data_3CA5 # _entry.id 3CA5 # _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 3CA5 RCSB RCSB046532 WWPDB D_1000046532 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 3C9Z 'Sambucus nigra agglutinin II - tetragonal crystal form' unspecified PDB 3CA0 'Sambucus nigra agglutinin II - hexagonal crystal form' unspecified PDB 3CA1 'Sambucus nigra agglutinin II - tetragonal crystal form - complexed to galactose' unspecified PDB 3CA3 'Sambucus nigra agglutinin II - tetragonal crystal form - complexed to N-acetygalactosamine' unspecified PDB 3CA4 'Sambucus nigra agglutinin II - tetragonal crystal form - complexed to lactose' unspecified PDB 3CA6 'Sambucus nigra agglutinin II - tetragonal crystal form - complexed to Tn antigen' unspecified PDB 3CAH 'Sambucus nigra agglutinin II - tetragonal crystal form - fucose' unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 3CA5 _pdbx_database_status.recvd_initial_deposition_date 2008-02-19 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_cs ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Maveyraud, L.' 1 'Mourey, L.' 2 # _citation.id primary _citation.title 'Structural basis for sugar recognition, including the Tn carcinoma antigen, by the lectin SNA-II from Sambucus nigra' _citation.journal_abbrev Proteins _citation.journal_volume 75 _citation.page_first 89 _citation.page_last 103 _citation.year 2009 _citation.journal_id_ASTM PSFGEY _citation.country US _citation.journal_id_ISSN 0887-3585 _citation.journal_id_CSD 0867 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 18798567 _citation.pdbx_database_id_DOI 10.1002/prot.22222 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Maveyraud, L.' 1 primary 'Niwa, H.' 2 primary 'Guillet, V.' 3 primary 'Svergun, D.I.' 4 primary 'Konarev, P.V.' 5 primary 'Palmer, R.A.' 6 primary 'Peumans, W.J.' 7 primary 'Rouge, P.' 8 primary 'Van Damme, E.J.' 9 primary 'Reynolds, C.D.' 10 primary 'Mourey, L.' 11 # _cell.entry_id 3CA5 _cell.length_a 126.124 _cell.length_b 126.124 _cell.length_c 76.039 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 16 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 3CA5 _symmetry.space_group_name_H-M 'I 41 2 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 98 _symmetry.space_group_name_Hall ? # 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 'Agglutinin II' 28439.059 1 ? ? ? ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 7 ? ? ? ? 3 non-polymer man ALPHA-L-FUCOSE 164.156 2 ? ? ? ? 4 non-polymer man ALPHA-METHYL-D-GALACTOSIDE 194.182 2 ? ? ? ? 5 non-polymer syn 'SULFATE ION' 96.063 5 ? ? ? ? 6 non-polymer syn 'ACETATE ION' 59.044 1 ? ? ? ? 7 water nat water 18.015 341 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name SNA-II # _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 ;TSFTRNIVGRDGLCVDVRNGYDTDGTPLQLWPCGTQRNQRWTFDSDDTIRSMGKCMTANGLNNGSNIVIFNCSTAAENAI KWEVPIDGSIINPSSGLVMTAPRAASRTILLLEDNIYAASQGWTVTNNVKPIVASIVGYKEMCLQSNGENNGVWMEDCEA TSLQQQWALYGDRTIRVNSTRGLCVTTNGYNSKDLIIILKCQGLPSQRWFFNSDGAIVNPKSRLVMDVRASNVSLREIII FPATGNPNQQWVTQVLPS ; _entity_poly.pdbx_seq_one_letter_code_can ;TSFTRNIVGRDGLCVDVRNGYDTDGTPLQLWPCGTQRNQRWTFDSDDTIRSMGKCMTANGLNNGSNIVIFNCSTAAENAI KWEVPIDGSIINPSSGLVMTAPRAASRTILLLEDNIYAASQGWTVTNNVKPIVASIVGYKEMCLQSNGENNGVWMEDCEA TSLQQQWALYGDRTIRVNSTRGLCVTTNGYNSKDLIIILKCQGLPSQRWFFNSDGAIVNPKSRLVMDVRASNVSLREIII FPATGNPNQQWVTQVLPS ; _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 THR n 1 2 SER n 1 3 PHE n 1 4 THR n 1 5 ARG n 1 6 ASN n 1 7 ILE n 1 8 VAL n 1 9 GLY n 1 10 ARG n 1 11 ASP n 1 12 GLY n 1 13 LEU n 1 14 CYS n 1 15 VAL n 1 16 ASP n 1 17 VAL n 1 18 ARG n 1 19 ASN n 1 20 GLY n 1 21 TYR n 1 22 ASP n 1 23 THR n 1 24 ASP n 1 25 GLY n 1 26 THR n 1 27 PRO n 1 28 LEU n 1 29 GLN n 1 30 LEU n 1 31 TRP n 1 32 PRO n 1 33 CYS n 1 34 GLY n 1 35 THR n 1 36 GLN n 1 37 ARG n 1 38 ASN n 1 39 GLN n 1 40 ARG n 1 41 TRP n 1 42 THR n 1 43 PHE n 1 44 ASP n 1 45 SER n 1 46 ASP n 1 47 ASP n 1 48 THR n 1 49 ILE n 1 50 ARG n 1 51 SER n 1 52 MET n 1 53 GLY n 1 54 LYS n 1 55 CYS n 1 56 MET n 1 57 THR n 1 58 ALA n 1 59 ASN n 1 60 GLY n 1 61 LEU n 1 62 ASN n 1 63 ASN n 1 64 GLY n 1 65 SER n 1 66 ASN n 1 67 ILE n 1 68 VAL n 1 69 ILE n 1 70 PHE n 1 71 ASN n 1 72 CYS n 1 73 SER n 1 74 THR n 1 75 ALA n 1 76 ALA n 1 77 GLU n 1 78 ASN n 1 79 ALA n 1 80 ILE n 1 81 LYS n 1 82 TRP n 1 83 GLU n 1 84 VAL n 1 85 PRO n 1 86 ILE n 1 87 ASP n 1 88 GLY n 1 89 SER n 1 90 ILE n 1 91 ILE n 1 92 ASN n 1 93 PRO n 1 94 SER n 1 95 SER n 1 96 GLY n 1 97 LEU n 1 98 VAL n 1 99 MET n 1 100 THR n 1 101 ALA n 1 102 PRO n 1 103 ARG n 1 104 ALA n 1 105 ALA n 1 106 SER n 1 107 ARG n 1 108 THR n 1 109 ILE n 1 110 LEU n 1 111 LEU n 1 112 LEU n 1 113 GLU n 1 114 ASP n 1 115 ASN n 1 116 ILE n 1 117 TYR n 1 118 ALA n 1 119 ALA n 1 120 SER n 1 121 GLN n 1 122 GLY n 1 123 TRP n 1 124 THR n 1 125 VAL n 1 126 THR n 1 127 ASN n 1 128 ASN n 1 129 VAL n 1 130 LYS n 1 131 PRO n 1 132 ILE n 1 133 VAL n 1 134 ALA n 1 135 SER n 1 136 ILE n 1 137 VAL n 1 138 GLY n 1 139 TYR n 1 140 LYS n 1 141 GLU n 1 142 MET n 1 143 CYS n 1 144 LEU n 1 145 GLN n 1 146 SER n 1 147 ASN n 1 148 GLY n 1 149 GLU n 1 150 ASN n 1 151 ASN n 1 152 GLY n 1 153 VAL n 1 154 TRP n 1 155 MET n 1 156 GLU n 1 157 ASP n 1 158 CYS n 1 159 GLU n 1 160 ALA n 1 161 THR n 1 162 SER n 1 163 LEU n 1 164 GLN n 1 165 GLN n 1 166 GLN n 1 167 TRP n 1 168 ALA n 1 169 LEU n 1 170 TYR n 1 171 GLY n 1 172 ASP n 1 173 ARG n 1 174 THR n 1 175 ILE n 1 176 ARG n 1 177 VAL n 1 178 ASN n 1 179 SER n 1 180 THR n 1 181 ARG n 1 182 GLY n 1 183 LEU n 1 184 CYS n 1 185 VAL n 1 186 THR n 1 187 THR n 1 188 ASN n 1 189 GLY n 1 190 TYR n 1 191 ASN n 1 192 SER n 1 193 LYS n 1 194 ASP n 1 195 LEU n 1 196 ILE n 1 197 ILE n 1 198 ILE n 1 199 LEU n 1 200 LYS n 1 201 CYS n 1 202 GLN n 1 203 GLY n 1 204 LEU n 1 205 PRO n 1 206 SER n 1 207 GLN n 1 208 ARG n 1 209 TRP n 1 210 PHE n 1 211 PHE n 1 212 ASN n 1 213 SER n 1 214 ASP n 1 215 GLY n 1 216 ALA n 1 217 ILE n 1 218 VAL n 1 219 ASN n 1 220 PRO n 1 221 LYS n 1 222 SER n 1 223 ARG n 1 224 LEU n 1 225 VAL n 1 226 MET n 1 227 ASP n 1 228 VAL n 1 229 ARG n 1 230 ALA n 1 231 SER n 1 232 ASN n 1 233 VAL n 1 234 SER n 1 235 LEU n 1 236 ARG n 1 237 GLU n 1 238 ILE n 1 239 ILE n 1 240 ILE n 1 241 PHE n 1 242 PRO n 1 243 ALA n 1 244 THR n 1 245 GLY n 1 246 ASN n 1 247 PRO n 1 248 ASN n 1 249 GLN n 1 250 GLN n 1 251 TRP n 1 252 VAL n 1 253 THR n 1 254 GLN n 1 255 VAL n 1 256 LEU n 1 257 PRO n 1 258 SER 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 'European elder, elderberry' _entity_src_nat.pdbx_organism_scientific 'Sambucus nigra' _entity_src_nat.pdbx_ncbi_taxonomy_id ? _entity_src_nat.genus ? _entity_src_nat.species ? _entity_src_nat.strain ? _entity_src_nat.tissue BARK _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 NIGB_SAMNI _struct_ref.pdbx_db_accession P33183 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;TSFTRNIVGRDGLCVDVRNGYDTDGTPLQLWPCGTQRNQRWTFDSDDTIRSMGKCMTANGLNNGSNIVIFNCSTAAENAI KWEVPIDGSIINPSSGLVMTAPRAASRTILLLEDNIYAASQGWTVTNNVKPIVASIVGYKEMCLQSNGENNGVWMEDCEA TSLQQQWALYGDRTIRVNSTRGLCVTTNGYNSKDLIIILKCQGLPSQRWFFNSDGAIVNPKSRHVMDVRASNVSLREIII FPATGNPNQQWVTQVLPS ; _struct_ref.pdbx_align_begin 306 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 3CA5 _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 258 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession P33183 _struct_ref_seq.db_align_beg 306 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 563 _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 258 # _struct_ref_seq_dif.align_id 1 _struct_ref_seq_dif.pdbx_pdb_id_code 3CA5 _struct_ref_seq_dif.mon_id LEU _struct_ref_seq_dif.pdbx_pdb_strand_id A _struct_ref_seq_dif.seq_num 224 _struct_ref_seq_dif.pdbx_pdb_ins_code ? _struct_ref_seq_dif.pdbx_seq_db_name UNP _struct_ref_seq_dif.pdbx_seq_db_accession_code P33183 _struct_ref_seq_dif.db_mon_id HIS _struct_ref_seq_dif.pdbx_seq_db_seq_num 529 _struct_ref_seq_dif.details 'SEE REMARK 999' _struct_ref_seq_dif.pdbx_auth_seq_num 224 _struct_ref_seq_dif.pdbx_ordinal 1 # 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 ACT non-polymer . 'ACETATE ION' ? 'C2 H3 O2 -1' 59.044 ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 AMG non-polymer . ALPHA-METHYL-D-GALACTOSIDE ? 'C7 H14 O6' 194.182 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 FUC saccharide . ALPHA-L-FUCOSE ? 'C6 H12 O5' 164.156 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 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 SO4 non-polymer . 'SULFATE ION' ? 