data_1OM0 # _entry.id 1OM0 # _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 1OM0 RCSB RCSB018433 WWPDB D_1000018433 # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 1OM0 _pdbx_database_status.recvd_initial_deposition_date 2003-02-24 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site PDBJ _pdbx_database_status.status_code_sf REL _pdbx_database_status.SG_entry . _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_cs ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Payan, F.' 1 'Flatman, R.' 2 'Porciero, S.' 3 'Williamson, G.' 4 'Juge, N.' 5 'Roussel, A.' 6 # _citation.id primary _citation.title ;Structural analysis of xylanase inhibitor protein I (XIP-I), a proteinaceous xylanase inhibitor from wheat (Triticum aestivum, var. Soisson). ; _citation.journal_abbrev Biochem.J. _citation.journal_volume 372 _citation.page_first 399 _citation.page_last 405 _citation.year 2003 _citation.journal_id_ASTM BIJOAK _citation.country UK _citation.journal_id_ISSN 0264-6021 _citation.journal_id_CSD 0043 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 12617724 _citation.pdbx_database_id_DOI 10.1042/BJ20021802 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Payan, F.' 1 primary 'Flatman, R.' 2 primary 'Porciero, S.' 3 primary 'Williamson, G.' 4 primary 'Juge, N.' 5 primary 'Roussel, A.' 6 # _cell.entry_id 1OM0 _cell.length_a 58.475 _cell.length_b 58.475 _cell.length_c 191.954 _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 1OM0 _symmetry.space_group_name_H-M 'P 43 21 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 96 # 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 nat 'Xylanase Inhibitor Protein I' 30323.990 1 ? ? ? ? 2 non-polymer man '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' 221.208 1 ? ? ? ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 1 ? ? ? ? 4 non-polymer syn 1,2-ETHANEDIOL 62.068 9 ? ? ? ? 5 water nat water 18.015 297 ? ? ? ? # _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 ;AGGKTGQVTVFWGRNKAEGSLREACDSGMYTMVTMSFLDVFGANGKYHLDLSGHDLSSVGADIKHCQSKGVPVSLSIGGY GTGYSLPSNRSALDLFDHLWNSYFGGSKPSVPRPFGDAWLDGVDLFLEHGTPADRYDVLALELAKHNIRGGPGKPLHLTA TVRCGYPPAAHVGRALATGIFERVHVRTYESDKWCNQNLGWEGSWDKWTAAYPATRFYVGLTADDKSHQWVHPKNVYYGV APVAQKKDNYGGIMLWDRYFDKQTNYSSLIKYYA ; _entity_poly.pdbx_seq_one_letter_code_can ;AGGKTGQVTVFWGRNKAEGSLREACDSGMYTMVTMSFLDVFGANGKYHLDLSGHDLSSVGADIKHCQSKGVPVSLSIGGY GTGYSLPSNRSALDLFDHLWNSYFGGSKPSVPRPFGDAWLDGVDLFLEHGTPADRYDVLALELAKHNIRGGPGKPLHLTA TVRCGYPPAAHVGRALATGIFERVHVRTYESDKWCNQNLGWEGSWDKWTAAYPATRFYVGLTADDKSHQWVHPKNVYYGV APVAQKKDNYGGIMLWDRYFDKQTNYSSLIKYYA ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ALA n 1 2 GLY n 1 3 GLY n 1 4 LYS n 1 5 THR n 1 6 GLY n 1 7 GLN n 1 8 VAL n 1 9 THR n 1 10 VAL n 1 11 PHE n 1 12 TRP n 1 13 GLY n 1 14 ARG n 1 15 ASN n 1 16 LYS n 1 17 ALA n 1 18 GLU n 1 19 GLY n 1 20 SER n 1 21 LEU n 1 22 ARG n 1 23 GLU n 1 24 ALA n 1 25 CYS n 1 26 ASP n 1 27 SER n 1 28 GLY n 1 29 MET n 1 30 TYR n 1 31 THR n 1 32 MET n 1 33 VAL n 1 34 THR n 1 35 MET n 1 36 SER n 1 37 PHE n 1 38 LEU n 1 39 ASP n 1 40 VAL n 1 41 PHE n 1 42 GLY n 1 43 ALA n 1 44 ASN n 1 45 GLY n 1 46 LYS n 1 47 TYR n 1 48 HIS n 1 49 LEU n 1 50 ASP n 1 51 LEU n 1 52 SER n 1 53 GLY n 1 54 HIS n 1 55 ASP n 1 56 LEU n 1 57 SER n 1 58 SER n 1 59 VAL n 1 60 GLY n 1 61 ALA n 1 62 ASP n 1 63 ILE n 1 64 LYS n 1 65 HIS n 1 66 CYS n 1 67 GLN n 1 68 SER n 1 69 LYS n 1 70 GLY n 1 71 VAL n 1 72 PRO n 1 73 VAL n 1 74 SER n 1 75 LEU n 1 76 SER n 1 77 ILE n 1 78 GLY n 1 79 GLY n 1 80 TYR n 1 81 GLY n 1 82 THR n 1 83 GLY n 1 84 TYR n 1 85 SER n 1 86 LEU n 1 87 PRO n 1 88 SER n 1 89 ASN n 1 90 ARG n 1 91 SER n 1 92 ALA n 1 93 LEU n 1 94 ASP n 1 95 LEU n 1 96 PHE n 1 97 ASP n 1 98 HIS n 1 99 LEU n 1 100 TRP n 1 101 ASN n 1 102 SER n 1 103 TYR n 1 104 PHE n 1 105 GLY n 1 106 GLY n 1 107 SER n 1 108 LYS n 1 109 PRO n 1 110 SER n 1 111 VAL n 1 112 PRO n 1 113 ARG n 1 114 PRO n 1 115 PHE n 1 116 GLY n 1 117 ASP n 1 118 ALA n 1 119 TRP n 1 120 LEU n 1 121 ASP n 1 122 GLY n 1 123 VAL n 1 124 ASP n 1 125 LEU n 1 126 PHE n 1 127 LEU n 1 128 GLU n 1 129 HIS n 1 130 GLY n 1 131 THR n 1 132 PRO n 1 133 ALA n 1 134 ASP n 1 135 ARG n 1 136 TYR n 1 137 ASP n 1 138 VAL n 1 139 LEU n 1 140 ALA n 1 141 LEU n 1 142 GLU n 1 143 LEU n 1 144 ALA n 1 145 LYS n 1 146 HIS n 1 147 ASN n 1 148 ILE n 1 149 ARG n 1 150 GLY n 1 151 GLY n 1 152 PRO n 1 153 GLY n 1 154 LYS n 1 155 PRO n 1 156 LEU n 1 157 HIS n 1 158 LEU n 1 159 THR n 1 160 ALA n 1 161 THR n 1 162 VAL n 1 163 ARG n 1 164 CYS n 1 165 GLY n 1 166 TYR n 1 167 PRO n 1 168 PRO n 1 169 ALA n 1 170 ALA n 1 171 HIS n 1 172 VAL n 1 173 GLY n 1 174 ARG n 1 175 ALA n 1 176 LEU n 1 177 ALA n 1 178 THR n 1 179 GLY n 1 180 ILE n 1 181 PHE n 1 182 GLU n 1 183 ARG n 1 184 VAL n 1 185 HIS n 1 186 VAL n 1 187 ARG n 1 188 THR n 1 189 TYR n 1 190 GLU n 1 191 SER n 1 192 ASP n 1 193 LYS n 1 194 TRP n 1 195 CYS n 1 196 ASN n 1 197 GLN n 1 198 ASN n 1 199 LEU n 1 200 GLY n 1 201 TRP n 1 202 GLU n 1 203 GLY n 1 204 SER n 1 205 TRP n 1 206 ASP n 1 207 LYS n 1 208 TRP n 1 209 THR n 1 210 ALA n 1 211 ALA n 1 212 TYR n 1 213 PRO n 1 214 ALA n 1 215 THR n 1 216 ARG n 1 217 PHE n 1 218 TYR n 1 219 VAL n 1 220 GLY n 1 221 LEU n 1 222 THR n 1 223 ALA n 1 224 ASP n 1 225 ASP n 1 226 LYS n 1 227 SER n 1 228 HIS n 1 229 GLN n 1 230 TRP n 1 231 VAL n 1 232 HIS n 1 233 PRO n 1 234 LYS n 1 235 ASN n 1 236 VAL n 1 237 TYR n 1 238 TYR n 1 239 GLY n 1 240 VAL n 1 241 ALA n 1 242 PRO n 1 243 VAL n 1 244 ALA n 1 245 GLN n 1 246 LYS n 1 247 LYS n 1 248 ASP n 1 249 ASN n 1 250 TYR n 1 251 GLY n 1 252 GLY n 1 253 ILE n 1 254 MET n 1 255 LEU n 1 256 TRP n 1 257 ASP n 1 258 ARG n 1 259 TYR n 1 260 PHE n 1 261 ASP n 1 262 LYS n 1 263 GLN n 1 264 THR n 1 265 ASN n 1 266 TYR n 1 267 SER n 1 268 SER n 1 269 LEU n 1 270 ILE n 1 271 LYS n 1 272 TYR n 1 273 TYR n 1 274 ALA n # _entity_src_nat.entity_id 1 _entity_src_nat.pdbx_src_id 1 _entity_src_nat.pdbx_alt_source_flag sample _entity_src_nat.pdbx_beg_seq_num ? _entity_src_nat.pdbx_end_seq_num ? _entity_src_nat.common_name 'bread wheat' _entity_src_nat.pdbx_organism_scientific 'Triticum aestivum' _entity_src_nat.pdbx_ncbi_taxonomy_id 4565 _entity_src_nat.genus Triticum _entity_src_nat.species ? _entity_src_nat.strain ? _entity_src_nat.tissue ? _entity_src_nat.tissue_fraction ? _entity_src_nat.pdbx_secretion ? _entity_src_nat.pdbx_fragment ? _entity_src_nat.pdbx_variant ? _entity_src_nat.pdbx_cell_line ? _entity_src_nat.pdbx_atcc ? _entity_src_nat.pdbx_cellular_location ? _entity_src_nat.pdbx_organ ? _entity_src_nat.pdbx_organelle ? _entity_src_nat.pdbx_cell ? _entity_src_nat.pdbx_plasmid_name ? _entity_src_nat.pdbx_plasmid_details ? _entity_src_nat.details ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code XIP1_WHEAT _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;AGGKTGQVTVFWGRNKAEGSLREACDSGMYTMVTMSLLDVFGANGKYHLDLSGHDLSSVGADIKHCQSKGVPVSLSIGGY GTGYSLPSNRSALDLFDHLWNSYFGGSKPSVPRPFGDAWLDGVDLFLEHGTPADRYDVLALELAKHNIRGGPGKPLHLTA TVRCGYPPAAHVGRALATGIFERAHVRTYESDKWCNQNLGWEGSWDKWTAAYPATRFYVGLTADDKSHQWVHPKNVYYGV APVAQKKDNYGGIMLWDRYFDKQTNYSSLIKYYA ; _struct_ref.pdbx_align_begin 31 _struct_ref.pdbx_db_accession Q8L5C6 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 1OM0 _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 274 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession Q8L5C6 _struct_ref_seq.db_align_beg 31 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 304 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 1 _struct_ref_seq.pdbx_auth_seq_align_end 274 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 1OM0 PHE A 37 ? UNP Q8L5C6 LEU 67 'SEE REMARK 999' 37 1 1 1OM0 VAL A 184 ? UNP Q8L5C6 ALA 214 'SEE REMARK 999' 184 2 # 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 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 EDO non-polymer . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL' 'C2 H6 O2' 62.068 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 NDG D-saccharide . '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' ? '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 1OM0 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.33 _exptl_crystal.density_percent_sol 46.88 _exptl_crystal.description ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 294 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 8.5 _exptl_crystal_grow.pdbx_details 'PEG 4000, LiCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K' _exptl_crystal_grow.pdbx_pH_range ? # _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 4' _diffrn_detector.pdbx_collection_date 2003-02-01 _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 0.933 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'ESRF BEAMLINE ID14-2' _diffrn_source.pdbx_synchrotron_site ESRF _diffrn_source.pdbx_synchrotron_beamline ID14-2 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 0.933 # _reflns.entry_id 1OM0 _reflns.observed_criterion_sigma_I ? _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 15 _reflns.d_resolution_high 1.8 _reflns.number_obs 31670 _reflns.number_all 31878 _reflns.percent_possible_obs 99.1 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value 0.074 _reflns.pdbx_netI_over_sigmaI 11.2 _reflns.B_iso_Wilson_estimate 19.3 _reflns.pdbx_redundancy 4.7 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 1.8 _reflns_shell.d_res_low 1.83 _reflns_shell.percent_possible_all 99.5 _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value 0.245 _reflns_shell.meanI_over_sigI_obs 2.3 _reflns_shell.pdbx_redundancy 4.6 _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all 1581 _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 1OM0 _refine.ls_number_reflns_obs 31670 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 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 14.99 _refine.ls_d_res_high 1.80 _refine.ls_percent_reflns_obs 99.3 _refine.ls_R_factor_obs 0.197 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.197 _refine.ls_R_factor_R_free 0.225 _refine.ls_R_factor_R_free_error 0.006 _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.0 _refine.ls_number_reflns_R_free 1573 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean 28.2 _refine.aniso_B[1][1] 2.93 _refine.aniso_B[2][2] 2.93 _refine.aniso_B[3][3] -5.86 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details 'FLAT MODEL' _refine.solvent_model_param_ksol 0.392855 _refine.solvent_model_param_bsol 66.2624 _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 ? _refine.pdbx_starting_model 'PDB ENTRY 2HVM' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model RESTRAINED _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.overall_SU_B ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_phase_error ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_analyze.entry_id 1OM0 _refine_analyze.Luzzati_coordinate_error_obs 0.20 _refine_analyze.Luzzati_sigma_a_obs 0.15 _refine_analyze.Luzzati_d_res_low_obs 5.00 _refine_analyze.Luzzati_coordinate_error_free 0.23 _refine_analyze.Luzzati_sigma_a_free 0.15 _refine_analyze.Luzzati_d_res_low_free ? _refine_analyze.number_disordered_residues ? _refine_analyze.occupancy_sum_hydrogen ? _refine_analyze.occupancy_sum_non_hydrogen ? _refine_analyze.pdbx_Luzzati_d_res_high_obs ? _refine_analyze.pdbx_refine_id 'X-RAY DIFFRACTION' # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 2140 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 64 _refine_hist.number_atoms_solvent 297 _refine_hist.number_atoms_total 2501 _refine_hist.d_res_high 1.80 _refine_hist.d_res_low 14.99 # 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 c_bond_d 0.005 ? ? ? 'X-RAY DIFFRACTION' ? c_bond_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? c_bond_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? c_angle_d ? ? ? ? 'X-RAY DIFFRACTION' ? c_angle_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? c_angle_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? c_angle_deg 1.3 ? ? ? 'X-RAY DIFFRACTION' ? c_angle_deg_na ? ? ? ? 'X-RAY DIFFRACTION' ? c_angle_deg_prot ? ? ? ? 'X-RAY DIFFRACTION' ? c_dihedral_angle_d 23.9 ? ? ? 'X-RAY DIFFRACTION' ? c_dihedral_angle_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? c_dihedral_angle_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? c_improper_angle_d 0.68 ? ? ? 'X-RAY DIFFRACTION' ? c_improper_angle_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? c_improper_angle_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? c_mcbond_it 1.33 1.50 ? ? 'X-RAY DIFFRACTION' ? c_mcangle_it 2.12 2.00 ? ? 'X-RAY DIFFRACTION' ? c_scbond_it 2.06 2.00 ? ? 'X-RAY DIFFRACTION' ? c_scangle_it 3.10 2.50 ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_total_number_of_bins_used 6 _refine_ls_shell.d_res_high 1.80 _refine_ls_shell.d_res_low 1.91 _refine_ls_shell.number_reflns_R_work 4915 _refine_ls_shell.R_factor_R_work 0.235 _refine_ls_shell.percent_reflns_obs 100.0 _refine_ls_shell.R_factor_R_free 0.248 _refine_ls_shell.R_factor_R_free_error 0.015 _refine_ls_shell.percent_reflns_R_free 5.2 _refine_ls_shell.number_reflns_R_free 272 _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.number_reflns_all ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.R_factor_all ? # loop_ _pdbx_xplor_file.serial_no _pdbx_xplor_file.param_file _pdbx_xplor_file.topol_file _pdbx_xplor_file.pdbx_refine_id 1 PROTEIN_REP.PARAM PROTEIN.TOP 'X-RAY DIFFRACTION' 2 WATER_REP.PARAM CARBOHYDRATE.TOP 'X-RAY DIFFRACTION' 3 CARBOHYDRATE.PARAM WATER.TOP 'X-RAY DIFFRACTION' 4 CIS_PEPTIDE.PARAM ? 'X-RAY DIFFRACTION' 5 EGL-MX.PARAM EGL-MX.TOP 'X-RAY DIFFRACTION' # _struct.entry_id 1OM0 _struct.title 'crystal structure of xylanase inhibitor protein (XIP-I) from wheat' _struct.pdbx_descriptor 'xylanase inhibitor protein I' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 1OM0 _struct_keywords.pdbx_keywords 'SUGAR BINDING PROTEIN' _struct_keywords.text 'BETA-ALPHA BARREL, SUGAR BINDING PROTEIN' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 4 ? E N N 4 ? F N N 4 ? G N N 4 ? H N N 4 ? I N N 4 ? J N N 4 ? K N N 4 ? L N N 4 ? M N N 5 ? # _struct_biol.id 1 _struct_biol.pdbx_parent_biol_id ? _struct_biol.details ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 ASN A 15 ? GLY A 19 ? ASN A 15 GLY A 19 5 ? 5 HELX_P HELX_P2 2 SER A 20 ? SER A 27 ? SER A 20 SER A 27 1 ? 8 HELX_P HELX_P3 3 ASP A 55 ? SER A 57 ? ASP A 55 SER A 57 5 ? 3 HELX_P HELX_P4 4 SER A 58 ? LYS A 69 ? SER A 58 LYS A 69 1 ? 12 HELX_P HELX_P5 5 SER A 88 ? PHE A 104 ? SER A 88 PHE A 104 1 ? 17 HELX_P HELX_P6 6 ARG A 135 ? HIS A 146 ? ARG A 135 HIS A 146 1 ? 12 HELX_P HELX_P7 7 ALA A 169 ? ALA A 177 ? ALA A 169 ALA A 177 1 ? 9 HELX_P HELX_P8 8 GLY A 200 ? TYR A 212 ? GLY A 200 TYR A 212 1 ? 13 HELX_P HELX_P9 9 HIS A 232 ? GLY A 239 ? HIS A 232 GLY A 239 1 ? 8 HELX_P HELX_P10 10 GLY A 239 ? GLN A 245 ? GLY A 239 GLN A 245 1 ? 7 HELX_P HELX_P11 11 ASP A 257 ? ASN A 265 ? ASP A 257 ASN A 265 1 ? 9 HELX_P HELX_P12 12 TYR A 266 ? LYS A 271 ? TYR A 266 LYS A 271 1 ? 6 # _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 25 SG ? ? ? 1_555 A CYS 66 SG ? ? A CYS 25 A CYS 66 1_555 ? ? ? ? ? ? ? 2.035 ? covale1 covale ? ? B NDG . C1 ? ? ? 1_555 A ASN 265 ND2 ? ? A NDG 900 A ASN 265 1_555 ? ? ? ? ? ? ? 1.449 ? covale2 covale ? ? C NAG . C1 ? ? ? 1_555 A ASN 89 ND2 ? ? A NAG 901 A ASN 89 1_555 ? ? ? ? ? ? ? 1.452 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 SER 36 A . ? SER 36 A PHE 37 A ? PHE 37 A 1 0.34 2 TYR 166 A . ? TYR 166 A PRO 167 A ? PRO 167 A 1 0.20 3 TRP 256 A . ? TRP 256 A ASP 257 A ? ASP 257 A 1 -0.71 # _struct_sheet.id A _struct_sheet.type ? _struct_sheet.number_strands 10 _struct_sheet.details ? # 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 A 1 2 ? anti-parallel A 2 3 ? parallel A 3 4 ? parallel A 4 5 ? parallel A 5 6 ? parallel A 6 7 ? parallel A 7 8 ? parallel A 8 9 ? parallel A 9 10 ? 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 A 1 HIS A 48 ? LEU A 49 ? HIS A 48 LEU A 49 A 2 MET A 32 ? VAL A 40 ? MET A 32 VAL A 40 A 3 VAL A 8 ? TRP A 12 ? VAL A 8 TRP A 12 A 4 TYR A 250 ? TRP A 256 ? TYR A 250 TRP A 256 A 5 ARG A 216 ? THR A 222 ? ARG A 216 THR A 222 A 6 ARG A 183 ? ARG A 187 ? ARG A 183 ARG A 187 A 7 HIS A 157 ? ARG A 163 ? HIS A 157 ARG A 163 A 8 GLY A 122 ? LEU A 127 ? GLY A 122 LEU A 127 A 9 VAL A 73 ? GLY A 79 ? VAL A 73 GLY A 79 A 10 MET A 32 ? VAL A 40 ? MET A 32 VAL A 40 # 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 A 1 2 O HIS A 48 ? O HIS A 48 N ASP A 39 ? N ASP A 39 A 2 3 N MET A 32 ? N MET A 32 O VAL A 8 ? O VAL A 8 A 3 4 N THR A 9 ? N THR A 9 O ILE A 253 ? O ILE A 253 A 4 5 N GLY A 251 ? N GLY A 251 O PHE A 217 ? O PHE A 217 A 5 6 N TYR A 218 ? N TYR A 218 O VAL A 184 ? O VAL A 184 A 6 7 N ARG A 183 ? N ARG A 183 O LEU A 158 ? O LEU A 158 A 7 8 N THR A 159 ? N THR A 159 O VAL A 123 ? O VAL A 123 A 8 9 N GLY A 122 ? N GLY A 122 O VAL A 73 ? O VAL A 73 A 9 10 N SER A 74 ? N SER A 74 O VAL A 33 ? O VAL A 33 # 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 ? ? ? ? 2 'BINDING SITE FOR RESIDUE NDG A 900' AC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 901' AC3 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE EDO A 2000' AC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE EDO A 2001' AC5 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE EDO A 2004' AC6 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE EDO A 2005' AC7 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE EDO A 2007' AC8 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE EDO A 2008' AC9 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE EDO A 2009' BC1 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE EDO A 2010' BC2 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE EDO A 2011' # 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 2 ASN A 265 ? ASN A 265 . ? 1_555 ? 2 AC1 2 HOH M . ? HOH A 802 . ? 1_555 ? 3 AC2 4 ASN A 89 ? ASN A 89 . ? 1_555 ? 4 AC2 4 TYR A 259 ? TYR A 259 . ? 5_545 ? 5 AC2 4 HOH M . ? HOH A 656 . ? 1_555 ? 6 AC2 4 HOH M . ? HOH A 784 . ? 5_545 ? 7 AC3 8 GLY A 83 ? GLY A 83 . ? 1_555 ? 8 AC3 8 PRO A 213 ? PRO A 213 . ? 5_555 ? 9 AC3 8 ALA A 214 ? ALA A 214 . ? 5_555 ? 10 AC3 8 ARG A 216 ? ARG A 216 . ? 5_555 ? 11 AC3 8 ASN A 249 ? ASN A 249 . ? 5_555 ? 12 AC3 8 HOH M . ? HOH A 650 . ? 1_555 ? 13 AC3 8 HOH M . ? HOH A 780 . ? 5_555 ? 14 AC3 8 HOH M . ? HOH A 787 . ? 5_555 ? 15 AC4 5 PRO A 112 ? PRO A 112 . ? 3_554 ? 16 AC4 5 ARG A 113 ? ARG A 113 . ? 3_554 ? 17 AC4 5 GLY A 116 ? GLY A 116 . ? 3_554 ? 18 AC4 5 LYS A 234 ? LYS A 234 . ? 1_555 ? 19 AC4 5 ASN A 235 ? ASN A 235 . ? 1_555 ? 20 AC5 5 SER A 20 ? SER A 20 . ? 1_555 ? 21 AC5 5 HIS A 54 ? HIS A 54 . ? 1_555 ? 22 AC5 5 ASP A 55 ? ASP A 55 . ? 1_555 ? 23 AC5 5 HOH M . ? HOH A 688 . ? 1_555 ? 24 AC5 5 HOH M . ? HOH A 807 . ? 1_555 ? 25 AC6 5 LEU A 38 ? LEU A 38 . ? 1_555 ? 26 AC6 5 TYR A 47 ? TYR A 47 . ? 1_555 ? 27 AC6 5 HIS A 98 ? HIS A 98 . ? 1_555 ? 28 AC6 5 TYR A 103 ? TYR A 103 . ? 1_555 ? 29 AC6 5 HOH M . ? HOH A 570 . ? 1_555 ? 30 AC7 6 HIS A 48 ? HIS A 48 . ? 1_555 ? 31 AC7 6 ALA A 210 ? ALA A 210 . ? 5_555 ? 32 AC7 6 ALA A 211 ? ALA A 211 . ? 5_555 ? 33 AC7 6 PRO A 213 ? PRO A 213 . ? 5_555 ? 34 AC7 6 HOH M . ? HOH A 806 . ? 1_555 ? 35 AC7 6 EDO L . ? EDO A 2011 . ? 1_555 ? 36 AC8 7 ARG A 14 ? ARG A 14 . ? 1_555 ? 37 AC8 7 TYR A 80 ? TYR A 80 . ? 1_555 ? 38 AC8 7 LEU A 141 ? LEU A 141 . ? 5_555 ? 39 AC8 7 TRP A 256 ? TRP A 256 . ? 1_555 ? 40 AC8 7 HOH M . ? HOH A 617 . ? 5_555 ? 41 AC8 7 HOH M . ? HOH A 673 . ? 1_555 ? 42 AC8 7 HOH M . ? HOH A 730 . ? 1_555 ? 43 AC9 7 SER A 27 ? SER A 27 . ? 1_555 ? 44 AC9 7 ARG A 258 ? ARG A 258 . ? 1_555 ? 45 AC9 7 ASP A 261 ? ASP A 261 . ? 1_555 ? 46 AC9 7 ASN A 265 ? ASN A 265 . ? 1_555 ? 47 AC9 7 HOH M . ? HOH A 587 . ? 1_555 ? 48 AC9 7 HOH M . ? HOH A 696 . ? 1_555 ? 49 AC9 7 HOH M . ? HOH A 801 . ? 1_555 ? 50 BC1 7 ARG A 14 ? ARG A 14 . ? 1_555 ? 51 BC1 7 ASP A 39 ? ASP A 39 . ? 1_555 ? 52 BC1 7 ASP A 50 ? ASP A 50 . ? 1_555 ? 53 BC1 7 THR A 178 ? THR A 178 . ? 5_555 ? 54 BC1 7 HOH M . ? HOH A 510 . ? 1_555 ? 55 BC1 7 HOH M . ? HOH A 683 . ? 1_555 ? 56 BC1 7 HOH M . ? HOH A 804 . ? 1_555 ? 57 BC2 7 ASP A 50 ? ASP A 50 . ? 1_555 ? 58 BC2 7 ALA A 177 ? ALA A 177 . ? 5_555 ? 59 BC2 7 GLY A 179 ? GLY A 179 . ? 5_555 ? 60 BC2 7 ALA A 211 ? ALA A 211 . ? 5_555 ? 61 BC2 7 TYR A 212 ? TYR A 212 . ? 5_555 ? 62 BC2 7 HOH M . ? HOH A 806 . ? 1_555 ? 63 BC2 7 EDO H . ? EDO A 2007 . ? 1_555 ? # _database_PDB_matrix.entry_id 1OM0 _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 1OM0 _atom_sites.fract_transf_matrix[1][1] 0.017101 _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] 0.017101 _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] 0.005210 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . ALA A 1 1 ? 16.367 1.583 49.183 1.00 51.60 ? 1 ALA A N 1 ATOM 2 C CA . ALA A 1 1 ? 16.080 3.029 48.967 1.00 51.29 ? 1 ALA A CA 1 ATOM 3 C C . ALA A 1 1 ? 14.734 3.402 49.572 1.00 50.59 ? 1 ALA A C 1 ATOM 4 O O . ALA A 1 1 ? 13.779 2.628 49.516 1.00 51.37 ? 1 ALA A O 1 ATOM 5 C CB . ALA A 1 1 ? 16.085 3.343 47.474 1.00 52.32 ? 1 ALA A CB 1 ATOM 6 N N . GLY A 1 2 ? 14.663 4.592 50.156 1.00 49.45 ? 2 GLY A N 1 ATOM 7 C CA . GLY A 1 2 ? 13.420 5.035 50.756 1.00 46.68 ? 2 GLY A CA 1 ATOM 8 C C . GLY A 1 2 ? 12.393 5.401 49.704 1.00 45.09 ? 2 GLY A C 1 ATOM 9 O O . GLY A 1 2 ? 12.600 5.180 48.508 1.00 45.36 ? 2 GLY A O 1 ATOM 10 N N . GLY A 1 3 ? 11.280 5.967 50.155 1.00 42.62 ? 3 GLY A N 1 ATOM 11 C CA . GLY A 1 3 ? 10.222 6.363 49.247 1.00 39.23 ? 3 GLY A CA 1 ATOM 12 C C . GLY A 1 3 ? 9.174 7.132 50.020 1.00 36.84 ? 3 GLY A C 1 ATOM 13 O O . GLY A 1 3 ? 9.332 7.351 51.220 1.00 36.68 ? 3 GLY A O 1 ATOM 14 N N . LYS A 1 4 ? 8.107 7.540 49.343 1.00 34.74 ? 4 LYS A N 1 ATOM 15 C CA . LYS A 1 4 ? 7.034 8.289 49.988 1.00 33.09 ? 4 LYS A CA 1 ATOM 16 C C . LYS A 1 4 ? 6.488 7.518 51.186 1.00 31.59 ? 4 LYS A C 1 ATOM 17 O O . LYS A 1 4 ? 6.418 6.286 51.160 1.00 29.97 ? 4 LYS A O 1 ATOM 18 C CB . LYS A 1 4 ? 5.914 8.559 48.980 1.00 35.50 ? 4 LYS A CB 1 ATOM 19 C CG . LYS A 1 4 ? 6.362 9.400 47.791 1.00 37.89 ? 4 LYS A CG 1 ATOM 20 C CD . LYS A 1 4 ? 5.325 9.409 46.679 1.00 39.87 ? 4 LYS A CD 1 ATOM 21 C CE . LYS A 1 4 ? 4.021 10.036 47.128 1.00 41.19 ? 4 LYS A CE 1 ATOM 22 N NZ . LYS A 1 4 ? 3.021 10.064 46.019 1.00 42.51 ? 4 LYS A NZ 1 ATOM 23 N N . THR A 1 5 ? 6.114 8.245 52.237 1.00 27.78 ? 5 THR A N 1 ATOM 24 C CA . THR A 1 5 ? 5.572 7.631 53.446 1.00 26.71 ? 5 THR A CA 1 ATOM 25 C C . THR A 1 5 ? 4.204 8.208 53.780 1.00 26.52 ? 5 THR A C 1 ATOM 26 O O . THR A 1 5 ? 3.473 7.664 54.610 1.00 25.60 ? 5 THR A O 1 ATOM 27 C CB . THR A 1 5 ? 6.489 7.869 54.659 1.00 26.92 ? 5 THR A CB 1 ATOM 28 O OG1 . THR A 1 5 ? 6.607 9.281 54.898 1.00 25.62 ? 5 THR A OG1 1 ATOM 29 C CG2 . THR A 1 5 ? 7.865 7.275 54.411 1.00 25.40 ? 5 THR A CG2 1 ATOM 30 N N . GLY A 1 6 ? 3.869 9.322 53.141 1.00 25.15 ? 6 GLY A N 1 ATOM 31 C CA . GLY A 1 6 ? 2.591 9.968 53.386 1.00 26.32 ? 6 GLY A CA 1 ATOM 32 C C . GLY A 1 6 ? 2.514 10.633 54.751 1.00 26.08 ? 6 GLY A C 1 ATOM 33 O O . GLY A 1 6 ? 1.432 11.010 55.202 1.00 27.92 ? 6 GLY A O 1 ATOM 34 N N . GLN A 1 7 ? 3.661 10.783 55.407 1.00 24.25 ? 7 GLN A N 1 ATOM 35 C CA . GLN A 1 7 ? 3.710 11.394 56.733 1.00 21.79 ? 7 GLN A CA 1 ATOM 36 C C . GLN A 1 7 ? 4.051 12.877 56.704 1.00 21.71 ? 7 GLN A C 1 ATOM 37 O O . GLN A 1 7 ? 5.047 13.279 56.106 1.00 19.29 ? 7 GLN A O 1 ATOM 38 C CB . GLN A 1 7 ? 4.730 10.671 57.608 1.00 23.41 ? 7 GLN A CB 1 ATOM 39 C CG . GLN A 1 7 ? 4.404 9.195 57.813 1.00 27.63 ? 7 GLN A CG 1 ATOM 40 C CD . GLN A 1 7 ? 2.972 8.988 58.272 1.00 29.71 ? 7 GLN A CD 1 ATOM 41 O OE1 . GLN A 1 7 ? 2.598 9.379 59.376 1.00 31.09 ? 7 GLN A OE1 1 ATOM 42 N NE2 . GLN A 1 7 ? 2.159 8.379 57.414 1.00 34.41 ? 7 GLN A NE2 1 ATOM 43 N N . VAL A 1 8 ? 3.216 13.671 57.366 1.00 19.52 ? 8 VAL A N 1 ATOM 44 C CA . VAL A 1 8 ? 3.404 15.114 57.457 1.00 20.43 ? 8 VAL A CA 1 ATOM 45 C C . VAL A 1 8 ? 3.197 15.573 58.897 1.00 18.36 ? 8 VAL A C 1 ATOM 46 O O . VAL A 1 8 ? 2.094 15.477 59.432 1.00 18.47 ? 8 VAL A O 1 ATOM 47 C CB . VAL A 1 8 ? 2.397 15.874 56.561 1.00 20.86 ? 8 VAL A CB 1 ATOM 48 C CG1 . VAL A 1 8 ? 2.620 17.375 56.692 1.00 22.50 ? 8 VAL A CG1 1 ATOM 49 C CG2 . VAL A 1 8 ? 2.552 15.435 55.108 1.00 23.43 ? 8 VAL A CG2 1 ATOM 50 N N . THR A 1 9 ? 4.262 16.066 59.521 1.00 17.71 ? 9 THR A N 1 ATOM 51 C CA . THR A 1 9 ? 4.195 16.562 60.896 1.00 17.60 ? 9 THR A CA 1 ATOM 52 C C . THR A 1 9 ? 4.219 18.086 60.850 1.00 17.62 ? 9 THR A C 1 ATOM 53 O O . THR A 1 9 ? 5.052 18.668 60.159 1.00 18.23 ? 9 THR A O 1 ATOM 54 C CB . THR A 1 9 ? 5.401 16.090 61.731 1.00 17.95 ? 9 THR A CB 1 ATOM 55 O OG1 . THR A 1 9 ? 5.328 14.673 61.929 1.00 19.18 ? 9 THR A OG1 1 ATOM 56 C CG2 . THR A 1 9 ? 5.428 16.789 63.094 1.00 18.62 ? 9 THR A CG2 1 ATOM 57 N N . VAL A 1 10 ? 3.315 18.723 61.586 1.00 16.41 ? 10 VAL A N 1 ATOM 58 C CA . VAL A 1 10 ? 3.253 20.185 61.606 1.00 16.87 ? 10 VAL A CA 1 ATOM 59 C C . VAL A 1 10 ? 3.368 20.730 63.025 1.00 17.36 ? 10 VAL A C 1 ATOM 60 O O . VAL A 1 10 ? 2.943 20.084 63.983 1.00 18.60 ? 10 VAL A O 1 ATOM 61 C CB . VAL A 1 10 ? 1.916 20.690 60.999 1.00 16.52 ? 10 VAL A CB 1 ATOM 62 C CG1 . VAL A 1 10 ? 0.756 20.355 61.932 1.00 17.93 ? 10 VAL A CG1 1 ATOM 63 C CG2 . VAL A 1 10 ? 1.978 22.202 60.764 1.00 17.77 ? 10 VAL A CG2 1 ATOM 64 N N . PHE A 1 11 ? 3.955 21.914 63.162 1.00 16.64 ? 11 PHE A N 1 ATOM 65 C CA . PHE A 1 11 ? 4.062 22.541 64.474 1.00 17.45 ? 11 PHE A CA 1 ATOM 66 C C . PHE A 1 11 ? 2.856 23.458 64.683 1.00 17.81 ? 11 PHE A C 1 ATOM 67 O O . PHE A 1 11 ? 2.357 24.078 63.741 1.00 19.54 ? 11 PHE A O 1 ATOM 68 C CB . PHE A 1 11 ? 5.358 23.348 64.598 1.00 17.66 ? 11 PHE A CB 1 ATOM 69 C CG . PHE A 1 11 ? 6.522 22.551 65.114 1.00 19.03 ? 11 PHE A CG 1 ATOM 70 C CD1 . PHE A 1 11 ? 7.191 21.648 64.294 1.00 20.30 ? 11 PHE A CD1 1 ATOM 71 C CD2 . PHE A 1 11 ? 6.937 22.692 66.434 1.00 16.92 ? 11 PHE A CD2 1 ATOM 72 C CE1 . PHE A 1 11 ? 8.258 20.896 64.785 1.00 21.04 ? 11 PHE A CE1 1 ATOM 73 C CE2 . PHE A 1 11 ? 8.000 21.947 66.938 1.00 19.93 ? 11 PHE A CE2 1 ATOM 74 C CZ . PHE A 1 11 ? 8.663 21.045 66.111 1.00 20.92 ? 11 PHE A CZ 1 ATOM 75 N N . TRP A 1 12 ? 2.388 23.529 65.922 1.00 17.34 ? 12 TRP A N 1 ATOM 76 C CA . TRP A 1 12 ? 1.240 24.355 66.273 1.00 18.28 ? 12 TRP A CA 1 ATOM 77 C C . TRP A 1 12 ? 1.516 24.986 67.634 1.00 18.35 ? 12 TRP A C 1 ATOM 78 O O . TRP A 1 12 ? 2.282 24.438 68.431 1.00 16.03 ? 12 TRP A O 1 ATOM 79 C CB . TRP A 1 12 ? -0.012 23.480 66.348 1.00 19.83 ? 12 TRP A CB 1 ATOM 80 C CG . TRP A 1 12 ? -1.258 24.167 66.842 1.00 20.35 ? 12 TRP A CG 1 ATOM 81 C CD1 . TRP A 1 12 ? -2.213 24.786 66.081 1.00 21.60 ? 12 TRP A CD1 1 ATOM 82 C CD2 . TRP A 1 12 ? -1.705 24.264 68.202 1.00 21.50 ? 12 TRP A CD2 1 ATOM 83 N NE1 . TRP A 1 12 ? -3.228 25.256 66.884 1.00 21.75 ? 12 TRP A NE1 1 ATOM 84 C CE2 . TRP A 1 12 ? -2.942 24.951 68.189 1.00 21.21 ? 12 TRP A CE2 1 ATOM 85 C CE3 . TRP A 1 12 ? -1.182 23.836 69.431 1.00 21.86 ? 12 TRP A CE3 1 ATOM 86 C CZ2 . TRP A 1 12 ? -3.664 25.219 69.358 1.00 22.14 ? 12 TRP A CZ2 1 ATOM 87 C CZ3 . TRP A 1 12 ? -1.902 24.102 70.596 1.00 22.85 ? 12 TRP A CZ3 1 ATOM 88 C CH2 . TRP A 1 12 ? -3.131 24.788 70.548 1.00 22.86 ? 12 TRP A CH2 1 ATOM 89 N N . GLY A 1 13 ? 0.907 26.144 67.885 1.00 17.13 ? 13 GLY A N 1 ATOM 90 C CA . GLY A 1 13 ? 1.084 26.817 69.160 1.00 18.12 ? 13 GLY A CA 1 ATOM 91 C C . GLY A 1 13 ? 1.907 28.095 69.150 1.00 17.95 ? 13 GLY A C 1 ATOM 92 O O . GLY A 1 13 ? 2.034 28.749 70.183 1.00 19.15 ? 13 GLY A O 1 ATOM 93 N N . ARG A 1 14 ? 2.444 28.467 67.990 1.00 16.91 ? 14 ARG A N 1 ATOM 94 C CA . ARG A 1 14 ? 3.286 29.656 67.872 1.00 17.42 ? 14 ARG A CA 1 ATOM 95 C C . ARG A 1 14 ? 2.523 30.947 67.592 1.00 18.85 ? 14 ARG A C 1 ATOM 96 O O . ARG A 1 14 ? 3.087 32.035 67.692 1.00 19.55 ? 14 ARG A O 1 ATOM 97 C CB . ARG A 1 14 ? 4.318 29.448 66.759 1.00 16.97 ? 14 ARG A CB 1 ATOM 98 C CG . ARG A 1 14 ? 5.112 28.150 66.864 1.00 17.23 ? 14 ARG A CG 1 ATOM 99 C CD . ARG A 1 14 ? 6.123 28.172 67.991 1.00 17.69 ? 14 ARG A CD 1 ATOM 100 N NE . ARG A 1 14 ? 5.511 28.133 69.317 1.00 16.66 ? 14 ARG A NE 1 ATOM 101 C CZ . ARG A 1 14 ? 5.767 29.015 70.279 1.00 17.65 ? 14 ARG A CZ 1 ATOM 102 N NH1 . ARG A 1 14 ? 5.171 28.903 71.461 1.00 16.48 ? 14 ARG A NH1 1 ATOM 103 N NH2 . ARG A 1 14 ? 6.613 30.016 70.058 1.00 18.82 ? 14 ARG A NH2 1 ATOM 104 N N . ASN A 1 15 ? 1.251 30.832 67.237 1.00 20.19 ? 15 ASN A N 1 ATOM 105 C CA . ASN A 1 15 ? 0.450 32.019 66.939 1.00 22.22 ? 15 ASN A CA 1 ATOM 106 C C . ASN A 1 15 ? -1.032 31.716 67.149 1.00 22.67 ? 15 ASN A C 1 ATOM 107 O O . ASN A 1 15 ? -1.617 30.919 66.416 1.00 22.96 ? 15 ASN A O 1 ATOM 108 C CB . ASN A 1 15 ? 0.693 32.448 65.494 1.00 23.14 ? 15 ASN A CB 1 ATOM 109 C CG . ASN A 1 15 ? 0.182 33.841 65.213 1.00 25.83 ? 15 ASN A CG 1 ATOM 110 O OD1 . ASN A 1 15 ? -0.938 34.183 65.582 1.00 25.70 ? 15 ASN A OD1 1 ATOM 111 N ND2 . ASN A 1 15 ? 1.001 34.653 64.550 1.00 25.69 ? 15 ASN A ND2 1 ATOM 112 N N . LYS A 1 16 ? -1.639 32.366 68.138 1.00 24.76 ? 16 LYS A N 1 ATOM 113 C CA . LYS A 1 16 ? -3.045 32.125 68.462 1.00 26.68 ? 16 LYS A CA 1 ATOM 114 C C . LYS A 1 16 ? -4.020 32.345 67.311 1.00 27.37 ? 16 LYS A C 1 ATOM 115 O O . LYS A 1 16 ? -5.154 31.864 67.355 1.00 29.44 ? 16 LYS A O 1 ATOM 116 C CB . LYS A 1 16 ? -3.469 32.976 69.666 1.00 27.68 ? 16 LYS A CB 1 ATOM 117 C CG . LYS A 1 16 ? -3.443 34.481 69.431 1.00 30.47 ? 16 LYS A CG 1 ATOM 118 C CD . LYS A 1 16 ? -3.897 35.230 70.674 1.00 34.38 ? 16 LYS A CD 1 ATOM 119 C CE . LYS A 1 16 ? -3.804 36.739 70.479 1.00 36.75 ? 16 LYS A CE 1 ATOM 120 N NZ . LYS A 1 16 ? -4.192 37.486 71.709 1.00 40.04 ? 16 LYS A NZ 1 ATOM 121 N N . ALA A 1 17 ? -3.589 33.058 66.277 1.00 26.82 ? 17 ALA A N 1 ATOM 122 C CA . ALA A 1 17 ? -4.461 33.311 65.138 1.00 27.22 ? 17 ALA A CA 1 ATOM 123 C C . ALA A 1 17 ? -4.515 32.129 64.165 1.00 27.46 ? 17 ALA A C 1 ATOM 124 O O . ALA A 1 17 ? -5.251 32.162 63.181 1.00 28.59 ? 