -0.2569 0.3424 206 TYR A N 1493 C CA . TYR A 187 ? 1.5931 1.4687 1.2871 -0.2396 -0.2605 0.3199 206 TYR A CA 1494 C C . TYR A 187 ? 1.6278 1.5013 1.2864 -0.2609 -0.2869 0.3323 206 TYR A C 1495 O O . TYR A 187 ? 1.6385 1.5236 1.3529 -0.2639 -0.2932 0.3486 206 TYR A O 1496 C CB . TYR A 187 ? 1.5241 1.3751 1.1834 -0.2213 -0.2344 0.2749 206 TYR A CB 1497 C CG . TYR A 187 ? 1.5077 1.3587 1.2044 -0.2097 -0.2192 0.2601 206 TYR A CG 1498 C CD1 . TYR A 187 ? 1.5108 1.3593 1.1882 -0.2183 -0.2268 0.2605 206 TYR A CD1 1499 C CD2 . TYR A 187 ? 1.5066 1.3597 1.2528 -0.1903 -0.1966 0.2434 206 TYR A CD2 1500 C CE1 . TYR A 187 ? 1.5092 1.3667 1.2197 -0.2078 -0.2090 0.2522 206 TYR A CE1 1501 C CE2 . TYR A 187 ? 1.5140 1.3717 1.2823 -0.1786 -0.1777 0.2270 206 TYR A CE2 1502 C CZ . TYR A 187 ? 1.5165 1.3805 1.2672 -0.1872 -0.1820 0.2344 206 TYR A CZ 1503 O OH . TYR A 187 ? 1.5413 1.4188 1.3140 -0.1758 -0.1599 0.2239 206 TYR A OH 1504 N N . PRO A 188 ? 1.6640 1.5227 1.2334 -0.2754 -0.3023 0.3242 207 PRO A N 1505 C CA . PRO A 188 ? 1.7180 1.5666 1.2474 -0.2982 -0.3336 0.3306 207 PRO A CA 1506 C C . PRO A 188 ? 1.6769 1.5080 1.2176 -0.2935 -0.3298 0.3118 207 PRO A C 1507 O O . PRO A 188 ? 1.6207 1.4349 1.1455 -0.2756 -0.3042 0.2794 207 PRO A O 1508 C CB . PRO A 188 ? 1.7744 1.6027 1.1987 -0.3057 -0.3389 0.3080 207 PRO A CB 1509 C CG . PRO A 188 ? 1.7694 1.6162 1.1958 -0.2942 -0.3179 0.3143 207 PRO A CG 1510 C CD . PRO A 188 ? 1.6754 1.5273 1.1801 -0.2712 -0.2911 0.3091 207 PRO A CD 1511 N N . LYS A 189 ? 1.7191 1.5585 1.2933 -0.3117 -0.3576 0.3384 208 LYS A N 1512 C CA . LYS A 189 ? 1.7033 1.5342 1.2988 -0.3120 -0.3590 0.3332 208 LYS A CA 1513 C C . LYS A 189 ? 1.7392 1.5291 1.2517 -0.3226 -0.3765 0.3027 208 LYS A C 1514 O O . LYS A 189 ? 1.7921 1.5628 1.2312 -0.3321 -0.3903 0.2879 208 LYS A O 1515 C CB . LYS A 189 ? 1.7570 1.6137 1.4251 -0.3307 -0.3874 0.3794 208 LYS A CB 1516 C CG . LYS A 189 ? 1.7424 1.6395 1.5122 -0.3180 -0.3690 0.4106 208 LYS A CG 1517 C CD . LYS A 189 ? 1.8120 1.7360 1.6574 -0.3391 -0.4014 0.4622 208 LYS A CD 1518 C CE . LYS A 189 ? 1.8271 1.7911 1.7851 -0.3268 -0.3857 0.4966 208 LYS A CE 1519 N NZ . LYS A 189 ? 1.8397 1.8094 1.7953 -0.3286 -0.3919 0.5072 208 LYS A NZ 1520 N N . SER A 190 ? 1.7275 1.5056 1.2549 -0.3208 -0.3750 0.2942 209 SER A N 1521 C CA . SER A 190 ? 1.7821 1.5185 1.2551 -0.3312 -0.3955 0.2687 209 SER A CA 1522 C C . SER A 190 ? 1.7929 1.4952 1.1828 -0.3207 -0.3822 0.2245 209 SER A C 1523 O O . SER A 190 ? 1.8856 1.5507 1.2154 -0.3331 -0.4061 0.2015 209 SER A O 1524 C CB . SER A 190 ? 1.8815 1.6069 1.3496 -0.3629 -0.4469 0.2893 209 SER A CB 1525 O OG . SER A 190 ? 1.8773 1.6399 1.4347 -0.3722 -0.4582 0.3367 209 SER A OG 1526 N N . SER A 191 ? 1.7188 1.4332 1.1092 -0.2973 -0.3441 0.2118 210 SER A N 1527 C CA . SER A 191 ? 1.7284 1.4198 1.0561 -0.2844 -0.3259 0.1769 210 SER A CA 1528 C C . SER A 191 ? 1.6826 1.3609 1.0190 -0.2652 -0.3003 0.1543 210 SER A C 1529 O O . SER A 191 ? 1.6302 1.3267 1.0174 -0.2590 -0.2892 0.1667 210 SER A O 1530 C CB . SER A 191 ? 1.7059 1.4228 1.0269 -0.2773 -0.3096 0.1869 210 SER A CB 1531 O OG . SER A 191 ? 1.7783 1.5082 1.0838 -0.2984 -0.3375 0.2111 210 SER A OG 1532 N N . GLU A 192 ? 1.7208 1.3699 1.0075 -0.2563 -0.2907 0.1221 211 GLU A N 1533 C CA . GLU A 192 ? 1.7014 1.3358 0.9965 -0.2399 -0.2707 0.1028 211 GLU A CA 1534 C C . GLU A 192 ? 1.7056 1.3371 0.9673 -0.2233 -0.2447 0.0834 211 GLU A C 1535 O O . GLU A 192 ? 1.7938 1.3991 1.0068 -0.2213 -0.2445 0.0581 211 GLU A O 1536 C CB . GLU A 192 ? 1.7862 1.3818 1.0738 -0.2481 -0.2920 0.0866 211 GLU A CB 1537 C CG . GLU A 192 ? 1.7879 1.3721 1.1012 -0.2353 -0.2782 0.0772 211 GLU A CG 1538 C CD . GLU A 192 ? 1.8901 1.4375 1.2151 -0.2450 -0.3036 0.0685 211 GLU A CD 1539 O OE1 . GLU A 192 ? 1.9871 1.4929 1.2744 -0.2449 -0.3129 0.0367 211 GLU A OE1 1540 O OE2 . GLU A 192 ? 1.8898 1.4506 1.2631 -0.2528 -0.3140 0.0935 211 GLU A OE2 1541 N N . CYS A 193 ? 1.6242 1.2839 0.9150 -0.2112 -0.2227 0.0953 212 CYS A N 1542 C CA . CYS A 193 ? 1.6231 1.2896 0.8997 -0.1964 -0.1987 0.0877 212 CYS A CA 1543 C C . CYS A 193 ? 1.6086 1.2633 0.9018 -0.1810 -0.1814 0.0734 212 CYS A C 1544 O O . CYS A 193 ? 1.5609 1.2225 0.8911 -0.1792 -0.1811 0.0804 212 CYS A O 1545 C CB . CYS A 193 ? 1.5661 1.2675 0.8729 -0.1951 -0.1914 0.1122 212 CYS A CB 1546 S SG . CYS A 193 ? 1.6101 1.3322 0.9176 -0.2148 -0.2150 0.1401 212 CYS A SG 1547 N N . LEU A 194 ? 1.6708 1.3113 0.9371 -0.1697 -0.1659 0.0548 213 LEU A N 1548 C CA . LEU A 194 ? 1.6748 1.3060 0.9658 -0.1544 -0.1494 0.0456 213 LEU A CA 1549 C C . LEU A 194 ? 1.6666 1.3210 0.9642 -0.1412 -0.1246 0.0532 213 LEU A C 1550 O O . LEU A 194 ? 1.7367 1.3932 0.9976 -0.1353 -0.1099 0.0447 213 LEU A O 1551 C CB . LEU A 194 ? 1.7793 1.3720 1.0529 -0.1494 -0.1505 0.0178 213 LEU A CB 1552 C CG . LEU A 194 ? 1.8181 1.3843 1.0956 -0.1638 -0.1790 0.0129 213 LEU A CG 1553 C CD1 . LEU A 194 ? 1.9548 1.4767 1.2127 -0.1585 -0.1817 -0.0201 213 LEU A CD1 1554 C CD2 . LEU A 194 ? 1.7686 1.3449 1.0983 -0.1673 -0.1872 0.0330 213 LEU A CD2 1555 N N . TYR A 195 ? 1.5932 1.2671 0.9362 -0.1378 -0.1212 0.0705 214 TYR A N 1556 C CA . TYR A 195 ? 1.5884 1.2856 0.9552 -0.1273 -0.1027 0.0844 214 TYR A CA 1557 C C . TYR A 195 ? 1.6125 1.3013 1.0130 -0.1153 -0.0926 0.0808 214 TYR A C 1558 O O . TYR A 195 ? 1.5832 1.2641 1.0096 -0.1196 -0.1063 0.0823 214 TYR A O 1559 C CB . TYR A 195 ? 1.5181 1.2388 0.9199 -0.1336 -0.1113 0.1056 214 TYR A CB 1560 C CG . TYR A 195 ? 1.5043 1.2349 0.8906 -0.1457 -0.1237 0.1145 214 TYR A CG 1561 C CD1 . TYR A 195 ? 1.5392 1.2908 0.9099 -0.1483 -0.1187 0.1307 214 TYR A CD1 1562 C CD2 . TYR A 195 ? 1.4676 1.1919 0.8601 -0.1550 -0.1402 0.1121 214 TYR A CD2 1563 C CE1 . TYR A 195 ? 1.5423 1.3059 0.9084 -0.1617 -0.1344 0.1456 214 TYR A CE1 1564 C CE2 . TYR A 195 ? 1.4568 1.1930 0.8493 -0.1657 -0.1520 0.1251 214 TYR A CE2 1565 C CZ . TYR A 195 ? 1.4995 1.2539 0.8805 -0.1698 -0.1513 0.1425 214 TYR A CZ 1566 O OH . TYR A 195 ? 1.5190 1.2874 0.9081 -0.1824 -0.1670 0.1614 214 TYR A OH 1567 N N . THR A 196 ? 1.6775 1.3710 1.0782 -0.1005 -0.0681 0.0782 215 THR A N 1568 C CA . THR A 196 ? 1.7201 1.4074 1.1640 -0.0873 -0.0566 0.0782 215 THR A CA 1569 C C . THR A 196 ? 1.7196 1.4377 1.2114 -0.0785 -0.0411 0.1039 215 THR A C 1570 O O . THR A 196 ? 1.7636 1.5050 1.2445 -0.0703 -0.0182 0.1122 215 THR A O 1571 C CB . THR A 196 ? 1.8355 1.4965 1.2563 -0.0741 -0.0396 0.0502 215 THR A CB 1572 O OG1 . THR A 196 ? 1.8445 1.4765 1.2225 -0.0858 -0.0596 0.0289 215 THR A OG1 1573 C CG2 . THR A 196 ? 1.8871 1.5360 1.3666 -0.0618 -0.0335 0.0512 215 THR A CG2 1574 N N . ILE A 197 ? 1.6864 1.4067 1.2319 -0.0818 -0.0556 0.1193 216 ILE A N 1575 C CA . ILE A 197 ? 1.6971 1.4429 1.3021 -0.0759 -0.0483 0.1469 216 ILE A CA 1576 C C . ILE A 197 ? 1.7803 1.5188 1.4283 -0.0623 -0.0357 0.1482 216 ILE A C 1577 O O . ILE A 197 ? 1.7948 1.5123 1.4548 -0.0682 -0.0547 0.1425 216 ILE A O 1578 C CB . ILE A 197 ? 1.6322 1.3843 1.2697 -0.0914 -0.0781 0.1631 216 ILE A CB 1579 C CG1 . ILE A 197 ? 1.5681 1.3231 1.1731 -0.1026 -0.0896 0.1584 216 ILE A CG1 1580 C CG2 . ILE A 197 ? 1.6545 1.4313 1.3611 -0.0873 -0.0750 0.1944 216 ILE A CG2 1581 C CD1 . ILE A 197 ? 1.5245 1.2753 1.1502 -0.1161 -0.1183 0.1599 216 ILE A CD1 1582 N N . GLU A 198 ? 1.8546 1.6134 1.5284 -0.0435 -0.0021 0.1578 217 GLU A N 1583 C CA . GLU A 198 ? 1.9556 1.7114 1.6846 -0.0260 0.0163 0.1611 217 GLU A CA 1584 C C . GLU A 198 ? 1.9831 1.7777 1.7857 -0.0167 0.0327 0.1991 217 GLU A C 1585 O O . GLU A 198 ? 2.0304 1.8548 1.8267 -0.0034 0.0668 0.2074 217 GLU A O 1586 C CB . GLU A 198 ? 2.0682 1.8057 1.7567 -0.0061 0.0499 0.1261 217 GLU A CB 1587 C CG . GLU A 198 ? 2.0925 1.7854 1.7375 -0.0147 0.0284 0.0929 217 GLU A CG 1588 C CD . GLU A 198 ? 2.2298 1.8942 1.9248 -0.0031 0.0298 0.0822 217 GLU A CD 1589 O OE1 . GLU A 198 ? 2.2787 1.9580 2.0553 0.0061 0.0360 0.1081 217 GLU A OE1 1590 O OE2 . GLU A 198 ? 2.2730 1.9000 1.9337 -0.0049 0.0209 0.0511 217 GLU A OE2 1591 N N . LEU A 199 ? 1.9704 1.7684 1.8431 -0.0260 0.0062 0.2262 218 LEU A N 1592 C CA . LEU A 199 ? 2.0148 1.8487 1.9734 -0.0203 0.0141 0.2683 218 LEU A CA 1593 C C . LEU A 199 ? 2.1171 1.9496 2.1501 -0.0049 0.0267 0.2794 218 LEU A C 1594 O O . LEU A 199 ? 2.1502 1.9506 2.1707 -0.0034 0.0197 0.2565 218 LEU A O 1595 C CB . LEU A 199 ? 1.9445 1.7838 1.9349 -0.0457 -0.0320 0.2943 218 LEU A CB 1596 C CG . LEU A 199 ? 1.8604 1.6919 1.7891 -0.0630 -0.0533 0.2799 218 LEU A CG 1597 C CD1 . LEU A 199 ? 1.8342 1.6602 1.7943 -0.0856 -0.0992 0.2943 218 LEU A CD1 1598 C CD2 . LEU A 199 ? 1.8592 1.7212 1.7773 -0.0548 -0.0254 0.2918 218 LEU A CD2 1599 N N . GLU A 200 ? 2.1839 2.0531 2.3050 0.0064 0.0442 0.3190 219 GLU A N 1600 C CA . GLU A 200 ? 2.2988 2.1744 2.5141 0.0226 0.0577 0.3393 219 GLU A CA 1601 C C . GLU A 200 ? 2.2845 2.1407 2.5424 -0.0018 0.0021 0.3574 219 GLU A C 1602 O O . GLU A 200 ? 2.1996 2.0503 2.4312 -0.0300 -0.0432 0.3645 219 GLU A O 1603 C CB . GLU A 200 ? 2.3661 2.2940 2.6715 0.0370 0.0866 0.3860 219 GLU A CB 1604 C CG . GLU A 200 ? 2.4913 2.4345 2.9161 0.0549 0.1022 0.4168 219 GLU A CG 1605 C CD . GLU A 200 ? 2.7699 2.7701 3.2970 0.0632 0.1213 0.4740 219 GLU A CD 1606 O OE1 . GLU A 200 ? 2.6550 2.6856 3.1515 0.0631 0.1386 0.4837 219 GLU A OE1 1607 O OE2 . GLU A 200 ? 3.2574 3.1856 3.5986 0.0409 0.0678 0.3378 219 GLU A OE2 1608 N N . GLU A 201 ? 2.3911 2.2378 2.7157 0.0094 0.0060 0.3649 220 GLU A N 1609 C CA . GLU A 201 ? 2.4194 2.2547 2.7943 -0.0134 -0.0451 0.3906 220 GLU A CA 1610 C C . GLU A 201 ? 2.3936 2.2554 2.8232 -0.0371 -0.0849 0.4374 220 GLU A C 1611 O O . GLU A 201 ? 2.4331 2.3299 2.9379 -0.0250 -0.0639 0.4707 220 GLU A O 1612 C CB . GLU A 201 ? 2.5708 2.4030 3.0421 0.0076 -0.0268 0.4040 220 GLU A CB 1613 C CG . GLU A 201 ? 2.6803 2.5027 3.2052 -0.0176 -0.0816 0.4353 220 GLU A CG 1614 C CD . GLU A 201 ? 2.6044 2.3916 3.0480 -0.0380 -0.1144 0.4078 220 GLU A CD 1615 O OE1 . GLU A 201 ? 2.4946 2.2681 2.8281 -0.0482 -0.1179 0.3728 220 GLU A OE1 1616 O OE2 . GLU A 201 ? 2.8434 2.6207 3.3423 -0.0453 -0.1385 0.4276 220 GLU A OE2 1617 N N . GLY A 202 ? 2.3457 2.1917 2.7338 -0.0709 -0.1416 0.4385 221 GLY A N 1618 C CA . GLY A 202 ? 2.3467 2.2088 2.7761 -0.0973 -0.1879 0.4751 221 GLY A CA 1619 C C . GLY A 202 ? 2.2442 2.0998 2.5994 -0.1143 -0.2069 0.4548 221 GLY A C 1620 O O . GLY A 202 ? 2.2599 2.1173 2.6344 -0.1403 -0.2543 0.4747 221 GLY A O 1621 N N . PHE A 203 ? 2.1576 2.0048 2.4344 -0.1003 -0.1725 0.4164 222 PHE A N 1622 C CA . PHE A 203 ? 2.0689 1.9086 2.2819 -0.1138 -0.1873 0.3961 222 PHE A CA 1623 C C . PHE A 203 ? 2.0241 1.8322 2.1432 -0.1320 -0.2151 0.3586 222 PHE A C 1624 O O . PHE A 203 ? 2.0295 1.8237 2.1158 -0.1269 -0.2057 0.3418 222 PHE A O 1625 C CB . PHE A 203 ? 2.0175 1.8710 2.2014 -0.0918 -0.1386 0.3823 222 PHE A CB 1626 C CG . PHE A 203 ? 2.0672 1.9613 2.3368 -0.0786 -0.1142 0.4241 222 PHE A CG 1627 C CD1 . PHE A 203 ? 2.0755 1.9839 2.4017 -0.0962 -0.1472 0.4565 222 PHE A CD1 1628 C CD2 . PHE A 203 ? 2.1312 2.0502 2.4256 -0.0484 -0.0575 0.4305 222 PHE A CD2 1629 C CE1 . PHE A 203 ? 2.1356 2.0875 2.5518 -0.0853 -0.1255 0.5033 222 PHE A CE1 1630 C CE2 . PHE A 203 ? 2.1929 2.1584 2.5676 -0.0352 -0.0298 0.4738 222 PHE A CE2 1631 C CZ . PHE A 203 ? 2.1851 2.1692 2.6239 -0.0545 -0.0645 0.5137 222 PHE A CZ 1632 N N . MET A 204 ? 1.9976 1.7949 2.0804 -0.1529 -0.2493 0.3466 223 MET A N 1633 C CA . MET A 204 ? 1.9773 1.7505 1.9712 -0.1687 -0.2711 0.3109 223 MET A CA 1634 C C . MET A 204 ? 1.8924 1.6571 1.8334 -0.1663 -0.2610 0.2809 223 MET A C 1635 O O . MET A 204 ? 1.8949 1.6628 1.8669 -0.1718 -0.2745 0.2886 223 MET A O 1636 C CB . MET A 204 ? 2.0650 1.8314 2.0598 -0.1973 -0.3247 0.3200 223 MET A CB 1637 C CG . MET A 204 ? 2.1629 1.9380 2.2002 -0.2041 -0.3405 0.3511 223 MET A CG 1638 S SD . MET A 204 ? 2.3205 2.0944 2.3620 -0.2427 -0.4103 0.3715 223 MET A SD 1639 C CE . MET A 204 ? 2.3068 2.0577 2.2570 -0.2565 -0.4291 0.3217 223 MET A CE 1640 N N . VAL A 205 ? 1.8313 1.5856 1.7030 -0.1587 -0.2394 0.2506 224 VAL A N 1641 C CA . VAL A 205 ? 1.7564 1.5053 1.5846 -0.1551 -0.2272 0.2260 224 VAL A CA 1642 C C . VAL A 205 ? 1.7666 1.4988 1.5516 -0.1717 -0.2561 0.1999 224 VAL A C 1643 O O . VAL A 205 ? 1.7951 1.5187 1.5310 -0.1811 -0.2679 0.1837 224 VAL A O 1644 C CB . VAL A 205 ? 1.7037 1.4504 1.4832 -0.1403 -0.1928 0.2081 224 VAL A CB 1645 C CG1 . VAL A 205 ? 1.6346 1.3809 1.3814 -0.1379 -0.1825 0.1917 224 VAL A CG1 1646 C CG2 . VAL A 205 ? 1.7223 1.4819 1.5361 -0.1214 -0.1606 0.2247 224 VAL A CG2 1647 N N . ASN A 206 ? 1.7590 1.4881 1.5635 -0.1740 -0.2648 0.1955 225 ASN A N 1648 C CA . ASN A 206 ? 1.7833 1.4930 1.5506 -0.1848 -0.2858 0.1630 225 ASN A CA 1649 C C . ASN A 206 ? 1.7070 1.4165 1.4526 -0.1735 -0.2613 0.1462 225 ASN A C 1650 O O . ASN A 206 ? 1.6577 1.3805 1.4418 -0.1643 -0.2451 0.1660 225 ASN A O 1651 C CB . ASN A 206 ? 1.8630 1.5617 1.6781 -0.1981 -0.3222 0.1671 225 ASN A CB 1652 C CG . ASN A 206 ? 1.9689 1.6680 1.8056 -0.2141 -0.3545 0.1863 225 ASN A CG 1653 O OD1 . ASN A 206 ? 1.9978 1.7034 1.8052 -0.2178 -0.3542 0.1920 225 ASN A OD1 1654 N ND2 . ASN A 206 ? 2.0387 1.7314 1.9349 -0.2259 -0.3874 0.2008 225 ASN A ND2 1655 N N . LEU A 207 ? 1.7082 1.4080 1.3942 -0.1746 -0.2574 0.1150 226 LEU A N 1656 C CA . LEU A 207 ? 1.6518 1.3529 1.3214 -0.1654 -0.2369 0.1015 226 LEU A CA 1657 C C . LEU A 207 ? 1.7068 1.3916 1.3809 -0.1682 -0.2501 0.0733 226 LEU A C 1658 O O . LEU A 207 ? 1.7945 1.4654 1.4416 -0.1770 -0.2687 0.0487 226 LEU A O 1659 C CB . LEU A 207 ? 1.6156 1.3216 1.2279 -0.1624 -0.2185 0.0918 226 LEU A CB 1660 C CG . LEU A 207 ? 1.5880 1.3024 1.1945 -0.1581 -0.2052 0.1114 226 LEU A CG 1661 C CD1 . LEU A 207 ? 1.5804 1.2944 1.1376 -0.1597 -0.1976 0.1007 226 LEU A CD1 1662 C CD2 . LEU A 207 ? 1.5325 1.2574 1.1631 -0.1470 -0.1847 0.1291 226 LEU A CD2 1663 N N . GLN A 208 ? 1.6751 1.3621 1.3836 -0.1608 -0.2410 0.0767 227 GLN A N 1664 C CA . GLN A 208 ? 1.7432 1.4122 1.4744 -0.1599 -0.2513 0.0503 227 GLN A CA 1665 C C . GLN A 208 ? 1.6990 1.3776 1.4472 -0.1503 -0.2320 0.0542 227 GLN A C 1666 O O . GLN A 208 ? 1.6591 1.3531 1.4511 -0.1483 -0.2275 0.0871 227 GLN A O 1667 C CB . GLN A 208 ? 1.8060 1.4616 1.6061 -0.1663 -0.2793 0.0600 227 GLN A CB 1668 C CG . GLN A 208 ? 1.9013 1.5316 1.7416 -0.1644 -0.2933 0.0315 227 GLN A CG 1669 C CD . GLN A 208 ? 2.0144 1.6210 1.9085 -0.1753 -0.3307 0.0293 227 GLN A CD 1670 O OE1 . GLN A 208 ? 1.9974 1.6166 1.9413 -0.1820 -0.3435 0.0696 227 GLN A OE1 1671 N NE2 . GLN A 208 ? 2.1386 1.7101 2.0273 -0.1771 -0.3491 -0.0186 227 GLN A NE2 1672 N N . PHE A 209 ? 1.7235 1.3972 1.4399 -0.1454 -0.2208 0.0244 228 PHE A N 1673 C CA . PHE A 209 ? 1.6965 1.3800 1.4378 -0.1373 -0.2053 0.0298 228 PHE A CA 1674 C C . PHE A 209 ? 1.7724 1.4410 1.5911 -0.1335 -0.2179 0.0246 228 PHE A C 1675 O O . PHE A 209 ? 1.8679 1.5104 1.7020 -0.1348 -0.2353 -0.0041 228 PHE A O 1676 C CB . PHE A 209 ? 1.7118 1.4002 1.4049 -0.1322 -0.1870 0.0050 228 PHE A CB 1677 C CG . PHE A 209 ? 1.6372 1.3434 1.2744 -0.1362 -0.1754 0.0210 228 PHE A CG 1678 C CD1 . PHE A 209 ? 1.6547 1.3596 1.2397 -0.1427 -0.1793 0.0130 228 PHE A CD1 1679 C CD2 . PHE A 209 ? 1.5664 1.2894 1.2071 -0.1355 -0.1647 0.0456 228 PHE A CD2 1680 C CE1 . PHE A 209 ? 1.6042 1.3218 1.1506 -0.1464 -0.1715 0.0289 228 PHE A CE1 1681 C CE2 . PHE A 209 ? 1.5171 1.2495 1.1104 -0.1399 -0.1583 0.0565 228 PHE A CE2 1682 C CZ . PHE A 209 ? 1.5340 1.2626 1.0850 -0.1444 -0.1610 0.0477 228 PHE A CZ 1683 N N . GLU A 210 ? 1.7412 1.4256 1.6114 -0.1305 -0.2126 0.0539 229 GLU A N 1684 C CA . GLU A 210 ? 1.8251 1.4990 1.7866 -0.1275 -0.2260 0.0591 229 GLU A CA 1685 C C . GLU A 210 ? 1.8171 1.5092 1.8190 -0.1223 -0.2146 0.0791 229 GLU A C 1686 O O . GLU A 210 ? 1.7392 1.4558 1.6984 -0.1245 -0.2002 0.0986 229 GLU A O 1687 C CB . GLU A 210 ? 1.8333 1.5121 1.8521 -0.1361 -0.2465 0.0966 229 GLU A CB 1688 C CG . GLU A 210 ? 1.7436 1.4593 1.7407 -0.1417 -0.2358 0.1456 229 GLU A CG 1689 C CD . GLU A 210 ? 1.7611 1.4874 1.7923 -0.1485 -0.2481 0.1785 229 GLU A CD 1690 O OE1 . GLU A 210 ? 1.8102 1.5125 1.8583 -0.1519 -0.2673 0.1600 229 GLU A OE1 1691 O OE2 . GLU A 210 ? 1.7314 1.4927 1.7696 -0.1512 -0.2380 0.2238 229 GLU A OE2 1692 N N . ASP A 211 ? 1.9199 1.5980 2.0108 -0.1164 -0.2245 0.0746 230 ASP A N 1693 C CA . ASP A 211 ? 1.9471 1.6407 2.1028 -0.1114 -0.2187 0.0966 230 ASP A CA 1694 C C . ASP A 211 ? 1.9290 1.6298 2.0398 -0.1020 -0.1934 0.0721 230 ASP A C 1695 O O . ASP A 211 ? 1.9523 1.6361 2.0064 -0.0946 -0.1809 0.0243 230 ASP A O 1696 C CB . ASP A 211 ? 1.8911 1.6225 2.0744 -0.1242 -0.2268 0.1640 230 ASP A CB 1697 C CG . ASP A 211 ? 1.9325 1.6672 2.1718 -0.1331 -0.2484 0.1976 230 ASP A CG 1698 O OD1 . ASP A 211 ? 2.0069 1.7109 2.3113 -0.1295 -0.2655 0.1768 230 ASP A OD1 1699 O OD2 . ASP A 211 ? 1.9065 1.6753 2.1270 -0.1437 -0.2482 0.2451 230 ASP A OD2 1700 N N . ILE A 212 ? 1.9025 1.6319 2.0399 -0.1041 -0.1877 0.1086 231 ILE A N 1701 C CA . ILE A 212 ? 1.8919 1.6349 2.0049 -0.0972 -0.1663 0.0980 231 ILE A CA 1702 C C . ILE A 212 ? 1.7950 1.5448 1.7965 -0.1025 -0.1543 0.0852 231 ILE A C 1703 O O . ILE A 212 ? 1.7042 1.4630 1.6551 -0.1152 -0.1628 0.1087 231 ILE A O 1704 C CB . ILE A 212 ? 1.8858 1.6599 2.0597 -0.1036 -0.1719 0.1503 231 ILE A CB 1705 C CG1 . ILE A 212 ? 2.0116 1.7794 2.3152 -0.0952 -0.1813 0.1617 231 ILE A CG1 1706 C CG2 . ILE A 212 ? 1.8571 1.6511 1.9984 -0.1016 -0.1541 0.1506 231 ILE A CG2 1707 C CD1 . ILE A 212 ? 2.0204 1.8222 2.3944 -0.1092 -0.2002 0.2306 231 ILE A CD1 1708 N N . PHE A 213 ? 1.8333 1.5808 1.8023 -0.0920 -0.1332 0.0493 232 PHE A N 1709 C CA . PHE A 213 ? 1.7718 1.5303 1.6514 -0.0970 -0.1219 0.0424 232 PHE A CA 1710 C C . PHE A 213 ? 1.8023 1.5839 1.7022 -0.0897 -0.1018 0.0469 232 PHE A C 1711 O O . PHE A 213 ? 1.9052 1.6847 1.8340 -0.0732 -0.0815 0.0158 232 PHE A O 1712 C CB . PHE A 213 ? 1.8130 1.5525 1.6290 -0.0943 -0.1176 -0.0005 232 PHE A CB 1713 C CG . PHE A 213 ? 1.7534 1.5063 1.4863 -0.1031 -0.1120 0.0035 232 PHE A CG 1714 C CD1 . PHE A 213 ? 