'O4 S -2' 96.063 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 3CA5 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number ? # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.67 _exptl_crystal.density_percent_sol 53.87 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 293 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 4.5 _exptl_crystal_grow.pdbx_details 'PROTEIN 16 MG/ML, AMMONIUM SULFATE 2.0 M, SODIUM ACETATE 100 mM, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K' _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 'MAR CCD 165 mm' _diffrn_detector.pdbx_collection_date 2003-09-26 _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 'Si(111)' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.9795 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'ESRF BEAMLINE BM30A' _diffrn_source.pdbx_synchrotron_site ESRF _diffrn_source.pdbx_synchrotron_beamline BM30A _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 0.9795 # _reflns.entry_id 3CA5 _reflns.observed_criterion_sigma_F 0 _reflns.observed_criterion_sigma_I 0 _reflns.d_resolution_high 1.55 _reflns.d_resolution_low 37.78 _reflns.number_all 42458 _reflns.number_obs 42458 _reflns.percent_possible_obs 96.9 _reflns.pdbx_Rmerge_I_obs 0.058 _reflns.pdbx_Rsym_value 0.058 _reflns.pdbx_netI_over_sigmaI 17.2 _reflns.B_iso_Wilson_estimate 25.2 _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_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 1.55 _reflns_shell.d_res_low 1.64 _reflns_shell.percent_possible_all 77.2 _reflns_shell.Rmerge_I_obs 0.216 _reflns_shell.pdbx_Rsym_value 0.216 _reflns_shell.meanI_over_sigI_obs 4.3 _reflns_shell.pdbx_redundancy 3.1 _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all 4882 _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 3CA5 _refine.ls_number_reflns_obs 40281 _refine.ls_number_reflns_all 40281 _refine.pdbx_ls_sigma_I 0 _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 20.00 _refine.ls_d_res_high 1.55 _refine.ls_percent_reflns_obs 96.62 _refine.ls_R_factor_obs 0.135 _refine.ls_R_factor_all 0.135 _refine.ls_R_factor_R_work 0.13280 _refine.ls_R_factor_R_free 0.17977 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.0 _refine.ls_number_reflns_R_free 2125 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.973 _refine.correlation_coeff_Fo_to_Fc_free 0.957 _refine.B_iso_mean 25.219 _refine.aniso_B[1][1] 0.10 _refine.aniso_B[2][2] 0.10 _refine.aniso_B[3][3] -0.21 _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 'BABINET MODEL WITH MASK' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' _refine.pdbx_starting_model 'Sambucus nigra agglutinin II - tetragonal crystal form' _refine.pdbx_method_to_determine_struct 'FOURIER SYNTHESIS' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.084 _refine.pdbx_overall_ESU_R_Free 0.073 _refine.overall_SU_ML 0.041 _refine.overall_SU_B 2.443 _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.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_overall_phase_error ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 1976 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 173 _refine_hist.number_atoms_solvent 341 _refine_hist.number_atoms_total 2490 _refine_hist.d_res_high 1.55 _refine_hist.d_res_low 20.00 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.021 0.021 ? 2328 'X-RAY DIFFRACTION' ? r_bond_other_d ? ? ? ? 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.825 2.020 ? 3212 'X-RAY DIFFRACTION' ? r_angle_other_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 6.998 5.000 ? 287 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 36.218 24.787 ? 94 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 11.952 15.000 ? 352 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 20.511 15.000 ? 15 'X-RAY DIFFRACTION' ? r_chiral_restr 0.144 0.200 ? 384 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.010 0.020 ? 1709 'X-RAY DIFFRACTION' ? r_gen_planes_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_refined 0.216 0.200 ? 1032 'X-RAY DIFFRACTION' ? r_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_refined 0.313 0.200 ? 1631 'X-RAY DIFFRACTION' ? r_nbtor_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined 0.185 0.200 ? 236 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined 0.200 0.200 ? 72 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined 0.237 0.200 ? 52 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it 4.336 6.000 ? 1415 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it 5.225 9.000 ? 2251 'X-RAY DIFFRACTION' ? r_scbond_it 5.875 9.000 ? 1032 'X-RAY DIFFRACTION' ? r_scangle_it 7.833 13.000 ? 961 'X-RAY DIFFRACTION' ? r_rigid_bond_restr 3.498 3.000 ? 2447 'X-RAY DIFFRACTION' ? r_sphericity_free 9.476 3.000 ? 347 'X-RAY DIFFRACTION' ? r_sphericity_bonded 6.827 3.000 ? 2269 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.55 _refine_ls_shell.d_res_low 1.592 _refine_ls_shell.number_reflns_R_work 1514 _refine_ls_shell.R_factor_R_work 0.120 _refine_ls_shell.percent_reflns_obs 56.34 _refine_ls_shell.R_factor_R_free 0.263 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 77 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' # _struct.entry_id 3CA5 _struct.title 'Crystal structure of Sambucus nigra agglutinin II (SNA-II)-tetragonal crystal form- complexed to alpha1 methylgalactose' _struct.pdbx_descriptor 'Agglutinin II, SNA-II' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3CA5 _struct_keywords.pdbx_keywords 'SUGAR BINDING PROTEIN, Plant protein' _struct_keywords.text 'BETA-TREFOIL, RICIN-B DOMAIN, GLYCOSYLATION, LECTIN, Glycoprotein, SIGNALING PROTEIN, SUGAR BINDING PROTEIN, Plant 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 2 ? D N N 3 ? E N N 2 ? F N N 2 ? G N N 3 ? H N N 2 ? I N N 2 ? J N N 2 ? K N N 4 ? L N N 4 ? M N N 5 ? N N N 5 ? O N N 5 ? P N N 5 ? Q N N 5 ? R N N 6 ? S N N 7 ? # _struct_biol.id 1 _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 GLY A 9 ? LEU A 13 ? GLY A 9 LEU A 13 5 ? 5 HELX_P HELX_P2 2 ASN A 19 ? TYR A 21 ? ASN A 19 TYR A 21 5 ? 3 HELX_P HELX_P3 3 GLN A 36 ? ARG A 40 ? GLN A 36 ARG A 40 5 ? 5 HELX_P HELX_P4 4 ALA A 76 ? LYS A 81 ? ALA A 76 LYS A 81 1 ? 6 HELX_P HELX_P5 5 ALA A 118 ? GLY A 122 ? ALA A 118 GLY A 122 5 ? 5 HELX_P HELX_P6 6 GLY A 138 ? MET A 142 ? GLY A 138 MET A 142 5 ? 5 HELX_P HELX_P7 7 SER A 162 ? GLN A 165 ? SER A 162 GLN A 165 5 ? 4 HELX_P HELX_P8 8 LEU A 204 ? ARG A 208 ? LEU A 204 ARG A 208 5 ? 5 HELX_P HELX_P9 9 ALA A 230 ? ARG A 236 ? ALA A 230 ARG A 236 5 ? 7 HELX_P HELX_P10 10 ASN A 246 ? GLN A 250 ? ASN A 246 GLN A 250 5 ? 5 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 14 SG ? ? ? 1_555 A CYS 33 SG ? ? A CYS 14 A CYS 33 1_555 ? ? ? ? ? ? ? 2.056 ? disulf2 disulf ? ? A CYS 55 SG ? ? ? 1_555 A CYS 72 SG ? ? A CYS 55 A CYS 72 1_555 ? ? ? ? ? ? ? 2.079 ? disulf3 disulf ? ? A CYS 143 SG ? ? ? 1_555 A CYS 158 SG ? ? A CYS 143 A CYS 158 1_555 ? ? ? ? ? ? ? 2.084 ? disulf4 disulf ? ? A CYS 184 SG ? ? ? 1_555 A CYS 201 SG ? ? A CYS 184 A CYS 201 1_555 ? ? ? ? ? ? ? 2.088 ? covale1 covale ? ? A ASN 63 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 63 A NAG 258 1_555 ? ? ? ? ? ? ? 1.439 ? covale2 covale ? ? A ASN 71 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 71 A NAG 261 1_555 ? ? ? ? ? ? ? 1.451 ? covale3 covale ? ? A ASN 178 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 178 A NAG 264 1_555 ? ? ? ? ? ? ? 1.450 ? covale4 covale ? ? A ASN 232 ND2 ? ? ? 1_555 J NAG . C1 ? ? A ASN 232 A NAG 266 1_555 ? ? ? ? ? ? ? 1.454 ? covale5 covale ? ? B NAG . O3 ? ? ? 1_555 D FUC . C1 ? ? A NAG 258 A FUC 260 1_555 ? ? ? ? ? ? ? 1.483 ? covale6 covale ? ? B NAG . O4 ? ? ? 1_555 C NAG . C1 ? ? A NAG 258 A NAG 259 1_555 ? ? ? ? ? ? ? 1.436 ? covale7 covale ? ? E NAG . O3 ? ? ? 1_555 G FUC . C1 ? ? A NAG 261 A FUC 263 1_555 ? ? ? ? ? ? ? 1.451 ? covale8 covale ? ? E NAG . O4 ? ? ? 1_555 F NAG . C1 ? ? A NAG 261 A NAG 262 1_555 ? ? ? ? ? ? ? 1.441 ? covale9 covale ? ? H NAG . O4 ? ? ? 1_555 I NAG . C1 ? ? A NAG 264 A NAG 265 1_555 ? ? ? ? ? ? ? 1.439 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 8 ? B ? 2 ? C ? 6 ? D ? 2 ? E ? 2 ? F ? 2 ? # 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 ? anti-parallel A 3 4 ? anti-parallel A 4 5 ? anti-parallel A 5 6 ? anti-parallel A 6 7 ? anti-parallel A 7 8 ? anti-parallel B 1 2 ? anti-parallel C 1 2 ? anti-parallel C 2 3 ? anti-parallel C 3 4 ? anti-parallel C 4 5 ? anti-parallel C 5 6 ? anti-parallel D 1 2 ? anti-parallel E 1 2 ? anti-parallel F 1 2 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 VAL A 98 ? THR A 100 ? VAL A 98 THR A 100 A 2 LEU A 111 ? GLU A 113 ? LEU A 111 GLU A 113 A 3 SER A 65 ? PHE A 70 ? SER A 65 PHE A 70 A 4 LYS A 54 ? ASN A 59 ? LYS A 54 ASN A 59 A 5 ILE A 49 ? SER A 51 ? ILE A 49 SER A 51 A 6 TRP A 41 ? PHE A 43 ? TRP A 41 PHE A 43 A 7 PHE A 3 ? VAL A 8 ? PHE A 3 VAL A 8 A 8 THR A 124 ? THR A 126 ? THR A 124 THR A 126 B 1 CYS A 14 ? VAL A 17 ? CYS A 14 VAL A 17 B 2 LEU A 28 ? TRP A 31 ? LEU A 28 TRP A 31 C 1 ILE A 196 ? LYS A 200 ? ILE A 196 LYS A 200 C 2 THR A 180 ? THR A 187 ? THR A 180 THR A 187 C 3 ILE A 175 ? VAL A 177 ? ILE A 175 VAL A 177 C 4 TRP A 167 ? LEU A 169 ? TRP A 167 LEU A 169 C 5 ILE A 132 ? VAL A 137 ? ILE A 132 VAL A 137 C 6 VAL A 252 ? VAL A 255 ? VAL A 252 VAL A 255 D 1 CYS A 143 ? GLN A 145 ? CYS A 143 GLN A 145 D 2 TRP A 154 ? GLU A 156 ? TRP A 154 GLU A 156 E 1 PHE A 210 ? PHE A 211 ? PHE A 210 PHE A 211 E 2 ILE A 217 ? VAL A 218 ? ILE A 217 VAL A 218 F 1 VAL A 225 ? VAL A 228 ? VAL A 225 VAL A 228 F 2 ILE A 238 ? PHE A 241 ? ILE A 238 PHE A 241 # 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 N VAL A 98 ? N VAL A 98 O GLU A 113 ? O GLU A 113 A 2 3 O LEU A 112 ? O LEU A 112 N SER A 65 ? N SER A 65 A 3 4 O ASN A 66 ? O ASN A 66 N ASN A 59 ? N ASN A 59 A 4 5 O MET A 56 ? O MET A 56 N ILE A 49 ? N ILE A 49 A 5 6 O ARG A 50 ? O ARG A 50 N THR A 42 ? N THR A 42 A 6 7 O TRP A 41 ? O TRP A 41 N ARG A 5 ? N ARG A 5 A 7 8 N VAL A 8 ? N VAL A 8 O THR A 124 ? O THR A 124 B 1 2 N CYS A 14 ? N CYS A 14 O TRP A 31 ? O TRP A 31 C 1 2 O ILE A 197 ? O ILE A 197 N THR A 186 ? N THR A 186 C 2 3 O VAL A 185 ? O VAL A 185 N ILE A 175 ? N ILE A 175 C 3 4 O ARG A 176 ? O ARG A 176 N ALA A 168 ? N ALA A 168 C 4 5 O LEU A 169 ? O LEU A 169 N ILE A 132 ? N ILE A 132 C 5 6 N SER A 135 ? N SER A 135 O GLN A 254 ? O GLN A 254 D 1 2 N CYS A 143 ? N CYS A 143 O GLU A 156 ? O GLU A 156 E 1 2 N PHE A 210 ? N PHE A 210 O VAL A 218 ? O VAL A 218 F 1 2 N VAL A 225 ? N VAL A 225 O PHE A 241 ? O PHE A 241 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG A 258' AC2 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 259' AC3 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE FUC A 260' AC4 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 261' AC5 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 262' AC6 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE FUC A 263' AC7 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE NAG A 264' AC8 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 265' AC9 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 266' BC1 Software ? ? ? ? 