17 ALA A O 1 ATOM 125 C CB . ALA A 1 17 ? -4.001 34.571 64.405 1.00 28.48 ? 17 ALA A CB 1 ATOM 126 N N . GLU A 1 18 ? -3.759 31.074 64.450 1.00 26.01 ? 18 GLU A N 1 ATOM 127 C CA . GLU A 1 18 ? -3.717 29.914 63.560 1.00 26.19 ? 18 GLU A CA 1 ATOM 128 C C . GLU A 1 18 ? -4.870 28.933 63.714 1.00 26.62 ? 18 GLU A C 1 ATOM 129 O O . GLU A 1 18 ? -4.928 27.927 63.010 1.00 28.56 ? 18 GLU A O 1 ATOM 130 C CB . GLU A 1 18 ? -2.394 29.163 63.751 1.00 24.55 ? 18 GLU A CB 1 ATOM 131 C CG . GLU A 1 18 ? -2.314 28.373 65.044 1.00 24.10 ? 18 GLU A CG 1 ATOM 132 C CD . GLU A 1 18 ? -0.887 28.045 65.425 1.00 22.92 ? 18 GLU A CD 1 ATOM 133 O OE1 . GLU A 1 18 ? -0.080 27.777 64.511 1.00 22.67 ? 18 GLU A OE1 1 ATOM 134 O OE2 . GLU A 1 18 ? -0.577 28.051 66.633 1.00 22.61 ? 18 GLU A OE2 1 ATOM 135 N N . GLY A 1 19 ? -5.790 29.217 64.626 1.00 27.36 ? 19 GLY A N 1 ATOM 136 C CA . GLY A 1 19 ? -6.906 28.310 64.823 1.00 27.64 ? 19 GLY A CA 1 ATOM 137 C C . GLY A 1 19 ? -6.623 27.286 65.907 1.00 28.18 ? 19 GLY A C 1 ATOM 138 O O . GLY A 1 19 ? -5.483 27.122 66.347 1.00 25.85 ? 19 GLY A O 1 ATOM 139 N N . SER A 1 20 ? -7.664 26.578 66.328 1.00 27.45 ? 20 SER A N 1 ATOM 140 C CA . SER A 1 20 ? -7.534 25.579 67.379 1.00 27.01 ? 20 SER A CA 1 ATOM 141 C C . SER A 1 20 ? -6.813 24.325 66.913 1.00 26.59 ? 20 SER A C 1 ATOM 142 O O . SER A 1 20 ? -6.663 24.080 65.715 1.00 25.59 ? 20 SER A O 1 ATOM 143 C CB . SER A 1 20 ? -8.915 25.178 67.895 1.00 27.64 ? 20 SER A CB 1 ATOM 144 O OG . SER A 1 20 ? -9.601 24.414 66.918 1.00 29.44 ? 20 SER A OG 1 ATOM 145 N N . LEU A 1 21 ? -6.377 23.530 67.882 1.00 27.19 ? 21 LEU A N 1 ATOM 146 C CA . LEU A 1 21 ? -5.696 22.278 67.605 1.00 26.17 ? 21 LEU A CA 1 ATOM 147 C C . LEU A 1 21 ? -6.659 21.359 66.861 1.00 27.07 ? 21 LEU A C 1 ATOM 148 O O . LEU A 1 21 ? -6.261 20.606 65.972 1.00 25.91 ? 21 LEU A O 1 ATOM 149 C CB . LEU A 1 21 ? -5.264 21.621 68.917 1.00 24.26 ? 21 LEU A CB 1 ATOM 150 C CG . LEU A 1 21 ? -4.739 20.186 68.817 1.00 23.77 ? 21 LEU A CG 1 ATOM 151 C CD1 . LEU A 1 21 ? -3.480 20.143 67.948 1.00 22.42 ? 21 LEU A CD1 1 ATOM 152 C CD2 . LEU A 1 21 ? -4.441 19.665 70.218 1.00 22.63 ? 21 LEU A CD2 1 ATOM 153 N N . ARG A 1 22 ? -7.932 21.425 67.235 1.00 27.75 ? 22 ARG A N 1 ATOM 154 C CA . ARG A 1 22 ? -8.956 20.597 66.608 1.00 29.42 ? 22 ARG A CA 1 ATOM 155 C C . ARG A 1 22 ? -9.040 20.900 65.114 1.00 28.75 ? 22 ARG A C 1 ATOM 156 O O . ARG A 1 22 ? -9.122 19.991 64.289 1.00 29.59 ? 22 ARG A O 1 ATOM 157 C CB . ARG A 1 22 ? -10.317 20.858 67.264 1.00 30.73 ? 22 ARG A CB 1 ATOM 158 C CG . ARG A 1 22 ? -11.443 19.968 66.761 1.00 34.56 ? 22 ARG A CG 1 ATOM 159 C CD . ARG A 1 22 ? -12.798 20.474 67.255 1.00 36.97 ? 22 ARG A CD 1 ATOM 160 N NE . ARG A 1 22 ? -12.886 20.531 68.714 1.00 42.05 ? 22 ARG A NE 1 ATOM 161 C CZ . ARG A 1 22 ? -13.185 19.493 69.491 1.00 44.26 ? 22 ARG A CZ 1 ATOM 162 N NH1 . ARG A 1 22 ? -13.431 18.307 68.951 1.00 46.73 ? 22 ARG A NH1 1 ATOM 163 N NH2 . ARG A 1 22 ? -13.241 19.640 70.809 1.00 44.08 ? 22 ARG A NH2 1 ATOM 164 N N . GLU A 1 23 ? -9.020 22.185 64.778 1.00 29.08 ? 23 GLU A N 1 ATOM 165 C CA . GLU A 1 23 ? -9.092 22.621 63.387 1.00 30.51 ? 23 GLU A CA 1 ATOM 166 C C . GLU A 1 23 ? -7.932 22.042 62.582 1.00 29.97 ? 23 GLU A C 1 ATOM 167 O O . GLU A 1 23 ? -8.107 21.598 61.447 1.00 29.75 ? 23 GLU A O 1 ATOM 168 C CB . GLU A 1 23 ? -9.058 24.151 63.321 1.00 32.84 ? 23 GLU A CB 1 ATOM 169 C CG . GLU A 1 23 ? -9.103 24.728 61.914 1.00 37.44 ? 23 GLU A CG 1 ATOM 170 C CD . GLU A 1 23 ? -8.915 26.233 61.900 1.00 40.00 ? 23 GLU A CD 1 ATOM 171 O OE1 . GLU A 1 23 ? -9.804 26.954 62.406 1.00 41.05 ? 23 GLU A OE1 1 ATOM 172 O OE2 . GLU A 1 23 ? -7.870 26.695 61.391 1.00 40.17 ? 23 GLU A OE2 1 ATOM 173 N N . ALA A 1 24 ? -6.746 22.045 63.179 1.00 28.52 ? 24 ALA A N 1 ATOM 174 C CA . ALA A 1 24 ? -5.562 21.524 62.513 1.00 28.35 ? 24 ALA A CA 1 ATOM 175 C C . ALA A 1 24 ? -5.737 20.048 62.171 1.00 28.22 ? 24 ALA A C 1 ATOM 176 O O . ALA A 1 24 ? -5.482 19.628 61.045 1.00 26.32 ? 24 ALA A O 1 ATOM 177 C CB . ALA A 1 24 ? -4.331 21.720 63.405 1.00 28.20 ? 24 ALA A CB 1 ATOM 178 N N . CYS A 1 25 ? -6.176 19.259 63.145 1.00 29.50 ? 25 CYS A N 1 ATOM 179 C CA . CYS A 1 25 ? -6.370 17.834 62.916 1.00 31.11 ? 25 CYS A CA 1 ATOM 180 C C . CYS A 1 25 ? -7.495 17.564 61.917 1.00 32.20 ? 25 CYS A C 1 ATOM 181 O O . CYS A 1 25 ? -7.420 16.619 61.127 1.00 32.20 ? 25 CYS A O 1 ATOM 182 C CB . CYS A 1 25 ? -6.662 17.122 64.241 1.00 32.39 ? 25 CYS A CB 1 ATOM 183 S SG . CYS A 1 25 ? -5.319 17.287 65.466 1.00 37.00 ? 25 CYS A SG 1 ATOM 184 N N . ASP A 1 26 ? -8.526 18.403 61.947 1.00 33.15 ? 26 ASP A N 1 ATOM 185 C CA . ASP A 1 26 ? -9.671 18.252 61.050 1.00 34.46 ? 26 ASP A CA 1 ATOM 186 C C . ASP A 1 26 ? -9.382 18.636 59.601 1.00 34.51 ? 26 ASP A C 1 ATOM 187 O O . ASP A 1 26 ? -10.203 18.392 58.717 1.00 34.12 ? 26 ASP A O 1 ATOM 188 C CB . ASP A 1 26 ? -10.851 19.084 61.560 1.00 35.31 ? 26 ASP A CB 1 ATOM 189 C CG . ASP A 1 26 ? -11.631 18.384 62.657 1.00 37.83 ? 26 ASP A CG 1 ATOM 190 O OD1 . ASP A 1 26 ? -12.529 19.026 63.242 1.00 38.23 ? 26 ASP A OD1 1 ATOM 191 O OD2 . ASP A 1 26 ? -11.354 17.194 62.927 1.00 38.51 ? 26 ASP A OD2 1 ATOM 192 N N . SER A 1 27 ? -8.225 19.238 59.352 1.00 33.63 ? 27 SER A N 1 ATOM 193 C CA . SER A 1 27 ? -7.868 19.643 57.995 1.00 32.34 ? 27 SER A CA 1 ATOM 194 C C . SER A 1 27 ? -7.538 18.435 57.124 1.00 32.74 ? 27 SER A C 1 ATOM 195 O O . SER A 1 27 ? -7.647 18.496 55.898 1.00 33.12 ? 27 SER A O 1 ATOM 196 C CB . SER A 1 27 ? -6.666 20.588 58.020 1.00 32.14 ? 27 SER A CB 1 ATOM 197 O OG . SER A 1 27 ? -5.503 19.905 58.451 1.00 30.15 ? 27 SER A OG 1 ATOM 198 N N . GLY A 1 28 ? -7.132 17.340 57.761 1.00 31.55 ? 28 GLY A N 1 ATOM 199 C CA . GLY A 1 28 ? -6.781 16.138 57.026 1.00 31.47 ? 28 GLY A CA 1 ATOM 200 C C . GLY A 1 28 ? -5.445 16.281 56.320 1.00 31.01 ? 28 GLY A C 1 ATOM 201 O O . GLY A 1 28 ? -5.088 15.460 55.477 1.00 31.10 ? 28 GLY A O 1 ATOM 202 N N . MET A 1 29 ? -4.700 17.324 56.677 1.00 30.75 ? 29 MET A N 1 ATOM 203 C CA . MET A 1 29 ? -3.401 17.597 56.069 1.00 30.53 ? 29 MET A CA 1 ATOM 204 C C . MET A 1 29 ? -2.210 17.035 56.844 1.00 28.87 ? 29 MET A C 1 ATOM 205 O O . MET A 1 29 ? -1.103 16.960 56.305 1.00 28.25 ? 29 MET A O 1 ATOM 206 C CB . MET A 1 29 ? -3.194 19.111 55.933 1.00 32.17 ? 29 MET A CB 1 ATOM 207 C CG . MET A 1 29 ? -4.319 19.860 55.241 1.00 36.61 ? 29 MET A CG 1 ATOM 208 S SD . MET A 1 29 ? -4.506 19.403 53.512 1.00 41.49 ? 29 MET A SD 1 ATOM 209 C CE . MET A 1 29 ? -5.712 18.110 53.627 1.00 40.53 ? 29 MET A CE 1 ATOM 210 N N . TYR A 1 30 ? -2.429 16.627 58.091 1.00 26.36 ? 30 TYR A N 1 ATOM 211 C CA . TYR A 1 30 ? -1.327 16.153 58.925 1.00 25.30 ? 30 TYR A CA 1 ATOM 212 C C . TYR A 1 30 ? -1.500 14.778 59.558 1.00 25.60 ? 30 TYR A C 1 ATOM 213 O O . TYR A 1 30 ? -2.613 14.372 59.893 1.00 26.23 ? 30 TYR A O 1 ATOM 214 C CB . TYR A 1 30 ? -1.089 17.163 60.050 1.00 21.73 ? 30 TYR A CB 1 ATOM 215 C CG . TYR A 1 30 ? -1.266 18.604 59.625 1.00 22.56 ? 30 TYR A CG 1 ATOM 216 C CD1 . TYR A 1 30 ? -0.365 19.210 58.747 1.00 20.17 ? 30 TYR A CD1 1 ATOM 217 C CD2 . TYR A 1 30 ? -2.336 19.361 60.097 1.00 21.27 ? 30 TYR A CD2 1 ATOM 218 C CE1 . TYR A 1 30 ? -0.530 20.541 58.348 1.00 20.63 ? 30 TYR A CE1 1 ATOM 219 C CE2 . TYR A 1 30 ? -2.511 20.689 59.709 1.00 21.98 ? 30 TYR A CE2 1 ATOM 220 C CZ . TYR A 1 30 ? -1.603 21.272 58.834 1.00 21.57 ? 30 TYR A CZ 1 ATOM 221 O OH . TYR A 1 30 ? -1.771 22.584 58.454 1.00 20.24 ? 30 TYR A OH 1 ATOM 222 N N . THR A 1 31 ? -0.384 14.077 59.742 1.00 25.35 ? 31 THR A N 1 ATOM 223 C CA . THR A 1 31 ? -0.405 12.764 60.374 1.00 24.42 ? 31 THR A CA 1 ATOM 224 C C . THR A 1 31 ? 0.143 12.884 61.795 1.00 24.89 ? 31 THR A C 1 ATOM 225 O O . THR A 1 31 ? 0.275 11.894 62.516 1.00 23.87 ? 31 THR A O 1 ATOM 226 C CB . THR A 1 31 ? 0.429 11.722 59.586 1.00 25.17 ? 31 THR A CB 1 ATOM 227 O OG1 . THR A 1 31 ? 1.770 12.197 59.405 1.00 24.79 ? 31 THR A OG1 1 ATOM 228 C CG2 . THR A 1 31 ? -0.209 11.455 58.229 1.00 25.92 ? 31 THR A CG2 1 ATOM 229 N N . MET A 1 32 ? 0.458 14.114 62.193 1.00 24.25 ? 32 MET A N 1 ATOM 230 C CA . MET A 1 32 ? 0.983 14.385 63.529 1.00 23.89 ? 32 MET A CA 1 ATOM 231 C C . MET A 1 32 ? 1.043 15.888 63.763 1.00 22.61 ? 32 MET A C 1 ATOM 232 O O . MET A 1 32 ? 1.470 16.637 62.889 1.00 21.81 ? 32 MET A O 1 ATOM 233 C CB . MET A 1 32 ? 2.389 13.792 63.680 1.00 26.29 ? 32 MET A CB 1 ATOM 234 C CG . MET A 1 32 ? 3.168 14.285 64.899 1.00 30.89 ? 32 MET A CG 1 ATOM 235 S SD . MET A 1 32 ? 2.624 13.588 66.468 1.00 37.82 ? 32 MET A SD 1 ATOM 236 C CE . MET A 1 32 ? 3.668 12.123 66.550 1.00 33.97 ? 32 MET A CE 1 ATOM 237 N N . VAL A 1 33 ? 0.595 16.323 64.936 1.00 22.06 ? 33 VAL A N 1 ATOM 238 C CA . VAL A 1 33 ? 0.635 17.740 65.292 1.00 20.09 ? 33 VAL A CA 1 ATOM 239 C C . VAL A 1 33 ? 1.503 17.852 66.536 1.00 19.84 ? 33 VAL A C 1 ATOM 240 O O . VAL A 1 33 ? 1.296 17.135 67.514 1.00 19.07 ? 33 VAL A O 1 ATOM 241 C CB . VAL A 1 33 ? -0.775 18.301 65.592 1.00 19.79 ? 33 VAL A CB 1 ATOM 242 C CG1 . VAL A 1 33 ? -0.677 19.773 66.000 1.00 21.22 ? 33 VAL A CG1 1 ATOM 243 C CG2 . VAL A 1 33 ? -1.659 18.161 64.362 1.00 22.14 ? 33 VAL A CG2 1 ATOM 244 N N . THR A 1 34 ? 2.486 18.745 66.492 1.00 18.48 ? 34 THR A N 1 ATOM 245 C CA . THR A 1 34 ? 3.393 18.928 67.611 1.00 17.86 ? 34 THR A CA 1 ATOM 246 C C . THR A 1 34 ? 3.188 20.316 68.205 1.00 18.66 ? 34 THR A C 1 ATOM 247 O O . THR A 1 34 ? 3.459 21.327 67.550 1.00 16.47 ? 34 THR A O 1 ATOM 248 C CB . THR A 1 34 ? 4.868 18.754 67.149 1.00 19.14 ? 34 THR A CB 1 ATOM 249 O OG1 . THR A 1 34 ? 5.037 17.439 66.597 1.00 21.44 ? 34 THR A OG1 1 ATOM 250 C CG2 . THR A 1 34 ? 5.828 18.921 68.316 1.00 18.93 ? 34 THR A CG2 1 ATOM 251 N N . MET A 1 35 ? 2.685 20.361 69.437 1.00 16.80 ? 35 MET A N 1 ATOM 252 C CA . MET A 1 35 ? 2.450 21.638 70.107 1.00 17.34 ? 35 MET A CA 1 ATOM 253 C C . MET A 1 35 ? 3.804 22.169 70.561 1.00 15.38 ? 35 MET A C 1 ATOM 254 O O . MET A 1 35 ? 4.710 21.396 70.847 1.00 16.29 ? 35 MET A O 1 ATOM 255 C CB . MET A 1 35 ? 1.525 21.447 71.317 1.00 19.42 ? 35 MET A CB 1 ATOM 256 C CG . MET A 1 35 ? 0.194 20.772 70.984 1.00 23.49 ? 35 MET A CG 1 ATOM 257 S SD . MET A 1 35 ? -0.932 20.651 72.411 1.00 26.40 ? 35 MET A SD 1 ATOM 258 C CE . MET A 1 35 ? -0.099 19.425 73.389 1.00 27.04 ? 35 MET A CE 1 ATOM 259 N N . SER A 1 36 ? 3.938 23.489 70.640 1.00 15.64 ? 36 SER A N 1 ATOM 260 C CA . SER A 1 36 ? 5.201 24.104 71.038 1.00 15.18 ? 36 SER A CA 1 ATOM 261 C C . SER A 1 36 ? 4.885 25.411 71.766 1.00 15.73 ? 36 SER A C 1 ATOM 262 O O . SER A 1 36 ? 3.998 26.134 71.318 1.00 16.57 ? 36 SER A O 1 ATOM 263 C CB . SER A 1 36 ? 6.033 24.387 69.783 1.00 15.75 ? 36 SER A CB 1 ATOM 264 O OG . SER A 1 36 ? 5.260 25.080 68.806 1.00 17.61 ? 36 SER A OG 1 ATOM 265 N N . PHE A 1 37 ? 5.581 25.737 72.861 1.00 15.62 ? 37 PHE A N 1 ATOM 266 C CA . PHE A 1 37 ? 6.667 24.952 73.468 1.00 17.03 ? 37 PHE A CA 1 ATOM 267 C C . PHE A 1 37 ? 6.595 24.955 74.999 1.00 18.78 ? 37 PHE A C 1 ATOM 268 O O . PHE A 1 37 ? 6.025 25.865 75.604 1.00 18.30 ? 37 PHE A O 1 ATOM 269 C CB . PHE A 1 37 ? 8.042 25.574 73.193 1.00 17.18 ? 37 PHE A CB 1 ATOM 270 C CG . PHE A 1 37 ? 8.500 25.518 71.768 1.00 17.19 ? 37 PHE A CG 1 ATOM 271 C CD1 . PHE A 1 37 ? 8.445 26.654 70.962 1.00 18.48 ? 37 PHE A CD1 1 ATOM 272 C CD2 . PHE A 1 37 ? 9.067 24.356 71.256 1.00 15.32 ? 37 PHE A CD2 1 ATOM 273 C CE1 . PHE A 1 37 ? 8.958 26.634 69.665 1.00 18.83 ? 37 PHE A CE1 1 ATOM 274 C CE2 . PHE A 1 37 ? 9.581 24.321 69.967 1.00 15.73 ? 37 PHE A CE2 1 ATOM 275 C CZ . PHE A 1 37 ? 9.529 25.468 69.163 1.00 17.39 ? 37 PHE A CZ 1 ATOM 276 N N . LEU A 1 38 ? 7.200 23.945 75.619 1.00 17.76 ? 38 LEU A N 1 ATOM 277 C CA . LEU A 1 38 ? 7.338 23.932 77.076 1.00 15.87 ? 38 LEU A CA 1 ATOM 278 C C . LEU A 1 38 ? 8.679 24.669 77.047 1.00 17.56 ? 38 LEU A C 1 ATOM 279 O O . LEU A 1 38 ? 9.714 24.059 76.777 1.00 16.56 ? 38 LEU A O 1 ATOM 280 C CB . LEU A 1 38 ? 7.527 22.509 77.621 1.00 17.54 ? 38 LEU A CB 1 ATOM 281 C CG . LEU A 1 38 ? 7.782 22.473 79.135 1.00 18.02 ? 38 LEU A CG 1 ATOM 282 C CD1 . LEU A 1 38 ? 6.474 22.733 79.883 1.00 19.96 ? 38 LEU A CD1 1 ATOM 283 C CD2 . LEU A 1 38 ? 8.363 21.115 79.536 1.00 19.68 ? 38 LEU A CD2 1 ATOM 284 N N . ASP A 1 39 ? 8.663 25.980 77.302 1.00 16.35 ? 39 ASP A N 1 ATOM 285 C CA . ASP A 1 39 ? 9.877 26.794 77.178 1.00 16.58 ? 39 ASP A CA 1 ATOM 286 C C . ASP A 1 39 ? 10.719 27.108 78.406 1.00 15.88 ? 39 ASP A C 1 ATOM 287 O O . ASP A 1 39 ? 11.776 27.746 78.288 1.00 15.83 ? 39 ASP A O 1 ATOM 288 C CB . ASP A 1 39 ? 9.526 28.101 76.465 1.00 19.76 ? 39 ASP A CB 1 ATOM 289 C CG . ASP A 1 39 ? 8.651 28.999 77.303 1.00 23.59 ? 39 ASP A CG 1 ATOM 290 O OD1 . ASP A 1 39 ? 7.922 28.476 78.172 1.00 23.19 ? 39 ASP A OD1 1 ATOM 291 O OD2 . ASP A 1 39 ? 8.681 30.231 77.083 1.00 26.25 ? 39 ASP A OD2 1 ATOM 292 N N . VAL A 1 40 ? 10.264 26.668 79.574 1.00 14.82 ? 40 VAL A N 1 ATOM 293 C CA . VAL A 1 40 ? 11.011 26.871 80.801 1.00 14.88 ? 40 VAL A CA 1 ATOM 294 C C . VAL A 1 40 ? 11.091 25.571 81.586 1.00 16.87 ? 40 VAL A C 1 ATOM 295 O O . VAL A 1 40 ? 10.072 24.939 81.859 1.00 17.51 ? 40 VAL A O 1 ATOM 296 C CB . VAL A 1 40 ? 10.365 27.939 81.704 1.00 16.36 ? 40 VAL A CB 1 ATOM 297 C CG1 . VAL A 1 40 ? 11.193 28.113 82.980 1.00 14.32 ? 40 VAL A CG1 1 ATOM 298 C CG2 . VAL A 1 40 ? 10.264 29.253 80.957 1.00 16.96 ? 40 VAL A CG2 1 ATOM 299 N N . PHE A 1 41 ? 12.314 25.170 81.909 1.00 17.58 ? 41 PHE A N 1 ATOM 300 C CA . PHE A 1 41 ? 12.568 23.971 82.700 1.00 19.16 ? 41 PHE A CA 1 ATOM 301 C C . PHE A 1 41 ? 14.041 23.978 83.077 1.00 21.54 ? 41 PHE A C 1 ATOM 302 O O . PHE A 1 41 ? 14.840 24.675 82.453 1.00 20.89 ? 41 PHE A O 1 ATOM 303 C CB . PHE A 1 41 ? 12.184 22.685 81.930 1.00 16.68 ? 41 PHE A CB 1 ATOM 304 C CG . PHE A 1 41 ? 12.916 22.487 80.627 1.00 15.48 ? 41 PHE A CG 1 ATOM 305 C CD1 . PHE A 1 41 ? 14.245 22.061 80.608 1.00 15.46 ? 41 PHE A CD1 1 ATOM 306 C CD2 . PHE A 1 41 ? 12.257 22.677 79.414 1.00 14.93 ? 41 PHE A CD2 1 ATOM 307 C CE1 . PHE A 1 41 ? 14.904 21.822 79.396 1.00 13.83 ? 41 PHE A CE1 1 ATOM 308 C CE2 . PHE A 1 41 ? 12.906 22.440 78.198 1.00 13.28 ? 41 PHE A CE2 1 ATOM 309 C CZ . PHE A 1 41 ? 14.228 22.012 78.190 1.00 14.53 ? 41 PHE A CZ 1 ATOM 310 N N . GLY A 1 42 ? 14.402 23.225 84.110 1.00 22.28 ? 42 GLY A N 1 ATOM 311 C CA . GLY A 1 42 ? 15.791 23.203 84.533 1.00 25.97 ? 42 GLY A CA 1 ATOM 312 C C . GLY A 1 42 ? 15.988 22.568 85.894 1.00 28.83 ? 42 GLY A C 1 ATOM 313 O O . GLY A 1 42 ? 15.124 21.837 86.377 1.00 30.52 ? 42 GLY A O 1 ATOM 314 N N . ALA A 1 43 ? 17.123 22.857 86.519 1.00 31.06 ? 43 ALA A N 1 ATOM 315 C CA . ALA A 1 43 ? 17.452 22.294 87.828 1.00 34.23 ? 43 ALA A CA 1 ATOM 316 C C . ALA A 1 43 ? 16.720 22.930 89.017 1.00 37.51 ? 43 ALA A C 1 ATOM 317 O O . ALA A 1 43 ? 16.858 22.469 90.152 1.00 38.38 ? 43 ALA A O 1 ATOM 318 C CB . ALA A 1 43 ? 18.958 22.371 88.048 1.00 32.24 ? 43 ALA A CB 1 ATOM 319 N N . ASN A 1 44 ? 15.940 23.976 88.760 1.00 38.04 ? 44 ASN A N 1 ATOM 320 C CA . ASN A 1 44 ? 15.223 24.646 89.834 1.00 39.53 ? 44 ASN A CA 1 ATOM 321 C C . ASN A 1 44 ? 13.790 24.203 90.073 1.00 39.63 ? 44 ASN A C 1 ATOM 322 O O . ASN A 1 44 ? 13.131 24.712 90.984 1.00 42.06 ? 44 ASN A O 1 ATOM 323 N N . GLY A 1 45 ? 13.291 23.277 89.258 1.00 38.78 ? 45 GLY A N 1 ATOM 324 C CA . GLY A 1 45 ? 11.932 22.791 89.438 1.00 37.65 ? 45 GLY A CA 1 ATOM 325 C C . GLY A 1 45 ? 10.800 23.699 88.978 1.00 36.44 ? 45 GLY A C 1 ATOM 326 O O . GLY A 1 45 ? 9.655 23.519 89.395 1.00 38.49 ? 45 GLY A O 1 ATOM 327 N N . LYS A 1 46 ? 11.104 24.669 88.121 1.00 34.50 ? 46 LYS A N 1 ATOM 328 C CA . LYS A 1 46 ? 10.084 25.586 87.615 1.00 30.67 ? 46 LYS A CA 1 ATOM 329 C C . LYS A 1 46 ? 9.807 25.274 86.148 1.00 26.27 ? 46 LYS A C 1 ATOM 330 O O . LYS A 1 46 ? 10.729 25.230 85.337 1.00 25.46 ? 46 LYS A O 1 ATOM 331 C CB . LYS A 1 46 ? 10.557 27.034 87.761 1.00 33.15 ? 46 LYS A CB 1 ATOM 332 C CG . LYS A 1 46 ? 10.939 27.421 89.188 1.00 38.55 ? 46 LYS A CG 1 ATOM 333 C CD . LYS A 1 46 ? 9.756 27.307 90.142 1.00 42.16 ? 46 LYS A CD 1 ATOM 334 C CE . LYS A 1 46 ? 10.156 27.711 91.557 1.00 44.60 ? 46 LYS A CE 1 ATOM 335 N NZ . LYS A 1 46 ? 9.014 27.627 92.516 1.00 46.67 ? 46 LYS A NZ 1 ATOM 336 N N . TYR A 1 47 ? 8.537 25.067 85.811 1.00 21.33 ? 47 TYR A N 1 ATOM 337 C CA . TYR A 1 47 ? 8.163 24.731 84.442 1.00 21.20 ? 47 TYR A CA 1 ATOM 338 C C . TYR A 1 47 ? 7.109 25.658 83.849 1.00 21.03 ? 47 TYR A C 1 ATOM 339 O O . TYR A 1 47 ? 6.182 26.089 84.537 1.00 22.96 ? 47 TYR A O 1 ATOM 340 C CB . TYR A 1 47 ? 7.652 23.284 84.387 1.00 20.62 ? 47 TYR A CB 1 ATOM 341 C CG . TYR A 1 47 ? 8.604 22.291 85.005 1.00 20.50 ? 47 TYR A CG 1 ATOM 342 C CD1 . TYR A 1 47 ? 8.453 21.877 86.331 1.00 20.47 ? 47 TYR A CD1 1 ATOM 343 C CD2 . TYR A 1 47 ? 9.690 21.800 84.280 1.00 19.86 ? 47 TYR A CD2 1 ATOM 344 C CE1 . TYR A 1 47 ? 9.365 21.001 86.917 1.00 22.11 ? 47 TYR A CE1 1 ATOM 345 C CE2 . TYR A 1 47 ? 10.608 20.929 84.858 1.00 19.86 ? 47 TYR A CE2 1 ATOM 346 C CZ . TYR A 1 47 ? 10.442 20.535 86.173 1.00 21.59 ? 47 TYR A CZ 1 ATOM 347 O OH . TYR A 1 47 ? 11.368 19.695 86.747 1.00 22.47 ? 47 TYR A OH 1 ATOM 348 N N . HIS A 1 48 ? 7.246 25.959 82.562 1.00 18.29 ? 48 HIS A N 1 ATOM 349 C CA . HIS A 1 48 ? 6.286 26.823 81.894 1.00 18.92 ? 48 HIS A CA 1 ATOM 350 C C . HIS A 1 48 ? 5.947 26.348 80.494 1.00 19.31 ? 48 HIS A C 1 ATOM 351 O O . HIS A 1 48 ? 6.822 25.933 79.734 1.00 18.93 ? 48 HIS A O 1 ATOM 352 C CB . HIS A 1 48 ? 6.815 28.261 81.808 1.00 20.41 ? 48 HIS A CB 1 ATOM 353 C CG . HIS A 1 48 ? 5.908 29.189 81.060 1.00 25.48 ? 48 HIS A CG 1 ATOM 354 N ND1 . HIS A 1 48 ? 4.676 29.580 81.545 1.00 29.13 ? 48 HIS A ND1 1 ATOM 355 C CD2 . HIS A 1 48 ? 6.045 29.791 79.854 1.00 25.51 ? 48 HIS A CD2 1 ATOM 356 C CE1 . HIS A 1 48 ? 4.095 30.382 80.670 1.00 26.50 ? 48 HIS A CE1 1 ATOM 357 N NE2 . HIS A 1 48 ? 4.905 30.526 79.635 1.00 29.05 ? 48 HIS A NE2 1 ATOM 358 N N . LEU A 1 49 ? 4.663 26.420 80.168 1.00 17.56 ? 49 LEU A N 1 ATOM 359 C CA . LEU A 1 49 ? 4.159 26.036 78.860 1.00 19.48 ? 49 LEU A CA 1 ATOM 360 C C . LEU A 1 49 ? 3.735 27.322 78.157 1.00 21.22 ? 49 LEU A C 1 ATOM 361 O O . LEU A 1 49 ? 2.980 28.119 78.718 1.00 22.51 ? 49 LEU A O 1 ATOM 362 C CB . LEU A 1 49 ? 2.942 25.125 79.009 1.00 20.79 ? 49 LEU A CB 1 ATOM 363 C CG . LEU A 1 49 ? 2.254 24.744 77.698 1.00 21.86 ? 49 LEU A CG 1 ATOM 364 C CD1 . LEU A 1 49 ? 3.184 23.874 76.878 1.00 22.42 ? 49 LEU A CD1 1 ATOM 365 C CD2 . LEU A 1 49 ? 0.953 24.015 77.988 1.00 25.54 ? 49 LEU A CD2 1 ATOM 366 N N . ASP A 1 50 ? 4.223 27.534 76.940 1.00 20.62 ? 50 ASP A N 1 ATOM 367 C CA . ASP A 1 50 ? 3.867 28.734 76.201 1.00 21.89 ? 50 ASP A CA 1 ATOM 368 C C . ASP A 1 50 ? 3.204 28.406 74.872 1.00 20.88 ? 50 ASP A C 1 ATOM 369 O O . ASP A 1 50 ? 3.871 28.002 73.922 1.00 20.87 ? 50 ASP A O 1 ATOM 370 C CB . ASP A 1 50 ? 5.106 29.599 75.951 1.00 25.13 ? 50 ASP A CB 1 ATOM 371 C CG . ASP A 1 50 ? 4.750 30.990 75.449 1.00 32.51 ? 50 ASP A CG 1 ATOM 372 O OD1 . ASP A 1 50 ? 4.011 31.091 74.450 1.00 32.28 ? 50 ASP A OD1 1 ATOM 373 O OD2 . ASP A 1 50 ? 5.204 31.982 76.058 1.00 36.23 ? 50 ASP A OD2 1 ATOM 374 N N . LEU A 1 51 ? 1.886 28.573 74.813 1.00 18.94 ? 51 LEU A N 1 ATOM 375 C CA . LEU A 1 51 ? 1.156 28.310 73.585 1.00 20.18 ? 51 LEU A CA 1 ATOM 376 C C . LEU A 1 51 ? 0.667 29.618 72.956 1.00 19.37 ? 51 LEU A C 1 ATOM 377 O O . LEU A 1 51 ? -0.402 29.682 72.360 1.00 20.18 ? 51 LEU A O 1 ATOM 378 C CB . LEU A 1 51 ? -0.008 27.344 73.840 1.00 19.93 ? 51 LEU A CB 1 ATOM 379 C CG . LEU A 1 51 ? 0.432 25.930 74.255 1.00 20.69 ? 51 LEU A CG 1 ATOM 380 C CD1 . LEU A 1 51 ? -0.792 25.070 74.550 1.00 21.16 ? 51 LEU A CD1 1 ATOM 381 C CD2 . LEU A 1 51 ? 1.265 25.298 73.140 1.00 20.44 ? 51 LEU A CD2 1 ATOM 382 N N . SER A 1 52 ? 1.467 30.665 73.137 1.00 21.46 ? 52 SER A N 1 ATOM 383 C CA . SER A 1 52 ? 1.211 31.975 72.543 1.00 22.76 ? 52 SER A CA 1 ATOM 384 C C . SER A 1 52 ? -0.174 32.592 72.720 1.00 24.99 ? 52 SER A C 1 ATOM 385 O O . SER A 1 52 ? -0.670 33.272 71.817 1.00 26.01 ? 52 SER A O 1 ATOM 386 C CB . SER A 1 52 ? 1.529 31.903 71.051 1.00 22.90 ? 52 SER A CB 1 ATOM 387 O OG . SER A 1 52 ? 2.765 31.246 70.838 1.00 22.62 ? 52 SER A OG 1 ATOM 388 N N . GLY A 1 53 ? -0.801 32.366 73.867 1.00 25.54 ? 53 GLY A N 1 ATOM 389 C CA . GLY A 1 53 ? -2.112 32.947 74.088 1.00 27.57 ? 53 GLY A CA 1 ATOM 390 C C . GLY A 1 53 ? -3.294 32.110 73.640 1.00 29.15 ? 53 GLY A C 1 ATOM 391 O O . GLY A 1 53 ? -4.436 32.565 73.714 1.00 30.18 ? 53 GLY A O 1 ATOM 392 N N . HIS A 1 54 ? -3.038 30.898 73.158 1.00 28.25 ? 54 HIS A N 1 ATOM 393 C CA . HIS A 1 54 ? -4.123 30.017 72.737 1.00 29.15 ? 54 HIS A CA 1 ATOM 394 C C . HIS A 1 54 ? -5.000 29.711 73.955 1.00 30.59 ? 54 HIS A C 1 ATOM 395 O O . HIS A 1 54 ? -4.509 29.667 75.083 1.00 29.68 ? 54 HIS A O 1 ATOM 396 C CB . HIS A 1 54 ? -3.564 28.699 72.194 1.00 26.74 ? 54 HIS A CB 1 ATOM 397 C CG . HIS A 1 54 ? -3.295 28.703 70.721 1.00 24.23 ? 54 HIS A CG 1 ATOM 398 N ND1 . HIS A 1 54 ? -4.303 28.725 69.780 1.00 23.84 ? 54 HIS A ND1 1 ATOM 399 C CD2 . HIS A 1 54 ? -2.135 28.620 70.027 1.00 22.76 ? 54 HIS A CD2 1 ATOM 400 C CE1 . HIS A 1 54 ? -3.776 28.648 68.571 1.00 25.66 ? 54 HIS A CE1 1 ATOM 401 N NE2 . HIS A 1 54 ? -2.462 28.582 68.693 1.00 23.42 ? 54 HIS A NE2 1 ATOM 402 N N . ASP A 1 55 ? -6.292 29.495 73.725 1.00 33.40 ? 55 ASP A N 1 ATOM 403 C CA . ASP A 1 55 ? -7.212 29.172 74.813 1.00 35.83 ? 55 ASP A CA 1 ATOM 404 C C . ASP A 1 55 ? -6.921 27.757 75.300 1.00 35.35 ? 55 ASP A C 1 ATOM 405 O O . ASP A 1 55 ? -7.269 26.780 74.641 1.00 37.16 ? 55 ASP A O 1 ATOM 406 C CB . ASP A 1 55 ? -8.659 29.266 74.331 1.00 38.92 ? 55 ASP A CB 1 ATOM 407 C CG . ASP A 1 55 ? -9.656 28.844 75.392 1.00 42.81 ? 55 ASP A CG 1 ATOM 408 O OD1 . ASP A 1 55 ? -9.589 29.378 76.521 1.00 43.14 ? 55 ASP A OD1 1 ATOM 409 O OD2 . ASP A 1 55 ? -10.509 27.982 75.092 1.00 45.98 ? 55 ASP A OD2 1 ATOM 410 N N . LEU A 1 56 ? -6.284 27.654 76.459 1.00 34.98 ? 56 LEU A N 1 ATOM 411 C CA . LEU A 1 56 ? -5.916 26.361 77.025 1.00 35.25 ? 56 LEU A CA 1 ATOM 412 C C . LEU A 1 56 ? -7.093 25.502 77.468 1.00 35.46 ? 56 LEU A C 1 ATOM 413 O O . LEU A 1 56 ? -6.988 24.275 77.509 1.00 34.59 ? 56 LEU A O 1 ATOM 414 C CB . LEU A 1 56 ? -4.979 26.570 78.215 1.00 37.36 ? 56 LEU A CB 1 ATOM 415 C CG . LEU A 1 56 ? -3.676 27.318 77.932 1.00 38.96 ? 56 LEU A CG 1 ATOM 416 C CD1 . LEU A 1 56 ? -2.940 27.588 79.234 1.00 40.68 ? 56 LEU A CD1 1 ATOM 417 C CD2 . LEU A 1 56 ? -2.814 26.496 76.989 1.00 39.87 ? 56 LEU A CD2 1 ATOM 418 N N . SER A 1 57 ? -8.212 26.145 77.788 1.00 36.06 ? 57 SER A N 1 ATOM 419 C CA . SER A 1 57 ? -9.396 25.438 78.268 1.00 37.00 ? 57 SER A CA 1 ATOM 420 C C . SER A 1 57 ? -9.967 24.362 77.351 1.00 36.47 ? 57 SER A C 1 ATOM 421 O O . SER A 1 57 ? -10.576 23.405 77.829 1.00 35.84 ? 57 SER A O 1 ATOM 422 C CB . SER A 1 57 ? -10.499 26.442 78.614 1.00 38.03 ? 57 SER A CB 1 ATOM 423 O OG . SER A 1 57 ? -10.889 27.192 77.480 1.00 41.94 ? 57 SER A OG 1 ATOM 424 N N . SER A 1 58 ? -9.771 24.502 76.043 1.00 35.01 ? 58 SER A N 1 ATOM 425 C CA . SER A 1 58 ? -10.306 23.517 75.110 1.00 35.25 ? 58 SER A CA 1 ATOM 426 C C . SER A 1 58 ? -9.273 22.570 74.495 1.00 33.00 ? 58 SER A C 1 ATOM 427 O O . SER A 1 58 ? -9.629 21.698 73.703 1.00 33.19 ? 58 SER A O 1 ATOM 428 C CB . SER A 1 58 ? -11.062 24.228 73.985 1.00 38.22 ? 58 SER A CB 1 ATOM 429 O OG . SER A 1 58 ? -10.187 25.048 73.230 1.00 42.21 ? 58 SER A OG 1 ATOM 430 N N . VAL A 1 59 ? -8.004 22.721 74.864 1.00 30.83 ? 59 VAL A N 1 ATOM 431 C CA . VAL A 1 59 ? -6.954 21.869 74.303 1.00 28.00 ? 59 VAL A CA 1 ATOM 432 C C . VAL A 1 59 ? -7.108 20.383 74.625 1.00 27.84 ? 59 VAL A C 1 ATOM 433 O O . VAL A 1 59 ? -6.927 19.533 73.750 1.00 27.26 ? 59 VAL A O 1 ATOM 434 C CB . VAL A 1 59 ? -5.556 22.348 74.752 1.00 27.85 ? 59 VAL A CB 1 ATOM 435 C CG1 . VAL A 1 59 ? -4.478 21.425 74.194 1.00 27.01 ? 59 VAL A CG1 1 ATOM 436 C CG2 . VAL A 1 59 ? -5.327 23.773 74.269 1.00 26.60 ? 59 VAL A CG2 1 ATOM 437 N N . GLY A 1 60 ? -7.440 20.069 75.874 1.00 27.32 ? 60 GLY A N 1 ATOM 438 C CA . GLY A 1 60 ? -7.613 18.680 76.264 1.00 27.57 ? 60 GLY A CA 1 ATOM 439 C C . GLY A 1 60 ? -8.645 17.970 75.407 1.00 27.37 ? 60 GLY A C 1 ATOM 440 O O . GLY A 1 60 ? -8.404 16.868 74.908 1.00 26.93 ? 60 GLY A O 1 ATOM 441 N N . ALA A 1 61 ? -9.801 18.601 75.229 1.00 28.40 ? 61 ALA A N 1 ATOM 442 C CA . ALA A 1 61 ? -10.859 18.013 74.419 1.00 28.45 ? 61 ALA A CA 1 ATOM 443 C C . ALA A 1 61 ? -10.395 17.866 72.973 1.00 28.02 ? 61 ALA A C 1 ATOM 444 O O . ALA A 1 61 ? -10.671 16.854 72.331 1.00 29.12 ? 61 ALA A O 1 ATOM 445 C CB . ALA A 1 61 ? -12.116 18.878 74.483 1.00 29.06 ? 61 ALA A CB 1 ATOM 446 N N . ASP A 1 62 ? -9.688 18.874 72.465 1.00 27.60 ? 62 ASP A N 1 ATOM 447 C CA . ASP A 1 62 ? -9.195 18.840 71.091 1.00 27.65 ? 62 ASP A CA 1 ATOM 448 C C . ASP A 1 62 ? -8.173 17.728 70.883 1.00 27.03 ? 62 ASP A C 1 ATOM 449 O O . ASP A 1 62 ? -8.147 17.094 69.831 1.00 27.49 ? 62 ASP A O 1 ATOM 450 C CB . ASP A 1 62 ? -8.575 20.188 70.705 1.00 30.05 ? 62 ASP A CB 1 ATOM 451 C CG . ASP A 1 62 ? -9.609 21.291 70.576 1.00 31.11 ? 62 ASP A CG 1 ATOM 452 O OD1 . ASP A 1 62 ? -10.818 20.981 70.604 1.00 34.85 ? 62 ASP A OD1 1 ATOM 453 O OD2 . ASP A 1 62 ? -9.215 22.470 70.436 1.00 33.00 ? 62 ASP A OD2 1 ATOM 454 N N . ILE A 1 63 ? -7.327 17.501 71.884 1.00 27.15 ? 63 ILE A N 1 ATOM 455 C CA . ILE A 1 63 ? -6.317 16.454 71.803 1.00 25.42 ? 63 ILE A CA 1 ATOM 456 C C . ILE A 1 63 ? -7.003 15.103 71.631 1.00 26.94 ? 63 ILE A C 1 ATOM 457 O O . ILE A 1 63 ? -6.673 14.339 70.726 1.00 24.80 ? 63 ILE A O 1 ATOM 458 C CB . ILE A 1 63 ? -5.452 16.404 73.079 1.00 25.34 ? 63 ILE A CB 1 ATOM 459 C CG1 . ILE A 1 63 ? -4.546 17.635 73.145 1.00 23.79 ? 63 ILE A CG1 1 ATOM 460 C CG2 . ILE A 1 63 ? -4.633 15.119 73.106 1.00 25.14 ? 63 ILE A CG2 1 ATOM 461 C CD1 . ILE A 1 63 ? -3.780 17.763 74.461 1.00 21.56 ? 63 ILE A CD1 1 ATOM 462 N N . LYS A 1 64 ? -7.961 14.814 72.507 1.00 27.35 ? 64 LYS A N 1 ATOM 463 C CA . LYS A 1 64 ? -8.679 13.550 72.442 1.00 29.63 ? 64 LYS A CA 1 ATOM 464 C C . LYS A 1 64 ? -9.409 13.419 71.108 1.00 29.70 ? 64 LYS A C 1 ATOM 465 O O . LYS A 1 64 ? -9.468 12.334 70.528 1.00 29.11 ? 64 LYS A O 1 ATOM 466 C CB . LYS A 1 64 ? -9.650 13.434 73.627 1.00 30.06 ? 64 LYS A CB 1 ATOM 467 C CG . LYS A 1 64 ? -8.921 13.390 74.975 1.00 32.50 ? 64 LYS A CG 1 ATOM 468 C CD . LYS A 1 64 ? -9.840 13.085 76.149 1.00 33.82 ? 64 LYS A CD 1 ATOM 469 C CE . LYS A 1 64 ? -10.779 14.235 76.457 1.00 35.71 ? 64 LYS A CE 1 ATOM 470 N NZ . LYS A 1 64 ? -11.586 13.936 77.676 1.00 37.23 ? 64 LYS A NZ 1 ATOM 471 N N . HIS A 1 65 ? -9.942 14.528 70.610 1.00 30.71 ? 65 HIS A N 1 ATOM 472 C CA . HIS A 1 65 ? -10.633 14.513 69.326 1.00 32.05 ? 65 HIS A CA 1 ATOM 473 C C . HIS A 1 65 ? -9.641 14.169 68.216 1.00 32.68 ? 65 HIS A C 1 ATOM 474 O O . HIS A 1 65 ? -9.947 13.383 67.320 1.00 33.03 ? 65 HIS A O 1 ATOM 475 C CB . HIS A 1 65 ? -11.281 15.870 69.047 1.00 33.40 ? 65 HIS A CB 1 ATOM 476 C CG . HIS A 1 65 ? -11.952 15.952 67.711 1.00 36.01 ? 65 HIS A CG 1 ATOM 477 N ND1 . HIS A 1 65 ? -11.265 16.229 66.549 1.00 36.51 ? 65 HIS A ND1 1 ATOM 478 C CD2 . HIS A 1 65 ? -13.241 15.751 67.348 1.00 36.93 ? 65 HIS A CD2 1 ATOM 479 C CE1 . HIS A 1 65 ? -12.102 16.197 65.528 1.00 36.92 ? 65 HIS A CE1 1 ATOM 480 N NE2 . HIS A 1 65 ? -13.307 15.908 65.985 1.00 38.34 ? 65 HIS A NE2 1 ATOM 481 N N . CYS A 1 66 ? -8.450 14.760 68.277 1.00 32.67 ? 66 CYS A N 1 ATOM 482 C CA . CYS A 1 66 ? -7.420 14.490 67.278 1.00 30.77 ? 66 CYS A CA 1 ATOM 483 C C . CYS A 1 66 ? -7.079 13.007 67.264 1.00 30.21 ? 66 CYS A C 1 ATOM 484 O O . CYS A 1 66 ? -6.995 12.384 66.205 1.00 28.28 ? 66 CYS A O 1 ATOM 485 C CB . CYS A 1 66 ? -6.148 15.284 67.586 1.00 30.83 ? 66 CYS A CB 1 ATOM 486 S SG . CYS A 1 66 ? -6.243 17.073 67.266 1.00 31.97 ? 66 CYS A SG 1 ATOM 487 N N . GLN A 1 67 ? -6.875 12.451 68.452 1.00 28.65 ? 67 GLN A N 1 ATOM 488 C CA . GLN A 1 67 ? -6.525 11.046 68.591 1.00 29.91 ? 67 GLN A CA 1 ATOM 489 C C . GLN A 1 67 ? -7.616 10.120 68.061 1.00 30.97 ? 67 GLN A C 1 ATOM 490 O O . GLN A 1 67 ? -7.318 9.065 67.503 1.00 31.44 ? 67 GLN A O 1 ATOM 491 C CB . GLN A 1 67 ? -6.222 10.735 70.059 1.00 29.27 ? 67 GLN A CB 1 ATOM 492 C CG . GLN A 1 67 ? -5.143 11.644 70.638 1.00 28.87 ? 67 GLN A CG 1 ATOM 493 C CD . GLN A 1 67 ? -4.869 11.389 72.106 1.00 30.25 ? 67 GLN A CD 1 ATOM 494 O OE1 . GLN A 1 67 ? -5.793 11.204 72.899 1.00 28.98 ? 67 GLN A OE1 1 ATOM 495 N NE2 . GLN A 1 67 ? -3.593 11.399 72.480 1.00 28.53 ? 67 GLN A NE2 1 ATOM 496 N N . SER A 1 68 ? -8.873 10.522 68.224 1.00 33.27 ? 68 SER A N 1 ATOM 497 C CA . SER A 1 68 ? -9.990 9.711 67.750 1.00 35.06 ? 68 SER A CA 1 ATOM 498 C C . SER A 1 68 ? -10.008 9.693 66.224 1.00 36.10 ? 68 SER A C 1 ATOM 499 O O . SER A 1 68 ? -10.598 8.805 65.611 1.00 37.17 ? 68 SER A O 1 ATOM 500 C CB . SER A 1 68 ? -11.321 10.263 68.271 1.00 34.34 ? 68 SER A CB 1 ATOM 501 O OG . SER A 1 68 ? -11.725 11.413 67.548 1.00 35.96 ? 68 SER A OG 1 ATOM 502 N N . LYS A 1 69 ? -9.362 10.680 65.613 1.00 36.55 ? 69 LYS A N 1 ATOM 503 C CA . LYS A 1 69 ? -9.303 10.756 64.160 1.00 36.15 ? 69 LYS A CA 1 ATOM 504 C C . LYS A 1 69 ? -7.998 10.164 63.645 1.00 35.04 ? 69 LYS A C 1 ATOM 505 O O . LYS A 1 69 ? -7.699 10.239 62.455 1.00 36.46 ? 69 LYS A O 1 ATOM 506 C CB . LYS A 1 69 ? -9.444 12.206 63.693 1.00 37.83 ? 69 LYS A CB 1 ATOM 507 C CG . LYS A 1 69 ? -10.805 12.814 63.994 1.00 39.87 ? 69 LYS A CG 1 ATOM 508 C CD . LYS A 1 69 ? -11.915 11.979 63.373 1.00 41.67 ? 69 LYS A CD 1 ATOM 509 C CE . LYS A 1 69 ? -13.291 12.495 63.759 1.00 43.61 ? 69 LYS A CE 1 ATOM 510 N NZ . LYS A 1 69 ? -14.367 11.593 63.256 1.00 44.69 ? 69 LYS A NZ 1 ATOM 511 N N . GLY A 1 70 ? -7.221 9.581 64.552 1.00 33.41 ? 70 GLY A N 1 ATOM 512 C CA . GLY A 1 70 ? -5.964 8.966 64.168 1.00 31.68 ? 70 GLY A CA 1 ATOM 513 C C . GLY A 1 70 ? -4.787 9.917 64.039 1.00 30.43 ? 70 GLY A C 1 ATOM 514 O O . GLY A 1 70 ? -3.761 9.558 63.463 1.00 30.51 ? 70 GLY A O 1 ATOM 515 N N . VAL A 1 71 ? -4.931 11.128 64.567 1.00 28.47 ? 