1.6660 1.4153 1.3574 -0.1158 -0.1270 0.0219 232 PHE A CD1 1715 C CD2 . PHE A 213 ? 1.7991 1.5705 1.5037 -0.0980 -0.0905 -0.0082 232 PHE A CD2 1716 C CE1 . PHE A 213 ? 1.6318 1.3900 1.2598 -0.1234 -0.1241 0.0264 232 PHE A CE1 1717 C CE2 . PHE A 213 ? 1.7621 1.5470 1.4019 -0.1079 -0.0891 0.0018 232 PHE A CE2 1718 C CZ . PHE A 213 ? 1.6817 1.4570 1.2859 -0.1207 -0.1076 0.0179 232 PHE A CZ 1719 N N . ASP A 214 ? 1.7254 1.5293 1.6160 -0.1017 -0.1079 0.0860 233 ASP A N 1720 C CA . ASP A 214 ? 1.7523 1.5826 1.6748 -0.0988 -0.0950 0.1029 233 ASP A CA 1721 C C . ASP A 214 ? 1.6738 1.5190 1.5388 -0.1154 -0.1032 0.1284 233 ASP A C 1722 O O . ASP A 214 ? 1.6216 1.4726 1.4892 -0.1307 -0.1247 0.1635 233 ASP A O 1723 C CB . ASP A 214 ? 1.7905 1.6316 1.8152 -0.0969 -0.1035 0.1344 233 ASP A CB 1724 C CG . ASP A 214 ? 1.8291 1.7009 1.9086 -0.0951 -0.0941 0.1613 233 ASP A CG 1725 O OD1 . ASP A 214 ? 1.8433 1.7294 1.8945 -0.0888 -0.0721 0.1478 233 ASP A OD1 1726 O OD2 . ASP A 214 ? 1.8564 1.7417 2.0137 -0.1006 -0.1096 0.2004 233 ASP A OD2 1727 N N . ILE A 215 ? 1.6853 1.5366 1.4979 -0.1132 -0.0878 0.1104 234 ILE A N 1728 C CA . ILE A 215 ? 1.6366 1.4995 1.4040 -0.1280 -0.0959 0.1317 234 ILE A CA 1729 C C . ILE A 215 ? 1.7071 1.6013 1.5025 -0.1210 -0.0735 0.1380 234 ILE A C 1730 O O . ILE A 215 ? 1.7922 1.6943 1.5821 -0.1055 -0.0462 0.1090 234 ILE A O 1731 C CB . ILE A 215 ? 1.5997 1.4451 1.2863 -0.1349 -0.1016 0.1147 234 ILE A CB 1732 C CG1 . ILE A 215 ? 1.5490 1.3684 1.2184 -0.1381 -0.1175 0.1087 234 ILE A CG1 1733 C CG2 . ILE A 215 ? 1.5678 1.4202 1.2207 -0.1502 -0.1134 0.1371 234 ILE A CG2 1734 C CD1 . ILE A 215 ? 1.5161 1.3194 1.1221 -0.1438 -0.1237 0.0970 234 ILE A CD1 1735 N N . GLU A 216 ? 1.6898 1.6039 1.5146 -0.1329 -0.0852 0.1766 235 GLU A N 1736 C CA . GLU A 216 ? 1.7584 1.7093 1.6230 -0.1282 -0.0655 0.1941 235 GLU A CA 1737 C C . GLU A 216 ? 1.8087 1.7718 1.6165 -0.1242 -0.0442 0.1756 235 GLU A C 1738 O O . GLU A 216 ? 1.7634 1.7099 1.5063 -0.1372 -0.0607 0.1725 235 GLU A O 1739 C CB . GLU A 216 ? 1.7250 1.6885 1.6144 -0.1494 -0.0937 0.2412 235 GLU A CB 1740 C CG . GLU A 216 ? 1.8021 1.8092 1.7643 -0.1452 -0.0770 0.2720 235 GLU A CG 1741 C CD . GLU A 216 ? 1.7837 1.8011 1.7657 -0.1706 -0.1114 0.3194 235 GLU A CD 1742 O OE1 . GLU A 216 ? 1.7151 1.7017 1.6458 -0.1911 -0.1482 0.3226 235 GLU A OE1 1743 O OE2 . GLU A 216 ? 1.8509 1.9072 1.9014 -0.1699 -0.1016 0.3526 235 GLU A OE2 1744 N N . ASP A 217 ? 1.9201 1.9140 1.7539 -0.1057 -0.0066 0.1636 236 ASP A N 1745 C CA . ASP A 217 ? 2.0023 2.0181 1.7808 -0.1023 0.0169 0.1499 236 ASP A CA 1746 C C . ASP A 217 ? 2.1171 2.1877 1.9440 -0.0927 0.0504 0.1732 236 ASP A C 1747 O O . ASP A 217 ? 2.1240 2.2132 2.0350 -0.0879 0.0545 0.1998 236 ASP A O 1748 C CB . ASP A 217 ? 2.0705 2.0661 1.7991 -0.0874 0.0345 0.0956 236 ASP A CB 1749 C CG . ASP A 217 ? 2.1991 2.2006 1.9756 -0.0605 0.0691 0.0623 236 ASP A CG 1750 O OD1 . ASP A 217 ? 2.2244 2.2440 2.0877 -0.0513 0.0796 0.0836 236 ASP A OD1 1751 O OD2 . ASP A 217 ? 2.2964 2.2825 2.0274 -0.0490 0.0837 0.0143 236 ASP A OD2 1752 N N . HIS A 218 ? 2.2233 2.3240 2.0001 -0.0900 0.0752 0.1665 237 HIS A N 1753 C CA . HIS A 218 ? 2.3591 2.5212 2.1706 -0.0791 0.1150 0.1880 237 HIS A CA 1754 C C . HIS A 218 ? 2.5294 2.7079 2.2831 -0.0583 0.1591 0.1392 237 HIS A C 1755 O O . HIS A 218 ? 2.5333 2.6860 2.2020 -0.0656 0.1464 0.1095 237 HIS A O 1756 C CB . HIS A 218 ? 2.3499 2.5423 2.1529 -0.1026 0.0976 0.2402 237 HIS A CB 1757 C CG . HIS A 218 ? 2.4816 2.7429 2.3453 -0.0953 0.1323 0.2801 237 HIS A CG 1758 N ND1 . HIS A 218 ? 2.6783 2.9914 2.5039 -0.0837 0.1771 0.2739 237 HIS A ND1 1759 C CD2 . HIS A 218 ? 2.4744 2.7634 2.4349 -0.0988 0.1280 0.3287 237 HIS A CD2 1760 C CE1 . HIS A 218 ? 3.6367 3.7172 3.4612 -0.0935 0.1949 0.1667 237 HIS A CE1 1761 N NE2 . HIS A 218 ? 2.6382 2.9983 2.6294 -0.0877 0.1728 0.3551 237 HIS A NE2 1762 N N . PRO A 219 ? 2.6887 2.9098 2.4873 -0.0323 0.2104 0.1295 238 PRO A N 1763 C CA . PRO A 219 ? 3.7581 3.7978 3.6842 -0.0085 0.0691 0.0142 238 PRO A CA 1768 C CD . PRO A 219 ? 2.7112 2.9666 2.6257 -0.0198 0.2301 0.1647 238 PRO A CD 1771 C C . GLU A 220 ? 3.7910 3.7957 3.7458 -0.0057 0.0214 0.0143 239 GLU A C 1772 O O . GLU A 220 ? 3.7888 3.7946 3.7141 -0.0073 0.0302 0.0206 239 GLU A O 1778 N N . VAL A 221 ? 3.7833 3.7867 3.6851 -0.0145 0.0432 0.0383 240 VAL A N 1779 C CA . VAL A 221 ? 3.7306 3.7313 3.3170 -0.0580 0.1339 0.1784 240 VAL A CA 1780 C C . VAL A 221 ? 2.5952 2.7935 2.1493 -0.1388 0.0769 0.2222 240 VAL A C 1781 O O . VAL A 221 ? 2.4160 2.5794 2.0080 -0.1281 0.0725 0.2008 240 VAL A O 1782 C CB . VAL A 221 ? 2.9316 3.2146 2.6045 -0.1531 0.0835 0.3254 240 VAL A CB 1783 C CG1 . VAL A 221 ? 2.7146 2.9591 2.3684 -0.1805 0.0306 0.3465 240 VAL A CG1 1784 C CG2 . VAL A 221 ? 3.7814 3.7681 3.6712 -0.0239 0.0482 0.0636 240 VAL A CG2 1785 N N . PRO A 222 ? 2.7275 2.9052 2.2164 -0.1542 0.0519 0.2163 241 PRO A N 1786 C CA . PRO A 222 ? 2.3897 2.5026 1.8508 -0.1568 0.0216 0.1819 241 PRO A CA 1787 C C . PRO A 222 ? 2.2149 2.2866 1.7217 -0.1676 -0.0152 0.2011 241 PRO A C 1788 O O . PRO A 222 ? 2.1923 2.2640 1.7111 -0.1858 -0.0407 0.2373 241 PRO A O 1789 C CB . PRO A 222 ? 2.5974 2.7121 1.9898 -0.1715 0.0068 0.1822 241 PRO A CB 1790 C CG . PRO A 222 ? 3.4742 3.6442 2.8739 -0.1817 0.0150 0.2316 241 PRO A CG 1791 C CD . PRO A 222 ? 3.7887 3.7628 3.4121 -0.0200 0.0648 0.1194 241 PRO A CD 1792 N N . CYS A 223 ? 2.1170 2.1546 1.6500 -0.1566 -0.0179 0.1766 242 CYS A N 1793 C CA . CYS A 223 ? 1.9741 1.9722 1.5379 -0.1647 -0.0494 0.1860 242 CYS A CA 1794 C C . CYS A 223 ? 1.9477 1.9534 1.5459 -0.1829 -0.0732 0.2309 242 CYS A C 1795 O O . CYS A 223 ? 1.9018 1.8778 1.4808 -0.1974 -0.1032 0.2377 242 CYS A O 1796 C CB . CYS A 223 ? 1.8997 1.8502 1.4213 -0.1683 -0.0718 0.1606 242 CYS A CB 1797 S SG . CYS A 223 ? 1.9584 1.8955 1.4442 -0.1521 -0.0541 0.1109 242 CYS A SG 1798 N N . PRO A 224 ? 1.9928 2.0368 1.6477 -0.1820 -0.0610 0.2613 243 PRO A N 1799 C CA . PRO A 224 ? 1.9868 2.0365 1.6805 -0.2021 -0.0892 0.3057 243 PRO A CA 1800 C C . PRO A 224 ? 1.8832 1.8954 1.6039 -0.2120 -0.1230 0.3108 243 PRO A C 1801 O O . PRO A 224 ? 1.8823 1.8851 1.6241 -0.2316 -0.1555 0.3394 243 PRO A O 1802 C CB . PRO A 224 ? 2.0937 2.2074 1.8413 -0.1965 -0.0594 0.3397 243 PRO A CB 1803 C CG . PRO A 224 ? 2.1124 2.2387 1.8725 -0.1714 -0.0218 0.3098 243 PRO A CG 1804 C CD . PRO A 224 ? 2.0697 2.1545 1.7628 -0.1623 -0.0206 0.2577 243 PRO A CD 1805 N N . TYR A 225 ? 1.8172 1.8092 1.5382 -0.2004 -0.1180 0.2850 244 TYR A N 1806 C CA . TYR A 225 ? 1.7480 1.7137 1.4906 -0.2104 -0.1478 0.2932 244 TYR A CA 1807 C C . TYR A 225 ? 1.6714 1.5873 1.3575 -0.2132 -0.1672 0.2633 244 TYR A C 1808 O O . TYR A 225 ? 1.6520 1.5380 1.3133 -0.2295 -0.1985 0.2669 244 TYR A O 1809 C CB . TYR A 225 ? 1.7601 1.7503 1.5662 -0.1977 -0.1299 0.3011 244 TYR A CB 1810 C CG . TYR A 225 ? 1.8555 1.9006 1.7237 -0.1885 -0.0997 0.3272 244 TYR A CG 1811 C CD1 . TYR A 225 ? 1.8997 1.9713 1.8074 -0.2050 -0.1147 0.3721 244 TYR A CD1 1812 C CD2 . TYR A 225 ? 1.9200 1.9910 1.8111 -0.1625 -0.0552 0.3065 244 TYR A CD2 1813 C CE1 . TYR A 225 ? 2.0006 2.1309 1.9706 -0.1955 -0.0824 0.4014 244 TYR A CE1 1814 C CE2 . TYR A 225 ? 2.0317 2.1579 1.9789 -0.1506 -0.0200 0.3284 244 TYR A CE2 1815 C CZ . TYR A 225 ? 2.0670 2.2264 2.0545 -0.1670 -0.0321 0.3789 244 TYR A CZ 1816 O OH . TYR A 225 ? 2.1891 2.4106 2.2388 -0.1546 0.0060 0.4066 244 TYR A OH 1817 N N . ASP A 226 ? 1.6409 1.5485 1.3116 -0.1969 -0.1482 0.2338 245 ASP A N 1818 C CA . ASP A 226 ? 1.5757 1.4456 1.2026 -0.1963 -0.1597 0.2092 245 ASP A CA 1819 C C . ASP A 226 ? 1.5843 1.4474 1.1728 -0.1848 -0.1415 0.1800 245 ASP A C 1820 O O . ASP A 226 ? 1.6412 1.5293 1.2370 -0.1745 -0.1172 0.1733 245 ASP A O 1821 C CB . ASP A 226 ? 1.5464 1.4148 1.2046 -0.1912 -0.1607 0.2100 245 ASP A CB 1822 C CG . ASP A 226 ? 1.5642 1.4475 1.2709 -0.2036 -0.1795 0.2449 245 ASP A CG 1823 O OD1 . ASP A 226 ? 1.5728 1.4520 1.2706 -0.2212 -0.2032 0.2635 245 ASP A OD1 1824 O OD2 . ASP A 226 ? 1.5676 1.4653 1.3267 -0.1972 -0.1741 0.2551 245 ASP A OD2 1825 N N . TYR A 227 ? 1.5411 1.3727 1.0882 -0.1867 -0.1528 0.1634 246 TYR A N 1826 C CA . TYR A 227 ? 1.5567 1.3812 1.0722 -0.1793 -0.1424 0.1411 246 TYR A CA 1827 C C . TYR A 227 ? 1.5122 1.3055 0.9997 -0.1794 -0.1533 0.1279 246 TYR A C 1828 O O . TYR A 227 ? 1.4809 1.2558 0.9591 -0.1861 -0.1680 0.1334 246 TYR A O 1829 C CB . TYR A 227 ? 1.6243 1.4643 1.1240 -0.1858 -0.1410 0.1509 246 TYR A CB 1830 C CG . TYR A 227 ? 1.6294 1.4553 1.1275 -0.2005 -0.1642 0.1702 246 TYR A CG 1831 C CD1 . TYR A 227 ? 1.6160 1.4107 1.0897 -0.2039 -0.1784 0.1612 246 TYR A CD1 1832 C CD2 . TYR A 227 ? 1.6547 1.4972 1.1834 -0.2107 -0.1728 0.1973 246 TYR A CD2 1833 C CE1 . TYR A 227 ? 1.6417 1.4165 1.1186 -0.2157 -0.2003 0.1724 246 TYR A CE1 1834 C CE2 . TYR A 227 ? 1.6781 1.5011 1.2097 -0.2257 -0.1994 0.2119 246 TYR A CE2 1835 C CZ . TYR A 227 ? 1.6777 1.4644 1.1818 -0.2275 -0.2128 0.1965 246 TYR A CZ 1836 O OH . TYR A 227 ? 1.7273 1.4883 1.2386 -0.2406 -0.2394 0.2048 246 TYR A OH 1837 N N . ILE A 228 ? 1.5241 1.3131 0.9966 -0.1725 -0.1458 0.1103 247 ILE A N 1838 C CA . ILE A 228 ? 1.4991 1.2652 0.9540 -0.1713 -0.1528 0.1014 247 ILE A CA 1839 C C . ILE A 228 ? 1.5555 1.3226 0.9909 -0.1762 -0.1568 0.1027 247 ILE A C 1840 O O . ILE A 228 ? 1.6194 1.4057 1.0465 -0.1768 -0.1501 0.0999 247 ILE A O 1841 C CB . ILE A 228 ? 1.4883 1.2494 0.9558 -0.1622 -0.1476 0.0870 247 ILE A CB 1842 C CG1 . ILE A 228 ? 1.4452 1.2079 0.9416 -0.1590 -0.1469 0.0935 247 ILE A CG1 1843 C CG2 . ILE A 228 ? 1.4786 1.2231 0.9356 -0.1615 -0.1538 0.0835 247 ILE A CG2 1844 C CD1 . ILE A 228 ? 1.4481 1.2071 0.9730 -0.1511 -0.1445 0.0838 247 ILE A CD1 1845 N N . LYS A 229 ? 1.5511 1.2988 0.9801 -0.1796 -0.1673 0.1072 248 LYS A N 1846 C CA . LYS A 229 ? 1.6093 1.3551 1.0331 -0.1846 -0.1752 0.1136 248 LYS A CA 1847 C C . LYS A 229 ? 1.5860 1.3124 1.0152 -0.1777 -0.1763 0.1057 248 LYS A C 1848 O O . LYS A 229 ? 1.5364 1.2479 0.9682 -0.1714 -0.1722 0.1000 248 LYS A O 1849 C CB . LYS A 229 ? 1.6539 1.3924 1.0850 -0.1935 -0.1874 0.1293 248 LYS A CB 1850 C CG . LYS A 229 ? 1.7120 1.4787 1.1477 -0.2032 -0.1884 0.1484 248 LYS A CG 1851 C CD . LYS A 229 ? 1.7509 1.5043 1.2059 -0.2134 -0.2062 0.1657 248 LYS A CD 1852 C CE . LYS A 229 ? 1.8319 1.6188 1.3025 -0.2250 -0.2090 0.1945 248 LYS A CE 1853 N NZ . LYS A 229 ? 1.8879 1.6579 1.3883 -0.2371 -0.2324 0.2140 248 LYS A NZ 1854 N N . ILE A 230 ? 1.6297 1.3605 1.0608 -0.1797 -0.1817 0.1080 249 ILE A N 1855 C CA . ILE A 230 ? 1.6204 1.3382 1.0693 -0.1738 -0.1834 0.1070 249 ILE A CA 1856 C C . ILE A 230 ? 1.6963 1.4104 1.1613 -0.1793 -0.1956 0.1230 249 ILE A C 1857 O O . ILE A 230 ? 1.7647 1.4944 1.2236 -0.1900 -0.2076 0.1337 249 ILE A O 1858 C CB . ILE A 230 ? 1.6137 1.3372 1.0664 -0.1717 -0.1840 0.0981 249 ILE A CB 1859 C CG1 . ILE A 230 ? 1.5546 1.2801 1.0077 -0.1653 -0.1732 0.0858 249 ILE A CG1 1860 C CG2 . ILE A 230 ? 1.6124 1.3273 1.0954 -0.1672 -0.1878 0.1056 249 ILE A CG2 1861 C CD1 . ILE A 230 ? 1.5716 1.2988 1.0344 -0.1639 -0.1766 0.0730 249 ILE A CD1 1862 N N . LYS A 231 ? 1.7009 1.3954 1.1873 -0.1721 -0.1926 0.1246 250 LYS A N 1863 C CA . LYS A 231 ? 1.7875 1.4756 1.3066 -0.1749 -0.2038 0.1412 250 LYS A CA 1864 C C . LYS A 231 ? 1.7991 1.4857 1.3522 -0.1673 -0.2019 0.1469 250 LYS A C 1865 O O . LYS A 231 ? 1.7581 1.4353 1.3213 -0.1528 -0.1846 0.1364 250 LYS A O 1866 C CB . LYS A 231 ? 1.8248 1.4887 1.3580 -0.1711 -0.2034 0.1378 250 LYS A CB 1867 C CG . LYS A 231 ? 1.9354 1.5919 1.5174 -0.1741 -0.2172 0.1580 250 LYS A CG 1868 C CD . LYS A 231 ? 2.0052 1.6333 1.6065 -0.1725 -0.2223 0.1527 250 LYS A CD 1869 C CE . LYS A 231 ? 2.1283 1.7506 1.7920 -0.1767 -0.2392 0.1779 250 LYS A CE 1870 N NZ . LYS A 231 ? 2.2179 1.8049 1.9106 -0.1742 -0.2467 0.1690 250 LYS A NZ 1871 N N . VAL A 232 ? 1.8678 1.5683 1.4391 -0.1786 -0.2206 0.1675 251 VAL A N 1872 C CA . VAL A 232 ? 1.9049 1.6082 1.5202 -0.1761 -0.2268 0.1824 251 VAL A CA 1873 C C . VAL A 232 ? 2.0229 1.7298 1.6791 -0.1860 -0.2471 0.2118 251 VAL A C 1874 O O . VAL A 232 ? 2.0909 1.8150 1.7261 -0.2049 -0.2678 0.2276 251 VAL A O 1875 C CB . VAL A 232 ? 1.8830 1.5994 1.4828 -0.1836 -0.2370 0.1796 251 VAL A CB 1876 C CG1 . VAL A 232 ? 1.8977 1.6266 1.4399 -0.1976 -0.2464 0.1684 251 VAL A CG1 1877 C CG2 . VAL A 232 ? 1.9644 1.6887 1.6115 -0.1914 -0.2582 0.2055 251 VAL A CG2 1878 N N . GLY A 233 ? 2.0677 1.7602 1.7844 -0.1723 -0.2387 0.2200 252 GLY A N 1879 C CA . GLY A 233 ? 2.1980 1.8900 1.9737 -0.1786 -0.2568 0.2501 252 GLY A CA 1880 C C . GLY A 233 ? 2.2349 1.9188 1.9925 -0.1863 -0.2635 0.2493 252 GLY A C 1881 O O . GLY A 233 ? 2.1655 1.8317 1.8883 -0.1769 -0.2460 0.2201 252 GLY A O 1882 N N . PRO A 234 ? 2.3533 2.0541 2.1339 -0.2063 -0.2917 0.2853 253 PRO A N 1883 C CA . PRO A 234 ? 2.4066 2.1054 2.1798 -0.2160 -0.3005 0.2926 253 PRO A CA 1884 C C . PRO A 234 ? 2.3737 2.1042 2.0717 -0.2337 -0.3054 0.2944 253 PRO A C 1885 O O . PRO A 234 ? 3.0325 2.7832 2.7302 -0.2506 -0.3212 0.3217 253 PRO A O 1886 C CB . PRO A 234 ? 3.4938 3.2575 3.3620 -0.1443 -0.2192 0.2611 253 PRO A CB 1887 C CG . PRO A 234 ? 3.5001 3.2916 3.3754 -0.1319 -0.2087 0.2620 253 PRO A CG 1888 C CD . PRO A 234 ? 2.4903 2.2148 2.3134 -0.2226 -0.3199 0.3273 253 PRO A CD 1889 N N . LYS A 235 ? 2.2617 1.9983 1.9029 -0.2287 -0.2905 0.2668 254 LYS A N 1890 C CA . LYS A 235 ? 2.2530 2.0179 1.8266 -0.2406 -0.2895 0.2614 254 LYS A CA 1891 C C . LYS A 235 ? 2.1141 1.8673 1.6468 -0.2266 -0.2643 0.2231 254 LYS A C 1892 O O . LYS A 235 ? 2.0227 1.7557 1.5612 -0.2114 -0.2508 0.2005 254 LYS A O 1893 C CB . LYS A 235 ? 2.3182 2.1062 1.8680 -0.2536 -0.3052 0.2704 254 LYS A CB 1894 C CG . LYS A 235 ? 2.3760 2.1960 1.8534 -0.2668 -0.3050 0.2642 254 LYS A CG 1895 C CD . LYS A 235 ? 2.4538 2.2822 1.8995 -0.2759 -0.3194 0.2558 254 LYS A CD 1896 C CE . LYS A 235 ? 2.7780 2.6332 2.1450 -0.2852 -0.3144 0.2383 254 LYS A CE 1897 N NZ . LYS A 235 ? 2.8563 2.7104 2.1893 -0.2944 -0.3322 0.2216 254 LYS A NZ 1898 N N . VAL A 236 ? 2.1128 1.8842 1.6096 -0.2326 -0.2582 0.2214 255 VAL A N 1899 C CA . VAL A 236 ? 1.9998 1.7656 1.4662 -0.2219 -0.2374 0.1924 255 VAL A CA 1900 C C . VAL A 236 ? 2.0156 1.8085 1.4352 -0.2258 -0.2301 0.1807 255 VAL A C 1901 O O . VAL A 236 ? 2.1221 1.9470 1.5181 -0.2388 -0.2348 0.1975 255 VAL A O 1902 C CB . VAL A 236 ? 1.9884 1.7495 1.4637 -0.2228 -0.2345 0.1973 255 VAL A CB 1903 C CG1 . VAL A 236 ? 1.8785 1.6364 1.3303 -0.2135 -0.2167 0.1730 255 VAL A CG1 1904 C CG2 . VAL A 236 ? 2.0037 1.7303 1.5223 -0.2184 -0.2434 0.2003 255 VAL A CG2 1905 N N . LEU A 237 ? 1.9289 1.7095 1.3368 -0.2141 -0.2179 0.1520 256 LEU A N 1906 C CA . LEU A 237 ? 1.9520 1.7483 1.3231 -0.2135 -0.2090 0.1312 256 LEU A CA 1907 C C . LEU A 237 ? 1.8882 1.6894 1.2562 -0.2045 -0.1886 0.1191 256 LEU A C 1908 O O . LEU A 237 ? 1.7926 1.5755 1.1838 -0.1970 -0.1841 0.1180 256 LEU A O 1909 C CB . LEU A 237 ? 1.9183 1.6966 1.2941 -0.2077 -0.2136 0.1106 256 LEU A CB 1910 C CG . LEU A 237 ? 1.9831 1.7571 1.3725 -0.2173 -0.2369 0.1253 256 LEU A CG 1911 C CD1 . LEU A 237 ? 1.9312 1.6859 1.3428 -0.2104 -0.2410 0.1104 256 LEU A CD1 1912 C CD2 . LEU A 237 ? 2.1396 1.9388 1.4876 -0.2353 -0.2530 0.1332 256 LEU A CD2 1913 N N . GLY A 238 ? 1.9585 1.7863 1.2976 -0.2055 -0.1761 0.1111 257 GLY A N 1914 C CA . GLY A 238 ? 1.9205 1.7599 1.2667 -0.1967 -0.1553 0.1041 257 GLY A CA 1915 C C . GLY A 238 ? 1.9974 1.8703 1.3430 -0.2051 -0.1500 0.1326 257 GLY A C 1916 O O . GLY A 238 ? 2.1079 2.0034 1.4338 -0.2176 -0.1583 0.1524 257 GLY A O 1917 N N . PRO A 239 ? 1.9530 1.8329 1.3253 -0.2005 -0.1390 0.1403 258 PRO A N 1918 C CA . PRO A 239 ? 1.8393 1.6988 1.2380 -0.1893 -0.1329 0.1255 258 PRO A CA 1919 C C . PRO A 239 ? 1.8525 1.7156 1.2478 -0.1755 -0.1138 0.0952 258 PRO A C 1920 O O . PRO A 239 ? 1.9593 1.8478 1.3306 -0.1725 -0.0975 0.0840 258 PRO A O 1921 C CB . PRO A 239 ? 1.8331 1.7096 1.2615 -0.1942 -0.1317 0.1520 258 PRO A CB 1922 C CG . PRO A 239 ? 1.9704 1.8898 1.3877 -0.2014 -0.1224 0.1736 258 PRO A CG 1923 C CD . PRO A 239 ? 2.0291 1.9441 1.4135 -0.2096 -0.1355 0.1736 258 PRO A CD 1924 N N . PHE A 240 ? 1.7612 1.5988 1.1808 -0.1673 -0.1162 0.0818 259 PHE A N 1925 C CA . PHE A 240 ? 1.7794 1.6136 1.2136 -0.1541 -0.1026 0.0549 259 PHE A CA 1926 C C . PHE A 240 ? 1.7323 1.5721 1.2147 -0.1471 -0.0941 0.0638 259 PHE A C 1927 O O . PHE A 240 ? 1.6484 1.4774 1.1480 -0.1530 -0.1078 0.0833 259 PHE A O 1928 C CB . PHE A 240 ? 1.7382 1.5418 1.1727 -0.1522 -0.1165 0.0374 259 PHE A CB 1929 C CG . PHE A 240 ? 1.7911 1.5885 1.1882 -0.1608 -0.1301 0.0325 259 PHE A CG 1930 C CD1 . PHE A 240 ? 1.9179 1.7286 1.2774 -0.1624 -0.1251 0.0136 259 PHE A CD1 1931 C CD2 . PHE A 240 ? 1.7301 1.5101 1.1304 -0.1673 -0.1478 0.0472 259 PHE A CD2 1932 C CE1 . PHE A 240 ? 1.9847 1.7921 1.3104 -0.1743 -0.1436 0.0143 259 PHE A CE1 1933 C CE2 . PHE A 240 ? 1.7930 1.5697 1.1717 -0.1761 -0.1630 0.0485 259 PHE A CE2 1934 C CZ . PHE A 240 ? 1.9143 1.7049 1.2560 -0.1814 -0.1638 0.0344 259 PHE A CZ 1935 N N . CYS A 241 ? 1.8040 1.6609 1.3086 -0.1345 -0.0718 0.0490 260 CYS A N 1936 C CA . CYS A 241 ? 1.7822 1.6493 1.3472 -0.1265 -0.0623 0.0600 260 CYS A CA 1937 C C . CYS A 241 ? 1.8827 1.7540 1.4749 -0.1075 -0.0379 0.0279 260 CYS A C 1938 O O . CYS A 241 ? 1.9676 1.8307 1.5211 -0.1024 -0.0310 -0.0060 260 CYS A O 1939 C CB . CYS A 241 ? 1.7882 1.6863 1.3695 -0.1334 -0.0577 0.0939 260 CYS A CB 1940 S SG . CYS A 241 ? 1.9344 1.8768 1.4880 -0.1295 -0.0282 0.0929 260 CYS A SG 1941 N N . GLY A 242 ? 1.8904 1.7728 1.5517 -0.0975 -0.0269 0.0378 261 GLY A N 1942 C CA . GLY A 242 ? 2.0095 1.8943 1.7126 -0.0760 -0.0008 0.0063 261 GLY A CA 1943 C C . GLY A 242 ? 1.9958 1.8484 1.7529 -0.0694 -0.0144 -0.0069 261 GLY A C 1944 O O . GLY A 242 ? 1.8843 1.7223 1.6566 -0.0816 -0.0417 0.0189 261 GLY A O 1945 N N . GLU A 243 ? 2.1313 1.9740 1.9185 -0.0496 0.0057 -0.0474 262 GLU A N 1946 C CA . GLU A 243 ? 2.1614 1.9726 2.0160 -0.0409 -0.0059 -0.0630 262 GLU A CA 1947 C C . GLU A 243 ? 