12 'BINDING SITE FOR RESIDUE AMG A 267' BC2 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE AMG A 268' BC3 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE SO4 A 901' BC4 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE SO4 A 902' BC5 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE SO4 A 903' BC6 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE SO4 A 904' BC7 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE SO4 A 905' BC8 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ACT A 910' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 7 TYR A 21 ? TYR A 21 . ? 5_554 ? 2 AC1 7 ASN A 63 ? ASN A 63 . ? 1_555 ? 3 AC1 7 ASP A 114 ? ASP A 114 . ? 1_555 ? 4 AC1 7 NAG C . ? NAG A 259 . ? 1_555 ? 5 AC1 7 FUC D . ? FUC A 260 . ? 1_555 ? 6 AC1 7 HOH S . ? HOH A 1229 . ? 1_555 ? 7 AC1 7 HOH S . ? HOH A 1241 . ? 1_555 ? 8 AC2 2 NAG B . ? NAG A 258 . ? 1_555 ? 9 AC2 2 FUC D . ? FUC A 260 . ? 1_555 ? 10 AC3 2 NAG B . ? NAG A 258 . ? 1_555 ? 11 AC3 2 NAG C . ? NAG A 259 . ? 1_555 ? 12 AC4 6 ASN A 71 ? ASN A 71 . ? 1_555 ? 13 AC4 6 SER A 73 ? SER A 73 . ? 1_555 ? 14 AC4 6 NAG F . ? NAG A 262 . ? 1_555 ? 15 AC4 6 FUC G . ? FUC A 263 . ? 1_555 ? 16 AC4 6 SO4 O . ? SO4 A 903 . ? 1_555 ? 17 AC4 6 HOH S . ? HOH A 1145 . ? 1_555 ? 18 AC5 2 NAG E . ? NAG A 261 . ? 1_555 ? 19 AC5 2 FUC G . ? FUC A 263 . ? 1_555 ? 20 AC6 2 NAG E . ? NAG A 261 . ? 1_555 ? 21 AC6 2 NAG F . ? NAG A 262 . ? 1_555 ? 22 AC7 9 VAL A 133 ? VAL A 133 . ? 1_555 ? 23 AC7 9 GLN A 166 ? GLN A 166 . ? 1_555 ? 24 AC7 9 ASN A 178 ? ASN A 178 . ? 1_555 ? 25 AC7 9 ARG A 181 ? ARG A 181 . ? 1_555 ? 26 AC7 9 NAG I . ? NAG A 265 . ? 1_555 ? 27 AC7 9 HOH S . ? HOH A 975 . ? 1_555 ? 28 AC7 9 HOH S . ? HOH A 1177 . ? 1_555 ? 29 AC7 9 HOH S . ? HOH A 1194 . ? 1_555 ? 30 AC7 9 HOH S . ? HOH A 1222 . ? 1_555 ? 31 AC8 2 NAG H . ? NAG A 264 . ? 1_555 ? 32 AC8 2 HOH S . ? HOH A 1013 . ? 1_555 ? 33 AC9 4 ASN A 232 ? ASN A 232 . ? 1_555 ? 34 AC9 4 SER A 234 ? SER A 234 . ? 1_555 ? 35 AC9 4 LEU A 235 ? LEU A 235 . ? 1_555 ? 36 AC9 4 HOH S . ? HOH A 1091 . ? 1_555 ? 37 BC1 12 ASP A 16 ? ASP A 16 . ? 1_555 ? 38 BC1 12 VAL A 17 ? VAL A 17 . ? 1_555 ? 39 BC1 12 ASN A 19 ? ASN A 19 . ? 1_555 ? 40 BC1 12 GLY A 20 ? GLY A 20 . ? 1_555 ? 41 BC1 12 GLN A 29 ? GLN A 29 . ? 1_555 ? 42 BC1 12 TRP A 31 ? TRP A 31 . ? 1_555 ? 43 BC1 12 GLN A 36 ? GLN A 36 . ? 1_555 ? 44 BC1 12 ASN A 38 ? ASN A 38 . ? 1_555 ? 45 BC1 12 HOH S . ? HOH A 945 . ? 1_555 ? 46 BC1 12 HOH S . ? HOH A 972 . ? 1_555 ? 47 BC1 12 HOH S . ? HOH A 985 . ? 1_555 ? 48 BC1 12 HOH S . ? HOH A 1113 . ? 1_555 ? 49 BC2 10 ASP A 47 ? ASP A 47 . ? 10_655 ? 50 BC2 10 GLU A 83 ? GLU A 83 . ? 10_655 ? 51 BC2 10 PRO A 93 ? PRO A 93 . ? 10_655 ? 52 BC2 10 ASP A 227 ? ASP A 227 . ? 1_555 ? 53 BC2 10 ARG A 229 ? ARG A 229 . ? 1_555 ? 54 BC2 10 ALA A 230 ? ALA A 230 . ? 1_555 ? 55 BC2 10 ASN A 248 ? ASN A 248 . ? 1_555 ? 56 BC2 10 HOH S . ? HOH A 938 . ? 1_555 ? 57 BC2 10 HOH S . ? HOH A 1124 . ? 1_555 ? 58 BC2 10 HOH S . ? HOH A 1220 . ? 1_555 ? 59 BC3 3 ALA A 76 ? ALA A 76 . ? 1_555 ? 60 BC3 3 GLU A 77 ? GLU A 77 . ? 1_555 ? 61 BC3 3 HOH S . ? HOH A 1166 . ? 1_555 ? 62 BC4 9 THR A 4 ? THR A 4 . ? 1_555 ? 63 BC4 9 ARG A 37 ? ARG A 37 . ? 1_555 ? 64 BC4 9 ARG A 40 ? ARG A 40 . ? 1_555 ? 65 BC4 9 ASN A 151 ? ASN A 151 . ? 12_555 ? 66 BC4 9 HOH S . ? HOH A 1028 . ? 12_555 ? 67 BC4 9 HOH S . ? HOH A 1134 . ? 1_555 ? 68 BC4 9 HOH S . ? HOH A 1186 . ? 1_555 ? 69 BC4 9 HOH S . ? HOH A 1190 . ? 1_555 ? 70 BC4 9 HOH S . ? HOH A 1251 . ? 1_555 ? 71 BC5 5 CYS A 72 ? CYS A 72 . ? 1_555 ? 72 BC5 5 SER A 73 ? SER A 73 . ? 1_555 ? 73 BC5 5 NAG E . ? NAG A 261 . ? 1_555 ? 74 BC5 5 HOH S . ? HOH A 950 . ? 1_555 ? 75 BC5 5 HOH S . ? HOH A 1072 . ? 1_555 ? 76 BC6 10 SER A 162 ? SER A 162 . ? 1_555 ? 77 BC6 10 SER A 162 ? SER A 162 . ? 6_555 ? 78 BC6 10 LEU A 163 ? LEU A 163 . ? 1_555 ? 79 BC6 10 LEU A 163 ? LEU A 163 . ? 6_555 ? 80 BC6 10 GLN A 164 ? GLN A 164 . ? 1_555 ? 81 BC6 10 GLN A 164 ? GLN A 164 . ? 6_555 ? 82 BC6 10 HOH S . ? HOH A 1016 . ? 1_555 ? 83 BC6 10 HOH S . ? HOH A 1016 . ? 6_555 ? 84 BC6 10 HOH S . ? HOH A 1046 . ? 6_555 ? 85 BC6 10 HOH S . ? HOH A 1046 . ? 1_555 ? 86 BC7 10 ARG A 18 ? ARG A 18 . ? 1_555 ? 87 BC7 10 ASN A 19 ? ASN A 19 . ? 1_555 ? 88 BC7 10 ARG A 103 ? ARG A 103 . ? 5_554 ? 89 BC7 10 ARG A 107 ? ARG A 107 . ? 1_555 ? 90 BC7 10 THR A 108 ? THR A 108 . ? 5_554 ? 91 BC7 10 ILE A 109 ? ILE A 109 . ? 5_554 ? 92 BC7 10 HOH S . ? HOH A 945 . ? 1_555 ? 93 BC7 10 HOH S . ? HOH A 1000 . ? 1_555 ? 94 BC7 10 HOH S . ? HOH A 1023 . ? 1_555 ? 95 BC7 10 HOH S . ? HOH A 1250 . ? 1_555 ? 96 BC8 5 GLY A 25 ? GLY A 25 . ? 5_554 ? 97 BC8 5 ASN A 59 ? ASN A 59 . ? 1_555 ? 98 BC8 5 ASN A 59 ? ASN A 59 . ? 5_554 ? 99 BC8 5 VAL A 68 ? VAL A 68 . ? 5_554 ? 100 BC8 5 PHE A 70 ? PHE A 70 . ? 5_554 ? # _database_PDB_matrix.entry_id 3CA5 _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 3CA5 _atom_sites.fract_transf_matrix[1][1] 0.007929 _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] 0.007929 _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] 0.013151 _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 . THR A 1 1 ? 39.628 -10.680 19.222 1.00 55.03 ? 1 THR A N 1 ATOM 2 C CA . THR A 1 1 ? 40.358 -10.919 17.937 1.00 50.72 ? 1 THR A CA 1 ATOM 3 C C . THR A 1 1 ? 39.799 -10.195 16.699 1.00 44.21 ? 1 THR A C 1 ATOM 4 O O . THR A 1 1 ? 40.281 -10.430 15.577 1.00 43.29 ? 1 THR A O 1 ATOM 5 C CB . THR A 1 1 ? 40.437 -12.389 17.597 1.00 52.04 ? 1 THR A CB 1 ATOM 6 O OG1 . THR A 1 1 ? 41.578 -12.571 16.765 1.00 56.12 ? 1 THR A OG1 1 ATOM 7 C CG2 . THR A 1 1 ? 39.164 -12.862 16.858 1.00 51.05 ? 1 THR A CG2 1 ATOM 8 N N . SER A 1 2 ? 38.753 -9.392 16.894 1.00 34.96 ? 2 SER A N 1 ATOM 9 C CA . SER A 1 2 ? 38.350 -8.441 15.865 1.00 27.87 ? 2 SER A CA 1 ATOM 10 C C . SER A 1 2 ? 38.215 -7.043 16.454 1.00 25.86 ? 2 SER A C 1 ATOM 11 O O . SER A 1 2 ? 37.943 -6.889 17.658 1.00 27.98 ? 2 SER A O 1 ATOM 12 C CB . SER A 1 2 ? 37.049 -8.883 15.216 1.00 33.93 ? 2 SER A CB 1 ATOM 13 O OG . SER A 1 2 ? 35.958 -8.647 16.057 1.00 36.77 ? 2 SER A OG 1 ATOM 14 N N . PHE A 1 3 ? 38.430 -6.009 15.614 1.00 19.72 ? 3 PHE A N 1 ATOM 15 C CA . PHE A 1 3 ? 38.302 -4.630 16.066 1.00 19.16 ? 3 PHE A CA 1 ATOM 16 C C . PHE A 1 3 ? 37.866 -3.822 14.842 1.00 16.00 ? 3 PHE A C 1 ATOM 17 O O . PHE A 1 3 ? 38.125 -4.266 13.687 1.00 20.40 ? 3 PHE A O 1 ATOM 18 C CB . PHE A 1 3 ? 39.622 -4.086 16.624 1.00 19.73 ? 3 PHE A CB 1 ATOM 19 C CG . PHE A 1 3 ? 40.743 -4.072 15.641 1.00 17.95 ? 3 PHE A CG 1 ATOM 20 C CD1 . PHE A 1 3 ? 41.516 -5.240 15.410 1.00 22.83 ? 3 PHE A CD1 1 ATOM 21 C CD2 . PHE A 1 3 ? 41.031 -2.895 14.898 1.00 19.78 ? 3 PHE A CD2 1 ATOM 22 C CE1 . PHE A 1 3 ? 42.619 -5.207 14.468 1.00 20.94 ? 3 PHE A CE1 1 ATOM 23 C CE2 . PHE A 1 3 ? 42.110 -2.880 13.970 1.00 21.40 ? 3 PHE A CE2 1 ATOM 24 C CZ . PHE A 1 3 ? 42.872 -4.042 13.763 1.00 20.33 ? 3 PHE A CZ 1 ATOM 25 N N . THR A 1 4 ? 37.242 -2.665 15.074 1.00 17.05 ? 4 THR A N 1 ATOM 26 C CA . THR A 1 4 ? 36.601 -1.938 13.976 1.00 16.10 ? 4 THR A CA 1 ATOM 27 C C . THR A 1 4 ? 37.089 -0.505 13.922 1.00 18.59 ? 4 THR A C 1 ATOM 28 O O . THR A 1 4 ? 37.278 0.121 14.981 1.00 18.94 ? 4 THR A O 1 ATOM 29 C CB . THR A 1 4 ? 35.041 -1.964 14.224 1.00 20.75 ? 4 THR A CB 1 ATOM 30 O OG1 . THR A 1 4 ? 34.608 -3.357 14.340 1.00 20.54 ? 4 THR A OG1 1 ATOM 31 C CG2 . THR A 1 4 ? 34.240 -1.167 13.102 1.00 18.82 ? 4 THR A CG2 1 ATOM 32 N N . ARG A 1 5 ? 37.317 0.007 12.700 1.00 18.27 ? 5 ARG A N 1 ATOM 33 C CA . ARG A 1 5 ? 37.928 1.307 12.505 1.00 17.62 ? 5 ARG A CA 1 ATOM 34 C C . ARG A 1 5 ? 37.401 1.898 11.204 1.00 20.16 ? 5 ARG A C 1 ATOM 35 O O . ARG A 1 5 ? 36.804 1.154 10.417 1.00 19.22 ? 5 ARG A O 1 ATOM 36 C CB . ARG A 1 5 ? 39.481 1.164 12.339 1.00 18.26 ? 5 ARG A CB 1 ATOM 37 C CG . ARG A 1 5 ? 40.201 0.581 13.566 1.00 19.15 ? 5 ARG A CG 1 ATOM 38 C CD . ARG A 1 5 ? 40.200 1.621 14.665 1.00 18.68 ? 5 ARG A CD 1 ATOM 39 N NE . ARG A 1 5 ? 41.081 1.255 15.797 1.00 21.26 ? 5 ARG A NE 1 ATOM 40 C CZ . ARG A 1 5 ? 40.701 0.573 16.876 1.00 18.49 ? 5 ARG A CZ 1 ATOM 41 N NH1 . ARG A 1 5 ? 39.425 0.144 17.024 1.00 18.74 ? 5 ARG A NH1 1 ATOM 42 N NH2 . ARG A 1 5 ? 41.624 0.333 17.825 1.00 22.24 ? 5 ARG A NH2 1 ATOM 43 N N . ASN A 1 6 ? 