71 VAL A N 1 ATOM 516 C CA . VAL A 1 71 ? -3.857 12.114 64.509 1.00 27.15 ? 71 VAL A CA 1 ATOM 517 C C . VAL A 1 71 ? -3.254 12.303 65.894 1.00 25.70 ? 71 VAL A C 1 ATOM 518 O O . VAL A 1 71 ? -3.859 12.936 66.757 1.00 26.87 ? 71 VAL A O 1 ATOM 519 C CB . VAL A 1 71 ? -4.367 13.488 64.025 1.00 27.66 ? 71 VAL A CB 1 ATOM 520 C CG1 . VAL A 1 71 ? -3.206 14.484 63.988 1.00 26.22 ? 71 VAL A CG1 1 ATOM 521 C CG2 . VAL A 1 71 ? -5.009 13.358 62.649 1.00 28.15 ? 71 VAL A CG2 1 ATOM 522 N N . PRO A 1 72 ? -2.058 11.746 66.130 1.00 24.92 ? 72 PRO A N 1 ATOM 523 C CA . PRO A 1 72 ? -1.423 11.893 67.440 1.00 23.79 ? 72 PRO A CA 1 ATOM 524 C C . PRO A 1 72 ? -0.954 13.325 67.674 1.00 23.57 ? 72 PRO A C 1 ATOM 525 O O . PRO A 1 72 ? -0.661 14.054 66.722 1.00 22.19 ? 72 PRO A O 1 ATOM 526 C CB . PRO A 1 72 ? -0.271 10.898 67.377 1.00 24.36 ? 72 PRO A CB 1 ATOM 527 C CG . PRO A 1 72 ? 0.095 10.900 65.922 1.00 26.95 ? 72 PRO A CG 1 ATOM 528 C CD . PRO A 1 72 ? -1.252 10.886 65.244 1.00 25.43 ? 72 PRO A CD 1 ATOM 529 N N . VAL A 1 73 ? -0.898 13.719 68.943 1.00 21.59 ? 73 VAL A N 1 ATOM 530 C CA . VAL A 1 73 ? -0.472 15.060 69.322 1.00 20.09 ? 73 VAL A CA 1 ATOM 531 C C . VAL A 1 73 ? 0.760 14.954 70.222 1.00 20.36 ? 73 VAL A C 1 ATOM 532 O O . VAL A 1 73 ? 0.777 14.200 71.197 1.00 21.33 ? 73 VAL A O 1 ATOM 533 C CB . VAL A 1 73 ? -1.612 15.805 70.053 1.00 20.97 ? 73 VAL A CB 1 ATOM 534 C CG1 . VAL A 1 73 ? -1.167 17.213 70.452 1.00 19.38 ? 73 VAL A CG1 1 ATOM 535 C CG2 . VAL A 1 73 ? -2.838 15.881 69.140 1.00 19.08 ? 73 VAL A CG2 1 ATOM 536 N N . SER A 1 74 ? 1.801 15.704 69.879 1.00 19.23 ? 74 SER A N 1 ATOM 537 C CA . SER A 1 74 ? 3.044 15.680 70.638 1.00 16.78 ? 74 SER A CA 1 ATOM 538 C C . SER A 1 74 ? 3.297 17.041 71.269 1.00 17.61 ? 74 SER A C 1 ATOM 539 O O . SER A 1 74 ? 2.652 18.024 70.909 1.00 16.23 ? 74 SER A O 1 ATOM 540 C CB . SER A 1 74 ? 4.207 15.319 69.705 1.00 20.88 ? 74 SER A CB 1 ATOM 541 O OG . SER A 1 74 ? 5.445 15.297 70.399 1.00 25.63 ? 74 SER A OG 1 ATOM 542 N N . LEU A 1 75 ? 4.234 17.082 72.211 1.00 16.87 ? 75 LEU A N 1 ATOM 543 C CA . LEU A 1 75 ? 4.602 18.323 72.886 1.00 16.55 ? 75 LEU A CA 1 ATOM 544 C C . LEU A 1 75 ? 6.089 18.550 72.680 1.00 16.90 ? 75 LEU A C 1 ATOM 545 O O . LEU A 1 75 ? 6.901 17.696 73.031 1.00 16.69 ? 75 LEU A O 1 ATOM 546 C CB . LEU A 1 75 ? 4.332 18.233 74.391 1.00 16.44 ? 75 LEU A CB 1 ATOM 547 C CG . LEU A 1 75 ? 4.870 19.421 75.205 1.00 16.48 ? 75 LEU A CG 1 ATOM 548 C CD1 . LEU A 1 75 ? 4.208 20.698 74.717 1.00 16.70 ? 75 LEU A CD1 1 ATOM 549 C CD2 . LEU A 1 75 ? 4.618 19.215 76.690 1.00 18.85 ? 75 LEU A CD2 1 ATOM 550 N N . SER A 1 76 ? 6.449 19.693 72.108 1.00 15.72 ? 76 SER A N 1 ATOM 551 C CA . SER A 1 76 ? 7.856 20.013 71.905 1.00 14.39 ? 76 SER A CA 1 ATOM 552 C C . SER A 1 76 ? 8.342 20.856 73.084 1.00 15.39 ? 76 SER A C 1 ATOM 553 O O . SER A 1 76 ? 7.634 21.756 73.546 1.00 15.06 ? 76 SER A O 1 ATOM 554 C CB . SER A 1 76 ? 8.045 20.802 70.606 1.00 14.53 ? 76 SER A CB 1 ATOM 555 O OG . SER A 1 76 ? 9.421 21.025 70.347 1.00 16.79 ? 76 SER A OG 1 ATOM 556 N N . ILE A 1 77 ? 9.542 20.562 73.570 1.00 12.97 ? 77 ILE A N 1 ATOM 557 C CA . ILE A 1 77 ? 10.112 21.316 74.680 1.00 15.08 ? 77 ILE A CA 1 ATOM 558 C C . ILE A 1 77 ? 11.354 22.038 74.185 1.00 16.09 ? 77 ILE A C 1 ATOM 559 O O . ILE A 1 77 ? 12.062 21.547 73.303 1.00 14.67 ? 77 ILE A O 1 ATOM 560 C CB . ILE A 1 77 ? 10.473 20.400 75.877 1.00 15.80 ? 77 ILE A CB 1 ATOM 561 C CG1 . ILE A 1 77 ? 11.705 19.548 75.556 1.00 18.78 ? 77 ILE A CG1 1 ATOM 562 C CG2 . ILE A 1 77 ? 9.278 19.535 76.228 1.00 18.36 ? 77 ILE A CG2 1 ATOM 563 C CD1 . ILE A 1 77 ? 12.229 18.757 76.762 1.00 19.04 ? 77 ILE A CD1 1 ATOM 564 N N . GLY A 1 78 ? 11.611 23.220 74.739 1.00 15.10 ? 78 GLY A N 1 ATOM 565 C CA . GLY A 1 78 ? 12.765 23.981 74.308 1.00 15.02 ? 78 GLY A CA 1 ATOM 566 C C . GLY A 1 78 ? 12.298 25.205 73.553 1.00 15.94 ? 78 GLY A C 1 ATOM 567 O O . GLY A 1 78 ? 11.525 26.002 74.093 1.00 15.33 ? 78 GLY A O 1 ATOM 568 N N . GLY A 1 79 ? 12.746 25.343 72.308 1.00 15.04 ? 79 GLY A N 1 ATOM 569 C CA . GLY A 1 79 ? 12.366 26.487 71.496 1.00 15.40 ? 79 GLY A CA 1 ATOM 570 C C . GLY A 1 79 ? 13.551 27.405 71.256 1.00 15.23 ? 79 GLY A C 1 ATOM 571 O O . GLY A 1 79 ? 14.686 27.049 71.568 1.00 16.56 ? 79 GLY A O 1 ATOM 572 N N . TYR A 1 80 ? 13.294 28.591 70.709 1.00 14.92 ? 80 TYR A N 1 ATOM 573 C CA . TYR A 1 80 ? 14.370 29.538 70.429 1.00 16.47 ? 80 TYR A CA 1 ATOM 574 C C . TYR A 1 80 ? 14.742 30.402 71.630 1.00 17.62 ? 80 TYR A C 1 ATOM 575 O O . TYR A 1 80 ? 15.717 31.156 71.574 1.00 18.49 ? 80 TYR A O 1 ATOM 576 C CB . TYR A 1 80 ? 13.980 30.455 69.266 1.00 15.43 ? 80 TYR A CB 1 ATOM 577 C CG . TYR A 1 80 ? 13.822 29.759 67.934 1.00 16.74 ? 80 TYR A CG 1 ATOM 578 C CD1 . TYR A 1 80 ? 12.557 29.451 67.433 1.00 17.70 ? 80 TYR A CD1 1 ATOM 579 C CD2 . TYR A 1 80 ? 14.934 29.458 67.148 1.00 16.66 ? 80 TYR A CD2 1 ATOM 580 C CE1 . TYR A 1 80 ? 12.402 28.870 66.177 1.00 18.82 ? 80 TYR A CE1 1 ATOM 581 C CE2 . TYR A 1 80 ? 14.790 28.874 65.887 1.00 16.09 ? 80 TYR A CE2 1 ATOM 582 C CZ . TYR A 1 80 ? 13.521 28.588 65.411 1.00 16.83 ? 80 TYR A CZ 1 ATOM 583 O OH . TYR A 1 80 ? 13.359 28.042 64.161 1.00 19.74 ? 80 TYR A OH 1 ATOM 584 N N . GLY A 1 81 ? 13.975 30.282 72.710 1.00 17.77 ? 81 GLY A N 1 ATOM 585 C CA . GLY A 1 81 ? 14.226 31.070 73.911 1.00 18.00 ? 81 GLY A CA 1 ATOM 586 C C . GLY A 1 81 ? 15.412 30.667 74.769 1.00 18.40 ? 81 GLY A C 1 ATOM 587 O O . GLY A 1 81 ? 16.092 29.684 74.495 1.00 18.76 ? 81 GLY A O 1 ATOM 588 N N . THR A 1 82 ? 15.648 31.419 75.841 1.00 17.44 ? 82 THR A N 1 ATOM 589 C CA . THR A 1 82 ? 16.783 31.159 76.723 1.00 17.97 ? 82 THR A CA 1 ATOM 590 C C . THR A 1 82 ? 16.360 30.776 78.139 1.00 18.47 ? 82 THR A C 1 ATOM 591 O O . THR A 1 82 ? 17.155 30.870 79.069 1.00 20.94 ? 82 THR A O 1 ATOM 592 C CB . THR A 1 82 ? 17.676 32.408 76.824 1.00 21.81 ? 82 THR A CB 1 ATOM 593 O OG1 . THR A 1 82 ? 16.874 33.521 77.245 1.00 22.33 ? 82 THR A OG1 1 ATOM 594 C CG2 . THR A 1 82 ? 18.304 32.735 75.473 1.00 25.12 ? 82 THR A CG2 1 ATOM 595 N N . GLY A 1 83 ? 15.119 30.328 78.303 1.00 18.01 ? 83 GLY A N 1 ATOM 596 C CA . GLY A 1 83 ? 14.652 29.982 79.635 1.00 18.57 ? 83 GLY A CA 1 ATOM 597 C C . GLY A 1 83 ? 14.738 28.523 80.042 1.00 18.46 ? 83 GLY A C 1 ATOM 598 O O . GLY A 1 83 ? 14.080 28.116 80.998 1.00 18.67 ? 83 GLY A O 1 ATOM 599 N N . TYR A 1 84 ? 15.555 27.737 79.350 1.00 17.05 ? 84 TYR A N 1 ATOM 600 C CA . TYR A 1 84 ? 15.660 26.317 79.679 1.00 17.22 ? 84 TYR A CA 1 ATOM 601 C C . TYR A 1 84 ? 17.068 25.737 79.615 1.00 17.06 ? 84 TYR A C 1 ATOM 602 O O . TYR A 1 84 ? 17.946 26.245 78.921 1.00 17.09 ? 84 TYR A O 1 ATOM 603 C CB . TYR A 1 84 ? 14.731 25.514 78.756 1.00 14.08 ? 84 TYR A CB 1 ATOM 604 C CG . TYR A 1 84 ? 15.135 25.543 77.300 1.00 15.64 ? 84 TYR A CG 1 ATOM 605 C CD1 . TYR A 1 84 ? 16.116 24.678 76.809 1.00 16.29 ? 84 TYR A CD1 1 ATOM 606 C CD2 . TYR A 1 84 ? 14.556 26.455 76.413 1.00 15.97 ? 84 TYR A CD2 1 ATOM 607 C CE1 . TYR A 1 84 ? 16.512 24.720 75.473 1.00 17.03 ? 84 TYR A CE1 1 ATOM 608 C CE2 . TYR A 1 84 ? 14.945 26.504 75.075 1.00 15.62 ? 84 TYR A CE2 1 ATOM 609 C CZ . TYR A 1 84 ? 15.924 25.635 74.614 1.00 15.74 ? 84 TYR A CZ 1 ATOM 610 O OH . TYR A 1 84 ? 16.321 25.686 73.300 1.00 17.10 ? 84 TYR A OH 1 ATOM 611 N N . SER A 1 85 ? 17.261 24.652 80.357 1.00 16.71 ? 85 SER A N 1 ATOM 612 C CA . SER A 1 85 ? 18.527 23.937 80.408 1.00 19.20 ? 85 SER A CA 1 ATOM 613 C C . SER A 1 85 ? 18.244 22.653 81.186 1.00 18.83 ? 85 SER A C 1 ATOM 614 O O . SER A 1 85 ? 17.176 22.508 81.780 1.00 18.14 ? 85 SER A O 1 ATOM 615 C CB . SER A 1 85 ? 19.594 24.765 81.128 1.00 19.24 ? 85 SER A CB 1 ATOM 616 O OG . SER A 1 85 ? 19.268 24.945 82.492 1.00 22.34 ? 85 SER A OG 1 ATOM 617 N N . LEU A 1 86 ? 19.191 21.725 81.183 1.00 21.29 ? 86 LEU A N 1 ATOM 618 C CA . LEU A 1 86 ? 19.010 20.461 81.898 1.00 19.33 ? 86 LEU A CA 1 ATOM 619 C C . LEU A 1 86 ? 20.419 20.014 82.291 1.00 20.42 ? 86 LEU A C 1 ATOM 620 O O . LEU A 1 86 ? 20.897 18.969 81.858 1.00 20.28 ? 86 LEU A O 1 ATOM 621 C CB . LEU A 1 86 ? 18.359 19.452 80.953 1.00 19.90 ? 86 LEU A CB 1 ATOM 622 C CG . LEU A 1 86 ? 17.534 18.323 81.568 1.00 18.88 ? 86 LEU A CG 1 ATOM 623 C CD1 . LEU A 1 86 ? 16.355 18.897 82.345 1.00 19.45 ? 86 LEU A CD1 1 ATOM 624 C CD2 . LEU A 1 86 ? 17.038 17.412 80.447 1.00 20.41 ? 86 LEU A CD2 1 ATOM 625 N N . PRO A 1 87 ? 21.086 20.799 83.150 1.00 21.47 ? 87 PRO A N 1 ATOM 626 C CA . PRO A 1 87 ? 22.450 20.583 83.644 1.00 21.74 ? 87 PRO A CA 1 ATOM 627 C C . PRO A 1 87 ? 22.792 19.417 84.565 1.00 22.26 ? 87 PRO A C 1 ATOM 628 O O . PRO A 1 87 ? 23.877 19.403 85.144 1.00 24.69 ? 87 PRO A O 1 ATOM 629 C CB . PRO A 1 87 ? 22.778 21.921 84.292 1.00 21.91 ? 87 PRO A CB 1 ATOM 630 C CG . PRO A 1 87 ? 21.488 22.271 84.923 1.00 22.77 ? 87 PRO A CG 1 ATOM 631 C CD . PRO A 1 87 ? 20.485 21.970 83.820 1.00 22.17 ? 87 PRO A CD 1 ATOM 632 N N . SER A 1 88 ? 21.906 18.443 84.710 1.00 22.73 ? 88 SER A N 1 ATOM 633 C CA . SER A 1 88 ? 22.222 17.310 85.579 1.00 23.75 ? 88 SER A CA 1 ATOM 634 C C . SER A 1 88 ? 21.273 16.144 85.378 1.00 24.05 ? 88 SER A C 1 ATOM 635 O O . SER A 1 88 ? 20.189 16.310 84.824 1.00 22.00 ? 88 SER A O 1 ATOM 636 C CB . SER A 1 88 ? 22.183 17.734 87.047 1.00 23.48 ? 88 SER A CB 1 ATOM 637 O OG . SER A 1 88 ? 20.867 18.061 87.454 1.00 23.07 ? 88 SER A OG 1 ATOM 638 N N . ASN A 1 89 ? 21.692 14.964 85.834 1.00 25.00 ? 89 ASN A N 1 ATOM 639 C CA . ASN A 1 89 ? 20.864 13.770 85.729 1.00 26.98 ? 89 ASN A CA 1 ATOM 640 C C . ASN A 1 89 ? 19.587 14.002 86.529 1.00 25.50 ? 89 ASN A C 1 ATOM 641 O O . ASN A 1 89 ? 18.496 13.644 86.092 1.00 24.68 ? 89 ASN A O 1 ATOM 642 C CB . ASN A 1 89 ? 21.609 12.541 86.283 1.00 30.96 ? 89 ASN A CB 1 ATOM 643 C CG . ASN A 1 89 ? 22.713 12.053 85.357 1.00 35.37 ? 89 ASN A CG 1 ATOM 644 O OD1 . ASN A 1 89 ? 23.047 12.718 84.378 1.00 36.57 ? 89 ASN A OD1 1 ATOM 645 N ND2 . ASN A 1 89 ? 23.286 10.892 85.668 1.00 40.22 ? 89 ASN A ND2 1 ATOM 646 N N . ARG A 1 90 ? 19.732 14.615 87.699 1.00 26.65 ? 90 ARG A N 1 ATOM 647 C CA . ARG A 1 90 ? 18.595 14.898 88.564 1.00 27.30 ? 90 ARG A CA 1 ATOM 648 C C . ARG A 1 90 ? 17.590 15.818 87.871 1.00 25.31 ? 90 ARG A C 1 ATOM 649 O O . ARG A 1 90 ? 16.390 15.553 87.887 1.00 25.58 ? 90 ARG A O 1 ATOM 650 C CB . ARG A 1 90 ? 19.068 15.545 89.869 1.00 30.60 ? 90 ARG A CB 1 ATOM 651 C CG . ARG A 1 90 ? 17.941 15.989 90.805 1.00 37.26 ? 90 ARG A CG 1 ATOM 652 C CD . ARG A 1 90 ? 17.376 14.838 91.632 1.00 43.10 ? 90 ARG A CD 1 ATOM 653 N NE . ARG A 1 90 ? 16.644 13.853 90.840 1.00 48.21 ? 90 ARG A NE 1 ATOM 654 C CZ . ARG A 1 90 ? 16.107 12.744 91.344 1.00 50.18 ? 90 ARG A CZ 1 ATOM 655 N NH1 . ARG A 1 90 ? 16.222 12.479 92.638 1.00 51.59 ? 90 ARG A NH1 1 ATOM 656 N NH2 . ARG A 1 90 ? 15.454 11.899 90.557 1.00 50.77 ? 90 ARG A NH2 1 ATOM 657 N N . SER A 1 91 ? 18.069 16.900 87.265 1.00 23.52 ? 91 SER A N 1 ATOM 658 C CA . SER A 1 91 ? 17.151 17.815 86.586 1.00 22.01 ? 91 SER A CA 1 ATOM 659 C C . SER A 1 91 ? 16.453 17.113 85.422 1.00 19.40 ? 91 SER A C 1 ATOM 660 O O . SER A 1 91 ? 15.283 17.371 85.145 1.00 16.44 ? 91 SER A O 1 ATOM 661 C CB . SER A 1 91 ? 17.887 19.069 86.088 1.00 21.75 ? 91 SER A CB 1 ATOM 662 O OG . SER A 1 91 ? 18.852 18.765 85.098 1.00 27.01 ? 91 SER A OG 1 ATOM 663 N N . ALA A 1 92 ? 17.162 16.217 84.743 1.00 20.76 ? 92 ALA A N 1 ATOM 664 C CA . ALA A 1 92 ? 16.558 15.498 83.624 1.00 19.23 ? 92 ALA A CA 1 ATOM 665 C C . ALA A 1 92 ? 15.433 14.601 84.123 1.00 19.78 ? 92 ALA A C 1 ATOM 666 O O . ALA A 1 92 ? 14.363 14.541 83.519 1.00 19.50 ? 92 ALA A O 1 ATOM 667 C CB . ALA A 1 92 ? 17.605 14.662 82.894 1.00 19.01 ? 92 ALA A CB 1 ATOM 668 N N . LEU A 1 93 ? 15.677 13.899 85.225 1.00 19.86 ? 93 LEU A N 1 ATOM 669 C CA . LEU A 1 93 ? 14.664 13.012 85.780 1.00 20.56 ? 93 LEU A CA 1 ATOM 670 C C . LEU A 1 93 ? 13.481 13.793 86.340 1.00 20.29 ? 93 LEU A C 1 ATOM 671 O O . LEU A 1 93 ? 12.344 13.324 86.276 1.00 19.88 ? 93 LEU A O 1 ATOM 672 C CB . LEU A 1 93 ? 15.269 12.121 86.872 1.00 24.48 ? 93 LEU A CB 1 ATOM 673 C CG . LEU A 1 93 ? 16.329 11.120 86.404 1.00 28.14 ? 93 LEU A CG 1 ATOM 674 C CD1 . LEU A 1 93 ? 16.882 10.373 87.608 1.00 30.48 ? 93 LEU A CD1 1 ATOM 675 C CD2 . LEU A 1 93 ? 15.727 10.153 85.397 1.00 28.16 ? 93 LEU A CD2 1 ATOM 676 N N . ASP A 1 94 ? 13.739 14.978 86.896 1.00 19.92 ? 94 ASP A N 1 ATOM 677 C CA . ASP A 1 94 ? 12.653 15.795 87.434 1.00 20.46 ? 94 ASP A CA 1 ATOM 678 C C . ASP A 1 94 ? 11.765 16.283 86.295 1.00 18.45 ? 94 ASP A C 1 ATOM 679 O O . ASP A 1 94 ? 10.542 16.373 86.441 1.00 20.03 ? 94 ASP A O 1 ATOM 680 C CB . ASP A 1 94 ? 13.191 17.003 88.211 1.00 22.18 ? 94 ASP A CB 1 ATOM 681 C CG . ASP A 1 94 ? 13.760 16.621 89.567 1.00 28.12 ? 94 ASP A CG 1 ATOM 682 O OD1 . ASP A 1 94 ? 13.378 15.552 90.093 1.00 29.69 ? 94 ASP A OD1 1 ATOM 683 O OD2 . ASP A 1 94 ? 14.575 17.395 90.114 1.00 28.11 ? 94 ASP A OD2 1 ATOM 684 N N . LEU A 1 95 ? 12.382 16.599 85.161 1.00 16.66 ? 95 LEU A N 1 ATOM 685 C CA . LEU A 1 95 ? 11.620 17.056 84.009 1.00 16.66 ? 95 LEU A CA 1 ATOM 686 C C . LEU A 1 95 ? 10.780 15.897 83.489 1.00 16.90 ? 95 LEU A C 1 ATOM 687 O O . LEU A 1 95 ? 9.624 16.081 83.102 1.00 15.96 ? 95 LEU A O 1 ATOM 688 C CB . LEU A 1 95 ? 12.553 17.581 82.909 1.00 17.37 ? 95 LEU A CB 1 ATOM 689 C CG . LEU A 1 95 ? 11.895 17.910 81.562 1.00 16.25 ? 95 LEU A CG 1 ATOM 690 C CD1 . LEU A 1 95 ? 10.749 18.896 81.755 1.00 17.20 ? 95 LEU A CD1 1 ATOM 691 C CD2 . LEU A 1 95 ? 12.946 18.475 80.615 1.00 16.67 ? 95 LEU A CD2 1 ATOM 692 N N . PHE A 1 96 ? 11.350 14.695 83.474 1.00 17.02 ? 96 PHE A N 1 ATOM 693 C CA . PHE A 1 96 ? 10.571 13.556 83.012 1.00 17.88 ? 96 PHE A CA 1 ATOM 694 C C . PHE A 1 96 ? 9.353 13.409 83.917 1.00 16.53 ? 96 PHE A C 1 ATOM 695 O O . PHE A 1 96 ? 8.227 13.264 83.440 1.00 16.46 ? 96 PHE A O 1 ATOM 696 C CB . PHE A 1 96 ? 11.353 12.241 83.059 1.00 19.52 ? 96 PHE A CB 1 ATOM 697 C CG . PHE A 1 96 ? 10.473 11.044 82.832 1.00 20.42 ? 96 PHE A CG 1 ATOM 698 C CD1 . PHE A 1 96 ? 10.053 10.708 81.547 1.00 20.08 ? 96 PHE A CD1 1 ATOM 699 C CD2 . PHE A 1 96 ? 9.940 10.346 83.915 1.00 20.81 ? 96 PHE A CD2 1 ATOM 700 C CE1 . PHE A 1 96 ? 9.106 9.701 81.341 1.00 21.99 ? 96 PHE A CE1 1 ATOM 701 C CE2 . PHE A 1 96 ? 8.997 9.343 83.722 1.00 20.84 ? 96 PHE A CE2 1 ATOM 702 C CZ . PHE A 1 96 ? 8.577 9.020 82.434 1.00 21.51 ? 96 PHE A CZ 1 ATOM 703 N N . ASP A 1 97 ? 9.579 13.445 85.229 1.00 19.53 ? 97 ASP A N 1 ATOM 704 C CA . ASP A 1 97 ? 8.471 13.310 86.172 1.00 21.60 ? 97 ASP A CA 1 ATOM 705 C C . ASP A 1 97 ? 7.405 14.357 85.914 1.00 20.31 ? 97 ASP A C 1 ATOM 706 O O . ASP A 1 97 ? 6.213 14.049 85.905 1.00 19.68 ? 97 ASP A O 1 ATOM 707 C CB . ASP A 1 97 ? 8.951 13.427 87.623 1.00 24.02 ? 97 ASP A CB 1 ATOM 708 C CG . ASP A 1 97 ? 9.696 12.194 88.091 1.00 27.84 ? 97 ASP A CG 1 ATOM 709 O OD1 . ASP A 1 97 ? 9.484 11.110 87.505 1.00 29.92 ? 97 ASP A OD1 1 ATOM 710 O OD2 . ASP A 1 97 ? 10.483 12.307 89.053 1.00 32.93 ? 97 ASP A OD2 1 ATOM 711 N N . HIS A 1 98 ? 7.833 15.598 85.705 1.00 19.44 ? 98 HIS A N 1 ATOM 712 C CA . HIS A 1 98 ? 6.890 16.669 85.438 1.00 18.10 ? 98 HIS A CA 1 ATOM 713 C C . HIS A 1 98 ? 6.080 16.384 84.178 1.00 17.21 ? 98 HIS A C 1 ATOM 714 O O . HIS A 1 98 ? 4.864 16.541 84.165 1.00 16.87 ? 98 HIS A O 1 ATOM 715 C CB . HIS A 1 98 ? 7.616 18.009 85.295 1.00 20.42 ? 98 HIS A CB 1 ATOM 716 C CG . HIS A 1 98 ? 6.699 19.149 84.984 1.00 20.16 ? 98 HIS A CG 1 ATOM 717 N ND1 . HIS A 1 98 ? 6.533 19.644 83.709 1.00 23.05 ? 98 HIS A ND1 1 ATOM 718 C CD2 . HIS A 1 98 ? 5.845 19.845 85.773 1.00 20.22 ? 98 HIS A CD2 1 ATOM 719 C CE1 . HIS A 1 98 ? 5.615 20.595 83.725 1.00 18.90 ? 98 HIS A CE1 1 ATOM 720 N NE2 . HIS A 1 98 ? 5.182 20.737 84.965 1.00 22.62 ? 98 HIS A NE2 1 ATOM 721 N N . LEU A 1 99 ? 6.753 15.963 83.111 1.00 17.47 ? 99 LEU A N 1 ATOM 722 C CA . LEU A 1 99 ? 6.056 15.665 81.872 1.00 17.10 ? 99 LEU A CA 1 ATOM 723 C C . LEU A 1 99 ? 5.093 14.503 82.074 1.00 16.74 ? 99 LEU A C 1 ATOM 724 O O . LEU A 1 99 ? 3.938 14.562 81.662 1.00 19.44 ? 99 LEU A O 1 ATOM 725 C CB . LEU A 1 99 ? 7.054 15.304 80.769 1.00 17.17 ? 99 LEU A CB 1 ATOM 726 C CG . LEU A 1 99 ? 7.924 16.445 80.238 1.00 17.98 ? 99 LEU A CG 1 ATOM 727 C CD1 . LEU A 1 99 ? 8.989 15.877 79.304 1.00 18.91 ? 99 LEU A CD1 1 ATOM 728 C CD2 . LEU A 1 99 ? 7.049 17.452 79.510 1.00 20.00 ? 99 LEU A CD2 1 ATOM 729 N N . TRP A 1 100 ? 5.580 13.452 82.719 1.00 18.39 ? 100 TRP A N 1 ATOM 730 C CA . TRP A 1 100 ? 4.766 12.264 82.946 1.00 19.36 ? 100 TRP A CA 1 ATOM 731 C C . TRP A 1 100 ? 3.490 12.555 83.732 1.00 19.05 ? 100 TRP A C 1 ATOM 732 O O . TRP A 1 100 ? 2.397 12.152 83.329 1.00 19.43 ? 100 TRP A O 1 ATOM 733 C CB . TRP A 1 100 ? 5.594 11.198 83.666 1.00 20.36 ? 100 TRP A CB 1 ATOM 734 C CG . TRP A 1 100 ? 4.881 9.891 83.779 1.00 22.88 ? 100 TRP A CG 1 ATOM 735 C CD1 . TRP A 1 100 ? 4.404 9.312 84.920 1.00 24.87 ? 100 TRP A CD1 1 ATOM 736 C CD2 . TRP A 1 100 ? 4.525 9.014 82.704 1.00 24.95 ? 100 TRP A CD2 1 ATOM 737 N NE1 . TRP A 1 100 ? 3.769 8.129 84.624 1.00 27.06 ? 100 TRP A NE1 1 ATOM 738 C CE2 . TRP A 1 100 ? 3.828 7.921 83.270 1.00 27.37 ? 100 TRP A CE2 1 ATOM 739 C CE3 . TRP A 1 100 ? 4.726 9.046 81.316 1.00 25.63 ? 100 TRP A CE3 1 ATOM 740 C CZ2 . TRP A 1 100 ? 3.329 6.866 82.496 1.00 27.34 ? 100 TRP A CZ2 1 ATOM 741 C CZ3 . TRP A 1 100 ? 4.230 7.997 80.544 1.00 27.08 ? 100 TRP A CZ3 1 ATOM 742 C CH2 . TRP A 1 100 ? 3.539 6.921 81.140 1.00 27.62 ? 100 TRP A CH2 1 ATOM 743 N N . ASN A 1 101 ? 3.631 13.279 84.838 1.00 19.38 ? 101 ASN A N 1 ATOM 744 C CA . ASN A 1 101 ? 2.493 13.610 85.688 1.00 19.39 ? 101 ASN A CA 1 ATOM 745 C C . ASN A 1 101 ? 1.612 14.743 85.185 1.00 19.39 ? 101 ASN A C 1 ATOM 746 O O . ASN A 1 101 ? 0.465 14.860 85.606 1.00 19.15 ? 101 ASN A O 1 ATOM 747 C CB . ASN A 1 101 ? 2.981 13.934 87.105 1.00 20.13 ? 101 ASN A CB 1 ATOM 748 C CG . ASN A 1 101 ? 3.641 12.746 87.773 1.00 22.39 ? 101 ASN A CG 1 ATOM 749 O OD1 . ASN A 1 101 ? 3.125 11.634 87.718 1.00 24.25 ? 101 ASN A OD1 1 ATOM 750 N ND2 . ASN A 1 101 ? 4.780 12.977 88.419 1.00 24.06 ? 101 ASN A ND2 1 ATOM 751 N N . SER A 1 102 ? 2.132 15.576 84.285 1.00 18.01 ? 102 SER A N 1 ATOM 752 C CA . SER A 1 102 ? 1.350 16.694 83.764 1.00 18.68 ? 102 SER A CA 1 ATOM 753 C C . SER A 1 102 ? 0.655 16.435 82.433 1.00 18.47 ? 102 SER A C 1 ATOM 754 O O . SER A 1 102 ? -0.472 16.888 82.224 1.00 18.65 ? 102 SER A O 1 ATOM 755 C CB . SER A 1 102 ? 2.232 17.939 83.592 1.00 17.26 ? 102 SER A CB 1 ATOM 756 O OG . SER A 1 102 ? 2.982 18.213 84.757 1.00 19.58 ? 102 SER A OG 1 ATOM 757 N N . TYR A 1 103 ? 1.328 15.711 81.538 1.00 18.59 ? 103 TYR A N 1 ATOM 758 C CA . TYR A 1 103 ? 0.787 15.465 80.205 1.00 18.70 ? 103 TYR A CA 1 ATOM 759 C C . TYR A 1 103 ? 0.636 14.022 79.759 1.00 19.42 ? 103 TYR A C 1 ATOM 760 O O . TYR A 1 103 ? -0.001 13.765 78.734 1.00 19.75 ? 103 TYR A O 1 ATOM 761 C CB . TYR A 1 103 ? 1.653 16.165 79.150 1.00 18.68 ? 103 TYR A CB 1 ATOM 762 C CG . TYR A 1 103 ? 1.916 17.621 79.425 1.00 18.41 ? 103 TYR A CG 1 ATOM 763 C CD1 . TYR A 1 103 ? 3.081 18.029 80.080 1.00 20.15 ? 103 TYR A CD1 1 ATOM 764 C CD2 . TYR A 1 103 ? 0.996 18.590 79.044 1.00 20.60 ? 103 TYR A CD2 1 ATOM 765 C CE1 . TYR A 1 103 ? 3.320 19.375 80.348 1.00 19.50 ? 103 TYR A CE1 1 ATOM 766 C CE2 . TYR A 1 103 ? 1.221 19.935 79.311 1.00 22.31 ? 103 TYR A CE2 1 ATOM 767 C CZ . TYR A 1 103 ? 2.384 20.319 79.963 1.00 22.28 ? 103 TYR A CZ 1 ATOM 768 O OH . TYR A 1 103 ? 2.597 21.649 80.241 1.00 22.19 ? 103 TYR A OH 1 ATOM 769 N N . PHE A 1 104 ? 1.218 13.083 80.491 1.00 20.19 ? 104 PHE A N 1 ATOM 770 C CA . PHE A 1 104 ? 1.121 11.694 80.071 1.00 20.74 ? 104 PHE A CA 1 ATOM 771 C C . PHE A 1 104 ? 0.330 10.784 81.011 1.00 21.82 ? 104 PHE A C 1 ATOM 772 O O . PHE A 1 104 ? -0.753 11.158 81.454 1.00 23.15 ? 104 PHE A O 1 ATOM 773 C CB . PHE A 1 104 ? 2.525 11.158 79.791 1.00 20.35 ? 104 PHE A CB 1 ATOM 774 C CG . PHE A 1 104 ? 3.192 11.833 78.614 1.00 21.35 ? 104 PHE A CG 1 ATOM 775 C CD1 . PHE A 1 104 ? 3.105 11.287 77.333 1.00 19.46 ? 104 PHE A CD1 1 ATOM 776 C CD2 . PHE A 1 104 ? 3.837 13.059 78.776 1.00 20.38 ? 104 PHE A CD2 1 ATOM 777 C CE1 . PHE A 1 104 ? 3.645 11.951 76.228 1.00 22.64 ? 104 PHE A CE1 1 ATOM 778 C CE2 . PHE A 1 104 ? 4.382 13.735 77.679 1.00 20.07 ? 104 PHE A CE2 1 ATOM 779 C CZ . PHE A 1 104 ? 4.285 13.182 76.402 1.00 21.15 ? 104 PHE A CZ 1 ATOM 780 N N . GLY A 1 105 ? 0.862 9.601 81.305 1.00 23.43 ? 105 GLY A N 1 ATOM 781 C CA . GLY A 1 105 ? 0.139 8.659 82.147 1.00 25.49 ? 105 GLY A CA 1 ATOM 782 C C . GLY A 1 105 ? 0.269 8.786 83.650 1.00 27.48 ? 105 GLY A C 1 ATOM 783 O O . GLY A 1 105 ? -0.291 7.973 84.393 1.00 28.89 ? 105 GLY A O 1 ATOM 784 N N . GLY A 1 106 ? 0.990 9.799 84.112 1.00 25.32 ? 106 GLY A N 1 ATOM 785 C CA . GLY A 1 106 ? 1.162 9.971 85.541 1.00 26.30 ? 106 GLY A CA 1 ATOM 786 C C . GLY A 1 106 ? 0.053 10.756 86.206 1.00 25.33 ? 106 GLY A C 1 ATOM 787 O O . GLY A 1 106 ? -0.692 11.488 85.557 1.00 26.23 ? 106 GLY A O 1 ATOM 788 N N . SER A 1 107 ? -0.060 10.596 87.519 1.00 26.88 ? 107 SER A N 1 ATOM 789 C CA . SER A 1 107 ? -1.067 11.305 88.294 1.00 28.12 ? 107 SER A CA 1 ATOM 790 C C . SER A 1 107 ? -0.538 11.537 89.700 1.00 27.84 ? 107 SER A C 1 ATOM 791 O O . SER A 1 107 ? -0.255 10.589 90.434 1.00 27.60 ? 107 SER A O 1 ATOM 792 C CB . SER A 1 107 ? -2.365 10.501 88.360 1.00 30.54 ? 107 SER A CB 1 ATOM 793 O OG . SER A 1 107 ? -3.342 11.204 89.104 1.00 32.98 ? 107 SER A OG 1 ATOM 794 N N . LYS A 1 108 ? -0.396 12.805 90.064 1.00 25.26 ? 108 LYS A N 1 ATOM 795 C CA . LYS A 1 108 ? 0.104 13.179 91.379 1.00 25.18 ? 108 LYS A CA 1 ATOM 796 C C . LYS A 1 108 ? -0.777 14.337 91.839 1.00 23.97 ? 108 LYS A C 1 ATOM 797 O O . LYS A 1 108 ? -1.014 15.283 91.089 1.00 22.62 ? 108 LYS A O 1 ATOM 798 C CB . LYS A 1 108 ? 1.570 13.614 91.270 1.00 27.51 ? 108 LYS A CB 1 ATOM 799 C CG . LYS A 1 108 ? 2.306 13.703 92.592 1.00 32.49 ? 108 LYS A CG 1 ATOM 800 C CD . LYS A 1 108 ? 3.735 14.226 92.414 1.00 36.28 ? 108 LYS A CD 1 ATOM 801 C CE . LYS A 1 108 ? 4.446 14.360 93.759 1.00 38.22 ? 108 LYS A CE 1 ATOM 802 N NZ . LYS A 1 108 ? 5.785 15.006 93.652 1.00 41.40 ? 108 LYS A NZ 1 ATOM 803 N N . PRO A 1 109 ? -1.279 14.276 93.081 1.00 23.67 ? 109 PRO A N 1 ATOM 804 C CA . PRO A 1 109 ? -2.147 15.326 93.628 1.00 22.68 ? 109 PRO A CA 1 ATOM 805 C C . PRO A 1 109 ? -1.591 16.748 93.542 1.00 21.27 ? 109 PRO A C 1 ATOM 806 O O . PRO A 1 109 ? -2.333 17.697 93.299 1.00 21.38 ? 109 PRO A O 1 ATOM 807 C CB . PRO A 1 109 ? -2.361 14.876 95.074 1.00 23.87 ? 109 PRO A CB 1 ATOM 808 C CG . PRO A 1 109 ? -2.255 13.378 94.983 1.00 26.30 ? 109 PRO A CG 1 ATOM 809 C CD . PRO A 1 109 ? -1.064 13.204 94.069 1.00 23.42 ? 109 PRO A CD 1 ATOM 810 N N . SER A 1 110 ? -0.286 16.895 93.731 1.00 18.99 ? 110 SER A N 1 ATOM 811 C CA . SER A 1 110 ? 0.331 18.217 93.696 1.00 19.87 ? 110 SER A CA 1 ATOM 812 C C . SER A 1 110 ? 0.583 18.765 92.290 1.00 19.98 ? 110 SER A C 1 ATOM 813 O O . SER A 1 110 ? 0.871 19.949 92.128 1.00 19.73 ? 110 SER A O 1 ATOM 814 C CB . SER A 1 110 ? 1.656 18.187 94.463 1.00 22.51 ? 110 SER A CB 1 ATOM 815 O OG . SER A 1 110 ? 2.551 17.248 93.885 1.00 24.86 ? 110 SER A OG 1 ATOM 816 N N . VAL A 1 111 ? 0.463 17.913 91.280 1.00 19.18 ? 111 VAL A N 1 ATOM 817 C CA . VAL A 1 111 ? 0.720 18.329 89.906 1.00 20.25 ? 111 VAL A CA 1 ATOM 818 C C . VAL A 1 111 ? -0.540 18.500 89.069 1.00 19.23 ? 111 VAL A C 1 ATOM 819 O O . VAL A 1 111 ? -1.254 17.537 88.800 1.00 20.12 ? 111 VAL A O 1 ATOM 820 C CB . VAL A 1 111 ? 1.647 17.315 89.202 1.00 21.39 ? 111 VAL A CB 1 ATOM 821 C CG1 . VAL A 1 111 ? 1.922 17.769 87.772 1.00 22.24 ? 111 VAL A CG1 1 ATOM 822 C CG2 . VAL A 1 111 ? 2.943 17.174 89.983 1.00 19.86 ? 111 VAL A CG2 1 ATOM 823 N N . PRO A 1 112 ? -0.828 19.735 88.636 1.00 19.89 ? 112 PRO A N 1 ATOM 824 C CA . PRO A 1 112 ? -2.024 19.962 87.825 1.00 20.49 ? 112 PRO A CA 1 ATOM 825 C C . PRO A 1 112 ? -1.793 19.508 86.387 1.00 21.53 ? 112 PRO A C 1 ATOM 826 O O . PRO A 1 112 ? -0.662 19.514 85.905 1.00 23.41 ? 112 PRO A O 1 ATOM 827 C CB . PRO A 1 112 ? -2.214 21.465 87.922 1.00 20.22 ? 112 PRO A CB 1 ATOM 828 C CG . PRO A 1 112 ? -0.800 21.956 87.908 1.00 20.77 ? 112 PRO A CG 1 ATOM 829 C CD . PRO A 1 112 ? -0.100 20.999 88.861 1.00 21.40 ? 112 PRO A CD 1 ATOM 830 N N . ARG A 1 113 ? -2.863 19.114 85.709 1.00 22.37 ? 113 ARG A N 1 ATOM 831 C CA . ARG A 1 113 ? -2.748 18.679 84.325 1.00 24.32 ? 113 ARG A CA 1 ATOM 832 C C . ARG A 1 113 ? -3.356 19.751 83.431 1.00 22.85 ? 113 ARG A C 1 ATOM 833 O O . ARG A 1 113 ? -4.571 19.932 83.399 1.00 24.62 ? 113 ARG A O 1 ATOM 834 C CB . ARG A 1 113 ? -3.451 17.335 84.136 1.00 24.72 ? 113 ARG A CB 1 ATOM 835 C CG . ARG A 1 113 ? -2.762 16.195 84.891 1.00 27.68 ? 113 ARG A CG 1 ATOM 836 C CD . ARG A 1 113 ? -3.394 14.853 84.584 1.00 27.39 ? 113 ARG A CD 1 ATOM 837 N NE . ARG A 1 113 ? -3.258 14.493 83.172 1.00 26.28 ? 113 ARG A NE 1 ATOM 838 C CZ . ARG A 1 113 ? -2.238 13.814 82.657 1.00 25.91 ? 113 ARG A CZ 1 ATOM 839 N NH1 . ARG A 1 113 ? -1.243 13.404 83.431 1.00 23.82 ? 113 ARG A NH1 1 ATOM 840 N NH2 . ARG A 1 113 ? -2.215 13.542 81.358 1.00 26.43 ? 113 ARG A NH2 1 ATOM 841 N N . PRO A 1 114 ? -2.506 20.489 82.697 1.00 24.22 ? 114 PRO A N 1 ATOM 842 C CA . PRO A 1 114 ? -2.961 21.558 81.803 1.00 24.40 ? 114 PRO A CA 1 ATOM 843 C C . PRO A 1 114 ? -4.098 21.166 80.869 1.00 25.97 ? 114 PRO A C 1 ATOM 844 O O . PRO A 1 114 ? -4.976 21.978 80.577 1.00 26.50 ? 114 PRO A O 1 ATOM 845 C CB . PRO A 1 114 ? -1.692 21.926 81.034 1.00 23.93 ? 114 PRO A CB 1 ATOM 846 C CG . PRO A 1 114 ? -0.619 21.698 82.050 1.00 23.65 ? 114 PRO A CG 1 ATOM 847 C CD . PRO A 1 114 ? -1.035 20.377 82.670 1.00 24.00 ? 114 PRO A CD 1 ATOM 848 N N . PHE A 1 115 ? -4.080 19.922 80.402 1.00 25.05 ? 115 PHE A N 1 ATOM 849 C CA . PHE A 1 115 ? -5.099 19.451 79.474 1.00 25.79 ? 115 PHE A CA 1 ATOM 850 C C . PHE A 1 115 ? -5.996 18.362 80.059 1.00 25.02 ? 115 PHE A C 1 ATOM 851 O O . PHE A 1 115 ? -6.568 17.561 79.322 1.00 24.22 ? 115 PHE A O 1 ATOM 852 C CB . PHE A 1 115 ? -4.427 18.931 78.198 1.00 26.21 ? 115 PHE A CB 1 ATOM 853 C CG . PHE A 1 115 ? -3.377 19.855 77.638 1.00 26.93 ? 115 PHE A CG 1 ATOM 854 C CD1 . PHE A 1 115 ? -2.196 19.341 77.113 1.00 26.96 ? 115 PHE A CD1 1 ATOM 855 C CD2 . PHE A 1 115 ? -3.569 21.233 77.629 1.00 27.04 ? 115 PHE A CD2 1 ATOM 856 C CE1 . PHE A 1 115 ? -1.220 20.184 76.586 1.00 26.02 ? 115 PHE A CE1 1 ATOM 857 C CE2 . PHE A 1 115 ? -2.600 22.087 77.105 1.00 24.59 ? 115 PHE A CE2 1 ATOM 858 C CZ . PHE A 1 115 ? -1.425 21.562 76.583 1.00 25.93 ? 115 PHE A CZ 1 ATOM 859 N N . GLY A 1 116 ? -6.117 18.327 81.383 1.00 25.21 ? 116 GLY A N 1 ATOM 860 C CA . GLY A 1 116 ? -6.965 17.328 82.008 1.00 26.91 ? 116 GLY A CA 1 ATOM 861 C C . GLY A 1 116 ? -6.562 15.889 81.738 1.00 27.97 ? 116 GLY A C 1 ATOM 862 O O . GLY A 1 116 ? -5.373 15.558 81.726 1.00 27.27 ? 116 GLY A O 1 ATOM 863 N N . ASP A 1 117 ? -7.557 15.034 81.509 1.00 29.39 ? 117 ASP A N 1 ATOM 864 C CA . ASP A 1 117 ? -7.321 13.615 81.267 1.00 31.18 ? 117 ASP A CA 1 ATOM 865 C C . ASP A 1 117 ? -6.743 13.254 79.899 1.00 30.25 ? 117 ASP A C 1 ATOM 866 O O . ASP A 1 117 ? -6.639 12.075 79.558 1.00 29.13 ? 117 ASP A O 1 ATOM 867 C CB . ASP A 1 117 ? -8.612 12.818 81.516 1.00 34.92 ? 117 ASP A CB 1 ATOM 868 C CG . ASP A 1 117 ? -9.757 13.241 80.611 1.00 38.38 ? 117 ASP A CG 1 ATOM 869 O OD1 . ASP A 1 117 ? -10.893 12.770 80.838 1.00 42.22 ? 117 ASP A OD1 1 ATOM 870 O OD2 . ASP A 1 117 ? -9.535 14.033 79.674 1.00 40.77 ? 117 ASP A OD2 1 ATOM 871 N N . ALA A 1 118 ? -6.365 14.257 79.114 1.00 28.22 ? 118 ALA A N 1 ATOM 872 C CA . ALA A 1 118 ? -5.768 13.987 77.811 1.00 25.48 ? 118 ALA A CA 1 ATOM 873 C C . ALA A 1 118 ? -4.383 13.409 78.086 1.00 23.89 ? 118 ALA A C 1 ATOM 874 O O . ALA A 1 118 ? -3.704 13.829 79.024 1.00 23.71 ? 118 ALA A O 1 ATOM 875 C CB . ALA A 1 118 ? -5.657 15.277 76.990 1.00 25.52 ? 118 ALA A CB 1 ATOM 876 N N . TRP A 1 119 ? -3.975 12.442 77.272 1.00 23.42 ? 119 TRP A N 1 ATOM 877 C CA . TRP A 1 119 ? -2.681 11.779 77.418 1.00 22.92 ? 119 TRP A CA 1 ATOM 878 C C . TRP A 1 119 ? -1.977 11.926 76.068 1.00 23.15 ? 119 TRP A C 1 ATOM 879 O O . TRP A 1 119 ? -2.352 11.271 75.095 1.00 23.20 ? 119 TRP A O 1 ATOM 880 C CB . TRP A 1 119 ? -2.917 10.300 77.755 1.00 23.00 ? 119 TRP A CB 1 ATOM 881 C CG . TRP A 1 119 ? -1.704 9.465 78.093 1.00 24.64 ? 119 TRP A CG 1 ATOM 882 C CD1 . TRP A 1 119 ? -0.437 9.585 77.580 1.00 22.31 ? 119 TRP A CD1 1 ATOM 883 C CD2 . TRP A 1 119 ? -1.686 8.291 78.921 1.00 24.28 ? 119 TRP A CD2 1 ATOM 884 N NE1 . TRP A 1 119 ? 0.358 8.557 78.034 1.00 24.09 ? 119 TRP A NE1 1 ATOM 885 C CE2 . TRP A 1 119 ? -0.384 7.749 78.856 1.00 25.64 ? 119 TRP A CE2 1 ATOM 886 C CE3 . TRP A 1 119 ? -2.651 7.643 79.707 1.00 27.01 ? 119 TRP A CE3 1 ATOM 887 C CZ2 . TRP A 1 119 ? -0.021 6.584 79.547 1.00 26.56 ? 119 TRP A CZ2 1 ATOM 888 C CZ3 . TRP A 1 119 ? -2.291 6.487 80.394 1.00 25.20 ? 119 TRP A CZ3 1 ATOM 889 C CH2 . TRP A 1 119 ? -0.986 5.969 80.308 1.00 27.61 ? 119 TRP A CH2 1 ATOM 890 N N . LEU A 1 120 ? -0.971 12.799 76.017 1.00 22.06 ? 120 LEU A N 1 ATOM 891 C CA . LEU A 1 120 ? -0.228 13.062 74.786 1.00 21.54 ? 120 LEU A CA 1 ATOM 892 C C . LEU A 1 120 ? 0.449 11.843 74.167 1.00 20.54 ? 120 LEU A C 1 ATOM 893 O O . LEU A 1 120 ? 0.671 10.827 74.828 1.00 20.49 ? 120 LEU A O 1 ATOM 894 C CB . LEU A 1 120 ? 0.796 14.176 75.024 1.00 20.43 ? 120 LEU A CB 1 ATOM 895 C CG . LEU A 1 120 ? 0.152 15.516 75.400 1.00 21.11 ? 120 LEU A CG 1 ATOM 896 C CD1 . LEU A 1 120 ? 1.226 16.589 75.548 1.00 20.36 ? 120 LEU A CD1 1 ATOM 897 C CD2 . LEU A 1 120 ? -0.850 15.919 74.326 1.00 23.54 ? 120 LEU A CD2 1 ATOM 898 N N . ASP A 1 121 ? 0.796 11.968 72.889 1.00 18.29 ? 121 ASP A N 1 ATOM 899 C CA . ASP A 1 121 ? 1.399 10.870 72.140 1.00 18.36 ? 121 ASP A CA 1 ATOM 900 C C . ASP A 1 121 ? 2.901 10.934 71.905 1.00 18.45 ? 121 ASP A C 1 ATOM 901 O O . ASP A 1 121 ? 3.472 10.023 71.307 1.00 20.12 ? 121 ASP A O 1 ATOM 902 C CB . ASP A 1 121 ? 