2.2022 1.9752 2.0121 -0.0431 -0.0220 -0.1036 262 GLU A C 1948 O O . GLU A 243 ? 2.2277 1.9714 2.0936 -0.0399 -0.0389 -0.1129 262 GLU A O 1949 C CB . GLU A 243 ? 2.3088 2.1286 2.2456 -0.0159 0.0246 -0.0826 262 GLU A CB 1950 C CG . GLU A 243 ? 2.2802 2.1371 2.2885 -0.0151 0.0336 -0.0335 262 GLU A CG 1951 C CD . GLU A 243 ? 2.4548 2.3336 2.5348 0.0119 0.0748 -0.0506 262 GLU A CD 1952 O OE1 . GLU A 243 ? 2.5772 2.4312 2.7233 0.0315 0.0836 -0.0847 262 GLU A OE1 1953 O OE2 . GLU A 243 ? 2.4835 2.4050 2.5632 0.0140 0.0984 -0.0277 262 GLU A OE2 1954 N N . LYS A 244 ? 2.2226 1.9978 1.9386 -0.0510 -0.0206 -0.1224 263 LYS A N 1955 C CA . LYS A 244 ? 2.2773 2.0199 1.9450 -0.0572 -0.0403 -0.1567 263 LYS A CA 1956 C C . LYS A 244 ? 2.1463 1.8896 1.7599 -0.0792 -0.0663 -0.1260 263 LYS A C 1957 O O . LYS A 244 ? 2.1199 1.8886 1.6783 -0.0877 -0.0595 -0.1090 263 LYS A O 1958 C CB . LYS A 244 ? 2.4727 2.2168 2.0782 -0.0472 -0.0174 -0.2104 263 LYS A CB 1959 C CG . LYS A 244 ? 2.5749 2.2812 2.1328 -0.0549 -0.0425 -0.2518 263 LYS A CG 1960 C CD . LYS A 244 ? 2.7307 2.3949 2.3489 -0.0393 -0.0460 -0.2996 263 LYS A CD 1961 C CE . LYS A 244 ? 2.8814 2.5075 2.4438 -0.0479 -0.0715 -0.3481 263 LYS A CE 1962 N NZ . LYS A 244 ? 2.7542 2.3628 2.3179 -0.0710 -0.1163 -0.3156 263 LYS A NZ 1963 N N . ALA A 245 ? 2.0793 1.7962 1.7182 -0.0875 -0.0953 -0.1163 264 ALA A N 1964 C CA . ALA A 245 ? 1.9710 1.6863 1.5746 -0.1046 -0.1177 -0.0887 264 ALA A CA 1965 C C . ALA A 245 ? 2.0513 1.7616 1.5809 -0.1138 -0.1262 -0.1110 264 ALA A C 1966 O O . ALA A 245 ? 2.1928 1.8865 1.7059 -0.1095 -0.1271 -0.1533 264 ALA A O 1967 C CB . ALA A 245 ? 1.9073 1.6017 1.5668 -0.1083 -0.1414 -0.0727 264 ALA A CB 1968 N N . PRO A 246 ? 1.9804 1.7036 1.4674 -0.1274 -0.1351 -0.0834 265 PRO A N 1969 C CA . PRO A 246 ? 2.0666 1.7886 1.4916 -0.1394 -0.1487 -0.0954 265 PRO A CA 1970 C C . PRO A 246 ? 2.1061 1.7968 1.5487 -0.1457 -0.1779 -0.1090 265 PRO A C 1971 O O . PRO A 246 ? 2.0273 1.7032 1.5311 -0.1428 -0.1879 -0.0950 265 PRO A O 1972 C CB . PRO A 246 ? 1.9707 1.7102 1.3756 -0.1507 -0.1537 -0.0552 265 PRO A CB 1973 C CG . PRO A 246 ? 1.8290 1.5672 1.2830 -0.1458 -0.1499 -0.0285 265 PRO A CG 1974 C CD . PRO A 246 ? 1.8406 1.5801 1.3337 -0.1324 -0.1332 -0.0421 265 PRO A CD 1975 N N . GLU A 247 ? 2.2404 1.9241 1.6306 -0.1562 -0.1939 -0.1325 266 GLU A N 1976 C CA . GLU A 247 ? 2.2985 1.9519 1.7031 -0.1662 -0.2284 -0.1448 266 GLU A CA 1977 C C . GLU A 247 ? 2.1666 1.8217 1.6076 -0.1763 -0.2482 -0.0984 266 GLU A C 1978 O O . GLU A 247 ? 2.0728 1.7508 1.5011 -0.1781 -0.2373 -0.0663 266 GLU A O 1979 C CB . GLU A 247 ? 2.4910 2.1407 1.8188 -0.1793 -0.2442 -0.1776 266 GLU A CB 1980 C CG . GLU A 247 ? 2.6652 2.3095 1.9549 -0.1667 -0.2224 -0.2334 266 GLU A CG 1981 C CD . GLU A 247 ? 2.7271 2.3341 2.0805 -0.1512 -0.2225 -0.2702 266 GLU A CD 1982 O OE1 . GLU A 247 ? 2.7658 2.3375 2.1542 -0.1600 -0.2583 -0.2792 266 GLU A OE1 1983 O OE2 . GLU A 247 ? 2.7511 2.3650 2.1281 -0.1308 -0.1883 -0.2872 266 GLU A OE2 1984 N N . PRO A 248 ? 2.1723 1.8040 1.6653 -0.1816 -0.2759 -0.0938 267 PRO A N 1985 C CA . PRO A 248 ? 2.0698 1.7084 1.6050 -0.1881 -0.2891 -0.0484 267 PRO A CA 1986 C C . PRO A 248 ? 2.0760 1.7329 1.5686 -0.2003 -0.2956 -0.0257 267 PRO A C 1987 O O . PRO A 248 ? 2.2010 1.8582 1.6382 -0.2130 -0.3109 -0.0427 267 PRO A O 1988 C CB . PRO A 248 ? 2.1445 1.7569 1.7310 -0.1963 -0.3234 -0.0533 267 PRO A CB 1989 C CG . PRO A 248 ? 2.2282 1.8172 1.8294 -0.1869 -0.3202 -0.0946 267 PRO A CG 1990 C CD . PRO A 248 ? 2.2901 1.8886 1.8189 -0.1793 -0.2934 -0.1286 267 PRO A CD 1991 N N . ILE A 249 ? 1.9595 1.6323 1.4775 -0.1963 -0.2835 0.0123 268 ILE A N 1992 C CA . ILE A 249 ? 1.9684 1.6569 1.4649 -0.2051 -0.2879 0.0378 268 ILE A CA 1993 C C . ILE A 249 ? 1.9580 1.6461 1.5097 -0.2106 -0.3068 0.0709 268 ILE A C 1994 O O . ILE A 249 ? 1.8660 1.5572 1.4687 -0.1994 -0.2928 0.0912 268 ILE A O 1995 C CB . ILE A 249 ? 1.8776 1.5821 1.3578 -0.1956 -0.2587 0.0501 268 ILE A CB 1996 C CG1 . ILE A 249 ? 1.9085 1.6206 1.3404 -0.1920 -0.2412 0.0243 268 ILE A CG1 1997 C CG2 . ILE A 249 ? 1.8919 1.6083 1.3689 -0.2035 -0.2655 0.0792 268 ILE A CG2 1998 C CD1 . ILE A 249 ? 1.8155 1.5385 1.2488 -0.1818 -0.2152 0.0348 268 ILE A CD1 1999 N N . SER A 250 ? 2.0664 1.7553 1.6081 -0.2284 -0.3375 0.0797 269 SER A N 2000 C CA . SER A 250 ? 2.0792 1.7720 1.6820 -0.2350 -0.3576 0.1167 269 SER A CA 2001 C C . SER A 250 ? 2.0792 1.7898 1.6817 -0.2364 -0.3512 0.1463 269 SER A C 2002 O O . SER A 250 ? 2.1837 1.9025 1.7458 -0.2528 -0.3705 0.1499 269 SER A O 2003 C CB . SER A 250 ? 2.2192 1.9001 1.8236 -0.2569 -0.4033 0.1123 269 SER A CB 2004 O OG . SER A 250 ? 2.2465 1.9045 1.8625 -0.2553 -0.4126 0.0829 269 SER A OG 2005 N N . THR A 251 ? 1.9829 1.6999 1.6286 -0.2191 -0.3234 0.1663 270 THR A N 2006 C CA . THR A 251 ? 1.9981 1.7256 1.6583 -0.2171 -0.3164 0.1914 270 THR A CA 2007 C C . THR A 251 ? 2.0657 1.8005 1.7979 -0.2234 -0.3375 0.2288 270 THR A C 2008 O O . THR A 251 ? 2.0794 1.8127 1.8540 -0.2263 -0.3517 0.2370 270 THR A O 2009 C CB . THR A 251 ? 1.8995 1.6255 1.5661 -0.1951 -0.2769 0.1880 270 THR A CB 2010 O OG1 . THR A 251 ? 1.8598 1.5888 1.5870 -0.1802 -0.2605 0.2036 270 THR A OG1 2011 C CG2 . THR A 251 ? 1.8158 1.5363 1.4280 -0.1888 -0.2579 0.1570 270 THR A CG2 2012 N N . GLN A 252 ? 2.1230 1.8666 1.8796 -0.2259 -0.3412 0.2550 271 GLN A N 2013 C CA . GLN A 252 ? 2.1912 1.9449 2.0309 -0.2295 -0.3579 0.2963 271 GLN A CA 2014 C C . GLN A 252 ? 2.1419 1.8961 2.0333 -0.2028 -0.3182 0.3055 271 GLN A C 2015 O O . GLN A 252 ? 2.2180 1.9797 2.1779 -0.2002 -0.3217 0.3374 271 GLN A O 2016 C CB . GLN A 252 ? 2.3357 2.1004 2.1686 -0.2556 -0.3979 0.3221 271 GLN A CB 2017 C CG . GLN A 252 ? 2.4216 2.1863 2.1766 -0.2826 -0.4340 0.3042 271 GLN A CG 2018 C CD . GLN A 252 ? 2.4489 2.2050 2.2225 -0.2928 -0.4610 0.3000 271 GLN A CD 2019 O OE1 . GLN A 252 ? 2.4042 2.1450 2.1361 -0.2891 -0.4549 0.2621 271 GLN A OE1 2020 N NE2 . GLN A 252 ? 2.5210 2.2863 2.3674 -0.3063 -0.4938 0.3412 271 GLN A NE2 2021 N N . SER A 253 ? 2.0349 1.7803 1.8936 -0.1831 -0.2809 0.2762 272 SER A N 2022 C CA . SER A 253 ? 2.0098 1.7505 1.8908 -0.1581 -0.2415 0.2716 272 SER A CA 2023 C C . SER A 253 ? 1.9413 1.6877 1.8388 -0.1374 -0.2074 0.2649 272 SER A C 2024 O O . SER A 253 ? 1.8747 1.6231 1.7425 -0.1412 -0.2089 0.2528 272 SER A O 2025 C CB . SER A 253 ? 1.9791 1.7053 1.7942 -0.1573 -0.2317 0.2446 272 SER A CB 2026 O OG . SER A 253 ? 1.9994 1.7139 1.8318 -0.1366 -0.2015 0.2361 272 SER A OG 2027 N N . HIS A 254 ? 1.9739 1.7241 1.9189 -0.1148 -0.1747 0.2724 273 HIS A N 2028 C CA . HIS A 254 ? 1.9448 1.7076 1.9010 -0.0930 -0.1351 0.2689 273 HIS A CA 2029 C C . HIS A 254 ? 1.8965 1.6441 1.7772 -0.0823 -0.1084 0.2318 273 HIS A C 2030 O O . HIS A 254 ? 1.8813 1.6408 1.7479 -0.0684 -0.0781 0.2259 273 HIS A O 2031 C CB . HIS A 254 ? 2.0346 1.8128 2.0772 -0.0718 -0.1082 0.2933 273 HIS A CB 2032 C CG . HIS A 254 ? 2.1175 1.8761 2.1745 -0.0591 -0.0954 0.2817 273 HIS A CG 2033 N ND1 . HIS A 254 ? 2.1320 1.8737 2.1457 -0.0386 -0.0586 0.2461 273 HIS A ND1 2034 C CD2 . HIS A 254 ? 2.2080 1.9602 2.3211 -0.0662 -0.1187 0.3024 273 HIS A CD2 2035 C CE1 . HIS A 254 ? 2.2270 1.9484 2.2767 -0.0322 -0.0601 0.2429 273 HIS A CE1 2036 N NE2 . HIS A 254 ? 2.2765 2.0057 2.3909 -0.0481 -0.0951 0.2794 273 HIS A NE2 2037 N N . SER A 255 ? 1.8905 1.6149 1.7258 -0.0904 -0.1213 0.2114 274 SER A N 2038 C CA . SER A 255 ? 1.8606 1.5676 1.6286 -0.0844 -0.1044 0.1785 274 SER A CA 2039 C C . SER A 255 ? 1.8020 1.4996 1.5132 -0.1044 -0.1306 0.1661 274 SER A C 2040 O O . SER A 255 ? 1.8336 1.5287 1.5520 -0.1193 -0.1573 0.1763 274 SER A O 2041 C CB . SER A 255 ? 1.9516 1.6376 1.7339 -0.0684 -0.0858 0.1642 274 SER A CB 2042 O OG . SER A 255 ? 2.0142 1.6882 1.8275 -0.0796 -0.1127 0.1761 274 SER A OG 2043 N N . VAL A 256 ? 1.7325 1.4296 1.3901 -0.1051 -0.1223 0.1480 275 VAL A N 2044 C CA . VAL A 256 ? 1.6814 1.3742 1.2907 -0.1205 -0.1404 0.1365 275 VAL A CA 2045 C C . VAL A 256 ? 1.6590 1.3401 1.2203 -0.1166 -0.1274 0.1156 275 VAL A C 2046 O O . VAL A 256 ? 1.6566 1.3416 1.2063 -0.1058 -0.1066 0.1099 275 VAL A O 2047 C CB . VAL A 256 ? 1.6284 1.3359 1.2365 -0.1294 -0.1522 0.1412 275 VAL A CB 2048 C CG1 . VAL A 256 ? 1.5871 1.2923 1.1499 -0.1404 -0.1626 0.1262 275 VAL A CG1 2049 C CG2 . VAL A 256 ? 1.6661 1.3809 1.3153 -0.1379 -0.1734 0.1595 275 VAL A CG2 2050 N N . LEU A 257 ? 1.6550 1.3258 1.1885 -0.1274 -0.1415 0.1077 276 LEU A N 2051 C CA . LEU A 257 ? 1.6365 1.2966 1.1283 -0.1288 -0.1378 0.0917 276 LEU A CA 2052 C C . LEU A 257 ? 1.5765 1.2496 1.0468 -0.1411 -0.1493 0.0934 276 LEU A C 2053 O O . LEU A 257 ? 1.5872 1.2674 1.0612 -0.1507 -0.1628 0.1001 276 LEU A O 2054 C CB . LEU A 257 ? 1.7075 1.3423 1.1970 -0.1299 -0.1444 0.0826 276 LEU A CB 2055 C CG . LEU A 257 ? 1.7028 1.3248 1.1515 -0.1371 -0.1506 0.0689 276 LEU A CG 2056 C CD1 . LEU A 257 ? 1.7146 1.3286 1.1295 -0.1277 -0.1337 0.0509 276 LEU A CD1 2057 C CD2 . LEU A 257 ? 1.7728 1.3722 1.2329 -0.1443 -0.1676 0.0673 276 LEU A CD2 2058 N N . ILE A 258 ? 1.5337 1.2128 0.9831 -0.1404 -0.1426 0.0891 277 ILE A N 2059 C CA . ILE A 258 ? 1.4893 1.1806 0.9290 -0.1490 -0.1500 0.0908 277 ILE A CA 2060 C C . ILE A 258 ? 1.4991 1.1813 0.9121 -0.1550 -0.1548 0.0863 277 ILE A C 2061 O O . ILE A 258 ? 1.5150 1.1905 0.9075 -0.1522 -0.1492 0.0813 277 ILE A O 2062 C CB . ILE A 258 ? 1.4507 1.1580 0.9055 -0.1460 -0.1447 0.0965 277 ILE A CB 2063 C CG1 . ILE A 258 ? 1.4616 1.1740 0.9481 -0.1426 -0.1463 0.1012 277 ILE A CG1 2064 C CG2 . ILE A 258 ? 1.4266 1.1444 0.8824 -0.1522 -0.1503 0.0966 277 ILE A CG2 2065 C CD1 . ILE A 258 ? 1.4469 1.1709 0.9599 -0.1368 -0.1389 0.1128 277 ILE A CD1 2066 N N . LEU A 259 ? 1.5036 1.1880 0.9161 -0.1645 -0.1660 0.0899 278 LEU A N 2067 C CA . LEU A 259 ? 1.5154 1.1930 0.9133 -0.1736 -0.1765 0.0910 278 LEU A CA 2068 C C . LEU A 259 ? 1.4754 1.1762 0.8835 -0.1785 -0.1773 0.1013 278 LEU A C 2069 O O . LEU A 259 ? 1.4703 1.1886 0.8944 -0.1782 -0.1733 0.1053 278 LEU A O 2070 C CB . LEU A 259 ? 1.5710 1.2371 0.9762 -0.1814 -0.1898 0.0950 278 LEU A CB 2071 C CG . LEU A 259 ? 1.6132 1.2688 1.0125 -0.1938 -0.2073 0.0990 278 LEU A CG 2072 C CD1 . LEU A 259 ? 1.6959 1.3234 1.1044 -0.1979 -0.2216 0.0954 278 LEU A CD1 2073 C CD2 . LEU A 259 ? 1.5976 1.2830 1.0159 -0.2028 -0.2111 0.1194 278 LEU A CD2 2074 N N . PHE A 260 ? 1.4633 1.1654 0.8627 -0.1831 -0.1822 0.1056 279 PHE A N 2075 C CA . PHE A 260 ? 1.4432 1.1675 0.8658 -0.1876 -0.1844 0.1198 279 PHE A CA 2076 C C . PHE A 260 ? 1.4724 1.1935 0.8912 -0.2018 -0.2031 0.1311 279 PHE A C 2077 O O . PHE A 260 ? 1.5028 1.2083 0.8928 -0.2090 -0.2156 0.1286 279 PHE A O 2078 C CB . PHE A 260 ? 1.4186 1.1549 0.8532 -0.1831 -0.1785 0.1258 279 PHE A CB 2079 C CG . PHE A 260 ? 1.4126 1.1708 0.8863 -0.1864 -0.1814 0.1426 279 PHE A CG 2080 C CD1 . PHE A 260 ? 1.4148 1.1870 0.9204 -0.1817 -0.1728 0.1415 279 PHE A CD1 2081 C CD2 . PHE A 260 ? 1.4245 1.1924 0.9053 -0.1939 -0.1916 0.1611 279 PHE A CD2 2082 C CE1 . PHE A 260 ? 1.4252 1.2180 0.9777 -0.1813 -0.1713 0.1560 279 PHE A CE1 2083 C CE2 . PHE A 260 ? 1.4296 1.2188 0.9615 -0.1965 -0.1955 0.1812 279 PHE A CE2 2084 C CZ . PHE A 260 ? 1.4306 1.2309 1.0024 -0.1886 -0.1837 0.1771 279 PHE A CZ 2085 N N . HIS A 261 ? 1.4822 1.2195 0.9288 -0.2065 -0.2055 0.1440 280 HIS A N 2086 C CA . HIS A 261 ? 1.5198 1.2584 0.9780 -0.2218 -0.2261 0.1617 280 HIS A CA 2087 C C . HIS A 261 ? 1.5076 1.2766 1.0085 -0.2239 -0.2246 0.1839 280 HIS A C 2088 O O . HIS A 261 ? 1.4965 1.2892 1.0275 -0.2123 -0.2034 0.1848 280 HIS A O 2089 C CB . HIS A 261 ? 1.5630 1.3033 1.0340 -0.2268 -0.2304 0.1692 280 HIS A CB 2090 C CG . HIS A 261 ? 1.6117 1.3541 1.1058 -0.2442 -0.2549 0.1921 280 HIS A CG 2091 N ND1 . HIS A 261 ? 1.6210 1.4007 1.1624 -0.2475 -0.2506 0.2201 280 HIS A ND1 2092 C CD2 . HIS A 261 ? 1.6680 1.3788 1.1487 -0.2588 -0.2842 0.1903 280 HIS A CD2 2093 C CE1 . HIS A 261 ? 1.6732 1.4459 1.2329 -0.2658 -0.2798 0.2401 280 HIS A CE1 2094 N NE2 . HIS A 261 ? 1.7056 1.4340 1.2276 -0.2741 -0.3031 0.2210 280 HIS A NE2 2095 N N . SER A 262 ? 1.5289 1.2965 1.0341 -0.2388 -0.2482 0.2009 281 SER A N 2096 C CA . SER A 262 ? 1.5354 1.3333 1.0950 -0.2432 -0.2517 0.2296 281 SER A CA 2097 C C . SER A 262 ? 1.5871 1.3870 1.1667 -0.2638 -0.2812 0.2553 281 SER A C 2098 O O . SER A 262 ? 1.6266 1.3967 1.1642 -0.2792 -0.3092 0.2486 281 SER A O 2099 C CB . SER A 262 ? 1.5245 1.3269 1.0846 -0.2439 -0.2560 0.2362 281 SER A CB 2100 O OG . SER A 262 ? 1.5657 1.3490 1.0779 -0.2616 -0.2843 0.2384 281 SER A OG 2101 N N . ASP A 263 ? 1.6023 1.4366 1.2477 -0.2635 -0.2746 0.2831 282 ASP A N 2102 C CA . ASP A 263 ? 1.6601 1.5029 1.3417 -0.2840 -0.3037 0.3158 282 ASP A CA 2103 C C . ASP A 263 ? 1.6891 1.5400 1.3977 -0.3011 -0.3335 0.3445 282 ASP A C 2104 O O . ASP A 263 ? 1.6691 1.5166 1.3586 -0.2980 -0.3323 0.3377 282 ASP A O 2105 C CB . ASP A 263 ? 1.6880 1.5710 1.4312 -0.2760 -0.2806 0.3382 282 ASP A CB 2106 C CG . ASP A 263 ? 1.6907 1.6171 1.5020 -0.2600 -0.2509 0.3548 282 ASP A CG 2107 O OD1 . ASP A 263 ? 1.6634 1.5893 1.4895 -0.2584 -0.2551 0.3571 282 ASP A OD1 2108 O OD2 . ASP A 263 ? 1.7353 1.6989 1.5922 -0.2506 -0.2253 0.3703 282 ASP A OD2 2109 N N . ASN A 264 ? 1.7487 1.6147 1.5084 -0.3205 -0.3616 0.3821 283 ASN A N 2110 C CA . ASN A 264 ? 1.7983 1.6737 1.5886 -0.3424 -0.3985 0.4167 283 ASN A CA 2111 C C . ASN A 264 ? 1.7969 1.7192 1.6783 -0.3316 -0.3796 0.4506 283 ASN A C 2112 O O . ASN A 264 ? 1.8506 1.7894 1.7801 -0.3516 -0.4125 0.4914 283 ASN A O 2113 C CB . ASN A 264 ? 1.8761 1.7446 1.6892 -0.3710 -0.4438 0.4450 283 ASN A CB 2114 C CG . ASN A 264 ? 1.9042 1.8151 1.8120 -0.3672 -0.4295 0.4831 283 ASN A CG 2115 O OD1 . ASN A 264 ? 1.8718 1.8200 1.8251 -0.3411 -0.3811 0.4855 283 ASN A OD1 2116 N ND2 . ASN A 264 ? 1.9792 1.8864 1.9192 -0.3938 -0.4722 0.5141 283 ASN A ND2 2117 N N . SER A 265 ? 1.7503 1.6928 1.6601 -0.3012 -0.3297 0.4344 284 SER A N 2118 C CA . SER A 265 ? 1.7765 1.7597 1.7828 -0.2867 -0.3075 0.4605 284 SER A CA 2119 C C . SER A 265 ? 1.7395 1.7220 1.7443 -0.2574 -0.2663 0.4271 284 SER A C 2120 O O . SER A 265 ? 1.6952 1.6579 1.6379 -0.2431 -0.2424 0.3855 284 SER A O 2121 C CB . SER A 265 ? 1.8216 1.8452 1.9090 -0.2798 -0.2877 0.4884 284 SER A CB 2122 O OG . SER A 265 ? 1.8690 1.9326 2.0592 -0.2622 -0.2615 0.5115 284 SER A OG 2123 N N . GLY A 266 ? 1.7738 1.7781 1.8575 -0.2496 -0.2608 0.4483 285 GLY A N 2124 C CA . GLY A 266 ? 1.7657 1.7685 1.8710 -0.2226 -0.2262 0.4204 285 GLY A CA 2125 C C . GLY A 266 ? 1.7562 1.7440 1.8491 -0.2300 -0.2471 0.4245 285 GLY A C 2126 O O . GLY A 266 ? 1.7460 1.7193 1.7780 -0.2545 -0.2832 0.4364 285 GLY A O 2127 N N . GLU A 267 ? 1.7780 1.7699 1.9288 -0.2083 -0.2233 0.4136 286 GLU A N 2128 C CA . GLU A 267 ? 1.7845 1.7690 1.9448 -0.2130 -0.2397 0.4238 286 GLU A CA 2129 C C . GLU A 267 ? 1.7582 1.7198 1.8991 -0.1898 -0.2114 0.3778 286 GLU A C 2130 O O . GLU A 267 ? 1.7922 1.7533 1.9810 -0.1862 -0.2165 0.3876 286 GLU A O 2131 C CB . GLU A 267 ? 1.8744 1.8893 2.1594 -0.2166 -0.2540 0.4749 286 GLU A CB 2132 C CG . GLU A 267 ? 1.9244 1.9638 2.2370 -0.2447 -0.2913 0.5290 286 GLU A CG 2133 C CD . GLU A 267 ? 1.9175 1.9453 2.1305 -0.2795 -0.3366 0.5452 286 GLU A CD 2134 O OE1 . GLU A 267 ? 1.8987 1.9116 2.0478 -0.2849 -0.3446 0.5345 286 GLU A OE1 2135 O OE2 . GLU A 267 ? 1.9423 1.9771 2.1446 -0.3018 -0.3648 0.5697 286 GLU A OE2 2136 N N . ASN A 268 ? 1.7100 1.6536 1.7836 -0.1769 -0.1864 0.3320 287 ASN A N 2137 C CA . ASN A 268 ? 1.6973 1.6176 1.7445 -0.1576 -0.1633 0.2862 287 ASN A CA 2138 C C . ASN A 268 ? 1.6608 1.5635 1.6676 -0.1671 -0.1822 0.2880 287 ASN A C 2139 O O . ASN A 268 ? 1.6266 1.5282 1.5749 -0.1873 -0.2054 0.3067 287 ASN A O 2140 C CB . ASN A 268 ? 1.6713 1.5822 1.6506 -0.1482 -0.1398 0.2472 287 ASN A CB 2141 C CG . ASN A 268 ? 1.7312 1.6687 1.7526 -0.1383 -0.1167 0.2509 287 ASN A CG 2142 O OD1 . ASN A 268 ? 1.8092 1.7537 1.8712 -0.1153 -0.0846 0.2257 287 ASN A OD1 2143 N ND2 . ASN A 268 ? 1.7044 1.6590 1.7220 -0.1553 -0.1327 0.2835 287 ASN A ND2 2144 N N . ARG A 269 ? 1.6872 1.5779 1.7320 -0.1526 -0.1725 0.2701 288 ARG A N 2145 C CA . ARG A 269 ? 1.6767 1.5584 1.7103 -0.1594 -0.1878 0.2795 288 ARG A CA 2146 C C . ARG A 269 ? 1.6090 1.4708 1.5450 -0.1623 -0.1857 0.2542 288 ARG A C 2147 O O . ARG A 269 ? 1.6024 1.4663 1.5169 -0.1721 -0.1987 0.2726 288 ARG A O 2148 C CB . ARG A 269 ? 1.7541 1.6301 1.8839 -0.1448 -0.1837 0.2761 288 ARG A CB 2149 C CG . ARG A 269 ? 1.8422 1.7402 2.0854 -0.1429 -0.1893 0.3107 288 ARG A CG 2150 C CD . ARG A 269 ? 1.9434 1.8312 2.2936 -0.1283 -0.1883 0.3076 288 ARG A CD 2151 N NE . ARG A 269 ? 1.9716 1.8682 2.3474 -0.1446 -0.2163 0.3504 288 ARG A NE 2152 C CZ . ARG A 269 ? 2.0729 1.9663 2.5565 -0.1391 -0.2266 0.3668 288 ARG A CZ 2153 N NH1 . ARG A 269 ? 2.1605 2.0357 2.7368 -0.1158 -0.2107 0.3367 288 ARG A NH1 2154 N NH2 . ARG A 269 ? 2.0998 2.0095 2.6026 -0.1566 -0.2520 0.4138 288 ARG A NH2 2155 N N . GLY A 270 ? 1.5750 1.4221 1.4571 -0.1538 -0.1685 0.2166 289 GLY A N 2156 C CA . GLY A 270 ? 1.5197 1.3494 1.3207 -0.1565 -0.1675 0.1964 289 GLY A CA 2157 C C . GLY A 270 ? 1.5313 1.3416 1.3320 -0.1440 -0.1577 0.1646 289 GLY A C 2158 O O . GLY A 270 ? 1.5861 1.3898 1.4214 -0.1308 -0.1454 0.1393 289 GLY A O 2159 N N . TRP A 271 ? 1.4974 1.2987 1.2573 -0.1485 -0.1632 0.1649 290 TRP A N 2160 C CA . TRP A 271 ? 1.5034 1.2865 1.2573 -0.1410 -0.1598 0.1396 290 TRP A CA 2161 C C . TRP A 271 ? 1.4856 1.2703 1.2370 -0.1459 -0.1679 0.1590 290 TRP A C 2162 O O . TRP A 271 ? 1.4661 1.2654 1.1931 -0.1545 -0.1712 0.1853 290 TRP A O 2163 C CB . TRP A 271 ? 1.4796 1.2521 1.1682 -0.1398 -0.1512 0.1123 290 TRP A CB 2164 C CG . TRP A 271 ? 1.4320 1.2076 1.0639 -0.1490 -0.1535 0.1246 290 TRP A CG 2165 C CD1 . TRP A 271 ? 1.4214 1.2050 1.0345 -0.1556 -0.1547 0.1336 290 TRP A CD1 2166 C CD2 . TRP A 271 ? 1.4061 1.1748 1.0006 -0.1522 -0.1558 0.1285 290 TRP A CD2 2167 N NE1 . TRP A 271 ? 1.4013 1.1778 0.9636 -0.1632 -0.1601 0.1379 290 TRP A NE1 2168 C CE2 . TRP A 271 ? 1.3908 1.1587 0.9404 -0.1595 -0.1578 0.1334 290 TRP A CE2 2169 C CE3 . TRP A 271 ? 