37.661 3.193 10.961 1.00 16.89 ? 6 ASN A N 1 ATOM 44 C CA . ASN A 1 6 ? 37.566 3.747 9.586 1.00 14.14 ? 6 ASN A CA 1 ATOM 45 C C . ASN A 1 6 ? 38.871 3.452 8.840 1.00 15.00 ? 6 ASN A C 1 ATOM 46 O O . ASN A 1 6 ? 39.905 3.074 9.474 1.00 17.39 ? 6 ASN A O 1 ATOM 47 C CB . ASN A 1 6 ? 37.340 5.277 9.613 1.00 14.78 ? 6 ASN A CB 1 ATOM 48 C CG . ASN A 1 6 ? 35.904 5.661 9.982 1.00 16.59 ? 6 ASN A CG 1 ATOM 49 O OD1 . ASN A 1 6 ? 35.457 5.391 11.113 1.00 19.98 ? 6 ASN A OD1 1 ATOM 50 N ND2 . ASN A 1 6 ? 35.188 6.305 9.063 1.00 18.12 ? 6 ASN A ND2 1 ATOM 51 N N . ILE A 1 7 ? 38.861 3.633 7.513 1.00 15.33 ? 7 ILE A N 1 ATOM 52 C CA . ILE A 1 7 ? 40.120 3.539 6.732 1.00 15.69 ? 7 ILE A CA 1 ATOM 53 C C . ILE A 1 7 ? 40.202 4.854 5.962 1.00 14.86 ? 7 ILE A C 1 ATOM 54 O O . ILE A 1 7 ? 39.336 5.120 5.085 1.00 17.19 ? 7 ILE A O 1 ATOM 55 C CB . ILE A 1 7 ? 40.105 2.372 5.704 1.00 15.45 ? 7 ILE A CB 1 ATOM 56 C CG1 . ILE A 1 7 ? 39.841 1.016 6.413 1.00 16.15 ? 7 ILE A CG1 1 ATOM 57 C CG2 . ILE A 1 7 ? 41.497 2.267 4.998 1.00 17.21 ? 7 ILE A CG2 1 ATOM 58 C CD1 . ILE A 1 7 ? 39.614 -0.203 5.427 1.00 16.86 ? 7 ILE A CD1 1 ATOM 59 N N . VAL A 1 8 ? 41.204 5.686 6.298 1.00 14.79 ? 8 VAL A N 1 ATOM 60 C CA . VAL A 1 8 ? 41.376 7.011 5.693 1.00 15.01 ? 8 VAL A CA 1 ATOM 61 C C . VAL A 1 8 ? 42.447 6.911 4.584 1.00 16.64 ? 8 VAL A C 1 ATOM 62 O O . VAL A 1 8 ? 43.511 6.304 4.806 1.00 18.33 ? 8 VAL A O 1 ATOM 63 C CB . VAL A 1 8 ? 41.830 8.047 6.769 1.00 15.50 ? 8 VAL A CB 1 ATOM 64 C CG1 . VAL A 1 8 ? 41.950 9.441 6.137 1.00 16.96 ? 8 VAL A CG1 1 ATOM 65 C CG2 . VAL A 1 8 ? 40.889 7.992 8.051 1.00 16.02 ? 8 VAL A CG2 1 ATOM 66 N N . GLY A 1 9 ? 42.212 7.561 3.434 1.00 16.12 ? 9 GLY A N 1 ATOM 67 C CA . GLY A 1 9 ? 43.187 7.559 2.337 1.00 16.93 ? 9 GLY A CA 1 ATOM 68 C C . GLY A 1 9 ? 43.229 8.902 1.649 1.00 15.08 ? 9 GLY A C 1 ATOM 69 O O . GLY A 1 9 ? 43.237 9.946 2.322 1.00 17.28 ? 9 GLY A O 1 ATOM 70 N N . ARG A 1 10 ? 43.310 8.845 0.304 1.00 15.55 ? 10 ARG A N 1 ATOM 71 C CA . ARG A 1 10 ? 43.628 10.011 -0.509 1.00 16.17 ? 10 ARG A CA 1 ATOM 72 C C . ARG A 1 10 ? 42.864 11.270 -0.136 1.00 15.81 ? 10 ARG A C 1 ATOM 73 O O . ARG A 1 10 ? 41.629 11.241 -0.010 1.00 17.46 ? 10 ARG A O 1 ATOM 74 C CB . ARG A 1 10 ? 43.415 9.650 -1.980 1.00 16.52 ? 10 ARG A CB 1 ATOM 75 C CG . ARG A 1 10 ? 43.971 10.736 -2.929 1.00 19.73 ? 10 ARG A CG 1 ATOM 76 C CD . ARG A 1 10 ? 44.006 10.272 -4.362 1.00 18.15 ? 10 ARG A CD 1 ATOM 77 N NE . ARG A 1 10 ? 44.625 11.333 -5.175 1.00 17.10 ? 10 ARG A NE 1 ATOM 78 C CZ . ARG A 1 10 ? 45.017 11.157 -6.456 1.00 18.30 ? 10 ARG A CZ 1 ATOM 79 N NH1 . ARG A 1 10 ? 44.816 9.982 -7.069 1.00 19.12 ? 10 ARG A NH1 1 ATOM 80 N NH2 . ARG A 1 10 ? 45.623 12.180 -7.124 1.00 22.10 ? 10 ARG A NH2 1 ATOM 81 N N . ASP A 1 11 ? 43.603 12.364 0.098 1.00 16.97 ? 11 ASP A N 1 ATOM 82 C CA . ASP A 1 11 ? 43.040 13.675 0.479 1.00 16.59 ? 11 ASP A CA 1 ATOM 83 C C . ASP A 1 11 ? 42.221 13.626 1.788 1.00 18.20 ? 11 ASP A C 1 ATOM 84 O O . ASP A 1 11 ? 41.406 14.551 2.053 1.00 21.38 ? 11 ASP A O 1 ATOM 85 C CB . ASP A 1 11 ? 42.142 14.191 -0.643 1.00 19.15 ? 11 ASP A CB 1 ATOM 86 C CG . ASP A 1 11 ? 42.877 15.033 -1.636 1.00 24.27 ? 11 ASP A CG 1 ATOM 87 O OD1 . ASP A 1 11 ? 42.190 15.857 -2.362 1.00 26.52 ? 11 ASP A OD1 1 ATOM 88 O OD2 . ASP A 1 11 ? 44.128 14.827 -1.735 1.00 23.59 ? 11 ASP A OD2 1 ATOM 89 N N . GLY A 1 12 ? 42.435 12.567 2.600 1.00 15.79 ? 12 GLY A N 1 ATOM 90 C CA . GLY A 1 12 ? 41.732 12.499 3.887 1.00 18.03 ? 12 GLY A CA 1 ATOM 91 C C . GLY A 1 12 ? 40.317 11.959 3.794 1.00 15.57 ? 12 GLY A C 1 ATOM 92 O O . GLY A 1 12 ? 39.579 11.965 4.813 1.00 17.94 ? 12 GLY A O 1 ATOM 93 N N . LEU A 1 13 ? 39.923 11.502 2.608 1.00 15.96 ? 13 LEU A N 1 ATOM 94 C CA . LEU A 1 13 ? 38.577 10.892 2.464 1.00 15.05 ? 13 LEU A CA 1 ATOM 95 C C . LEU A 1 13 ? 38.656 9.419 2.925 1.00 17.46 ? 13 LEU A C 1 ATOM 96 O O . LEU A 1 13 ? 39.748 8.889 3.065 1.00 17.81 ? 13 LEU A O 1 ATOM 97 C CB . LEU A 1 13 ? 38.103 10.946 0.998 1.00 15.51 ? 13 LEU A CB 1 ATOM 98 C CG . LEU A 1 13 ? 37.862 12.362 0.467 1.00 19.91 ? 13 LEU A CG 1 ATOM 99 C CD1 . LEU A 1 13 ? 37.321 12.223 -1.021 1.00 26.87 ? 13 LEU A CD1 1 ATOM 100 C CD2 . LEU A 1 13 ? 36.888 13.071 1.316 1.00 29.54 ? 13 LEU A CD2 1 ATOM 101 N N . CYS A 1 14 ? 37.528 8.770 3.164 1.00 16.03 ? 14 CYS A N 1 ATOM 102 C CA . CYS A 1 14 ? 37.502 7.436 3.755 1.00 15.50 ? 14 CYS A CA 1 ATOM 103 C C . CYS A 1 14 ? 36.981 6.415 2.746 1.00 16.07 ? 14 CYS A C 1 ATOM 104 O O . CYS A 1 14 ? 36.180 6.746 1.843 1.00 16.57 ? 14 CYS A O 1 ATOM 105 C CB . CYS A 1 14 ? 36.517 7.405 4.964 1.00 16.90 ? 14 CYS A CB 1 ATOM 106 S SG . CYS A 1 14 ? 37.339 7.937 6.511 1.00 17.69 ? 14 CYS A SG 1 ATOM 107 N N . VAL A 1 15 ? 37.321 5.160 3.006 1.00 14.95 ? 15 VAL A N 1 ATOM 108 C CA . VAL A 1 15 ? 36.854 4.001 2.212 1.00 14.92 ? 15 VAL A CA 1 ATOM 109 C C . VAL A 1 15 ? 35.392 3.760 2.605 1.00 17.03 ? 15 VAL A C 1 ATOM 110 O O . VAL A 1 15 ? 35.065 3.584 3.798 1.00 16.93 ? 15 VAL A O 1 ATOM 111 C CB . VAL A 1 15 ? 37.687 2.762 2.559 1.00 14.90 ? 15 VAL A CB 1 ATOM 112 C CG1 . VAL A 1 15 ? 37.158 1.465 1.845 1.00 18.00 ? 15 VAL A CG1 1 ATOM 113 C CG2 . VAL A 1 15 ? 39.134 3.005 2.203 1.00 15.11 ? 15 VAL A CG2 1 ATOM 114 N N . ASP A 1 16 ? 34.505 3.757 1.604 1.00 16.95 ? 16 ASP A N 1 ATOM 115 C CA . ASP A 1 16 ? 33.047 3.818 1.851 1.00 16.09 ? 16 ASP A CA 1 ATOM 116 C C . ASP A 1 16 ? 32.359 2.911 0.871 1.00 17.57 ? 16 ASP A C 1 ATOM 117 O O . ASP A 1 16 ? 32.672 2.919 -0.328 1.00 16.94 ? 16 ASP A O 1 ATOM 118 C CB . ASP A 1 16 ? 32.707 5.285 1.596 1.00 14.78 ? 16 ASP A CB 1 ATOM 119 C CG . ASP A 1 16 ? 31.175 5.633 1.662 1.00 16.46 ? 16 ASP A CG 1 ATOM 120 O OD1 . ASP A 1 16 ? 30.760 6.393 2.592 1.00 16.85 ? 16 ASP A OD1 1 ATOM 121 O OD2 . ASP A 1 16 ? 30.413 5.198 0.752 1.00 19.13 ? 16 ASP A OD2 1 ATOM 122 N N . VAL A 1 17 ? 31.444 2.065 1.351 1.00 15.75 ? 17 VAL A N 1 ATOM 123 C CA . VAL A 1 17 ? 30.690 1.184 0.436 1.00 14.90 ? 17 VAL A CA 1 ATOM 124 C C . VAL A 1 17 ? 29.595 2.018 -0.249 1.00 16.74 ? 17 VAL A C 1 ATOM 125 O O . VAL A 1 17 ? 28.744 2.647 0.431 1.00 16.69 ? 17 VAL A O 1 ATOM 126 C CB . VAL A 1 17 ? 30.072 -0.030 1.154 1.00 16.92 ? 17 VAL A CB 1 ATOM 127 C CG1 . VAL A 1 17 ? 29.423 -1.004 0.083 1.00 20.74 ? 17 VAL A CG1 1 ATOM 128 C CG2 . VAL A 1 17 ? 31.150 -0.730 1.979 1.00 17.33 ? 17 VAL A CG2 1 ATOM 129 N N . ARG A 1 18 ? 29.662 2.096 -1.594 1.00 15.31 ? 18 ARG A N 1 ATOM 130 C CA . ARG A 1 18 ? 28.935 3.141 -2.336 1.00 15.94 ? 18 ARG A CA 1 ATOM 131 C C . ARG A 1 18 ? 27.412 3.144 -2.036 1.00 15.92 ? 18 ARG A C 1 ATOM 132 O O . ARG A 1 18 ? 26.752 2.083 -2.109 1.00 17.79 ? 18 ARG A O 1 ATOM 133 C CB . ARG A 1 18 ? 29.181 2.950 -3.853 1.00 15.83 ? 18 ARG A CB 1 ATOM 134 C CG . ARG A 1 18 ? 28.726 4.168 -4.686 1.00 15.74 ? 18 ARG A CG 1 ATOM 135 C CD . ARG A 1 18 ? 29.300 3.984 -6.112 1.00 18.50 ? 18 ARG A CD 1 ATOM 136 N NE . ARG A 1 18 ? 29.090 5.086 -7.077 1.00 16.69 ? 18 ARG A NE 1 ATOM 137 C CZ . ARG A 1 18 ? 30.033 5.955 -7.494 1.00 15.81 ? 18 ARG A CZ 1 ATOM 138 N NH1 . ARG A 1 18 ? 29.781 6.789 -8.495 1.00 19.18 ? 18 ARG A NH1 1 ATOM 139 N NH2 . ARG A 1 18 ? 31.270 5.935 -6.979 1.00 16.98 ? 18 ARG A NH2 1 ATOM 140 N N . ASN A 1 19 ? 26.873 4.333 -1.744 1.00 16.51 ? 19 ASN A N 1 ATOM 141 C CA . ASN A 1 19 ? 25.440 4.534 -1.409 1.00 17.62 ? 19 ASN A CA 1 ATOM 142 C C . ASN A 1 19 ? 24.998 3.932 -0.068 1.00 16.14 ? 19 ASN A C 1 ATOM 143 O O . ASN A 1 19 ? 23.801 4.042 0.287 1.00 20.65 ? 19 ASN A O 1 ATOM 144 C CB . ASN A 1 19 ? 24.480 4.041 -2.526 1.00 19.46 ? 19 ASN A CB 1 ATOM 145 C CG . ASN A 1 19 ? 24.835 4.646 -3.862 1.00 21.99 ? 19 ASN A CG 1 ATOM 146 O OD1 . ASN A 1 19 ? 24.985 5.904 -4.010 1.00 27.16 ? 19 ASN A OD1 1 ATOM 147 N ND2 . ASN A 1 19 ? 25.028 3.793 -4.823 1.00 25.14 ? 19 ASN A ND2 1 ATOM 148 N N . GLY A 1 20 ? 25.932 3.324 0.652 1.00 16.95 ? 20 GLY A N 1 ATOM 149 C CA . GLY A 1 20 ? 25.602 2.482 1.823 1.00 19.14 ? 20 GLY A CA 1 ATOM 150 C C . GLY A 1 20 ? 24.820 1.219 1.499 1.00 19.69 ? 20 GLY A C 1 ATOM 151 O O . GLY A 1 20 ? 24.249 0.603 2.402 1.00 23.22 ? 20 GLY A O 1 ATOM 152 N N . TYR A 1 21 ? 24.800 0.807 0.209 1.00 18.22 ? 21 TYR A N 1 ATOM 153 C CA . TYR A 1 21 ? 24.140 -0.432 -0.194 1.00 19.85 ? 21 TYR A CA 1 ATOM 154 C C . TYR A 1 21 ? 25.003 -1.626 0.219 1.00 19.32 ? 21 TYR A C 1 ATOM 155 O O . TYR A 1 21 ? 26.251 -1.559 0.144 1.00 20.03 ? 21 TYR A O 1 ATOM 156 C CB . TYR A 1 21 ? 23.860 -0.462 -1.695 1.00 21.35 ? 21 TYR A CB 1 ATOM 157 C CG . TYR A 1 21 ? 22.859 0.560 -2.148 1.00 19.59 ? 21 TYR A CG 1 ATOM 158 C CD1 . TYR A 1 21 ? 22.608 0.721 -3.506 1.00 24.68 ? 21 TYR A CD1 1 ATOM 159 C CD2 . TYR A 1 21 ? 22.126 1.353 -1.242 1.00 22.39 ? 21 TYR A CD2 1 ATOM 160 C CE1 . TYR A 1 21 ? 21.657 1.672 -3.977 1.00 22.88 ? 21 TYR A CE1 1 ATOM 161 C CE2 . TYR A 1 21 ? 21.173 2.296 -1.704 1.00 24.77 ? 21 TYR A CE2 1 ATOM 162 C CZ . TYR A 1 21 ? 20.965 2.440 -3.071 1.00 24.40 ? 21 TYR A CZ 1 ATOM 163 O OH . TYR A 1 21 ? 20.045 3.378 -3.526 1.00 28.29 ? 21 TYR A OH 1 ATOM 164 N N . ASP A 1 22 ? 24.355 -2.725 0.619 1.00 24.23 ? 22 ASP A N 1 ATOM 165 C CA . ASP A 1 22 ? 25.103 -3.951 0.968 1.00 22.64 ? 22 ASP A CA 1 ATOM 166 C C . ASP A 1 22 ? 24.938 -5.110 0.004 1.00 21.21 ? 22 ASP A C 1 ATOM 167 O O . ASP A 1 22 ? 25.331 -6.249 0.325 1.00 22.78 ? 