0.684 10.753 70.796 1.00 20.76 ? 121 ASP A CB 1 ATOM 903 C CG . ASP A 1 121 ? -0.813 10.568 70.957 1.00 21.75 ? 121 ASP A CG 1 ATOM 904 O OD1 . ASP A 1 121 ? -1.225 9.477 71.401 1.00 25.54 ? 121 ASP A OD1 1 ATOM 905 O OD2 . ASP A 1 121 ? -1.578 11.510 70.657 1.00 22.71 ? 121 ASP A OD2 1 ATOM 906 N N . GLY A 1 122 ? 3.550 11.999 72.356 1.00 18.34 ? 122 GLY A N 1 ATOM 907 C CA . GLY A 1 122 ? 4.982 12.080 72.140 1.00 16.44 ? 122 GLY A CA 1 ATOM 908 C C . GLY A 1 122 ? 5.614 13.343 72.675 1.00 16.53 ? 122 GLY A C 1 ATOM 909 O O . GLY A 1 122 ? 4.921 14.239 73.151 1.00 14.48 ? 122 GLY A O 1 ATOM 910 N N . VAL A 1 123 ? 6.939 13.383 72.615 1.00 15.47 ? 123 VAL A N 1 ATOM 911 C CA . VAL A 1 123 ? 7.719 14.525 73.072 1.00 16.75 ? 123 VAL A CA 1 ATOM 912 C C . VAL A 1 123 ? 8.779 14.834 72.023 1.00 16.83 ? 123 VAL A C 1 ATOM 913 O O . VAL A 1 123 ? 9.480 13.939 71.562 1.00 17.78 ? 123 VAL A O 1 ATOM 914 C CB . VAL A 1 123 ? 8.447 14.225 74.400 1.00 16.80 ? 123 VAL A CB 1 ATOM 915 C CG1 . VAL A 1 123 ? 9.303 15.423 74.812 1.00 19.23 ? 123 VAL A CG1 1 ATOM 916 C CG2 . VAL A 1 123 ? 7.430 13.898 75.489 1.00 17.49 ? 123 VAL A CG2 1 ATOM 917 N N . ASP A 1 124 ? 8.888 16.104 71.646 1.00 15.55 ? 124 ASP A N 1 ATOM 918 C CA . ASP A 1 124 ? 9.887 16.521 70.677 1.00 14.86 ? 124 ASP A CA 1 ATOM 919 C C . ASP A 1 124 ? 10.881 17.417 71.409 1.00 16.42 ? 124 ASP A C 1 ATOM 920 O O . ASP A 1 124 ? 10.484 18.237 72.245 1.00 16.75 ? 124 ASP A O 1 ATOM 921 C CB . ASP A 1 124 ? 9.236 17.306 69.539 1.00 17.18 ? 124 ASP A CB 1 ATOM 922 C CG . ASP A 1 124 ? 10.256 17.895 68.582 1.00 21.06 ? 124 ASP A CG 1 ATOM 923 O OD1 . ASP A 1 124 ? 10.856 17.126 67.802 1.00 19.94 ? 124 ASP A OD1 1 ATOM 924 O OD2 . ASP A 1 124 ? 10.467 19.130 68.620 1.00 21.07 ? 124 ASP A OD2 1 ATOM 925 N N . LEU A 1 125 ? 12.165 17.244 71.115 1.00 14.63 ? 125 LEU A N 1 ATOM 926 C CA . LEU A 1 125 ? 13.207 18.056 71.732 1.00 16.61 ? 125 LEU A CA 1 ATOM 927 C C . LEU A 1 125 ? 13.691 19.058 70.688 1.00 17.35 ? 125 LEU A C 1 ATOM 928 O O . LEU A 1 125 ? 14.286 18.668 69.687 1.00 16.51 ? 125 LEU A O 1 ATOM 929 C CB . LEU A 1 125 ? 14.386 17.184 72.180 1.00 18.41 ? 125 LEU A CB 1 ATOM 930 C CG . LEU A 1 125 ? 14.110 16.013 73.129 1.00 20.75 ? 125 LEU A CG 1 ATOM 931 C CD1 . LEU A 1 125 ? 15.432 15.556 73.731 1.00 21.02 ? 125 LEU A CD1 1 ATOM 932 C CD2 . LEU A 1 125 ? 13.159 16.418 74.222 1.00 18.65 ? 125 LEU A CD2 1 ATOM 933 N N . PHE A 1 126 ? 13.415 20.339 70.935 1.00 15.69 ? 126 PHE A N 1 ATOM 934 C CA . PHE A 1 126 ? 13.797 21.457 70.056 1.00 16.23 ? 126 PHE A CA 1 ATOM 935 C C . PHE A 1 126 ? 14.843 22.223 70.876 1.00 16.39 ? 126 PHE A C 1 ATOM 936 O O . PHE A 1 126 ? 14.566 23.283 71.438 1.00 16.55 ? 126 PHE A O 1 ATOM 937 C CB . PHE A 1 126 ? 12.556 22.327 69.810 1.00 14.30 ? 126 PHE A CB 1 ATOM 938 C CG . PHE A 1 126 ? 12.671 23.264 68.638 1.00 14.25 ? 126 PHE A CG 1 ATOM 939 C CD1 . PHE A 1 126 ? 11.854 23.098 67.522 1.00 13.76 ? 126 PHE A CD1 1 ATOM 940 C CD2 . PHE A 1 126 ? 13.552 24.340 68.670 1.00 16.45 ? 126 PHE A CD2 1 ATOM 941 C CE1 . PHE A 1 126 ? 11.901 23.988 66.454 1.00 16.21 ? 126 PHE A CE1 1 ATOM 942 C CE2 . PHE A 1 126 ? 13.613 25.244 67.602 1.00 15.79 ? 126 PHE A CE2 1 ATOM 943 C CZ . PHE A 1 126 ? 12.783 25.068 66.491 1.00 16.12 ? 126 PHE A CZ 1 ATOM 944 N N . LEU A 1 127 ? 16.057 21.689 70.922 1.00 17.47 ? 127 LEU A N 1 ATOM 945 C CA . LEU A 1 127 ? 17.106 22.269 71.752 1.00 17.89 ? 127 LEU A CA 1 ATOM 946 C C . LEU A 1 127 ? 18.084 23.262 71.129 1.00 19.90 ? 127 LEU A C 1 ATOM 947 O O . LEU A 1 127 ? 19.245 22.943 70.890 1.00 21.83 ? 127 LEU A O 1 ATOM 948 C CB . LEU A 1 127 ? 17.878 21.122 72.416 1.00 17.11 ? 127 LEU A CB 1 ATOM 949 C CG . LEU A 1 127 ? 16.931 20.061 72.995 1.00 17.65 ? 127 LEU A CG 1 ATOM 950 C CD1 . LEU A 1 127 ? 17.748 18.902 73.526 1.00 17.43 ? 127 LEU A CD1 1 ATOM 951 C CD2 . LEU A 1 127 ? 16.052 20.661 74.102 1.00 15.86 ? 127 LEU A CD2 1 ATOM 952 N N . GLU A 1 128 ? 17.612 24.480 70.901 1.00 21.71 ? 128 GLU A N 1 ATOM 953 C CA . GLU A 1 128 ? 18.445 25.528 70.333 1.00 24.37 ? 128 GLU A CA 1 ATOM 954 C C . GLU A 1 128 ? 19.609 25.858 71.262 1.00 26.16 ? 128 GLU A C 1 ATOM 955 O O . GLU A 1 128 ? 20.719 26.138 70.812 1.00 27.66 ? 128 GLU A O 1 ATOM 956 C CB . GLU A 1 128 ? 17.612 26.792 70.106 1.00 24.65 ? 128 GLU A CB 1 ATOM 957 C CG . GLU A 1 128 ? 16.835 26.812 68.809 1.00 26.66 ? 128 GLU A CG 1 ATOM 958 C CD . GLU A 1 128 ? 17.725 27.064 67.609 1.00 28.35 ? 128 GLU A CD 1 ATOM 959 O OE1 . GLU A 1 128 ? 17.889 26.146 66.788 1.00 24.84 ? 128 GLU A OE1 1 ATOM 960 O OE2 . GLU A 1 128 ? 18.268 28.186 67.488 1.00 30.21 ? 128 GLU A OE2 1 ATOM 961 N N A HIS A 1 129 ? 19.359 25.818 72.564 0.50 25.79 ? 129 HIS A N 1 ATOM 962 N N B HIS A 1 129 ? 19.334 25.827 72.562 0.50 25.65 ? 129 HIS A N 1 ATOM 963 C CA A HIS A 1 129 ? 20.405 26.140 73.520 0.50 26.10 ? 129 HIS A CA 1 ATOM 964 C CA B HIS A 1 129 ? 20.331 26.133 73.581 0.50 25.94 ? 129 HIS A CA 1 ATOM 965 C C A HIS A 1 129 ? 20.768 24.970 74.418 0.50 26.08 ? 129 HIS A C 1 ATOM 966 C C B HIS A 1 129 ? 20.773 24.905 74.367 0.50 25.82 ? 129 HIS A C 1 ATOM 967 O O A HIS A 1 129 ? 19.905 24.211 74.858 0.50 25.93 ? 129 HIS A O 1 ATOM 968 O O B HIS A 1 129 ? 19.961 24.033 74.678 0.50 25.31 ? 129 HIS A O 1 ATOM 969 C CB A HIS A 1 129 ? 19.979 27.361 74.323 0.50 25.95 ? 129 HIS A CB 1 ATOM 970 C CB B HIS A 1 129 ? 19.766 27.158 74.570 0.50 25.82 ? 129 HIS A CB 1 ATOM 971 C CG A HIS A 1 129 ? 19.637 28.532 73.458 0.50 26.27 ? 129 HIS A CG 1 ATOM 972 C CG B HIS A 1 129 ? 20.518 27.224 75.865 0.50 27.25 ? 129 HIS A CG 1 ATOM 973 N ND1 A HIS A 1 129 ? 20.544 29.103 72.592 0.50 25.91 ? 129 HIS A ND1 1 ATOM 974 N ND1 B HIS A 1 129 ? 21.731 27.866 75.992 0.50 28.78 ? 129 HIS A ND1 1 ATOM 975 C CD2 A HIS A 1 129 ? 18.470 29.192 73.269 0.50 26.00 ? 129 HIS A CD2 1 ATOM 976 C CD2 B HIS A 1 129 ? 20.252 26.683 77.078 0.50 26.99 ? 129 HIS A CD2 1 ATOM 977 C CE1 A HIS A 1 129 ? 19.949 30.062 71.905 0.50 25.36 ? 129 HIS A CE1 1 ATOM 978 C CE1 B HIS A 1 129 ? 22.179 27.720 77.226 0.50 27.41 ? 129 HIS A CE1 1 ATOM 979 N NE2 A HIS A 1 129 ? 18.691 30.136 72.297 0.50 24.50 ? 129 HIS A NE2 1 ATOM 980 N NE2 B HIS A 1 129 ? 21.300 27.005 77.906 0.50 28.42 ? 129 HIS A NE2 1 ATOM 981 N N . GLY A 1 130 ? 22.063 24.843 74.683 1.00 25.69 ? 130 GLY A N 1 ATOM 982 C CA . GLY A 1 130 ? 22.564 23.745 75.483 1.00 25.51 ? 130 GLY A CA 1 ATOM 983 C C . GLY A 1 130 ? 24.067 23.803 75.664 1.00 27.12 ? 130 GLY A C 1 ATOM 984 O O . GLY A 1 130 ? 24.758 24.577 75.000 1.00 27.58 ? 130 GLY A O 1 ATOM 985 N N . THR A 1 131 ? 24.569 22.981 76.577 1.00 27.48 ? 131 THR A N 1 ATOM 986 C CA . THR A 1 131 ? 25.995 22.908 76.864 1.00 28.90 ? 131 THR A CA 1 ATOM 987 C C . THR A 1 131 ? 26.345 21.441 77.070 1.00 30.09 ? 131 THR A C 1 ATOM 988 O O . THR A 1 131 ? 25.456 20.600 77.202 1.00 28.20 ? 131 THR A O 1 ATOM 989 C CB . THR A 1 131 ? 26.352 23.669 78.152 1.00 29.48 ? 131 THR A CB 1 ATOM 990 O OG1 . THR A 1 131 ? 25.723 23.034 79.273 1.00 32.33 ? 131 THR A OG1 1 ATOM 991 C CG2 . THR A 1 131 ? 25.882 25.110 78.066 1.00 29.76 ? 131 THR A CG2 1 ATOM 992 N N . PRO A 1 132 ? 27.646 21.110 77.095 1.00 31.17 ? 132 PRO A N 1 ATOM 993 C CA . PRO A 1 132 ? 28.049 19.714 77.293 1.00 31.30 ? 132 PRO A CA 1 ATOM 994 C C . PRO A 1 132 ? 27.593 19.181 78.649 1.00 30.13 ? 132 PRO A C 1 ATOM 995 O O . PRO A 1 132 ? 27.565 17.974 78.871 1.00 31.42 ? 132 PRO A O 1 ATOM 996 C CB . PRO A 1 132 ? 29.571 19.775 77.180 1.00 32.51 ? 132 PRO A CB 1 ATOM 997 C CG . PRO A 1 132 ? 29.788 20.917 76.231 1.00 31.57 ? 132 PRO A CG 1 ATOM 998 C CD . PRO A 1 132 ? 28.809 21.945 76.742 1.00 32.72 ? 132 PRO A CD 1 ATOM 999 N N . ALA A 1 133 ? 27.235 20.089 79.551 1.00 28.72 ? 133 ALA A N 1 ATOM 1000 C CA . ALA A 1 133 ? 26.786 19.708 80.883 1.00 27.18 ? 133 ALA A CA 1 ATOM 1001 C C . ALA A 1 133 ? 25.340 19.212 80.897 1.00 26.36 ? 133 ALA A C 1 ATOM 1002 O O . ALA A 1 133 ? 24.910 18.582 81.862 1.00 24.98 ? 133 ALA A O 1 ATOM 1003 C CB . ALA A 1 133 ? 26.938 20.883 81.840 1.00 28.34 ? 133 ALA A CB 1 ATOM 1004 N N . ASP A 1 134 ? 24.588 19.496 79.836 1.00 23.57 ? 134 ASP A N 1 ATOM 1005 C CA . ASP A 1 134 ? 23.192 19.062 79.778 1.00 22.16 ? 134 ASP A CA 1 ATOM 1006 C C . ASP A 1 134 ? 23.089 17.548 79.683 1.00 21.45 ? 134 ASP A C 1 ATOM 1007 O O . ASP A 1 134 ? 23.960 16.892 79.121 1.00 22.19 ? 134 ASP A O 1 ATOM 1008 C CB . ASP A 1 134 ? 22.464 19.695 78.590 1.00 22.20 ? 134 ASP A CB 1 ATOM 1009 C CG . ASP A 1 134 ? 22.186 21.177 78.796 1.00 22.06 ? 134 ASP A CG 1 ATOM 1010 O OD1 . ASP A 1 134 ? 21.888 21.575 79.940 1.00 22.50 ? 134 ASP A OD1 1 ATOM 1011 O OD2 . ASP A 1 134 ? 22.245 21.941 77.811 1.00 24.37 ? 134 ASP A OD2 1 ATOM 1012 N N . ARG A 1 135 ? 22.009 17.003 80.225 1.00 20.64 ? 135 ARG A N 1 ATOM 1013 C CA . ARG A 1 135 ? 21.804 15.563 80.208 1.00 21.35 ? 135 ARG A CA 1 ATOM 1014 C C . ARG A 1 135 ? 20.493 15.175 79.540 1.00 19.95 ? 135 ARG A C 1 ATOM 1015 O O . ARG A 1 135 ? 19.648 14.497 80.136 1.00 19.80 ? 135 ARG A O 1 ATOM 1016 C CB . ARG A 1 135 ? 21.860 15.023 81.638 1.00 21.57 ? 135 ARG A CB 1 ATOM 1017 C CG . ARG A 1 135 ? 23.256 15.117 82.256 1.00 26.30 ? 135 ARG A CG 1 ATOM 1018 C CD . ARG A 1 135 ? 24.233 14.209 81.513 1.00 26.13 ? 135 ARG A CD 1 ATOM 1019 N NE . ARG A 1 135 ? 25.594 14.309 82.027 1.00 33.86 ? 135 ARG A NE 1 ATOM 1020 C CZ . ARG A 1 135 ? 26.473 15.243 81.670 1.00 35.23 ? 135 ARG A CZ 1 ATOM 1021 N NH1 . ARG A 1 135 ? 26.143 16.173 80.782 1.00 35.29 ? 135 ARG A NH1 1 ATOM 1022 N NH2 . ARG A 1 135 ? 27.688 15.247 82.210 1.00 36.08 ? 135 ARG A NH2 1 ATOM 1023 N N . TYR A 1 136 ? 20.320 15.607 78.295 1.00 19.76 ? 136 TYR A N 1 ATOM 1024 C CA . TYR A 1 136 ? 19.113 15.269 77.561 1.00 18.53 ? 136 TYR A CA 1 ATOM 1025 C C . TYR A 1 136 ? 19.108 13.784 77.224 1.00 19.67 ? 136 TYR A C 1 ATOM 1026 O O . TYR A 1 136 ? 18.072 13.224 76.877 1.00 18.63 ? 136 TYR A O 1 ATOM 1027 C CB . TYR A 1 136 ? 18.997 16.108 76.291 1.00 18.60 ? 136 TYR A CB 1 ATOM 1028 C CG . TYR A 1 136 ? 18.658 17.552 76.587 1.00 18.03 ? 136 TYR A CG 1 ATOM 1029 C CD1 . TYR A 1 136 ? 19.643 18.541 76.568 1.00 18.46 ? 136 TYR A CD1 1 ATOM 1030 C CD2 . TYR A 1 136 ? 17.353 17.924 76.919 1.00 18.86 ? 136 TYR A CD2 1 ATOM 1031 C CE1 . TYR A 1 136 ? 19.332 19.872 76.874 1.00 18.74 ? 136 TYR A CE1 1 ATOM 1032 C CE2 . TYR A 1 136 ? 17.036 19.248 77.227 1.00 19.36 ? 136 TYR A CE2 1 ATOM 1033 C CZ . TYR A 1 136 ? 18.026 20.213 77.201 1.00 19.18 ? 136 TYR A CZ 1 ATOM 1034 O OH . TYR A 1 136 ? 17.711 21.524 77.505 1.00 18.05 ? 136 TYR A OH 1 ATOM 1035 N N . ASP A 1 137 ? 20.269 13.148 77.335 1.00 19.81 ? 137 ASP A N 1 ATOM 1036 C CA . ASP A 1 137 ? 20.360 11.717 77.069 1.00 21.02 ? 137 ASP A CA 1 ATOM 1037 C C . ASP A 1 137 ? 19.591 10.970 78.157 1.00 21.54 ? 137 ASP A C 1 ATOM 1038 O O . ASP A 1 137 ? 18.921 9.972 77.884 1.00 19.45 ? 137 ASP A O 1 ATOM 1039 C CB . ASP A 1 137 ? 21.828 11.268 77.041 1.00 22.41 ? 137 ASP A CB 1 ATOM 1040 C CG . ASP A 1 137 ? 22.577 11.625 78.312 1.00 25.51 ? 137 ASP A CG 1 ATOM 1041 O OD1 . ASP A 1 137 ? 22.493 12.791 78.758 1.00 23.73 ? 137 ASP A OD1 1 ATOM 1042 O OD2 . ASP A 1 137 ? 23.266 10.737 78.864 1.00 28.70 ? 137 ASP A OD2 1 ATOM 1043 N N . VAL A 1 138 ? 19.676 11.465 79.389 1.00 21.62 ? 138 VAL A N 1 ATOM 1044 C CA . VAL A 1 138 ? 18.972 10.847 80.509 1.00 21.60 ? 138 VAL A CA 1 ATOM 1045 C C . VAL A 1 138 ? 17.462 11.006 80.330 1.00 21.61 ? 138 VAL A C 1 ATOM 1046 O O . VAL A 1 138 ? 16.703 10.076 80.573 1.00 20.32 ? 138 VAL A O 1 ATOM 1047 C CB . VAL A 1 138 ? 19.410 11.471 81.855 1.00 22.58 ? 138 VAL A CB 1 ATOM 1048 C CG1 . VAL A 1 138 ? 18.515 10.980 82.989 1.00 22.71 ? 138 VAL A CG1 1 ATOM 1049 C CG2 . VAL A 1 138 ? 20.861 11.119 82.132 1.00 23.84 ? 138 VAL A CG2 1 ATOM 1050 N N . LEU A 1 139 ? 17.028 12.187 79.898 1.00 19.69 ? 139 LEU A N 1 ATOM 1051 C CA . LEU A 1 139 ? 15.604 12.435 79.677 1.00 19.76 ? 139 LEU A CA 1 ATOM 1052 C C . LEU A 1 139 ? 15.097 11.574 78.526 1.00 19.74 ? 139 LEU A C 1 ATOM 1053 O O . LEU A 1 139 ? 14.049 10.942 78.629 1.00 19.76 ? 139 LEU A O 1 ATOM 1054 C CB . LEU A 1 139 ? 15.354 13.912 79.329 1.00 19.20 ? 139 LEU A CB 1 ATOM 1055 C CG . LEU A 1 139 ? 13.928 14.257 78.869 1.00 16.93 ? 139 LEU A CG 1 ATOM 1056 C CD1 . LEU A 1 139 ? 12.955 14.185 80.046 1.00 18.29 ? 139 LEU A CD1 1 ATOM 1057 C CD2 . LEU A 1 139 ? 13.913 15.660 78.253 1.00 19.30 ? 139 LEU A CD2 1 ATOM 1058 N N . ALA A 1 140 ? 15.855 11.551 77.433 1.00 19.32 ? 140 ALA A N 1 ATOM 1059 C CA . ALA A 1 140 ? 15.462 10.788 76.253 1.00 19.61 ? 140 ALA A CA 1 ATOM 1060 C C . ALA A 1 140 ? 15.295 9.309 76.559 1.00 20.86 ? 140 ALA A C 1 ATOM 1061 O O . ALA A 1 140 ? 14.323 8.684 76.130 1.00 19.17 ? 140 ALA A O 1 ATOM 1062 C CB . ALA A 1 140 ? 16.484 10.978 75.135 1.00 20.34 ? 140 ALA A CB 1 ATOM 1063 N N . LEU A 1 141 ? 16.238 8.748 77.307 1.00 22.68 ? 141 LEU A N 1 ATOM 1064 C CA . LEU A 1 141 ? 16.149 7.333 77.638 1.00 23.80 ? 141 LEU A CA 1 ATOM 1065 C C . LEU A 1 141 ? 14.902 7.049 78.470 1.00 23.34 ? 141 LEU A C 1 ATOM 1066 O O . LEU A 1 141 ? 14.188 6.080 78.212 1.00 22.18 ? 141 LEU A O 1 ATOM 1067 C CB . LEU A 1 141 ? 17.405 6.873 78.386 1.00 26.25 ? 141 LEU A CB 1 ATOM 1068 C CG . LEU A 1 141 ? 17.490 5.362 78.644 1.00 31.39 ? 141 LEU A CG 1 ATOM 1069 C CD1 . LEU A 1 141 ? 17.322 4.604 77.333 1.00 31.48 ? 141 LEU A CD1 1 ATOM 1070 C CD2 . LEU A 1 141 ? 18.825 5.025 79.288 1.00 32.19 ? 141 LEU A CD2 1 ATOM 1071 N N . GLU A 1 142 ? 14.617 7.898 79.454 1.00 21.90 ? 142 GLU A N 1 ATOM 1072 C CA . GLU A 1 142 ? 13.440 7.671 80.281 1.00 22.87 ? 142 GLU A CA 1 ATOM 1073 C C . GLU A 1 142 ? 12.162 7.760 79.446 1.00 21.79 ? 142 GLU A C 1 ATOM 1074 O O . GLU A 1 142 ? 11.245 6.963 79.620 1.00 22.22 ? 142 GLU A O 1 ATOM 1075 C CB . GLU A 1 142 ? 13.390 8.663 81.448 1.00 24.56 ? 142 GLU A CB 1 ATOM 1076 C CG . GLU A 1 142 ? 12.428 8.233 82.543 1.00 28.74 ? 142 GLU A CG 1 ATOM 1077 C CD . GLU A 1 142 ? 12.868 6.948 83.238 1.00 33.19 ? 142 GLU A CD 1 ATOM 1078 O OE1 . GLU A 1 142 ? 12.031 6.328 83.929 1.00 34.90 ? 142 GLU A OE1 1 ATOM 1079 O OE2 . GLU A 1 142 ? 14.050 6.564 83.102 1.00 33.60 ? 142 GLU A OE2 1 ATOM 1080 N N . LEU A 1 143 ? 12.099 8.721 78.528 1.00 20.78 ? 143 LEU A N 1 ATOM 1081 C CA . LEU A 1 143 ? 10.923 8.848 77.677 1.00 19.55 ? 143 LEU A CA 1 ATOM 1082 C C . LEU A 1 143 ? 10.777 7.610 76.786 1.00 20.16 ? 143 LEU A C 1 ATOM 1083 O O . LEU A 1 143 ? 9.676 7.100 76.593 1.00 19.95 ? 143 LEU A O 1 ATOM 1084 C CB . LEU A 1 143 ? 11.028 10.105 76.803 1.00 19.49 ? 143 LEU A CB 1 ATOM 1085 C CG . LEU A 1 143 ? 10.835 11.431 77.549 1.00 17.64 ? 143 LEU A CG 1 ATOM 1086 C CD1 . LEU A 1 143 ? 11.213 12.618 76.638 1.00 17.72 ? 143 LEU A CD1 1 ATOM 1087 C CD2 . LEU A 1 143 ? 9.393 11.543 78.002 1.00 19.14 ? 143 LEU A CD2 1 ATOM 1088 N N . ALA A 1 144 ? 11.898 7.139 76.250 1.00 21.32 ? 144 ALA A N 1 ATOM 1089 C CA . ALA A 1 144 ? 11.897 5.976 75.372 1.00 22.71 ? 144 ALA A CA 1 ATOM 1090 C C . ALA A 1 144 ? 11.387 4.739 76.107 1.00 22.50 ? 144 ALA A C 1 ATOM 1091 O O . ALA A 1 144 ? 10.701 3.902 75.523 1.00 22.87 ? 144 ALA A O 1 ATOM 1092 C CB . ALA A 1 144 ? 13.295 5.727 74.835 1.00 22.26 ? 144 ALA A CB 1 ATOM 1093 N N . LYS A 1 145 ? 11.707 4.631 77.391 1.00 23.27 ? 145 LYS A N 1 ATOM 1094 C CA . LYS A 1 145 ? 11.269 3.477 78.175 1.00 24.13 ? 145 LYS A CA 1 ATOM 1095 C C . LYS A 1 145 ? 9.771 3.481 78.431 1.00 24.41 ? 145 LYS A C 1 ATOM 1096 O O . LYS A 1 145 ? 9.202 2.463 78.824 1.00 26.40 ? 145 LYS A O 1 ATOM 1097 C CB . LYS A 1 145 ? 12.020 3.417 79.503 1.00 23.19 ? 145 LYS A CB 1 ATOM 1098 C CG . LYS A 1 145 ? 13.497 3.145 79.341 1.00 27.99 ? 145 LYS A CG 1 ATOM 1099 C CD . LYS A 1 145 ? 14.200 3.070 80.680 1.00 31.69 ? 145 LYS A CD 1 ATOM 1100 C CE . LYS A 1 145 ? 15.678 2.791 80.492 1.00 35.07 ? 145 LYS A CE 1 ATOM 1101 N NZ . LYS A 1 145 ? 16.431 2.871 81.774 1.00 38.11 ? 145 LYS A NZ 1 ATOM 1102 N N . HIS A 1 146 ? 9.124 4.622 78.208 1.00 22.89 ? 146 HIS A N 1 ATOM 1103 C CA . HIS A 1 146 ? 7.689 4.713 78.410 1.00 22.58 ? 146 HIS A CA 1 ATOM 1104 C C . HIS A 1 146 ? 6.927 4.627 77.092 1.00 22.61 ? 146 HIS A C 1 ATOM 1105 O O . HIS A 1 146 ? 5.712 4.807 77.042 1.00 25.61 ? 146 HIS A O 1 ATOM 1106 C CB . HIS A 1 146 ? 7.351 5.992 79.186 1.00 23.95 ? 146 HIS A CB 1 ATOM 1107 C CG . HIS A 1 146 ? 7.798 5.947 80.614 1.00 21.40 ? 146 HIS A CG 1 ATOM 1108 N ND1 . HIS A 1 146 ? 6.929 5.720 81.660 1.00 25.50 ? 146 HIS A ND1 1 ATOM 1109 C CD2 . HIS A 1 146 ? 9.035 6.006 81.160 1.00 20.47 ? 146 HIS A CD2 1 ATOM 1110 C CE1 . HIS A 1 146 ? 7.612 5.637 82.787 1.00 21.21 ? 146 HIS A CE1 1 ATOM 1111 N NE2 . HIS A 1 146 ? 8.892 5.806 82.512 1.00 24.55 ? 146 HIS A NE2 1 ATOM 1112 N N . ASN A 1 147 ? 7.657 4.350 76.019 1.00 23.74 ? 147 ASN A N 1 ATOM 1113 C CA . ASN A 1 147 ? 7.043 4.168 74.715 1.00 25.67 ? 147 ASN A CA 1 ATOM 1114 C C . ASN A 1 147 ? 6.663 2.692 74.752 1.00 29.07 ? 147 ASN A C 1 ATOM 1115 O O . ASN A 1 147 ? 7.451 1.825 74.384 1.00 28.15 ? 147 ASN A O 1 ATOM 1116 C CB . ASN A 1 147 ? 8.058 4.448 73.604 1.00 23.81 ? 147 ASN A CB 1 ATOM 1117 C CG . ASN A 1 147 ? 7.559 4.027 72.239 1.00 21.38 ? 147 ASN A CG 1 ATOM 1118 O OD1 . ASN A 1 147 ? 6.363 4.089 71.952 1.00 22.47 ? 147 ASN A OD1 1 ATOM 1119 N ND2 . ASN A 1 147 ? 8.480 3.611 71.378 1.00 22.31 ? 147 ASN A ND2 1 ATOM 1120 N N . ILE A 1 148 ? 5.450 2.418 75.216 1.00 33.14 ? 148 ILE A N 1 ATOM 1121 C CA . ILE A 1 148 ? 4.986 1.047 75.370 1.00 39.09 ? 148 ILE A CA 1 ATOM 1122 C C . ILE A 1 148 ? 4.144 0.516 74.225 1.00 42.26 ? 148 ILE A C 1 ATOM 1123 O O . ILE A 1 148 ? 3.104 1.080 73.882 1.00 43.57 ? 148 ILE A O 1 ATOM 1124 C CB . ILE A 1 148 ? 4.180 0.890 76.687 1.00 39.63 ? 148 ILE A CB 1 ATOM 1125 C CG1 . ILE A 1 148 ? 5.003 1.412 77.868 1.00 40.36 ? 148 ILE A CG1 1 ATOM 1126 C CG2 . ILE A 1 148 ? 3.823 -0.573 76.915 1.00 39.68 ? 148 ILE A CG2 1 ATOM 1127 C CD1 . ILE A 1 148 ? 6.331 0.700 78.067 1.00 41.02 ? 148 ILE A CD1 1 ATOM 1128 N N . ARG A 1 149 ? 4.613 -0.581 73.640 1.00 46.03 ? 149 ARG A N 1 ATOM 1129 C CA . ARG A 1 149 ? 3.916 -1.241 72.546 1.00 50.00 ? 149 ARG A CA 1 ATOM 1130 C C . ARG A 1 149 ? 3.654 -2.692 72.933 1.00 51.72 ? 149 ARG A C 1 ATOM 1131 O O . ARG A 1 149 ? 4.300 -3.611 72.426 1.00 53.47 ? 149 ARG A O 1 ATOM 1132 C CB . ARG A 1 149 ? 4.750 -1.179 71.263 1.00 50.96 ? 149 ARG A CB 1 ATOM 1133 C CG . ARG A 1 149 ? 4.716 0.179 70.585 1.00 52.86 ? 149 ARG A CG 1 ATOM 1134 C CD . ARG A 1 149 ? 5.473 0.165 69.271 1.00 53.19 ? 149 ARG A CD 1 ATOM 1135 N NE . ARG A 1 149 ? 5.299 1.411 68.530 1.00 53.95 ? 149 ARG A NE 1 ATOM 1136 C CZ . ARG A 1 149 ? 4.149 1.808 67.995 1.00 54.17 ? 149 ARG A CZ 1 ATOM 1137 N NH1 . ARG A 1 149 ? 3.064 1.053 68.115 1.00 54.39 ? 149 ARG A NH1 1 ATOM 1138 N NH2 . ARG A 1 149 ? 4.080 2.961 67.342 1.00 53.75 ? 149 ARG A NH2 1 ATOM 1139 N N . GLY A 1 150 ? 2.703 -2.882 73.845 1.00 52.53 ? 150 GLY A N 1 ATOM 1140 C CA . GLY A 1 150 ? 2.359 -4.215 74.306 1.00 53.13 ? 150 GLY A CA 1 ATOM 1141 C C . GLY A 1 150 ? 2.223 -4.285 75.817 1.00 54.05 ? 150 GLY A C 1 ATOM 1142 O O . GLY A 1 150 ? 2.768 -5.189 76.454 1.00 54.96 ? 150 GLY A O 1 ATOM 1143 N N . GLY A 1 151 ? 1.497 -3.332 76.395 1.00 53.83 ? 151 GLY A N 1 ATOM 1144 C CA . GLY A 1 151 ? 1.312 -3.317 77.835 1.00 53.59 ? 151 GLY A CA 1 ATOM 1145 C C . GLY A 1 151 ? 0.505 -2.130 78.334 1.00 53.38 ? 151 GLY A C 1 ATOM 1146 O O . GLY A 1 151 ? -0.114 -1.419 77.540 1.00 54.12 ? 151 GLY A O 1 ATOM 1147 N N . PRO A 1 152 ? 0.497 -1.889 79.657 1.00 52.80 ? 152 PRO A N 1 ATOM 1148 C CA . PRO A 1 152 ? -0.236 -0.782 80.282 1.00 51.90 ? 152 PRO A CA 1 ATOM 1149 C C . PRO A 1 152 ? 0.330 0.586 79.905 1.00 50.70 ? 152 PRO A C 1 ATOM 1150 O O . PRO A 1 152 ? 1.248 1.094 80.552 1.00 51.57 ? 152 PRO A O 1 ATOM 1151 C CB . PRO A 1 152 ? -0.089 -1.077 81.769 1.00 52.42 ? 152 PRO A CB 1 ATOM 1152 C CG . PRO A 1 152 ? 1.277 -1.682 81.840 1.00 53.24 ? 152 PRO A CG 1 ATOM 1153 C CD . PRO A 1 152 ? 1.266 -2.639 80.667 1.00 53.00 ? 152 PRO A CD 1 ATOM 1154 N N . GLY A 1 153 ? -0.231 1.179 78.858 1.00 48.66 ? 153 GLY A N 1 ATOM 1155 C CA . GLY A 1 153 ? 0.227 2.477 78.402 1.00 44.70 ? 153 GLY A CA 1 ATOM 1156 C C . GLY A 1 153 ? 0.024 2.587 76.906 1.00 41.72 ? 153 GLY A C 1 ATOM 1157 O O . GLY A 1 153 ? -0.624 1.734 76.304 1.00 43.49 ? 153 GLY A O 1 ATOM 1158 N N . LYS A 1 154 ? 0.580 3.629 76.298 1.00 38.57 ? 154 LYS A N 1 ATOM 1159 C CA . LYS A 1 154 ? 0.441 3.829 74.863 1.00 33.75 ? 154 LYS A CA 1 ATOM 1160 C C . LYS A 1 154 ? 1.788 4.186 74.250 1.00 31.20 ? 154 LYS A C 1 ATOM 1161 O O . LYS A 1 154 ? 2.762 4.438 74.962 1.00 30.91 ? 154 LYS A O 1 ATOM 1162 C CB . LYS A 1 154 ? -0.566 4.951 74.582 1.00 35.47 ? 154 LYS A CB 1 ATOM 1163 C CG . LYS A 1 154 ? -0.158 6.305 75.159 1.00 35.80 ? 154 LYS A CG 1 ATOM 1164 C CD . LYS A 1 154 ? -1.074 7.434 74.694 1.00 34.28 ? 154 LYS A CD 1 ATOM 1165 C CE . LYS A 1 154 ? -2.481 7.293 75.257 1.00 36.66 ? 154 LYS A CE 1 ATOM 1166 N NZ . LYS A 1 154 ? -3.354 8.440 74.867 1.00 35.73 ? 154 LYS A NZ 1 ATOM 1167 N N . PRO A 1 155 ? 1.871 4.196 72.913 1.00 28.78 ? 155 PRO A N 1 ATOM 1168 C CA . PRO A 1 155 ? 3.162 4.545 72.322 1.00 27.22 ? 155 PRO A CA 1 ATOM 1169 C C . PRO A 1 155 ? 3.506 6.007 72.607 1.00 22.92 ? 155 PRO A C 1 ATOM 1170 O O . PRO A 1 155 ? 2.618 6.843 72.765 1.00 22.45 ? 155 PRO A O 1 ATOM 1171 C CB . PRO A 1 155 ? 2.949 4.269 70.836 1.00 27.49 ? 155 PRO A CB 1 ATOM 1172 C CG . PRO A 1 155 ? 1.488 4.527 70.647 1.00 32.37 ? 155 PRO A CG 1 ATOM 1173 C CD . PRO A 1 155 ? 0.874 3.886 71.873 1.00 30.22 ? 155 PRO A CD 1 ATOM 1174 N N . LEU A 1 156 ? 4.799 6.287 72.695 1.00 20.85 ? 156 LEU A N 1 ATOM 1175 C CA . LEU A 1 156 ? 5.288 7.636 72.942 1.00 20.38 ? 156 LEU A CA 1 ATOM 1176 C C . LEU A 1 156 ? 6.327 7.879 71.856 1.00 19.10 ? 156 LEU A C 1 ATOM 1177 O O . LEU A 1 156 ? 7.384 7.248 71.842 1.00 20.41 ? 156 LEU A O 1 ATOM 1178 C CB . LEU A 1 156 ? 5.926 7.723 74.334 1.00 20.02 ? 156 LEU A CB 1 ATOM 1179 C CG . LEU A 1 156 ? 6.274 9.118 74.870 1.00 20.99 ? 156 LEU A CG 1 ATOM 1180 C CD1 . LEU A 1 156 ? 6.517 9.026 76.367 1.00 22.41 ? 156 LEU A CD1 1 ATOM 1181 C CD2 . LEU A 1 156 ? 7.498 9.682 74.150 1.00 20.43 ? 156 LEU A CD2 1 ATOM 1182 N N . HIS A 1 157 ? 6.006 8.775 70.930 1.00 19.86 ? 157 HIS A N 1 ATOM 1183 C CA . HIS A 1 157 ? 6.902 9.086 69.830 1.00 19.69 ? 157 HIS A CA 1 ATOM 1184 C C . HIS A 1 157 ? 7.934 10.106 70.279 1.00 18.67 ? 157 HIS A C 1 ATOM 1185 O O . HIS A 1 157 ? 7.596 11.269 70.503 1.00 18.10 ? 157 HIS A O 1 ATOM 1186 C CB . HIS A 1 157 ? 6.096 9.638 68.656 1.00 22.25 ? 157 HIS A CB 1 ATOM 1187 C CG . HIS A 1 157 ? 5.015 8.716 68.182 1.00 25.57 ? 157 HIS A CG 1 ATOM 1188 N ND1 . HIS A 1 157 ? 5.280 7.542 67.509 1.00 27.51 ? 157 HIS A ND1 1 ATOM 1189 C CD2 . HIS A 1 157 ? 3.668 8.783 68.304 1.00 26.57 ? 157 HIS A CD2 1 ATOM 1190 C CE1 . HIS A 1 157 ? 4.143 6.925 67.238 1.00 27.75 ? 157 HIS A CE1 1 ATOM 1191 N NE2 . HIS A 1 157 ? 3.150 7.657 67.709 1.00 26.95 ? 157 HIS A NE2 1 ATOM 1192 N N . LEU A 1 158 ? 9.183 9.662 70.411 1.00 17.60 ? 158 LEU A N 1 ATOM 1193 C CA . LEU A 1 158 ? 10.274 10.536 70.834 1.00 18.03 ? 158 LEU A CA 1 ATOM 1194 C C . LEU A 1 158 ? 10.972 11.119 69.614 1.00 18.13 ? 158 LEU A C 1 ATOM 1195 O O . LEU A 1 158 ? 11.486 10.387 68.767 1.00 16.78 ? 158 LEU A O 1 ATOM 1196 C CB . LEU A 1 158 ? 11.284 9.763 71.681 1.00 17.32 ? 158 LEU A CB 1 ATOM 1197 C CG . LEU A 1 158 ? 12.542 10.547 72.062 1.00 16.29 ? 158 LEU A CG 1 ATOM 1198 C CD1 . LEU A 1 158 ? 12.157 11.813 72.832 1.00 15.96 ? 158 LEU A CD1 1 ATOM 1199 C CD2 . LEU A 1 158 ? 13.458 9.671 72.898 1.00 17.14 ? 158 LEU A CD2 1 ATOM 1200 N N . THR A 1 159 ? 11.001 12.443 69.529 1.00 16.92 ? 159 THR A N 1 ATOM 1201 C CA . THR A 1 159 ? 11.616 13.093 68.385 1.00 16.44 ? 159 THR A CA 1 ATOM 1202 C C . THR A 1 159 ? 12.504 14.266 68.778 1.00 14.87 ? 159 THR A C 1 ATOM 1203 O O . THR A 1 159 ? 12.492 14.720 69.926 1.00 13.08 ? 159 THR A O 1 ATOM 1204 C CB . THR A 1 159 ? 10.536 13.631 67.415 1.00 17.95 ? 159 THR A CB 1 ATOM 1205 O OG1 . THR A 1 159 ? 9.826 14.714 68.037 1.00 18.16 ? 159 THR A OG1 1 ATOM 1206 C CG2 . THR A 1 159 ? 9.547 12.531 67.048 1.00 19.35 ? 159 THR A CG2 1 ATOM 1207 N N . ALA A 1 160 ? 13.287 14.728 67.807 1.00 15.95 ? 160 ALA A N 1 ATOM 1208 C CA . ALA A 1 160 ? 14.155 15.883 67.982 1.00 14.24 ? 160 ALA A CA 1 ATOM 1209 C C . ALA A 1 160 ? 14.035 16.721 66.717 1.00 15.43 ? 160 ALA A C 1 ATOM 1210 O O . ALA A 1 160 ? 13.930 16.190 65.610 1.00 13.46 ? 160 ALA A O 1 ATOM 1211 C CB . ALA A 1 160 ? 15.611 15.452 68.183 1.00 15.53 ? 160 ALA A CB 1 ATOM 1212 N N . THR A 1 161 ? 14.033 18.036 66.887 1.00 14.28 ? 161 THR A N 1 ATOM 1213 C CA . THR A 1 161 ? 13.957 18.943 65.753 1.00 15.48 ? 161 THR A CA 1 ATOM 1214 C C . THR A 1 161 ? 15.285 19.676 65.816 1.00 15.74 ? 161 THR A C 1 ATOM 1215 O O . THR A 1 161 ? 15.550 20.442 66.745 1.00 18.09 ? 161 THR A O 1 ATOM 1216 C CB . THR A 1 161 ? 12.760 19.890 65.894 1.00 15.68 ? 161 THR A CB 1 ATOM 1217 O OG1 . THR A 1 161 ? 11.557 19.113 65.924 1.00 16.81 ? 161 THR A OG1 1 ATOM 1218 C CG2 . THR A 1 161 ? 12.693 20.853 64.719 1.00 15.86 ? 161 THR A CG2 1 ATOM 1219 N N . VAL A 1 162 ? 16.117 19.424 64.815 1.00 14.98 ? 162 VAL A N 1 ATOM 1220 C CA . VAL A 1 162 ? 17.471 19.955 64.782 1.00 16.26 ? 162 VAL A CA 1 ATOM 1221 C C . VAL A 1 162 ? 17.807 20.893 63.633 1.00 16.33 ? 162 VAL A C 1 ATOM 1222 O O . VAL A 1 162 ? 17.067 20.998 62.657 1.00 14.10 ? 162 VAL A O 1 ATOM 1223 C CB . VAL A 1 162 ? 18.472 18.780 64.727 1.00 17.05 ? 162 VAL A CB 1 ATOM 1224 C CG1 . VAL A 1 162 ? 18.185 17.800 65.865 1.00 16.52 ? 162 VAL A CG1 1 ATOM 1225 C CG2 . VAL A 1 162 ? 18.347 18.051 63.388 1.00 15.31 ? 162 VAL A CG2 1 ATOM 1226 N N . ARG A 1 163 ? 18.945 21.569 63.774 1.00 17.92 ? 163 ARG A N 1 ATOM 1227 C CA . ARG A 1 163 ? 19.445 22.475 62.747 1.00 20.01 ? 163 ARG A CA 1 ATOM 1228 C C . ARG A 1 163 ? 19.979 21.605 61.619 1.00 20.25 ? 163 ARG A C 1 ATOM 1229 O O . ARG A 1 163 ? 20.319 20.441 61.826 1.00 21.28 ? 163 ARG A O 1 ATOM 1230 C CB . ARG A 1 163 ? 20.576 23.339 63.306 1.00 21.18 ? 163 ARG A CB 1 ATOM 1231 C CG . ARG A 1 163 ? 20.118 24.387 64.300 1.00 25.70 ? 163 ARG A CG 1 ATOM 1232 C CD . ARG A 1 163 ? 19.894 25.704 63.598 1.00 26.70 ? 163 ARG A CD 1 ATOM 1233 N NE . ARG A 1 163 ? 19.442 26.751 64.509 1.00 26.96 ? 163 ARG A NE 1 ATOM 1234 C CZ . ARG A 1 163 ? 19.386 28.036 64.178 1.00 27.91 ? 163 ARG A CZ 1 ATOM 1235 N NH1 . ARG A 1 163 ? 19.762 28.420 62.966 1.00 27.21 ? 163 ARG A NH1 1 ATOM 1236 N NH2 . ARG A 1 163 ? 18.944 28.930 65.050 1.00 26.05 ? 163 ARG A NH2 1 ATOM 1237 N N . CYS A 1 164 ? 20.073 22.188 60.433 1.00 20.42 ? 164 CYS A N 1 ATOM 1238 C CA . CYS A 1 164 ? 20.534 21.482 59.244 1.00 22.20 ? 164 CYS A CA 1 ATOM 1239 C C . CYS A 1 164 ? 21.975 20.961 59.341 1.00 23.51 ? 164 CYS A C 1 ATOM 1240 O O . CYS A 1 164 ? 22.266 19.825 58.951 1.00 22.54 ? 164 CYS A O 1 ATOM 1241 C CB . CYS A 1 164 ? 20.383 22.420 58.040 1.00 24.77 ? 164 CYS A CB 1 ATOM 1242 S SG . CYS A 1 164 ? 20.444 21.630 56.425 1.00 33.69 ? 164 CYS A SG 1 ATOM 1243 N N . GLY A 1 165 ? 22.862 21.788 59.884 1.00 23.86 ? 165 GLY A N 1 ATOM 1244 C CA . GLY A 1 165 ? 24.267 21.432 60.001 1.00 25.30 ? 165 GLY A CA 1 ATOM 1245 C C . GLY A 1 165 ? 24.647 20.163 60.742 1.00 26.86 ? 165 GLY A C 1 ATOM 1246 O O . GLY A 1 165 ? 24.115 19.857 61.808 1.00 26.41 ? 165 GLY A O 1 ATOM 1247 N N . TYR A 1 166 ? 25.591 19.425 60.167 1.00 27.94 ? 166 TYR A N 1 ATOM 1248 C CA . TYR A 1 166 ? 26.076 18.192 60.769 1.00 28.02 ? 166 TYR A CA 1 ATOM 1249 C C . TYR A 1 166 ? 27.588 18.295 60.976 1.00 29.65 ? 166 TYR A C 1 ATOM 1250 O O . TYR A 1 166 ? 28.307 18.755 60.093 1.00 29.77 ? 166 TYR A O 1 ATOM 1251 C CB . TYR A 1 166 ? 25.776 16.997 59.865 1.00 28.00 ? 166 TYR A CB 1 ATOM 1252 C CG . TYR A 1 166 ? 26.111 15.693 60.537 1.00 27.96 ? 166 TYR A CG 1 ATOM 1253 C CD1 . TYR A 1 166 ? 25.179 15.048 61.346 1.00 28.39 ? 166 TYR A CD1 1 ATOM 1254 C CD2 . TYR A 1 166 ? 27.397 15.159 60.455 1.00 28.23 ? 166 TYR A CD2 1 ATOM 1255 C CE1 . TYR A 1 166 ? 25.517 13.907 62.063 1.00 29.26 ? 166 TYR A CE1 1 ATOM 1256 C CE2 . TYR A 1 166 ? 27.746 14.017 61.169 1.00 29.35 ? 166 TYR A CE2 1 ATOM 1257 C CZ . TYR A 1 166 ? 26.802 13.399 61.972 1.00 30.66 ? 166 TYR A CZ 1 ATOM 1258 O OH . TYR A 1 166 ? 27.149 12.286 62.702 1.00 32.64 ? 166 TYR A OH 1 ATOM 1259 N N . PRO A 1 167 ? 28.094 17.855 62.139 1.00 29.42 ? 167 PRO A N 1 ATOM 1260 C CA . PRO A 1 167 ? 27.367 17.268 63.268 1.00 28.82 ? 167 PRO A CA 1 ATOM 1261 C C . PRO A 1 167 ? 26.623 18.316 64.087 1.00 27.11 ? 167 PRO A C 1 ATOM 1262 O O . PRO A 1 167 ? 26.908 19.510 63.996 1.00 27.23 ? 167 PRO A O 1 ATOM 1263 C CB . PRO A 1 167 ? 28.477 16.597 64.069 1.00 29.25 ? 167 PRO A CB 1 ATOM 1264 C CG . PRO A 1 167 ? 29.605 17.552 63.892 1.00 30.90 ? 167 PRO A CG 1 ATOM 1265 C CD . PRO A 1 167 ? 29.544 17.860 62.407 1.00 30.48 ? 167 PRO A CD 1 ATOM 1266 N N . PRO A 1 168 ? 25.663 17.875 64.910 1.00 27.04 ? 168 PRO A N 1 ATOM 1267 C CA . PRO A 1 168 ? 24.871 18.773 65.753 1.00 26.55 ? 168 PRO A CA 1 ATOM 1268 C C . PRO A 1 168 ? 25.654 19.285 66.954 1.00 26.07 ? 168 PRO A C 1 ATOM 1269 O O . PRO A 1 168 ? 26.760 18.822 67.232 1.00 25.89 ? 168 PRO A O 1 ATOM 1270 C CB . PRO A 1 168 ? 23.711 17.890 66.183 1.00 27.32 ? 168 PRO A CB 1 ATOM 1271 C CG . PRO A 1 168 ? 24.391 16.559 66.362 1.00 27.14 ? 168 PRO A CG 1 ATOM 1272 C CD . PRO A 1 168 ? 25.248 16.472 65.109 1.00 26.60 ? 168 PRO A CD 1 ATOM 1273 N N . ALA A 1 169 ? 25.069 20.241 67.665 1.00 25.62 ? 169 ALA A N 1 ATOM 1274 C CA . ALA A 1 169 ? 25.689 20.788 68.860 1.00 25.46 ? 169 ALA A CA 1 ATOM 1275 C C . ALA A 1 169 ? 25.873 19.617 69.830 1.00 26.73 ? 169 ALA A C 1 ATOM 1276 O O . ALA A 1 169 ? 25.103 18.656 69.803 1.00 24.57 ? 169 ALA A O 1 ATOM 1277 C CB . ALA A 1 169 ? 24.790 21.850 69.476 1.00 26.02 ? 169 ALA A CB 1 ATOM 1278 N N . ALA A 1 170 ? 26.889 19.708 70.678 1.00 25.10 ? 170 ALA A N 1 ATOM 1279 C CA . ALA A 1 170 ? 27.207 18.656 71.638 1.00 25.96 ? 170 ALA A CA 1 ATOM 1280 C C . ALA A 1 170 ? 26.040 18.129 72.474 1.00 25.08 ? 