1.4101 1.1734 1.0109 -0.1489 -0.1560 0.1287 290 TRP A CE3 2170 C CZ2 . TRP A 271 ? 1.3815 1.1403 0.8898 -0.1608 -0.1566 0.1323 290 TRP A CZ2 2171 C CZ3 . TRP A 271 ? 1.3960 1.1570 0.9601 -0.1499 -0.1524 0.1336 290 TRP A CZ3 2172 C CH2 . TRP A 271 ? 1.3880 1.1453 0.9049 -0.1545 -0.1510 0.1324 290 TRP A CH2 2173 N N . ARG A 272 ? 1.5085 1.2791 1.2806 -0.1408 -0.1707 0.1448 291 ARG A N 2174 C CA . ARG A 272 ? 1.5066 1.2816 1.2883 -0.1438 -0.1763 0.1645 291 ARG A CA 2175 C C . ARG A 272 ? 1.5151 1.2697 1.2840 -0.1404 -0.1788 0.1384 291 ARG A C 2176 O O . ARG A 272 ? 1.5596 1.2953 1.3425 -0.1363 -0.1831 0.1083 291 ARG A O 2177 C CB . ARG A 272 ? 1.5646 1.3509 1.4296 -0.1456 -0.1881 0.1942 291 ARG A CB 2178 C CG . ARG A 272 ? 1.5857 1.3791 1.4803 -0.1480 -0.1947 0.2170 291 ARG A CG 2179 C CD . ARG A 272 ? 1.6601 1.4636 1.6508 -0.1510 -0.2104 0.2486 291 ARG A CD 2180 N NE . ARG A 272 ? 1.7008 1.5074 1.7332 -0.1532 -0.2197 0.2672 291 ARG A NE 2181 C CZ . ARG A 272 ? 1.7489 1.5898 1.8230 -0.1599 -0.2226 0.3194 291 ARG A CZ 2182 N NH1 . ARG A 272 ? 1.7666 1.6411 1.8379 -0.1665 -0.2187 0.3569 291 ARG A NH1 2183 N NH2 . ARG A 272 ? 1.7802 1.6257 1.9006 -0.1617 -0.2308 0.3384 291 ARG A NH2 2184 N N . LEU A 273 ? 1.4916 1.2511 1.2354 -0.1423 -0.1762 0.1502 292 LEU A N 2185 C CA . LEU A 273 ? 1.5113 1.2559 1.2542 -0.1420 -0.1834 0.1360 292 LEU A CA 2186 C C . LEU A 273 ? 1.5221 1.2817 1.2974 -0.1430 -0.1844 0.1679 292 LEU A C 2187 O O . LEU A 273 ? 1.5105 1.2940 1.2800 -0.1425 -0.1720 0.1958 292 LEU A O 2188 C CB . LEU A 273 ? 1.4892 1.2241 1.1675 -0.1423 -0.1776 0.1137 292 LEU A CB 2189 C CG . LEU A 273 ? 1.4516 1.1956 1.0870 -0.1416 -0.1643 0.1258 292 LEU A CG 2190 C CD1 . LEU A 273 ? 1.4618 1.2099 1.1141 -0.1397 -0.1634 0.1412 292 LEU A CD1 2191 C CD2 . LEU A 273 ? 1.4376 1.1720 1.0225 -0.1435 -0.1618 0.1058 292 LEU A CD2 2192 N N . SER A 274 ? 1.5570 1.3051 1.3641 -0.1451 -0.1992 0.1645 293 SER A N 2193 C CA . SER A 274 ? 1.5733 1.3383 1.4199 -0.1457 -0.1999 0.1974 293 SER A CA 2194 C C . SER A 274 ? 1.5734 1.3272 1.3956 -0.1466 -0.2036 0.1853 293 SER A C 2195 O O . SER A 274 ? 1.5941 1.3242 1.3918 -0.1512 -0.2183 0.1543 293 SER A O 2196 C CB . SER A 274 ? 1.6361 1.3999 1.5683 -0.1507 -0.2222 0.2157 293 SER A CB 2197 O OG . SER A 274 ? 1.6926 1.4224 1.6382 -0.1557 -0.2481 0.1830 293 SER A OG 2198 N N . TYR A 275 ? 1.5700 1.3437 1.3976 -0.1420 -0.1885 0.2106 294 TYR A N 2199 C CA . TYR A 275 ? 1.5852 1.3521 1.4068 -0.1426 -0.1927 0.2076 294 TYR A CA 2200 C C . TYR A 275 ? 1.6322 1.4168 1.5276 -0.1433 -0.1992 0.2439 294 TYR A C 2201 O O . TYR A 275 ? 1.6453 1.4566 1.5829 -0.1394 -0.1875 0.2759 294 TYR A O 2202 C CB . TYR A 275 ? 1.5546 1.3247 1.3214 -0.1340 -0.1676 0.2001 294 TYR A CB 2203 C CG . TYR A 275 ? 1.5641 1.3614 1.3413 -0.1220 -0.1376 0.2257 294 TYR A CG 2204 C CD1 . TYR A 275 ? 1.6146 1.4275 1.4383 -0.1155 -0.1288 0.2500 294 TYR A CD1 2205 C CD2 . TYR A 275 ? 1.5488 1.3586 1.2881 -0.1172 -0.1171 0.2260 294 TYR A CD2 2206 C CE1 . TYR A 275 ? 1.6459 1.4883 1.4774 -0.1014 -0.0945 0.2712 294 TYR A CE1 2207 C CE2 . TYR A 275 ? 1.5934 1.4301 1.3282 -0.1061 -0.0870 0.2450 294 TYR A CE2 2208 C CZ . TYR A 275 ? 1.6451 1.4989 1.4253 -0.0966 -0.0726 0.2661 294 TYR A CZ 2209 O OH . TYR A 275 ? 1.7109 1.5954 1.4849 -0.0827 -0.0363 0.2826 294 TYR A OH 2210 N N . ARG A 276 ? 1.6746 1.4490 1.5882 -0.1496 -0.2185 0.2443 295 ARG A N 2211 C CA . ARG A 276 ? 1.7345 1.5258 1.7269 -0.1523 -0.2292 0.2821 295 ARG A CA 2212 C C . ARG A 276 ? 1.7633 1.5537 1.7539 -0.1519 -0.2302 0.2864 295 ARG A C 2213 O O . ARG A 276 ? 1.7746 1.5414 1.7222 -0.1617 -0.2506 0.2604 295 ARG A O 2214 C CB . ARG A 276 ? 1.7919 1.5649 1.8359 -0.1686 -0.2725 0.2822 295 ARG A CB 2215 C CG . ARG A 276 ? 1.8009 1.5813 1.8878 -0.1685 -0.2741 0.2951 295 ARG A CG 2216 C CD . ARG A 276 ? 1.8656 1.6094 1.9746 -0.1826 -0.3162 0.2688 295 ARG A CD 2217 N NE . ARG A 276 ? 1.8706 1.6174 2.0217 -0.1809 -0.3165 0.2773 295 ARG A NE 2218 C CZ . ARG A 276 ? 1.8307 1.5694 1.9394 -0.1746 -0.3020 0.2514 295 ARG A CZ 2219 N NH1 . ARG A 276 ? 1.7603 1.4879 1.7809 -0.1692 -0.2850 0.2148 295 ARG A NH1 2220 N NH2 . ARG A 276 ? 1.8623 1.6067 2.0259 -0.1745 -0.3061 0.2674 295 ARG A NH2 2221 N N . ALA A 277 ? 1.7966 1.6163 1.8376 -0.1401 -0.2066 0.3218 296 ALA A N 2222 C CA . ALA A 277 ? 1.8483 1.6708 1.9108 -0.1373 -0.2056 0.3335 296 ALA A CA 2223 C C . ALA A 277 ? 1.9251 1.7520 2.0697 -0.1527 -0.2440 0.3657 296 ALA A C 2224 O O . ALA A 277 ? 1.9625 1.8172 2.1864 -0.1496 -0.2394 0.4054 296 ALA A O 2225 C CB . ALA A 277 ? 1.8623 1.7136 1.9425 -0.1135 -0.1563 0.3515 296 ALA A CB 2226 N N . ALA A 278 ? 1.9742 1.7764 2.0996 -0.1714 -0.2841 0.3515 297 ALA A N 2227 C CA . ALA A 278 ? 2.0715 1.8721 2.2626 -0.1919 -0.3312 0.3782 297 ALA A CA 2228 C C . ALA A 278 ? 2.1314 1.9481 2.3722 -0.1903 -0.3314 0.4106 297 ALA A C 2229 O O . ALA A 278 ? 2.1108 1.9404 2.3468 -0.1694 -0.2899 0.4128 297 ALA A O 2230 C CB . ALA A 278 ? 2.1247 1.8892 2.2549 -0.2161 -0.3784 0.3407 297 ALA A CB 2231 N N . GLY A 279 ? 2.4965 2.3092 2.7854 -0.2141 -0.3825 0.4339 298 GLY A N 2232 C CA . GLY A 279 ? 2.5180 2.3460 2.8677 -0.2187 -0.3955 0.4717 298 GLY A CA 2233 C C . GLY A 279 ? 2.9940 2.8192 3.3034 -0.2131 -0.3945 0.4247 298 GLY A C 2234 O O . GLY A 279 ? 3.0487 2.8624 3.3035 -0.2172 -0.4030 0.3779 298 GLY A O 2235 N N . ASN A 280 ? 2.2409 2.4093 2.1472 -0.1838 -0.1888 0.0449 299 ASN A N 2236 C CA . ASN A 280 ? 2.2506 2.4441 2.1260 -0.1794 -0.1605 0.0365 299 ASN A CA 2237 C C . ASN A 280 ? 2.1569 2.3324 1.9905 -0.1712 -0.1563 0.0109 299 ASN A C 2238 O O . ASN A 280 ? 2.0875 2.2271 1.8980 -0.1716 -0.1769 0.0025 299 ASN A O 2239 C CB . ASN A 280 ? 2.2959 2.4879 2.1473 -0.1859 -0.1642 0.0473 299 ASN A CB 2240 C CG . ASN A 280 ? 2.4464 2.6680 2.3361 -0.1947 -0.1604 0.0748 299 ASN A CG 2241 O OD1 . ASN A 280 ? 2.5041 2.7547 2.4384 -0.1956 -0.1489 0.0862 299 ASN A OD1 2242 N ND2 . ASN A 280 ? 2.5346 2.7513 2.4112 -0.2018 -0.1699 0.0870 299 ASN A ND2 2243 N N . GLU A 281 ? 2.1666 2.3678 1.9913 -0.1641 -0.1298 -0.0015 300 GLU A N 2244 C CA . GLU A 281 ? 2.0962 2.2837 1.8866 -0.1562 -0.1252 -0.0247 300 GLU A CA 2245 C C . GLU A 281 ? 2.0610 2.2389 1.7988 -0.1568 -0.1223 -0.0307 300 GLU A C 2246 O O . GLU A 281 ? 2.1610 2.3615 1.8888 -0.1596 -0.1082 -0.0234 300 GLU A O 2247 C CB . GLU A 281 ? 2.1487 2.3661 1.9581 -0.1476 -0.1004 -0.0380 300 GLU A CB 2248 C CG . GLU A 281 ? 2.0999 2.3020 1.8841 -0.1393 -0.0994 -0.0613 300 GLU A CG 2249 C CD . GLU A 281 ? 2.1768 2.4078 1.9628 -0.1303 -0.0725 -0.0790 300 GLU A CD 2250 O OE1 . GLU A 281 ? 2.2659 2.5254 2.0957 -0.1272 -0.0574 -0.0793 300 GLU A OE1 2251 O OE2 . GLU A 281 ? 2.1865 2.4109 1.9317 -0.1262 -0.0669 -0.0940 300 GLU A OE2 2252 N N . CYS A 282 ? 1.9666 2.1120 1.6727 -0.1551 -0.1361 -0.0427 301 CYS A N 2253 C CA . CYS A 282 ? 1.9399 2.0738 1.6017 -0.1547 -0.1344 -0.0502 301 CYS A CA 2254 C C . CYS A 282 ? 1.9538 2.0993 1.5953 -0.1468 -0.1164 -0.0673 301 CYS A C 2255 O O . CYS A 282 ? 1.9212 2.0688 1.5778 -0.1411 -0.1133 -0.0777 301 CYS A O 2256 C CB . CYS A 282 ? 1.8592 1.9556 1.4988 -0.1568 -0.1550 -0.0555 301 CYS A CB 2257 S SG . CYS A 282 ? 1.8822 1.9623 1.5311 -0.1657 -0.1754 -0.0403 301 CYS A SG 2258 N N . PRO A 283 ? 2.0116 2.1637 1.6224 -0.1469 -0.1070 -0.0699 302 PRO A N 2259 C CA . PRO A 283 ? 2.0436 2.2054 1.6339 -0.1400 -0.0921 -0.0865 302 PRO A CA 2260 C C . PRO A 283 ? 1.9437 2.0812 1.5205 -0.1340 -0.0999 -0.1027 302 PRO A C 2261 O O . PRO A 283 ? 1.8582 1.9695 1.4282 -0.1366 -0.1157 -0.1011 302 PRO A O 2262 C CB . PRO A 283 ? 2.1416 2.3092 1.7025 -0.1444 -0.0877 -0.0811 302 PRO A CB 2263 C CG . PRO A 283 ? 2.1101 2.2580 1.6720 -0.1511 -0.1050 -0.0680 302 PRO A CG 2264 C CD . PRO A 283 ? 2.0744 2.2238 1.6713 -0.1540 -0.1124 -0.0571 302 PRO A CD 2265 N N . GLU A 284 ? 1.9752 2.1223 1.5479 -0.1266 -0.0887 -0.1186 303 GLU A N 2266 C CA . GLU A 284 ? 1.9015 2.0297 1.4653 -0.1211 -0.0952 -0.1329 303 GLU A CA 2267 C C . GLU A 284 ? 1.8518 1.9583 1.3823 -0.1239 -0.1035 -0.1322 303 GLU A C 2268 O O . GLU A 284 ? 1.9089 2.0213 1.4198 -0.1262 -0.0983 -0.1291 303 GLU A O 2269 C CB . GLU A 284 ? 2.0027 2.1475 1.5673 -0.1128 -0.0812 -0.1505 303 GLU A CB 2270 C CG . GLU A 284 ? 1.9829 2.1103 1.5475 -0.1070 -0.0896 -0.1643 303 GLU A CG 2271 C CD . GLU A 284 ? 2.1468 2.2874 1.7108 -0.0984 -0.0783 -0.1839 303 GLU A CD 2272 N N . LEU A 285 ? 1.7594 1.8419 1.2857 -0.1249 -0.1165 -0.1338 304 LEU A N 2273 C CA . LEU A 285 ? 1.7329 1.7962 1.2321 -0.1270 -0.1219 -0.1349 304 LEU A CA 2274 C C . LEU A 285 ? 1.7501 1.8080 1.2396 -0.1219 -0.1207 -0.1467 304 LEU A C 2275 O O . LEU A 285 ? 1.7600 1.8160 1.2642 -0.1190 -0.1245 -0.1519 304 LEU A O 2276 C CB . LEU A 285 ? 1.6572 1.6985 1.1525 -0.1329 -0.1354 -0.1294 304 LEU A CB 2277 C CG . LEU A 285 ? 1.6538 1.6927 1.1560 -0.1388 -0.1416 -0.1185 304 LEU A CG 2278 C CD1 . LEU A 285 ? 1.5991 1.6130 1.0898 -0.1440 -0.1552 -0.1185 304 LEU A CD1 2279 C CD2 . LEU A 285 ? 1.7011 1.7462 1.1954 -0.1401 -0.1367 -0.1144 304 LEU A CD2 2280 N N . GLN A 286 ? 1.7831 1.8378 1.2525 -0.1212 -0.1175 -0.1496 305 GLN A N 2281 C CA . GLN A 286 ? 1.8302 1.8784 1.2920 -0.1169 -0.1181 -0.1590 305 GLN A CA 2282 C C . GLN A 286 ? 1.7365 1.7650 1.1859 -0.1205 -0.1243 -0.1566 305 GLN A C 2283 O O . GLN A 286 ? 1.7228 1.7460 1.1625 -0.1239 -0.1238 -0.1521 305 GLN A O 2284 C CB . GLN A 286 ? 1.9873 2.0461 1.4375 -0.1139 -0.1111 -0.1644 305 GLN A CB 2285 C CG . GLN A 286 ? 2.1276 2.2044 1.5868 -0.1083 -0.1036 -0.1745 305 GLN A CG 2286 C CD . GLN A 286 ? 2.2896 2.3657 1.7386 -0.1033 -0.1034 -0.1870 305 GLN A CD 2287 O OE1 . GLN A 286 ? 2.2910 2.3530 1.7435 -0.1009 -0.1112 -0.1915 305 GLN A OE1 2288 N NE2 . GLN A 286 ? 2.4652 2.5570 1.9013 -0.1023 -0.0951 -0.1925 305 GLN A NE2 2289 N N . PRO A 287 ? 1.6915 1.7100 1.1435 -0.1204 -0.1302 -0.1591 306 PRO A N 2290 C CA . PRO A 287 ? 1.6470 1.6502 1.0852 -0.1249 -0.1332 -0.1566 306 PRO A CA 2291 C C . PRO A 287 ? 1.6675 1.6695 1.0970 -0.1229 -0.1277 -0.1593 306 PRO A C 2292 O O . PRO A 287 ? 1.7533 1.7628 1.1866 -0.1181 -0.1258 -0.1637 306 PRO A O 2293 C CB . PRO A 287 ? 1.6622 1.6600 1.1084 -0.1258 -0.1409 -0.1563 306 PRO A CB 2294 C CG . PRO A 287 ? 1.7252 1.7345 1.1913 -0.1188 -0.1410 -0.1630 306 PRO A CG 2295 C CD . PRO A 287 ? 1.7297 1.7518 1.2004 -0.1169 -0.1346 -0.1637 306 PRO A CD 2296 N N . PRO A 288 ? 1.6298 1.6222 1.0490 -0.1266 -0.1255 -0.1578 307 PRO A N 2297 C CA . PRO A 288 ? 1.6894 1.6805 1.1082 -0.1248 -0.1210 -0.1597 307 PRO A CA 2298 C C . PRO A 288 ? 1.7359 1.7255 1.1589 -0.1228 -0.1219 -0.1612 307 PRO A C 2299 O O . PRO A 288 ? 1.7031 1.6896 1.1262 -0.1250 -0.1255 -0.1595 307 PRO A O 2300 C CB . PRO A 288 ? 1.6469 1.6285 1.0587 -0.1288 -0.1174 -0.1603 307 PRO A CB 2301 C CG . PRO A 288 ? 1.6117 1.5868 1.0126 -0.1337 -0.1207 -0.1592 307 PRO A CG 2302 C CD . PRO A 288 ? 1.5958 1.5777 1.0045 -0.1326 -0.1273 -0.1558 307 PRO A CD 2303 N N . VAL A 289 ? 1.8232 1.8144 1.2520 -0.1198 -0.1211 -0.1626 308 VAL A N 2304 C CA . VAL A 289 ? 1.8730 1.8620 1.3104 -0.1180 -0.1237 -0.1630 308 VAL A CA 2305 C C . VAL A 289 ? 1.8357 1.8188 1.2712 -0.1227 -0.1186 -0.1594 308 VAL A C 2306 O O . VAL A 289 ? 1.7861 1.7665 1.2173 -0.1249 -0.1113 -0.1602 308 VAL A O 2307 C CB . VAL A 289 ? 1.9734 1.9631 1.4181 -0.1152 -0.1259 -0.1639 308 VAL A CB 2308 C CG1 . VAL A 289 ? 2.0322 2.0181 1.4902 -0.1139 -0.1302 -0.1629 308 VAL A CG1 2309 C CG2 . VAL A 289 ? 2.0448 2.0417 1.4833 -0.1124 -0.1300 -0.1675 308 VAL A CG2 2310 N N . HIS A 290 ? 1.8654 1.8472 1.3044 -0.1250 -0.1226 -0.1557 309 HIS A N 2311 C CA . HIS A 290 ? 1.8601 1.8390 1.2931 -0.1318 -0.1176 -0.1500 309 HIS A CA 2312 C C . HIS A 290 ? 1.7603 1.7354 1.1721 -0.1380 -0.1155 -0.1495 309 HIS A C 2313 O O . HIS A 290 ? 1.7593 1.7320 1.1571 -0.1442 -0.1074 -0.1483 309 HIS A O 2314 C CB . HIS A 290 ? 1.9178 1.8976 1.3577 -0.1318 -0.1067 -0.1503 309 HIS A CB 2315 C CG . HIS A 290 ? 2.0172 1.9987 1.4798 -0.1277 -0.1114 -0.1481 309 HIS A CG 2316 N ND1 . HIS A 290 ? 2.0949 2.0774 1.5695 -0.1299 -0.1176 -0.1407 309 HIS A ND1 2317 C CD2 . HIS A 290 ? 2.0775 2.0589 1.5539 -0.1228 -0.1127 -0.1510 309 HIS A CD2 2318 C CE1 . HIS A 290 ? 2.1864 2.1686 1.6817 -0.1254 -0.1226 -0.1407 309 HIS A CE1 2319 N NE2 . HIS A 290 ? 2.1804 2.1616 1.6761 -0.1214 -0.1201 -0.1467 309 HIS A NE2 2320 N N . GLY A 291 ? 1.7014 1.6761 1.1109 -0.1368 -0.1226 -0.1509 310 GLY A N 2321 C CA . GLY A 291 ? 1.6647 1.6339 1.0569 -0.1430 -0.1243 -0.1497 310 GLY A CA 2322 C C . GLY A 291 ? 1.6468 1.6161 1.0457 -0.1437 -0.1364 -0.1463 310 GLY A C 2323 O O . GLY A 291 ? 1.6722 1.6462 1.0898 -0.1397 -0.1430 -0.1456 310 GLY A O 2324 N N . LYS A 292 ? 1.6202 1.5838 1.0070 -0.1486 -0.1400 -0.1451 311 LYS A N 2325 C CA . LYS A 292 ? 1.6272 1.5902 1.0244 -0.1505 -0.1522 -0.1405 311 LYS A CA 2326 C C . LYS A 292 ? 1.5964 1.5550 0.9867 -0.1527 -0.1544 -0.1412 311 LYS A C 2327 O O . LYS A 292 ? 1.5930 1.5457 0.9659 -0.1546 -0.1486 -0.1455 311 LYS A O 2328 C CB . LYS A 292 ? 1.6757 1.6318 1.0696 -0.1598 -0.1644 -0.1306 311 LYS A CB 2329 C CG . LYS A 292 ? 1.7041 1.6492 1.0640 -0.1714 -0.1643 -0.1269 311 LYS A CG 2330 C CD . LYS A 292 ? 1.7666 1.7042 1.1214 -0.1835 -0.1809 -0.1136 311 LYS A CD 2331 C CE . LYS A 292 ? 1.8345 1.7618 1.1475 -0.1964 -0.1798 -0.1109 311 LYS A CE 2332 N NZ . LYS A 292 ? 1.8934 1.8113 1.1975 -0.2107 -0.2004 -0.0958 311 LYS A NZ 2333 N N . ILE A 293 ? 1.5730 1.5346 0.9819 -0.1523 -0.1637 -0.1373 312 ILE A N 2334 C CA . ILE A 293 ? 1.5500 1.5081 0.9607 -0.1551 -0.1695 -0.1348 312 ILE A CA 2335 C C . ILE A 293 ? 1.5602 1.5110 0.9795 -0.1624 -0.1864 -0.1258 312 ILE A C 2336 O O . ILE A 293 ? 1.5754 1.5328 1.0199 -0.1599 -0.1916 -0.1231 312 ILE A O 2337 C CB . ILE A 293 ? 1.5385 1.5118 0.9715 -0.1472 -0.1629 -0.1368 312 ILE A CB 2338 C CG1 . ILE A 293 ? 1.5537 1.5327 0.9784 -0.1421 -0.1501 -0.1427 312 ILE A CG1 2339 C CG2 . ILE A 293 ? 1.5222 1.4931 0.9647 -0.1510 -0.1711 -0.1309 312 ILE A CG2 2340 C CD1 . ILE A 293 ? 1.5813 1.5773 1.0227 -0.1366 -0.1435 -0.1422 312 ILE A CD1 2341 N N . GLU A 294 ? 1.5816 1.5177 0.9821 -0.1717 -0.1968 -0.1219 313 GLU A N 2342 C CA . GLU A 294 ? 1.6293 1.5554 1.0366 -0.1811 -0.2169 -0.1111 313 GLU A CA 2343 C C . GLU A 294 ? 1.6438 1.5625 1.0546 -0.1842 -0.2263 -0.1088 313 GLU A C 2344 O O . GLU A 294 ? 1.6564 1.5690 1.0457 -0.1844 -0.2206 -0.1157 313 GLU A O 2345 C CB . GLU A 294 ? 1.6755 1.5869 1.0486 -0.1936 -0.2255 -0.1057 313 GLU A CB 2346 C CG . GLU A 294 ? 1.7075 1.6256 1.0855 -0.1930 -0.2220 -0.1027 313 GLU A CG 2347 C CD . GLU A 294 ? 1.7990 1.7057 1.1509 -0.2082 -0.2345 -0.0911 313 GLU A CD 2348 O OE1 . GLU A 294 ? 1.8435 1.7356 1.1624 -0.2201 -0.2436 -0.0878 313 GLU A OE1 2349 O OE2 . GLU A 294 ? 1.8540 1.7660 1.2176 -0.2091 -0.2362 -0.0847 313 GLU A OE2 2350 N N . PRO A 295 ? 1.6632 1.5820 1.1057 -0.1868 -0.2417 -0.0991 314 PRO A N 2351 C CA . PRO A 295 ? 1.6783 1.6040 1.1563 -0.1861 -0.2505 -0.0920 314 PRO A CA 2352 C C . PRO A 295 ? 1.6532 1.6027 1.1687 -0.1721 -0.2343 -0.0990 314 PRO A C 2353 O O . PRO A 295 ? 1.6325 1.5936 1.1567 -0.1659 -0.2228 -0.1027 314 PRO A O 2354 C CB . PRO A 295 ? 1.7189 1.6329 1.2153 -0.1954 -0.2741 -0.0797 314 PRO A CB 2355 C CG . PRO A 295 ? 1.7091 1.6214 1.2004 -0.1942 -0.2712 -0.0822 314 PRO A CG 2356 C CD . PRO A 295 ? 1.6853 1.5951 1.1340 -0.1916 -0.2545 -0.0943 314 PRO A CD 2357 N N . SER A 296 ? 1.6755 1.6324 1.2124 -0.1679 -0.2341 -0.1007 315 SER A N 2358 C CA . SER A 296 ? 1.6852 1.6639 1.2548 -0.1548 -0.2191 -0.1106 315 SER A CA 2359 C C . SER A 296 ? 1.7241 1.7133 1.3428 -0.1524 -0.2246 -0.1071 315 SER A C 2360 O O . SER A 296 ? 1.7708 1.7539 1.4200 -0.1567 -0.2422 -0.1000 315 SER A O 2361 C CB . SER A 296 ? 1.7300 1.7107 1.3079 -0.1509 -0.2192 -0.1159 315 SER A CB 2362 O OG . SER A 296 ? 1.7430 1.7163 1.2810 -0.1531 -0.2129 -0.1180 315 SER A OG 2363 N N . GLN A 297 ? 1.7259 1.7314 1.3548 -0.1466 -0.2103 -0.1101 316 GLN A N 2364 C CA . GLN A 297 ? 1.7700 1.7905 1.4484 -0.1437 -0.2106 -0.1067 316 GLN A CA 2365 C C . GLN A 297 ? 1.8012 1.8501 1.4986 -0.1313 -0.1863 -0.1201 316 GLN A C 2366 O O . GLN A 297 ? 1.7857 1.8406 1.4511 -0.1270 -0.1710 -0.1286 316 GLN A O 2367 C CB . GLN A 297 ? 1.7686 1.7849 1.4444 -0.1504 -0.2163 -0.0951 316 GLN A CB 2368 C CG . GLN A 297 ? 1.7701 1.7573 1.4256 -0.1636 -0.2420 -0.0834 316 GLN A CG 2369 C CD . GLN A 297 ? 1.7812 1.7613 1.4303 -0.1696 -0.2489 -0.0748 316 GLN A CD 2370 O OE1 . GLN A 297 ? 1.8036 1.7591 1.4238 -0.1799 -0.2670 -0.0694 316 GLN A OE1 2371 N NE2 . GLN A 297 ? 1.7910 1.7924 1.4665 -0.1641 -0.2356 -0.0732 316 GLN A NE2 2372 N N . ALA A 298 ? 1.8529 1.9198 1.6029 -0.1261 -0.1827 -0.1224 317 ALA A N 2373 C CA . ALA A 298 ? 1.9036 2.0005 1.6718 -0.1149 -0.1575 -0.1366 317 ALA A CA 2374 C C . ALA A 298 ? 1.9054 2.0166 1.6542 -0.1171 -0.1428 -0.1297 317 ALA A C 2375 O O . ALA A 298 ? 1.9171 2.0404 1.6362 -0.1133 -0.1252 -0.1377 317 ALA A O 2376 C CB . ALA A 298 ? 1.9669 2.0798 1.8011 -0.1095 -0.1570 -0.1408 317 ALA A CB 2377 N N . LYS A 299 ? 1.9010 2.0088 1.6678 -0.1245 -0.1532 -0.1130 318 LYS A N 2378 C CA A LYS A 299 ? 1.8982 2.0173 1.6551 -0.1285 -0.1448 -0.1020 318 LYS A CA 2379 C CA B LYS A 299 ? 1.9013 2.0206 1.6589 -0.1285 -0.1448 -0.1019 318 LYS A CA 2380 C C . LYS A 299 ? 1.8599 1.9510 1.5970 -0.1391 -0.1675 -0.0876 318 LYS A C 2381 O O . LYS A 299 ? 1.8397 1.9081 1.5829 -0.1443 -0.1892 -0.0832 318 LYS A O 2382 C CB A LYS A 299 ? 1.9702 2.1194 1.7795 -0.1262 -0.1324 -0.0967 318 LYS A CB 2383 C CB B LYS A 299 ? 1.9767 2.1255 1.7879 -0.1265 -0.1333 -0.0960 318 LYS A CB 2384 C CG A LYS A 299 ? 2.0474 2.2299 1.8662 -0.1163 -0.1034 -0.1129 318 LYS A CG 2385 C CG B LYS A 299 ? 2.0484 2.2216 1.8997 -0.1160 -0.1165 -0.1122 318 LYS A CG 2386 C CD A LYS A 299 ? 2.0969 2.2873 1.9652 -0.1080 -0.1019 -0.1267 318 LYS A CD 2387 C CD B LYS A 299 ? 2.1007 2.2971 1.9246 -0.1083 -0.0891 -0.1294 318 LYS A CD 2388 C CE A LYS A 299 ? 2.1943 2.4173 2.0696 -0.0975 -0.0721 -0.1473 318 LYS A CE 2389 C CE B LYS A 299 ? 