22 ASP A O 1 ATOM 168 C CB . ASP A 1 22 ? 24.875 -4.408 2.413 1.00 24.51 ? 22 ASP A CB 1 ATOM 169 C CG . ASP A 1 22 ? 23.473 -4.915 2.669 1.00 28.99 ? 22 ASP A CG 1 ATOM 170 O OD1 . ASP A 1 22 ? 23.176 -5.320 3.825 1.00 33.53 ? 22 ASP A OD1 1 ATOM 171 O OD2 . ASP A 1 22 ? 22.646 -4.879 1.756 1.00 27.62 ? 22 ASP A OD2 1 ATOM 172 N N A THR A 1 23 ? 24.352 -4.866 -1.166 0.50 22.63 ? 23 THR A N 1 ATOM 173 N N B THR A 1 23 ? 24.393 -4.829 -1.195 0.50 20.41 ? 23 THR A N 1 ATOM 174 C CA A THR A 1 23 ? 24.186 -5.961 -2.090 0.50 23.28 ? 23 THR A CA 1 ATOM 175 C CA B THR A 1 23 ? 24.235 -5.850 -2.232 0.50 20.01 ? 23 THR A CA 1 ATOM 176 C C A THR A 1 23 ? 25.571 -6.417 -2.584 0.50 22.78 ? 23 THR A C 1 ATOM 177 C C B THR A 1 23 ? 25.592 -6.390 -2.695 0.50 20.75 ? 23 THR A C 1 ATOM 178 O O A THR A 1 23 ? 26.501 -5.605 -2.672 0.50 19.70 ? 23 THR A O 1 ATOM 179 O O B THR A 1 23 ? 26.533 -5.609 -2.875 0.50 20.51 ? 23 THR A O 1 ATOM 180 C CB A THR A 1 23 ? 23.260 -5.559 -3.270 0.50 25.71 ? 23 THR A CB 1 ATOM 181 C CB B THR A 1 23 ? 23.419 -5.300 -3.493 0.50 18.03 ? 23 THR A CB 1 ATOM 182 O OG1 A THR A 1 23 ? 22.607 -6.715 -3.758 0.50 28.68 ? 23 THR A OG1 1 ATOM 183 O OG1 B THR A 1 23 ? 24.061 -4.135 -4.032 0.50 24.71 ? 23 THR A OG1 1 ATOM 184 C CG2 A THR A 1 23 ? 24.040 -4.923 -4.384 0.50 23.05 ? 23 THR A CG2 1 ATOM 185 C CG2 B THR A 1 23 ? 22.029 -4.892 -3.068 0.50 19.17 ? 23 THR A CG2 1 ATOM 186 N N . ASP A 1 24 ? 25.719 -7.711 -2.858 1.00 20.70 ? 24 ASP A N 1 ATOM 187 C CA . ASP A 1 24 ? 26.987 -8.260 -3.358 1.00 20.09 ? 24 ASP A CA 1 ATOM 188 C C . ASP A 1 24 ? 27.451 -7.511 -4.602 1.00 23.48 ? 24 ASP A C 1 ATOM 189 O O . ASP A 1 24 ? 26.664 -7.284 -5.539 1.00 23.00 ? 24 ASP A O 1 ATOM 190 C CB . ASP A 1 24 ? 26.806 -9.719 -3.731 1.00 22.91 ? 24 ASP A CB 1 ATOM 191 C CG . ASP A 1 24 ? 26.706 -10.662 -2.508 1.00 22.19 ? 24 ASP A CG 1 ATOM 192 O OD1 . ASP A 1 24 ? 26.204 -11.803 -2.693 1.00 26.68 ? 24 ASP A OD1 1 ATOM 193 O OD2 . ASP A 1 24 ? 27.105 -10.266 -1.374 1.00 21.80 ? 24 ASP A OD2 1 ATOM 194 N N . GLY A 1 25 ? 28.732 -7.145 -4.629 1.00 19.69 ? 25 GLY A N 1 ATOM 195 C CA . GLY A 1 25 ? 29.251 -6.452 -5.788 1.00 19.82 ? 25 GLY A CA 1 ATOM 196 C C . GLY A 1 25 ? 29.256 -4.957 -5.697 1.00 17.99 ? 25 GLY A C 1 ATOM 197 O O . GLY A 1 25 ? 29.782 -4.302 -6.606 1.00 20.44 ? 25 GLY A O 1 ATOM 198 N N . THR A 1 26 ? 28.749 -4.395 -4.592 1.00 16.40 ? 26 THR A N 1 ATOM 199 C CA . THR A 1 26 ? 28.696 -2.923 -4.491 1.00 18.35 ? 26 THR A CA 1 ATOM 200 C C . THR A 1 26 ? 30.145 -2.395 -4.358 1.00 16.51 ? 26 THR A C 1 ATOM 201 O O . THR A 1 26 ? 30.889 -2.838 -3.474 1.00 19.21 ? 26 THR A O 1 ATOM 202 C CB . THR A 1 26 ? 27.863 -2.443 -3.255 1.00 19.38 ? 26 THR A CB 1 ATOM 203 O OG1 . THR A 1 26 ? 26.498 -2.889 -3.402 1.00 18.67 ? 26 THR A OG1 1 ATOM 204 C CG2 . THR A 1 26 ? 27.888 -0.899 -3.113 1.00 19.04 ? 26 THR A CG2 1 ATOM 205 N N A PRO A 1 27 ? 30.582 -1.529 -5.301 0.50 15.84 ? 27 PRO A N 1 ATOM 206 N N B PRO A 1 27 ? 30.502 -1.405 -5.178 0.50 15.44 ? 27 PRO A N 1 ATOM 207 C CA A PRO A 1 27 ? 31.963 -0.974 -5.243 0.50 16.15 ? 27 PRO A CA 1 ATOM 208 C CA B PRO A 1 27 ? 31.934 -1.073 -5.145 0.50 16.37 ? 27 PRO A CA 1 ATOM 209 C C A PRO A 1 27 ? 32.328 -0.082 -4.044 0.50 16.33 ? 27 PRO A C 1 ATOM 210 C C B PRO A 1 27 ? 32.300 -0.288 -3.889 0.50 15.68 ? 27 PRO A C 1 ATOM 211 O O A PRO A 1 27 ? 31.494 0.714 -3.557 0.50 12.54 ? 27 PRO A O 1 ATOM 212 O O B PRO A 1 27 ? 31.408 0.199 -3.174 0.50 16.53 ? 27 PRO A O 1 ATOM 213 C CB A PRO A 1 27 ? 32.071 -0.123 -6.529 0.50 18.11 ? 27 PRO A CB 1 ATOM 214 C CB B PRO A 1 27 ? 32.124 -0.213 -6.404 0.50 19.48 ? 27 PRO A CB 1 ATOM 215 C CG A PRO A 1 27 ? 30.994 -0.598 -7.444 0.50 15.15 ? 27 PRO A CG 1 ATOM 216 C CG B PRO A 1 27 ? 30.767 0.367 -6.693 0.50 16.90 ? 27 PRO A CG 1 ATOM 217 C CD A PRO A 1 27 ? 29.882 -1.131 -6.546 0.50 13.12 ? 27 PRO A CD 1 ATOM 218 C CD B PRO A 1 27 ? 29.734 -0.577 -6.132 0.50 18.56 ? 27 PRO A CD 1 ATOM 219 N N . LEU A 1 28 ? 33.609 -0.141 -3.648 1.00 16.17 ? 28 LEU A N 1 ATOM 220 C CA . LEU A 1 28 ? 34.128 0.750 -2.623 1.00 15.87 ? 28 LEU A CA 1 ATOM 221 C C . LEU A 1 28 ? 34.566 2.043 -3.302 1.00 15.81 ? 28 LEU A C 1 ATOM 222 O O . LEU A 1 28 ? 35.031 2.028 -4.481 1.00 16.57 ? 28 LEU A O 1 ATOM 223 C CB . LEU A 1 28 ? 35.326 0.120 -1.934 1.00 15.83 ? 28 LEU A CB 1 ATOM 224 C CG . LEU A 1 28 ? 35.055 -1.209 -1.207 1.00 20.67 ? 28 LEU A CG 1 ATOM 225 C CD1 . LEU A 1 28 ? 36.227 -1.560 -0.255 1.00 20.08 ? 28 LEU A CD1 1 ATOM 226 C CD2 . LEU A 1 28 ? 33.688 -1.464 -0.635 1.00 23.35 ? 28 LEU A CD2 1 ATOM 227 N N . GLN A 1 29 ? 34.418 3.161 -2.595 1.00 15.03 ? 29 GLN A N 1 ATOM 228 C CA . GLN A 1 29 ? 34.735 4.472 -3.164 1.00 15.66 ? 29 GLN A CA 1 ATOM 229 C C . GLN A 1 29 ? 35.348 5.338 -2.065 1.00 15.57 ? 29 GLN A C 1 ATOM 230 O O . GLN A 1 29 ? 35.319 4.962 -0.865 1.00 16.82 ? 29 GLN A O 1 ATOM 231 C CB . GLN A 1 29 ? 33.447 5.158 -3.667 1.00 15.67 ? 29 GLN A CB 1 ATOM 232 C CG . GLN A 1 29 ? 32.515 5.518 -2.520 1.00 15.01 ? 29 GLN A CG 1 ATOM 233 C CD . GLN A 1 29 ? 31.206 6.179 -2.929 1.00 16.19 ? 29 GLN A CD 1 ATOM 234 O OE1 . GLN A 1 29 ? 30.987 6.542 -4.116 1.00 18.34 ? 29 GLN A OE1 1 ATOM 235 N NE2 . GLN A 1 29 ? 30.318 6.400 -1.919 1.00 17.73 ? 29 GLN A NE2 1 ATOM 236 N N . LEU A 1 30 ? 35.844 6.517 -2.440 1.00 14.86 ? 30 LEU A N 1 ATOM 237 C CA . LEU A 1 30 ? 36.148 7.550 -1.441 1.00 15.92 ? 30 LEU A CA 1 ATOM 238 C C . LEU A 1 30 ? 34.912 8.399 -1.133 1.00 17.37 ? 30 LEU A C 1 ATOM 239 O O . LEU A 1 30 ? 34.149 8.782 -2.044 1.00 17.29 ? 30 LEU A O 1 ATOM 240 C CB . LEU A 1 30 ? 37.182 8.540 -2.036 1.00 19.14 ? 30 LEU A CB 1 ATOM 241 C CG . LEU A 1 30 ? 38.547 7.964 -2.373 1.00 19.44 ? 30 LEU A CG 1 ATOM 242 C CD1 . LEU A 1 30 ? 39.403 9.173 -2.878 1.00 19.84 ? 30 LEU A CD1 1 ATOM 243 C CD2 . LEU A 1 30 ? 39.089 7.399 -1.114 1.00 20.06 ? 30 LEU A CD2 1 ATOM 244 N N . TRP A 1 31 ? 34.754 8.775 0.138 1.00 16.97 ? 31 TRP A N 1 ATOM 245 C CA . TRP A 1 31 ? 33.677 9.672 0.550 1.00 16.43 ? 31 TRP A CA 1 ATOM 246 C C . TRP A 1 31 ? 34.144 10.374 1.839 1.00 17.25 ? 31 TRP A C 1 ATOM 247 O O . TRP A 1 31 ? 34.932 9.802 2.596 1.00 17.43 ? 31 TRP A O 1 ATOM 248 C CB . TRP A 1 31 ? 32.432 8.853 0.824 1.00 18.22 ? 31 TRP A CB 1 ATOM 249 C CG . TRP A 1 31 ? 31.191 9.684 1.071 1.00 17.12 ? 31 TRP A CG 1 ATOM 250 C CD1 . TRP A 1 31 ? 30.554 9.892 2.286 1.00 18.72 ? 31 TRP A CD1 1 ATOM 251 C CD2 . TRP A 1 31 ? 30.433 10.418 0.072 1.00 16.17 ? 31 TRP A CD2 1 ATOM 252 N NE1 . TRP A 1 31 ? 29.389 10.686 2.081 1.00 18.79 ? 31 TRP A NE1 1 ATOM 253 C CE2 . TRP A 1 31 ? 29.326 11.033 0.743 1.00 17.86 ? 31 TRP A CE2 1 ATOM 254 C CE3 . TRP A 1 31 ? 30.606 10.637 -1.333 1.00 19.68 ? 31 TRP A CE3 1 ATOM 255 C CZ2 . TRP A 1 31 ? 28.395 11.833 0.053 1.00 20.67 ? 31 TRP A CZ2 1 ATOM 256 C CZ3 . TRP A 1 31 ? 29.696 11.448 -2.002 1.00 19.62 ? 31 TRP A CZ3 1 ATOM 257 C CH2 . TRP A 1 31 ? 28.594 12.036 -1.295 1.00 19.58 ? 31 TRP A CH2 1 ATOM 258 N N . PRO A 1 32 ? 33.715 11.630 2.074 1.00 15.44 ? 32 PRO A N 1 ATOM 259 C CA . PRO A 1 32 ? 34.130 12.280 3.306 1.00 16.90 ? 32 PRO A CA 1 ATOM 260 C C . PRO A 1 32 ? 33.818 11.403 4.554 1.00 16.49 ? 32 PRO A C 1 ATOM 261 O O . PRO A 1 32 ? 32.765 10.710 4.625 1.00 17.80 ? 32 PRO A O 1 ATOM 262 C CB . PRO A 1 32 ? 33.292 13.570 3.309 1.00 17.91 ? 32 PRO A CB 1 ATOM 263 C CG . PRO A 1 32 ? 33.131 13.909 1.821 1.00 17.98 ? 32 PRO A CG 1 ATOM 264 C CD . PRO A 1 32 ? 32.859 12.500 1.220 1.00 17.29 ? 32 PRO A CD 1 ATOM 265 N N . CYS A 1 33 ? 34.741 11.428 5.510 1.00 16.20 ? 33 CYS A N 1 ATOM 266 C CA . CYS A 1 33 ? 34.700 10.467 6.617 1.00 16.68 ? 33 CYS A CA 1 ATOM 267 C C . CYS A 1 33 ? 33.518 10.737 7.542 1.00 17.46 ? 33 CYS A C 1 ATOM 268 O O . CYS A 1 33 ? 33.199 11.919 7.833 1.00 20.09 ? 33 CYS A O 1 ATOM 269 C CB . CYS A 1 33 ? 35.967 10.498 7.446 1.00 17.23 ? 33 CYS A CB 1 ATOM 270 S SG . CYS A 1 33 ? 37.444 9.990 6.510 1.00 17.75 ? 33 CYS A SG 1 ATOM 271 N N . GLY A 1 34 ? 32.937 9.651 8.032 1.00 17.18 ? 34 GLY A N 1 ATOM 272 C CA . GLY A 1 34 ? 31.857 9.742 9.041 1.00 18.76 ? 34 GLY A CA 1 ATOM 273 C C . GLY A 1 34 ? 31.699 8.413 9.752 1.00 20.79 ? 34 GLY A C 1 ATOM 274 O O . GLY A 1 34 ? 32.469 7.468 9.540 1.00 20.72 ? 34 GLY A O 1 ATOM 275 N N . THR A 1 35 ? 30.673 8.345 10.606 1.00 20.70 ? 35 THR A N 1 ATOM 276 C CA . THR A 1 35 ? 30.435 7.205 11.479 1.00 21.93 ? 35 THR A CA 1 ATOM 277 C C . THR A 1 35 ? 29.478 6.161 10.850 1.00 17.93 ? 35 THR A C 1 ATOM 278 O O . THR A 1 35 ? 29.176 5.106 11.465 1.00 20.01 ? 35 THR A O 1 ATOM 279 C CB . THR A 1 35 ? 29.748 7.736 12.844 1.00 21.05 ? 35 THR A CB 1 ATOM 280 O OG1 . THR A 1 35 ? 28.525 8.436 12.486 1.00 30.24 ? 35 THR A OG1 1 ATOM 281 C CG2 . THR A 1 35 ? 30.611 8.717 13.526 1.00 30.99 ? 35 THR A CG2 1 ATOM 282 N N . GLN A 1 36 ? 29.003 6.416 9.616 1.00 18.58 ? 36 GLN A N 1 ATOM 283 C CA . GLN A 1 36 ? 28.026 5.494 8.988 1.00 18.46 ? 36 GLN A CA 1 ATOM 284 C C . GLN A 1 36 ? 28.585 4.093 8.882 1.00 15.74 ? 36 GLN A C 1 ATOM 285 O O . GLN A 1 36 ? 29.812 3.931 8.688 1.00 18.09 ? 36 GLN A O 1 ATOM 286 C CB . GLN A 1 36 ? 27.532 6.036 7.634 1.00 19.35 ? 36 GLN A CB 1 ATOM 287 C CG . GLN A 1 36 ? 28.624 6.368 6.592 1.00 17.74 ? 36 GLN A CG 1 ATOM 288 C CD . GLN A 1 36 ? 28.958 7.869 6.522 1.00 18.60 ? 36 GLN A CD 1 ATOM 289 O OE1 . GLN A 1 36 ? 28.946 8.497 5.417 1.00 23.93 ? 