170 ALA A C 1 ATOM 1281 O O . ALA A 1 170 ? 25.900 16.916 72.638 1.00 24.60 ? 170 ALA A O 1 ATOM 1282 C CB . ALA A 1 170 ? 28.332 19.129 72.561 1.00 27.41 ? 170 ALA A CB 1 ATOM 1283 N N . HIS A 1 171 ? 25.207 19.019 73.007 1.00 24.06 ? 171 HIS A N 1 ATOM 1284 C CA . HIS A 1 171 ? 24.091 18.569 73.836 1.00 22.91 ? 171 HIS A CA 1 ATOM 1285 C C . HIS A 1 171 ? 23.074 17.761 73.036 1.00 22.94 ? 171 HIS A C 1 ATOM 1286 O O . HIS A 1 171 ? 22.443 16.842 73.571 1.00 23.41 ? 171 HIS A O 1 ATOM 1287 C CB . HIS A 1 171 ? 23.420 19.756 74.540 1.00 23.55 ? 171 HIS A CB 1 ATOM 1288 C CG . HIS A 1 171 ? 22.837 20.773 73.609 1.00 22.87 ? 171 HIS A CG 1 ATOM 1289 N ND1 . HIS A 1 171 ? 21.491 20.827 73.317 1.00 23.69 ? 171 HIS A ND1 1 ATOM 1290 C CD2 . HIS A 1 171 ? 23.413 21.785 72.919 1.00 21.94 ? 171 HIS A CD2 1 ATOM 1291 C CE1 . HIS A 1 171 ? 21.263 21.833 72.490 1.00 20.73 ? 171 HIS A CE1 1 ATOM 1292 N NE2 . HIS A 1 171 ? 22.413 22.430 72.233 1.00 23.25 ? 171 HIS A NE2 1 ATOM 1293 N N . VAL A 1 172 ? 22.924 18.092 71.757 1.00 21.78 ? 172 VAL A N 1 ATOM 1294 C CA . VAL A 1 172 ? 22.008 17.367 70.889 1.00 21.78 ? 172 VAL A CA 1 ATOM 1295 C C . VAL A 1 172 ? 22.650 16.032 70.540 1.00 22.98 ? 172 VAL A C 1 ATOM 1296 O O . VAL A 1 172 ? 21.994 14.991 70.549 1.00 23.36 ? 172 VAL A O 1 ATOM 1297 C CB . VAL A 1 172 ? 21.726 18.150 69.584 1.00 21.47 ? 172 VAL A CB 1 ATOM 1298 C CG1 . VAL A 1 172 ? 20.954 17.278 68.596 1.00 20.82 ? 172 VAL A CG1 1 ATOM 1299 C CG2 . VAL A 1 172 ? 20.924 19.400 69.909 1.00 20.03 ? 172 VAL A CG2 1 ATOM 1300 N N . GLY A 1 173 ? 23.943 16.072 70.236 1.00 24.00 ? 173 GLY A N 1 ATOM 1301 C CA . GLY A 1 173 ? 24.650 14.853 69.898 1.00 23.35 ? 173 GLY A CA 1 ATOM 1302 C C . GLY A 1 173 ? 24.610 13.861 71.045 1.00 22.44 ? 173 GLY A C 1 ATOM 1303 O O . GLY A 1 173 ? 24.481 12.663 70.820 1.00 23.58 ? 173 GLY A O 1 ATOM 1304 N N . ARG A 1 174 ? 24.718 14.357 72.273 1.00 22.19 ? 174 ARG A N 1 ATOM 1305 C CA . ARG A 1 174 ? 24.699 13.487 73.446 1.00 23.72 ? 174 ARG A CA 1 ATOM 1306 C C . ARG A 1 174 ? 23.365 12.761 73.563 1.00 23.47 ? 174 ARG A C 1 ATOM 1307 O O . ARG A 1 174 ? 23.317 11.566 73.864 1.00 23.44 ? 174 ARG A O 1 ATOM 1308 C CB . ARG A 1 174 ? 24.955 14.292 74.722 1.00 26.22 ? 174 ARG A CB 1 ATOM 1309 C CG . ARG A 1 174 ? 25.117 13.425 75.962 1.00 28.69 ? 174 ARG A CG 1 ATOM 1310 C CD . ARG A 1 174 ? 25.177 14.252 77.237 1.00 32.32 ? 174 ARG A CD 1 ATOM 1311 N NE . ARG A 1 174 ? 25.233 13.398 78.421 1.00 36.22 ? 174 ARG A NE 1 ATOM 1312 C CZ . ARG A 1 174 ? 26.343 12.834 78.888 1.00 38.56 ? 174 ARG A CZ 1 ATOM 1313 N NH1 . ARG A 1 174 ? 27.502 13.036 78.278 1.00 39.93 ? 174 ARG A NH1 1 ATOM 1314 N NH2 . ARG A 1 174 ? 26.291 12.056 79.962 1.00 39.22 ? 174 ARG A NH2 1 ATOM 1315 N N . ALA A 1 175 ? 22.279 13.488 73.329 1.00 21.90 ? 175 ALA A N 1 ATOM 1316 C CA . ALA A 1 175 ? 20.951 12.896 73.407 1.00 20.98 ? 175 ALA A CA 1 ATOM 1317 C C . ALA A 1 175 ? 20.750 11.861 72.299 1.00 19.99 ? 175 ALA A C 1 ATOM 1318 O O . ALA A 1 175 ? 20.312 10.738 72.555 1.00 19.84 ? 175 ALA A O 1 ATOM 1319 C CB . ALA A 1 175 ? 19.886 13.984 73.302 1.00 22.27 ? 175 ALA A CB 1 ATOM 1320 N N . LEU A 1 176 ? 21.076 12.242 71.069 1.00 19.25 ? 176 LEU A N 1 ATOM 1321 C CA . LEU A 1 176 ? 20.908 11.348 69.930 1.00 20.06 ? 176 LEU A CA 1 ATOM 1322 C C . LEU A 1 176 ? 21.776 10.098 70.023 1.00 21.52 ? 176 LEU A C 1 ATOM 1323 O O . LEU A 1 176 ? 21.411 9.050 69.490 1.00 21.77 ? 176 LEU A O 1 ATOM 1324 C CB . LEU A 1 176 ? 21.211 12.087 68.623 1.00 21.26 ? 176 LEU A CB 1 ATOM 1325 C CG . LEU A 1 176 ? 20.289 13.270 68.307 1.00 20.81 ? 176 LEU A CG 1 ATOM 1326 C CD1 . LEU A 1 176 ? 20.668 13.850 66.949 1.00 20.90 ? 176 LEU A CD1 1 ATOM 1327 C CD2 . LEU A 1 176 ? 18.832 12.818 68.304 1.00 21.67 ? 176 LEU A CD2 1 ATOM 1328 N N . ALA A 1 177 ? 22.915 10.215 70.701 1.00 21.94 ? 177 ALA A N 1 ATOM 1329 C CA . ALA A 1 177 ? 23.841 9.093 70.863 1.00 24.35 ? 177 ALA A CA 1 ATOM 1330 C C . ALA A 1 177 ? 23.215 7.888 71.562 1.00 26.03 ? 177 ALA A C 1 ATOM 1331 O O . ALA A 1 177 ? 23.721 6.768 71.447 1.00 26.63 ? 177 ALA A O 1 ATOM 1332 C CB . ALA A 1 177 ? 25.081 9.547 71.626 1.00 25.16 ? 177 ALA A CB 1 ATOM 1333 N N . THR A 1 178 ? 22.125 8.108 72.291 1.00 24.18 ? 178 THR A N 1 ATOM 1334 C CA . THR A 1 178 ? 21.457 7.008 72.976 1.00 23.91 ? 178 THR A CA 1 ATOM 1335 C C . THR A 1 178 ? 20.908 6.050 71.928 1.00 23.93 ? 178 THR A C 1 ATOM 1336 O O . THR A 1 178 ? 20.634 4.885 72.220 1.00 25.31 ? 178 THR A O 1 ATOM 1337 C CB . THR A 1 178 ? 20.286 7.502 73.841 1.00 24.32 ? 178 THR A CB 1 ATOM 1338 O OG1 . THR A 1 178 ? 19.331 8.178 73.011 1.00 24.77 ? 178 THR A OG1 1 ATOM 1339 C CG2 . THR A 1 178 ? 20.785 8.441 74.926 1.00 22.99 ? 178 THR A CG2 1 ATOM 1340 N N . GLY A 1 179 ? 20.739 6.566 70.713 1.00 22.05 ? 179 GLY A N 1 ATOM 1341 C CA . GLY A 1 179 ? 20.231 5.774 69.608 1.00 22.85 ? 179 GLY A CA 1 ATOM 1342 C C . GLY A 1 179 ? 18.749 5.460 69.656 1.00 23.57 ? 179 GLY A C 1 ATOM 1343 O O . GLY A 1 179 ? 18.232 4.791 68.757 1.00 27.04 ? 179 GLY A O 1 ATOM 1344 N N . ILE A 1 180 ? 18.045 5.951 70.671 1.00 21.89 ? 180 ILE A N 1 ATOM 1345 C CA . ILE A 1 180 ? 16.631 5.644 70.788 1.00 21.34 ? 180 ILE A CA 1 ATOM 1346 C C . ILE A 1 180 ? 15.610 6.662 70.281 1.00 20.35 ? 180 ILE A C 1 ATOM 1347 O O . ILE A 1 180 ? 14.424 6.557 70.592 1.00 20.45 ? 180 ILE A O 1 ATOM 1348 C CB . ILE A 1 180 ? 16.276 5.230 72.249 1.00 23.66 ? 180 ILE A CB 1 ATOM 1349 C CG1 . ILE A 1 180 ? 16.799 6.257 73.258 1.00 26.42 ? 180 ILE A CG1 1 ATOM 1350 C CG2 . ILE A 1 180 ? 16.897 3.874 72.556 1.00 22.99 ? 180 ILE A CG2 1 ATOM 1351 C CD1 . ILE A 1 180 ? 16.136 7.603 73.174 1.00 27.18 ? 180 ILE A CD1 1 ATOM 1352 N N . PHE A 1 181 ? 16.042 7.649 69.503 1.00 19.53 ? 181 PHE A N 1 ATOM 1353 C CA . PHE A 1 181 ? 15.064 8.593 68.970 1.00 18.42 ? 181 PHE A CA 1 ATOM 1354 C C . PHE A 1 181 ? 14.352 7.953 67.792 1.00 17.77 ? 181 PHE A C 1 ATOM 1355 O O . PHE A 1 181 ? 14.977 7.310 66.948 1.00 19.12 ? 181 PHE A O 1 ATOM 1356 C CB . PHE A 1 181 ? 15.722 9.900 68.533 1.00 19.05 ? 181 PHE A CB 1 ATOM 1357 C CG . PHE A 1 181 ? 15.963 10.848 69.663 1.00 17.92 ? 181 PHE A CG 1 ATOM 1358 C CD1 . PHE A 1 181 ? 16.977 10.605 70.589 1.00 18.88 ? 181 PHE A CD1 1 ATOM 1359 C CD2 . PHE A 1 181 ? 15.152 11.972 69.823 1.00 19.35 ? 181 PHE A CD2 1 ATOM 1360 C CE1 . PHE A 1 181 ? 17.186 11.470 71.667 1.00 18.74 ? 181 PHE A CE1 1 ATOM 1361 C CE2 . PHE A 1 181 ? 15.346 12.844 70.891 1.00 17.24 ? 181 PHE A CE2 1 ATOM 1362 C CZ . PHE A 1 181 ? 16.365 12.596 71.818 1.00 19.46 ? 181 PHE A CZ 1 ATOM 1363 N N . GLU A 1 182 ? 13.038 8.133 67.739 1.00 15.80 ? 182 GLU A N 1 ATOM 1364 C CA . GLU A 1 182 ? 12.235 7.562 66.673 1.00 17.09 ? 182 GLU A CA 1 ATOM 1365 C C . GLU A 1 182 ? 12.317 8.390 65.403 1.00 17.09 ? 182 GLU A C 1 ATOM 1366 O O . GLU A 1 182 ? 12.431 7.843 64.308 1.00 15.01 ? 182 GLU A O 1 ATOM 1367 C CB . GLU A 1 182 ? 10.782 7.465 67.120 1.00 18.31 ? 182 GLU A CB 1 ATOM 1368 C CG . GLU A 1 182 ? 9.871 6.762 66.142 1.00 21.38 ? 182 GLU A CG 1 ATOM 1369 C CD . GLU A 1 182 ? 8.434 6.827 66.583 1.00 26.25 ? 182 GLU A CD 1 ATOM 1370 O OE1 . GLU A 1 182 ? 8.140 6.382 67.716 1.00 29.95 ? 182 GLU A OE1 1 ATOM 1371 O OE2 . GLU A 1 182 ? 7.596 7.330 65.807 1.00 29.13 ? 182 GLU A OE2 1 ATOM 1372 N N . ARG A 1 183 ? 12.259 9.709 65.551 1.00 16.07 ? 183 ARG A N 1 ATOM 1373 C CA . ARG A 1 183 ? 12.313 10.596 64.393 1.00 16.02 ? 183 ARG A CA 1 ATOM 1374 C C . ARG A 1 183 ? 13.130 11.841 64.686 1.00 15.61 ? 183 ARG A C 1 ATOM 1375 O O . ARG A 1 183 ? 13.235 12.271 65.832 1.00 14.41 ? 183 ARG A O 1 ATOM 1376 C CB . ARG A 1 183 ? 10.916 11.077 64.003 1.00 17.25 ? 183 ARG A CB 1 ATOM 1377 C CG . ARG A 1 183 ? 9.817 10.050 64.091 1.00 19.83 ? 183 ARG A CG 1 ATOM 1378 C CD . ARG A 1 183 ? 8.461 10.682 63.820 1.00 23.14 ? 183 ARG A CD 1 ATOM 1379 N NE . ARG A 1 183 ? 7.388 9.711 64.006 1.00 23.82 ? 183 ARG A NE 1 ATOM 1380 C CZ . ARG A 1 183 ? 6.094 9.977 63.864 1.00 27.34 ? 183 ARG A CZ 1 ATOM 1381 N NH1 . ARG A 1 183 ? 5.692 11.195 63.531 1.00 26.67 ? 183 ARG A NH1 1 ATOM 1382 N NH2 . ARG A 1 183 ? 5.198 9.015 64.052 1.00 28.69 ? 183 ARG A NH2 1 ATOM 1383 N N . VAL A 1 184 ? 13.695 12.417 63.632 1.00 15.03 ? 184 VAL A N 1 ATOM 1384 C CA . VAL A 1 184 ? 14.449 13.662 63.748 1.00 15.49 ? 184 VAL A CA 1 ATOM 1385 C C . VAL A 1 184 ? 13.984 14.549 62.597 1.00 15.93 ? 184 VAL A C 1 ATOM 1386 O O . VAL A 1 184 ? 13.987 14.130 61.439 1.00 16.53 ? 184 VAL A O 1 ATOM 1387 C CB . VAL A 1 184 ? 15.979 13.438 63.649 1.00 16.82 ? 184 VAL A CB 1 ATOM 1388 C CG1 . VAL A 1 184 ? 16.696 14.776 63.407 1.00 18.21 ? 184 VAL A CG1 1 ATOM 1389 C CG2 . VAL A 1 184 ? 16.495 12.816 64.946 1.00 15.80 ? 184 VAL A CG2 1 ATOM 1390 N N . HIS A 1 185 ? 13.555 15.764 62.922 1.00 15.77 ? 185 HIS A N 1 ATOM 1391 C CA . HIS A 1 185 ? 13.097 16.702 61.905 1.00 16.59 ? 185 HIS A CA 1 ATOM 1392 C C . HIS A 1 185 ? 14.268 17.629 61.627 1.00 16.93 ? 185 HIS A C 1 ATOM 1393 O O . HIS A 1 185 ? 14.664 18.404 62.496 1.00 15.11 ? 185 HIS A O 1 ATOM 1394 C CB . HIS A 1 185 ? 11.911 17.529 62.416 1.00 17.67 ? 185 HIS A CB 1 ATOM 1395 C CG . HIS A 1 185 ? 10.812 16.712 63.021 1.00 19.51 ? 185 HIS A CG 1 ATOM 1396 N ND1 . HIS A 1 185 ? 10.490 16.778 64.361 1.00 20.41 ? 185 HIS A ND1 1 ATOM 1397 C CD2 . HIS A 1 185 ? 9.980 15.790 62.480 1.00 20.91 ? 185 HIS A CD2 1 ATOM 1398 C CE1 . HIS A 1 185 ? 9.510 15.929 64.618 1.00 19.95 ? 185 HIS A CE1 1 ATOM 1399 N NE2 . HIS A 1 185 ? 9.183 15.317 63.495 1.00 21.07 ? 185 HIS A NE2 1 ATOM 1400 N N . VAL A 1 186 ? 14.822 17.550 60.422 1.00 15.58 ? 186 VAL A N 1 ATOM 1401 C CA . VAL A 1 186 ? 15.962 18.389 60.067 1.00 15.88 ? 186 VAL A CA 1 ATOM 1402 C C . VAL A 1 186 ? 15.476 19.694 59.451 1.00 14.52 ? 186 VAL A C 1 ATOM 1403 O O . VAL A 1 186 ? 14.940 19.705 58.347 1.00 15.36 ? 186 VAL A O 1 ATOM 1404 C CB . VAL A 1 186 ? 16.882 17.673 59.060 1.00 15.81 ? 186 VAL A CB 1 ATOM 1405 C CG1 . VAL A 1 186 ? 18.091 18.541 58.755 1.00 17.12 ? 186 VAL A CG1 1 ATOM 1406 C CG2 . VAL A 1 186 ? 17.334 16.330 59.635 1.00 17.34 ? 186 VAL A CG2 1 ATOM 1407 N N . ARG A 1 187 ? 15.662 20.795 60.174 1.00 15.35 ? 187 ARG A N 1 ATOM 1408 C CA . ARG A 1 187 ? 15.235 22.098 59.681 1.00 16.13 ? 187 ARG A CA 1 ATOM 1409 C C . ARG A 1 187 ? 16.164 22.561 58.555 1.00 18.19 ? 187 ARG A C 1 ATOM 1410 O O . ARG A 1 187 ? 17.363 22.737 58.770 1.00 21.37 ? 187 ARG A O 1 ATOM 1411 C CB . ARG A 1 187 ? 15.253 23.110 60.827 1.00 13.75 ? 187 ARG A CB 1 ATOM 1412 C CG . ARG A 1 187 ? 14.127 22.931 61.846 1.00 17.18 ? 187 ARG A CG 1 ATOM 1413 C CD . ARG A 1 187 ? 14.303 23.894 63.014 1.00 19.72 ? 187 ARG A CD 1 ATOM 1414 N NE . ARG A 1 187 ? 15.107 23.306 64.086 1.00 23.90 ? 187 ARG A NE 1 ATOM 1415 C CZ . ARG A 1 187 ? 15.929 23.990 64.870 1.00 22.76 ? 187 ARG A CZ 1 ATOM 1416 N NH1 . ARG A 1 187 ? 16.078 25.298 64.702 1.00 24.19 ? 187 ARG A NH1 1 ATOM 1417 N NH2 . ARG A 1 187 ? 16.584 23.372 65.844 1.00 25.04 ? 187 ARG A NH2 1 ATOM 1418 N N . THR A 1 188 ? 15.613 22.746 57.359 1.00 16.77 ? 188 THR A N 1 ATOM 1419 C CA . THR A 1 188 ? 16.412 23.184 56.214 1.00 16.89 ? 188 THR A CA 1 ATOM 1420 C C . THR A 1 188 ? 16.023 24.594 55.786 1.00 17.90 ? 188 THR A C 1 ATOM 1421 O O . THR A 1 188 ? 16.496 25.095 54.760 1.00 17.71 ? 188 THR A O 1 ATOM 1422 C CB . THR A 1 188 ? 16.217 22.258 54.997 1.00 17.52 ? 188 THR A CB 1 ATOM 1423 O OG1 . THR A 1 188 ? 14.866 22.349 54.527 1.00 19.08 ? 188 THR A OG1 1 ATOM 1424 C CG2 . THR A 1 188 ? 16.520 20.818 55.371 1.00 17.81 ? 188 THR A CG2 1 ATOM 1425 N N . TYR A 1 189 ? 15.173 25.232 56.581 1.00 16.93 ? 189 TYR A N 1 ATOM 1426 C CA . TYR A 1 189 ? 14.693 26.569 56.260 1.00 17.22 ? 189 TYR A CA 1 ATOM 1427 C C . TYR A 1 189 ? 15.307 27.702 57.072 1.00 19.66 ? 189 TYR A C 1 ATOM 1428 O O . TYR A 1 189 ? 14.885 28.852 56.935 1.00 20.92 ? 189 TYR A O 1 ATOM 1429 C CB . TYR A 1 189 ? 13.164 26.611 56.387 1.00 16.53 ? 189 TYR A CB 1 ATOM 1430 C CG . TYR A 1 189 ? 12.649 26.115 57.719 1.00 16.28 ? 189 TYR A CG 1 ATOM 1431 C CD1 . TYR A 1 189 ? 12.274 24.776 57.890 1.00 16.08 ? 189 TYR A CD1 1 ATOM 1432 C CD2 . TYR A 1 189 ? 12.544 26.973 58.811 1.00 16.01 ? 189 TYR A CD2 1 ATOM 1433 C CE1 . TYR A 1 189 ? 11.803 24.311 59.116 1.00 16.87 ? 189 TYR A CE1 1 ATOM 1434 C CE2 . TYR A 1 189 ? 12.077 26.517 60.049 1.00 17.35 ? 189 TYR A CE2 1 ATOM 1435 C CZ . TYR A 1 189 ? 11.707 25.185 60.190 1.00 17.60 ? 189 TYR A CZ 1 ATOM 1436 O OH . TYR A 1 189 ? 11.232 24.737 61.398 1.00 16.64 ? 189 TYR A OH 1 ATOM 1437 N N . GLU A 1 190 ? 16.285 27.392 57.922 1.00 19.35 ? 190 GLU A N 1 ATOM 1438 C CA . GLU A 1 190 ? 16.952 28.430 58.709 1.00 21.74 ? 190 GLU A CA 1 ATOM 1439 C C . GLU A 1 190 ? 17.922 29.117 57.746 1.00 24.20 ? 190 GLU A C 1 ATOM 1440 O O . GLU A 1 190 ? 18.337 28.519 56.751 1.00 24.67 ? 190 GLU A O 1 ATOM 1441 C CB . GLU A 1 190 ? 17.722 27.817 59.886 1.00 22.09 ? 190 GLU A CB 1 ATOM 1442 C CG . GLU A 1 190 ? 16.867 26.988 60.855 1.00 20.78 ? 190 GLU A CG 1 ATOM 1443 C CD . GLU A 1 190 ? 15.933 27.824 61.727 1.00 24.98 ? 190 GLU A CD 1 ATOM 1444 O OE1 . GLU A 1 190 ? 15.794 29.042 61.479 1.00 24.58 ? 190 GLU A OE1 1 ATOM 1445 O OE2 . GLU A 1 190 ? 15.330 27.258 62.665 1.00 20.73 ? 190 GLU A OE2 1 ATOM 1446 N N . SER A 1 191 ? 18.290 30.360 58.034 1.00 25.67 ? 191 SER A N 1 ATOM 1447 C CA . SER A 1 191 ? 19.187 31.100 57.148 1.00 28.81 ? 191 SER A CA 1 ATOM 1448 C C . SER A 1 191 ? 20.621 30.567 57.098 1.00 29.53 ? 191 SER A C 1 ATOM 1449 O O . SER A 1 191 ? 21.404 30.972 56.235 1.00 31.33 ? 191 SER A O 1 ATOM 1450 C CB . SER A 1 191 ? 19.205 32.580 57.545 1.00 28.75 ? 191 SER A CB 1 ATOM 1451 O OG . SER A 1 191 ? 19.704 32.741 58.859 1.00 34.10 ? 191 SER A OG 1 ATOM 1452 N N . ASP A 1 192 ? 20.949 29.657 58.011 1.00 28.64 ? 192 ASP A N 1 ATOM 1453 C CA . ASP A 1 192 ? 22.282 29.063 58.102 1.00 29.82 ? 192 ASP A CA 1 ATOM 1454 C C . ASP A 1 192 ? 23.033 29.002 56.777 1.00 30.57 ? 192 ASP A C 1 ATOM 1455 O O . ASP A 1 192 ? 22.658 28.263 55.866 1.00 27.35 ? 192 ASP A O 1 ATOM 1456 C CB . ASP A 1 192 ? 22.192 27.652 58.694 1.00 31.34 ? 192 ASP A CB 1 ATOM 1457 C CG . ASP A 1 192 ? 21.526 27.636 60.054 1.00 33.09 ? 192 ASP A CG 1 ATOM 1458 O OD1 . ASP A 1 192 ? 21.239 28.731 60.582 1.00 34.11 ? 192 ASP A OD1 1 ATOM 1459 O OD2 . ASP A 1 192 ? 21.294 26.534 60.594 1.00 33.63 ? 192 ASP A OD2 1 ATOM 1460 N N . LYS A 1 193 ? 24.096 29.789 56.678 1.00 33.48 ? 193 LYS A N 1 ATOM 1461 C CA . LYS A 1 193 ? 24.904 29.819 55.471 1.00 36.16 ? 193 LYS A CA 1 ATOM 1462 C C . LYS A 1 193 ? 25.537 28.450 55.273 1.00 36.45 ? 193 LYS A C 1 ATOM 1463 O O . LYS A 1 193 ? 26.037 27.850 56.224 1.00 39.61 ? 193 LYS A O 1 ATOM 1464 C CB . LYS A 1 193 ? 26.001 30.881 55.592 1.00 39.16 ? 193 LYS A CB 1 ATOM 1465 C CG . LYS A 1 193 ? 26.936 30.948 54.392 1.00 42.34 ? 193 LYS A CG 1 ATOM 1466 C CD . LYS A 1 193 ? 27.980 32.050 54.541 1.00 46.62 ? 193 LYS A CD 1 ATOM 1467 C CE . LYS A 1 193 ? 28.900 31.812 55.732 1.00 49.05 ? 193 LYS A CE 1 ATOM 1468 N NZ . LYS A 1 193 ? 29.967 32.855 55.828 1.00 51.15 ? 193 LYS A NZ 1 ATOM 1469 N N . TRP A 1 194 ? 25.501 27.961 54.039 1.00 36.72 ? 194 TRP A N 1 ATOM 1470 C CA . TRP A 1 194 ? 26.082 26.666 53.696 1.00 36.76 ? 194 TRP A CA 1 ATOM 1471 C C . TRP A 1 194 ? 25.176 25.480 54.014 1.00 34.07 ? 194 TRP A C 1 ATOM 1472 O O . TRP A 1 194 ? 25.443 24.368 53.560 1.00 33.97 ? 194 TRP A O 1 ATOM 1473 C CB . TRP A 1 194 ? 27.420 26.455 54.420 1.00 40.72 ? 194 TRP A CB 1 ATOM 1474 C CG . TRP A 1 194 ? 28.469 27.485 54.130 1.00 46.31 ? 194 TRP A CG 1 ATOM 1475 C CD1 . TRP A 1 194 ? 29.114 28.271 55.040 1.00 47.24 ? 194 TRP A CD1 1 ATOM 1476 C CD2 . TRP A 1 194 ? 29.022 27.817 52.849 1.00 48.58 ? 194 TRP A CD2 1 ATOM 1477 N NE1 . TRP A 1 194 ? 30.035 29.072 54.409 1.00 49.65 ? 194 TRP A NE1 1 ATOM 1478 C CE2 . TRP A 1 194 ? 30.000 28.814 53.063 1.00 49.63 ? 194 TRP A CE2 1 ATOM 1479 C CE3 . TRP A 1 194 ? 28.787 27.369 51.542 1.00 50.59 ? 194 TRP A CE3 1 ATOM 1480 C CZ2 . TRP A 1 194 ? 30.746 29.372 52.018 1.00 50.62 ? 194 TRP A CZ2 1 ATOM 1481 C CZ3 . TRP A 1 194 ? 29.529 27.924 50.501 1.00 51.45 ? 194 TRP A CZ3 1 ATOM 1482 C CH2 . TRP A 1 194 ? 30.497 28.916 50.748 1.00 51.64 ? 194 TRP A CH2 1 ATOM 1483 N N . CYS A 1 195 ? 24.113 25.699 54.784 1.00 30.11 ? 195 CYS A N 1 ATOM 1484 C CA . CYS A 1 195 ? 23.236 24.587 55.130 1.00 27.81 ? 195 CYS A CA 1 ATOM 1485 C C . CYS A 1 195 ? 21.746 24.927 55.187 1.00 25.12 ? 195 CYS A C 1 ATOM 1486 O O . CYS A 1 195 ? 21.159 25.066 56.265 1.00 23.78 ? 195 CYS A O 1 ATOM 1487 C CB . CYS A 1 195 ? 23.683 23.978 56.459 1.00 30.16 ? 195 CYS A CB 1 ATOM 1488 S SG . CYS A 1 195 ? 23.446 22.195 56.532 1.00 34.91 ? 195 CYS A SG 1 ATOM 1489 N N . ASN A 1 196 ? 21.144 25.050 54.009 1.00 22.24 ? 196 ASN A N 1 ATOM 1490 C CA . ASN A 1 196 ? 19.726 25.353 53.884 1.00 21.86 ? 196 ASN A CA 1 ATOM 1491 C C . ASN A 1 196 ? 19.261 24.981 52.480 1.00 20.78 ? 196 ASN A C 1 ATOM 1492 O O . ASN A 1 196 ? 20.043 24.501 51.660 1.00 21.48 ? 196 ASN A O 1 ATOM 1493 C CB . ASN A 1 196 ? 19.470 26.841 54.149 1.00 23.46 ? 196 ASN A CB 1 ATOM 1494 C CG . ASN A 1 196 ? 20.253 27.741 53.212 1.00 25.39 ? 196 ASN A CG 1 ATOM 1495 O OD1 . ASN A 1 196 ? 20.213 27.569 51.997 1.00 26.60 ? 196 ASN A OD1 1 ATOM 1496 N ND2 . ASN A 1 196 ? 20.967 28.710 53.776 1.00 30.54 ? 196 ASN A ND2 1 ATOM 1497 N N . GLN A 1 197 ? 17.986 25.211 52.201 1.00 20.26 ? 197 GLN A N 1 ATOM 1498 C CA . GLN A 1 197 ? 17.418 24.876 50.902 1.00 21.79 ? 197 GLN A CA 1 ATOM 1499 C C . GLN A 1 197 ? 18.106 25.544 49.715 1.00 22.77 ? 197 GLN A C 1 ATOM 1500 O O . GLN A 1 197 ? 18.097 25.008 48.612 1.00 22.42 ? 197 GLN A O 1 ATOM 1501 C CB . GLN A 1 197 ? 15.926 25.201 50.891 1.00 20.99 ? 197 GLN A CB 1 ATOM 1502 C CG . GLN A 1 197 ? 15.069 24.150 51.590 1.00 21.22 ? 197 GLN A CG 1 ATOM 1503 C CD . GLN A 1 197 ? 15.195 22.782 50.937 1.00 22.48 ? 197 GLN A CD 1 ATOM 1504 O OE1 . GLN A 1 197 ? 15.293 22.680 49.718 1.00 22.05 ? 197 GLN A OE1 1 ATOM 1505 N NE2 . GLN A 1 197 ? 15.180 21.727 51.745 1.00 21.78 ? 197 GLN A NE2 1 ATOM 1506 N N . ASN A 1 198 ? 18.696 26.712 49.938 1.00 22.66 ? 198 ASN A N 1 ATOM 1507 C CA . ASN A 1 198 ? 19.390 27.405 48.858 1.00 24.85 ? 198 ASN A CA 1 ATOM 1508 C C . ASN A 1 198 ? 20.729 26.748 48.576 1.00 24.45 ? 198 ASN A C 1 ATOM 1509 O O . ASN A 1 198 ? 21.146 26.640 47.421 1.00 24.59 ? 198 ASN A O 1 ATOM 1510 C CB . ASN A 1 198 ? 19.615 28.873 49.223 1.00 25.64 ? 198 ASN A CB 1 ATOM 1511 C CG . ASN A 1 198 ? 18.409 29.736 48.926 1.00 27.79 ? 198 ASN A CG 1 ATOM 1512 O OD1 . ASN A 1 198 ? 18.170 30.115 47.777 1.00 28.95 ? 198 ASN A OD1 1 ATOM 1513 N ND2 . ASN A 1 198 ? 17.637 30.048 49.957 1.00 29.29 ? 198 ASN A ND2 1 ATOM 1514 N N . LEU A 1 199 ? 21.399 26.304 49.634 1.00 24.40 ? 199 LEU A N 1 ATOM 1515 C CA . LEU A 1 199 ? 22.703 25.682 49.478 1.00 25.78 ? 199 LEU A CA 1 ATOM 1516 C C . LEU A 1 199 ? 23.142 24.782 50.628 1.00 25.20 ? 199 LEU A C 1 ATOM 1517 O O . LEU A 1 199 ? 23.113 25.187 51.791 1.00 25.72 ? 199 LEU A O 1 ATOM 1518 C CB . LEU A 1 199 ? 23.757 26.773 49.278 1.00 28.39 ? 199 LEU A CB 1 ATOM 1519 C CG . LEU A 1 199 ? 25.225 26.344 49.273 1.00 31.00 ? 199 LEU A CG 1 ATOM 1520 C CD1 . LEU A 1 199 ? 25.476 25.374 48.125 1.00 33.14 ? 199 LEU A CD1 1 ATOM 1521 C CD2 . LEU A 1 199 ? 26.108 27.580 49.139 1.00 34.98 ? 199 LEU A CD2 1 ATOM 1522 N N . GLY A 1 200 ? 23.537 23.557 50.287 1.00 23.53 ? 200 GLY A N 1 ATOM 1523 C CA . GLY A 1 200 ? 24.052 22.628 51.278 1.00 23.25 ? 200 GLY A CA 1 ATOM 1524 C C . GLY A 1 200 ? 23.185 21.638 52.033 1.00 22.27 ? 200 GLY A C 1 ATOM 1525 O O . GLY A 1 200 ? 23.734 20.737 52.668 1.00 24.19 ? 200 GLY A O 1 ATOM 1526 N N . TRP A 1 201 ? 21.862 21.758 51.980 1.00 21.98 ? 201 TRP A N 1 ATOM 1527 C CA . TRP A 1 201 ? 21.037 20.823 52.745 1.00 22.11 ? 201 TRP A CA 1 ATOM 1528 C C . TRP A 1 201 ? 21.196 19.361 52.338 1.00 23.68 ? 201 TRP A C 1 ATOM 1529 O O . TRP A 1 201 ? 21.125 18.472 53.188 1.00 23.92 ? 201 TRP A O 1 ATOM 1530 C CB . TRP A 1 201 ? 19.550 21.196 52.678 1.00 21.97 ? 201 TRP A CB 1 ATOM 1531 C CG . TRP A 1 201 ? 18.847 20.722 51.450 1.00 22.76 ? 201 TRP A CG 1 ATOM 1532 C CD1 . TRP A 1 201 ? 18.777 21.362 50.248 1.00 21.71 ? 201 TRP A CD1 1 ATOM 1533 C CD2 . TRP A 1 201 ? 18.107 19.502 51.300 1.00 21.79 ? 201 TRP A CD2 1 ATOM 1534 N NE1 . TRP A 1 201 ? 18.035 20.622 49.358 1.00 23.30 ? 201 TRP A NE1 1 ATOM 1535 C CE2 . TRP A 1 201 ? 17.613 19.474 49.977 1.00 22.85 ? 201 TRP A CE2 1 ATOM 1536 C CE3 . TRP A 1 201 ? 17.814 18.429 52.157 1.00 23.39 ? 201 TRP A CE3 1 ATOM 1537 C CZ2 . TRP A 1 201 ? 16.840 18.415 49.485 1.00 23.45 ? 201 TRP A CZ2 1 ATOM 1538 C CZ3 . TRP A 1 201 ? 17.043 17.372 51.667 1.00 22.05 ? 201 TRP A CZ3 1 ATOM 1539 C CH2 . TRP A 1 201 ? 16.566 17.376 50.342 1.00 23.48 ? 201 TRP A CH2 1 ATOM 1540 N N . GLU A 1 202 ? 21.414 19.103 51.052 1.00 23.78 ? 202 GLU A N 1 ATOM 1541 C CA . GLU A 1 202 ? 21.548 17.723 50.587 1.00 25.15 ? 202 GLU A CA 1 ATOM 1542 C C . GLU A 1 202 ? 22.747 17.010 51.198 1.00 25.53 ? 202 GLU A C 1 ATOM 1543 O O . GLU A 1 202 ? 22.651 15.846 51.591 1.00 24.96 ? 202 GLU A O 1 ATOM 1544 C CB . GLU A 1 202 ? 21.635 17.675 49.059 1.00 27.83 ? 202 GLU A CB 1 ATOM 1545 C CG . GLU A 1 202 ? 20.399 18.218 48.363 1.00 33.50 ? 202 GLU A CG 1 ATOM 1546 C CD . GLU A 1 202 ? 20.402 17.968 46.864 1.00 38.32 ? 202 GLU A CD 1 ATOM 1547 O OE1 . GLU A 1 202 ? 19.603 18.620 46.155 1.00 41.70 ? 202 GLU A OE1 1 ATOM 1548 O OE2 . GLU A 1 202 ? 21.190 17.116 46.395 1.00 36.62 ? 202 GLU A OE2 1 ATOM 1549 N N . GLY A 1 203 ? 23.874 17.710 51.272 1.00 24.66 ? 203 GLY A N 1 ATOM 1550 C CA . GLY A 1 203 ? 25.068 17.124 51.850 1.00 25.87 ? 203 GLY A CA 1 ATOM 1551 C C . GLY A 1 203 ? 24.854 16.803 53.318 1.00 26.25 ? 203 GLY A C 1 ATOM 1552 O O . GLY A 1 203 ? 25.252 15.741 53.796 1.00 26.95 ? 203 GLY A O 1 ATOM 1553 N N . SER A 1 204 ? 24.216 17.719 54.040 1.00 25.94 ? 204 SER A N 1 ATOM 1554 C CA . SER A 1 204 ? 23.957 17.498 55.453 1.00 26.75 ? 204 SER A CA 1 ATOM 1555 C C . SER A 1 204 ? 22.974 16.343 55.620 1.00 23.05 ? 204 SER A C 1 ATOM 1556 O O . SER A 1 204 ? 23.121 15.528 56.534 1.00 22.74 ? 204 SER A O 1 ATOM 1557 C CB . SER A 1 204 ? 23.397 18.766 56.102 1.00 29.36 ? 204 SER A CB 1 ATOM 1558 O OG . SER A 1 204 ? 22.125 19.087 55.572 1.00 37.43 ? 204 SER A OG 1 ATOM 1559 N N . TRP A 1 205 ? 21.981 16.274 54.735 1.00 22.52 ? 205 TRP A N 1 ATOM 1560 C CA . TRP A 1 205 ? 20.982 15.211 54.783 1.00 22.80 ? 205 TRP A CA 1 ATOM 1561 C C . TRP A 1 205 ? 21.677 13.852 54.667 1.00 23.67 ? 205 TRP A C 1 ATOM 1562 O O . TRP A 1 205 ? 21.317 12.899 55.367 1.00 21.34 ? 205 TRP A O 1 ATOM 1563 C CB . TRP A 1 205 ? 19.957 15.399 53.656 1.00 23.22 ? 205 TRP A CB 1 ATOM 1564 C CG . TRP A 1 205 ? 18.862 14.370 53.630 1.00 22.33 ? 205 TRP A CG 1 ATOM 1565 C CD1 . TRP A 1 205 ? 18.770 13.293 52.798 1.00 22.80 ? 205 TRP A CD1 1 ATOM 1566 C CD2 . TRP A 1 205 ? 17.705 14.323 54.476 1.00 20.98 ? 205 TRP A CD2 1 ATOM 1567 N NE1 . TRP A 1 205 ? 17.627 12.579 53.070 1.00 22.54 ? 205 TRP A NE1 1 ATOM 1568 C CE2 . TRP A 1 205 ? 16.955 13.188 54.096 1.00 21.24 ? 205 TRP A CE2 1 ATOM 1569 C CE3 . TRP A 1 205 ? 17.229 15.130 55.518 1.00 20.86 ? 205 TRP A CE3 1 ATOM 1570 C CZ2 . TRP A 1 205 ? 15.752 12.839 54.721 1.00 20.73 ? 205 TRP A CZ2 1 ATOM 1571 C CZ3 . TRP A 1 205 ? 16.026 14.783 56.143 1.00 19.29 ? 205 TRP A CZ3 1 ATOM 1572 C CH2 . TRP A 1 205 ? 15.304 13.645 55.738 1.00 20.02 ? 205 TRP A CH2 1 ATOM 1573 N N . ASP A 1 206 ? 22.679 13.773 53.793 1.00 23.23 ? 206 ASP A N 1 ATOM 1574 C CA . ASP A 1 206 ? 23.435 12.533 53.609 1.00 25.70 ? 206 ASP A CA 1 ATOM 1575 C C . ASP A 1 206 ? 24.080 12.105 54.921 1.00 25.04 ? 206 ASP A C 1 ATOM 1576 O O . ASP A 1 206 ? 23.993 10.943 55.319 1.00 24.64 ? 206 ASP A O 1 ATOM 1577 C CB . ASP A 1 206 ? 24.557 12.706 52.575 1.00 28.26 ? 206 ASP A CB 1 ATOM 1578 C CG . ASP A 1 206 ? 24.041 12.907 51.172 1.00 32.01 ? 206 ASP A CG 1 ATOM 1579 O OD1 . ASP A 1 206 ? 23.063 12.229 50.793 1.00 35.89 ? 206 ASP A OD1 1 ATOM 1580 O OD2 . ASP A 1 206 ? 24.628 13.733 50.438 1.00 34.26 ? 206 ASP A OD2 1 ATOM 1581 N N . LYS A 1 207 ? 24.742 13.051 55.579 1.00 23.30 ? 207 LYS A N 1 ATOM 1582 C CA . LYS A 1 207 ? 25.423 12.779 56.836 1.00 24.39 ? 207 LYS A CA 1 ATOM 1583 C C . LYS A 1 207 ? 24.461 12.408 57.963 1.00 23.73 ? 207 LYS A C 1 ATOM 1584 O O . LYS A 1 207 ? 24.702 11.449 58.693 1.00 22.94 ? 207 LYS A O 1 ATOM 1585 C CB . LYS A 1 207 ? 26.269 13.987 57.243 1.00 27.22 ? 207 LYS A CB 1 ATOM 1586 C CG . LYS A 1 207 ? 27.349 14.345 56.229 1.00 29.13 ? 207 LYS A CG 1 ATOM 1587 C CD . LYS A 1 207 ? 28.149 15.561 56.679 1.00 32.63 ? 207 LYS A CD 1 ATOM 1588 C CE . LYS A 1 207 ? 29.198 15.961 55.646 1.00 34.76 ? 207 LYS A CE 1 ATOM 1589 N NZ . LYS A 1 207 ? 28.583 16.437 54.372 1.00 38.66 ? 207 LYS A NZ 1 ATOM 1590 N N . TRP A 1 208 ? 23.379 13.168 58.106 1.00 21.56 ? 208 TRP A N 1 ATOM 1591 C CA . TRP A 1 208 ? 22.390 12.900 59.153 1.00 20.61 ? 208 TRP A CA 1 ATOM 1592 C C . TRP A 1 208 ? 21.800 11.493 59.075 1.00 20.77 ? 208 TRP A C 1 ATOM 1593 O O . TRP A 1 208 ? 21.825 10.743 60.057 1.00 21.14 ? 208 TRP A O 1 ATOM 1594 C CB . TRP A 1 208 ? 21.242 13.913 59.082 1.00 20.17 ? 208 TRP A CB 1 ATOM 1595 C CG . TRP A 1 208 ? 21.482 15.159 59.885 1.00 19.55 ? 208 TRP A CG 1 ATOM 1596 C CD1 . TRP A 1 208 ? 21.731 16.422 59.406 1.00 19.90 ? 208 TRP A CD1 1 ATOM 1597 C CD2 . TRP A 1 208 ? 21.488 15.265 61.312 1.00 19.00 ? 208 TRP A CD2 1 ATOM 1598 N NE1 . TRP A 1 208 ? 21.891 17.300 60.452 1.00 18.09 ? 208 TRP A NE1 1 ATOM 1599 C CE2 . TRP A 1 208 ? 21.745 16.617 61.632 1.00 18.75 ? 208 TRP A CE2 1 ATOM 1600 C CE3 . TRP A 1 208 ? 21.298 14.347 62.353 1.00 17.42 ? 208 TRP A CE3 1 ATOM 1601 C CZ2 . TRP A 1 208 ? 21.816 17.072 62.953 1.00 19.87 ? 208 TRP A CZ2 1 ATOM 1602 C CZ3 . TRP A 1 208 ? 21.370 14.800 63.665 1.00 19.49 ? 208 TRP A CZ3 1 ATOM 1603 C CH2 . TRP A 1 208 ? 21.626 16.152 63.953 1.00 19.06 ? 208 TRP A CH2 1 ATOM 1604 N N . THR A 1 209 ? 21.263 11.150 57.908 1.00 20.31 ? 209 THR A N 1 ATOM 1605 C CA . THR A 1 209 ? 20.635 9.849 57.697 1.00 22.61 ? 209 THR A CA 1 ATOM 1606 C C . THR A 1 209 ? 21.593 8.675 57.868 1.00 24.07 ? 209 THR A C 1 ATOM 1607 O O . THR A 1 209 ? 21.217 7.629 58.405 1.00 24.77 ? 209 THR A O 1 ATOM 1608 C CB . THR A 1 209 ? 19.978 9.765 56.299 1.00 21.13 ? 209 THR A CB 1 ATOM 1609 O OG1 . THR A 1 209 ? 20.946 10.075 55.289 1.00 21.32 ? 209 THR A OG1 1 ATOM 1610 C CG2 . THR A 1 209 ? 18.804 10.737 56.201 1.00 21.24 ? 209 THR A CG2 1 ATOM 1611 N N . ALA A 1 210 ? 22.831 8.846 57.421 1.00 25.17 ? 210 ALA A N 1 ATOM 1612 C CA . ALA A 1 210 ? 23.821 7.785 57.540 1.00 26.64 ? 210 ALA A CA 1 ATOM 1613 C C . ALA A 1 210 ? 24.272 7.576 58.985 1.00 26.18 ? 210 ALA A C 1 ATOM 1614 O O . ALA A 1 210 ? 24.588 6.460 59.387 1.00 27.04 ? 210 ALA A O 1 ATOM 1615 C CB . ALA A 1 210 ? 25.029 8.100 56.661 1.00 26.07 ? 210 ALA A CB 1 ATOM 1616 N N . ALA A 1 211 ? 24.289 8.648 59.767 1.00 24.66 ? 211 ALA A N 1 ATOM 1617 C CA . ALA A 1 211 ? 24.737 8.570 61.149 1.00 23.80 ? 211 ALA A CA 1 ATOM 1618 C C . ALA A 1 211 ? 23.764 7.921 62.127 1.00 22.75 ? 211 ALA A C 1 ATOM 1619 O O . ALA A 1 211 ? 24.189 7.419 63.162 1.00 23.49 ? 211 ALA A O 1 ATOM 1620 C CB . ALA A 1 211 ? 25.108 9.967 61.650 1.00 23.42 ? 211 ALA A CB 1 ATOM 1621 N N . TYR A 1 212 ? 22.474 7.924 61.808 1.00 22.23 ? 212 TYR A N 1 ATOM 1622 C CA . TYR A 1 212 ? 21.468 7.350 62.706 1.00 21.81 ? 212 TYR A CA 1 ATOM 1623 C C . TYR A 1 212 ? 20.507 6.418 61.974 1.00 21.27 ? 212 TYR A C 1 ATOM 1624 O O . TYR A 1 212 ? 19.336 6.736 61.767 1.00 19.33 ? 212 TYR A O 1 ATOM 1625 C CB . TYR A 1 212 ? 20.696 8.488 63.388 1.00 20.27 ? 212 TYR A CB 1 ATOM 1626 C CG . TYR A 1 212 ? 21.585 9.408 64.198 1.00 22.55 ? 212 TYR A CG 1 ATOM 1627 C CD1 . TYR A 1 212 ? 21.987 9.067 65.492 1.00 21.99 ? 212 TYR A CD1 1 ATOM 1628 C CD2 . TYR A 1 212 ? 22.058 10.608 63.655 1.00 23.25 ? 212 TYR A CD2 1 ATOM 1629 C CE1 . TYR A 1 212 ? 22.840 9.895 66.226 1.00 21.30 ? 212 TYR A CE1 1 ATOM 1630 C CE2 . TYR A 1 212 ? 22.909 11.443 64.380 1.00 21.88 ? 212 TYR A CE2 1 ATOM 1631 C CZ . TYR A 1 212 ? 23.296 11.079 65.661 1.00 24.20 ? 212 TYR A CZ 1 ATOM 1632 O OH . TYR A 1 212 ? 24.145 11.891 66.377 1.00 26.20 ? 212 TYR A OH 1 ATOM 1633 N N . PRO A 1 213 ? 20.995 5.229 61.589 1.00 22.59 ? 213 PRO A N 1 ATOM 1634 C CA . PRO A 1 213 ? 20.238 4.198 60.868 1.00 23.55 ? 213 PRO A CA 1 ATOM 1635 C C . PRO A 1 213 ? 18.891 3.797 61.477 1.00 22.12 ? 213 PRO A C 1 ATOM 1636 O O . PRO A 1 213 ? 17.953 3.458 60.754 1.00 21.73 ? 213 PRO A O 1 ATOM 1637 C CB . PRO A 1 213 ? 21.207 3.019 60.840 1.00 23.92 ? 213 PRO A CB 1 ATOM 1638 C CG . PRO A 1 213 ? 22.537 3.662 60.874 1.00 27.38 ? 213 PRO A CG 1 ATOM 1639 C CD . PRO A 1 213 ? 22.358 4.757 61.891 1.00 23.34 ? 213 PRO A CD 1 ATOM 1640 N N . ALA A 1 214 ? 18.795 3.828 62.801 1.00 20.85 ? 214 ALA A N 1 ATOM 1641 C CA . ALA A 1 214 ? 17.565 3.427 63.485 1.00 21.28 ? 214 ALA A CA 1 ATOM 1642 C C . ALA A 1 214 ? 16.497 4.510 63.560 1.00 22.41 ? 214 ALA A C 1 ATOM 1643 O O . ALA A 1 214 ? 15.356 4.251 63.959 1.00 23.44 ? 214 ALA A O 1 ATOM 1644 C CB . ALA A 1 214 ? 17.901 2.941 64.898 1.00 22.00 ? 214 ALA A CB 1 ATOM 1645 N N . THR A 1 215 ? 16.860 5.720 63.156 1.00 19.95 ? 215 THR A N 1 ATOM 1646 C CA . THR A 1 215 ? 15.941 6.847 63.225 1.00 19.38 ? 215 THR A CA 1 ATOM 1647 C C . THR A 1 215 ? 15.379 7.276 61.874 1.00 18.34 ? 215 THR A C 1 ATOM 1648 O O . THR A 1 215 ? 16.078 7.246 60.859 1.00 17.98 ? 215 THR A O 1 ATOM 1649 C CB . THR A 1 215 ? 16.651 8.049 63.887 1.00 19.32 ? 215 THR A CB 1 ATOM 1650 O OG1 . THR A 1 215 ? 17.052 7.681 65.212 1.00 18.01 ? 215 THR A OG1 1 ATOM 1651 C CG2 . THR A 1 215 ? 15.727 9.271 63.947 1.00 18.89 ? 215 THR A CG2 1 ATOM 1652 N N . ARG A 1 216 ? 14.108 7.663 61.870 1.00 17.59 ? 216 ARG A N 1 ATOM 1653 C CA . ARG A 1 216 ? 13.446 8.128 60.656 1.00 17.49 ? 216 ARG A CA 1 ATOM 1654 C C . ARG A 1 216 ? 13.674 9.629 60.555 1.00 18.35 ? 216 ARG A C 1 ATOM 1655 O O . ARG A 1 216 ? 13.502 10.352 61.532 1.00 17.86 ? 