2.1683 2.3849 2.0314 -0.0971 -0.0745 -0.1501 318 LYS A CE 2390 N NZ A LYS A 299 ? 2.2625 2.4936 2.1948 -0.0883 -0.0709 -0.1632 318 LYS A NZ 2391 N NZ B LYS A 299 ? 2.3063 2.5426 2.1366 -0.0902 -0.0499 -0.1693 318 LYS A NZ 2392 N N . TYR A 300 ? 1.8534 1.9454 1.5665 -0.1430 -0.1638 -0.0805 319 TYR A N 2393 C CA . TYR A 300 ? 1.8199 1.8858 1.5137 -0.1520 -0.1839 -0.0706 319 TYR A CA 2394 C C . TYR A 300 ? 1.8613 1.9384 1.5835 -0.1567 -0.1864 -0.0546 319 TYR A C 2395 O O . TYR A 300 ? 1.9064 2.0111 1.6392 -0.1543 -0.1680 -0.0509 319 TYR A O 2396 C CB . TYR A 300 ? 1.7807 1.8324 1.4236 -0.1523 -0.1810 -0.0780 319 TYR A CB 2397 C CG . TYR A 300 ? 1.7412 1.7793 1.3566 -0.1495 -0.1813 -0.0908 319 TYR A CG 2398 C CD1 . TYR A 300 ? 1.7178 1.7279 1.3121 -0.1559 -0.1993 -0.0909 319 TYR A CD1 2399 C CD2 . TYR A 300 ? 1.7385 1.7917 1.3472 -0.1416 -0.1642 -0.1022 319 TYR A CD2 2400 C CE1 . TYR A 300 ? 1.6895 1.6896 1.2609 -0.1548 -0.1994 -0.0995 319 TYR A CE1 2401 C CE2 . TYR A 300 ? 1.7079 1.7488 1.2962 -0.1395 -0.1661 -0.1119 319 TYR A CE2 2402 C CZ . TYR A 300 ? 1.6839 1.6992 1.2550 -0.1464 -0.1833 -0.1093 319 TYR A CZ 2403 O OH . TYR A 300 ? 1.6694 1.6749 1.2224 -0.1458 -0.1850 -0.1158 319 TYR A OH 2404 N N . PHE A 301 ? 1.8601 1.9157 1.5934 -0.1645 -0.2105 -0.0441 320 PHE A N 2405 C CA . PHE A 301 ? 1.9130 1.9757 1.6791 -0.1699 -0.2181 -0.0270 320 PHE A CA 2406 C C . PHE A 301 ? 1.9128 1.9467 1.6543 -0.1775 -0.2391 -0.0229 320 PHE A C 2407 O O . PHE A 301 ? 1.8896 1.8971 1.5885 -0.1789 -0.2478 -0.0344 320 PHE A O 2408 C CB . PHE A 301 ? 1.9451 2.0140 1.7668 -0.1718 -0.2284 -0.0165 320 PHE A CB 2409 C CG . PHE A 301 ? 1.9644 2.0651 1.8206 -0.1632 -0.2058 -0.0225 320 PHE A CG 2410 C CD1 . PHE A 301 ? 2.0209 2.1597 1.9024 -0.1595 -0.1806 -0.0180 320 PHE A CD1 2411 C CD2 . PHE A 301 ? 1.9441 2.0376 1.8081 -0.1593 -0.2096 -0.0331 320 PHE A CD2 2412 C CE1 . PHE A 301 ? 2.0607 2.2298 1.9723 -0.1510 -0.1574 -0.0276 320 PHE A CE1 2413 C CE2 . PHE A 301 ? 1.9781 2.1002 1.8783 -0.1502 -0.1891 -0.0423 320 PHE A CE2 2414 C CZ . PHE A 301 ? 2.0371 2.1969 1.9597 -0.1455 -0.1620 -0.0413 320 PHE A CZ 2415 N N . PHE A 302 ? 1.9568 1.9968 1.7267 -0.1824 -0.2467 -0.0072 321 PHE A N 2416 C CA . PHE A 302 ? 1.9775 1.9914 1.7334 -0.1891 -0.2680 -0.0040 321 PHE A CA 2417 C C . PHE A 302 ? 1.9548 1.9292 1.6785 -0.1937 -0.2917 -0.0144 321 PHE A C 2418 O O . PHE A 302 ? 1.9534 1.9185 1.6917 -0.1971 -0.3056 -0.0108 321 PHE A O 2419 C CB . PHE A 302 ? 2.0438 2.0686 1.8495 -0.1949 -0.2789 0.0178 321 PHE A CB 2420 C CG . PHE A 302 ? 2.0861 2.0831 1.8861 -0.2015 -0.3044 0.0209 321 PHE A CG 2421 C CD1 . PHE A 302 ? 2.0913 2.0758 1.8552 -0.2003 -0.3028 0.0095 321 PHE A CD1 2422 C CD2 . PHE A 302 ? 2.1352 2.1182 1.9706 -0.2088 -0.3313 0.0345 321 PHE A CD2 2423 C CE1 . PHE A 302 ? 2.1538 2.1122 1.9170 -0.2053 -0.3265 0.0091 321 PHE A CE1 2424 C CE2 . PHE A 302 ? 2.1988 2.1539 2.0293 -0.2145 -0.3567 0.0346 321 PHE A CE2 2425 C CZ . PHE A 302 ? 2.2091 2.1527 2.0044 -0.2123 -0.3534 0.0210 321 PHE A CZ 2426 N N . LYS A 303 ? 1.9522 1.9052 1.6322 -0.1943 -0.2952 -0.0276 322 LYS A N 2427 C CA A LYS A 303 ? 1.9331 1.8499 1.5702 -0.1991 -0.3129 -0.0412 322 LYS A CA 2428 C CA B LYS A 303 ? 1.9327 1.8497 1.5696 -0.1990 -0.3127 -0.0413 322 LYS A CA 2429 C C . LYS A 303 ? 1.9016 1.8130 1.5025 -0.1973 -0.3044 -0.0533 322 LYS A C 2430 O O . LYS A 303 ? 1.9242 1.8085 1.4860 -0.2029 -0.3173 -0.0632 322 LYS A O 2431 C CB A LYS A 303 ? 1.9915 1.8840 1.6437 -0.2085 -0.3448 -0.0327 322 LYS A CB 2432 C CB B LYS A 303 ? 1.9921 1.8843 1.6432 -0.2085 -0.3446 -0.0331 322 LYS A CB 2433 C CG A LYS A 303 ? 2.0619 1.9241 1.6867 -0.2130 -0.3627 -0.0436 322 LYS A CG 2434 C CG B LYS A 303 ? 2.0576 1.9381 1.7211 -0.2115 -0.3598 -0.0303 322 LYS A CG 2435 C CD A LYS A 303 ? 2.1265 1.9527 1.7235 -0.2230 -0.3917 -0.0487 322 LYS A CD 2436 C CD B LYS A 303 ? 2.1313 1.9738 1.7788 -0.2210 -0.3929 -0.0343 322 LYS A CD 2437 C CE A LYS A 303 ? 2.1832 2.0054 1.8208 -0.2306 -0.4158 -0.0291 322 LYS A CE 2438 C CE B LYS A 303 ? 2.1401 1.9787 1.8184 -0.2280 -0.4130 -0.0180 322 LYS A CE 2439 N NZ A LYS A 303 ? 2.1832 2.0203 1.8811 -0.2301 -0.4222 -0.0110 322 LYS A NZ 2440 N NZ B LYS A 303 ? 2.1584 1.9627 1.7921 -0.2369 -0.4350 -0.0273 322 LYS A NZ 2441 N N . ASP A 304 ? 1.8359 1.7731 1.4485 -0.1902 -0.2831 -0.0530 323 ASP A N 2442 C CA . ASP A 304 ? 1.7825 1.7150 1.3663 -0.1886 -0.2766 -0.0631 323 ASP A CA 2443 C C . ASP A 304 ? 1.7629 1.6843 1.2988 -0.1868 -0.2670 -0.0786 323 ASP A C 2444 O O . ASP A 304 ? 1.7434 1.6752 1.2795 -0.1819 -0.2542 -0.0818 323 ASP A O 2445 C CB . ASP A 304 ? 1.7451 1.7067 1.3550 -0.1804 -0.2568 -0.0622 323 ASP A CB 2446 C CG . ASP A 304 ? 1.7521 1.7204 1.4053 -0.1819 -0.2665 -0.0524 323 ASP A CG 2447 O OD1 . ASP A 304 ? 1.7774 1.7247 1.4366 -0.1909 -0.2915 -0.0444 323 ASP A OD1 2448 O OD2 . ASP A 304 ? 1.7400 1.7336 1.4217 -0.1743 -0.2498 -0.0537 323 ASP A OD2 2449 N N . GLN A 305 ? 1.7680 1.6684 1.2652 -0.1920 -0.2743 -0.0868 324 GLN A N 2450 C CA . GLN A 305 ? 1.7676 1.6578 1.2210 -0.1909 -0.2641 -0.1022 324 GLN A CA 2451 C C . GLN A 305 ? 1.7081 1.6074 1.1463 -0.1874 -0.2495 -0.1067 324 GLN A C 2452 O O . GLN A 305 ? 1.6916 1.5902 1.1355 -0.1911 -0.2572 -0.1000 324 GLN A O 2453 C CB . GLN A 305 ? 1.8419 1.7020 1.2568 -0.2008 -0.2815 -0.1096 324 GLN A CB 2454 C CG . GLN A 305 ? 1.9168 1.7613 1.3453 -0.2061 -0.3031 -0.1057 324 GLN A CG 2455 C CD . GLN A 305 ? 1.9460 1.7951 1.3903 -0.2001 -0.2970 -0.1108 324 GLN A CD 2456 O OE1 . GLN A 305 ? 1.9647 1.8108 1.3869 -0.1960 -0.2844 -0.1260 324 GLN A OE1 2457 N NE2 . GLN A 305 ? 1.9680 1.8244 1.4551 -0.2003 -0.3072 -0.0970 324 GLN A NE2 2458 N N . VAL A 306 ? 1.6845 1.5915 1.1079 -0.1808 -0.2306 -0.1170 325 VAL A N 2459 C CA . VAL A 306 ? 1.6491 1.5638 1.0590 -0.1773 -0.2171 -0.1215 325 VAL A CA 2460 C C . VAL A 306 ? 1.6579 1.5639 1.0333 -0.1771 -0.2063 -0.1348 325 VAL A C 2461 O O . VAL A 306 ? 1.6729 1.5769 1.0482 -0.1741 -0.2016 -0.1419 325 VAL A O 2462 C CB . VAL A 306 ? 1.5983 1.5380 1.0371 -0.1679 -0.2030 -0.1188 325 VAL A CB 2463 C CG1 . VAL A 306 ? 1.6043 1.5561 1.0817 -0.1672 -0.2096 -0.1083 325 VAL A CG1 2464 C CG2 . VAL A 306 ? 1.5775 1.5284 1.0186 -0.1612 -0.1886 -0.1237 325 VAL A CG2 2465 N N . LEU A 307 ? 1.6630 1.5648 1.0136 -0.1806 -0.2028 -0.1373 326 LEU A N 2466 C CA . LEU A 307 ? 1.6756 1.5729 0.9971 -0.1805 -0.1894 -0.1493 326 LEU A CA 2467 C C . LEU A 307 ? 1.6395 1.5530 0.9722 -0.1729 -0.1740 -0.1496 326 LEU A C 2468 O O . LEU A 307 ? 1.6055 1.5260 0.9481 -0.1730 -0.1767 -0.1418 326 LEU A O 2469 C CB . LEU A 307 ? 1.7327 1.6149 1.0144 -0.1921 -0.1954 -0.1507 326 LEU A CB 2470 C CG . LEU A 307 ? 1.8117 1.6732 1.0677 -0.2012 -0.2097 -0.1555 326 LEU A CG 2471 C CD1 . LEU A 307 ? 1.8824 1.7321 1.0954 -0.2148 -0.2159 -0.1534 326 LEU A CD1 2472 C CD2 . LEU A 307 ? 1.8515 1.7072 1.1000 -0.1964 -0.2002 -0.1735 326 LEU A CD2 2473 N N . VAL A 308 ? 1.6691 1.5873 1.0037 -0.1665 -0.1601 -0.1588 327 VAL A N 2474 C CA . VAL A 308 ? 1.6735 1.6045 1.0181 -0.1598 -0.1471 -0.1597 327 VAL A CA 2475 C C . VAL A 308 ? 1.7233 1.6498 1.0438 -0.1636 -0.1376 -0.1656 327 VAL A C 2476 O O . VAL A 308 ? 1.7859 1.7037 1.0889 -0.1661 -0.1322 -0.1760 327 VAL A O 2477 C CB . VAL A 308 ? 1.6742 1.6139 1.0399 -0.1520 -0.1402 -0.1628 327 VAL A CB 2478 C CG1 . VAL A 308 ? 1.6758 1.6252 1.0487 -0.1464 -0.1291 -0.1643 327 VAL A CG1 2479 C CG2 . VAL A 308 ? 1.6548 1.6038 1.0429 -0.1498 -0.1472 -0.1541 327 VAL A CG2 2480 N N . SER A 309 ? 1.7232 1.6562 1.0449 -0.1643 -0.1356 -0.1592 328 SER A N 2481 C CA . SER A 309 ? 1.7780 1.7107 1.0810 -0.1691 -0.1261 -0.1604 328 SER A CA 2482 C C . SER A 309 ? 1.7719 1.7163 1.0953 -0.1625 -0.1178 -0.1583 328 SER A C 2483 O O . SER A 309 ? 1.7234 1.6747 1.0701 -0.1559 -0.1225 -0.1550 328 SER A O 2484 C CB . SER A 309 ? 1.8241 1.7507 1.1066 -0.1808 -0.1373 -0.1500 328 SER A CB 2485 O OG . SER A 309 ? 1.8896 1.8028 1.1437 -0.1893 -0.1439 -0.1536 328 SER A OG 2486 N N . CYS A 310 ? 1.8252 1.7722 1.1398 -0.1649 -0.1053 -0.1605 329 CYS A N 2487 C CA . CYS A 310 ? 1.8379 1.7945 1.1733 -0.1599 -0.0986 -0.1574 329 CYS A CA 2488 C C . CYS A 310 ? 1.8903 1.8499 1.2181 -0.1682 -0.0999 -0.1462 329 CYS A C 2489 O O . CYS A 310 ? 1.9438 1.8988 1.2436 -0.1791 -0.1008 -0.1425 329 CYS A O 2490 C CB . CYS A 310 ? 1.8584 1.8179 1.2031 -0.1547 -0.0830 -0.1679 329 CYS A CB 2491 S SG . CYS A 310 ? 1.8115 1.7687 1.1745 -0.1459 -0.0855 -0.1765 329 CYS A SG 2492 N N . ASP A 311 ? 1.8994 1.8663 1.2516 -0.1642 -0.1012 -0.1400 330 ASP A N 2493 C CA . ASP A 311 ? 1.9857 1.9568 1.3397 -0.1719 -0.1039 -0.1268 330 ASP A CA 2494 C C . ASP A 311 ? 2.0602 2.0364 1.3968 -0.1789 -0.0856 -0.1271 330 ASP A C 2495 O O . ASP A 311 ? 2.0467 2.0234 1.3796 -0.1745 -0.0705 -0.1404 330 ASP A O 2496 C CB . ASP A 311 ? 2.0429 2.0194 1.4315 -0.1643 -0.1097 -0.1229 330 ASP A CB 2497 C CG . ASP A 311 ? 2.0125 1.9866 1.4191 -0.1577 -0.1261 -0.1240 330 ASP A CG 2498 O OD1 . ASP A 311 ? 1.9840 1.9536 1.3821 -0.1613 -0.1359 -0.1220 330 ASP A OD1 2499 O OD2 . ASP A 311 ? 2.0592 2.0362 1.4892 -0.1492 -0.1293 -0.1274 330 ASP A OD2 2500 N N . THR A 312 ? 2.1549 2.1359 1.4833 -0.1903 -0.0868 -0.1124 331 THR A N 2501 C CA . THR A 312 ? 2.2729 2.2628 1.5839 -0.1984 -0.0666 -0.1113 331 THR A CA 2502 C C . THR A 312 ? 2.3075 2.3069 1.6525 -0.1887 -0.0522 -0.1163 331 THR A C 2503 O O . THR A 312 ? 2.3056 2.3073 1.6841 -0.1832 -0.0625 -0.1085 331 THR A O 2504 C CB . THR A 312 ? 2.4008 2.3955 1.6956 -0.2150 -0.0729 -0.0902 331 THR A CB 2505 O OG1 . THR A 312 ? 2.3613 2.3449 1.6428 -0.2218 -0.0959 -0.0817 331 THR A OG1 2506 C CG2 . THR A 312 ? 2.5692 2.5719 1.8265 -0.2270 -0.0511 -0.0915 331 THR A CG2 2507 N N . GLY A 313 ? 2.3419 2.3453 1.6816 -0.1857 -0.0305 -0.1312 332 GLY A N 2508 C CA . GLY A 313 ? 2.3842 2.3957 1.7606 -0.1765 -0.0169 -0.1371 332 GLY A CA 2509 C C . GLY A 313 ? 2.2949 2.2979 1.6887 -0.1637 -0.0203 -0.1526 332 GLY A C 2510 O O . GLY A 313 ? 2.3374 2.3443 1.7654 -0.1559 -0.0140 -0.1569 332 GLY A O 2511 N N . TYR A 314 ? 2.1951 2.1868 1.5678 -0.1627 -0.0317 -0.1589 333 TYR A N 2512 C CA . TYR A 314 ? 2.1086 2.0928 1.4941 -0.1532 -0.0373 -0.1702 333 TYR A CA 2513 C C . TYR A 314 ? 2.0537 2.0287 1.4098 -0.1559 -0.0365 -0.1819 333 TYR A C 2514 O O . TYR A 314 ? 2.0442 2.0156 1.3670 -0.1651 -0.0393 -0.1786 333 TYR A O 2515 C CB . TYR A 314 ? 2.0445 2.0251 1.4428 -0.1483 -0.0575 -0.1623 333 TYR A CB 2516 C CG . TYR A 314 ? 2.0928 2.0787 1.5217 -0.1439 -0.0623 -0.1543 333 TYR A CG 2517 C CD1 . TYR A 314 ? 2.1462 2.1365 1.5789 -0.1489 -0.0670 -0.1417 333 TYR A CD1 2518 C CD2 . TYR A 314 ? 2.1085 2.0937 1.5629 -0.1359 -0.0662 -0.1578 333 TYR A CD2 2519 C CE1 . TYR A 314 ? 2.2129 2.2061 1.6755 -0.1447 -0.0745 -0.1351 333 TYR A CE1 2520 C CE2 . TYR A 314 ? 2.1681 2.1557 1.6483 -0.1325 -0.0736 -0.1510 333 TYR A CE2 2521 C CZ . TYR A 314 ? 2.2169 2.2081 1.7018 -0.1364 -0.0775 -0.1406 333 TYR A CZ 2522 O OH . TYR A 314 ? 2.2996 2.2913 1.8117 -0.1330 -0.0873 -0.1347 333 TYR A OH 2523 N N . LYS A 315 ? 2.0288 1.9989 1.3993 -0.1486 -0.0355 -0.1943 334 LYS A N 2524 C CA . LYS A 315 ? 1.9996 1.9592 1.3503 -0.1498 -0.0378 -0.2064 334 LYS A CA 2525 C C . LYS A 315 ? 1.9317 1.8862 1.3039 -0.1429 -0.0518 -0.2063 334 LYS A C 2526 O O . LYS A 315 ? 1.9612 1.9207 1.3634 -0.1369 -0.0547 -0.2014 334 LYS A O 2527 C CB . LYS A 315 ? 2.1068 2.0665 1.4538 -0.1497 -0.0183 -0.2253 334 LYS A CB 2528 C CG . LYS A 315 ? 2.2097 2.1764 1.5264 -0.1589 -0.0014 -0.2264 334 LYS A CG 2529 C CD . LYS A 315 ? 2.1797 2.1382 1.4475 -0.1704 -0.0110 -0.2217 334 LYS A CD 2530 C CE . LYS A 315 ? 2.3087 2.2759 1.5437 -0.1824 0.0034 -0.2175 334 LYS A CE 2531 N NZ . LYS A 315 ? 2.3035 2.2609 1.4910 -0.1956 -0.0104 -0.2101 334 LYS A NZ 2532 N N . VAL A 316 ? 1.8786 1.8235 1.2350 -0.1450 -0.0618 -0.2099 335 VAL A N 2533 C CA . VAL A 316 ? 1.8387 1.7805 1.2141 -0.1405 -0.0750 -0.2075 335 VAL A CA 2534 C C . VAL A 316 ? 1.9166 1.8571 1.3215 -0.1347 -0.0699 -0.2180 335 VAL A C 2535 O O . VAL A 316 ? 1.9942 1.9299 1.3963 -0.1347 -0.0593 -0.2337 335 VAL A O 2536 C CB . VAL A 316 ? 1.8193 1.7513 1.1750 -0.1450 -0.0876 -0.2075 335 VAL A CB 2537 C CG1 . VAL A 316 ? 1.8009 1.7324 1.1801 -0.1413 -0.0996 -0.2031 335 VAL A CG1 2538 C CG2 . VAL A 316 ? 1.7669 1.6996 1.1014 -0.1510 -0.0956 -0.1957 335 VAL A CG2 2539 N N . LEU A 317 ? 1.9531 1.8977 1.3865 -0.1305 -0.0783 -0.2096 336 LEU A N 2540 C CA . LEU A 317 ? 2.0722 2.0153 1.5407 -0.1262 -0.0785 -0.2152 336 LEU A CA 2541 C C . LEU A 317 ? 2.1022 2.0406 1.5836 -0.1267 -0.0941 -0.2109 336 LEU A C 2542 O O . LEU A 317 ? 2.0832 2.0274 1.5670 -0.1279 -0.1050 -0.1959 336 LEU A O 2543 C CB . LEU A 317 ? 2.1245 2.0758 1.6191 -0.1232 -0.0778 -0.2065 336 LEU A CB 2544 C CG . LEU A 317 ? 2.2463 2.1963 1.7838 -0.1195 -0.0779 -0.2109 336 LEU A CG 2545 C CD1 . LEU A 317 ? 2.3077 2.2567 1.8557 -0.1168 -0.0595 -0.2291 336 LEU A CD1 2546 C CD2 . LEU A 317 ? 2.2827 2.2388 1.8419 -0.1185 -0.0846 -0.1975 336 LEU A CD2 2547 N N . LYS A 318 ? 2.1867 2.1152 1.6771 -0.1261 -0.0948 -0.2246 337 LYS A N 2548 C CA . LYS A 318 ? 2.2570 2.1796 1.7677 -0.1269 -0.1108 -0.2210 337 LYS A CA 2549 C C . LYS A 318 ? 2.3893 2.3093 1.9449 -0.1229 -0.1116 -0.2281 337 LYS A C 2550 O O . LYS A 318 ? 2.4497 2.3650 2.0131 -0.1192 -0.0987 -0.2480 337 LYS A O 2551 C CB . LYS A 318 ? 2.2648 2.1751 1.7545 -0.1296 -0.1153 -0.2319 337 LYS A CB 2552 C CG . LYS A 318 ? 2.1617 2.0737 1.6185 -0.1347 -0.1216 -0.2201 337 LYS A CG 2553 C CD . LYS A 318 ? 2.1348 2.0561 1.6061 -0.1366 -0.1351 -0.1987 337 LYS A CD 2554 C CE . LYS A 318 ? 2.2144 2.1299 1.7114 -0.1383 -0.1507 -0.1951 337 LYS A CE 2555 N NZ . LYS A 318 ? 2.2372 2.1661 1.7581 -0.1400 -0.1591 -0.1744 337 LYS A NZ 2556 N N . ASP A 319 ? 2.4511 2.3753 2.0375 -0.1244 -0.1264 -0.2114 338 ASP A N 2557 C CA . ASP A 319 ? 2.6006 2.5229 2.2370 -0.1221 -0.1323 -0.2122 338 ASP A CA 2558 C C . ASP A 319 ? 2.6299 2.5572 2.2710 -0.1179 -0.1155 -0.2195 338 ASP A C 2559 O O . ASP A 319 ? 2.5873 2.5233 2.2108 -0.1194 -0.1135 -0.2067 338 ASP A O 2560 C CB . ASP A 319 ? 2.6953 2.6045 2.3608 -0.1195 -0.1372 -0.2299 338 ASP A CB 2561 C CG . ASP A 319 ? 3.1941 3.1009 2.9147 -0.1211 -0.1570 -0.2190 338 ASP A CG 2562 O OD1 . ASP A 319 ? 3.2067 3.1141 2.9311 -0.1272 -0.1754 -0.2010 338 ASP A OD1 2563 O OD2 . ASP A 319 ? 3.4758 3.3808 3.2388 -0.1171 -0.1546 -0.2271 338 ASP A OD2 2564 N N . ASN A 320 ? 2.7245 2.6473 2.3865 -0.1126 -0.1020 -0.2412 339 ASN A N 2565 C CA . ASN A 320 ? 2.7309 2.6609 2.3984 -0.1091 -0.0833 -0.2479 339 ASN A CA 2566 C C . ASN A 320 ? 2.7174 2.6461 2.3575 -0.1069 -0.0605 -0.2721 339 ASN A C 2567 O O . ASN A 320 ? 2.7855 2.7193 2.4436 -0.1029 -0.0416 -0.2858 339 ASN A O 2568 C CB . ASN A 320 ? 3.1285 3.0593 2.8577 -0.1058 -0.0876 -0.2467 339 ASN A CB 2569 C CG . ASN A 320 ? 3.3336 3.2646 3.0864 -0.1105 -0.1125 -0.2216 339 ASN A CG 2570 O OD1 . ASN A 320 ? 3.1394 3.0753 2.8605 -0.1156 -0.1213 -0.2029 339 ASN A OD1 2571 N ND2 . ASN A 320 ? 3.7632 3.7084 3.6516 -0.0576 -0.0734 -0.1161 339 ASN A ND2 2572 N N . VAL A 321 ? 2.6080 2.5309 2.2026 -0.1107 -0.0626 -0.2755 340 VAL A N 2573 C CA . VAL A 321 ? 2.6028 2.5219 2.1587 -0.1118 -0.0461 -0.2958 340 VAL A CA 2574 C C . VAL A 321 ? 2.4588 2.3831 1.9615 -0.1182 -0.0425 -0.2835 340 VAL A C 2575 O O . VAL A 321 ? 2.3371 2.2603 1.8242 -0.1218 -0.0585 -0.2661 340 VAL A O 2576 C CB . VAL A 321 ? 2.6420 2.5457 2.1932 -0.1121 -0.0570 -0.3108 340 VAL A CB 2577 C CG1 . VAL A 321 ? 2.6806 2.5789 2.1933 -0.1134 -0.0395 -0.3366 340 VAL A CG1 2578 C CG2 . VAL A 321 ? 2.7922 2.6897 2.4037 -0.1066 -0.0681 -0.3177 340 VAL A CG2 2579 N N . GLU A 322 ? 2.4928 2.4236 1.9710 -0.1202 -0.0214 -0.2924 341 GLU A N 2580 C CA A GLU A 322 ? 2.3972 2.3330 1.8297 -0.1275 -0.0185 -0.2802 341 GLU A CA 2581 C CA B GLU A 322 ? 2.4035 2.3391 1.8359 -0.1275 -0.0187 -0.2801 341 GLU A CA 2582 C C . GLU A 322 ? 2.3885 2.3138 1.7714 -0.1346 -0.0211 -0.2887 341 GLU A C 2583 O O . GLU A 322 ? 2.5029 2.4207 1.8776 -0.1341 -0.0130 -0.3113 341 GLU A O 2584 C CB A GLU A 322 ? 2.4552 2.4050 1.8890 -0.1282 0.0033 -0.2803 341 GLU A CB 2585 C CB B GLU A 322 ? 2.4590 2.4091 1.8936 -0.1283 0.0017 -0.2780 341 GLU A CB 2586 C CG A GLU A 322 ? 2.4410 2.4003 1.9131 -0.1242 -0.0002 -0.2637 341 GLU A CG 2587 C CG B GLU A 322 ? 2.6108 2.5658 2.0513 -0.1264 0.0271 -0.3013 341 GLU A CG 2588 C CD A GLU A 322 ? 2.5217 2.4950 2.0075 -0.1242 0.0205 -0.2637 341 GLU A CD 2589 C CD B GLU A 322 ? 2.7479 2.7018 2.1327 -0.1348 0.0405 -0.3133 341 GLU A CD 2590 O OE1 A GLU A 322 ? 2.5213 2.5014 1.9734 -0.1313 0.0294 -0.2576 341 GLU A OE1 2591 O OE1 B GLU A 322 ? 2.7181 2.6801 2.0710 -0.1432 0.0450 -0.2988 341 GLU A OE1 2592 O OE2 A GLU A 322 ? 2.6066 2.5847 2.1406 -0.1180 0.0267 -0.2680 341 GLU A OE2 2593 O OE2 B GLU A 322 ? 2.8936 2.8381 2.2671 -0.1338 0.0454 -0.3371 341 GLU A OE2 2594 N N . MET A 323 ? 2.2807 2.2048 1.6322 -0.1415 -0.0334 -0.2713 342 MET A N 2595 C CA . MET A 323 ? 2.2765 2.1895 1.5813 -0.1503 -0.0411 -0.2738 342 MET A CA 2596 C C . MET A 323 ? 2.1877 2.1050 1.4652 -0.1585 -0.0484 -0.2529 342 MET A C 2597 O O . MET A 323 ? 2.1221 2.0489 1.4205 -0.1557 -0.0522 -0.2367 342 MET A O 2598 C CB . MET A 323 ? 2.2712 2.1697 1.5829 -0.1489 -0.0607 -0.2775 342 MET A CB 2599 C CG . MET A 323 ? 2.1767 2.0783 1.5116 -0.1468 -0.0790 -0.2563 342 MET A CG 2600 S SD . MET A 323 ? 2.2249 2.1152 1.5891 -0.1433 -0.0978 -0.2594 342 MET A SD 2601 C CE . MET A 323 ? 2.2792 2.1504 1.6014 -0.1514 -0.1079 -0.2711 342 MET A CE 2602 N N . ASP A 324 ? 2.2252 2.1344 1.4575 -0.1692 -0.0525 -0.2536 343 ASP A N 2603 C CA . ASP A 324 ? 2.1742 2.0856 1.3829 -0.1788 -0.0622 -0.2335 343 ASP A CA 2604 C C . ASP A 324 ? 2.0539 1.9607 1.2767 -0.1780 -0.0855 -0.2176 343 ASP A C 2605 O O . ASP A 324 ? 1.9868 1.9019 1.2221 -0.1781 -0.0911 -0.2010 343 ASP A O 2606 C CB . ASP A 324 ? 2.2897 2.1941 1.4447 -0.1927 -0.0598 -0.2377 343 ASP A CB 2607 C CG . ASP A 324 ? 2.4201 2.3343 1.5570 -0.1953 -0.0328 -0.2512 343 ASP A CG 2608 O OD1 . ASP A 324 ? 