36 GLN A OE1 1 ATOM 290 N NE2 . GLN A 1 36 ? 29.157 8.476 7.676 1.00 19.95 ? 36 GLN A NE2 1 ATOM 291 N N . ARG A 1 37 ? 27.743 3.069 8.983 1.00 18.12 ? 37 ARG A N 1 ATOM 292 C CA . ARG A 1 37 ? 28.201 1.685 9.030 1.00 20.64 ? 37 ARG A CA 1 ATOM 293 C C . ARG A 1 37 ? 28.981 1.215 7.820 1.00 18.05 ? 37 ARG A C 1 ATOM 294 O O . ARG A 1 37 ? 29.854 0.334 7.952 1.00 19.04 ? 37 ARG A O 1 ATOM 295 C CB . ARG A 1 37 ? 27.044 0.718 9.325 1.00 24.78 ? 37 ARG A CB 1 ATOM 296 C CG . ARG A 1 37 ? 26.302 1.093 10.653 1.00 28.80 ? 37 ARG A CG 1 ATOM 297 C CD . ARG A 1 37 ? 27.219 1.413 11.867 1.00 34.16 ? 37 ARG A CD 1 ATOM 298 N NE . ARG A 1 37 ? 28.037 0.266 12.266 1.00 35.89 ? 37 ARG A NE 1 ATOM 299 C CZ . ARG A 1 37 ? 28.986 0.309 13.210 1.00 26.94 ? 37 ARG A CZ 1 ATOM 300 N NH1 . ARG A 1 37 ? 29.688 -0.785 13.476 1.00 33.91 ? 37 ARG A NH1 1 ATOM 301 N NH2 . ARG A 1 37 ? 29.192 1.446 13.913 1.00 36.03 ? 37 ARG A NH2 1 ATOM 302 N N . ASN A 1 38 ? 28.690 1.831 6.669 1.00 18.25 ? 38 ASN A N 1 ATOM 303 C CA . ASN A 1 38 ? 29.371 1.469 5.415 1.00 16.40 ? 38 ASN A CA 1 ATOM 304 C C . ASN A 1 38 ? 30.795 2.111 5.335 1.00 17.64 ? 38 ASN A C 1 ATOM 305 O O . ASN A 1 38 ? 31.471 1.987 4.279 1.00 17.22 ? 38 ASN A O 1 ATOM 306 C CB . ASN A 1 38 ? 28.497 1.823 4.176 1.00 16.42 ? 38 ASN A CB 1 ATOM 307 C CG . ASN A 1 38 ? 28.113 3.290 4.144 1.00 17.55 ? 38 ASN A CG 1 ATOM 308 O OD1 . ASN A 1 38 ? 27.555 3.821 5.123 1.00 18.91 ? 38 ASN A OD1 1 ATOM 309 N ND2 . ASN A 1 38 ? 28.441 3.986 3.003 1.00 19.13 ? 38 ASN A ND2 1 ATOM 310 N N . GLN A 1 39 ? 31.194 2.832 6.404 1.00 16.28 ? 39 GLN A N 1 ATOM 311 C CA . GLN A 1 39 ? 32.599 3.297 6.580 1.00 15.97 ? 39 GLN A CA 1 ATOM 312 C C . GLN A 1 39 ? 33.293 2.588 7.771 1.00 17.10 ? 39 GLN A C 1 ATOM 313 O O . GLN A 1 39 ? 34.443 2.917 8.078 1.00 16.56 ? 39 GLN A O 1 ATOM 314 C CB . GLN A 1 39 ? 32.694 4.807 6.759 1.00 17.33 ? 39 GLN A CB 1 ATOM 315 C CG . GLN A 1 39 ? 32.519 5.550 5.421 1.00 17.41 ? 39 GLN A CG 1 ATOM 316 C CD . GLN A 1 39 ? 32.872 6.998 5.534 1.00 17.07 ? 39 GLN A CD 1 ATOM 317 O OE1 . GLN A 1 39 ? 33.639 7.399 6.453 1.00 17.58 ? 39 GLN A OE1 1 ATOM 318 N NE2 . GLN A 1 39 ? 32.378 7.814 4.584 1.00 17.81 ? 39 GLN A NE2 1 ATOM 319 N N . ARG A 1 40 ? 32.588 1.655 8.431 1.00 18.12 ? 40 ARG A N 1 ATOM 320 C CA . ARG A 1 40 ? 33.158 0.996 9.616 1.00 16.09 ? 40 ARG A CA 1 ATOM 321 C C . ARG A 1 40 ? 33.622 -0.380 9.167 1.00 16.50 ? 40 ARG A C 1 ATOM 322 O O . ARG A 1 40 ? 32.807 -1.205 8.723 1.00 18.10 ? 40 ARG A O 1 ATOM 323 C CB . ARG A 1 40 ? 32.117 0.951 10.792 1.00 17.01 ? 40 ARG A CB 1 ATOM 324 C CG . ARG A 1 40 ? 31.694 2.363 11.308 1.00 20.46 ? 40 ARG A CG 1 ATOM 325 C CD . ARG A 1 40 ? 32.846 3.110 11.949 1.00 19.41 ? 40 ARG A CD 1 ATOM 326 N NE . ARG A 1 40 ? 33.315 2.427 13.155 1.00 19.29 ? 40 ARG A NE 1 ATOM 327 C CZ . ARG A 1 40 ? 34.439 2.746 13.806 1.00 18.90 ? 40 ARG A CZ 1 ATOM 328 N NH1 . ARG A 1 40 ? 35.281 3.640 13.306 1.00 20.09 ? 40 ARG A NH1 1 ATOM 329 N NH2 . ARG A 1 40 ? 34.761 2.129 14.952 1.00 20.11 ? 40 ARG A NH2 1 ATOM 330 N N . TRP A 1 41 ? 34.929 -0.630 9.297 1.00 17.65 ? 41 TRP A N 1 ATOM 331 C CA . TRP A 1 41 ? 35.572 -1.825 8.760 1.00 16.53 ? 41 TRP A CA 1 ATOM 332 C C . TRP A 1 41 ? 36.086 -2.628 9.963 1.00 16.01 ? 41 TRP A C 1 ATOM 333 O O . TRP A 1 41 ? 36.845 -2.104 10.796 1.00 17.56 ? 41 TRP A O 1 ATOM 334 C CB . TRP A 1 41 ? 36.741 -1.401 7.818 1.00 17.45 ? 41 TRP A CB 1 ATOM 335 C CG . TRP A 1 41 ? 36.192 -0.760 6.586 1.00 17.89 ? 41 TRP A CG 1 ATOM 336 C CD1 . TRP A 1 41 ? 36.066 0.593 6.347 1.00 16.06 ? 41 TRP A CD1 1 ATOM 337 C CD2 . TRP A 1 41 ? 35.634 -1.437 5.450 1.00 17.45 ? 41 TRP A CD2 1 ATOM 338 N NE1 . TRP A 1 41 ? 35.429 0.809 5.103 1.00 16.79 ? 41 TRP A NE1 1 ATOM 339 C CE2 . TRP A 1 41 ? 35.151 -0.423 4.545 1.00 16.54 ? 41 TRP A CE2 1 ATOM 340 C CE3 . TRP A 1 41 ? 35.455 -2.792 5.121 1.00 16.28 ? 41 TRP A CE3 1 ATOM 341 C CZ2 . TRP A 1 41 ? 34.560 -0.749 3.307 1.00 17.41 ? 41 TRP A CZ2 1 ATOM 342 C CZ3 . TRP A 1 41 ? 34.847 -3.130 3.882 1.00 17.22 ? 41 TRP A CZ3 1 ATOM 343 C CH2 . TRP A 1 41 ? 34.376 -2.102 3.012 1.00 16.98 ? 41 TRP A CH2 1 ATOM 344 N N . THR A 1 42 ? 35.701 -3.894 10.015 1.00 18.38 ? 42 THR A N 1 ATOM 345 C CA . THR A 1 42 ? 36.087 -4.794 11.095 1.00 17.67 ? 42 THR A CA 1 ATOM 346 C C . THR A 1 42 ? 37.197 -5.732 10.574 1.00 18.84 ? 42 THR A C 1 ATOM 347 O O . THR A 1 42 ? 37.017 -6.447 9.542 1.00 20.15 ? 42 THR A O 1 ATOM 348 C CB . THR A 1 42 ? 34.872 -5.599 11.544 1.00 20.05 ? 42 THR A CB 1 ATOM 349 O OG1 . THR A 1 42 ? 33.928 -4.662 12.081 1.00 20.23 ? 42 THR A OG1 1 ATOM 350 C CG2 . THR A 1 42 ? 35.282 -6.662 12.671 1.00 20.11 ? 42 THR A CG2 1 ATOM 351 N N . PHE A 1 43 ? 38.340 -5.725 11.275 1.00 19.86 ? 43 PHE A N 1 ATOM 352 C CA . PHE A 1 43 ? 39.532 -6.509 10.872 1.00 20.08 ? 43 PHE A CA 1 ATOM 353 C C . PHE A 1 43 ? 39.526 -7.751 11.737 1.00 23.52 ? 43 PHE A C 1 ATOM 354 O O . PHE A 1 43 ? 39.487 -7.627 12.976 1.00 24.66 ? 43 PHE A O 1 ATOM 355 C CB . PHE A 1 43 ? 40.830 -5.697 11.118 1.00 22.63 ? 43 PHE A CB 1 ATOM 356 C CG . PHE A 1 43 ? 40.948 -4.494 10.197 1.00 19.85 ? 43 PHE A CG 1 ATOM 357 C CD1 . PHE A 1 43 ? 41.843 -4.535 9.091 1.00 20.34 ? 43 PHE A CD1 1 ATOM 358 C CD2 . PHE A 1 43 ? 40.117 -3.364 10.398 1.00 19.89 ? 43 PHE A CD2 1 ATOM 359 C CE1 . PHE A 1 43 ? 41.924 -3.420 8.202 1.00 20.95 ? 43 PHE A CE1 1 ATOM 360 C CE2 . PHE A 1 43 ? 40.185 -2.276 9.549 1.00 19.90 ? 43 PHE A CE2 1 ATOM 361 C CZ . PHE A 1 43 ? 41.051 -2.297 8.410 1.00 21.27 ? 43 PHE A CZ 1 ATOM 362 N N A ASP A 1 44 ? 39.381 -8.903 11.091 0.50 25.39 ? 44 ASP A N 1 ATOM 363 N N B ASP A 1 44 ? 39.611 -8.937 11.130 0.50 31.57 ? 44 ASP A N 1 ATOM 364 C CA A ASP A 1 44 ? 39.216 -10.193 11.771 0.50 23.73 ? 44 ASP A CA 1 ATOM 365 C CA B ASP A 1 44 ? 39.709 -10.199 11.906 0.50 37.07 ? 44 ASP A CA 1 ATOM 366 C C A ASP A 1 44 ? 40.537 -10.940 11.723 0.50 22.18 ? 44 ASP A C 1 ATOM 367 C C B ASP A 1 44 ? 40.947 -11.038 11.614 0.50 37.13 ? 44 ASP A C 1 ATOM 368 O O A ASP A 1 44 ? 41.388 -10.640 10.886 0.50 22.92 ? 44 ASP A O 1 ATOM 369 O O B ASP A 1 44 ? 41.572 -10.940 10.549 0.50 38.89 ? 44 ASP A O 1 ATOM 370 C CB A ASP A 1 44 ? 38.106 -11.010 11.116 0.50 26.26 ? 44 ASP A CB 1 ATOM 371 C CB B ASP A 1 44 ? 38.473 -11.099 11.738 0.50 36.77 ? 44 ASP A CB 1 ATOM 372 C CG A ASP A 1 44 ? 36.702 -10.546 11.546 0.50 26.67 ? 44 ASP A CG 1 ATOM 373 C CG B ASP A 1 44 ? 38.498 -12.343 12.669 0.50 38.82 ? 44 ASP A CG 1 ATOM 374 O OD1 A ASP A 1 44 ? 36.588 -9.631 12.380 0.50 27.62 ? 44 ASP A OD1 1 ATOM 375 O OD1 B ASP A 1 44 ? 38.212 -12.212 13.887 0.50 38.79 ? 44 ASP A OD1 1 ATOM 376 O OD2 A ASP A 1 44 ? 35.706 -11.085 11.043 0.50 31.87 ? 44 ASP A OD2 1 ATOM 377 O OD2 B ASP A 1 44 ? 38.776 -13.470 12.189 0.50 37.72 ? 44 ASP A OD2 1 ATOM 378 N N A SER A 1 45 ? 40.712 -11.928 12.601 0.50 26.33 ? 45 SER A N 1 ATOM 379 N N B SER A 1 45 ? 41.243 -11.900 12.586 0.50 38.33 ? 45 SER A N 1 ATOM 380 C CA A SER A 1 45 ? 41.973 -12.675 12.570 0.50 27.64 ? 45 SER A CA 1 ATOM 381 C CA B SER A 1 45 ? 42.311 -12.889 12.526 0.50 34.62 ? 45 SER A CA 1 ATOM 382 C C A SER A 1 45 ? 42.257 -13.461 11.284 0.50 28.43 ? 45 SER A C 1 ATOM 383 C C B SER A 1 45 ? 42.302 -13.792 11.299 0.50 31.52 ? 45 SER A C 1 ATOM 384 O O A SER A 1 45 ? 43.439 -13.668 10.938 0.50 29.88 ? 45 SER A O 1 ATOM 385 O O B SER A 1 45 ? 43.314 -14.449 11.009 0.50 33.49 ? 45 SER A O 1 ATOM 386 C CB A SER A 1 45 ? 42.117 -13.571 13.813 0.50 32.67 ? 45 SER A CB 1 ATOM 387 C CB B SER A 1 45 ? 42.232 -13.777 13.778 0.50 36.40 ? 45 SER A CB 1 ATOM 388 O OG A SER A 1 45 ? 42.501 -12.780 14.915 0.50 34.29 ? 45 SER A OG 1 ATOM 389 O OG B SER A 1 45 ? 40.909 -14.280 13.911 0.50 34.96 ? 45 SER A OG 1 ATOM 390 N N . ASP A 1 46 ? 41.188 -13.854 10.569 1.00 25.96 ? 46 ASP A N 1 ATOM 391 C CA . ASP A 1 46 ? 41.229 -14.566 9.301 1.00 23.61 ? 46 ASP A CA 1 ATOM 392 C C . ASP A 1 46 ? 41.656 -13.702 8.090 1.00 23.86 ? 46 ASP A C 1 ATOM 393 O O . ASP A 1 46 ? 41.544 -14.143 6.957 1.00 24.41 ? 46 ASP A O 1 ATOM 394 C CB . ASP A 1 46 ? 39.891 -15.215 9.005 1.00 26.31 ? 46 ASP A CB 1 ATOM 395 C CG . ASP A 1 46 ? 38.743 -14.190 8.807 1.00 27.74 ? 46 ASP A CG 1 ATOM 396 O OD1 . ASP A 1 46 ? 39.000 -12.990 8.828 1.00 25.38 ? 46 ASP A OD1 1 ATOM 397 O OD2 . ASP A 1 46 ? 37.551 -14.597 8.672 1.00 31.82 ? 46 ASP A OD2 1 ATOM 398 N N . ASP A 1 47 ? 42.101 -12.469 8.366 1.00 20.81 ? 47 ASP A N 1 ATOM 399 C CA . ASP A 1 47 ? 42.613 -11.527 7.360 1.00 22.38 ? 47 ASP A CA 1 ATOM 400 C C . ASP A 1 47 ? 41.524 -10.960 6.461 1.00 21.54 ? 47 ASP A C 1 ATOM 401 O O . ASP A 1 47 ? 41.829 -10.396 5.409 1.00 22.41 ? 47 ASP A O 1 ATOM 402 C CB . ASP A 1 47 ? 43.762 -12.118 6.558 1.00 26.31 ? 47 ASP A CB 1 ATOM 403 C CG . ASP A 1 47 ? 44.901 -12.442 7.439 1.00 39.60 ? 47 ASP A CG 1 ATOM 404 O OD1 . ASP A 1 47 ? 45.292 -11.526 8.256 1.00 36.63 ? 47 ASP A OD1 1 ATOM 405 O OD2 . ASP A 1 47 ? 45.333 -13.613 7.359 1.00 45.60 ? 47 ASP A OD2 1 ATOM 406 N N . THR A 1 48 ? 40.262 -11.082 6.878 1.00 20.78 ? 48 THR A N 1 ATOM 407 C CA . THR A 1 48 ? 39.182 -10.391 6.147 1.00 20.24 ? 48 THR A CA 1 ATOM 408 C C . THR A 1 48 ? 38.963 -8.987 6.733 1.00 20.92 ? 48 THR A C 1 ATOM 409 O O . THR A 1 48 ? 39.344 -8.678 7.897 1.00 19.66 ? 48 THR A O 1 ATOM 410 C CB . THR A 1 48 ? 37.838 -11.190 6.207 1.00 19.97 ? 48 THR A CB 1 ATOM 411 O OG1 . THR A 1 48 ? 