216 ARG A O 1 ATOM 1656 C CB . ARG A 1 216 ? 11.953 7.817 60.716 1.00 21.30 ? 216 ARG A CB 1 ATOM 1657 C CG . ARG A 1 216 ? 11.637 6.347 60.451 1.00 28.16 ? 216 ARG A CG 1 ATOM 1658 C CD . ARG A 1 216 ? 10.161 6.055 60.651 1.00 35.16 ? 216 ARG A CD 1 ATOM 1659 N NE . ARG A 1 216 ? 9.932 5.353 61.908 1.00 41.27 ? 216 ARG A NE 1 ATOM 1660 C CZ . ARG A 1 216 ? 10.221 4.071 62.109 1.00 42.98 ? 216 ARG A CZ 1 ATOM 1661 N NH1 . ARG A 1 216 ? 10.744 3.343 61.130 1.00 45.14 ? 216 ARG A NH1 1 ATOM 1662 N NH2 . ARG A 1 216 ? 10.008 3.521 63.295 1.00 44.16 ? 216 ARG A NH2 1 ATOM 1663 N N . PHE A 1 217 ? 14.053 10.088 59.369 1.00 17.19 ? 217 PHE A N 1 ATOM 1664 C CA . PHE A 1 217 ? 14.347 11.497 59.163 1.00 18.35 ? 217 PHE A CA 1 ATOM 1665 C C . PHE A 1 217 ? 13.309 12.234 58.343 1.00 17.92 ? 217 PHE A C 1 ATOM 1666 O O . PHE A 1 217 ? 12.894 11.777 57.282 1.00 18.65 ? 217 PHE A O 1 ATOM 1667 C CB . PHE A 1 217 ? 15.731 11.632 58.523 1.00 17.39 ? 217 PHE A CB 1 ATOM 1668 C CG . PHE A 1 217 ? 16.853 11.474 59.500 1.00 17.90 ? 217 PHE A CG 1 ATOM 1669 C CD1 . PHE A 1 217 ? 17.420 12.586 60.104 1.00 15.84 ? 217 PHE A CD1 1 ATOM 1670 C CD2 . PHE A 1 217 ? 17.291 10.206 59.885 1.00 15.95 ? 217 PHE A CD2 1 ATOM 1671 C CE1 . PHE A 1 217 ? 18.405 12.451 61.081 1.00 16.11 ? 217 PHE A CE1 1 ATOM 1672 C CE2 . PHE A 1 217 ? 18.273 10.055 60.861 1.00 17.50 ? 217 PHE A CE2 1 ATOM 1673 C CZ . PHE A 1 217 ? 18.834 11.178 61.464 1.00 18.23 ? 217 PHE A CZ 1 ATOM 1674 N N . TYR A 1 218 ? 12.899 13.391 58.851 1.00 17.74 ? 218 TYR A N 1 ATOM 1675 C CA . TYR A 1 218 ? 11.916 14.223 58.180 1.00 16.94 ? 218 TYR A CA 1 ATOM 1676 C C . TYR A 1 218 ? 12.592 15.470 57.656 1.00 17.46 ? 218 TYR A C 1 ATOM 1677 O O . TYR A 1 218 ? 13.448 16.039 58.333 1.00 17.32 ? 218 TYR A O 1 ATOM 1678 C CB . TYR A 1 218 ? 10.817 14.655 59.152 1.00 18.86 ? 218 TYR A CB 1 ATOM 1679 C CG . TYR A 1 218 ? 9.779 13.606 59.452 1.00 19.01 ? 218 TYR A CG 1 ATOM 1680 C CD1 . TYR A 1 218 ? 10.140 12.364 59.977 1.00 21.51 ? 218 TYR A CD1 1 ATOM 1681 C CD2 . TYR A 1 218 ? 8.430 13.869 59.239 1.00 18.63 ? 218 TYR A CD2 1 ATOM 1682 C CE1 . TYR A 1 218 ? 9.173 11.411 60.282 1.00 20.16 ? 218 TYR A CE1 1 ATOM 1683 C CE2 . TYR A 1 218 ? 7.454 12.923 59.540 1.00 22.70 ? 218 TYR A CE2 1 ATOM 1684 C CZ . TYR A 1 218 ? 7.835 11.699 60.064 1.00 21.13 ? 218 TYR A CZ 1 ATOM 1685 O OH . TYR A 1 218 ? 6.868 10.777 60.388 1.00 23.17 ? 218 TYR A OH 1 ATOM 1686 N N . VAL A 1 219 ? 12.216 15.887 56.449 1.00 17.42 ? 219 VAL A N 1 ATOM 1687 C CA . VAL A 1 219 ? 12.771 17.107 55.871 1.00 17.99 ? 219 VAL A CA 1 ATOM 1688 C C . VAL A 1 219 ? 11.884 18.226 56.384 1.00 16.54 ? 219 VAL A C 1 ATOM 1689 O O . VAL A 1 219 ? 10.676 18.230 56.127 1.00 16.50 ? 219 VAL A O 1 ATOM 1690 C CB . VAL A 1 219 ? 12.705 17.115 54.320 1.00 19.04 ? 219 VAL A CB 1 ATOM 1691 C CG1 . VAL A 1 219 ? 13.274 18.437 53.776 1.00 17.63 ? 219 VAL A CG1 1 ATOM 1692 C CG2 . VAL A 1 219 ? 13.487 15.948 53.759 1.00 19.98 ? 219 VAL A CG2 1 ATOM 1693 N N . GLY A 1 220 ? 12.479 19.158 57.122 1.00 16.26 ? 220 GLY A N 1 ATOM 1694 C CA . GLY A 1 220 ? 11.720 20.278 57.657 1.00 15.84 ? 220 GLY A CA 1 ATOM 1695 C C . GLY A 1 220 ? 11.683 21.419 56.658 1.00 17.04 ? 220 GLY A C 1 ATOM 1696 O O . GLY A 1 220 ? 12.729 21.900 56.221 1.00 16.63 ? 220 GLY A O 1 ATOM 1697 N N . LEU A 1 221 ? 10.475 21.843 56.302 1.00 15.32 ? 221 LEU A N 1 ATOM 1698 C CA . LEU A 1 221 ? 10.266 22.923 55.339 1.00 16.95 ? 221 LEU A CA 1 ATOM 1699 C C . LEU A 1 221 ? 9.383 23.994 55.957 1.00 17.26 ? 221 LEU A C 1 ATOM 1700 O O . LEU A 1 221 ? 8.557 23.701 56.825 1.00 17.43 ? 221 LEU A O 1 ATOM 1701 C CB . LEU A 1 221 ? 9.561 22.381 54.096 1.00 16.03 ? 221 LEU A CB 1 ATOM 1702 C CG . LEU A 1 221 ? 10.223 21.214 53.366 1.00 16.18 ? 221 LEU A CG 1 ATOM 1703 C CD1 . LEU A 1 221 ? 9.248 20.645 52.344 1.00 15.91 ? 221 LEU A CD1 1 ATOM 1704 C CD2 . LEU A 1 221 ? 11.521 21.677 52.698 1.00 19.62 ? 221 LEU A CD2 1 ATOM 1705 N N . THR A 1 222 ? 9.536 25.233 55.500 1.00 18.22 ? 222 THR A N 1 ATOM 1706 C CA . THR A 1 222 ? 8.707 26.308 56.021 1.00 18.27 ? 222 THR A CA 1 ATOM 1707 C C . THR A 1 222 ? 7.507 26.500 55.097 1.00 18.85 ? 222 THR A C 1 ATOM 1708 O O . THR A 1 222 ? 7.617 26.340 53.878 1.00 20.90 ? 222 THR A O 1 ATOM 1709 C CB . THR A 1 222 ? 9.489 27.641 56.124 1.00 20.38 ? 222 THR A CB 1 ATOM 1710 O OG1 . THR A 1 222 ? 8.609 28.670 56.597 1.00 20.66 ? 222 THR A OG1 1 ATOM 1711 C CG2 . THR A 1 222 ? 10.064 28.044 54.766 1.00 20.29 ? 222 THR A CG2 1 ATOM 1712 N N . ALA A 1 223 ? 6.358 26.822 55.683 1.00 19.39 ? 223 ALA A N 1 ATOM 1713 C CA . ALA A 1 223 ? 5.144 27.045 54.910 1.00 20.19 ? 223 ALA A CA 1 ATOM 1714 C C . ALA A 1 223 ? 4.978 28.535 54.633 1.00 21.48 ? 223 ALA A C 1 ATOM 1715 O O . ALA A 1 223 ? 3.976 28.962 54.056 1.00 22.81 ? 223 ALA A O 1 ATOM 1716 C CB . ALA A 1 223 ? 3.928 26.510 55.667 1.00 22.05 ? 223 ALA A CB 1 ATOM 1717 N N . ASP A 1 224 ? 5.960 29.321 55.062 1.00 21.64 ? 224 ASP A N 1 ATOM 1718 C CA . ASP A 1 224 ? 5.941 30.770 54.857 1.00 21.31 ? 224 ASP A CA 1 ATOM 1719 C C . ASP A 1 224 ? 6.526 31.070 53.478 1.00 23.08 ? 224 ASP A C 1 ATOM 1720 O O . ASP A 1 224 ? 7.745 31.068 53.300 1.00 21.36 ? 224 ASP A O 1 ATOM 1721 C CB . ASP A 1 224 ? 6.767 31.458 55.945 1.00 23.56 ? 224 ASP A CB 1 ATOM 1722 C CG . ASP A 1 224 ? 6.869 32.959 55.745 1.00 23.65 ? 224 ASP A CG 1 ATOM 1723 O OD1 . ASP A 1 224 ? 6.106 33.508 54.924 1.00 25.65 ? 224 ASP A OD1 1 ATOM 1724 O OD2 . ASP A 1 224 ? 7.711 33.587 56.419 1.00 28.11 ? 224 ASP A OD2 1 ATOM 1725 N N . ASP A 1 225 ? 5.653 31.331 52.509 1.00 23.79 ? 225 ASP A N 1 ATOM 1726 C CA . ASP A 1 225 ? 6.096 31.599 51.145 1.00 26.67 ? 225 ASP A CA 1 ATOM 1727 C C . ASP A 1 225 ? 6.862 32.905 50.946 1.00 27.86 ? 225 ASP A C 1 ATOM 1728 O O . ASP A 1 225 ? 7.271 33.221 49.829 1.00 28.14 ? 225 ASP A O 1 ATOM 1729 C CB . ASP A 1 225 ? 4.908 31.523 50.176 1.00 29.18 ? 225 ASP A CB 1 ATOM 1730 C CG . ASP A 1 225 ? 3.825 32.543 50.481 1.00 31.43 ? 225 ASP A CG 1 ATOM 1731 O OD1 . ASP A 1 225 ? 2.808 32.548 49.757 1.00 34.48 ? 225 ASP A OD1 1 ATOM 1732 O OD2 . ASP A 1 225 ? 3.985 33.336 51.432 1.00 31.21 ? 225 ASP A OD2 1 ATOM 1733 N N . LYS A 1 226 ? 7.071 33.652 52.025 1.00 27.91 ? 226 LYS A N 1 ATOM 1734 C CA . LYS A 1 226 ? 7.819 34.905 51.953 1.00 29.86 ? 226 LYS A CA 1 ATOM 1735 C C . LYS A 1 226 ? 9.279 34.630 52.310 1.00 28.82 ? 226 LYS A C 1 ATOM 1736 O O . LYS A 1 226 ? 10.161 35.447 52.045 1.00 28.55 ? 226 LYS A O 1 ATOM 1737 C CB . LYS A 1 226 ? 7.262 35.931 52.946 1.00 32.87 ? 226 LYS A CB 1 ATOM 1738 C CG . LYS A 1 226 ? 5.767 36.197 52.847 1.00 38.18 ? 226 LYS A CG 1 ATOM 1739 C CD . LYS A 1 226 ? 5.385 36.830 51.524 1.00 41.93 ? 226 LYS A CD 1 ATOM 1740 C CE . LYS A 1 226 ? 3.945 37.336 51.560 1.00 44.46 ? 226 LYS A CE 1 ATOM 1741 N NZ . LYS A 1 226 ? 2.965 36.259 51.894 1.00 47.17 ? 226 LYS A NZ 1 ATOM 1742 N N . SER A 1 227 ? 9.524 33.478 52.930 1.00 26.62 ? 227 SER A N 1 ATOM 1743 C CA . SER A 1 227 ? 10.871 33.097 53.343 1.00 24.79 ? 227 SER A CA 1 ATOM 1744 C C . SER A 1 227 ? 11.818 32.887 52.164 1.00 24.50 ? 227 SER A C 1 ATOM 1745 O O . SER A 1 227 ? 11.407 32.420 51.107 1.00 24.58 ? 227 SER A O 1 ATOM 1746 C CB . SER A 1 227 ? 10.816 31.808 54.178 1.00 23.78 ? 227 SER A CB 1 ATOM 1747 O OG . SER A 1 227 ? 12.117 31.298 54.406 1.00 23.81 ? 227 SER A OG 1 ATOM 1748 N N . HIS A 1 228 ? 13.089 33.229 52.351 1.00 26.32 ? 228 HIS A N 1 ATOM 1749 C CA . HIS A 1 228 ? 14.076 33.042 51.296 1.00 28.45 ? 228 HIS A CA 1 ATOM 1750 C C . HIS A 1 228 ? 14.372 31.549 51.153 1.00 26.84 ? 228 HIS A C 1 ATOM 1751 O O . HIS A 1 228 ? 14.966 31.115 50.167 1.00 25.36 ? 228 HIS A O 1 ATOM 1752 C CB . HIS A 1 228 ? 15.370 33.792 51.629 1.00 33.12 ? 228 HIS A CB 1 ATOM 1753 C CG . HIS A 1 228 ? 15.196 35.275 51.738 1.00 38.68 ? 228 HIS A CG 1 ATOM 1754 N ND1 . HIS A 1 228 ? 14.704 36.044 50.705 1.00 42.07 ? 228 HIS A ND1 1 ATOM 1755 C CD2 . HIS A 1 228 ? 15.444 36.131 52.759 1.00 41.33 ? 228 HIS A CD2 1 ATOM 1756 C CE1 . HIS A 1 228 ? 14.657 37.309 51.084 1.00 42.65 ? 228 HIS A CE1 1 ATOM 1757 N NE2 . HIS A 1 228 ? 15.100 37.389 52.326 1.00 42.54 ? 228 HIS A NE2 1 ATOM 1758 N N . GLN A 1 229 ? 13.948 30.764 52.141 1.00 25.53 ? 229 GLN A N 1 ATOM 1759 C CA . GLN A 1 229 ? 14.182 29.321 52.113 1.00 24.89 ? 229 GLN A CA 1 ATOM 1760 C C . GLN A 1 229 ? 12.924 28.537 51.754 1.00 24.42 ? 229 GLN A C 1 ATOM 1761 O O . GLN A 1 229 ? 12.906 27.306 51.832 1.00 23.71 ? 229 GLN A O 1 ATOM 1762 C CB . GLN A 1 229 ? 14.728 28.858 53.464 1.00 24.47 ? 229 GLN A CB 1 ATOM 1763 C CG . GLN A 1 229 ? 15.907 29.696 53.936 1.00 28.46 ? 229 GLN A CG 1 ATOM 1764 C CD . GLN A 1 229 ? 17.054 29.703 52.944 1.00 30.00 ? 229 GLN A CD 1 ATOM 1765 O OE1 . GLN A 1 229 ? 17.854 30.640 52.913 1.00 30.20 ? 229 GLN A OE1 1 ATOM 1766 N NE2 . GLN A 1 229 ? 17.148 28.650 52.133 1.00 27.95 ? 229 GLN A NE2 1 ATOM 1767 N N . TRP A 1 230 ? 11.870 29.247 51.360 1.00 22.69 ? 230 TRP A N 1 ATOM 1768 C CA . TRP A 1 230 ? 10.628 28.588 50.969 1.00 21.68 ? 230 TRP A CA 1 ATOM 1769 C C . TRP A 1 230 ? 10.866 27.803 49.685 1.00 22.78 ? 230 TRP A C 1 ATOM 1770 O O . TRP A 1 230 ? 11.560 28.271 48.783 1.00 23.45 ? 230 TRP A O 1 ATOM 1771 C CB . TRP A 1 230 ? 9.521 29.617 50.721 1.00 22.41 ? 230 TRP A CB 1 ATOM 1772 C CG . TRP A 1 230 ? 8.185 29.007 50.400 1.00 22.17 ? 230 TRP A CG 1 ATOM 1773 C CD1 . TRP A 1 230 ? 7.375 28.307 51.256 1.00 23.83 ? 230 TRP A CD1 1 ATOM 1774 C CD2 . TRP A 1 230 ? 7.497 29.042 49.139 1.00 22.52 ? 230 TRP A CD2 1 ATOM 1775 N NE1 . TRP A 1 230 ? 6.229 27.909 50.607 1.00 22.14 ? 230 TRP A NE1 1 ATOM 1776 C CE2 . TRP A 1 230 ? 6.278 28.345 49.308 1.00 22.50 ? 230 TRP A CE2 1 ATOM 1777 C CE3 . TRP A 1 230 ? 7.792 29.596 47.884 1.00 23.69 ? 230 TRP A CE3 1 ATOM 1778 C CZ2 . TRP A 1 230 ? 5.355 28.187 48.271 1.00 21.49 ? 230 TRP A CZ2 1 ATOM 1779 C CZ3 . TRP A 1 230 ? 6.872 29.438 46.850 1.00 21.75 ? 230 TRP A CZ3 1 ATOM 1780 C CH2 . TRP A 1 230 ? 5.666 28.738 47.052 1.00 22.69 ? 230 TRP A CH2 1 ATOM 1781 N N . VAL A 1 231 ? 10.296 26.606 49.604 1.00 21.08 ? 231 VAL A N 1 ATOM 1782 C CA . VAL A 1 231 ? 10.446 25.784 48.413 1.00 20.67 ? 231 VAL A CA 1 ATOM 1783 C C . VAL A 1 231 ? 9.101 25.676 47.705 1.00 20.91 ? 231 VAL A C 1 ATOM 1784 O O . VAL A 1 231 ? 8.136 25.148 48.262 1.00 21.49 ? 231 VAL A O 1 ATOM 1785 C CB . VAL A 1 231 ? 10.938 24.353 48.759 1.00 18.73 ? 231 VAL A CB 1 ATOM 1786 C CG1 . VAL A 1 231 ? 11.150 23.551 47.468 1.00 20.05 ? 231 VAL A CG1 1 ATOM 1787 C CG2 . VAL A 1 231 ? 12.234 24.423 49.566 1.00 20.28 ? 231 VAL A CG2 1 ATOM 1788 N N . HIS A 1 232 ? 9.028 26.186 46.479 1.00 20.30 ? 232 HIS A N 1 ATOM 1789 C CA . HIS A 1 232 ? 7.783 26.109 45.721 1.00 20.40 ? 232 HIS A CA 1 ATOM 1790 C C . HIS A 1 232 ? 7.428 24.637 45.533 1.00 20.86 ? 232 HIS A C 1 ATOM 1791 O O . HIS A 1 232 ? 8.304 23.805 45.304 1.00 20.45 ? 232 HIS A O 1 ATOM 1792 C CB . HIS A 1 232 ? 7.946 26.785 44.352 1.00 20.45 ? 232 HIS A CB 1 ATOM 1793 C CG . HIS A 1 232 ? 6.683 26.841 43.551 1.00 20.58 ? 232 HIS A CG 1 ATOM 1794 N ND1 . HIS A 1 232 ? 6.147 25.738 42.922 1.00 19.76 ? 232 HIS A ND1 1 ATOM 1795 C CD2 . HIS A 1 232 ? 5.841 27.868 43.288 1.00 21.12 ? 232 HIS A CD2 1 ATOM 1796 C CE1 . HIS A 1 232 ? 5.030 26.082 42.306 1.00 20.49 ? 232 HIS A CE1 1 ATOM 1797 N NE2 . HIS A 1 232 ? 4.821 27.370 42.513 1.00 21.33 ? 232 HIS A NE2 1 ATOM 1798 N N . PRO A 1 233 ? 6.134 24.299 45.630 1.00 21.85 ? 233 PRO A N 1 ATOM 1799 C CA . PRO A 1 233 ? 5.650 22.925 45.473 1.00 23.41 ? 233 PRO A CA 1 ATOM 1800 C C . PRO A 1 233 ? 6.260 22.146 44.308 1.00 24.17 ? 233 PRO A C 1 ATOM 1801 O O . PRO A 1 233 ? 6.597 20.968 44.451 1.00 23.87 ? 233 PRO A O 1 ATOM 1802 C CB . PRO A 1 233 ? 4.146 23.112 45.330 1.00 23.01 ? 233 PRO A CB 1 ATOM 1803 C CG . PRO A 1 233 ? 3.885 24.251 46.257 1.00 23.93 ? 233 PRO A CG 1 ATOM 1804 C CD . PRO A 1 233 ? 5.019 25.213 45.940 1.00 22.59 ? 233 PRO A CD 1 ATOM 1805 N N . LYS A 1 234 ? 6.413 22.793 43.158 1.00 24.45 ? 234 LYS A N 1 ATOM 1806 C CA . LYS A 1 234 ? 6.983 22.102 42.008 1.00 25.46 ? 234 LYS A CA 1 ATOM 1807 C C . LYS A 1 234 ? 8.430 21.692 42.263 1.00 24.06 ? 234 LYS A C 1 ATOM 1808 O O . LYS A 1 234 ? 8.887 20.665 41.764 1.00 25.45 ? 234 LYS A O 1 ATOM 1809 C CB . LYS A 1 234 ? 6.907 22.979 40.755 1.00 27.42 ? 234 LYS A CB 1 ATOM 1810 C CG . LYS A 1 234 ? 7.326 22.246 39.487 1.00 30.60 ? 234 LYS A CG 1 ATOM 1811 C CD . LYS A 1 234 ? 7.070 23.073 38.230 1.00 33.41 ? 234 LYS A CD 1 ATOM 1812 C CE . LYS A 1 234 ? 7.427 22.278 36.977 1.00 34.98 ? 234 LYS A CE 1 ATOM 1813 N NZ . LYS A 1 234 ? 7.165 23.030 35.716 1.00 36.57 ? 234 LYS A NZ 1 ATOM 1814 N N . ASN A 1 235 ? 9.149 22.492 43.044 1.00 22.81 ? 235 ASN A N 1 ATOM 1815 C CA . ASN A 1 235 ? 10.537 22.178 43.346 1.00 21.62 ? 235 ASN A CA 1 ATOM 1816 C C . ASN A 1 235 ? 10.636 21.113 44.436 1.00 22.72 ? 235 ASN A C 1 ATOM 1817 O O . ASN A 1 235 ? 11.678 20.479 44.595 1.00 23.03 ? 235 ASN A O 1 ATOM 1818 C CB . ASN A 1 235 ? 11.306 23.444 43.742 1.00 21.98 ? 235 ASN A CB 1 ATOM 1819 C CG . ASN A 1 235 ? 11.595 24.341 42.544 1.00 22.49 ? 235 ASN A CG 1 ATOM 1820 O OD1 . ASN A 1 235 ? 11.826 23.849 41.442 1.00 24.92 ? 235 ASN A OD1 1 ATOM 1821 N ND2 . ASN A 1 235 ? 11.599 25.655 42.757 1.00 20.60 ? 235 ASN A ND2 1 ATOM 1822 N N . VAL A 1 236 ? 9.554 20.920 45.188 1.00 21.81 ? 236 VAL A N 1 ATOM 1823 C CA . VAL A 1 236 ? 9.543 19.877 46.212 1.00 23.62 ? 236 VAL A CA 1 ATOM 1824 C C . VAL A 1 236 ? 9.307 18.570 45.464 1.00 25.05 ? 236 VAL A C 1 ATOM 1825 O O . VAL A 1 236 ? 9.973 17.562 45.710 1.00 24.70 ? 236 VAL A O 1 ATOM 1826 C CB . VAL A 1 236 ? 8.394 20.068 47.244 1.00 23.90 ? 236 VAL A CB 1 ATOM 1827 C CG1 . VAL A 1 236 ? 8.303 18.845 48.158 1.00 23.99 ? 236 VAL A CG1 1 ATOM 1828 C CG2 . VAL A 1 236 ? 8.647 21.306 48.088 1.00 22.97 ? 236 VAL A CG2 1 ATOM 1829 N N . TYR A 1 237 ? 8.365 18.614 44.524 1.00 26.25 ? 237 TYR A N 1 ATOM 1830 C CA . TYR A 1 237 ? 8.005 17.445 43.728 1.00 29.23 ? 237 TYR A CA 1 ATOM 1831 C C . TYR A 1 237 ? 9.159 16.886 42.899 1.00 28.91 ? 237 TYR A C 1 ATOM 1832 O O . TYR A 1 237 ? 9.427 15.689 42.936 1.00 28.29 ? 237 TYR A O 1 ATOM 1833 C CB . TYR A 1 237 ? 6.838 17.782 42.797 1.00 32.14 ? 237 TYR A CB 1 ATOM 1834 C CG . TYR A 1 237 ? 6.378 16.612 41.952 1.00 37.58 ? 237 TYR A CG 1 ATOM 1835 C CD1 . TYR A 1 237 ? 5.703 15.535 42.525 1.00 39.47 ? 237 TYR A CD1 1 ATOM 1836 C CD2 . TYR A 1 237 ? 6.627 16.579 40.580 1.00 39.75 ? 237 TYR A CD2 1 ATOM 1837 C CE1 . TYR A 1 237 ? 5.283 14.451 41.753 1.00 41.93 ? 237 TYR A CE1 1 ATOM 1838 C CE2 . TYR A 1 237 ? 6.213 15.499 39.797 1.00 42.26 ? 237 TYR A CE2 1 ATOM 1839 C CZ . TYR A 1 237 ? 5.543 14.439 40.392 1.00 42.60 ? 237 TYR A CZ 1 ATOM 1840 O OH . TYR A 1 237 ? 5.135 13.370 39.627 1.00 44.79 ? 237 TYR A OH 1 ATOM 1841 N N . TYR A 1 238 ? 9.840 17.748 42.152 1.00 28.95 ? 238 TYR A N 1 ATOM 1842 C CA . TYR A 1 238 ? 10.943 17.300 41.308 1.00 29.97 ? 238 TYR A CA 1 ATOM 1843 C C . TYR A 1 238 ? 12.301 17.314 41.990 1.00 30.23 ? 238 TYR A C 1 ATOM 1844 O O . TYR A 1 238 ? 13.244 16.676 41.516 1.00 31.53 ? 238 TYR A O 1 ATOM 1845 C CB . TYR A 1 238 ? 11.029 18.153 40.033 1.00 32.01 ? 238 TYR A CB 1 ATOM 1846 C CG . TYR A 1 238 ? 9.892 17.941 39.062 1.00 33.78 ? 238 TYR A CG 1 ATOM 1847 C CD1 . TYR A 1 238 ? 8.801 18.808 39.033 1.00 34.43 ? 238 TYR A CD1 1 ATOM 1848 C CD2 . TYR A 1 238 ? 9.905 16.866 38.172 1.00 35.79 ? 238 TYR A CD2 1 ATOM 1849 C CE1 . TYR A 1 238 ? 7.748 18.610 38.138 1.00 37.01 ? 238 TYR A CE1 1 ATOM 1850 C CE2 . TYR A 1 238 ? 8.860 16.657 37.278 1.00 36.85 ? 238 TYR A CE2 1 ATOM 1851 C CZ . TYR A 1 238 ? 7.785 17.532 37.265 1.00 37.55 ? 238 TYR A CZ 1 ATOM 1852 O OH . TYR A 1 238 ? 6.746 17.328 36.382 1.00 39.37 ? 238 TYR A OH 1 ATOM 1853 N N . GLY A 1 239 ? 12.412 18.028 43.103 1.00 28.46 ? 239 GLY A N 1 ATOM 1854 C CA . GLY A 1 239 ? 13.697 18.103 43.765 1.00 27.62 ? 239 GLY A CA 1 ATOM 1855 C C . GLY A 1 239 ? 13.816 17.561 45.174 1.00 27.75 ? 239 GLY A C 1 ATOM 1856 O O . GLY A 1 239 ? 14.304 16.450 45.385 1.00 28.46 ? 239 GLY A O 1 ATOM 1857 N N . VAL A 1 240 ? 13.368 18.351 46.141 1.00 24.97 ? 240 VAL A N 1 ATOM 1858 C CA . VAL A 1 240 ? 13.468 17.983 47.546 1.00 25.01 ? 240 VAL A CA 1 ATOM 1859 C C . VAL A 1 240 ? 12.971 16.591 47.916 1.00 24.65 ? 240 VAL A C 1 ATOM 1860 O O . VAL A 1 240 ? 13.718 15.795 48.487 1.00 24.44 ? 240 VAL A O 1 ATOM 1861 C CB . VAL A 1 240 ? 12.744 19.012 48.430 1.00 26.09 ? 240 VAL A CB 1 ATOM 1862 C CG1 . VAL A 1 240 ? 12.894 18.635 49.899 1.00 24.84 ? 240 VAL A CG1 1 ATOM 1863 C CG2 . VAL A 1 240 ? 13.327 20.401 48.182 1.00 26.27 ? 240 VAL A CG2 1 ATOM 1864 N N . ALA A 1 241 ? 11.715 16.302 47.601 1.00 24.24 ? 241 ALA A N 1 ATOM 1865 C CA . ALA A 1 241 ? 11.132 15.006 47.938 1.00 26.51 ? 241 ALA A CA 1 ATOM 1866 C C . ALA A 1 241 ? 11.909 13.819 47.372 1.00 28.01 ? 241 ALA A C 1 ATOM 1867 O O . ALA A 1 241 ? 12.288 12.905 48.110 1.00 26.69 ? 241 ALA A O 1 ATOM 1868 C CB . ALA A 1 241 ? 9.675 14.958 47.478 1.00 27.04 ? 241 ALA A CB 1 ATOM 1869 N N . PRO A 1 242 ? 12.158 13.810 46.051 1.00 28.89 ? 242 PRO A N 1 ATOM 1870 C CA . PRO A 1 242 ? 12.897 12.705 45.430 1.00 29.49 ? 242 PRO A CA 1 ATOM 1871 C C . PRO A 1 242 ? 14.282 12.499 46.040 1.00 29.45 ? 242 PRO A C 1 ATOM 1872 O O . PRO A 1 242 ? 14.701 11.368 46.281 1.00 30.11 ? 242 PRO A O 1 ATOM 1873 C CB . PRO A 1 242 ? 12.974 13.123 43.962 1.00 30.90 ? 242 PRO A CB 1 ATOM 1874 C CG . PRO A 1 242 ? 11.722 13.924 43.776 1.00 30.96 ? 242 PRO A CG 1 ATOM 1875 C CD . PRO A 1 242 ? 11.689 14.762 45.030 1.00 28.43 ? 242 PRO A CD 1 ATOM 1876 N N . VAL A 1 243 ? 14.990 13.596 46.287 1.00 27.62 ? 243 VAL A N 1 ATOM 1877 C CA . VAL A 1 243 ? 16.327 13.523 46.864 1.00 27.67 ? 243 VAL A CA 1 ATOM 1878 C C . VAL A 1 243 ? 16.303 12.985 48.294 1.00 27.30 ? 243 VAL A C 1 ATOM 1879 O O . VAL A 1 243 ? 17.099 12.116 48.650 1.00 26.75 ? 243 VAL A O 1 ATOM 1880 C CB . VAL A 1 243 ? 17.010 14.911 46.860 1.00 29.20 ? 243 VAL A CB 1 ATOM 1881 C CG1 . VAL A 1 243 ? 18.302 14.868 47.660 1.00 30.28 ? 243 VAL A CG1 1 ATOM 1882 C CG2 . VAL A 1 243 ? 17.298 15.335 45.430 1.00 31.23 ? 243 VAL A CG2 1 ATOM 1883 N N . ALA A 1 244 ? 15.384 13.492 49.110 1.00 24.35 ? 244 ALA A N 1 ATOM 1884 C CA . ALA A 1 244 ? 15.300 13.050 50.497 1.00 24.82 ? 244 ALA A CA 1 ATOM 1885 C C . ALA A 1 244 ? 14.928 11.577 50.596 1.00 23.49 ? 244 ALA A C 1 ATOM 1886 O O . ALA A 1 244 ? 15.494 10.830 51.399 1.00 22.23 ? 244 ALA A O 1 ATOM 1887 C CB . ALA A 1 244 ? 14.279 13.887 51.251 1.00 23.18 ? 244 ALA A CB 1 ATOM 1888 N N . GLN A 1 245 ? 13.980 11.171 49.761 1.00 23.98 ? 245 GLN A N 1 ATOM 1889 C CA . GLN A 1 245 ? 13.481 9.805 49.754 1.00 25.56 ? 245 GLN A CA 1 ATOM 1890 C C . GLN A 1 245 ? 14.440 8.731 49.243 1.00 26.48 ? 245 GLN A C 1 ATOM 1891 O O . GLN A 1 245 ? 14.112 7.544 49.261 1.00 27.06 ? 245 GLN A O 1 ATOM 1892 C CB . GLN A 1 245 ? 12.154 9.777 48.996 1.00 25.09 ? 245 GLN A CB 1 ATOM 1893 C CG . GLN A 1 245 ? 11.086 10.578 49.737 1.00 25.50 ? 245 GLN A CG 1 ATOM 1894 C CD . GLN A 1 245 ? 9.887 10.941 48.889 1.00 26.11 ? 245 GLN A CD 1 ATOM 1895 O OE1 . GLN A 1 245 ? 8.978 11.638 49.352 1.00 27.76 ? 245 GLN A OE1 1 ATOM 1896 N NE2 . GLN A 1 245 ? 9.873 10.479 47.647 1.00 24.41 ? 245 GLN A NE2 1 ATOM 1897 N N . LYS A 1 246 ? 15.628 9.136 48.811 1.00 28.57 ? 246 LYS A N 1 ATOM 1898 C CA . LYS A 1 246 ? 16.615 8.168 48.339 1.00 30.17 ? 246 LYS A CA 1 ATOM 1899 C C . LYS A 1 246 ? 17.183 7.386 49.520 1.00 30.20 ? 246 LYS A C 1 ATOM 1900 O O . LYS A 1 246 ? 17.661 6.262 49.359 1.00 28.56 ? 246 LYS A O 1 ATOM 1901 C CB . LYS A 1 246 ? 17.757 8.871 47.602 1.00 33.46 ? 246 LYS A CB 1 ATOM 1902 C CG . LYS A 1 246 ? 17.364 9.433 46.248 1.00 37.38 ? 246 LYS A CG 1 ATOM 1903 C CD . LYS A 1 246 ? 18.560 10.053 45.544 1.00 42.48 ? 246 LYS A CD 1 ATOM 1904 C CE . LYS A 1 246 ? 18.165 10.622 44.186 1.00 44.84 ? 246 LYS A CE 1 ATOM 1905 N NZ . LYS A 1 246 ? 19.329 11.227 43.476 1.00 46.40 ? 246 LYS A NZ 1 ATOM 1906 N N . LYS A 1 247 ? 17.126 7.984 50.709 1.00 28.50 ? 247 LYS A N 1 ATOM 1907 C CA . LYS A 1 247 ? 17.640 7.342 51.916 1.00 28.92 ? 247 LYS A CA 1 ATOM 1908 C C . LYS A 1 247 ? 16.634 6.337 52.470 1.00 27.99 ? 247 LYS A C 1 ATOM 1909 O O . LYS A 1 247 ? 15.426 6.589 52.475 1.00 26.77 ? 247 LYS A O 1 ATOM 1910 C CB . LYS A 1 247 ? 17.958 8.395 52.980 1.00 29.89 ? 247 LYS A CB 1 ATOM 1911 C CG . LYS A 1 247 ? 18.923 9.471 52.517 1.00 33.15 ? 247 LYS A CG 1 ATOM 1912 C CD . LYS A 1 247 ? 20.264 8.886 52.087 1.00 34.88 ? 247 LYS A CD 1 ATOM 1913 C CE . LYS A 1 247 ? 21.201 9.986 51.607 1.00 37.09 ? 247 LYS A CE 1 ATOM 1914 N NZ . LYS A 1 247 ? 22.521 9.463 51.170 1.00 38.44 ? 247 LYS A NZ 1 ATOM 1915 N N . ASP A 1 248 ? 17.143 5.201 52.939 1.00 27.57 ? 248 ASP A N 1 ATOM 1916 C CA . ASP A 1 248 ? 16.301 4.140 53.484 1.00 28.72 ? 248 ASP A CA 1 ATOM 1917 C C . ASP A 1 248 ? 15.509 4.570 54.709 1.00 26.91 ? 248 ASP A C 1 ATOM 1918 O O . ASP A 1 248 ? 14.395 4.091 54.931 1.00 26.65 ? 248 ASP A O 1 ATOM 1919 C CB . ASP A 1 248 ? 17.146 2.922 53.859 1.00 31.61 ? 248 ASP A CB 1 ATOM 1920 C CG . ASP A 1 248 ? 17.881 2.336 52.675 1.00 35.92 ? 248 ASP A CG 1 ATOM 1921 O OD1 . ASP A 1 248 ? 17.242 2.152 51.619 1.00 38.31 ? 248 ASP A OD1 1 ATOM 1922 O OD2 . ASP A 1 248 ? 19.092 2.052 52.803 1.00 38.50 ? 248 ASP A OD2 1 ATOM 1923 N N . ASN A 1 249 ? 16.085 5.464 55.508 1.00 25.01 ? 249 ASN A N 1 ATOM 1924 C CA . ASN A 1 249 ? 15.406 5.918 56.714 1.00 22.81 ? 249 ASN A CA 1 ATOM 1925 C C . ASN A 1 249 ? 14.683 7.264 56.606 1.00 23.17 ? 249 ASN A C 1 ATOM 1926 O O . ASN A 1 249 ? 14.531 7.979 57.600 1.00 20.63 ? 249 ASN A O 1 ATOM 1927 C CB . ASN A 1 249 ? 16.375 5.905 57.911 1.00 21.51 ? 249 ASN A CB 1 ATOM 1928 C CG . ASN A 1 249 ? 17.658 6.675 57.656 1.00 22.25 ? 249 ASN A CG 1 ATOM 1929 O OD1 . ASN A 1 249 ? 18.029 6.941 56.510 1.00 22.31 ? 249 ASN A OD1 1 ATOM 1930 N ND2 . ASN A 1 249 ? 18.363 7.015 58.736 1.00 18.37 ? 249 ASN A ND2 1 ATOM 1931 N N . TYR A 1 250 ? 14.237 7.597 55.396 1.00 22.71 ? 250 TYR A N 1 ATOM 1932 C CA . TYR A 1 250 ? 13.464 8.815 55.172 1.00 21.56 ? 250 TYR A CA 1 ATOM 1933 C C . TYR A 1 250 ? 12.113 8.545 55.835 1.00 22.03 ? 250 TYR A C 1 ATOM 1934 O O . TYR A 1 250 ? 11.522 7.477 55.636 1.00 20.48 ? 250 TYR A O 1 ATOM 1935 C CB . TYR A 1 250 ? 13.258 9.062 53.671 1.00 21.32 ? 250 TYR A CB 1 ATOM 1936 C CG . TYR A 1 250 ? 12.107 9.991 53.358 1.00 19.95 ? 250 TYR A CG 1 ATOM 1937 C CD1 . TYR A 1 250 ? 12.277 11.376 53.349 1.00 19.44 ? 250 TYR A CD1 1 ATOM 1938 C CD2 . TYR A 1 250 ? 10.831 9.485 53.107 1.00 18.73 ? 250 TYR A CD2 1 ATOM 1939 C CE1 . TYR A 1 250 ? 11.203 12.230 53.098 1.00 18.60 ? 250 TYR A CE1 1 ATOM 1940 C CE2 . TYR A 1 250 ? 9.756 10.330 52.859 1.00 21.13 ? 250 TYR A CE2 1 ATOM 1941 C CZ . TYR A 1 250 ? 9.950 11.702 52.855 1.00 20.12 ? 250 TYR A CZ 1 ATOM 1942 O OH . TYR A 1 250 ? 8.885 12.539 52.605 1.00 18.90 ? 250 TYR A OH 1 ATOM 1943 N N . GLY A 1 251 ? 11.623 9.505 56.614 1.00 20.56 ? 251 GLY A N 1 ATOM 1944 C CA . GLY A 1 251 ? 10.354 9.316 57.295 1.00 20.88 ? 251 GLY A CA 1 ATOM 1945 C C . GLY A 1 251 ? 9.193 10.174 56.832 1.00 20.01 ? 251 GLY A C 1 ATOM 1946 O O . GLY A 1 251 ? 8.034 9.774 56.979 1.00 20.85 ? 251 GLY A O 1 ATOM 1947 N N . GLY A 1 252 ? 9.481 11.355 56.288 1.00 18.46 ? 252 GLY A N 1 ATOM 1948 C CA . GLY A 1 252 ? 8.406 12.215 55.828 1.00 17.98 ? 252 GLY A CA 1 ATOM 1949 C C . GLY A 1 252 ? 8.811 13.674 55.786 1.00 17.01 ? 252 GLY A C 1 ATOM 1950 O O . GLY A 1 252 ? 9.997 13.988 55.731 1.00 17.11 ? 252 GLY A O 1 ATOM 1951 N N . ILE A 1 253 ? 7.820 14.557 55.819 1.00 16.76 ? 253 ILE A N 1 ATOM 1952 C CA . ILE A 1 253 ? 8.057 15.994 55.783 1.00 17.85 ? 253 ILE A CA 1 ATOM 1953 C C . ILE A 1 253 ? 7.526 16.686 57.036 1.00 16.46 ? 253 ILE A C 1 ATOM 1954 O O . ILE A 1 253 ? 6.444 16.370 57.516 1.00 17.92 ? 253 ILE A O 1 ATOM 1955 C CB . ILE A 1 253 ? 7.365 16.626 54.547 1.00 18.30 ? 253 ILE A CB 1 ATOM 1956 C CG1 . ILE A 1 253 ? 8.079 16.180 53.272 1.00 19.40 ? 253 ILE A CG1 1 ATOM 1957 C CG2 . ILE A 1 253 ? 7.351 18.160 54.665 1.00 18.58 ? 253 ILE A CG2 1 ATOM 1958 C CD1 . ILE A 1 253 ? 7.411 16.638 51.988 1.00 20.94 ? 253 ILE A CD1 1 ATOM 1959 N N . MET A 1 254 ? 8.296 17.630 57.567 1.00 17.35 ? 254 MET A N 1 ATOM 1960 C CA . MET A 1 254 ? 7.859 18.392 58.737 1.00 17.00 ? 254 MET A CA 1 ATOM 1961 C C . MET A 1 254 ? 7.585 19.799 58.234 1.00 16.81 ? 254 MET A C 1 ATOM 1962 O O . MET A 1 254 ? 8.353 20.320 57.428 1.00 16.59 ? 254 MET A O 1 ATOM 1963 C CB . MET A 1 254 ? 8.953 18.438 59.807 1.00 16.54 ? 254 MET A CB 1 ATOM 1964 C CG . MET A 1 254 ? 8.592 19.274 61.031 1.00 19.33 ? 254 MET A CG 1 ATOM 1965 S SD . MET A 1 254 ? 8.974 21.032 60.809 1.00 21.44 ? 254 MET A SD 1 ATOM 1966 C CE . MET A 1 254 ? 10.683 21.019 61.221 1.00 17.30 ? 254 MET A CE 1 ATOM 1967 N N . LEU A 1 255 ? 6.496 20.404 58.699 1.00 16.27 ? 255 LEU A N 1 ATOM 1968 C CA . LEU A 1 255 ? 6.143 21.754 58.274 1.00 16.40 ? 255 LEU A CA 1 ATOM 1969 C C . LEU A 1 255 ? 6.080 22.753 59.415 1.00 16.71 ? 255 LEU A C 1 ATOM 1970 O O . LEU A 1 255 ? 5.513 22.483 60.475 1.00 16.21 ? 255 LEU A O 1 ATOM 1971 C CB . LEU A 1 255 ? 4.788 21.761 57.556 1.00 16.60 ? 255 LEU A CB 1 ATOM 1972 C CG . LEU A 1 255 ? 4.672 20.988 56.240 1.00 19.89 ? 255 LEU A CG 1 ATOM 1973 C CD1 . LEU A 1 255 ? 3.250 21.109 55.714 1.00 20.73 ? 255 LEU A CD1 1 ATOM 1974 C CD2 . LEU A 1 255 ? 5.663 21.535 55.224 1.00 19.00 ? 255 LEU A CD2 1 ATOM 1975 N N . TRP A 1 256 ? 6.665 23.922 59.183 1.00 16.98 ? 256 TRP A N 1 ATOM 1976 C CA . TRP A 1 256 ? 6.636 25.006 60.156 1.00 17.41 ? 256 TRP A CA 1 ATOM 1977 C C . TRP A 1 256 ? 5.921 26.159 59.452 1.00 18.36 ? 256 TRP A C 1 ATOM 1978 O O . TRP A 1 256 ? 6.469 26.701 58.496 1.00 18.76 ? 256 TRP A O 1 ATOM 1979 C CB . TRP A 1 256 ? 8.057 25.444 60.520 1.00 18.42 ? 256 TRP A CB 1 ATOM 1980 C CG . TRP A 1 256 ? 8.079 26.577 61.501 1.00 17.35 ? 256 TRP A CG 1 ATOM 1981 C CD1 . TRP A 1 256 ? 7.848 27.903 61.238 1.00 19.07 ? 256 TRP A CD1 1 ATOM 1982 C CD2 . TRP A 1 256 ? 8.261 26.476 62.916 1.00 17.95 ? 256 TRP A CD2 1 ATOM 1983 N NE1 . TRP A 1 256 ? 7.872 28.629 62.407 1.00 19.29 ? 256 TRP A NE1 1 ATOM 1984 C CE2 . TRP A 1 256 ? 8.124 27.778 63.452 1.00 19.97 ? 256 TRP A CE2 1 ATOM 1985 C CE3 . TRP A 1 256 ? 8.523 25.408 63.787 1.00 18.42 ? 256 TRP A CE3 1 ATOM 1986 C CZ2 . TRP A 1 256 ? 8.242 28.040 64.819 1.00 20.08 ? 256 TRP A CZ2 1 ATOM 1987 C CZ3 . TRP A 1 256 ? 8.639 25.668 65.145 1.00 19.24 ? 256 TRP A CZ3 1 ATOM 1988 C CH2 . TRP A 1 256 ? 8.498 26.977 65.648 1.00 19.58 ? 256 TRP A CH2 1 ATOM 1989 N N . ASP A 1 257 ? 4.707 26.523 59.874 1.00 18.56 ? 257 ASP A N 1 ATOM 1990 C CA . ASP A 1 257 ? 3.968 25.896 60.969 1.00 17.11 ? 257 ASP A CA 1 ATOM 1991 C C . ASP A 1 257 ? 2.481 25.945 60.599 1.00 18.91 ? 257 ASP A C 1 ATOM 1992 O O . ASP A 1 257 ? 2.147 26.258 59.462 1.00 18.02 ? 257 ASP A O 1 ATOM 1993 C CB . ASP A 1 257 ? 4.217 26.642 62.288 1.00 16.49 ? 257 ASP A CB 1 ATOM 1994 C CG . ASP A 1 257 ? 3.746 28.095 62.248 1.00 18.59 ? 257 ASP A CG 1 ATOM 1995 O OD1 . ASP A 1 257 ? 3.338 28.573 61.170 1.00 19.01 ? 257 ASP A OD1 1 ATOM 1996 O OD2 . ASP A 1 257 ? 3.793 28.757 63.305 1.00 20.08 ? 257 ASP A OD2 1 ATOM 1997 N N . ARG A 1 258 ? 1.588 25.635 61.538 1.00 18.27 ? 258 ARG A N 1 ATOM 1998 C CA . ARG A 1 258 ? 0.158 25.652 61.229 1.00 20.23 ? 258 ARG A CA 1 ATOM 1999 C C . ARG A 1 258 ? -0.291 27.027 60.736 1.00 20.76 ? 258 ARG A C 1 ATOM 2000 O O . ARG A 1 258 ? -1.032 27.132 59.758 1.00 21.87 ? 258 ARG A O 1 ATOM 2001 C CB . ARG A 1 258 ? -0.664 25.234 62.457 1.00 20.31 ? 258 ARG A CB 1 ATOM 2002 C CG . ARG A 1 258 ? -2.186 25.351 62.289 1.00 22.56 ? 258 ARG A CG 1 ATOM 2003 C CD . ARG A 1 258 ? -2.727 24.544 61.106 1.00 21.75 ? 258 ARG A CD 1 ATOM 2004 N NE . ARG A 1 258 ? -4.185 24.657 61.020 1.00 24.51 ? 258 ARG A NE 1 ATOM 2005 C CZ . ARG A 1 258 ? -4.909 24.348 59.947 1.00 27.27 ? 258 ARG A CZ 1 ATOM 2006 N NH1 . ARG A 1 258 ? -4.319 23.900 58.844 1.00 26.55 ? 258 ARG A NH1 1 ATOM 2007 N NH2 . ARG A 1 258 ? -6.232 24.496 59.975 1.00 27.01 ? 258 ARG A NH2 1 ATOM 2008 N N . TYR A 1 259 ? 0.172 28.075 61.411 1.00 21.28 ? 259 TYR A N 1 ATOM 2009 C CA . TYR A 1 259 ? -0.169 29.448 61.045 1.00 22.55 ? 259 TYR A CA 1 ATOM 2010 C C . TYR A 1 259 ? 0.130 29.725 59.573 1.00 21.89 ? 259 TYR A C 1 ATOM 2011 O O . TYR A 1 259 ? -0.761 30.091 58.801 1.00 21.72 ? 259 TYR A O 1 ATOM 2012 C CB . TYR A 1 259 ? 0.626 30.428 61.908 1.00 22.64 ? 259 TYR A CB 1 ATOM 2013 C CG . TYR A 1 259 ? 0.370 31.882 61.576 1.00 26.06 ? 259 TYR A CG 1 ATOM 2014 C CD1 . TYR A 1 259 ? -0.797 32.522 62.001 1.00 27.09 ? 259 TYR A CD1 1 ATOM 2015 C CD2 . TYR A 1 259 ? 1.288 32.614 60.828 1.00 26.01 ? 259 TYR A CD2 1 ATOM 2016 C CE1 . TYR A 1 259 ? -1.041 33.864 61.686 1.00 28.46 ? 259 TYR A CE1 1 ATOM 2017 C CE2 . TYR A 1 259 ? 1.055 33.954 60.507 1.00 28.67 ? 259 TYR A CE2 1 ATOM 2018 C CZ . TYR A 1 259 ? -0.109 34.572 60.939 1.00 29.84 ? 259 TYR A CZ 1 ATOM 2019 O OH . TYR A 1 259 ? -0.330 35.899 60.630 1.00 32.43 ? 259 TYR A OH 1 ATOM 2020 N N . PHE A 1 260 ? 1.392 29.554 59.189 1.00 20.77 ? 260 PHE A N 1 ATOM 2021 C CA . PHE A 1 260 ? 1.805 29.796 57.816 1.00 22.23 ? 260 PHE A CA 1 ATOM 2022 C C . PHE A 1 260 ? 1.100 28.878 56.829 1.00 23.25 ? 260 PHE A C 1 ATOM 2023 O O . PHE A 1 260 ? 0.682 29.316 55.753 1.00 24.83 ? 260 PHE A O 1 ATOM 2024 C CB . PHE A 1 260 ? 3.324 29.629 57.675 1.00 20.36 ? 260 PHE A CB 1 ATOM 2025 C CG . PHE A 1 260 ? 4.120 30.716 58.339 1.00 23.54 ? 260 PHE A CG 1 ATOM 2026 C CD1 . PHE A 1 260 ? 3.803 32.058 58.128 1.00 24.58 ? 260 PHE A CD1 1 ATOM 2027 C CD2 . PHE A 1 260 ? 5.213 30.404 59.143 1.00 23.74 ? 260 PHE A CD2 1 ATOM 2028 C CE1 . PHE A 1 260 ? 4.564 33.071 58.708 1.00 23.54 ? 260 PHE A CE1 1 ATOM 2029 C CE2 . PHE A 1 260 ? 5.981 31.410 59.729 1.00 23.17 ? 260 PHE A CE2 1 ATOM 2030 C CZ . PHE A 1 260 ? 5.654 32.747 59.509 1.00 24.35 ? 260 PHE A CZ 1 ATOM 2031 N N . ASP A 1 261 ? 0.953 27.608 57.199 1.00 24.33 ? 261 ASP A N 1 ATOM 2032 C CA . ASP A 1 261 ? 0.311 26.638 56.320 1.00 26.65 ? 