2.3978 2.3271 1.5668 -0.1881 -0.0170 -0.2499 343 ASP A OD1 2609 O OD2 . ASP A 324 ? 2.5559 2.4634 1.6466 -0.2053 -0.0273 -0.2627 343 ASP A OD2 2610 N N . THR A 325 ? 2.0429 1.9370 1.2658 -0.1775 -0.0991 -0.2233 344 THR A N 2611 C CA . THR A 325 ? 1.9599 1.8516 1.2005 -0.1766 -0.1192 -0.2092 344 THR A CA 2612 C C . THR A 325 ? 1.9579 1.8444 1.2242 -0.1698 -0.1258 -0.2162 344 THR A C 2613 O O . THR A 325 ? 2.0495 1.9265 1.3103 -0.1688 -0.1219 -0.2336 344 THR A O 2614 C CB . THR A 325 ? 1.9659 1.8460 1.1777 -0.1885 -0.1371 -0.2001 344 THR A CB 2615 O OG1 . THR A 325 ? 2.0704 1.9336 1.2530 -0.1942 -0.1416 -0.2146 344 THR A OG1 2616 C CG2 . THR A 325 ? 1.9756 1.8605 1.1661 -0.1975 -0.1363 -0.1876 344 THR A CG2 2617 N N . PHE A 326 ? 1.8810 1.7742 1.1763 -0.1658 -0.1361 -0.2028 345 PHE A N 2618 C CA . PHE A 326 ? 1.8745 1.7652 1.1968 -0.1617 -0.1454 -0.2029 345 PHE A CA 2619 C C . PHE A 326 ? 1.8118 1.7019 1.1412 -0.1655 -0.1627 -0.1881 345 PHE A C 2620 O O . PHE A 326 ? 1.7384 1.6389 1.0727 -0.1657 -0.1635 -0.1757 345 PHE A O 2621 C CB . PHE A 326 ? 1.8751 1.7794 1.2313 -0.1532 -0.1378 -0.2000 345 PHE A CB 2622 C CG . PHE A 326 ? 1.9147 1.8175 1.2999 -0.1511 -0.1485 -0.1972 345 PHE A CG 2623 C CD1 . PHE A 326 ? 2.0013 1.8891 1.3891 -0.1517 -0.1544 -0.2106 345 PHE A CD1 2624 C CD2 . PHE A 326 ? 1.8847 1.8015 1.2946 -0.1490 -0.1529 -0.1813 345 PHE A CD2 2625 C CE1 . PHE A 326 ? 2.0504 1.9367 1.4702 -0.1506 -0.1671 -0.2056 345 PHE A CE1 2626 C CE2 . PHE A 326 ? 1.9411 1.8587 1.3786 -0.1490 -0.1633 -0.1750 345 PHE A CE2 2627 C CZ . PHE A 326 ? 2.0178 1.9197 1.4624 -0.1500 -0.1716 -0.1859 345 PHE A CZ 2628 N N . GLN A 327 ? 1.8324 1.7102 1.1662 -0.1683 -0.1770 -0.1901 346 GLN A N 2629 C CA . GLN A 327 ? 1.7738 1.6503 1.1197 -0.1725 -0.1943 -0.1757 346 GLN A CA 2630 C C . GLN A 327 ? 1.7585 1.6457 1.1442 -0.1682 -0.1993 -0.1655 346 GLN A C 2631 O O . GLN A 327 ? 1.8053 1.6869 1.2048 -0.1662 -0.2022 -0.1718 346 GLN A O 2632 C CB . GLN A 327 ? 1.8564 1.7102 1.1776 -0.1813 -0.2110 -0.1816 346 GLN A CB 2633 C CG . GLN A 327 ? 1.8489 1.7003 1.1824 -0.1873 -0.2305 -0.1648 346 GLN A CG 2634 C CD . GLN A 327 ? 1.9335 1.7603 1.2384 -0.1979 -0.2500 -0.1692 346 GLN A CD 2635 O OE1 . GLN A 327 ? 1.9839 1.7997 1.2463 -0.2048 -0.2483 -0.1774 346 GLN A OE1 2636 N NE2 . GLN A 327 ? 1.9650 1.7833 1.2922 -0.2008 -0.2701 -0.1616 346 GLN A NE2 2637 N N . ILE A 328 ? 1.7058 1.6093 1.1117 -0.1673 -0.2003 -0.1497 347 ILE A N 2638 C CA . ILE A 328 ? 1.7160 1.6342 1.1575 -0.1653 -0.2035 -0.1364 347 ILE A CA 2639 C C . ILE A 328 ? 1.7243 1.6441 1.1820 -0.1699 -0.2168 -0.1234 347 ILE A C 2640 O O . ILE A 328 ? 1.7105 1.6256 1.1561 -0.1729 -0.2206 -0.1224 347 ILE A O 2641 C CB . ILE A 328 ? 1.7117 1.6530 1.1666 -0.1593 -0.1882 -0.1309 347 ILE A CB 2642 C CG1 . ILE A 328 ? 1.6528 1.6060 1.1012 -0.1570 -0.1796 -0.1288 347 ILE A CG1 2643 C CG2 . ILE A 328 ? 1.7554 1.6935 1.2044 -0.1558 -0.1796 -0.1412 347 ILE A CG2 2644 C CD1 . ILE A 328 ? 1.6487 1.6243 1.1076 -0.1515 -0.1662 -0.1248 347 ILE A CD1 2645 N N . GLU A 329 ? 1.7542 1.6804 1.2429 -0.1713 -0.2253 -0.1117 348 GLU A N 2646 C CA . GLU A 329 ? 1.7709 1.7005 1.2841 -0.1755 -0.2379 -0.0977 348 GLU A CA 2647 C C . GLU A 329 ? 1.7793 1.7371 1.3299 -0.1737 -0.2307 -0.0812 348 GLU A C 2648 O O . GLU A 329 ? 1.8039 1.7731 1.3631 -0.1720 -0.2236 -0.0778 348 GLU A O 2649 C CB . GLU A 329 ? 1.8352 1.7401 1.3493 -0.1822 -0.2610 -0.0987 348 GLU A CB 2650 C CG . GLU A 329 ? 1.9009 1.8044 1.4393 -0.1827 -0.2689 -0.0947 348 GLU A CG 2651 C CD . GLU A 329 ? 1.9823 1.8606 1.5266 -0.1890 -0.2946 -0.0960 348 GLU A CD 2652 O OE1 . GLU A 329 ? 2.0030 1.8703 1.5446 -0.1945 -0.3089 -0.0917 348 GLU A OE1 2653 O OE2 . GLU A 329 ? 2.0393 1.9078 1.5941 -0.1888 -0.3025 -0.1011 348 GLU A OE2 2654 N N . CYS A 330 ? 1.7829 1.7528 1.3573 -0.1748 -0.2326 -0.0704 349 CYS A N 2655 C CA . CYS A 330 ? 1.8076 1.8075 1.4185 -0.1739 -0.2234 -0.0550 349 CYS A CA 2656 C C . CYS A 330 ? 1.8685 1.8650 1.5099 -0.1802 -0.2403 -0.0403 349 CYS A C 2657 O O . CYS A 330 ? 1.8794 1.8602 1.5338 -0.1849 -0.2591 -0.0362 349 CYS A O 2658 C CB . CYS A 330 ? 1.7930 1.8077 1.4227 -0.1715 -0.2172 -0.0522 349 CYS A CB 2659 S SG . CYS A 330 ? 1.8530 1.9089 1.5286 -0.1701 -0.2012 -0.0360 349 CYS A SG 2660 N N . LEU A 331 ? 1.9156 1.9247 1.5688 -0.1813 -0.2364 -0.0315 350 LEU A N 2661 C CA . LEU A 331 ? 1.9921 1.9991 1.6785 -0.1878 -0.2536 -0.0156 350 LEU A CA 2662 C C . LEU A 331 ? 2.0397 2.0749 1.7705 -0.1912 -0.2504 0.0065 350 LEU A C 2663 O O . LEU A 331 ? 2.0086 2.0691 1.7440 -0.1877 -0.2308 0.0079 350 LEU A O 2664 C CB . LEU A 331 ? 2.0594 2.0677 1.7455 -0.1891 -0.2539 -0.0129 350 LEU A CB 2665 C CG . LEU A 331 ? 2.0464 2.0290 1.6981 -0.1853 -0.2560 -0.0348 350 LEU A CG 2666 C CD1 . LEU A 331 ? 2.1466 2.1387 1.8043 -0.1857 -0.2515 -0.0299 350 LEU A CD1 2667 C CD2 . LEU A 331 ? 2.0559 2.0041 1.7039 -0.1876 -0.2790 -0.0464 350 LEU A CD2 2668 N N . LYS A 332 ? 2.1173 2.1485 1.8837 -0.1981 -0.2697 0.0229 351 LYS A N 2669 C CA . LYS A 332 ? 2.1766 2.2336 1.9931 -0.2028 -0.2697 0.0469 351 LYS A CA 2670 C C . LYS A 332 ? 2.2305 2.3307 2.0579 -0.2030 -0.2429 0.0606 351 LYS A C 2671 O O . LYS A 332 ? 2.2353 2.3635 2.0881 -0.2022 -0.2278 0.0690 351 LYS A O 2672 C CB . LYS A 332 ? 2.2687 2.3100 2.1192 -0.2107 -0.2982 0.0619 351 LYS A CB 2673 C CG . LYS A 332 ? 2.3238 2.3874 2.2318 -0.2166 -0.3029 0.0880 351 LYS A CG 2674 C CD . LYS A 332 ? 2.4244 2.4716 2.3677 -0.2248 -0.3333 0.1038 351 LYS A CD 2675 C CE . LYS A 332 ? 2.4839 2.5670 2.4855 -0.2325 -0.3303 0.1374 351 LYS A CE 2676 N NZ . LYS A 332 ? 2.4487 2.5532 2.4888 -0.2328 -0.3226 0.1491 351 LYS A NZ 2677 N N . ASP A 333 ? 2.3168 2.4225 2.1249 -0.2043 -0.2368 0.0618 352 ASP A N 2678 C CA . ASP A 333 ? 2.4290 2.5735 2.2384 -0.2070 -0.2139 0.0756 352 ASP A CA 2679 C C . ASP A 333 ? 2.3640 2.5260 2.1418 -0.1991 -0.1860 0.0591 352 ASP A C 2680 O O . ASP A 333 ? 2.4697 2.6638 2.2417 -0.2013 -0.1657 0.0674 352 ASP A O 2681 C CB . ASP A 333 ? 2.5668 2.7077 2.3687 -0.2128 -0.2224 0.0846 352 ASP A CB 2682 C CG . ASP A 333 ? 2.5140 2.6283 2.2741 -0.2068 -0.2243 0.0612 352 ASP A CG 2683 O OD1 . ASP A 333 ? 2.3749 2.4704 2.1086 -0.1985 -0.2209 0.0378 352 ASP A OD1 2684 O OD2 . ASP A 333 ? 2.6335 2.7465 2.3908 -0.2109 -0.2299 0.0677 352 ASP A OD2 2685 N N . GLY A 334 ? 2.2098 2.3505 1.9666 -0.1908 -0.1865 0.0364 353 GLY A N 2686 C CA . GLY A 334 ? 2.1595 2.3122 1.8914 -0.1827 -0.1644 0.0190 353 GLY A CA 2687 C C . GLY A 334 ? 2.1442 2.2844 1.8309 -0.1790 -0.1597 0.0036 353 GLY A C 2688 O O . GLY A 334 ? 2.1396 2.2924 1.8053 -0.1733 -0.1416 -0.0086 353 GLY A O 2689 N N . THR A 335 ? 2.1352 2.2504 1.8107 -0.1819 -0.1765 0.0031 354 THR A N 2690 C CA . THR A 335 ? 2.1109 2.2126 1.7512 -0.1788 -0.1741 -0.0105 354 THR A CA 2691 C C . THR A 335 ? 1.9899 2.0566 1.6114 -0.1744 -0.1860 -0.0296 354 THR A C 2692 O O . THR A 335 ? 1.9400 1.9893 1.5744 -0.1764 -0.2014 -0.0293 354 THR A O 2693 C CB . THR A 335 ? 2.2404 2.3446 1.8871 -0.1858 -0.1820 0.0039 354 THR A CB 2694 O OG1 . THR A 335 ? 2.2453 2.3243 1.9101 -0.1889 -0.2047 0.0061 354 THR A OG1 2695 C CG2 . THR A 335 ? 2.3778 2.5180 2.0430 -0.1937 -0.1727 0.0281 354 THR A CG2 2696 N N . TRP A 336 ? 1.9531 2.0098 1.5437 -0.1695 -0.1793 -0.0453 355 TRP A N 2697 C CA . TRP A 336 ? 1.8715 1.8985 1.4404 -0.1664 -0.1869 -0.0631 355 TRP A CA 2698 C C . TRP A 336 ? 1.9341 1.9421 1.5058 -0.1690 -0.2000 -0.0650 355 TRP A C 2699 O O . TRP A 336 ? 2.0396 2.0577 1.6248 -0.1720 -0.2009 -0.0542 355 TRP A O 2700 C CB . TRP A 336 ? 1.8155 1.8428 1.3560 -0.1601 -0.1730 -0.0777 355 TRP A CB 2701 C CG . TRP A 336 ? 1.7514 1.7899 1.2921 -0.1566 -0.1645 -0.0808 355 TRP A CG 2702 C CD1 . TRP A 336 ? 1.7774 1.8414 1.3233 -0.1537 -0.1498 -0.0785 355 TRP A CD1 2703 C CD2 . TRP A 336 ? 1.6638 1.6882 1.2029 -0.1563 -0.1719 -0.0867 355 TRP A CD2 2704 N NE1 . TRP A 336 ? 1.7157 1.7821 1.2684 -0.1500 -0.1471 -0.0845 355 TRP A NE1 2705 C CE2 . TRP A 336 ? 1.6549 1.6971 1.2047 -0.1522 -0.1618 -0.0877 355 TRP A CE2 2706 C CE3 . TRP A 336 ? 1.6535 1.6516 1.1818 -0.1598 -0.1868 -0.0918 355 TRP A CE3 2707 C CZ2 . TRP A 336 ? 1.6329 1.6670 1.1897 -0.1518 -0.1686 -0.0910 355 TRP A CZ2 2708 C CZ3 . TRP A 336 ? 1.6359 1.6259 1.1636 -0.1609 -0.1934 -0.0937 355 TRP A CZ3 2709 C CH2 . TRP A 336 ? 1.6231 1.6307 1.1678 -0.1570 -0.1854 -0.0923 355 TRP A CH2 2710 N N . SER A 337 ? 1.8944 1.8750 1.4542 -0.1687 -0.2110 -0.0788 356 SER A N 2711 C CA . SER A 337 ? 1.9673 1.9273 1.5308 -0.1698 -0.2230 -0.0866 356 SER A CA 2712 C C . SER A 337 ? 1.9978 1.9587 1.5525 -0.1660 -0.2131 -0.0950 356 SER A C 2713 O O . SER A 337 ? 2.0902 2.0446 1.6637 -0.1671 -0.2215 -0.0947 356 SER A O 2714 C CB . SER A 337 ? 1.9373 1.8693 1.4809 -0.1702 -0.2331 -0.1035 356 SER A CB 2715 O OG . SER A 337 ? 1.8563 1.7828 1.3653 -0.1666 -0.2206 -0.1186 356 SER A OG 2716 N N . ASN A 338 ? 1.9316 1.9001 1.4629 -0.1616 -0.1972 -0.1019 357 ASN A N 2717 C CA . ASN A 338 ? 1.9679 1.9381 1.4916 -0.1579 -0.1876 -0.1088 357 ASN A CA 2718 C C . ASN A 338 ? 1.9216 1.9091 1.4297 -0.1549 -0.1731 -0.1068 357 ASN A C 2719 O O . ASN A 338 ? 1.8778 1.8736 1.3795 -0.1544 -0.1690 -0.1045 357 ASN A O 2720 C CB . ASN A 338 ? 1.9555 1.9040 1.4629 -0.1545 -0.1859 -0.1302 357 ASN A CB 2721 C CG . ASN A 338 ? 2.0673 2.0039 1.5958 -0.1543 -0.1938 -0.1364 357 ASN A CG 2722 O OD1 . ASN A 338 ? 2.1205 2.0628 1.6635 -0.1530 -0.1911 -0.1338 357 ASN A OD1 2723 N ND2 . ASN A 338 ? 2.1142 2.0327 1.6470 -0.1558 -0.2056 -0.1454 357 ASN A ND2 2724 N N . LYS A 339 ? 1.9490 1.9407 1.4543 -0.1528 -0.1668 -0.1086 358 LYS A N 2725 C CA . LYS A 339 ? 1.9069 1.9115 1.3965 -0.1497 -0.1551 -0.1095 358 LYS A CA 2726 C C . LYS A 339 ? 1.8162 1.8081 1.2862 -0.1449 -0.1487 -0.1256 358 LYS A C 2727 O O . LYS A 339 ? 1.7977 1.7726 1.2639 -0.1449 -0.1515 -0.1356 358 LYS A O 2728 C CB . LYS A 339 ? 1.9894 2.0011 1.4846 -0.1509 -0.1549 -0.1033 358 LYS A CB 2729 C CG . LYS A 339 ? 2.1218 2.1516 1.6300 -0.1579 -0.1598 -0.0835 358 LYS A CG 2730 N N . ILE A 340 ? 1.7729 1.7734 1.2305 -0.1416 -0.1405 -0.1282 359 ILE A N 2731 C CA . ILE A 340 ? 1.7032 1.6942 1.1453 -0.1385 -0.1355 -0.1395 359 ILE A CA 2732 C C . ILE A 340 ? 1.7350 1.7197 1.1774 -0.1365 -0.1317 -0.1455 359 ILE A C 2733 O O . ILE A 340 ? 1.7951 1.7881 1.2429 -0.1354 -0.1306 -0.1413 359 ILE A O 2734 C CB . ILE A 340 ? 1.6640 1.6651 1.1000 -0.1355 -0.1310 -0.1402 359 ILE A CB 2735 C CG1 . ILE A 340 ? 1.6308 1.6377 1.0740 -0.1371 -0.1346 -0.1354 359 ILE A CG1 2736 C CG2 . ILE A 340 ? 1.6275 1.6194 1.0516 -0.1336 -0.1280 -0.1485 359 ILE A CG2 2737 C CD1 . ILE A 340 ? 1.6800 1.7060 1.1358 -0.1375 -0.1321 -0.1266 359 ILE A CD1 2738 N N . PRO A 341 ? 1.7260 1.6966 1.1630 -0.1365 -0.1296 -0.1555 360 PRO A N 2739 C CA . PRO A 341 ? 1.7659 1.7324 1.2097 -0.1340 -0.1239 -0.1620 360 PRO A CA 2740 C C . PRO A 341 ? 1.7497 1.7201 1.1849 -0.1315 -0.1170 -0.1637 360 PRO A C 2741 O O . PRO A 341 ? 1.6962 1.6704 1.1196 -0.1316 -0.1174 -0.1616 360 PRO A O 2742 C CB . PRO A 341 ? 1.7814 1.7339 1.2211 -0.1351 -0.1216 -0.1741 360 PRO A CB 2743 C CG . PRO A 341 ? 1.7294 1.6773 1.1482 -0.1386 -0.1251 -0.1743 360 PRO A CG 2744 C CD . PRO A 341 ? 1.6982 1.6567 1.1221 -0.1394 -0.1322 -0.1616 360 PRO A CD 2745 N N . THR A 342 ? 1.8302 1.7996 1.2770 -0.1292 -0.1125 -0.1667 361 THR A N 2746 C CA . THR A 342 ? 1.8596 1.8320 1.3044 -0.1270 -0.1078 -0.1670 361 THR A CA 2747 C C . THR A 342 ? 1.8562 1.8231 1.2936 -0.1278 -0.0978 -0.1746 361 THR A C 2748 O O . THR A 342 ? 1.8433 1.8036 1.2773 -0.1294 -0.0928 -0.1826 361 THR A O 2749 C CB . THR A 342 ? 1.9575 1.9330 1.4220 -0.1251 -0.1109 -0.1630 361 THR A CB 2750 O OG1 . THR A 342 ? 2.0066 1.9764 1.4921 -0.1249 -0.1089 -0.1670 361 THR A OG1 2751 C CG2 . THR A 342 ? 1.9937 1.9770 1.4570 -0.1263 -0.1202 -0.1539 361 THR A CG2 2752 N N . CYS A 343 ? 1.8831 1.8533 1.3181 -0.1274 -0.0950 -0.1722 362 CYS A N 2753 C CA . CYS A 343 ? 1.9127 1.8814 1.3411 -0.1298 -0.0847 -0.1757 362 CYS A CA 2754 C C . CYS A 343 ? 2.0087 1.9802 1.4616 -0.1270 -0.0774 -0.1769 362 CYS A C 2755 O O . CYS A 343 ? 2.0409 2.0151 1.5110 -0.1239 -0.0844 -0.1714 362 CYS A O 2756 C CB . CYS A 343 ? 1.8756 1.8463 1.2901 -0.1330 -0.0884 -0.1692 362 CYS A CB 2757 S SG . CYS A 343 ? 1.7680 1.7339 1.1583 -0.1381 -0.0966 -0.1675 362 CYS A SG 2758 N N . LYS A 344 ? 2.0726 2.0434 1.5278 -0.1282 -0.0635 -0.1851 363 LYS A N 2759 C CA . LYS A 344 ? 2.1789 2.1537 1.6638 -0.1254 -0.0537 -0.1877 363 LYS A CA 2760 C C . LYS A 344 ? 2.2045 2.1857 1.6807 -0.1295 -0.0394 -0.1870 363 LYS A C 2761 O O . LYS A 344 ? 2.2141 2.1946 1.6623 -0.1345 -0.0304 -0.1927 363 LYS A O 2762 C CB . LYS A 344 ? 2.2686 2.2394 1.7719 -0.1226 -0.0476 -0.2002 363 LYS A CB 2763 C CG . LYS A 344 ? 2.4033 2.3772 1.9512 -0.1184 -0.0436 -0.2012 363 LYS A CG 2764 C CD . LYS A 344 ? 2.5217 2.5002 2.0814 -0.1176 -0.0213 -0.2153 363 LYS A CD 2765 C CE . LYS A 344 ? 2.6311 2.6144 2.2427 -0.1133 -0.0162 -0.2155 363 LYS A CE 2766 N NZ . LYS A 344 ? 2.6256 2.6172 2.2465 -0.1147 -0.0144 -0.2024 363 LYS A NZ 2767 N N . LYS A 345 ? 2.6833 2.6706 2.1825 -0.1285 -0.0389 -0.1786 364 LYS A N 2768 C CA . LYS A 345 ? 2.8017 2.7980 2.3007 -0.1331 -0.0261 -0.1735 364 LYS A CA 2769 C C . LYS A 345 ? 2.9734 2.9758 2.4759 -0.1342 -0.0023 -0.1861 364 LYS A C 2770 O O . LYS A 345 ? 3.0425 3.0413 2.5620 -0.1291 0.0022 -0.1991 364 LYS A O 2771 C CB . LYS A 345 ? 2.4090 2.4093 1.9433 -0.1304 -0.0331 -0.1624 364 LYS A CB 2772 C CG . LYS A 345 ? 2.4396 2.4507 1.9819 -0.1357 -0.0230 -0.1525 364 LYS A CG 2773 C CD . LYS A 345 ? 2.4401 2.4537 2.0263 -0.1322 -0.0301 -0.1433 364 LYS A CD 2774 C CE . LYS A 345 ? 2.4947 2.5224 2.1017 -0.1369 -0.0135 -0.1351 364 LYS A CE 2775 N NZ . LYS A 345 ? 2.5076 2.5374 2.1658 -0.1330 -0.0195 -0.1273 364 LYS A NZ 2776 N N . ASN A 346 ? 2.6741 2.6866 2.1632 -0.1412 0.0130 -0.1824 365 ASN A N 2777 C CA . ASN A 346 ? 2.7857 2.8075 2.2756 -0.1429 0.0397 -0.1957 365 ASN A CA 2778 C C . ASN A 346 ? 2.7765 2.8095 2.3202 -0.1378 0.0521 -0.1951 365 ASN A C 2779 O O . ASN A 346 ? 2.8699 2.9116 2.4275 -0.1362 0.0757 -0.2098 365 ASN A O 2780 C CB . ASN A 346 ? 2.8816 2.9111 2.3280 -0.1549 0.0514 -0.1908 365 ASN A CB 2781 C CG . ASN A 346 ? 2.9025 2.9195 2.3003 -0.1608 0.0367 -0.1905 365 ASN A CG 2782 O OD1 . ASN A 346 ? 2.8542 2.8581 2.2516 -0.1555 0.0187 -0.1935 365 ASN A OD1 2783 N ND2 . ASN A 346 ? 2.9824 3.0038 2.3397 -0.1732 0.0430 -0.1845 365 ASN A ND2 2784 N N . GLU A 347 ? 2.7023 2.7344 2.2783 -0.1348 0.0355 -0.1795 366 GLU A N 2785 C CA . GLU A 347 ? 2.6856 2.7255 2.3179 -0.1305 0.0395 -0.1741 366 GLU A CA 2786 C C . GLU A 347 ? 2.8044 2.8640 2.4557 -0.1341 0.0686 -0.1748 366 GLU A C 2787 O O . GLU A 347 ? 2.8635 2.9299 2.5406 -0.1299 0.0890 -0.1908 366 GLU A O 2788 C CB . GLU A 347 ? 2.6171 2.6473 2.2879 -0.1217 0.0287 -0.1819 366 GLU A CB 2789 C CG . GLU A 347 ? 2.5005 2.5189 2.1781 -0.1197 -0.0014 -0.1689 366 GLU A CG 2790 C CD . GLU A 347 ? 2.4449 2.4579 2.1731 -0.1144 -0.0143 -0.1665 366 GLU A CD 2791 O OE1 . GLU A 347 ? 2.4868 2.5056 2.2575 -0.1113 -0.0002 -0.1741 366 GLU A OE1 2792 O OE2 . GLU A 347 ? 2.3697 2.3727 2.0960 -0.1140 -0.0390 -0.1570 366 GLU A OE2 2793 C C1 . NAG B . ? 2.5118 2.9899 2.4207 -0.0845 0.1467 0.1160 649 NAG A C1 2794 C C2 . NAG B . ? 2.2955 2.7359 2.1566 -0.0568 0.1625 0.1620 649 NAG A C2 2795 C C3 . NAG B . ? 2.3685 2.8166 2.2112 -0.0838 0.1801 0.1653 649 NAG A C3 2796 C C4 . NAG B . ? 2.8342 3.3711 2.6811 -0.0868 0.1592 0.1422 649 NAG A C4 2797 C C5 . NAG B . ? 2.9271 3.5027 2.8259 -0.1009 0.1363 0.0980 649 NAG A C5 2798 C C6 . NAG B . ? 3.4729 3.7887 3.3791 -0.0531 0.1179 0.0478 649 NAG A C6 2799 C C7 . NAG B . ? 2.2933 2.5922 2.1144 -0.0174 0.1940 0.2135 649 NAG A C7 2800 C C8 . NAG B . ? 2.1292 2.3264 1.9482 -0.0208 0.2168 0.2166 649 NAG A C8 2801 N N2 . NAG B . ? 2.0824 2.4309 1.9372 -0.0553 0.1841 0.1764 649 NAG A N2 2802 O O3 . NAG B . ? 2.5036 2.9044 2.2903 -0.0665 0.2040 0.2113 649 NAG A O3 2803 O O4 . NAG B . ? 3.1394 3.6813 2.9764 -0.1135 0.1813 0.1395 649 NAG A O4 2804 O O5 . NAG B . ? 2.8590 3.4167 2.7759 -0.0830 0.1255 0.0981 649 NAG A O5 2805 O O6 . NAG B . ? 3.5997 3.7935 3.4778 -0.0264 0.0997 0.0396 649 NAG A O6 2806 O O7 . NAG B . ? 2.4749 2.8088 2.2663 0.0204 0.1836 0.2414 649 NAG A O7 2807 C C1 . NAG C . ? 3.0804 3.6528 2.8640 -0.1008 0.1881 0.1592 650 NAG A C1 2808 C C2 . NAG C . ? 2.8086 3.3845 2.5987 -0.1355 0.2189 0.1488 650 NAG A C2 2809 C C3 . NAG C . ? 3.4185 3.7679 3.1399 -0.0877 0.2386 0.1313 650 NAG A C3 2810 C C4 . NAG C . ? 3.5831 3.7773 3.2428 -0.0498 0.2056 0.1097 650 NAG A C4 2811 C C5 . NAG C . ? 2.8250 3.5122 2.5472 -0.0739 0.1571 0.1458 650 NAG A C5 2812 C C6 . NAG C . ? 2.4919 3.2226 2.1848 -0.0345 0.1216 0.1558 650 NAG A C6 2813 C C7 . NAG C . ? 2.1145 2.7374 2.0056 -0.1899 0.2243 0.0801 650 NAG A C7 2814 C C8 . NAG C . ? 1.6309 2.3005 1.5726 -0.1987 0.2026 0.0334 650 NAG A C8 2815 N N2 . NAG C . ? 2.5494 3.1710 2.3977 -0.1578 0.2045 0.1002 650 NAG A N2 2816 O O3 . NAG C . ? 3.6973 3.7783 3.5034 -0.0466 0.1740 0.0794 650 NAG A O3 2817 O O4 . NAG C . ? 3.7436 3.7890 3.4911 -0.0243 0.1314 0.0571 650 NAG A O4 2818 O O5 . NAG C . ? 3.3710 3.7795 3.1487 -0.0622 0.1583 0.1038 650 NAG A O5 2819 O O6 . NAG C . ? 2.2496 2.9340 1.9273 -0.0037 0.1228 0.1967 650 NAG A O6 2820 O O7 . NAG C . ? 2.0753 2.6631 1.9659 -0.2102 0.2589 0.0986 650 NAG A O7 2821 C C1 . BMA D . ? 3.7615 3.7879 3.5007 -0.0210 0.1066 0.0589 651 BMA A C1 2822 C C2 . BMA D . ? 3.7728 3.7914 3.4870 -0.0147 0.0915 0.0504 651 BMA A C2 2823 C C3 . BMA D . ? 3.7830 3.7903 3.5001 -0.0124 0.0703 0.0526 651 BMA A C3 2824 C C4 . BMA D . ? 3.7766 3.7869 3.5036 -0.0171 0.0824 0.0613 651 BMA A C4 2825 C C5 . BMA D . ? 3.7685 3.7831 3.5157 -0.0226 0.0938 0.0683 651 BMA A C5 2826 C C6 . BMA D . ? 3.7617 3.7789 3.5248 -0.0280 0.1020 0.0753 651 BMA A C6 2827 O O2 . BMA D . ? 3.7627 3.7930 3.4696 -0.0155 0.1102 0.0465 651 BMA A O2 2828 O O3 . BMA D . ? 3.7887 3.7930 3.4919 -0.0084 0.0578 0.0448 651 BMA A O3 2829 O O4 . BMA D . ? 