37.384 -11.272 7.580 1.00 22.53 ? 48 THR A OG1 1 ATOM 412 C CG2 . THR A 1 48 ? 38.038 -12.608 5.586 1.00 21.88 ? 48 THR A CG2 1 ATOM 413 N N . ILE A 1 49 ? 38.345 -8.108 5.934 1.00 18.87 ? 49 ILE A N 1 ATOM 414 C CA . ILE A 1 49 ? 38.060 -6.735 6.390 1.00 19.20 ? 49 ILE A CA 1 ATOM 415 C C . ILE A 1 49 ? 36.592 -6.587 5.999 1.00 18.10 ? 49 ILE A C 1 ATOM 416 O O . ILE A 1 49 ? 36.280 -6.657 4.797 1.00 19.31 ? 49 ILE A O 1 ATOM 417 C CB . ILE A 1 49 ? 38.947 -5.669 5.691 1.00 16.11 ? 49 ILE A CB 1 ATOM 418 C CG1 . ILE A 1 49 ? 40.439 -6.041 5.827 1.00 19.52 ? 49 ILE A CG1 1 ATOM 419 C CG2 . ILE A 1 49 ? 38.693 -4.264 6.263 1.00 18.19 ? 49 ILE A CG2 1 ATOM 420 C CD1 . ILE A 1 49 ? 41.395 -5.114 5.064 1.00 19.73 ? 49 ILE A CD1 1 ATOM 421 N N . ARG A 1 50 ? 35.733 -6.373 6.995 1.00 17.09 ? 50 ARG A N 1 ATOM 422 C CA . ARG A 1 50 ? 34.284 -6.503 6.782 1.00 17.83 ? 50 ARG A CA 1 ATOM 423 C C . ARG A 1 50 ? 33.513 -5.224 7.098 1.00 20.19 ? 50 ARG A C 1 ATOM 424 O O . ARG A 1 50 ? 33.829 -4.503 8.045 1.00 19.74 ? 50 ARG A O 1 ATOM 425 C CB . ARG A 1 50 ? 33.690 -7.637 7.642 1.00 22.36 ? 50 ARG A CB 1 ATOM 426 C CG . ARG A 1 50 ? 34.412 -8.953 7.449 1.00 24.59 ? 50 ARG A CG 1 ATOM 427 C CD . ARG A 1 50 ? 33.793 -10.120 8.226 1.00 24.02 ? 50 ARG A CD 1 ATOM 428 N NE . ARG A 1 50 ? 34.588 -11.341 7.996 1.00 24.13 ? 50 ARG A NE 1 ATOM 429 C CZ . ARG A 1 50 ? 34.090 -12.575 8.044 1.00 22.65 ? 50 ARG A CZ 1 ATOM 430 N NH1 . ARG A 1 50 ? 34.886 -13.615 7.775 1.00 27.49 ? 50 ARG A NH1 1 ATOM 431 N NH2 . ARG A 1 50 ? 32.763 -12.758 8.284 1.00 24.29 ? 50 ARG A NH2 1 ATOM 432 N N . SER A 1 51 ? 32.488 -4.954 6.286 1.00 19.69 ? 51 SER A N 1 ATOM 433 C CA . SER A 1 51 ? 31.577 -3.870 6.594 1.00 18.11 ? 51 SER A CA 1 ATOM 434 C C . SER A 1 51 ? 30.181 -4.363 6.340 1.00 20.01 ? 51 SER A C 1 ATOM 435 O O . SER A 1 51 ? 29.949 -5.117 5.354 1.00 20.89 ? 51 SER A O 1 ATOM 436 C CB . SER A 1 51 ? 31.837 -2.624 5.687 1.00 18.63 ? 51 SER A CB 1 ATOM 437 O OG . SER A 1 51 ? 30.925 -1.585 6.004 1.00 19.22 ? 51 SER A OG 1 ATOM 438 N N . MET A 1 52 ? 29.264 -3.954 7.229 1.00 19.75 ? 52 MET A N 1 ATOM 439 C CA . MET A 1 52 ? 27.860 -4.385 7.090 1.00 21.41 ? 52 MET A CA 1 ATOM 440 C C . MET A 1 52 ? 27.720 -5.933 6.973 1.00 22.25 ? 52 MET A C 1 ATOM 441 O O . MET A 1 52 ? 26.798 -6.477 6.326 1.00 26.54 ? 52 MET A O 1 ATOM 442 C CB . MET A 1 52 ? 27.186 -3.686 5.894 1.00 20.25 ? 52 MET A CB 1 ATOM 443 C CG . MET A 1 52 ? 27.110 -2.187 6.080 1.00 21.05 ? 52 MET A CG 1 ATOM 444 S SD . MET A 1 52 ? 26.411 -1.338 4.687 1.00 23.29 ? 52 MET A SD 1 ATOM 445 C CE . MET A 1 52 ? 27.603 -1.738 3.373 1.00 23.85 ? 52 MET A CE 1 ATOM 446 N N . GLY A 1 53 ? 28.629 -6.631 7.641 1.00 22.59 ? 53 GLY A N 1 ATOM 447 C CA . GLY A 1 53 ? 28.620 -8.068 7.702 1.00 22.35 ? 53 GLY A CA 1 ATOM 448 C C . GLY A 1 53 ? 29.150 -8.806 6.488 1.00 19.95 ? 53 GLY A C 1 ATOM 449 O O . GLY A 1 53 ? 29.071 -10.062 6.431 1.00 24.69 ? 53 GLY A O 1 ATOM 450 N N . LYS A 1 54 ? 29.636 -8.042 5.494 1.00 20.41 ? 54 LYS A N 1 ATOM 451 C CA . LYS A 1 54 ? 30.183 -8.624 4.273 1.00 21.00 ? 54 LYS A CA 1 ATOM 452 C C . LYS A 1 54 ? 31.654 -8.245 4.116 1.00 22.25 ? 54 LYS A C 1 ATOM 453 O O . LYS A 1 54 ? 32.167 -7.398 4.844 1.00 23.15 ? 54 LYS A O 1 ATOM 454 C CB . LYS A 1 54 ? 29.399 -8.169 3.031 1.00 21.07 ? 54 LYS A CB 1 ATOM 455 C CG . LYS A 1 54 ? 27.941 -8.704 3.058 1.00 22.20 ? 54 LYS A CG 1 ATOM 456 C CD . LYS A 1 54 ? 27.297 -8.536 1.710 1.00 23.40 ? 54 LYS A CD 1 ATOM 457 C CE . LYS A 1 54 ? 25.877 -9.111 1.762 1.00 24.71 ? 54 LYS A CE 1 ATOM 458 N NZ . LYS A 1 54 ? 25.215 -8.952 0.440 1.00 24.69 ? 54 LYS A NZ 1 ATOM 459 N N . CYS A 1 55 ? 32.319 -8.887 3.181 1.00 17.76 ? 55 CYS A N 1 ATOM 460 C CA . CYS A 1 55 ? 33.801 -8.781 3.029 1.00 19.25 ? 55 CYS A CA 1 ATOM 461 C C . CYS A 1 55 ? 34.272 -7.837 1.931 1.00 20.26 ? 55 CYS A C 1 ATOM 462 O O . CYS A 1 55 ? 33.789 -7.897 0.780 1.00 18.73 ? 55 CYS A O 1 ATOM 463 C CB . CYS A 1 55 ? 34.384 -10.146 2.700 1.00 19.20 ? 55 CYS A CB 1 ATOM 464 S SG . CYS A 1 55 ? 34.626 -11.167 4.209 1.00 22.83 ? 55 CYS A SG 1 ATOM 465 N N . MET A 1 56 ? 35.285 -7.046 2.252 1.00 19.23 ? 56 MET A N 1 ATOM 466 C CA . MET A 1 56 ? 36.076 -6.365 1.196 1.00 18.64 ? 56 MET A CA 1 ATOM 467 C C . MET A 1 56 ? 36.618 -7.452 0.260 1.00 17.70 ? 56 MET A C 1 ATOM 468 O O . MET A 1 56 ? 37.247 -8.410 0.694 1.00 20.75 ? 56 MET A O 1 ATOM 469 C CB . MET A 1 56 ? 37.236 -5.549 1.823 1.00 17.79 ? 56 MET A CB 1 ATOM 470 C CG . MET A 1 56 ? 38.030 -4.791 0.787 1.00 19.01 ? 56 MET A CG 1 ATOM 471 S SD . MET A 1 56 ? 39.463 -4.008 1.572 1.00 20.05 ? 56 MET A SD 1 ATOM 472 C CE . MET A 1 56 ? 38.610 -2.739 2.554 1.00 21.33 ? 56 MET A CE 1 ATOM 473 N N . THR A 1 57 ? 36.321 -7.335 -1.026 1.00 19.35 ? 57 THR A N 1 ATOM 474 C CA . THR A 1 57 ? 36.564 -8.413 -2.003 1.00 19.38 ? 57 THR A CA 1 ATOM 475 C C . THR A 1 57 ? 37.132 -7.892 -3.313 1.00 19.64 ? 57 THR A C 1 ATOM 476 O O . THR A 1 57 ? 36.598 -6.929 -3.888 1.00 19.61 ? 57 THR A O 1 ATOM 477 C CB . THR A 1 57 ? 35.200 -9.122 -2.319 1.00 18.82 ? 57 THR A CB 1 ATOM 478 O OG1 . THR A 1 57 ? 34.649 -9.643 -1.125 1.00 20.22 ? 57 THR A OG1 1 ATOM 479 C CG2 . THR A 1 57 ? 35.350 -10.253 -3.351 1.00 20.75 ? 57 THR A CG2 1 ATOM 480 N N . ALA A 1 58 ? 38.213 -8.518 -3.796 1.00 19.45 ? 58 ALA A N 1 ATOM 481 C CA . ALA A 1 58 ? 38.741 -8.221 -5.141 1.00 19.36 ? 58 ALA A CA 1 ATOM 482 C C . ALA A 1 58 ? 37.795 -8.823 -6.171 1.00 20.95 ? 58 ALA A C 1 ATOM 483 O O . ALA A 1 58 ? 37.631 -10.034 -6.190 1.00 24.54 ? 58 ALA A O 1 ATOM 484 C CB . ALA A 1 58 ? 40.111 -8.764 -5.291 1.00 20.79 ? 58 ALA A CB 1 ATOM 485 N N . ASN A 1 59 ? 37.214 -7.973 -7.035 1.00 26.74 ? 59 ASN A N 1 ATOM 486 C CA . ASN A 1 59 ? 36.227 -8.481 -8.049 1.00 27.85 ? 59 ASN A CA 1 ATOM 487 C C . ASN A 1 59 ? 37.082 -8.703 -9.242 1.00 31.15 ? 59 ASN A C 1 ATOM 488 O O . ASN A 1 59 ? 37.054 -7.926 -10.180 1.00 32.74 ? 59 ASN A O 1 ATOM 489 C CB . ASN A 1 59 ? 35.123 -7.432 -8.349 1.00 24.80 ? 59 ASN A CB 1 ATOM 490 C CG . ASN A 1 59 ? 34.073 -7.947 -9.293 1.00 26.65 ? 59 ASN A CG 1 ATOM 491 O OD1 . ASN A 1 59 ? 34.069 -9.133 -9.680 1.00 28.53 ? 59 ASN A OD1 1 ATOM 492 N ND2 . ASN A 1 59 ? 33.216 -7.028 -9.757 1.00 29.05 ? 59 ASN A ND2 1 ATOM 493 N N . GLY A 1 60 ? 37.890 -9.751 -9.159 1.00 33.07 ? 60 GLY A N 1 ATOM 494 C CA . GLY A 1 60 ? 38.995 -9.949 -10.072 1.00 35.27 ? 60 GLY A CA 1 ATOM 495 C C . GLY A 1 60 ? 40.312 -9.642 -9.422 1.00 32.28 ? 60 GLY A C 1 ATOM 496 O O . GLY A 1 60 ? 40.389 -8.821 -8.489 1.00 29.52 ? 60 GLY A O 1 ATOM 497 N N . LEU A 1 61 ? 41.360 -10.293 -9.913 1.00 31.50 ? 61 LEU A N 1 ATOM 498 C CA . LEU A 1 61 ? 42.712 -10.090 -9.395 1.00 34.08 ? 61 LEU A CA 1 ATOM 499 C C . LEU A 1 61 ? 43.743 -9.623 -10.463 1.00 32.12 ? 61 LEU A C 1 ATOM 500 O O . LEU A 1 61 ? 44.898 -10.077 -10.440 1.00 34.05 ? 61 LEU A O 1 ATOM 501 C CB . LEU A 1 61 ? 43.219 -11.377 -8.697 1.00 34.82 ? 61 LEU A CB 1 ATOM 502 C CG . LEU A 1 61 ? 42.403 -12.029 -7.551 1.00 38.94 ? 61 LEU A CG 1 ATOM 503 C CD1 . LEU A 1 61 ? 42.832 -13.480 -7.259 1.00 44.71 ? 61 LEU A CD1 1 ATOM 504 C CD2 . LEU A 1 61 ? 42.441 -11.246 -6.275 1.00 28.00 ? 61 LEU A CD2 1 ATOM 505 N N . ASN A 1 62 ? 43.343 -8.695 -11.349 1.00 34.22 ? 62 ASN A N 1 ATOM 506 C CA . ASN A 1 62 ? 44.200 -8.045 -12.393 1.00 31.70 ? 62 ASN A CA 1 ATOM 507 C C . ASN A 1 62 ? 44.422 -6.525 -12.192 1.00 32.26 ? 62 ASN A C 1 ATOM 508 O O . ASN A 1 62 ? 43.656 -5.926 -11.429 1.00 30.38 ? 62 ASN A O 1 ATOM 509 C CB . ASN A 1 62 ? 43.516 -8.201 -13.755 1.00 37.14 ? 62 ASN A CB 1 ATOM 510 C CG . ASN A 1 62 ? 43.717 -9.585 -14.337 1.00 50.20 ? 62 ASN A CG 1 ATOM 511 O OD1 . ASN A 1 62 ? 43.134 -10.556 -13.855 1.00 53.50 ? 62 ASN A OD1 1 ATOM 512 N ND2 . ASN A 1 62 ? 44.561 -9.686 -15.364 1.00 55.25 ? 62 ASN A ND2 1 ATOM 513 N N . ASN A 1 63 ? 45.415 -5.913 -12.870 1.00 27.31 ? 63 ASN A N 1 ATOM 514 C CA . ASN A 1 63 ? 45.679 -4.455 -12.788 1.00 27.62 ? 63 ASN A CA 1 ATOM 515 C C . ASN A 1 63 ? 44.420 -3.739 -13.249 1.00 27.55 ? 63 ASN A C 1 ATOM 516 O O . ASN A 1 63 ? 43.999 -3.888 -14.432 1.00 26.86 ? 63 ASN A O 1 ATOM 517 C CB . ASN A 1 63 ? 46.920 -4.017 -13.615 1.00 26.31 ? 63 ASN A CB 1 ATOM 518 C CG . ASN A 1 63 ? 47.359 -2.557 -13.366 1.00 29.19 ? 63 ASN A CG 1 ATOM 519 O OD1 . ASN A 1 63 ? 47.376 -2.087 -12.214 1.00 27.73 ? 63 ASN A OD1 1 ATOM 520 N ND2 . ASN A 1 63 ? 47.779 -1.843 -14.464 1.00 28.65 ? 63 ASN A ND2 1 ATOM 521 N N . GLY A 1 64 ? 43.788 -3.025 -12.312 1.00 21.39 ? 64 GLY A N 1 ATOM 522 C CA . GLY A 1 64 ? 42.590 -2.228 -12.634 1.00 21.82 ? 64 GLY A CA 1 ATOM 523 C C . GLY A 1 64 ? 41.300 -2.879 -12.131 1.00 21.00 ? 64 GLY A C 1 ATOM 524 O O . GLY A 1 64 ? 40.207 -2.296 -12.314 1.00 22.65 ? 64 GLY A O 1 ATOM 525 N N . SER A 1 65 ? 41.392 -4.062 -11.532 1.00 22.00 ? 65 SER A N 1 ATOM 526 C CA . SER A 1 65 ? 40.221 -4.765 -10.986 1.00 20.31 ? 65 SER A CA 1 ATOM 527 C C . SER A 1 65 ? 39.562 -3.967 -9.869 1.00 18.60 ? 65 SER A C 1 ATOM 528 O O . SER A 1 65 ? 40.237 -3.309 -9.071 1.00 21.45 ? 65 SER A O 1 ATOM 529 C CB . SER A 1 65 ? 40.583 -6.144 -10.426 1.00 23.98 ? 65 SER A CB 1 ATOM 530 O OG . SER A 1 65 ? 40.804 -7.070 -11.452 1.00 27.31 ? 65 SER A OG 1 ATOM 531 N N . ASN A 1 66 ? 38.239 -3.963 -9.860 1.00 20.15 ? 66 ASN A N 1 ATOM 532 C CA . ASN A 1 66 ? 37.456 -3.288 -8.824 1.00 17.78 ? 