261 ASP A CA 1 ATOM 2033 C C . ASP A 1 261 ? -1.143 27.021 56.078 1.00 29.17 ? 261 ASP A C 1 ATOM 2034 O O . ASP A 1 261 ? -1.677 26.820 54.990 1.00 30.22 ? 261 ASP A O 1 ATOM 2035 C CB . ASP A 1 261 ? 0.390 25.232 56.924 1.00 25.83 ? 261 ASP A CB 1 ATOM 2036 C CG . ASP A 1 261 ? 0.060 24.145 55.914 1.00 24.85 ? 261 ASP A CG 1 ATOM 2037 O OD1 . ASP A 1 261 ? 0.494 24.273 54.752 1.00 25.94 ? 261 ASP A OD1 1 ATOM 2038 O OD2 . ASP A 1 261 ? -0.613 23.154 56.276 1.00 26.48 ? 261 ASP A OD2 1 ATOM 2039 N N . LYS A 1 262 ? -1.773 27.576 57.103 1.00 31.05 ? 262 LYS A N 1 ATOM 2040 C CA . LYS A 1 262 ? -3.163 27.991 57.019 1.00 35.46 ? 262 LYS A CA 1 ATOM 2041 C C . LYS A 1 262 ? -3.320 29.155 56.039 1.00 36.53 ? 262 LYS A C 1 ATOM 2042 O O . LYS A 1 262 ? -4.326 29.252 55.337 1.00 38.22 ? 262 LYS A O 1 ATOM 2043 C CB . LYS A 1 262 ? -3.652 28.391 58.415 1.00 36.74 ? 262 LYS A CB 1 ATOM 2044 C CG . LYS A 1 262 ? -5.121 28.749 58.513 1.00 40.80 ? 262 LYS A CG 1 ATOM 2045 C CD . LYS A 1 262 ? -5.513 28.988 59.963 1.00 42.32 ? 262 LYS A CD 1 ATOM 2046 C CE . LYS A 1 262 ? -6.968 29.404 60.078 1.00 43.90 ? 262 LYS A CE 1 ATOM 2047 N NZ . LYS A 1 262 ? -7.871 28.393 59.468 1.00 45.75 ? 262 LYS A NZ 1 ATOM 2048 N N . GLN A 1 263 ? -2.318 30.027 55.983 1.00 38.00 ? 263 GLN A N 1 ATOM 2049 C CA . GLN A 1 263 ? -2.361 31.186 55.091 1.00 39.63 ? 263 GLN A CA 1 ATOM 2050 C C . GLN A 1 263 ? -1.949 30.881 53.656 1.00 39.21 ? 263 GLN A C 1 ATOM 2051 O O . GLN A 1 263 ? -2.344 31.594 52.731 1.00 39.80 ? 263 GLN A O 1 ATOM 2052 C CB . GLN A 1 263 ? -1.452 32.301 55.612 1.00 41.77 ? 263 GLN A CB 1 ATOM 2053 C CG . GLN A 1 263 ? -1.829 32.867 56.963 1.00 46.66 ? 263 GLN A CG 1 ATOM 2054 C CD . GLN A 1 263 ? -1.022 34.109 57.300 1.00 50.68 ? 263 GLN A CD 1 ATOM 2055 O OE1 . GLN A 1 263 ? 0.209 34.108 57.210 1.00 52.34 ? 263 GLN A OE1 1 ATOM 2056 N NE2 . GLN A 1 263 ? -1.711 35.177 57.691 1.00 51.81 ? 263 GLN A NE2 1 ATOM 2057 N N . THR A 1 264 ? -1.156 29.831 53.468 1.00 36.45 ? 264 THR A N 1 ATOM 2058 C CA . THR A 1 264 ? -0.671 29.482 52.138 1.00 34.90 ? 264 THR A CA 1 ATOM 2059 C C . THR A 1 264 ? -1.200 28.166 51.580 1.00 34.19 ? 264 THR A C 1 ATOM 2060 O O . THR A 1 264 ? -1.062 27.899 50.386 1.00 32.95 ? 264 THR A O 1 ATOM 2061 C CB . THR A 1 264 ? 0.863 29.403 52.130 1.00 35.17 ? 264 THR A CB 1 ATOM 2062 O OG1 . THR A 1 264 ? 1.287 28.348 53.006 1.00 34.42 ? 264 THR A OG1 1 ATOM 2063 C CG2 . THR A 1 264 ? 1.469 30.719 52.602 1.00 34.95 ? 264 THR A CG2 1 ATOM 2064 N N . ASN A 1 265 ? -1.792 27.343 52.441 1.00 32.37 ? 265 ASN A N 1 ATOM 2065 C CA . ASN A 1 265 ? -2.317 26.049 52.020 1.00 32.61 ? 265 ASN A CA 1 ATOM 2066 C C . ASN A 1 265 ? -1.222 25.198 51.390 1.00 30.84 ? 265 ASN A C 1 ATOM 2067 O O . ASN A 1 265 ? -1.474 24.397 50.487 1.00 29.44 ? 265 ASN A O 1 ATOM 2068 C CB . ASN A 1 265 ? -3.473 26.243 51.036 1.00 38.13 ? 265 ASN A CB 1 ATOM 2069 C CG . ASN A 1 265 ? -4.730 26.745 51.715 1.00 44.08 ? 265 ASN A CG 1 ATOM 2070 O OD1 . ASN A 1 265 ? -5.271 26.078 52.592 1.00 46.27 ? 265 ASN A OD1 1 ATOM 2071 N ND2 . ASN A 1 265 ? -5.195 27.924 51.318 1.00 50.92 ? 265 ASN A ND2 1 ATOM 2072 N N . TYR A 1 266 ? -0.004 25.373 51.895 1.00 28.02 ? 266 TYR A N 1 ATOM 2073 C CA . TYR A 1 266 ? 1.169 24.653 51.412 1.00 25.68 ? 266 TYR A CA 1 ATOM 2074 C C . TYR A 1 266 ? 0.994 23.130 51.433 1.00 25.43 ? 266 TYR A C 1 ATOM 2075 O O . TYR A 1 266 ? 1.315 22.448 50.457 1.00 24.50 ? 266 TYR A O 1 ATOM 2076 C CB . TYR A 1 266 ? 2.385 25.062 52.254 1.00 24.66 ? 266 TYR A CB 1 ATOM 2077 C CG . TYR A 1 266 ? 3.732 24.636 51.709 1.00 22.77 ? 266 TYR A CG 1 ATOM 2078 C CD1 . TYR A 1 266 ? 4.137 24.999 50.423 1.00 22.45 ? 266 TYR A CD1 1 ATOM 2079 C CD2 . TYR A 1 266 ? 4.627 23.913 52.501 1.00 21.77 ? 266 TYR A CD2 1 ATOM 2080 C CE1 . TYR A 1 266 ? 5.404 24.655 49.944 1.00 21.41 ? 266 TYR A CE1 1 ATOM 2081 C CE2 . TYR A 1 266 ? 5.889 23.568 52.034 1.00 20.62 ? 266 TYR A CE2 1 ATOM 2082 C CZ . TYR A 1 266 ? 6.274 23.942 50.757 1.00 21.45 ? 266 TYR A CZ 1 ATOM 2083 O OH . TYR A 1 266 ? 7.530 23.612 50.304 1.00 20.01 ? 266 TYR A OH 1 ATOM 2084 N N . SER A 1 267 ? 0.473 22.595 52.534 1.00 24.37 ? 267 SER A N 1 ATOM 2085 C CA . SER A 1 267 ? 0.292 21.152 52.660 1.00 24.57 ? 267 SER A CA 1 ATOM 2086 C C . SER A 1 267 ? -0.727 20.538 51.702 1.00 25.91 ? 267 SER A C 1 ATOM 2087 O O . SER A 1 267 ? -0.713 19.327 51.479 1.00 25.39 ? 267 SER A O 1 ATOM 2088 C CB . SER A 1 267 ? -0.082 20.786 54.101 1.00 23.96 ? 267 SER A CB 1 ATOM 2089 O OG . SER A 1 267 ? -1.293 21.400 54.485 1.00 24.45 ? 267 SER A OG 1 ATOM 2090 N N . SER A 1 268 ? -1.614 21.358 51.143 1.00 27.45 ? 268 SER A N 1 ATOM 2091 C CA . SER A 1 268 ? -2.612 20.845 50.207 1.00 29.68 ? 268 SER A CA 1 ATOM 2092 C C . SER A 1 268 ? -1.932 20.044 49.102 1.00 30.39 ? 268 SER A C 1 ATOM 2093 O O . SER A 1 268 ? -2.454 19.030 48.643 1.00 30.29 ? 268 SER A O 1 ATOM 2094 C CB . SER A 1 268 ? -3.415 21.992 49.587 1.00 31.75 ? 268 SER A CB 1 ATOM 2095 O OG . SER A 1 268 ? -4.306 22.552 50.533 1.00 36.28 ? 268 SER A OG 1 ATOM 2096 N N . LEU A 1 269 ? -0.762 20.503 48.676 1.00 30.76 ? 269 LEU A N 1 ATOM 2097 C CA . LEU A 1 269 ? -0.018 19.805 47.638 1.00 31.69 ? 269 LEU A CA 1 ATOM 2098 C C . LEU A 1 269 ? 1.093 18.955 48.242 1.00 31.61 ? 269 LEU A C 1 ATOM 2099 O O . LEU A 1 269 ? 1.280 17.799 47.859 1.00 32.58 ? 269 LEU A O 1 ATOM 2100 C CB . LEU A 1 269 ? 0.592 20.805 46.650 1.00 33.93 ? 269 LEU A CB 1 ATOM 2101 C CG . LEU A 1 269 ? -0.366 21.602 45.761 1.00 35.65 ? 269 LEU A CG 1 ATOM 2102 C CD1 . LEU A 1 269 ? 0.432 22.556 44.875 1.00 36.15 ? 269 LEU A CD1 1 ATOM 2103 C CD2 . LEU A 1 269 ? -1.187 20.646 44.906 1.00 36.47 ? 269 LEU A CD2 1 ATOM 2104 N N . ILE A 1 270 ? 1.820 19.526 49.197 1.00 30.09 ? 270 ILE A N 1 ATOM 2105 C CA . ILE A 1 270 ? 2.931 18.823 49.829 1.00 30.04 ? 270 ILE A CA 1 ATOM 2106 C C . ILE A 1 270 ? 2.609 17.447 50.410 1.00 28.78 ? 270 ILE A C 1 ATOM 2107 O O . ILE A 1 270 ? 3.440 16.544 50.335 1.00 27.21 ? 270 ILE A O 1 ATOM 2108 C CB . ILE A 1 270 ? 3.595 19.706 50.929 1.00 30.99 ? 270 ILE A CB 1 ATOM 2109 C CG1 . ILE A 1 270 ? 4.815 20.420 50.343 1.00 31.66 ? 270 ILE A CG1 1 ATOM 2110 C CG2 . ILE A 1 270 ? 4.024 18.861 52.124 1.00 31.52 ? 270 ILE A CG2 1 ATOM 2111 C CD1 . ILE A 1 270 ? 4.517 21.251 49.114 1.00 31.27 ? 270 ILE A CD1 1 ATOM 2112 N N . LYS A 1 271 ? 1.417 17.277 50.979 1.00 29.10 ? 271 LYS A N 1 ATOM 2113 C CA . LYS A 1 271 ? 1.070 15.988 51.567 1.00 29.44 ? 271 LYS A CA 1 ATOM 2114 C C . LYS A 1 271 ? 1.099 14.858 50.548 1.00 30.07 ? 271 LYS A C 1 ATOM 2115 O O . LYS A 1 271 ? 1.255 13.694 50.914 1.00 28.20 ? 271 LYS A O 1 ATOM 2116 C CB . LYS A 1 271 ? -0.304 16.039 52.249 1.00 30.36 ? 271 LYS A CB 1 ATOM 2117 C CG . LYS A 1 271 ? -1.503 16.179 51.320 1.00 32.93 ? 271 LYS A CG 1 ATOM 2118 C CD . LYS A 1 271 ? -2.793 15.985 52.107 1.00 35.31 ? 271 LYS A CD 1 ATOM 2119 C CE . LYS A 1 271 ? -4.029 16.022 51.220 1.00 38.09 ? 271 LYS A CE 1 ATOM 2120 N NZ . LYS A 1 271 ? -4.276 17.370 50.642 1.00 40.45 ? 271 LYS A NZ 1 ATOM 2121 N N . TYR A 1 272 ? 0.959 15.200 49.270 1.00 30.25 ? 272 TYR A N 1 ATOM 2122 C CA . TYR A 1 272 ? 0.988 14.190 48.218 1.00 31.56 ? 272 TYR A CA 1 ATOM 2123 C C . TYR A 1 272 ? 2.410 13.809 47.821 1.00 30.77 ? 272 TYR A C 1 ATOM 2124 O O . TYR A 1 272 ? 2.624 12.781 47.180 1.00 30.86 ? 272 TYR A O 1 ATOM 2125 C CB . TYR A 1 272 ? 0.234 14.676 46.976 1.00 33.83 ? 272 TYR A CB 1 ATOM 2126 C CG . TYR A 1 272 ? -1.259 14.762 47.166 1.00 37.62 ? 272 TYR A CG 1 ATOM 2127 C CD1 . TYR A 1 272 ? -1.847 15.889 47.736 1.00 39.12 ? 272 TYR A CD1 1 ATOM 2128 C CD2 . TYR A 1 272 ? -2.084 13.697 46.807 1.00 40.15 ? 272 TYR A CD2 1 ATOM 2129 C CE1 . TYR A 1 272 ? -3.220 15.953 47.946 1.00 41.07 ? 272 TYR A CE1 1 ATOM 2130 C CE2 . TYR A 1 272 ? -3.459 13.750 47.014 1.00 42.27 ? 272 TYR A CE2 1 ATOM 2131 C CZ . TYR A 1 272 ? -4.019 14.880 47.585 1.00 42.34 ? 272 TYR A CZ 1 ATOM 2132 O OH . TYR A 1 272 ? -5.377 14.931 47.798 1.00 44.80 ? 272 TYR A OH 1 ATOM 2133 N N . TYR A 1 273 ? 3.383 14.633 48.196 1.00 29.62 ? 273 TYR A N 1 ATOM 2134 C CA . TYR A 1 273 ? 4.771 14.343 47.850 1.00 28.53 ? 273 TYR A CA 1 ATOM 2135 C C . TYR A 1 273 ? 5.525 13.699 49.008 1.00 26.89 ? 273 TYR A C 1 ATOM 2136 O O . TYR A 1 273 ? 6.618 13.176 48.821 1.00 26.95 ? 273 TYR A O 1 ATOM 2137 C CB . TYR A 1 273 ? 5.509 15.622 47.427 1.00 29.42 ? 273 TYR A CB 1 ATOM 2138 C CG . TYR A 1 273 ? 4.741 16.522 46.479 1.00 30.57 ? 273 TYR A CG 1 ATOM 2139 C CD1 . TYR A 1 273 ? 3.861 15.994 45.534 1.00 32.84 ? 273 TYR A CD1 1 ATOM 2140 C CD2 . TYR A 1 273 ? 4.900 17.908 46.527 1.00 31.29 ? 273 TYR A CD2 1 ATOM 2141 C CE1 . TYR A 1 273 ? 3.153 16.829 44.664 1.00 33.94 ? 273 TYR A CE1 1 ATOM 2142 C CE2 . TYR A 1 273 ? 4.203 18.746 45.664 1.00 33.34 ? 273 TYR A CE2 1 ATOM 2143 C CZ . TYR A 1 273 ? 3.330 18.202 44.737 1.00 34.35 ? 273 TYR A CZ 1 ATOM 2144 O OH . TYR A 1 273 ? 2.629 19.035 43.895 1.00 36.72 ? 273 TYR A OH 1 ATOM 2145 N N . ALA A 1 274 ? 4.937 13.739 50.200 1.00 26.77 ? 274 ALA A N 1 ATOM 2146 C CA . ALA A 1 274 ? 5.578 13.175 51.387 1.00 26.94 ? 274 ALA A CA 1 ATOM 2147 C C . ALA A 1 274 ? 5.549 11.650 51.411 1.00 26.98 ? 274 ALA A C 1 ATOM 2148 O O . ALA A 1 274 ? 4.576 11.070 50.892 1.00 27.78 ? 274 ALA A O 1 ATOM 2149 C CB . ALA A 1 274 ? 4.901 13.722 52.640 1.00 24.64 ? 274 ALA A CB 1 ATOM 2150 O OXT . ALA A 1 274 ? 6.491 11.054 51.980 1.00 27.94 ? 274 ALA A OXT 1 HETATM 2151 C C1 . NDG B 2 . ? -6.026 28.018 50.135 1.00 55.75 ? 900 NDG A C1 1 HETATM 2152 C C2 . NDG B 2 . ? -6.098 29.477 49.666 1.00 58.32 ? 900 NDG A C2 1 HETATM 2153 C C3 . NDG B 2 . ? -6.919 30.321 50.652 1.00 59.39 ? 900 NDG A C3 1 HETATM 2154 C C4 . NDG B 2 . ? -8.276 29.668 50.914 1.00 60.21 ? 900 NDG A C4 1 HETATM 2155 C C5 . NDG B 2 . ? -8.066 28.227 51.381 1.00 59.99 ? 900 NDG A C5 1 HETATM 2156 C C6 . NDG B 2 . ? -9.375 27.498 51.619 1.00 61.06 ? 900 NDG A C6 1 HETATM 2157 C C7 . NDG B 2 . ? -4.529 31.185 48.998 1.00 61.21 ? 900 NDG A C7 1 HETATM 2158 C C8 . NDG B 2 . ? -4.299 31.196 47.495 1.00 61.73 ? 900 NDG A C8 1 HETATM 2159 O O . NDG B 2 . ? -7.339 27.487 50.376 1.00 57.55 ? 900 NDG A O 1 HETATM 2160 O O3 . NDG B 2 . ? -7.115 31.624 50.121 1.00 60.19 ? 900 NDG A O3 1 HETATM 2161 O O4 . NDG B 2 . ? -8.984 30.402 51.904 1.00 60.68 ? 900 NDG A O4 1 HETATM 2162 O O6 . NDG B 2 . ? -10.110 28.093 52.679 1.00 63.11 ? 900 NDG A O6 1 HETATM 2163 O O7 . NDG B 2 . ? -4.498 32.240 49.633 1.00 61.98 ? 900 NDG A O7 1 HETATM 2164 N N2 . NDG B 2 . ? -4.751 30.007 49.570 1.00 59.72 ? 900 NDG A N2 1 HETATM 2165 C C1 . NAG C 3 . ? 24.292 10.321 84.790 1.00 45.47 ? 901 NAG A C1 1 HETATM 2166 C C2 . NAG C 3 . ? 25.369 9.604 85.608 1.00 48.06 ? 901 NAG A C2 1 HETATM 2167 C C3 . NAG C 3 . ? 26.430 9.010 84.675 1.00 49.66 ? 901 NAG A C3 1 HETATM 2168 C C4 . NAG C 3 . ? 25.769 8.124 83.616 1.00 50.16 ? 901 NAG A C4 1 HETATM 2169 C C5 . NAG C 3 . ? 24.659 8.902 82.895 1.00 49.81 ? 901 NAG A C5 1 HETATM 2170 C C6 . NAG C 3 . ? 23.894 8.039 81.909 1.00 49.46 ? 901 NAG A C6 1 HETATM 2171 C C7 . NAG C 3 . ? 26.025 10.227 87.829 1.00 51.05 ? 901 NAG A C7 1 HETATM 2172 C C8 . NAG C 3 . ? 27.244 9.469 88.333 1.00 52.38 ? 901 NAG A C8 1 HETATM 2173 N N2 . NAG C 3 . ? 25.989 10.526 86.537 1.00 49.72 ? 901 NAG A N2 1 HETATM 2174 O O3 . NAG C 3 . ? 27.353 8.240 85.431 1.00 49.87 ? 901 NAG A O3 1 HETATM 2175 O O4 . NAG C 3 . ? 26.744 7.696 82.675 1.00 52.43 ? 901 NAG A O4 1 HETATM 2176 O O5 . NAG C 3 . ? 23.701 9.409 83.854 1.00 47.28 ? 901 NAG A O5 1 HETATM 2177 O O6 . NAG C 3 . ? 23.084 7.086 82.583 1.00 50.28 ? 901 NAG A O6 1 HETATM 2178 O O7 . NAG C 3 . ? 25.123 10.527 88.608 1.00 53.05 ? 901 NAG A O7 1 HETATM 2179 C C1 . EDO D 4 . ? 14.978 32.049 83.012 1.00 48.84 ? 2000 EDO A C1 1 HETATM 2180 O O1 . EDO D 4 . ? 14.572 30.687 83.241 1.00 48.76 ? 2000 EDO A O1 1 HETATM 2181 C C2 . EDO D 4 . ? 14.721 32.911 84.230 1.00 49.04 ? 2000 EDO A C2 1 HETATM 2182 O O2 . EDO D 4 . ? 15.725 32.704 85.243 1.00 49.63 ? 2000 EDO A O2 1 HETATM 2183 C C1 . EDO E 4 . ? 11.556 22.030 37.975 1.00 51.25 ? 2001 EDO A C1 1 HETATM 2184 O O1 . EDO E 4 . ? 12.883 21.749 37.493 1.00 51.96 ? 2001 EDO A O1 1 HETATM 2185 C C2 . EDO E 4 . ? 11.461 23.437 38.532 1.00 51.24 ? 2001 EDO A C2 1 HETATM 2186 O O2 . EDO E 4 . ? 10.144 23.725 39.036 1.00 48.44 ? 2001 EDO A O2 1 HETATM 2187 C C1 . EDO F 4 . ? -7.776 29.073 69.495 1.00 52.66 ? 2004 EDO A C1 1 HETATM 2188 O O1 . EDO F 4 . ? -6.967 27.976 69.958 1.00 52.17 ? 2004 EDO A O1 1 HETATM 2189 C C2 . EDO F 4 . ? -7.262 30.400 70.022 1.00 52.76 ? 2004 EDO A C2 1 HETATM 2190 O O2 . EDO F 4 . ? -7.580 30.576 71.417 1.00 52.20 ? 2004 EDO A O2 1 HETATM 2191 C C1 . EDO G 4 . ? 2.589 24.147 83.346 1.00 34.30 ? 2005 EDO A C1 1 HETATM 2192 O O1 . EDO G 4 . ? 2.094 23.260 84.368 1.00 36.42 ? 2005 EDO A O1 1 HETATM 2193 C C2 . EDO G 4 . ? 3.997 23.777 82.923 1.00 32.93 ? 2005 EDO A C2 1 HETATM 2194 O O2 . EDO G 4 . ? 4.023 22.519 82.222 1.00 29.31 ? 2005 EDO A O2 1 HETATM 2195 C C1 . EDO H 4 . ? 1.916 33.135 81.070 1.00 60.32 ? 2007 EDO A C1 1 HETATM 2196 O O1 . EDO H 4 . ? 2.108 32.790 79.687 1.00 61.05 ? 2007 EDO A O1 1 HETATM 2197 C C2 . EDO H 4 . ? 3.102 33.901 81.618 1.00 59.48 ? 2007 EDO A C2 1 HETATM 2198 O O2 . EDO H 4 . ? 3.160 33.814 83.054 1.00 60.11 ? 2007 EDO A O2 1 HETATM 2199 C C1 . EDO I 4 . ? 8.793 31.705 66.082 1.00 33.98 ? 2008 EDO A C1 1 HETATM 2200 O O1 . EDO I 4 . ? 7.444 31.284 65.809 1.00 36.70 ? 2008 EDO A O1 1 HETATM 2201 C C2 . EDO I 4 . ? 9.528 30.700 66.948 1.00 33.38 ? 2008 EDO A C2 1 HETATM 2202 O O2 . EDO I 4 . ? 8.881 30.521 68.219 1.00 25.23 ? 2008 EDO A O2 1 HETATM 2203 C C1 . EDO J 4 . ? -4.176 23.931 55.769 1.00 51.24 ? 2009 EDO A C1 1 HETATM 2204 O O1 . EDO J 4 . ? -4.117 25.014 54.822 1.00 51.74 ? 2009 EDO A O1 1 HETATM 2205 C C2 . EDO J 4 . ? -5.607 23.511 56.042 1.00 50.37 ? 2009 EDO A C2 1 HETATM 2206 O O2 . EDO J 4 . ? -6.375 24.597 56.592 1.00 50.43 ? 2009 EDO A O2 1 HETATM 2207 C C1 . EDO K 4 . ? 7.705 31.371 73.641 1.00 45.08 ? 2010 EDO A C1 1 HETATM 2208 O O1 . EDO K 4 . ? 7.065 31.847 72.438 1.00 45.56 ? 2010 EDO A O1 1 HETATM 2209 C C2 . EDO K 4 . ? 8.198 29.944 73.484 1.00 44.15 ? 2010 EDO A C2 1 HETATM 2210 O O2 . EDO K 4 . ? 9.574 29.902 73.059 1.00 44.14 ? 2010 EDO A O2 1 HETATM 2211 C C1 . EDO L 4 . ? 5.626 35.640 76.523 1.00 54.70 ? 2011 EDO A C1 1 HETATM 2212 O O1 . EDO L 4 . ? 5.797 34.581 75.561 1.00 54.51 ? 2011 EDO A O1 1 HETATM 2213 C C2 . EDO L 4 . ? 5.412 35.093 77.921 1.00 54.83 ? 2011 EDO A C2 1 HETATM 2214 O O2 . EDO L 4 . ? 4.228 34.277 77.995 1.00 55.32 ? 2011 EDO A O2 1 HETATM 2215 O O . HOH M 5 . ? 2.662 27.036 82.191 1.00 25.19 ? 501 HOH A O 1 HETATM 2216 O O . HOH M 5 . ? 8.308 11.480 45.454 1.00 54.08 ? 502 HOH A O 1 HETATM 2217 O O . HOH M 5 . ? -4.836 16.080 59.704 1.00 28.21 ? 503 HOH A O 1 HETATM 2218 O O . HOH M 5 . ? -5.371 25.331 63.501 1.00 26.92 ? 504 HOH A O 1 HETATM 2219 O O . HOH M 5 . ? -9.845 22.116 59.564 1.00 34.86 ? 505 HOH A O 1 HETATM 2220 O O . HOH M 5 . ? 13.838 24.357 86.617 1.00 61.95 ? 507 HOH A O 1 HETATM 2221 O O . HOH M 5 . ? -7.057 24.121 70.547 1.00 29.74 ? 508 HOH A O 1 HETATM 2222 O O . HOH M 5 . ? -8.153 5.800 63.836 1.00 48.07 ? 509 HOH A O 1 HETATM 2223 O O . HOH M 5 . ? 10.722 29.708 70.683 1.00 22.15 ? 510 HOH A O 1 HETATM 2224 O O . HOH M 5 . ? 9.215 16.926 88.810 1.00 28.72 ? 511 HOH A O 1 HETATM 2225 O O . HOH M 5 . ? 10.284 14.852 90.420 1.00 38.07 ? 512 HOH A O 1 HETATM 2226 O O . HOH M 5 . ? 5.980 19.189 88.734 1.00 27.03 ? 513 HOH A O 1 HETATM 2227 O O . HOH M 5 . ? 6.366 15.971 89.053 1.00 24.25 ? 514 HOH A O 1 HETATM 2228 O O . HOH M 5 . ? -2.012 16.039 78.292 1.00 22.21 ? 515 HOH A O 1 HETATM 2229 O O . HOH M 5 . ? -2.649 17.616 80.558 1.00 26.21 ? 516 HOH A O 1 HETATM 2230 O O . HOH M 5 . ? -0.958 14.885 88.066 1.00 18.99 ? 517 HOH A O 1 HETATM 2231 O O . HOH M 5 . ? -5.685 11.221 75.610 1.00 29.49 ? 518 HOH A O 1 HETATM 2232 O O . HOH M 5 . ? 2.771 8.843 74.739 1.00 21.93 ? 519 HOH A O 1 HETATM 2233 O O . HOH M 5 . ? 7.285 13.856 69.085 1.00 23.41 ? 520 HOH A O 1 HETATM 2234 O O . HOH M 5 . ? 6.535 15.034 66.618 1.00 30.89 ? 521 HOH A O 1 HETATM 2235 O O . HOH M 5 . ? 17.808 30.549 69.059 1.00 27.62 ? 522 HOH A O 1 HETATM 2236 O O . HOH M 5 . ? 13.716 33.666 76.467 1.00 21.78 ? 523 HOH A O 1 HETATM 2237 O O . HOH M 5 . ? -9.088 16.444 78.882 1.00 37.99 ? 524 HOH A O 1 HETATM 2238 O O . HOH M 5 . ? 13.336 26.222 85.405 1.00 31.56 ? 525 HOH A O 1 HETATM 2239 O O . HOH M 5 . ? 21.898 27.694 68.565 1.00 51.48 ? 526 HOH A O 1 HETATM 2240 O O . HOH M 5 . ? 19.687 23.191 77.279 1.00 18.00 ? 527 HOH A O 1 HETATM 2241 O O . HOH M 5 . ? 25.081 17.774 76.910 1.00 26.22 ? 528 HOH A O 1 HETATM 2242 O O . HOH M 5 . ? 17.530 7.650 81.972 1.00 31.39 ? 529 HOH A O 1 HETATM 2243 O O . HOH M 5 . ? 13.783 3.599 84.295 1.00 42.09 ? 530 HOH A O 1 HETATM 2244 O O . HOH M 5 . ? 22.392 20.343 63.794 1.00 25.55 ? 531 HOH A O 1 HETATM 2245 O O . HOH M 5 . ? 27.562 16.336 68.357 1.00 32.28 ? 532 HOH A O 1 HETATM 2246 O O . HOH M 5 . ? 27.967 14.085 67.065 1.00 36.46 ? 533 HOH A O 1 HETATM 2247 O O . HOH M 5 . ? 18.765 8.288 68.405 1.00 21.88 ? 534 HOH A O 1 HETATM 2248 O O . HOH M 5 . ? 18.580 25.571 57.502 1.00 20.31 ? 535 HOH A O 1 HETATM 2249 O O . HOH M 5 . ? 11.567 8.978 87.108 1.00 61.02 ? 536 HOH A O 1 HETATM 2250 O O . HOH M 5 . ? 19.219 24.860 60.194 1.00 23.97 ? 537 HOH A O 1 HETATM 2251 O O . HOH M 5 . ? 22.228 31.142 61.158 1.00 46.50 ? 538 HOH A O 1 HETATM 2252 O O . HOH M 5 . ? 24.925 19.763 49.271 1.00 36.63 ? 539 HOH A O 1 HETATM 2253 O O . HOH M 5 . ? 24.638 4.104 57.787 1.00 48.40 ? 540 HOH A O 1 HETATM 2254 O O . HOH M 5 . ? 26.557 7.867 64.357 1.00 53.14 ? 541 HOH A O 1 HETATM 2255 O O . HOH M 5 . ? 19.220 6.395 66.323 1.00 23.73 ? 542 HOH A O 1 HETATM 2256 O O . HOH M 5 . ? 9.170 25.258 51.882 1.00 19.87 ? 543 HOH A O 1 HETATM 2257 O O . HOH M 5 . ? 3.343 20.994 41.932 1.00 46.42 ? 545 HOH A O 1 HETATM 2258 O O . HOH M 5 . ? 3.702 19.459 39.999 1.00 48.69 ? 546 HOH A O 1 HETATM 2259 O O . HOH M 5 . ? 22.332 14.714 89.237 1.00 30.90 ? 547 HOH A O 1 HETATM 2260 O O . HOH M 5 . ? 24.861 9.595 75.171 1.00 41.00 ? 548 HOH A O 1 HETATM 2261 O O . HOH M 5 . ? -7.623 21.882 78.432 1.00 29.04 ? 549 HOH A O 1 HETATM 2262 O O . HOH M 5 . ? -13.651 24.505 77.367 1.00 57.21 ? 550 HOH A O 1 HETATM 2263 O O . HOH M 5 . ? 0.828 9.917 47.904 1.00 56.41 ? 551 HOH A O 1 HETATM 2264 O O . HOH M 5 . ? -1.186 12.397 53.731 1.00 47.66 ? 552 HOH A O 1 HETATM 2265 O O . HOH M 5 . ? 2.530 10.151 62.907 1.00 29.70 ? 553 HOH A O 1 HETATM 2266 O O . HOH M 5 . ? -1.429 9.833 61.887 1.00 28.18 ? 554 HOH A O 1 HETATM 2267 O O . HOH M 5 . ? 3.942 12.503 60.994 1.00 22.52 ? 555 HOH A O 1 HETATM 2268 O O . HOH M 5 . ? 11.321 26.484 63.306 1.00 26.90 ? 556 HOH A O 1 HETATM 2269 O O . HOH M 5 . ? 6.922 13.840 63.955 1.00 24.25 ? 557 HOH A O 1 HETATM 2270 O O . HOH M 5 . ? -10.881 27.127 71.404 1.00 54.35 ? 558 HOH A O 1 HETATM 2271 O O . HOH M 5 . ? -11.595 27.480 68.919 1.00 60.65 ? 559 HOH A O 1 HETATM 2272 O O . HOH M 5 . ? 10.786 31.327 75.811 1.00 22.78 ? 560 HOH A O 1 HETATM 2273 O O . HOH M 5 . ? 13.872 19.840 85.571 1.00 23.88 ? 561 HOH A O 1 HETATM 2274 O O . HOH M 5 . ? 6.825 29.534 85.776 1.00 43.88 ? 562 HOH A O 1 HETATM 2275 O O . HOH M 5 . ? -9.118 32.710 76.392 1.00 58.80 ? 563 HOH A O 1 HETATM 2276 O O . HOH M 5 . ? 0.190 29.653 76.981 1.00 33.62 ? 564 HOH A O 1 HETATM 2277 O O . HOH M 5 . ? 12.305 9.900 89.463 1.00 62.08 ? 565 HOH A O 1 HETATM 2278 O O . HOH M 5 . ? 2.972 7.608 77.332 1.00 26.34 ? 567 HOH A O 1 HETATM 2279 O O . HOH M 5 . ? -3.830 14.370 88.283 1.00 40.14 ? 569 HOH A O 1 HETATM 2280 O O . HOH M 5 . ? 1.743 20.669 85.533 1.00 24.18 ? 570 HOH A O 1 HETATM 2281 O O . HOH M 5 . ? 23.052 24.968 78.170 1.00 56.79 ? 571 HOH A O 1 HETATM 2282 O O . HOH M 5 . ? 11.905 5.948 71.556 1.00 26.14 ? 572 HOH A O 1 HETATM 2283 O O . HOH M 5 . ? 9.508 6.876 70.192 1.00 18.70 ? 573 HOH A O 1 HETATM 2284 O O . HOH M 5 . ? 6.801 4.352 68.626 1.00 45.93 ? 574 HOH A O 1 HETATM 2285 O O . HOH M 5 . ? 26.935 20.249 57.408 1.00 46.92 ? 575 HOH A O 1 HETATM 2286 O O . HOH M 5 . ? 27.514 10.555 58.735 1.00 34.16 ? 576 HOH A O 1 HETATM 2287 O O . HOH M 5 . ? 20.986 4.917 64.787 1.00 27.52 ? 577 HOH A O 1 HETATM 2288 O O . HOH M 5 . ? 16.986 19.852 45.698 1.00 58.72 ? 578 HOH A O 1 HETATM 2289 O O . HOH M 5 . ? 18.472 29.120 81.190 1.00 47.46 ? 580 HOH A O 1 HETATM 2290 O O . HOH M 5 . ? -2.654 13.163 55.705 1.00 44.42 ? 581 HOH A O 1 HETATM 2291 O O . HOH M 5 . ? 11.654 5.576 53.629 1.00 33.53 ? 582 HOH A O 1 HETATM 2292 O O . HOH M 5 . ? -0.128 34.636 69.363 1.00 28.35 ? 583 HOH A O 1 HETATM 2293 O O . HOH M 5 . ? -11.700 33.866 68.516 1.00 51.55 ? 584 HOH A O 1 HETATM 2294 O O . HOH M 5 . ? -6.904 35.918 71.752 1.00 60.28 ? 585 HOH A O 1 HETATM 2295 O O . HOH M 5 . ? -2.916 37.091 61.525 1.00 56.01 ? 586 HOH A O 1 HETATM 2296 O O . HOH M 5 . ? -3.322 22.851 53.208 1.00 41.21 ? 587 HOH A O 1 HETATM 2297 O O . HOH M 5 . ? 6.584 25.243 87.884 1.00 38.64 ? 588 HOH A O 1 HETATM 2298 O O . HOH M 5 . ? 7.205 32.199 77.699 1.00 32.02 ? 589 HOH A O 1 HETATM 2299 O O . HOH M 5 . ? 2.141 35.070 72.118 1.00 51.37 ? 590 HOH A O 1 HETATM 2300 O O . HOH M 5 . ? -15.246 19.359 76.620 1.00 59.66 ? 592 HOH A O 1 HETATM 2301 O O . HOH M 5 . ? -12.814 12.345 71.881 1.00 54.36 ? 593 HOH A O 1 HETATM 2302 O O . HOH M 5 . ? -10.080 9.729 71.806 1.00 56.33 ? 594 HOH A O 1 HETATM 2303 O O . HOH M 5 . ? 17.372 28.144 77.000 1.00 21.60 ? 595 HOH A O 1 HETATM 2304 O O . HOH M 5 . ? 24.716 14.803 86.713 1.00 33.70 ? 596 HOH A O 1 HETATM 2305 O O . HOH M 5 . ? 17.277 32.873 54.422 1.00 52.76 ? 597 HOH A O 1 HETATM 2306 O O . HOH M 5 . ? 3.011 22.559 87.339 1.00 35.26 ? 598 HOH A O 1 HETATM 2307 O O . HOH M 5 . ? 3.974 20.957 89.037 1.00 35.97 ? 599 HOH A O 1 HETATM 2308 O O . HOH M 5 . ? 5.189 18.327 93.067 1.00 45.64 ? 600 HOH A O 1 HETATM 2309 O O . HOH M 5 . ? 6.028 17.679 95.856 1.00 56.80 ? 601 HOH A O 1 HETATM 2310 O O . HOH M 5 . ? 24.066 23.903 63.088 1.00 58.36 ? 602 HOH A O 1 HETATM 2311 O O . HOH M 5 . ? 0.214 7.207 71.086 1.00 25.79 ? 603 HOH A O 1 HETATM 2312 O O . HOH M 5 . ? 17.040 19.831 69.114 1.00 26.64 ? 604 HOH A O 1 HETATM 2313 O O . HOH M 5 . ? 26.365 21.881 73.520 1.00 25.79 ? 605 HOH A O 1 HETATM 2314 O O . HOH M 5 . ? 22.440 16.555 76.417 1.00 23.40 ? 608 HOH A O 1 HETATM 2315 O O . HOH M 5 . ? 11.247 3.641 72.658 1.00 19.90 ? 609 HOH A O 1 HETATM 2316 O O . HOH M 5 . ? -4.170 8.094 67.619 1.00 52.74 ? 610 HOH A O 1 HETATM 2317 O O . HOH M 5 . ? 25.776 24.996 59.556 1.00 41.15 ? 611 HOH A O 1 HETATM 2318 O O . HOH M 5 . ? 30.833 17.481 58.639 1.00 58.28 ? 612 HOH A O 1 HETATM 2319 O O . HOH M 5 . ? 26.271 12.981 65.341 1.00 33.46 ? 613 HOH A O 1 HETATM 2320 O O . HOH M 5 . ? 28.898 21.846 70.292 1.00 41.30 ? 614 HOH A O 1 HETATM 2321 O O . HOH M 5 . ? 28.144 14.796 72.739 1.00 43.19 ? 615 HOH A O 1 HETATM 2322 O O . HOH M 5 . ? 25.192 11.207 68.498 1.00 34.52 ? 616 HOH A O 1 HETATM 2323 O O . HOH M 5 . ? 20.838 4.002 75.056 1.00 41.16 ? 617 HOH A O 1 HETATM 2324 O O . HOH M 5 . ? 17.918 0.557 82.112 1.00 45.50 ? 618 HOH A O 1 HETATM 2325 O O . HOH M 5 . ? 17.454 31.151 60.743 1.00 25.38 ? 619 HOH A O 1 HETATM 2326 O O . HOH M 5 . ? 19.801 31.206 61.896 1.00 29.36 ? 620 HOH A O 1 HETATM 2327 O O . HOH M 5 . ? 13.277 21.172 41.233 1.00 54.73 ? 621 HOH A O 1 HETATM 2328 O O . HOH M 5 . ? 16.281 23.094 47.323 1.00 34.81 ? 622 HOH A O 1 HETATM 2329 O O . HOH M 5 . ? 21.874 20.773 48.663 1.00 37.14 ? 623 HOH A O 1 HETATM 2330 O O . HOH M 5 . ? 27.371 18.893 55.188 1.00 50.77 ? 624 HOH A O 1 HETATM 2331 O O . HOH M 5 . ? 11.426 4.794 56.704 1.00 53.67 ? 625 HOH A O 1 HETATM 2332 O O . HOH M 5 . ? 9.255 32.694 58.423 1.00 32.96 ? 626 HOH A O 1 HETATM 2333 O O . HOH M 5 . ? 8.695 33.188 61.494 1.00 50.34 ? 627 HOH A O 1 HETATM 2334 O O . HOH M 5 . ? 14.789 23.596 44.766 1.00 39.82 ? 628 HOH A O 1 HETATM 2335 O O . HOH M 5 . ? 13.733 9.036 45.447 1.00 39.10 ? 629 HOH A O 1 HETATM 2336 O O . HOH M 5 . ? 22.170 14.685 47.061 1.00 41.72 ? 630 HOH A O 1 HETATM 2337 O O . HOH M 5 . ? 19.859 4.834 52.518 1.00 38.28 ? 631 HOH A O 1 HETATM 2338 O O . HOH M 5 . ? 18.036 2.631 58.059 1.00 33.94 ? 632 HOH A O 1 HETATM 2339 O O . HOH M 5 . ? 7.937 13.548 43.953 1.00 47.21 ? 634 HOH A O 1 HETATM 2340 O O . HOH M 5 . ? 6.537 3.496 54.896 1.00 62.59 ? 635 HOH A O 1 HETATM 2341 O O . HOH M 5 . ? -3.762 8.435 72.010 1.00 43.35 ? 636 HOH A O 1 HETATM 2342 O O . HOH M 5 . ? 6.157 9.799 88.539 1.00 46.79 ? 637 HOH A O 1 HETATM 2343 O O . HOH M 5 . ? -3.757 10.354 83.745 1.00 50.35 ? 638 HOH A O 1 HETATM 2344 O O . HOH M 5 . ? -3.628 8.355 86.294 1.00 61.76 ? 639 HOH A O 1 HETATM 2345 O O . HOH M 5 . ? 5.431 26.606 36.927 1.00 31.18 ? 640 HOH A O 1 HETATM 2346 O O . HOH M 5 . ? 2.169 28.286 41.440 1.00 46.91 ? 641 HOH A O 1 HETATM 2347 O O . HOH M 5 . ? 2.589 23.773 41.703 1.00 48.97 ? 642 HOH A O 1 HETATM 2348 O O . HOH M 5 . ? 19.299 2.968 46.801 1.00 56.77 ? 643 HOH A O 1 HETATM 2349 O O . HOH M 5 . ? 2.078 11.286 50.183 1.00 31.93 ? 644 HOH A O 1 HETATM 2350 O O . HOH M 5 . ? -15.080 24.248 68.646 1.00 63.64 ? 645 HOH A O 1 HETATM 2351 O O . HOH M 5 . ? -11.323 24.324 70.123 1.00 53.33 ? 646 HOH A O 1 HETATM 2352 O O . HOH M 5 . ? -12.460 21.787 63.134 1.00 49.93 ? 647 HOH A O 1 HETATM 2353 O O . HOH M 5 . ? -8.413 13.674 59.566 1.00 45.02 ? 648 HOH A O 1 HETATM 2354 O O . HOH M 5 . ? -0.248 8.002 60.036 1.00 48.65 ? 649 HOH A O 1 HETATM 2355 O O . HOH M 5 . ? 14.933 28.110 83.473 1.00 39.60 ? 650 HOH A O 1 HETATM 2356 O O . HOH M 5 . ? 3.068 6.789 87.463 1.00 35.01 ? 651 HOH A O 1 HETATM 2357 O O . HOH M 5 . ? 2.664 9.382 88.927 1.00 39.91 ? 652 HOH A O 1 HETATM 2358 O O . HOH M 5 . ? -10.026 16.447 82.564 1.00 45.12 ? 653 HOH A O 1 HETATM 2359 O O . HOH M 5 . ? 26.952 13.383 85.004 1.00 34.99 ? 654 HOH A O 1 HETATM 2360 O O . HOH M 5 . ? 26.286 17.594 83.986 1.00 34.47 ? 655 HOH A O 1 HETATM 2361 O O . HOH M 5 . ? 22.520 9.443 88.196 1.00 43.30 ? 656 HOH A O 1 HETATM 2362 O O . HOH M 5 . ? 0.861 5.227 91.256 1.00 56.38 ? 657 HOH A O 1 HETATM 2363 O O . HOH M 5 . ? 24.472 27.437 62.879 1.00 58.06 ? 658 HOH A O 1 HETATM 2364 O O . HOH M 5 . ? 22.967 24.626 60.716 1.00 29.30 ? 659 HOH A O 1 HETATM 2365 O O . HOH M 5 . ? 28.029 23.372 50.305 1.00 51.15 ? 660 HOH A O 1 HETATM 2366 O O . HOH M 5 . ? 27.822 13.968 52.038 1.00 51.71 ? 661 HOH A O 1 HETATM 2367 O O . HOH M 5 . ? 22.909 6.051 54.202 1.00 59.25 ? 662 HOH A O 1 HETATM 2368 O O . HOH M 5 . ? 7.723 8.238 61.063 1.00 33.36 ? 663 HOH A O 1 HETATM 2369 O O . HOH M 5 . ? 9.890 30.075 58.457 1.00 34.90 ? 664 HOH A O 1 HETATM 2370 O O . HOH M 5 . ? 8.167 39.482 51.040 1.00 57.51 ? 665 HOH A O 1 HETATM 2371 O O . HOH M 5 . ? 2.764 21.742 91.538 1.00 38.67 ? 666 HOH A O 1 HETATM 2372 O O . HOH M 5 . ? 13.931 34.479 54.816 1.00 39.48 ? 667 HOH A O 1 HETATM 2373 O O . HOH M 5 . ? 14.086 29.460 48.514 1.00 44.84 ? 668 HOH A O 1 HETATM 2374 O O . HOH M 5 . ? 19.659 11.566 49.293 1.00 49.87 ? 669 HOH A O 1 HETATM 2375 O O . HOH M 5 . ? 20.388 6.127 55.197 1.00 45.75 ? 670 HOH A O 1 HETATM 2376 O O . HOH M 5 . ? 21.141 4.599 57.128 1.00 42.58 ? 671 HOH A O 1 HETATM 2377 O O . HOH M 5 . ? 4.207 31.317 63.103 1.00 33.51 ? 672 HOH A O 1 HETATM 2378 O O . HOH M 5 . ? 6.990 31.299 63.083 1.00 34.08 ? 673 HOH A O 1 HETATM 2379 O O . HOH M 5 . ? 1.795 30.109 48.116 1.00 49.43 ? 674 HOH A O 1 HETATM 2380 O O . HOH M 5 . ? 0.272 34.070 50.650 1.00 54.66 ? 675 HOH A O 1 HETATM 2381 O O . HOH M 5 . ? -6.783 23.815 50.596 1.00 54.88 ? 676 HOH A O 1 HETATM 2382 O O . HOH M 5 . ? 10.582 9.053 45.652 1.00 49.25 ? 677 HOH A O 1 HETATM 2383 O O . HOH M 5 . ? 2.212 7.201 50.732 1.00 53.63 ? 678 HOH A O 1 HETATM 2384 O O . HOH M 5 . ? 7.886 7.519 58.375 1.00 34.01 ? 679 HOH A O 1 HETATM 2385 O O . HOH M 5 . ? -2.654 7.848 58.214 1.00 59.64 ? 680 HOH A O 1 HETATM 2386 O O . HOH M 5 . ? 2.660 34.872 68.529 1.00 51.90 ? 681 HOH A O 1 HETATM 2387 O O . HOH M 5 . ? 4.064 33.936 63.613 1.00 37.51 ? 682 HOH A O 1 HETATM 2388 O O . HOH M 5 . ? 4.916 33.182 71.023 1.00 44.46 ? 683 HOH A O 1 HETATM 2389 O O . HOH M 5 . ? -1.595 36.545 66.532 1.00 45.00 ? 684 HOH A O 1 HETATM 2390 O O . HOH M 5 . ? 2.301 27.475 65.367 1.00 23.77 ? 685 HOH A O 1 HETATM 2391 O O . HOH M 5 . ? -9.769 29.712 62.218 1.00 55.87 ? 686 HOH A O 1 HETATM 2392 O O . HOH M 5 . ? -9.836 29.758 67.025 1.00 47.28 ? 687 HOH A O 1 HETATM 2393 O O . HOH M 5 . ? -7.680 26.156 71.776 1.00 41.23 ? 688 HOH A O 1 HETATM 2394 O O . HOH M 5 . ? -13.033 15.296 72.780 1.00 44.33 ? 689 HOH A O 1 HETATM 2395 O O . HOH M 5 . ? -14.335 15.813 75.627 1.00 54.45 ? 690 HOH A O 1 HETATM 2396 O O . HOH M 5 . ? -13.390 10.547 75.870 1.00 58.94 ? 691 HOH A O 1 HETATM 2397 O O . HOH M 5 . ? -9.333 19.660 80.490 1.00 56.42 ? 692 HOH A O 1 HETATM 2398 O O . HOH M 5 . ? -10.722 20.750 77.172 1.00 37.31 ? 693 HOH A O 1 HETATM 2399 O O . HOH M 5 . ? 5.167 6.097 64.066 1.00 50.40 ? 694 HOH A O 1 HETATM 2400 O O . HOH M 5 . ? 7.292 21.115 90.051 1.00 43.18 ? 695 HOH A O 1 HETATM 2401 O O . HOH M 5 . ? -8.584 24.469 58.103 1.00 44.60 ? 696 HOH A O 1 HETATM 2402 O O . HOH M 5 . ? 25.960 17.598 48.075 1.00 52.75 ? 697 HOH A O 1 HETATM 2403 O O . HOH M 5 . ? -8.235 21.515 81.642 1.00 44.82 ? 698 HOH A O 1 HETATM 2404 O O . HOH M 5 . ? 2.983 4.931 77.925 1.00 32.50 ? 699 HOH A O 1 HETATM 2405 O O . HOH M 5 . ? 27.335 23.450 57.578 1.00 51.27 ? 700 HOH A O 1 HETATM 2406 O O . HOH M 5 . ? 29.647 11.492 62.711 1.00 56.23 ? 701 HOH A O 1 HETATM 2407 O O . HOH M 5 . ? 28.421 7.111 59.244 1.00 60.51 ? 702 HOH A O 1 HETATM 2408 O O . HOH M 5 . ? 0.593 6.805 68.321 1.00 30.13 ? 703 HOH A O 1 HETATM 2409 O O . HOH M 5 . ? 26.927 8.925 68.259 1.00 56.96 ? 704 HOH A O 1 HETATM 2410 O O . HOH M 5 . ? 22.896 22.781 47.364 1.00 32.40 ? 705 HOH A O 1 HETATM 2411 O O . HOH M 5 . ? -1.673 15.714 43.300 1.00 47.34 ? 706 HOH A O 1 HETATM 2412 O O . HOH M 5 . ? 1.168 3.619 82.645 1.00 53.58 ? 