3.7848 3.7857 3.5210 -0.0143 0.0640 0.0620 651 BMA A O4 2830 O O5 . BMA D . ? 3.7553 3.7844 3.5058 -0.0259 0.1140 0.0668 651 BMA A O5 2831 O O6 . BMA D . ? 3.7652 3.7748 3.5508 -0.0291 0.0924 0.0784 651 BMA A O6 2832 C C1 . MAN E . ? 3.7961 3.7936 3.5080 -0.0045 0.0315 0.0417 652 MAN A C1 2833 C C2 . MAN E . ? 3.7977 3.7955 3.4945 -0.0028 0.0239 0.0352 652 MAN A C2 2834 C C3 . MAN E . ? 3.7983 3.7977 3.4763 -0.0015 0.0199 0.0247 652 MAN A C3 2835 C C4 . MAN E . ? 3.7995 3.7980 3.4837 -0.0001 0.0013 0.0218 652 MAN A C4 2836 C C5 . MAN E . ? 3.7989 3.7966 3.4885 -0.0013 0.0140 0.0300 652 MAN A C5 2837 C C6 . MAN E . ? 3.7994 3.7954 3.3281 0.0008 -0.0087 0.0443 652 MAN A C6 2838 O O2 . MAN E . ? 3.7995 3.7951 3.5078 -0.0006 0.0046 0.0358 652 MAN A O2 2839 O O3 . MAN E . ? 3.7993 3.7986 3.4727 -0.0005 0.0092 0.0174 652 MAN A O3 2840 O O4 . MAN E . ? 3.7995 3.7992 3.4470 0.0002 -0.0049 0.0110 652 MAN A O4 2841 O O5 . MAN E . ? 3.7985 3.7944 3.5178 -0.0023 0.0169 0.0379 652 MAN A O5 2842 O O6 . MAN E . ? 3.1557 3.7956 2.7496 0.0187 -0.0138 0.0598 652 MAN A O6 2843 C C1 . MAN F . ? 3.7783 3.7755 3.5731 -0.0226 0.0693 0.0738 653 MAN A C1 2844 C C2 . MAN F . ? 3.7813 3.7733 3.6059 -0.0219 0.0595 0.0713 653 MAN A C2 2845 C C3 . MAN F . ? 3.7784 3.7697 3.6218 -0.0251 0.0613 0.0728 653 MAN A C3 2846 C C4 . MAN F . ? 3.7805 3.7689 3.6158 -0.0242 0.0592 0.0750 653 MAN A C4 2847 C C5 . MAN F . ? 3.7768 3.7710 3.5847 -0.0255 0.0700 0.0784 653 MAN A C5 2848 C C6 . MAN F . ? 3.7793 3.7707 3.5769 -0.0242 0.0671 0.0802 653 MAN A C6 2849 O O2 . MAN F . ? 3.7900 3.7762 3.6324 -0.0149 0.0399 0.0625 653 MAN A O2 2850 O O3 . MAN F . ? 3.7828 3.7691 3.6511 -0.0226 0.0499 0.0672 653 MAN A O3 2851 O O4 . MAN F . ? 3.7774 3.7659 3.6288 -0.0273 0.0615 0.0758 653 MAN A O4 2852 O O5 . MAN F . ? 3.7810 3.7750 3.5748 -0.0214 0.0646 0.0743 653 MAN A O5 2853 O O6 . MAN F . ? 3.7763 3.7735 3.5501 -0.0246 0.0762 0.0806 653 MAN A O6 2854 C C1 . NAG G . ? 2.1972 2.5383 2.2465 -0.1239 -0.1332 0.1252 678 NAG A C1 2855 C C2 . NAG G . ? 2.5301 2.8950 2.5820 -0.1179 -0.1267 0.1318 678 NAG A C2 2856 C C3 . NAG G . ? 2.4586 2.8203 2.5125 -0.1145 -0.1502 0.1237 678 NAG A C3 2857 C C4 . NAG G . ? 1.8719 2.2039 1.9082 -0.1275 -0.1775 0.1206 678 NAG A C4 2858 C C5 . NAG G . ? 1.5752 1.8946 1.5957 -0.1421 -0.1730 0.1274 678 NAG A C5 2859 C C6 . NAG G . ? 1.3618 1.6546 1.3724 -0.1553 -0.1994 0.1230 678 NAG A C6 2860 C C7 . NAG G . ? 2.2212 2.6115 2.2573 -0.1189 -0.0954 0.1529 678 NAG A C7 2861 C C8 . NAG G . ? 1.7492 2.1528 1.7654 -0.1250 -0.0906 0.1672 678 NAG A C8 2862 N N2 . NAG G . ? 2.5466 2.9189 2.5805 -0.1241 -0.1189 0.1444 678 NAG A N2 2863 O O3 . NAG G . ? 2.8498 3.2242 2.9260 -0.1016 -0.1502 0.1134 678 NAG A O3 2864 O O4 . NAG G . ? 2.0008 2.3304 2.0242 -0.1315 -0.1954 0.1257 678 NAG A O4 2865 O O5 . NAG G . ? 1.7904 2.1113 1.8196 -0.1373 -0.1523 0.1252 678 NAG A O5 2866 O O6 . NAG G . ? 1.1407 1.4217 1.1665 -0.1490 -0.2055 0.1099 678 NAG A O6 2867 O O7 . NAG G . ? 1.8597 2.2569 1.9132 -0.1104 -0.0805 0.1509 678 NAG A O7 2868 C C1 . NAG H . ? 2.1102 2.4136 2.1231 -0.1382 -0.2312 0.1203 679 NAG A C1 2869 C C2 . NAG H . ? 2.0439 2.3469 2.0688 -0.1189 -0.2465 0.1035 679 NAG A C2 2870 C C3 . NAG H . ? 2.0192 2.3149 2.0306 -0.1182 -0.2689 0.1066 679 NAG A C3 2871 C C4 . NAG H . ? 2.3209 2.5855 2.3101 -0.1408 -0.3024 0.1172 679 NAG A C4 2872 C C5 . NAG H . ? 2.5360 2.8083 2.5162 -0.1624 -0.2869 0.1355 679 NAG A C5 2873 C C6 . NAG H . ? 2.6840 2.9334 2.6595 -0.1775 -0.3062 0.1335 679 NAG A C6 2874 C C7 . NAG H . ? 1.9912 2.3540 2.0502 -0.0891 -0.2018 0.0986 679 NAG A C7 2875 C C8 . NAG H . ? 1.7939 2.1892 1.8781 -0.0698 -0.1898 0.0886 679 NAG A C8 2876 N N2 . NAG H . ? 2.0671 2.3980 2.1153 -0.0988 -0.2255 0.0937 679 NAG A N2 2877 O O3 . NAG H . ? 1.9455 2.2403 1.9653 -0.0960 -0.2854 0.0870 679 NAG A O3 2878 O O4 . NAG H . ? 2.6367 2.8966 2.6114 -0.1443 -0.3207 0.1268 679 NAG A O4 2879 O O5 . NAG H . ? 2.5329 2.8324 2.5252 -0.1541 -0.2458 0.1366 679 NAG A O5 2880 O O6 . NAG H . ? 3.4575 3.6713 3.4362 -0.1049 -0.2319 0.0696 679 NAG A O6 2881 O O7 . NAG H . ? 2.2125 2.5821 2.2623 -0.0965 -0.1910 0.1125 679 NAG A O7 2882 C C1 . BMA I . ? 2.8815 3.1070 2.8451 -0.1426 -0.3661 0.1181 680 BMA A C1 2883 C C2 . BMA I . ? 2.7994 3.0195 2.7425 -0.1572 -0.3843 0.1390 680 BMA A C2 2884 C C3 . BMA I . ? 2.9230 3.1000 2.8516 -0.1543 -0.4380 0.1297 680 BMA A C3 2885 C C4 . BMA I . ? 3.0653 3.2386 3.0058 -0.1184 -0.4415 0.0968 680 BMA A C4 2886 C C5 . BMA I . ? 2.9145 3.1033 2.8773 -0.1049 -0.4181 0.0792 680 BMA A C5 2887 C C6 . BMA I . ? 2.6946 2.8978 2.6720 -0.0684 -0.4151 0.0500 680 BMA A C6 2888 O O2 . BMA I . ? 2.4279 2.6798 2.3770 -0.1453 -0.3528 0.1431 680 BMA A O2 2889 O O3 . BMA I . ? 2.8757 3.0469 2.7848 -0.1681 -0.4562 0.1508 680 BMA A O3 2890 O O4 . BMA I . ? 3.5604 3.7993 3.5250 -0.0081 -0.2563 -0.0087 680 BMA A O4 2891 O O5 . BMA I . ? 2.9575 3.1842 2.9332 -0.1125 -0.3699 0.0925 680 BMA A O5 2892 O O6 . BMA I . ? 2.5152 2.7602 2.5031 -0.0539 -0.3810 0.0509 680 BMA A O6 2893 C C1 . MAN J . ? 3.2396 3.3962 3.1336 -0.1773 -0.4724 0.1551 681 MAN A C1 2894 C C2 . MAN J . ? 3.2794 3.4628 3.1668 -0.1571 -0.4302 0.1531 681 MAN A C2 2895 C C3 . MAN J . ? 3.2115 3.4013 3.0849 -0.2016 -0.4494 0.1955 681 MAN A C3 2896 C C4 . MAN J . ? 3.2142 3.3833 3.0882 -0.1991 -0.4726 0.1782 681 MAN A C4 2897 C C5 . MAN J . ? 2.9549 3.0902 2.8284 -0.2552 -0.5360 0.2122 681 MAN A C5 2898 C C6 . MAN J . ? 2.9706 3.0513 2.8409 -0.2528 -0.5899 0.1944 681 MAN A C6 2899 O O2 . MAN J . ? 3.4560 3.6711 3.3578 -0.0482 -0.3453 0.0590 681 MAN A O2 2900 O O3 . MAN J . ? 2.7540 2.9507 2.5973 -0.2734 -0.5092 0.2746 681 MAN A O3 2901 O O4 . MAN J . ? 3.1718 3.3564 3.0363 -0.2268 -0.4779 0.2072 681 MAN A O4 2902 O O5 . MAN J . ? 2.9152 3.0679 2.8067 -0.2206 -0.4934 0.1855 681 MAN A O5 2903 O O6 . MAN J . ? 2.7839 2.8612 2.6725 -0.2382 -0.5754 0.1693 681 MAN A O6 2904 CA CA . CA K . ? 0.4952 1.0437 0.6048 -0.0596 0.0668 0.2308 701 CA A CA 2905 CA CA . CA L . ? 2.9641 3.7501 3.6135 -0.0489 0.0286 -0.0911 702 CA A CA 2906 CA CA . CA M . ? 2.1935 2.1279 2.0269 -0.2221 -0.2026 0.3191 703 CA A CA # _database_PDB_caveat.id 1 _database_PDB_caveat.text 'NAG A 650 WRONG CHIRALITY AT C1 NAG A 679 WRONG CHIRALITY AT C1' # 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 HIS 1 20 ? ? ? A . n A 1 2 THR 2 21 ? ? ? A . n A 1 3 VAL 3 22 22 VAL VAL A . n A 1 4 GLU 4 23 23 GLU GLU A . n A 1 5 LEU 5 24 24 LEU LEU A . n A 1 6 ASN 6 25 25 ASN ASN A . n A 1 7 ASN 7 26 26 ASN ASN A . n A 1 8 MET 8 27 27 MET MET A . n A 1 9 PHE 9 28 28 PHE PHE A . n A 1 10 GLY 10 29 29 GLY GLY A . n A 1 11 GLN 11 30 30 GLN GLN A . n A 1 12 ILE 12 31 31 ILE ILE A . n A 1 13 GLN 13 32 32 GLN GLN A . n A 1 14 SER 14 33 33 SER SER A . n A 1 15 PRO 15 34 34 PRO PRO A . n A 1 16 GLY 16 35 35 GLY GLY A . n A 1 17 TYR 17 36 36 TYR TYR A . n A 1 18 PRO 18 37 37 PRO PRO A . n A 1 19 ASP 19 38 38 ASP ASP A . n A 1 20 SER 20 39 39 SER SER A . n A 1 21 TYR 21 40 40 TYR TYR A . n A 1 22 PRO 22 41 41 PRO PRO A . n A 1 23 SER 23 42 42 SER SER A . n A 1 24 ASP 24 43 43 ASP ASP A . n A 1 25 SER 25 44 44 SER SER A . n A 1 26 GLU 26 45 45 GLU GLU A . n A 1 27 VAL 27 46 46 VAL VAL A . n A 1 28 THR 28 47 47 THR THR A . n A 1 29 TRP 29 48 48 TRP TRP A . n A 1 30 ASN 30 49 49 ASN ASN A . n A 1 31 ILE 31 50 50 ILE ILE A . n A 1 32 THR 32 51 51 THR THR A . n A 1 33 VAL 33 52 52 VAL VAL A . n A 1 34 PRO 34 53 53 PRO PRO A . n A 1 35 ASP 35 54 54 ASP ASP A . n A 1 36 GLY 36 55 55 GLY GLY A . n A 1 37 PHE 37 56 56 PHE PHE A . n A 1 38 ARG 38 57 57 ARG ARG A . n A 1 39 ILE 39 58 58 ILE ILE A . n A 1 40 LYS 40 59 59 LYS LYS A . n A 1 41 LEU 41 60 60 LEU LEU A . n A 1 42 TYR 42 61 61 TYR TYR A . n A 1 43 PHE 43 62 62 PHE PHE A . n A 1 44 MET 44 63 63 MET MET A . n A 1 45 HIS 45 64 64 HIS HIS A . n A 1 46 PHE 46 65 65 PHE PHE A . n A 1 47 ASN 47 66 66 ASN ASN A . n A 1 48 LEU 48 67 67 LEU LEU A . n A 1 49 GLU 49 68 68 GLU GLU A . n A 1 50 SER 50 69 69 SER SER A . n A 1 51 SER 51 70 70 SER SER A . n A 1 52 TYR 52 71 71 TYR TYR A . n A 1 53 LEU 53 72 72 LEU LEU A . n A 1 54 CYS 54 73 73 CYS CYS A . n A 1 55 GLU 55 74 74 GLU GLU A . n A 1 56 TYR 56 75 75 TYR TYR A . n A 1 57 ASP 57 76 76 ASP ASP A . n A 1 58 TYR 58 77 77 TYR TYR A . n A 1 59 VAL 59 78 78 VAL VAL A . n A 1 60 LYS 60 79 79 LYS LYS A . n A 1 61 VAL 61 80 80 VAL VAL A . n A 1 62 GLU 62 81 81 GLU GLU A . n A 1 63 THR 63 82 82 THR THR A . n A 1 64 GLU 64 83 83 GLU GLU A . n A 1 65 ASP 65 84 84 ASP ASP A . n A 1 66 GLN 66 85 85 GLN GLN A . n A 1 67 VAL 67 86 86 VAL VAL A . n A 1 68 LEU 68 87 87 LEU LEU A . n A 1 69 ALA 69 88 88 ALA ALA A . n A 1 70 THR 70 89 89 THR THR A . n A 1 71 PHE 71 90 90 PHE PHE A . n A 1 72 CYS 72 91 91 CYS CYS A . n A 1 73 GLY 73 92 92 GLY GLY A . n A 1 74 ARG 74 93 93 ARG ARG A . n A 1 75 GLU 75 94 94 GLU GLU A . n A 1 76 THR 76 95 95 THR THR A . n A 1 77 THR 77 96 96 THR THR A . n A 1 78 ASP 78 97 97 ASP ASP A . n A 1 79 THR 79 98 98 THR THR A . n A 1 80 GLU 80 99 99 GLU GLU A . n A 1 81 GLN 81 100 100 GLN GLN A . n A 1 82 THR 82 101 101 THR THR A . n A 1 83 PRO 83 102 102 PRO PRO A . n A 1 84 GLY 84 103 103 GLY GLY A . n A 1 85 GLN 85 104 104 GLN GLN A . n A 1 86 GLU 86 105 105 GLU GLU A . n A 1 87 VAL 87 106 106 VAL VAL A . n A 1 88 VAL 88 107 107 VAL VAL A . n A 1 89 LEU 89 108 108 LEU LEU A . n A 1 90 SER 90 109 109 SER SER A . n A 1 91 PRO 91 110 110 PRO PRO A . n A 1 92 GLY 92 111 111 GLY GLY A . n A 1 93 SER 93 112 112 SER SER A . n A 1 94 PHE 94 113 113 PHE PHE A . n A 1 95 MET 95 114 114 MET MET A . n A 1 96 SER 96 115 115 SER SER A . n A 1 97 ILE 97 116 116 ILE ILE A . n A 1 98 THR 98 117 117 THR THR A . n A 1 99 PHE 99 118 118 PHE PHE A . n A 1 100 ARG 100 119 119 ARG ARG A . n A 1 101 SER 101 120 120 SER SER A . n A 1 102 ASP 102 121 121 ASP ASP A . n A 1 103 PHE 103 122 122 PHE PHE A . n A 1 104 SER 104 123 123 SER SER A . n A 1 105 ASN 105 124 124 ASN ASN A . n A 1 106 GLU 106 125 125 GLU GLU A . n A 1 107 GLU 107 126 126 GLU GLU A . n A 1 108 ARG 108 127 127 ARG ARG A . n A 1 109 PHE 109 128 128 PHE PHE A . n A 1 110 THR 110 129 129 THR THR A . n A 1 111 GLY 111 130 130 GLY GLY A . n A 1 112 PHE 112 131 131 PHE PHE A . n A 1 113 ASP 113 132 132 ASP ASP A . n A 1 114 ALA 114 133 133 ALA ALA A . n A 1 115 HIS 115 134 134 HIS HIS A . n A 1 116 TYR 116 135 135 TYR TYR A . n A 1 117 MET 117 136 136 MET MET A . n A 1 118 ALA 118 137 137 ALA ALA A . n A 1 119 VAL 119 138 138 VAL VAL A . n A 1 120 ASP 120 139 139 ASP ASP A . n A 1 121 VAL 121 140 140 VAL VAL A . n A 1 122 ASP 122 141 141 ASP ASP A . n A 1 123 GLU 123 142 142 GLU GLU A . n A 1 124 CYS 124 143 143 CYS CYS A . n A 1 125 LYS 125 144 144 LYS LYS A . n A 1 126 GLU 126 145 145 GLU GLU A . n A 1 127 ARG 127 146 146 ARG ARG A . n A 1 128 GLU 128 147 147 GLU GLU A . n A 1 129 ASP 129 148 148 ASP ASP A . n A 1 130 GLU 130 149 149 GLU GLU A . n A 1 131 GLU 131 150 150 GLU GLU A . n A 1 132 LEU 132 151 151 LEU LEU A . n A 1 133 SER 133 152 152 SER SER A . n A 1 134 CYS 134 153 153 CYS CYS A . n A 1 135 ASP 135 154 154 ASP ASP A . n A 1 136 HIS 136 155 155 HIS HIS A . n A 1 137 TYR 137 156 156 TYR TYR A . n A 1 138 CYS 138 157 157 CYS CYS A . n A 1 139 HIS 139 158 158 HIS HIS A . n A 1 140 ASN 140 159 159 ASN ASN A . n A 1 141 TYR 141 160 160 TYR TYR A . n A 1 142 ILE 142 161 161 ILE ILE A . n A 1 143 GLY 143 162 162 GLY GLY A . n A 1 144 GLY 144 163 163 GLY GLY A . n A 1 145 TYR 145 164 164 TYR TYR A . n A 1 146 TYR 146 165 165 TYR TYR A . n A 1 147 CYS 147 166 166 CYS CYS A . n A 1 148 SER 148 167 167 SER SER A . n A 1 149 CYS 149 168 168 CYS CYS A . n A 1 150 ARG 150 169 169 ARG ARG A . n A 1 151 PHE 151 170 170 PHE PHE A . n A 1 152 GLY 152 171 171 GLY GLY A . n A 1 153 TYR 153 172 172 TYR TYR A . n A 1 154 ILE 154 173 173 ILE ILE A . n A 1 155 LEU 155 174 174 LEU LEU A . n A 1 156 HIS 156 175 175 HIS HIS A . n A 1 157 THR 157 176 176 THR THR A . n A 1 158 ASP 158 177 177 ASP ASP A . n A 1 159 ASN 159 178 178 ASN ASN A . n A 1 160 ARG 160 179 179 ARG ARG A . n A 1 161 THR 161 180 180 THR THR A . n A 1 162 CYS 162 181 181 CYS CYS A . n A 1 163 ARG 163 182 182 ARG ARG A . n A 1 164 VAL 164 183 183 VAL VAL A . n A 1 165 GLU 165 184 184 GLU GLU A . n A 1 166 CYS 166 185 185 CYS CYS A . n A 1 167 SER 167 186 186 SER SER A . n A 1 168 ASP 168 187 187 ASP ASP A . n A 1 169 ASN 169 188 188 ASN ASN A . n A 1 170 LEU 170 189 189 LEU LEU A . n A 1 171 PHE 171 190 190 PHE PHE A . n A 1 172 THR 172 191 191 THR THR A . n A 1 173 GLN 173 192 192 GLN GLN A . n A 1 174 ARG 174 193 193 ARG ARG A . n A 1 175 THR 175 194 194 THR THR A . n A 1 176 GLY 176 195 195 GLY GLY A . n A 1 177 VAL 177 196 196 VAL VAL A . n A 1 178 ILE 178 197 197 ILE ILE A . n A 1 179 THR 179 198 198 THR THR A . n A 1 180 SER 180 199 199 SER SER A . n A 1 181 PRO 181 200 200 PRO PRO A . n A 1 182 ASP 182 201 201 ASP ASP A . n A 1 183 PHE 183 202 202 PHE PHE A . n A 1 184 PRO 184 203 203 PRO PRO A . n A 1 185 ASN 185 204 204 ASN ASN A . n A 1 186 PRO 186 205 205 PRO PRO A . n A 1 187 TYR 187 206 206 TYR TYR A . n A 1 188 PRO 188 207 207 PRO PRO A . n A 1 189 LYS 189 208 208 LYS LYS A . n A 1 190 SER 190 209 209 SER SER A . n A 1 191 SER 191 210 210 SER SER A . n A 1 192 GLU 192 211 211 GLU GLU A . n A 1 193 CYS 193 212 212 CYS CYS A . n A 1 194 LEU 194 213 213 LEU LEU A . n A 1 195 TYR 195 214 214 TYR TYR A . n A 1 196 THR 196 215 215 THR THR A . n A 1 197 ILE 197 216 216 ILE ILE A . n A 1 198 GLU 198 217 217 GLU GLU A . n A 1 199 LEU 199 218 218 LEU LEU A . n A 1 200 GLU 200 219 219 GLU GLU A . n A 1 201 GLU 201 220 220 GLU GLU A . n A 1 202 GLY 202 221 221 GLY GLY A . n A 1 203 PHE 203 222 222 PHE PHE A . n A 1 204 MET 204 223 223 MET MET A . n A 1 205 VAL 205 224 224 VAL VAL A . n A 1 206 ASN 206 225 225 ASN ASN A . n A 1 207 LEU 207 226 226 LEU LEU A . n A 1 208 GLN 208 227 227 GLN GLN A . n A 1 209 PHE 209 228 228 PHE PHE A . n A 1 210 GLU 210 229 229 GLU GLU A . n A 1 211 ASP 211 230 230 ASP ASP A . n A 1 212 ILE 212 231 231 ILE ILE A . n A 1 213 PHE 213 232 232 PHE PHE A . n A 1 214 ASP 214 233 233 ASP ASP A . n A 1 215 ILE 215 234 234 ILE ILE A . n A 1 216 GLU 216 235 235 GLU GLU A . n A 1 217 ASP 217 236 236 ASP ASP A . n A 1 218 HIS 218 237 237 HIS HIS A . n A 1 219 PRO 219 238 238 PRO PRO A . n A 1 220 GLU 220 239 239 GLU GLU A . n A 1 221 VAL 221 240 240 VAL VAL A . n A 1 222 PRO 222 241 241 PRO PRO A . n A 1 223 CYS 223 242 242 CYS CYS A . n A 1 224 PRO 224 243 243 PRO PRO A . n A 1 225 TYR 225 244 244 TYR TYR A . n A 1 226 ASP 226 245 245 ASP ASP A . n A 1 227 TYR 227 246 246 TYR TYR A . n A 1 228 ILE 228 247 247 ILE ILE A . n A 1 229 LYS 229 248 248 LYS LYS A . n A 1 230 ILE 230 249 249 ILE ILE A . n A 1 231 LYS 231 250 250 LYS LYS A . n A 1 232 VAL 232 251 251 VAL VAL A . n A 1 233 GLY 233 252 252 GLY GLY A . n A 1 234 PRO 234 253 253 PRO PRO A . n A 1 235 LYS 235 254 254 LYS LYS A . n A 1 236 VAL 236 255 255 VAL VAL A . n A 1 237 LEU 237 256 256 LEU LEU A . n A 1 238 GLY 238 257 257 GLY GLY A . n A 1 239 PRO 239 258 258 PRO PRO A . n A 1 240 PHE 240 259 259 PHE PHE A . n A 1 241 CYS 241 260 260 CYS CYS A . n A 1 242 GLY 242 261 261 GLY GLY A . n A 1 243 GLU 243 262 262 GLU GLU A . n A 1 244 LYS 244 263 263 LYS LYS A . n A 1 245 ALA 245 264 264 ALA ALA A . n A 1 246 PRO 246 265 265 PRO PRO A . n A 1 247 GLU 247 266 266 GLU GLU A . n A 1 248 PRO 248 267 267 PRO PRO A . n A 1 249 ILE 249 268 268 ILE ILE A . n A 1 250 SER 250 269 269 SER SER A . n A 1 251 THR 251 270 270 THR THR A . n A 1 252 GLN 252 271 271 GLN GLN A . n A 1 253 SER 253 272 272 SER SER A . n A 1 254 HIS 254 273 273 HIS HIS A . n A 1 255 SER 255 274 274 SER SER A . n A 1 256 VAL 256 275 275 VAL VAL A . n A 1 257 LEU 257 276 276 LEU LEU A . n A 1 258 ILE 258 277 277 ILE ILE A . n A 1 259 LEU 259 278 278 LEU LEU A . n A 1 260 PHE 260 279 279 PHE PHE A . n A 1 261 HIS 261 280 280 HIS HIS A . n A 1 262 SER 262 281 281 SER SER A . n A 1 263 ASP 263 282 282 ASP ASP A . n A 1 264 ASN 264 283 283 ASN ASN A . n A 1 265 SER 265 284 284 SER SER A . n A 1 266 GLY 266 285 285 GLY GLY A . n A 1 267 GLU 267 286 286 GLU GLU A . n A 1 268 ASN 268 287 287 ASN ASN A . n A 1 269 ARG 269 288 288 ARG ARG A . n A 1 270 GLY 270 289 289 GLY GLY A . n A 1 271 TRP 271 290 290 TRP TRP A . n A 1 272 ARG 272 291 291 ARG ARG A . n A 1 273 LEU 273 292 292 LEU LEU A . n A 1 274 SER 274 293 293 SER SER A . n A 1 275 TYR 275 294 294 TYR TYR A . n A 1 276 ARG 276 295 295 ARG ARG A . n A 1 277 ALA 277 296 296 ALA ALA A . n A 1 278 ALA 278 297 297 ALA ALA A . n A 1 279 GLY 279 298 298 GLY GLY A . n A 1 280 ASN 280 299 299 ASN ASN A . n A 1 281 GLU 281 300 300 GLU GLU A . n A 1 282 CYS 282 301 301 CYS CYS A . n A 1 283 PRO 283 302 302 PRO PRO A . n A 1 284 GLU 284 303 303 GLU GLU A . n A 1 285 LEU 285 304 304 LEU LEU A . n A 1 286 GLN 286 305 305 GLN GLN A . n A 1 287 PRO 287 306 306 PRO PRO A . n A 1 288 PRO 288 307 307 PRO PRO A . n A 1 289 VAL 289 308 308 VAL VAL A . n A 1 290 HIS 290 309 309 HIS HIS A . n A 1 291 GLY 291 310 310 GLY GLY A . n A 1 292 LYS 292 311 311 LYS LYS A . n A 1 293 ILE 293 312 312 ILE ILE A . n A 1 294 GLU 294 313 313 GLU GLU A . n A 1 295 PRO 295 314 314 PRO PRO A . n A 1 296 SER 296 315 315 SER SER A . n A 1 297 GLN 297 316 316 GLN GLN A . n A 1 298 ALA 298 317 317 ALA ALA A . n A 1 299 LYS 299 318 318 LYS LYS A . n A 1 300 TYR 300 319 319 TYR TYR A . n A 1 301 PHE 301 320 320 PHE PHE A . n A 1 302 PHE 302 321 321 PHE PHE A . n A 1 303 LYS 303 322 322 LYS LYS A . n A 1 304 ASP 304 323 323 ASP ASP A . n A 1 305 GLN 305 324 324 GLN GLN A . n A 1 306 VAL 306 325 325 VAL VAL A . n A 1 307 LEU 307 326 326 LEU LEU A . n A 1 308 VAL 308 327 327 VAL VAL A . n A 1 309 SER 309 328 328 SER SER A . n A 1 310 CYS 310 329 329 CYS CYS A . n A 1 311 ASP 311 330 330 ASP ASP A . n A 1 312 THR 312 331 331 THR THR A . n A 1 313 GLY 313 332 332 GLY GLY A . n A 1 314 TYR 314 333 333 TYR TYR A . n A 1 315 LYS 315 334 334 LYS LYS A . n A 1 316 VAL 316 335 335 VAL VAL A . n A 1 317 LEU 317 336 336 LEU LEU A . n A 1 318 LYS 318 337 337 LYS LYS A . n A 1 319 ASP 319 338 338 ASP ASP A . n A 1 320 ASN 320 339 339 ASN ASN A . n A 1 321 VAL 321 340 340 VAL VAL A . n A 1 322 GLU 322 341 341 GLU GLU A . n A 1 323 MET 323 342 342 MET MET A . n A 1 324 ASP 324 343 343 ASP ASP A . n A 1 325 THR 325 344 344 THR THR A . n A 1 326 PHE 326 345 345 PHE PHE A . n A 1 327 GLN 327 346 346 GLN GLN A . n A 1 328 ILE 328 347 347 ILE ILE A . n A 1 329 GLU 329 348 348 GLU GLU A . n A 1 330 CYS 330 349 349 CYS CYS A . n A 1 331 LEU 331 350 350 LEU LEU A . n A 1 332 LYS 332 351 351 LYS LYS A . n A 1 333 ASP 333 352 352 ASP ASP A . n A 1 334 GLY 334 353 353 GLY GLY A . n A 1 335 THR 335 354 354 THR THR A . n A 1 336 TRP 336 355 355 TRP TRP A . n A 1 337 SER 337 356 356 SER SER A . n A 1 338 ASN 338 357 357 ASN ASN A . n A 1 339 LYS 339 358 358 LYS LYS A . n A 1 340 ILE 340 359 359 ILE ILE A . n A 1 341 PRO 341 360 360 PRO PRO A . n A 1 342 THR 342 361 361 THR THR A . n A 1 343 CYS 343 362 362 CYS CYS A . n A 1 344 LYS 344 363 363 LYS LYS A . n A 1 345 LYS 345 364 364 LYS LYS A . n A 1 346 ASN 346 365 365 ASN ASN A . n A 1 347 GLU 347 366 366 GLU GLU A . n A 1 348 ILE 348 367 ? ? ? A . n A 1 349 ASP 349 368 ? ? ? A . n A 1 350 LEU 350 369 ? ? ? A . n A 1 351 GLU 351 370 ? ? ? A . n A 1 352 SER 352 371 ? ? ? A . n A 1 353 GLU 353 372 ? ? ? A . n A 1 354 LEU 354 373 ? ? ? A . n A 1 355 LYS 355 374 ? ? ? A . n A 1 356 SER 356 375 ? ? ? A . n A 1 357 GLU 357 376 ? ? ? A . n A 1 358 GLN 358 377 ? ? ? A . n A 1 359 VAL 359 378 ? ? ? A . n A 1 360 THR 360 379 ? ? ? A . n A 1 361 GLU 361 380 ? ? ? 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 1 649 649 NAG NAG A . C 2 NAG 2 650 650 NAG NAG A . D 3 BMA 3 651 651 BMA BMA A . E 4 MAN 4 652 652 MAN MAN A . F 4 MAN 5 653 653 MAN MAN A . G 2 NAG 1 678 678 NAG NAG A . H 2 NAG 2 679 679 NAG NAG A . I 3 BMA 3 680 680 BMA BMA A . J 4 MAN 4 681 681 MAN MAN A . K 5 CA 1 701 701 CA CA A . L 5 CA 1 702 702 CA CA A . M 5 CA 1 703 703 CA CA A . N 5 CA 1 706 706 CA CA A . O 5 CA 1 707 707 CA CA A . P 5 CA 1 708 708 CA CA A . Q 6 HOH 1 2001 2001 HOH HOH A . Q 6 HOH 2 2002 2002 HOH HOH A . Q 6 HOH 3 2003 2003 HOH HOH A . Q 6 HOH 4 2004 2004 HOH HOH A . Q 6 HOH 5 2005 2005 HOH HOH A . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 30 A ASN 49 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 159 A ASN 178 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details dimeric _pdbx_struct_assembly.oligomeric_count 2 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1,2 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 5620 ? 1 MORE -43.4 ? 1 'SSA (A^2)' 40610 ? # loop_ _pdbx_struct_oper_list.id _pdbx_struct_oper_list.type _pdbx_struct_oper_list.name _pdbx_struct_oper_list.symmetry_operation _pdbx_struct_oper_list.matrix[1][1] _pdbx_struct_oper_list.matrix[1][2] _pdbx_struct_oper_list.matrix[1][3] _pdbx_struct_oper_list.vector[1] _pdbx_struct_oper_list.matrix[2][1] _pdbx_struct_oper_list.matrix[2][2] _pdbx_struct_oper_list.matrix[2][3] _pdbx_struct_oper_list.vector[2] _pdbx_struct_oper_list.matrix[3][1] _pdbx_struct_oper_list.matrix[3][2] _pdbx_struct_oper_list.matrix[3][3] _pdbx_struct_oper_list.vector[3] 1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 2 'crystal symmetry operation' 5_555 -x,y,-z -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 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 ? A VAL 121 ? A VAL 140 ? 1_555 CA ? K CA . ? A CA 701 ? 1_555 O ? Q HOH . ? A HOH 2001 ? 1_555 53.1 ? 2 O ? A VAL 121 ? A VAL 140 ? 1_555 CA ? K CA . ? A CA 701 ? 1_555 OE1 ? A GLU 123 ? A GLU 142 ? 1_555 70.2 ? 3 O ? Q HOH . ? A HOH 2001 ? 1_555 CA ? K CA . ? A CA 701 ? 1_555 OE1 ? A GLU 123 ? A GLU 142 ? 1_555 67.0 ? 4 O ? A VAL 121 ? A VAL 140 ? 1_555 CA ? K CA . ? A CA 701 ? 1_555 OD1 ? A ASN 140 ? A ASN 159 ? 1_555 87.0 ? 5 O ? Q HOH . ? A HOH 2001 ? 1_555 CA ? K CA . ? A CA 701 ? 1_555 OD1 ? A ASN 140 ? A ASN 159 ? 1_555 132.5 ? 6 OE1 ? A GLU 123 ? A GLU 142 ? 1_555 CA ? K CA . ? A CA 701 ? 1_555 OD1 ? A ASN 140 ? A ASN 159 ? 1_555 76.5 ? 7 O ? A VAL 121 ? A VAL 140 ? 1_555 CA ? K CA . ? A CA 701 ? 1_555 O ? A TYR 141 ? A TYR 160 ? 1_555 148.1 ? 8 O ? Q HOH . ? A HOH 2001 ? 1_555 CA ? K CA . ? A CA 701 ? 1_555 O ? A TYR 141 ? A TYR 160 ? 1_555 127.2 ? 9 OE1 ? A GLU 123 ? A GLU 142 ? 1_555 CA ? K CA . ? A CA 701 ? 1_555 O ? A TYR 141 ? A TYR 160 ? 1_555 141.7 ? 10 OD1 ? A ASN 140 ? A ASN 159 ? 1_555 CA ? K CA . ? A CA 701 ? 1_555 O ? A TYR 141 ? A TYR 160 ? 1_555 100.3 ? 11 O ? A VAL 121 ? A VAL 140 ? 1_555 CA ? K CA . ? A CA 701 ? 1_555 O ? A GLY 144 ? A GLY 163 ? 1_555 142.7 ? 12 O ? Q HOH . ? A HOH 2001 ? 1_555 CA ? K CA . ? A CA 701 ? 1_555 O ? A GLY 144 ? A GLY 163 ? 1_555 108.0 ? 13 OE1 ? A GLU 123 ? A GLU 142 ? 1_555 CA ? K CA . ? A CA 701 ? 1_555 O ? A GLY 144 ? A GLY 163 ? 1_555 72.8 ? 14 OD1 ? A ASN 140 ? A ASN 159 ? 1_555 CA ? K CA . ? A CA 701 ? 1_555 O ? A GLY 144 ? A GLY 163 ? 1_555 88.0 ? 15 O ? A TYR 141 ? A TYR 160 ? 1_555 CA ? K CA . ? A CA 701 ? 1_555 O ? A GLY 144 ? A GLY 163 ? 1_555 69.0 ? 16 O ? A VAL 121 ? A VAL 140 ? 1_555 CA ? K CA . ? A CA 701 ? 1_555 OD1 ? A ASP 120 ? A ASP 139 ? 1_555 79.1 ? 17 O ? Q HOH . ? A HOH 2001 ? 1_555 CA ? K CA . ? A CA 701 ? 1_555 OD1 ? A ASP 120 ? A ASP 139 ? 1_555 65.1 ? 18 OE1 ? A GLU 123 ? A GLU 142 ? 1_555 CA ? K CA . ? A CA 701 ? 1_555 OD1 ? A ASP 120 ? A ASP 139 ? 1_555 131.9 ? 19 OD1 ? A ASN 140 ? A ASN 159 ? 1_555 CA ? K CA . ? A CA 701 ? 1_555 OD1 ? A ASP 120 ? A ASP 139 ? 1_555 138.6 ? 20 O ? A TYR 141 ? A TYR 160 ? 1_555 CA ? K CA . ? A CA 701 ? 1_555 OD1 ? A ASP 120 ? A ASP 139 ? 1_555 75.0 ? 21 O ? A GLY 144 ? A GLY 163 ? 1_555 CA ? K CA . ? A CA 701 ? 1_555 OD1 ? A ASP 120 ? A ASP 139 ? 1_555 125.6 ? 22 O ? A VAL 121 ? A VAL 140 ? 1_555 CA ? K CA . ? A CA 701 ? 1_555 OD2 ? A ASP 120 ? A ASP 139 ? 1_555 73.2 ? 23 O ? Q HOH . ? A HOH 2001 ? 1_555 CA ? K CA . ? A CA 701 ? 1_555 OD2 ? A ASP 120 ? A ASP 139 ? 1_555 98.6 ? 24 OE1 ? A GLU 123 ? A GLU 142 ? 1_555 CA ? K CA . ? A CA 701 ? 1_555 OD2 ? A ASP 120 ? A ASP 139 ? 1_555 141.9 ? 25 OD1 ? A ASN 140 ? A ASN 159 ? 1_555 CA ? K CA . ? A CA 701 ? 1_555 OD2 ? A ASP 120 ? A ASP 139 ? 1_555 91.7 ? 26 O ? A TYR 141 ? A TYR 160 ? 1_555 CA ? K CA . ? A CA 701 ? 1_555 OD2 ? A ASP 120 ? A ASP 139 ? 1_555 75.6 ? 27 O ? A GLY 144 ? A GLY 163 ? 1_555 CA ? K CA . ? A CA 701 ? 1_555 OD2 ? A ASP 120 ? A ASP 139 ? 1_555 143.9 ? 28 OD1 ? A ASP 120 ? A ASP 139 ? 1_555 CA ? K CA . ? A CA 701 ? 1_555 OD2 ? A ASP 120 ? A ASP 139 ? 1_555 47.0 ? 29 OD1 ? A ASP 57 ? A ASP 76 ? 1_555 CA ? L CA . ? A CA 702 ? 1_555 OD2 ? A ASP 57 ? A ASP 76 ? 1_555 49.1 ? 30 OD1 ? A ASP 57 ? A ASP 76 ? 1_555 CA ? L CA . ? A CA 702 ? 1_555 OD1 ? A ASP 102 ? A ASP 121 ? 1_555 66.5 ? 31 OD2 ? A ASP 57 ? A ASP 76 ? 1_555 CA ? L CA . ? A CA 702 ? 1_555 OD1 ? A ASP 102 ? A ASP 121 ? 1_555 111.9 ? 32 OD1 ? A ASP 57 ? A ASP 76 ? 1_555 CA ? L CA . ? A CA 702 ? 1_555 O ? Q HOH . ? A HOH 2003 ? 1_555 78.5 ? 33 OD2 ? A ASP 57 ? A ASP 76 ? 1_555 CA ? L CA . ? A CA 702 ? 1_555 O ? Q HOH . ? A HOH 2003 ? 1_555 69.6 ? 34 OD1 ? A ASP 102 ? A ASP 121 ? 1_555 CA ? L CA . ? A CA 702 ? 1_555 O ? Q HOH . ? A HOH 2003 ? 1_555 79.5 ? 35 OD1 ? A ASP 57 ? A ASP 76 ? 1_555 CA ? L CA . ? A CA 702 ? 1_555 OE1 ? A GLU 49 ? A GLU 68 ? 1_555 88.0 ? 36 OD2 ? A ASP 57 ? A ASP 76 ? 1_555 CA ? L CA . ? A CA 702 ? 1_555 OE1 ? A GLU 49 ? A GLU 68 ? 1_555 93.2 ? 37 OD1 ? A ASP 102 ? A ASP 121 ? 1_555 CA ? L CA . ? A CA 702 ? 1_555 OE1 ? A GLU 49 ? A GLU 68 ? 1_555 105.5 ? 38 O ? Q HOH . ? A HOH 2003 ? 1_555 CA ? L CA . ? A CA 702 ? 1_555 OE1 ? A GLU 49 ? A GLU 68 ? 1_555 162.5 ? 39 OD1 ? A ASP 57 ? A ASP 76 ? 1_555 CA ? L CA . ? A CA 702 ? 1_555 OE2 ? A GLU 49 ? A GLU 68 ? 1_555 137.1 ? 40 OD2 ? A ASP 57 ? A ASP 76 ? 1_555 CA ? L CA . ? A CA 702 ? 1_555 OE2 ? A GLU 49 ? A GLU 68 ? 1_555 114.4 ? 41 OD1 ? A ASP 102 ? A ASP 121 ? 1_555 CA ? L CA . ? A CA 702 ? 1_555 OE2 ? A GLU 49 ? A GLU 68 ? 1_555 128.0 ? 42 O ? Q HOH . ? A HOH 2003 ? 1_555 CA ? L CA . ? A CA 702 ? 1_555 OE2 ? A GLU 49 ? A GLU 68 ? 1_555 138.8 ? 43 OE1 ? A GLU 49 ? A GLU 68 ? 1_555 CA ? L CA . ? A CA 702 ? 1_555 OE2 ? A GLU 49 ? A GLU 68 ? 1_555 50.4 ? 44 OD1 ? A ASP 57 ? A ASP 76 ? 1_555 CA ? L CA . ? A CA 702 ? 1_555 O ? Q HOH . ? A HOH 2002 ? 1_555 133.9 ? 45 OD2 ? A ASP 57 ? A ASP 76 ? 1_555 CA ? L CA . ? A CA 702 ? 1_555 O ? Q HOH . ? A HOH 2002 ? 1_555 85.3 ? 46 OD1 ? A ASP 102 ? A ASP 121 ? 1_555 CA ? L CA . ? A CA 702 ? 1_555 O ? Q HOH . ? A HOH 2002 ? 1_555 145.6 ? 47 O ? Q HOH . ? A HOH 2003 ? 1_555 CA ? L CA . ? A CA 702 ? 1_555 O ? Q HOH . ? A HOH 2002 ? 1_555 79.3 ? 48 OE1 ? A GLU 49 ? A GLU 68 ? 1_555 CA ? L CA . ? A CA 702 ? 1_555 O ? Q HOH . ? A HOH 2002 ? 1_555 102.9 ? 49 OE2 ? A GLU 49 ? A GLU 68 ? 1_555 CA ? L CA . ? A CA 702 ? 1_555 O ? Q HOH . ? A HOH 2002 ? 1_555 61.1 ? 50 OD1 ? A ASP 57 ? A ASP 76 ? 1_555 CA ? L CA . ? A CA 702 ? 1_555 O ? A SER 104 ? A SER 123 ? 1_555 145.2 ? 51 OD2 ? A ASP 57 ? A ASP 76 ? 1_555 CA ? L CA . ? A CA 702 ? 1_555 O ? A SER 104 ? A SER 123 ? 1_555 135.5 ? 52 OD1 ? A ASP 102 ? A ASP 121 ? 1_555 CA ? L CA . ? A CA 702 ? 1_555 O ? A SER 104 ? A SER 123 ? 1_555 86.6 ? 53 O ? Q HOH . ? A HOH 2003 ? 1_555 CA ? L CA . ? A CA 702 ? 1_555 O ? A SER 104 ? A SER 123 ? 1_555 75.1 ? 54 OE1 ? A GLU 49 ? A GLU 68 ? 1_555 CA ? L CA . ? A CA 702 ? 1_555 O ? A SER 104 ? A SER 123 ? 1_555 121.6 ? 55 OE2 ? A GLU 49 ? A GLU 68 ? 1_555 CA ? L CA . ? A CA 702 ? 1_555 O ? A SER 104 ? A SER 123 ? 1_555 76.8 ? 56 O ? Q HOH . ? A HOH 2002 ? 1_555 CA ? L CA . ? A CA 702 ? 1_555 O ? A SER 104 ? A SER 123 ? 1_555 61.9 ? 57 O ? Q HOH . ? A HOH 2005 ? 1_555 CA ? M CA . ? A CA 703 ? 1_555 OD1 ? A ASP 226 ? A ASP 245 ? 1_555 75.5 ? 58 O ? Q HOH . ? A HOH 2005 ? 1_555 CA ? M CA . ? A CA 703 ? 1_555 O ? Q HOH . ? A HOH 2004 ? 1_555 70.6 ? 59 OD1 ? A ASP 226 ? A ASP 245 ? 1_555 CA ? M CA . ? A CA 703 ? 1_555 O ? Q HOH . ? A HOH 2004 ? 1_555 101.5 ? 60 O ? Q HOH . ? A HOH 2005 ? 1_555 CA ? M CA . ? A CA 703 ? 1_555 OD2 ? A ASP 226 ? A ASP 245 ? 1_555 88.5 ? 61 OD1 ? A ASP 226 ? A ASP 245 ? 1_555 CA ? M CA . ? A CA 703 ? 1_555 OD2 ? A ASP 226 ? A ASP 245 ? 1_555 52.6 ? 62 O ? Q HOH . ? A HOH 2004 ? 1_555 CA ? M CA . ? A CA 703 ? 1_555 OD2 ? A ASP 226 ? A ASP 245 ? 1_555 57.9 ? 63 O ? Q HOH . ? A HOH 2005 ? 1_555 CA ? M CA . ? A CA 703 ? 1_555 OD1 ? A ASP 263 ? A ASP 282 ? 1_555 65.7 ? 64 OD1 ? A ASP 226 ? A ASP 245 ? 1_555 CA ? M CA . ? A CA 703 ? 1_555 OD1 ? A ASP 263 ? A ASP 282 ? 1_555 92.3 ? 65 O ? Q HOH . ? A HOH 2004 ? 1_555 CA ? M CA . ? A CA 703 ? 1_555 OD1 ? A ASP 263 ? A ASP 282 ? 1_555 128.8 ? 66 OD2 ? A ASP 226 ? A ASP 245 ? 1_555 CA ? M CA . ? A CA 703 ? 1_555 OD1 ? A ASP 263 ? A ASP 282 ? 1_555 141.8 ? 67 O ? Q HOH . ? A HOH 2005 ? 1_555 CA ? M CA . ? A CA 703 ? 1_555 OE1 ? A GLU 216 ? A GLU 235 ? 1_555 153.8 ? 68 OD1 ? A ASP 226 ? A ASP 245 ? 1_555 CA ? M CA . ? A CA 703 ? 1_555 OE1 ? A GLU 216 ? A GLU 235 ? 1_555 126.2 ? 69 O ? Q HOH . ? A HOH 2004 ? 1_555 CA ? M CA . ? A CA 703 ? 1_555 OE1 ? A GLU 216 ? A GLU 235 ? 1_555 89.0 ? 70 OD2 ? A ASP 226 ? A ASP 245 ? 1_555 CA ? M CA . ? A CA 703 ? 1_555 OE1 ? A GLU 216 ? A GLU 235 ? 1_555 94.5 ? 71 OD1 ? A ASP 263 ? A ASP 282 ? 1_555 CA ? M CA . ? A CA 703 ? 1_555 OE1 ? A GLU 216 ? A GLU 235 ? 1_555 121.2 ? 72 O ? Q HOH . ? A HOH 2005 ? 1_555 CA ? M CA . ? A CA 703 ? 1_555 O ? A SER 265 ? A SER 284 ? 1_555 71.5 ? 73 OD1 ? A ASP 226 ? A ASP 245 ? 1_555 CA ? M CA . ? A CA 703 ? 1_555 O ? A SER 265 ? A SER 284 ? 1_555 146.9 ? 74 O ? Q HOH . ? A HOH 2004 ? 1_555 CA ? M CA . ? A CA 703 ? 1_555 O ? A SER 265 ? A SER 284 ? 1_555 65.0 ? 75 OD2 ? A ASP 226 ? A ASP 245 ? 1_555 CA ? M CA . ? A CA 703 ? 1_555 O ? A SER 265 ? A SER 284 ? 1_555 123.0 ? 76 OD1 ? A ASP 263 ? A ASP 282 ? 1_555 CA ? M CA . ? A CA 703 ? 1_555 O ? A SER 265 ? A SER 284 ? 1_555 76.7 ? 77 OE1 ? A GLU 216 ? A GLU 235 ? 1_555 CA ? M CA . ? A CA 703 ? 1_555 O ? A SER 265 ? A SER 284 ? 1_555 85.2 ? # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2012-08-08 2 'Structure model' 1 1 2012-10-03 # _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 ? # _pdbx_audit_revision_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Database references' # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][3] 'X-RAY DIFFRACTION' 1 ? refined -22.1981 1.8495 9.9228 -0.2853 0.2851 -0.2055 -0.1520 0.0375 -0.1520 5.6274 6.9268 7.7296 -1.4636 -2.0046 1.5688 0.0749 -0.5350 -0.0560 -0.3367 -0.3183 0.5442 -0.0866 -0.5320 0.2435 'X-RAY DIFFRACTION' 2 ? refined 14.6116 1.0105 11.8990 -0.0444 0.3040 0.0605 -0.0984 -0.0604 0.1520 2.6314 0.0000 3.2180 0.0548 2.9104 -1.3430 0.0587 0.1971 0.3789 0.5442 -0.0249 -0.2950 -0.2757 -0.1090 -0.0338 'X-RAY DIFFRACTION' 3 ? refined 38.3816 5.3099 28.6848 0.2393 -0.0246 -0.2653 -0.1520 -0.1520 0.0961 8.3154 6.1439 2.1775 0.9554 1.5638 -2.9065 0.0052 0.0443 0.5442 -0.0050 0.0005 -0.0840 0.1500 -0.1388 -0.0057 'X-RAY DIFFRACTION' 4 ? refined 78.8382 10.5071 30.5146 0.2897 0.2460 -0.3039 -0.1488 -0.1520 -0.1476 3.6872 3.4684 0.5500 0.9470 1.4068 -0.4727 -0.0354 0.0541 -0.1982 -0.3990 0.1817 0.2231 0.1100 -0.0433 -0.1463 # loop_ _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection _pdbx_refine_tls_group.selection_details 'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESID 22-138, 702 AND 649-653)' 'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESID 139-183, 678-681, 701)' 'X-RAY DIFFRACTION' 3 3 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESID 184-298, 703)' 'X-RAY DIFFRACTION' 4 4 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESID 299-366)' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal _software.date _software.type _software.location _software.language BUSTER refinement 2.11.2 ? 1 ? ? ? ? XDS 'data reduction' . ? 2 ? ? ? ? XSCALE 'data scaling' . ? 3 ? ? ? ? PHASER phasing . ? 4 ? ? ? ? # _pdbx_entry_details.entry_id 4AQB _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ? _pdbx_entry_details.sequence_details ;NO SIGNAL PEPTIDE RESIDUES 1-19 ISOFORM 3 OF MASP-1, AKA MAP-1, AKA MAP44 ; # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 OD1 A ASN 26 ? ? O A PHE 28 ? ? 1.99 2 1 NH2 A ARG 146 ? ? SG A CYS 157 ? ? 2.11 3 1 O A VAL 140 ? ? O A HOH 2001 ? ? 2.12 4 1 NH1 A ARG 146 ? ? SG A CYS 157 ? ? 2.18 # _pdbx_validate_rmsd_angle.id 1 _pdbx_validate_rmsd_angle.PDB_model_num 1 _pdbx_validate_rmsd_angle.auth_atom_id_1 C _pdbx_validate_rmsd_angle.auth_asym_id_1 A _pdbx_validate_rmsd_angle.auth_comp_id_1 GLU _pdbx_validate_rmsd_angle.auth_seq_id_1 150 _pdbx_validate_rmsd_angle.PDB_ins_code_1 ? _pdbx_validate_rmsd_angle.label_alt_id_1 ? _pdbx_validate_rmsd_angle.auth_atom_id_2 N _pdbx_validate_rmsd_angle.auth_asym_id_2 A _pdbx_validate_rmsd_angle.auth_comp_id_2 LEU _pdbx_validate_rmsd_angle.auth_seq_id_2 151 _pdbx_validate_rmsd_angle.PDB_ins_code_2 ? _pdbx_validate_rmsd_angle.label_alt_id_2 ? _pdbx_validate_rmsd_angle.auth_atom_id_3 CA _pdbx_validate_rmsd_angle.auth_asym_id_3 A _pdbx_validate_rmsd_angle.auth_comp_id_3 LEU _pdbx_validate_rmsd_angle.auth_seq_id_3 151 _pdbx_validate_rmsd_angle.PDB_ins_code_3 ? _pdbx_validate_rmsd_angle.label_alt_id_3 ? _pdbx_validate_rmsd_angle.angle_value 142.73 _pdbx_validate_rmsd_angle.angle_target_value 121.70 _pdbx_validate_rmsd_angle.angle_deviation 21.03 _pdbx_validate_rmsd_angle.angle_standard_deviation 2.50 _pdbx_validate_rmsd_angle.linker_flag Y # 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 ASN A 26 ? ? -174.99 -166.70 2 1 TYR A 75 ? ? -84.58 -85.56 3 1 THR A 82 ? ? -108.09 -167.69 4 1 THR A 98 ? ? 73.22 49.42 5 1 ASP A 121 ? ? -77.17 -167.12 6 1 ASN A 124 ? ? -117.52 55.64 7 1 GLU A 149 ? ? -106.39 -123.87 8 1 GLU A 150 ? ? -123.74 -94.71 9 1 LEU A 151 ? ? 76.87 33.76 10 1 HIS A 155 ? ? -109.45 -85.55 11 1 ARG A 179 ? ? -136.17 -52.15 12 1 LEU A 189 ? ? -166.55 110.45 13 1 ASP A 230 ? ? 59.56 -147.73 14 1 CYS A 242 ? ? 35.10 68.31 15 1 TYR A 244 ? ? -107.74 -71.84 16 1 PRO A 253 ? ? -93.37 31.38 17 1 ASP A 338 ? ? 56.61 -111.63 # _pdbx_validate_peptide_omega.id 1 _pdbx_validate_peptide_omega.PDB_model_num 1 _pdbx_validate_peptide_omega.auth_comp_id_1 GLU _pdbx_validate_peptide_omega.auth_asym_id_1 A _pdbx_validate_peptide_omega.auth_seq_id_1 150 _pdbx_validate_peptide_omega.PDB_ins_code_1 ? _pdbx_validate_peptide_omega.label_alt_id_1 ? _pdbx_validate_peptide_omega.auth_comp_id_2 LEU _pdbx_validate_peptide_omega.auth_asym_id_2 A _pdbx_validate_peptide_omega.auth_seq_id_2 151 _pdbx_validate_peptide_omega.PDB_ins_code_2 ? _pdbx_validate_peptide_omega.label_alt_id_2 ? _pdbx_validate_peptide_omega.omega 31.67 # loop_ _pdbx_validate_chiral.id _pdbx_validate_chiral.PDB_model_num _pdbx_validate_chiral.auth_atom_id _pdbx_validate_chiral.label_alt_id _pdbx_validate_chiral.auth_asym_id _pdbx_validate_chiral.auth_comp_id _pdbx_validate_chiral.auth_seq_id _pdbx_validate_chiral.PDB_ins_code _pdbx_validate_chiral.details _pdbx_validate_chiral.omega 1 1 C1 ? A NAG 650 ? 'WRONG HAND' . 2 1 C1 ? A NAG 679 ? 'WRONG HAND' . # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 Y 1 A GLU 303 ? OE1 ? A GLU 284 OE1 2 1 Y 1 A GLU 303 ? OE2 ? A GLU 284 OE2 3 1 Y 1 A LYS 358 ? CD ? A LYS 339 CD 4 1 Y 1 A LYS 358 ? CE ? A LYS 339 CE 5 1 Y 1 A LYS 358 ? NZ ? A LYS 339 NZ # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A HIS 20 ? A HIS 1 2 1 Y 1 A THR 21 ? A THR 2 3 1 Y 1 A ILE 367 ? A ILE 348 4 1 Y 1 A ASP 368 ? A ASP 349 5 1 Y 1 A LEU 369 ? A LEU 350 6 1 Y 1 A GLU 370 ? A GLU 351 7 1 Y 1 A SER 371 ? A SER 352 8 1 Y 1 A GLU 372 ? A GLU 353 9 1 Y 1 A LEU 373 ? A LEU 354 10 1 Y 1 A LYS 374 ? A LYS 355 11 1 Y 1 A SER 375 ? A SER 356 12 1 Y 1 A GLU 376 ? A GLU 357 13 1 Y 1 A GLN 377 ? A GLN 358 14 1 Y 1 A VAL 378 ? A VAL 359 15 1 Y 1 A THR 379 ? A THR 360 16 1 Y 1 A GLU 380 ? A GLU 361 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 BETA-D-MANNOSE BMA 4 ALPHA-D-MANNOSE MAN 5 'CALCIUM ION' CA 6 water HOH #