707 HOH A O 1 HETATM 2413 O O . HOH M 5 . ? 26.373 27.341 58.563 1.00 42.49 ? 708 HOH A O 1 HETATM 2414 O O . HOH M 5 . ? 3.326 3.174 80.520 1.00 44.70 ? 709 HOH A O 1 HETATM 2415 O O . HOH M 5 . ? 12.543 30.451 56.883 1.00 43.47 ? 710 HOH A O 1 HETATM 2416 O O . HOH M 5 . ? 3.685 22.205 33.736 1.00 60.63 ? 711 HOH A O 1 HETATM 2417 O O . HOH M 5 . ? 21.115 13.617 49.775 1.00 44.96 ? 712 HOH A O 1 HETATM 2418 O O . HOH M 5 . ? 0.383 28.022 81.533 1.00 56.28 ? 713 HOH A O 1 HETATM 2419 O O . HOH M 5 . ? 16.958 26.642 83.009 1.00 33.07 ? 714 HOH A O 1 HETATM 2420 O O . HOH M 5 . ? -2.165 30.449 76.328 1.00 40.26 ? 715 HOH A O 1 HETATM 2421 O O . HOH M 5 . ? 23.477 23.496 80.390 1.00 43.78 ? 716 HOH A O 1 HETATM 2422 O O . HOH M 5 . ? 22.846 26.375 80.418 1.00 38.80 ? 717 HOH A O 1 HETATM 2423 O O . HOH M 5 . ? 12.970 12.355 89.984 1.00 54.17 ? 718 HOH A O 1 HETATM 2424 O O . HOH M 5 . ? -2.402 9.702 92.907 1.00 41.78 ? 719 HOH A O 1 HETATM 2425 O O . HOH M 5 . ? -3.383 11.914 91.890 1.00 54.38 ? 720 HOH A O 1 HETATM 2426 O O . HOH M 5 . ? 20.044 21.565 66.722 1.00 25.88 ? 721 HOH A O 1 HETATM 2427 O O . HOH M 5 . ? 21.627 25.275 67.577 1.00 56.19 ? 722 HOH A O 1 HETATM 2428 O O . HOH M 5 . ? 0.046 37.056 73.162 1.00 56.91 ? 723 HOH A O 1 HETATM 2429 O O . HOH M 5 . ? 16.114 19.293 89.446 1.00 40.14 ? 724 HOH A O 1 HETATM 2430 O O . HOH M 5 . ? 18.222 19.681 90.687 1.00 48.91 ? 725 HOH A O 1 HETATM 2431 O O . HOH M 5 . ? 20.721 19.199 89.926 1.00 42.80 ? 726 HOH A O 1 HETATM 2432 O O . HOH M 5 . ? 5.831 4.370 49.017 1.00 53.58 ? 727 HOH A O 1 HETATM 2433 O O . HOH M 5 . ? 7.267 6.229 46.445 1.00 46.08 ? 728 HOH A O 1 HETATM 2434 O O . HOH M 5 . ? 8.956 4.125 53.474 1.00 52.95 ? 729 HOH A O 1 HETATM 2435 O O . HOH M 5 . ? 5.395 33.097 66.445 1.00 43.67 ? 730 HOH A O 1 HETATM 2436 O O . HOH M 5 . ? -7.613 35.181 69.185 1.00 61.17 ? 731 HOH A O 1 HETATM 2437 O O . HOH M 5 . ? -10.126 27.374 65.173 1.00 45.85 ? 732 HOH A O 1 HETATM 2438 O O . HOH M 5 . ? -13.115 8.966 62.770 1.00 63.50 ? 733 HOH A O 1 HETATM 2439 O O . HOH M 5 . ? -14.224 9.671 65.167 1.00 62.57 ? 734 HOH A O 1 HETATM 2440 O O . HOH M 5 . ? 26.927 28.633 79.406 1.00 52.63 ? 735 HOH A O 1 HETATM 2441 O O . HOH M 5 . ? 29.882 22.911 80.341 1.00 61.69 ? 736 HOH A O 1 HETATM 2442 O O . HOH M 5 . ? 21.459 7.477 79.557 1.00 58.20 ? 737 HOH A O 1 HETATM 2443 O O . HOH M 5 . ? 26.385 20.441 53.251 1.00 40.15 ? 738 HOH A O 1 HETATM 2444 O O . HOH M 5 . ? 22.793 21.315 66.233 1.00 39.41 ? 739 HOH A O 1 HETATM 2445 O O . HOH M 5 . ? 23.664 30.063 52.090 1.00 41.55 ? 740 HOH A O 1 HETATM 2446 O O . HOH M 5 . ? 24.737 15.071 47.802 1.00 51.73 ? 741 HOH A O 1 HETATM 2447 O O . HOH M 5 . ? -4.013 12.088 57.705 1.00 49.68 ? 742 HOH A O 1 HETATM 2448 O O . HOH M 5 . ? -12.209 19.560 55.733 1.00 59.60 ? 743 HOH A O 1 HETATM 2449 O O . HOH M 5 . ? 20.528 31.301 51.473 1.00 36.59 ? 744 HOH A O 1 HETATM 2450 O O . HOH M 5 . ? 21.401 32.859 54.317 1.00 48.33 ? 745 HOH A O 1 HETATM 2451 O O . HOH M 5 . ? -5.635 8.122 76.906 1.00 51.50 ? 746 HOH A O 1 HETATM 2452 O O . HOH M 5 . ? -7.590 10.140 76.784 1.00 51.46 ? 748 HOH A O 1 HETATM 2453 O O . HOH M 5 . ? -12.831 16.241 77.713 1.00 50.07 ? 749 HOH A O 1 HETATM 2454 O O . HOH M 5 . ? 21.991 32.366 77.895 1.00 54.44 ? 750 HOH A O 1 HETATM 2455 O O . HOH M 5 . ? 20.303 30.072 79.433 1.00 52.86 ? 751 HOH A O 1 HETATM 2456 O O . HOH M 5 . ? -0.067 22.416 40.626 1.00 57.30 ? 752 HOH A O 1 HETATM 2457 O O . HOH M 5 . ? 3.495 21.253 37.916 1.00 56.76 ? 753 HOH A O 1 HETATM 2458 O O . HOH M 5 . ? 28.117 30.716 50.390 1.00 63.62 ? 754 HOH A O 1 HETATM 2459 O O . HOH M 5 . ? 2.134 27.105 48.722 1.00 51.10 ? 755 HOH A O 1 HETATM 2460 O O . HOH M 5 . ? -3.591 5.156 83.660 1.00 58.41 ? 756 HOH A O 1 HETATM 2461 O O . HOH M 5 . ? 26.045 22.286 64.093 1.00 51.49 ? 757 HOH A O 1 HETATM 2462 O O . HOH M 5 . ? 0.027 37.195 63.203 1.00 49.92 ? 758 HOH A O 1 HETATM 2463 O O . HOH M 5 . ? 28.304 9.880 55.595 1.00 51.09 ? 759 HOH A O 1 HETATM 2464 O O . HOH M 5 . ? 23.070 8.884 53.868 1.00 38.98 ? 760 HOH A O 1 HETATM 2465 O O . HOH M 5 . ? 20.949 2.136 54.714 1.00 55.29 ? 761 HOH A O 1 HETATM 2466 O O . HOH M 5 . ? -4.615 35.681 74.474 1.00 49.59 ? 763 HOH A O 1 HETATM 2467 O O . HOH M 5 . ? -4.685 4.903 77.346 1.00 47.56 ? 764 HOH A O 1 HETATM 2468 O O . HOH M 5 . ? -2.345 5.582 71.318 1.00 51.25 ? 765 HOH A O 1 HETATM 2469 O O . HOH M 5 . ? 9.005 5.056 57.612 1.00 42.88 ? 766 HOH A O 1 HETATM 2470 O O . HOH M 5 . ? 0.808 29.514 79.468 1.00 49.98 ? 768 HOH A O 1 HETATM 2471 O O . HOH M 5 . ? 1.828 25.115 87.154 1.00 48.69 ? 769 HOH A O 1 HETATM 2472 O O . HOH M 5 . ? -6.616 16.444 49.426 1.00 49.00 ? 770 HOH A O 1 HETATM 2473 O O . HOH M 5 . ? 5.551 24.426 90.326 1.00 49.86 ? 771 HOH A O 1 HETATM 2474 O O . HOH M 5 . ? 2.987 30.576 45.223 1.00 45.19 ? 772 HOH A O 1 HETATM 2475 O O . HOH M 5 . ? -10.932 18.398 78.838 1.00 43.68 ? 773 HOH A O 1 HETATM 2476 O O . HOH M 5 . ? 7.643 6.464 62.907 1.00 44.70 ? 774 HOH A O 1 HETATM 2477 O O . HOH M 5 . ? 16.566 34.190 79.909 1.00 25.04 ? 775 HOH A O 1 HETATM 2478 O O . HOH M 5 . ? 27.959 12.496 70.153 1.00 52.31 ? 776 HOH A O 1 HETATM 2479 O O . HOH M 5 . ? 30.121 13.735 65.375 1.00 50.60 ? 777 HOH A O 1 HETATM 2480 O O . HOH M 5 . ? 6.442 16.548 91.635 1.00 46.82 ? 778 HOH A O 1 HETATM 2481 O O . HOH M 5 . ? 5.899 5.559 57.794 1.00 47.02 ? 779 HOH A O 1 HETATM 2482 O O . HOH M 5 . ? 11.068 2.418 57.522 1.00 51.08 ? 780 HOH A O 1 HETATM 2483 O O . HOH M 5 . ? 19.622 18.460 55.913 1.00 42.91 ? 781 HOH A O 1 HETATM 2484 O O . HOH M 5 . ? 25.800 9.375 50.775 1.00 52.99 ? 782 HOH A O 1 HETATM 2485 O O . HOH M 5 . ? 3.477 33.634 54.477 1.00 40.69 ? 783 HOH A O 1 HETATM 2486 O O . HOH M 5 . ? 3.103 35.975 56.468 1.00 55.01 ? 784 HOH A O 1 HETATM 2487 O O . HOH M 5 . ? 9.750 33.050 48.880 1.00 39.54 ? 785 HOH A O 1 HETATM 2488 O O . HOH M 5 . ? 11.727 13.493 40.076 1.00 53.25 ? 786 HOH A O 1 HETATM 2489 O O . HOH M 5 . ? 15.642 1.906 57.336 1.00 51.13 ? 787 HOH A O 1 HETATM 2490 O O . HOH M 5 . ? -6.488 27.279 55.033 1.00 47.37 ? 788 HOH A O 1 HETATM 2491 O O . HOH M 5 . ? -0.084 25.460 82.327 1.00 46.69 ? 789 HOH A O 1 HETATM 2492 O O . HOH M 5 . ? 28.575 15.414 77.944 1.00 48.61 ? 790 HOH A O 1 HETATM 2493 O O . HOH M 5 . ? 29.720 16.046 70.260 1.00 52.52 ? 791 HOH A O 1 HETATM 2494 O O . HOH M 5 . ? -2.178 11.843 51.445 1.00 48.87 ? 792 HOH A O 1 HETATM 2495 O O . HOH M 5 . ? -4.873 8.462 59.594 1.00 51.90 ? 793 HOH A O 1 HETATM 2496 O O . HOH M 5 . ? 24.304 32.229 58.533 1.00 42.91 ? 794 HOH A O 1 HETATM 2497 O O . HOH M 5 . ? 21.964 35.106 58.193 1.00 46.23 ? 795 HOH A O 1 HETATM 2498 O O . HOH M 5 . ? 3.255 10.128 91.819 1.00 44.91 ? 796 HOH A O 1 HETATM 2499 O O . HOH M 5 . ? 5.725 35.995 56.419 1.00 36.73 ? 798 HOH A O 1 HETATM 2500 O O . HOH M 5 . ? 9.943 35.102 55.862 1.00 52.41 ? 799 HOH A O 1 HETATM 2501 O O . HOH M 5 . ? -0.198 -2.291 74.793 1.00 51.11 ? 800 HOH A O 1 HETATM 2502 O O . HOH M 5 . ? -8.327 26.967 56.776 1.00 46.68 ? 801 HOH A O 1 HETATM 2503 O O . HOH M 5 . ? -5.440 31.234 53.032 1.00 47.46 ? 802 HOH A O 1 HETATM 2504 O O . HOH M 5 . ? -12.044 24.553 67.195 1.00 41.81 ? 803 HOH A O 1 HETATM 2505 O O . HOH M 5 . ? 12.138 28.663 74.044 1.00 18.83 ? 804 HOH A O 1 HETATM 2506 O O . HOH M 5 . ? 17.119 26.287 86.814 1.00 48.47 ? 805 HOH A O 1 HETATM 2507 O O . HOH M 5 . ? 2.299 32.101 77.100 1.00 43.98 ? 806 HOH A O 1 HETATM 2508 O O . HOH M 5 . ? -6.989 33.270 72.201 1.00 45.47 ? 807 HOH A O 1 HETATM 2509 O O . HOH M 5 . ? -14.630 13.862 69.133 1.00 43.94 ? 808 HOH A O 1 HETATM 2510 O O . HOH M 5 . ? 2.063 14.897 95.016 1.00 41.94 ? 809 HOH A O 1 HETATM 2511 O O . HOH M 5 . ? 11.635 25.226 53.317 1.00 16.89 ? 810 HOH A O 1 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ALA 1 1 1 ALA ALA A . n A 1 2 GLY 2 2 2 GLY GLY A . n A 1 3 GLY 3 3 3 GLY GLY A . n A 1 4 LYS 4 4 4 LYS LYS A . n A 1 5 THR 5 5 5 THR THR A . n A 1 6 GLY 6 6 6 GLY GLY A . n A 1 7 GLN 7 7 7 GLN GLN A . n A 1 8 VAL 8 8 8 VAL VAL A . n A 1 9 THR 9 9 9 THR THR A . n A 1 10 VAL 10 10 10 VAL VAL A . n A 1 11 PHE 11 11 11 PHE PHE A . n A 1 12 TRP 12 12 12 TRP TRP A . n A 1 13 GLY 13 13 13 GLY GLY A . n A 1 14 ARG 14 14 14 ARG ARG A . n A 1 15 ASN 15 15 15 ASN ASN A . n A 1 16 LYS 16 16 16 LYS LYS A . n A 1 17 ALA 17 17 17 ALA ALA A . n A 1 18 GLU 18 18 18 GLU GLU A . n A 1 19 GLY 19 19 19 GLY GLY A . n A 1 20 SER 20 20 20 SER SER A . n A 1 21 LEU 21 21 21 LEU LEU A . n A 1 22 ARG 22 22 22 ARG ARG A . n A 1 23 GLU 23 23 23 GLU GLU A . n A 1 24 ALA 24 24 24 ALA ALA A . n A 1 25 CYS 25 25 25 CYS CYS A . n A 1 26 ASP 26 26 26 ASP ASP A . n A 1 27 SER 27 27 27 SER SER A . n A 1 28 GLY 28 28 28 GLY GLY A . n A 1 29 MET 29 29 29 MET MET A . n A 1 30 TYR 30 30 30 TYR TYR A . n A 1 31 THR 31 31 31 THR THR A . n A 1 32 MET 32 32 32 MET MET A . n A 1 33 VAL 33 33 33 VAL VAL A . n A 1 34 THR 34 34 34 THR THR A . n A 1 35 MET 35 35 35 MET MET A . n A 1 36 SER 36 36 36 SER SER A . n A 1 37 PHE 37 37 37 PHE PHE A . n A 1 38 LEU 38 38 38 LEU LEU A . n A 1 39 ASP 39 39 39 ASP ASP A . n A 1 40 VAL 40 40 40 VAL VAL A . n A 1 41 PHE 41 41 41 PHE PHE A . n A 1 42 GLY 42 42 42 GLY GLY A . n A 1 43 ALA 43 43 43 ALA ALA A . n A 1 44 ASN 44 44 44 ASN GLY A . n A 1 45 GLY 45 45 45 GLY GLY A . n A 1 46 LYS 46 46 46 LYS LYS A . n A 1 47 TYR 47 47 47 TYR TYR A . n A 1 48 HIS 48 48 48 HIS HIS A . n A 1 49 LEU 49 49 49 LEU LEU A . n A 1 50 ASP 50 50 50 ASP ASP A . n A 1 51 LEU 51 51 51 LEU LEU A . n A 1 52 SER 52 52 52 SER SER A . n A 1 53 GLY 53 53 53 GLY GLY A . n A 1 54 HIS 54 54 54 HIS HIS A . n A 1 55 ASP 55 55 55 ASP ASP A . n A 1 56 LEU 56 56 56 LEU LEU A . n A 1 57 SER 57 57 57 SER SER A . n A 1 58 SER 58 58 58 SER SER A . n A 1 59 VAL 59 59 59 VAL VAL A . n A 1 60 GLY 60 60 60 GLY GLY A . n A 1 61 ALA 61 61 61 ALA ALA A . n A 1 62 ASP 62 62 62 ASP ASP A . n A 1 63 ILE 63 63 63 ILE ILE A . n A 1 64 LYS 64 64 64 LYS LYS A . n A 1 65 HIS 65 65 65 HIS HIS A . n A 1 66 CYS 66 66 66 CYS CYS A . n A 1 67 GLN 67 67 67 GLN GLN A . n A 1 68 SER 68 68 68 SER SER A . n A 1 69 LYS 69 69 69 LYS LYS A . n A 1 70 GLY 70 70 70 GLY GLY A . n A 1 71 VAL 71 71 71 VAL VAL A . n A 1 72 PRO 72 72 72 PRO PRO A . n A 1 73 VAL 73 73 73 VAL VAL A . n A 1 74 SER 74 74 74 SER SER A . n A 1 75 LEU 75 75 75 LEU LEU A . n A 1 76 SER 76 76 76 SER SER A . n A 1 77 ILE 77 77 77 ILE ILE A . n A 1 78 GLY 78 78 78 GLY GLY A . n A 1 79 GLY 79 79 79 GLY GLY A . n A 1 80 TYR 80 80 80 TYR TYR A . n A 1 81 GLY 81 81 81 GLY GLY A . n A 1 82 THR 82 82 82 THR THR A . n A 1 83 GLY 83 83 83 GLY GLY A . n A 1 84 TYR 84 84 84 TYR TYR A . n A 1 85 SER 85 85 85 SER SER A . n A 1 86 LEU 86 86 86 LEU LEU A . n A 1 87 PRO 87 87 87 PRO PRO A . n A 1 88 SER 88 88 88 SER SER A . n A 1 89 ASN 89 89 89 ASN ASN A . n A 1 90 ARG 90 90 90 ARG ARG A . n A 1 91 SER 91 91 91 SER SER A . n A 1 92 ALA 92 92 92 ALA ALA A . n A 1 93 LEU 93 93 93 LEU LEU A . n A 1 94 ASP 94 94 94 ASP ASP A . n A 1 95 LEU 95 95 95 LEU LEU A . n A 1 96 PHE 96 96 96 PHE PHE A . n A 1 97 ASP 97 97 97 ASP ASP A . n A 1 98 HIS 98 98 98 HIS HIS A . n A 1 99 LEU 99 99 99 LEU LEU A . n A 1 100 TRP 100 100 100 TRP TRP A . n A 1 101 ASN 101 101 101 ASN ASN A . n A 1 102 SER 102 102 102 SER SER A . n A 1 103 TYR 103 103 103 TYR TYR A . n A 1 104 PHE 104 104 104 PHE PHE A . n A 1 105 GLY 105 105 105 GLY GLY A . n A 1 106 GLY 106 106 106 GLY GLY A . n A 1 107 SER 107 107 107 SER SER A . n A 1 108 LYS 108 108 108 LYS LYS A . n A 1 109 PRO 109 109 109 PRO PRO A . n A 1 110 SER 110 110 110 SER SER A . n A 1 111 VAL 111 111 111 VAL VAL A . n A 1 112 PRO 112 112 112 PRO PRO A . n A 1 113 ARG 113 113 113 ARG ARG A . n A 1 114 PRO 114 114 114 PRO PRO A . n A 1 115 PHE 115 115 115 PHE PHE A . n A 1 116 GLY 116 116 116 GLY GLY A . n A 1 117 ASP 117 117 117 ASP ASP A . n A 1 118 ALA 118 118 118 ALA ALA A . n A 1 119 TRP 119 119 119 TRP TRP A . n A 1 120 LEU 120 120 120 LEU LEU A . n A 1 121 ASP 121 121 121 ASP ASP A . n A 1 122 GLY 122 122 122 GLY GLY A . n A 1 123 VAL 123 123 123 VAL VAL A . n A 1 124 ASP 124 124 124 ASP ASP A . n A 1 125 LEU 125 125 125 LEU LEU A . n A 1 126 PHE 126 126 126 PHE PHE A . n A 1 127 LEU 127 127 127 LEU LEU A . n A 1 128 GLU 128 128 128 GLU GLU A . n A 1 129 HIS 129 129 129 HIS HIS A . n A 1 130 GLY 130 130 130 GLY GLY A . n A 1 131 THR 131 131 131 THR THR A . n A 1 132 PRO 132 132 132 PRO PRO A . n A 1 133 ALA 133 133 133 ALA ALA A . n A 1 134 ASP 134 134 134 ASP ASP A . n A 1 135 ARG 135 135 135 ARG ARG A . n A 1 136 TYR 136 136 136 TYR TYR A . n A 1 137 ASP 137 137 137 ASP ASP A . n A 1 138 VAL 138 138 138 VAL VAL A . n A 1 139 LEU 139 139 139 LEU LEU A . n A 1 140 ALA 140 140 140 ALA ALA A . n A 1 141 LEU 141 141 141 LEU LEU A . n A 1 142 GLU 142 142 142 GLU GLU A . n A 1 143 LEU 143 143 143 LEU LEU A . n A 1 144 ALA 144 144 144 ALA ALA A . n A 1 145 LYS 145 145 145 LYS LYS A . n A 1 146 HIS 146 146 146 HIS HIS A . n A 1 147 ASN 147 147 147 ASN ASN A . n A 1 148 ILE 148 148 148 ILE ILE A . n A 1 149 ARG 149 149 149 ARG ARG A . n A 1 150 GLY 150 150 150 GLY GLY A . n A 1 151 GLY 151 151 151 GLY GLY A . n A 1 152 PRO 152 152 152 PRO PRO A . n A 1 153 GLY 153 153 153 GLY GLY A . n A 1 154 LYS 154 154 154 LYS LYS A . n A 1 155 PRO 155 155 155 PRO PRO A . n A 1 156 LEU 156 156 156 LEU LEU A . n A 1 157 HIS 157 157 157 HIS HIS A . n A 1 158 LEU 158 158 158 LEU LEU A . n A 1 159 THR 159 159 159 THR THR A . n A 1 160 ALA 160 160 160 ALA ALA A . n A 1 161 THR 161 161 161 THR THR A . n A 1 162 VAL 162 162 162 VAL VAL A . n A 1 163 ARG 163 163 163 ARG ARG A . n A 1 164 CYS 164 164 164 CYS CYS A . n A 1 165 GLY 165 165 165 GLY GLY A . n A 1 166 TYR 166 166 166 TYR TYR A . n A 1 167 PRO 167 167 167 PRO PRO A . n A 1 168 PRO 168 168 168 PRO PRO A . n A 1 169 ALA 169 169 169 ALA ALA A . n A 1 170 ALA 170 170 170 ALA ALA A . n A 1 171 HIS 171 171 171 HIS HIS A . n A 1 172 VAL 172 172 172 VAL VAL A . n A 1 173 GLY 173 173 173 GLY GLY A . n A 1 174 ARG 174 174 174 ARG ARG A . n A 1 175 ALA 175 175 175 ALA ALA A . n A 1 176 LEU 176 176 176 LEU LEU A . n A 1 177 ALA 177 177 177 ALA ALA A . n A 1 178 THR 178 178 178 THR THR A . n A 1 179 GLY 179 179 179 GLY GLY A . n A 1 180 ILE 180 180 180 ILE ILE A . n A 1 181 PHE 181 181 181 PHE PHE A . n A 1 182 GLU 182 182 182 GLU GLU A . n A 1 183 ARG 183 183 183 ARG ARG A . n A 1 184 VAL 184 184 184 VAL VAL A . n A 1 185 HIS 185 185 185 HIS HIS A . n A 1 186 VAL 186 186 186 VAL VAL A . n A 1 187 ARG 187 187 187 ARG ARG A . n A 1 188 THR 188 188 188 THR THR A . n A 1 189 TYR 189 189 189 TYR TYR A . n A 1 190 GLU 190 190 190 GLU GLU A . n A 1 191 SER 191 191 191 SER SER A . n A 1 192 ASP 192 192 192 ASP ASP A . n A 1 193 LYS 193 193 193 LYS LYS A . n A 1 194 TRP 194 194 194 TRP TRP A . n A 1 195 CYS 195 195 195 CYS CYS A . n A 1 196 ASN 196 196 196 ASN ASN A . n A 1 197 GLN 197 197 197 GLN GLN A . n A 1 198 ASN 198 198 198 ASN ASN A . n A 1 199 LEU 199 199 199 LEU LEU A . n A 1 200 GLY 200 200 200 GLY GLY A . n A 1 201 TRP 201 201 201 TRP TRP A . n A 1 202 GLU 202 202 202 GLU GLU A . n A 1 203 GLY 203 203 203 GLY GLY A . n A 1 204 SER 204 204 204 SER SER A . n A 1 205 TRP 205 205 205 TRP TRP A . n A 1 206 ASP 206 206 206 ASP ASP A . n A 1 207 LYS 207 207 207 LYS LYS A . n A 1 208 TRP 208 208 208 TRP TRP A . n A 1 209 THR 209 209 209 THR THR A . n A 1 210 ALA 210 210 210 ALA ALA A . n A 1 211 ALA 211 211 211 ALA ALA A . n A 1 212 TYR 212 212 212 TYR TYR A . n A 1 213 PRO 213 213 213 PRO PRO A . n A 1 214 ALA 214 214 214 ALA ALA A . n A 1 215 THR 215 215 215 THR THR A . n A 1 216 ARG 216 216 216 ARG ARG A . n A 1 217 PHE 217 217 217 PHE PHE A . n A 1 218 TYR 218 218 218 TYR TYR A . n A 1 219 VAL 219 219 219 VAL VAL A . n A 1 220 GLY 220 220 220 GLY GLY A . n A 1 221 LEU 221 221 221 LEU LEU A . n A 1 222 THR 222 222 222 THR THR A . n A 1 223 ALA 223 223 223 ALA ALA A . n A 1 224 ASP 224 224 224 ASP ASP A . n A 1 225 ASP 225 225 225 ASP ASP A . n A 1 226 LYS 226 226 226 LYS LYS A . n A 1 227 SER 227 227 227 SER SER A . n A 1 228 HIS 228 228 228 HIS HIS A . n A 1 229 GLN 229 229 229 GLN GLN A . n A 1 230 TRP 230 230 230 TRP TRP A . n A 1 231 VAL 231 231 231 VAL VAL A . n A 1 232 HIS 232 232 232 HIS HIS A . n A 1 233 PRO 233 233 233 PRO PRO A . n A 1 234 LYS 234 234 234 LYS LYS A . n A 1 235 ASN 235 235 235 ASN ASN A . n A 1 236 VAL 236 236 236 VAL VAL A . n A 1 237 TYR 237 237 237 TYR TYR A . n A 1 238 TYR 238 238 238 TYR TYR A . n A 1 239 GLY 239 239 239 GLY GLY A . n A 1 240 VAL 240 240 240 VAL VAL A . n A 1 241 ALA 241 241 241 ALA ALA A . n A 1 242 PRO 242 242 242 PRO PRO A . n A 1 243 VAL 243 243 243 VAL VAL A . n A 1 244 ALA 244 244 244 ALA ALA A . n A 1 245 GLN 245 245 245 GLN GLN A . n A 1 246 LYS 246 246 246 LYS LYS A . n A 1 247 LYS 247 247 247 LYS LYS A . n A 1 248 ASP 248 248 248 ASP ASP A . n A 1 249 ASN 249 249 249 ASN ASN A . n A 1 250 TYR 250 250 250 TYR TYR A . n A 1 251 GLY 251 251 251 GLY GLY A . n A 1 252 GLY 252 252 252 GLY GLY A . n A 1 253 ILE 253 253 253 ILE ILE A . n A 1 254 MET 254 254 254 MET MET A . n A 1 255 LEU 255 255 255 LEU LEU A . n A 1 256 TRP 256 256 256 TRP TRP A . n A 1 257 ASP 257 257 257 ASP ASP A . n A 1 258 ARG 258 258 258 ARG ARG A . n A 1 259 TYR 259 259 259 TYR TYR A . n A 1 260 PHE 260 260 260 PHE PHE A . n A 1 261 ASP 261 261 261 ASP ASP A . n A 1 262 LYS 262 262 262 LYS LYS A . n A 1 263 GLN 263 263 263 GLN GLN A . n A 1 264 THR 264 264 264 THR THR A . n A 1 265 ASN 265 265 265 ASN ASN A . n A 1 266 TYR 266 266 266 TYR TYR A . n A 1 267 SER 267 267 267 SER SER A . n A 1 268 SER 268 268 268 SER SER A . n A 1 269 LEU 269 269 269 LEU LEU A . n A 1 270 ILE 270 270 270 ILE ILE A . n A 1 271 LYS 271 271 271 LYS LYS A . n A 1 272 TYR 272 272 272 TYR TYR A . n A 1 273 TYR 273 273 273 TYR TYR A . n A 1 274 ALA 274 274 274 ALA ALA 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 NDG 1 900 900 NDG NAG A . C 3 NAG 1 901 901 NAG NAG A . D 4 EDO 1 2000 2000 EDO EGL A . E 4 EDO 1 2001 2001 EDO EGL A . F 4 EDO 1 2004 2004 EDO EGL A . G 4 EDO 1 2005 2005 EDO EGL A . H 4 EDO 1 2007 2007 EDO EGL A . I 4 EDO 1 2008 2008 EDO EGL A . J 4 EDO 1 2009 2009 EDO EGL A . K 4 EDO 1 2010 2010 EDO EGL A . L 4 EDO 1 2011 2011 EDO EGL A . M 5 HOH 1 501 501 HOH WAT A . M 5 HOH 2 502 502 HOH WAT A . M 5 HOH 3 503 503 HOH WAT A . M 5 HOH 4 504 504 HOH WAT A . M 5 HOH 5 505 505 HOH WAT A . M 5 HOH 6 507 507 HOH WAT A . M 5 HOH 7 508 508 HOH WAT A . M 5 HOH 8 509 509 HOH WAT A . M 5 HOH 9 510 510 HOH WAT A . M 5 HOH 10 511 511 HOH WAT A . M 5 HOH 11 512 512 HOH WAT A . M 5 HOH 12 513 513 HOH WAT A . M 5 HOH 13 514 514 HOH WAT A . M 5 HOH 14 515 515 HOH WAT A . M 5 HOH 15 516 516 HOH WAT A . M 5 HOH 16 517 517 HOH WAT A . M 5 HOH 17 518 518 HOH WAT A . M 5 HOH 18 519 519 HOH WAT A . M 5 HOH 19 520 520 HOH WAT A . M 5 HOH 20 521 521 HOH WAT A . M 5 HOH 21 522 522 HOH WAT A . M 5 HOH 22 523 523 HOH WAT A . M 5 HOH 23 524 524 HOH WAT A . M 5 HOH 24 525 525 HOH WAT A . M 5 HOH 25 526 526 HOH WAT A . M 5 HOH 26 527 527 HOH WAT A . M 5 HOH 27 528 528 HOH WAT A . M 5 HOH 28 529 529 HOH WAT A . M 5 HOH 29 530 530 HOH WAT A . M 5 HOH 30 531 531 HOH WAT A . M 5 HOH 31 532 532 HOH WAT A . M 5 HOH 32 533 533 HOH WAT A . M 5 HOH 33 534 534 HOH WAT A . M 5 HOH 34 535 535 HOH WAT A . M 5 HOH 35 536 536 HOH WAT A . M 5 HOH 36 537 537 HOH WAT A . M 5 HOH 37 538 538 HOH WAT A . M 5 HOH 38 539 539 HOH WAT A . M 5 HOH 39 540 540 HOH WAT A . M 5 HOH 40 541 541 HOH WAT A . M 5 HOH 41 542 542 HOH WAT A . M 5 HOH 42 543 543 HOH WAT A . M 5 HOH 43 545 545 HOH WAT A . M 5 HOH 44 546 546 HOH WAT A . M 5 HOH 45 547 547 HOH WAT A . M 5 HOH 46 548 548 HOH WAT A . M 5 HOH 47 549 549 HOH WAT A . M 5 HOH 48 550 550 HOH WAT A . M 5 HOH 49 551 551 HOH WAT A . M 5 HOH 50 552 552 HOH WAT A . M 5 HOH 51 553 553 HOH WAT A . M 5 HOH 52 554 554 HOH WAT A . M 5 HOH 53 555 555 HOH WAT A . M 5 HOH 54 556 556 HOH WAT A . M 5 HOH 55 557 557 HOH WAT A . M 5 HOH 56 558 558 HOH WAT A . M 5 HOH 57 559 559 HOH WAT A . M 5 HOH 58 560 560 HOH WAT A . M 5 HOH 59 561 561 HOH WAT A . M 5 HOH 60 562 562 HOH WAT A . M 5 HOH 61 563 563 HOH WAT A . M 5 HOH 62 564 564 HOH WAT A . M 5 HOH 63 565 565 HOH WAT A . M 5 HOH 64 567 567 HOH WAT A . M 5 HOH 65 569 569 HOH WAT A . M 5 HOH 66 570 570 HOH WAT A . M 5 HOH 67 571 571 HOH WAT A . M 5 HOH 68 572 572 HOH WAT A . M 5 HOH 69 573 573 HOH WAT A . M 5 HOH 70 574 574 HOH WAT A . M 5 HOH 71 575 575 HOH WAT A . M 5 HOH 72 576 576 HOH WAT A . M 5 HOH 73 577 577 HOH WAT A . M 5 HOH 74 578 578 HOH WAT A . M 5 HOH 75 580 580 HOH WAT A . M 5 HOH 76 581 581 HOH WAT A . M 5 HOH 77 582 582 HOH WAT A . M 5 HOH 78 583 583 HOH WAT A . M 5 HOH 79 584 584 HOH WAT A . M 5 HOH 80 585 585 HOH WAT A . M 5 HOH 81 586 586 HOH WAT A . M 5 HOH 82 587 587 HOH WAT A . M 5 HOH 83 588 588 HOH WAT A . M 5 HOH 84 589 589 HOH WAT A . M 5 HOH 85 590 590 HOH WAT A . M 5 HOH 86 592 592 HOH WAT A . M 5 HOH 87 593 593 HOH WAT A . M 5 HOH 88 594 594 HOH WAT A . M 5 HOH 89 595 595 HOH WAT A . M 5 HOH 90 596 596 HOH WAT A . M 5 HOH 91 597 597 HOH WAT A . M 5 HOH 92 598 598 HOH WAT A . M 5 HOH 93 599 599 HOH WAT A . M 5 HOH 94 600 600 HOH WAT A . M 5 HOH 95 601 601 HOH WAT A . M 5 HOH 96 602 602 HOH WAT A . M 5 HOH 97 603 603 HOH WAT A . M 5 HOH 98 604 604 HOH WAT A . M 5 HOH 99 605 605 HOH WAT A . M 5 HOH 100 608 608 HOH WAT A . M 5 HOH 101 609 609 HOH WAT A . M 5 HOH 102 610 610 HOH WAT A . M 5 HOH 103 611 611 HOH WAT A . M 5 HOH 104 612 612 HOH WAT A . M 5 HOH 105 613 613 HOH WAT A . M 5 HOH 106 614 614 HOH WAT A . M 5 HOH 107 615 615 HOH WAT A . M 5 HOH 108 616 616 HOH WAT A . M 5 HOH 109 617 617 HOH WAT A . M 5 HOH 110 618 618 HOH WAT A . M 5 HOH 111 619 619 HOH WAT A . M 5 HOH 112 620 620 HOH WAT A . M 5 HOH 113 621 621 HOH WAT A . M 5 HOH 114 622 622 HOH WAT A . M 5 HOH 115 623 623 HOH WAT A . M 5 HOH 116 624 624 HOH WAT A . M 5 HOH 117 625 625 HOH WAT A . M 5 HOH 118 626 626 HOH WAT A . M 5 HOH 119 627 627 HOH WAT A . M 5 HOH 120 628 628 HOH WAT A . M 5 HOH 121 629 629 HOH WAT A . M 5 HOH 122 630 630 HOH WAT A . M 5 HOH 123 631 631 HOH WAT A . M 5 HOH 124 632 632 HOH WAT A . M 5 HOH 125 634 634 HOH WAT A . M 5 HOH 126 635 635 HOH WAT A . M 5 HOH 127 636 636 HOH WAT A . M 5 HOH 128 637 637 HOH WAT A . M 5 HOH 129 638 638 HOH WAT A . M 5 HOH 130 639 639 HOH WAT A . M 5 HOH 131 640 640 HOH WAT A . M 5 HOH 132 641 641 HOH WAT A . M 5 HOH 133 642 642 HOH WAT A . M 5 HOH 134 643 643 HOH WAT A . M 5 HOH 135 644 644 HOH WAT A . M 5 HOH 136 645 645 HOH WAT A . M 5 HOH 137 646 646 HOH WAT A . M 5 HOH 138 647 647 HOH WAT A . M 5 HOH 139 648 648 HOH WAT A . M 5 HOH 140 649 649 HOH WAT A . M 5 HOH 141 650 650 HOH WAT A . M 5 HOH 142 651 651 HOH WAT A . M 5 HOH 143 652 652 HOH WAT A . M 5 HOH 144 653 653 HOH WAT A . M 5 HOH 145 654 654 HOH WAT A . M 5 HOH 146 655 655 HOH WAT A . M 5 HOH 147 656 656 HOH WAT A . M 5 HOH 148 657 657 HOH WAT A . M 5 HOH 149 658 658 HOH WAT A . M 5 HOH 150 659 659 HOH WAT A . M 5 HOH 151 660 660 HOH WAT A . M 5 HOH 152 661 661 HOH WAT A . M 5 HOH 153 662 662 HOH WAT A . M 5 HOH 154 663 663 HOH WAT A . M 5 HOH 155 664 664 HOH WAT A . M 5 HOH 156 665 665 HOH WAT A . M 5 HOH 157 666 666 HOH WAT A . M 5 HOH 158 667 667 HOH WAT A . M 5 HOH 159 668 668 HOH WAT A . M 5 HOH 160 669 669 HOH WAT A . M 5 HOH 161 670 670 HOH WAT A . M 5 HOH 162 671 671 HOH WAT A . M 5 HOH 163 672 672 HOH WAT A . M 5 HOH 164 673 673 HOH WAT A . M 5 HOH 165 674 674 HOH WAT A . M 5 HOH 166 675 675 HOH WAT A . M 5 HOH 167 676 676 HOH WAT A . M 5 HOH 168 677 677 HOH WAT A . M 5 HOH 169 678 678 HOH WAT A . M 5 HOH 170 679 679 HOH WAT A . M 5 HOH 171 680 680 HOH WAT A . M 5 HOH 172 681 681 HOH WAT A . M 5 HOH 173 682 682 HOH WAT A . M 5 HOH 174 683 683 HOH WAT A . M 5 HOH 175 684 684 HOH WAT A . M 5 HOH 176 685 685 HOH WAT A . M 5 HOH 177 686 686 HOH WAT A . M 5 HOH 178 687 687 HOH WAT A . M 5 HOH 179 688 688 HOH WAT A . M 5 HOH 180 689 689 HOH WAT A . M 5 HOH 181 690 690 HOH WAT A . M 5 HOH 182 691 691 HOH WAT A . M 5 HOH 183 692 692 HOH WAT A . M 5 HOH 184 693 693 HOH WAT A . M 5 HOH 185 694 694 HOH WAT A . M 5 HOH 186 695 695 HOH WAT A . M 5 HOH 187 696 696 HOH WAT A . M 5 HOH 188 697 697 HOH WAT A . M 5 HOH 189 698 698 HOH WAT A . M 5 HOH 190 699 699 HOH WAT A . M 5 HOH 191 700 700 HOH WAT A . M 5 HOH 192 701 701 HOH WAT A . M 5 HOH 193 702 702 HOH WAT A . M 5 HOH 194 703 703 HOH WAT A . M 5 HOH 195 704 704 HOH WAT A . M 5 HOH 196 705 705 HOH WAT A . M 5 HOH 197 706 706 HOH WAT A . M 5 HOH 198 707 707 HOH WAT A . M 5 HOH 199 708 708 HOH WAT A . M 5 HOH 200 709 709 HOH WAT A . M 5 HOH 201 710 710 HOH WAT A . M 5 HOH 202 711 711 HOH WAT A . M 5 HOH 203 712 712 HOH WAT A . M 5 HOH 204 713 713 HOH WAT A . M 5 HOH 205 714 714 HOH WAT A . M 5 HOH 206 715 715 HOH WAT A . M 5 HOH 207 716 716 HOH WAT A . M 5 HOH 208 717 717 HOH WAT A . M 5 HOH 209 718 718 HOH WAT A . M 5 HOH 210 719 719 HOH WAT A . M 5 HOH 211 720 720 HOH WAT A . M 5 HOH 212 721 721 HOH WAT A . M 5 HOH 213 722 722 HOH WAT A . M 5 HOH 214 723 723 HOH WAT A . M 5 HOH 215 724 724 HOH WAT A . M 5 HOH 216 725 725 HOH WAT A . M 5 HOH 217 726 726 HOH WAT A . M 5 HOH 218 727 727 HOH WAT A . M 5 HOH 219 728 728 HOH WAT A . M 5 HOH 220 729 729 HOH WAT A . M 5 HOH 221 730 730 HOH WAT A . M 5 HOH 222 731 731 HOH WAT A . M 5 HOH 223 732 732 HOH WAT A . M 5 HOH 224 733 733 HOH WAT A . M 5 HOH 225 734 734 HOH WAT A . M 5 HOH 226 735 735 HOH WAT A . M 5 HOH 227 736 736 HOH WAT A . M 5 HOH 228 737 737 HOH WAT A . M 5 HOH 229 738 738 HOH WAT A . M 5 HOH 230 739 739 HOH WAT A . M 5 HOH 231 740 740 HOH WAT A . M 5 HOH 232 741 741 HOH WAT A . M 5 HOH 233 742 742 HOH WAT A . M 5 HOH 234 743 743 HOH WAT A . M 5 HOH 235 744 744 HOH WAT A . M 5 HOH 236 745 745 HOH WAT A . M 5 HOH 237 746 746 HOH WAT A . M 5 HOH 238 748 748 HOH WAT A . M 5 HOH 239 749 749 HOH WAT A . M 5 HOH 240 750 750 HOH WAT A . M 5 HOH 241 751 751 HOH WAT A . M 5 HOH 242 752 752 HOH WAT A . M 5 HOH 243 753 753 HOH WAT A . M 5 HOH 244 754 754 HOH WAT A . M 5 HOH 245 755 755 HOH WAT A . M 5 HOH 246 756 756 HOH WAT A . M 5 HOH 247 757 757 HOH WAT A . M 5 HOH 248 758 758 HOH WAT A . M 5 HOH 249 759 759 HOH WAT A . M 5 HOH 250 760 760 HOH WAT A . M 5 HOH 251 761 761 HOH WAT A . M 5 HOH 252 763 763 HOH WAT A . M 5 HOH 253 764 764 HOH WAT A . M 5 HOH 254 765 765 HOH WAT A . M 5 HOH 255 766 766 HOH WAT A . M 5 HOH 256 768 768 HOH WAT A . M 5 HOH 257 769 769 HOH WAT A . M 5 HOH 258 770 770 HOH WAT A . M 5 HOH 259 771 771 HOH WAT A . M 5 HOH 260 772 772 HOH WAT A . M 5 HOH 261 773 773 HOH WAT A . M 5 HOH 262 774 774 HOH WAT A . M 5 HOH 263 775 775 HOH WAT A . M 5 HOH 264 776 776 HOH WAT A . M 5 HOH 265 777 777 HOH WAT A . M 5 HOH 266 778 778 HOH WAT A . M 5 HOH 267 779 779 HOH WAT A . M 5 HOH 268 780 780 HOH WAT A . M 5 HOH 269 781 781 HOH WAT A . M 5 HOH 270 782 782 HOH WAT A . M 5 HOH 271 783 783 HOH WAT A . M 5 HOH 272 784 784 HOH WAT A . M 5 HOH 273 785 785 HOH WAT A . M 5 HOH 274 786 786 HOH WAT A . M 5 HOH 275 787 787 HOH WAT A . M 5 HOH 276 788 788 HOH WAT A . M 5 HOH 277 789 789 HOH WAT A . M 5 HOH 278 790 790 HOH WAT A . M 5 HOH 279 791 791 HOH WAT A . M 5 HOH 280 792 792 HOH WAT A . M 5 HOH 281 793 793 HOH WAT A . M 5 HOH 282 794 794 HOH WAT A . M 5 HOH 283 795 795 HOH WAT A . M 5 HOH 284 796 796 HOH WAT A . M 5 HOH 285 798 798 HOH WAT A . M 5 HOH 286 799 799 HOH WAT A . M 5 HOH 287 800 800 HOH WAT A . M 5 HOH 288 801 801 HOH WAT A . M 5 HOH 289 802 802 HOH WAT A . M 5 HOH 290 803 803 HOH WAT A . M 5 HOH 291 804 804 HOH WAT A . M 5 HOH 292 805 805 HOH WAT A . M 5 HOH 293 806 806 HOH WAT A . M 5 HOH 294 807 807 HOH WAT A . M 5 HOH 295 808 808 HOH WAT A . M 5 HOH 296 809 809 HOH WAT A . M 5 HOH 297 810 810 HOH WAT 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 265 A ASN 265 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 89 A ASN 89 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_defined_assembly _pdbx_struct_assembly.method_details ? _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2003-06-03 2 'Structure model' 1 1 2008-04-29 3 'Structure model' 1 2 2011-07-13 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Version format compliance' 2 3 'Structure model' 'Non-polymer description' 3 3 'Structure model' 'Version format compliance' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal CNS refinement 1.1 ? 1 DENZO 'data reduction' . ? 2 SCALEPACK 'data scaling' . ? 3 AMoRE phasing . ? 4 # _pdbx_validate_rmsd_angle.id 1 _pdbx_validate_rmsd_angle.PDB_model_num 1 _pdbx_validate_rmsd_angle.auth_atom_id_1 N _pdbx_validate_rmsd_angle.auth_asym_id_1 A _pdbx_validate_rmsd_angle.auth_comp_id_1 LEU _pdbx_validate_rmsd_angle.auth_seq_id_1 38 _pdbx_validate_rmsd_angle.PDB_ins_code_1 ? _pdbx_validate_rmsd_angle.label_alt_id_1 ? _pdbx_validate_rmsd_angle.auth_atom_id_2 CA _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 38 _pdbx_validate_rmsd_angle.PDB_ins_code_2 ? _pdbx_validate_rmsd_angle.label_alt_id_2 ? _pdbx_validate_rmsd_angle.auth_atom_id_3 C _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 38 _pdbx_validate_rmsd_angle.PDB_ins_code_3 ? _pdbx_validate_rmsd_angle.label_alt_id_3 ? _pdbx_validate_rmsd_angle.angle_value 93.41 _pdbx_validate_rmsd_angle.angle_target_value 111.00 _pdbx_validate_rmsd_angle.angle_deviation -17.59 _pdbx_validate_rmsd_angle.angle_standard_deviation 2.70 _pdbx_validate_rmsd_angle.linker_flag N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 MET A 32 ? ? -171.29 135.05 2 1 LEU A 86 ? ? -151.41 64.29 3 1 PRO A 87 ? ? -67.75 13.18 4 1 PHE A 104 ? ? -114.42 -134.52 5 1 PHE A 126 ? ? -112.26 77.18 6 1 PRO A 152 ? ? -67.02 93.00 7 1 ASP A 192 ? ? -28.38 111.87 8 1 TRP A 194 ? ? 82.03 -12.92 9 1 ASP A 225 ? ? -67.95 1.19 # 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 ASN 44 ? CB ? A ASN 44 CB 2 1 Y 1 A ASN 44 ? CG ? A ASN 44 CG 3 1 Y 1 A ASN 44 ? OD1 ? A ASN 44 OD1 4 1 Y 1 A ASN 44 ? ND2 ? A ASN 44 ND2 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' NDG 3 N-ACETYL-D-GLUCOSAMINE NAG 4 1,2-ETHANEDIOL EDO 5 water HOH #