66 ASN A CA 1 ATOM 533 C C . ASN A 1 66 ? 37.497 -4.018 -7.468 1.00 18.36 ? 66 ASN A C 1 ATOM 534 O O . ASN A 1 66 ? 37.594 -5.252 -7.398 1.00 22.30 ? 66 ASN A O 1 ATOM 535 C CB . ASN A 1 66 ? 36.016 -3.179 -9.295 1.00 20.02 ? 66 ASN A CB 1 ATOM 536 C CG . ASN A 1 66 ? 35.888 -2.165 -10.403 1.00 22.27 ? 66 ASN A CG 1 ATOM 537 O OD1 . ASN A 1 66 ? 35.634 -0.992 -10.141 1.00 25.56 ? 66 ASN A OD1 1 ATOM 538 N ND2 . ASN A 1 66 ? 36.171 -2.597 -11.648 1.00 21.25 ? 66 ASN A ND2 1 ATOM 539 N N . ILE A 1 67 ? 37.390 -3.231 -6.402 1.00 18.28 ? 67 ILE A N 1 ATOM 540 C CA . ILE A 1 67 ? 37.219 -3.800 -5.062 1.00 17.45 ? 67 ILE A CA 1 ATOM 541 C C . ILE A 1 67 ? 35.754 -3.483 -4.653 1.00 17.47 ? 67 ILE A C 1 ATOM 542 O O . ILE A 1 67 ? 35.290 -2.320 -4.826 1.00 17.17 ? 67 ILE A O 1 ATOM 543 C CB . ILE A 1 67 ? 38.204 -3.151 -4.095 1.00 17.64 ? 67 ILE A CB 1 ATOM 544 C CG1 . ILE A 1 67 ? 39.614 -3.354 -4.591 1.00 17.81 ? 67 ILE A CG1 1 ATOM 545 C CG2 . ILE A 1 67 ? 38.045 -3.696 -2.668 1.00 17.89 ? 67 ILE A CG2 1 ATOM 546 C CD1 . ILE A 1 67 ? 40.608 -2.438 -3.873 1.00 21.50 ? 67 ILE A CD1 1 ATOM 547 N N . VAL A 1 68 ? 35.074 -4.495 -4.109 1.00 17.27 ? 68 VAL A N 1 ATOM 548 C CA . VAL A 1 68 ? 33.646 -4.434 -3.812 1.00 17.32 ? 68 VAL A CA 1 ATOM 549 C C . VAL A 1 68 ? 33.385 -5.033 -2.454 1.00 18.20 ? 68 VAL A C 1 ATOM 550 O O . VAL A 1 68 ? 34.322 -5.584 -1.828 1.00 19.23 ? 68 VAL A O 1 ATOM 551 C CB . VAL A 1 68 ? 32.825 -5.239 -4.903 1.00 18.07 ? 68 VAL A CB 1 ATOM 552 C CG1 . VAL A 1 68 ? 33.190 -4.674 -6.361 1.00 18.52 ? 68 VAL A CG1 1 ATOM 553 C CG2 . VAL A 1 68 ? 33.118 -6.776 -4.808 1.00 21.25 ? 68 VAL A CG2 1 ATOM 554 N N . ILE A 1 69 ? 32.141 -4.952 -1.988 1.00 17.95 ? 69 ILE A N 1 ATOM 555 C CA . ILE A 1 69 ? 31.690 -5.768 -0.849 1.00 18.58 ? 69 ILE A CA 1 ATOM 556 C C . ILE A 1 69 ? 31.049 -7.037 -1.390 1.00 19.24 ? 69 ILE A C 1 ATOM 557 O O . ILE A 1 69 ? 30.398 -7.006 -2.468 1.00 20.59 ? 69 ILE A O 1 ATOM 558 C CB . ILE A 1 69 ? 30.667 -4.946 0.007 1.00 21.83 ? 69 ILE A CB 1 ATOM 559 C CG1 . ILE A 1 69 ? 30.719 -5.384 1.422 1.00 24.74 ? 69 ILE A CG1 1 ATOM 560 C CG2 . ILE A 1 69 ? 29.273 -4.826 -0.571 1.00 24.65 ? 69 ILE A CG2 1 ATOM 561 C CD1 . ILE A 1 69 ? 32.012 -4.772 2.083 1.00 25.57 ? 69 ILE A CD1 1 ATOM 562 N N . PHE A 1 70 ? 31.226 -8.146 -0.688 1.00 19.72 ? 70 PHE A N 1 ATOM 563 C CA . PHE A 1 70 ? 30.648 -9.427 -1.155 1.00 19.67 ? 70 PHE A CA 1 ATOM 564 C C . PHE A 1 70 ? 30.516 -10.328 0.045 1.00 23.49 ? 70 PHE A C 1 ATOM 565 O O . PHE A 1 70 ? 31.392 -10.308 0.951 1.00 21.27 ? 70 PHE A O 1 ATOM 566 C CB . PHE A 1 70 ? 31.538 -10.087 -2.227 1.00 22.16 ? 70 PHE A CB 1 ATOM 567 C CG . PHE A 1 70 ? 30.783 -10.980 -3.180 1.00 21.99 ? 70 PHE A CG 1 ATOM 568 C CD1 . PHE A 1 70 ? 30.349 -10.460 -4.386 1.00 23.66 ? 70 PHE A CD1 1 ATOM 569 C CD2 . PHE A 1 70 ? 30.533 -12.313 -2.889 1.00 24.83 ? 70 PHE A CD2 1 ATOM 570 C CE1 . PHE A 1 70 ? 29.645 -11.269 -5.309 1.00 29.08 ? 70 PHE A CE1 1 ATOM 571 C CE2 . PHE A 1 70 ? 29.824 -13.131 -3.798 1.00 26.74 ? 70 PHE A CE2 1 ATOM 572 C CZ . PHE A 1 70 ? 29.380 -12.601 -4.995 1.00 26.87 ? 70 PHE A CZ 1 ATOM 573 N N . ASN A 1 71 ? 29.459 -11.135 0.029 1.00 21.32 ? 71 ASN A N 1 ATOM 574 C CA . ASN A 1 71 ? 29.238 -12.211 1.036 1.00 20.58 ? 71 ASN A CA 1 ATOM 575 C C . ASN A 1 71 ? 30.547 -12.977 1.319 1.00 23.17 ? 71 ASN A C 1 ATOM 576 O O . ASN A 1 71 ? 31.192 -13.475 0.373 1.00 23.10 ? 71 ASN A O 1 ATOM 577 C CB . ASN A 1 71 ? 28.158 -13.144 0.477 1.00 23.21 ? 71 ASN A CB 1 ATOM 578 C CG . ASN A 1 71 ? 27.796 -14.226 1.428 1.00 29.86 ? 71 ASN A CG 1 ATOM 579 O OD1 . ASN A 1 71 ? 28.637 -15.045 1.802 1.00 27.03 ? 71 ASN A OD1 1 ATOM 580 N ND2 . ASN A 1 71 ? 26.541 -14.178 1.903 1.00 27.09 ? 71 ASN A ND2 1 ATOM 581 N N . CYS A 1 72 ? 30.962 -13.027 2.594 1.00 22.49 ? 72 CYS A N 1 ATOM 582 C CA . CYS A 1 72 ? 32.253 -13.631 2.965 1.00 21.80 ? 72 CYS A CA 1 ATOM 583 C C . CYS A 1 72 ? 32.346 -15.142 2.716 1.00 27.05 ? 72 CYS A C 1 ATOM 584 O O . CYS A 1 72 ? 33.419 -15.669 2.448 1.00 28.46 ? 72 CYS A O 1 ATOM 585 C CB . CYS A 1 72 ? 32.574 -13.368 4.451 1.00 25.90 ? 72 CYS A CB 1 ATOM 586 S SG . CYS A 1 72 ? 32.710 -11.629 4.871 1.00 24.44 ? 72 CYS A SG 1 ATOM 587 N N A SER A 1 73 ? 31.226 -15.847 2.807 0.50 25.75 ? 73 SER A N 1 ATOM 588 N N B SER A 1 73 ? 31.220 -15.835 2.830 0.50 24.85 ? 73 SER A N 1 ATOM 589 C CA A SER A 1 73 ? 31.306 -17.309 2.675 0.50 26.89 ? 73 SER A CA 1 ATOM 590 C CA B SER A 1 73 ? 31.262 -17.293 2.682 0.50 25.94 ? 73 SER A CA 1 ATOM 591 C C A SER A 1 73 ? 31.156 -17.771 1.233 0.50 28.99 ? 73 SER A C 1 ATOM 592 C C B SER A 1 73 ? 31.306 -17.679 1.213 0.50 27.75 ? 73 SER A C 1 ATOM 593 O O A SER A 1 73 ? 31.514 -18.899 0.911 0.50 34.33 ? 73 SER A O 1 ATOM 594 O O B SER A 1 73 ? 31.967 -18.641 0.851 0.50 31.60 ? 73 SER A O 1 ATOM 595 C CB A SER A 1 73 ? 30.265 -17.991 3.563 0.50 30.64 ? 73 SER A CB 1 ATOM 596 C CB B SER A 1 73 ? 30.062 -17.948 3.379 0.50 28.57 ? 73 SER A CB 1 ATOM 597 O OG A SER A 1 73 ? 28.958 -17.601 3.176 0.50 31.78 ? 73 SER A OG 1 ATOM 598 O OG B SER A 1 73 ? 29.990 -17.572 4.748 0.50 30.57 ? 73 SER A OG 1 ATOM 599 N N . THR A 1 74 ? 30.622 -16.920 0.360 1.00 24.80 ? 74 THR A N 1 ATOM 600 C CA . THR A 1 74 ? 30.507 -17.278 -1.048 1.00 28.38 ? 74 THR A CA 1 ATOM 601 C C . THR A 1 74 ? 31.597 -16.738 -1.944 1.00 30.59 ? 74 THR A C 1 ATOM 602 O O . THR A 1 74 ? 31.863 -17.341 -2.989 1.00 29.85 ? 74 THR A O 1 ATOM 603 C CB . THR A 1 74 ? 29.126 -16.948 -1.650 1.00 28.46 ? 74 THR A CB 1 ATOM 604 O OG1 . THR A 1 74 ? 28.888 -15.552 -1.575 1.00 30.12 ? 74 THR A OG1 1 ATOM 605 C CG2 . THR A 1 74 ? 28.016 -17.643 -0.854 1.00 33.96 ? 74 THR A CG2 1 ATOM 606 N N . ALA A 1 75 ? 32.250 -15.628 -1.538 1.00 25.43 ? 75 ALA A N 1 ATOM 607 C CA . ALA A 1 75 ? 33.384 -15.108 -2.335 1.00 25.64 ? 75 ALA A CA 1 ATOM 608 C C . ALA A 1 75 ? 34.539 -16.101 -2.352 1.00 27.95 ? 75 ALA A C 1 ATOM 609 O O . ALA A 1 75 ? 34.678 -16.938 -1.443 1.00 28.48 ? 75 ALA A O 1 ATOM 610 C CB . ALA A 1 75 ? 33.870 -13.807 -1.726 1.00 27.04 ? 75 ALA A CB 1 ATOM 611 N N . ALA A 1 76 ? 35.401 -15.976 -3.354 1.00 26.17 ? 76 ALA A N 1 ATOM 612 C CA . ALA A 1 76 ? 36.629 -16.781 -3.396 1.00 27.17 ? 76 ALA A CA 1 ATOM 613 C C . ALA A 1 76 ? 37.585 -16.382 -2.263 1.00 27.20 ? 76 ALA A C 1 ATOM 614 O O . ALA A 1 76 ? 37.781 -15.164 -2.015 1.00 25.55 ? 76 ALA A O 1 ATOM 615 C CB . ALA A 1 76 ? 37.290 -16.623 -4.717 1.00 30.30 ? 76 ALA A CB 1 ATOM 616 N N . GLU A 1 77 ? 38.179 -17.389 -1.589 1.00 26.86 ? 77 GLU A N 1 ATOM 617 C CA . GLU A 1 77 ? 39.082 -17.154 -0.464 1.00 25.94 ? 77 GLU A CA 1 ATOM 618 C C . GLU A 1 77 ? 40.203 -16.179 -0.850 1.00 24.09 ? 77 GLU A C 1 ATOM 619 O O . GLU A 1 77 ? 40.501 -15.265 -0.070 1.00 29.89 ? 77 GLU A O 1 ATOM 620 C CB . GLU A 1 77 ? 39.708 -18.472 0.060 1.00 31.09 ? 77 GLU A CB 1 ATOM 621 N N . ASN A 1 78 ? 40.806 -16.359 -2.037 1.00 26.68 ? 78 ASN A N 1 ATOM 622 C CA . ASN A 1 78 ? 41.924 -15.470 -2.488 1.00 26.47 ? 78 ASN A CA 1 ATOM 623 C C . ASN A 1 78 ? 41.499 -14.016 -2.574 1.00 26.35 ? 78 ASN A C 1 ATOM 624 O O . ASN A 1 78 ? 42.327 -13.113 -2.461 1.00 25.62 ? 78 ASN A O 1 ATOM 625 C CB . ASN A 1 78 ? 42.462 -15.846 -3.868 1.00 31.27 ? 78 ASN A CB 1 ATOM 626 C CG . ASN A 1 78 ? 43.312 -17.119 -3.845 1.00 37.82 ? 78 ASN A CG 1 ATOM 627 O OD1 . ASN A 1 78 ? 43.640 -17.672 -4.897 1.00 46.14 ? 78 ASN A OD1 1 ATOM 628 N ND2 . ASN A 1 78 ? 43.666 -17.577 -2.661 1.00 34.61 ? 78 ASN A ND2 1 ATOM 629 N N . ALA A 1 79 ? 40.198 -13.811 -2.794 1.00 22.82 ? 79 ALA A N 1 ATOM 630 C CA . ALA A 1 79 ? 39.662 -12.474 -3.096 1.00 21.97 ? 79 ALA A CA 1 ATOM 631 C C . ALA A 1 79 ? 39.305 -11.700 -1.836 1.00 18.80 ? 79 ALA A C 1 ATOM 632 O O . ALA A 1 79 ? 39.122 -10.470 -1.906 1.00 20.03 ? 79 ALA A O 1 ATOM 633 C CB . ALA A 1 79 ? 38.444 -12.578 -4.040 1.00 23.47 ? 79 ALA A CB 1 ATOM 634 N N . ILE A 1 80 ? 39.205 -12.393 -0.666 1.00 20.17 ? 80 ILE A N 1 ATOM 635 C CA . ILE A 1 80 ? 38.799 -11.719 0.566 1.00 20.57 ? 80 ILE A CA 1 ATOM 636 C C . ILE A 1 80 ? 39.883 -11.596 1.627 1.00 22.49 ? 80 ILE A C 1 ATOM 637 O O . ILE A 1 80 ? 39.621 -11.113 2.712 1.00 21.25 ? 80 ILE A O 1 ATOM 638 C CB . ILE A 1 80 ? 37.550 -12.366 1.178 1.00 20.62 ? 80 ILE A CB 1 ATOM 639 C CG1 . ILE A 1 80 ? 37.854 -13.822 1.629 1.00 21.20 ? 80 ILE A CG1 1 ATOM 640 C CG2 . ILE A 1 80 ? 36.368 -12.266 0.155 1.00 24.82 ? 80 ILE A CG2 1 ATOM 641 C CD1 . ILE A 1 80 ? 36.633 -14.461 2.389 1.00 21.47 ? 80 ILE A CD1 1 ATOM 642 N N . LYS A 1 81 ? 41.103 -12.001 1.293 1.00 20.36 ? 81 LYS A N 1 ATOM 643 C CA . LYS A 1 81 ? 42.221 -11.909 2.284 1.00 20.50 ? 81 LYS A CA 1 ATOM 644 C C . LYS A 1 81 ? 43.057 -10.664 1.963 1.00 20.76 ? 81 LYS A C 1 ATOM 645 O O . LYS A 1 81 ? 43.344 -10.398 0.772 1.00 22.54 ? 81 LYS A O 1 ATOM 646 C CB . LYS A 1 81 ? 43.079 -13.186 2.279 1.00 24.65 ? 81 LYS A CB 1 ATOM 647 C CG . LYS A 1 81 ? 42.312 -14.376 2.859 1.00 30.67 ? 81 LYS A CG 1 ATOM 648 C CD . LYS A 1 81 ? 43.247 -15.599 2.861 1.00 38.36 ? 81 LYS A CD 1 ATOM 649 C CE . LYS A 1 81 ? 42.816 -16.704 3.825 1.00 48.92 ? 81 LYS A CE 1 ATOM 650 N NZ . LYS A 1 81 ? 42.667 -16.270 5.258 1.00 53.55 ? 81 LYS A NZ 1 ATOM 651 N N . TRP A 1 82 ? 43.396 -9.882 3.006 1.00 18.20 ? 82 TRP A N 1 ATOM 652 C CA . TRP A 1 82 ? 44.085 -8.622 2.843 1.00 19.40 ? 82 TRP A CA 1 ATOM 653 C C . TRP A 1 82 ? 45.163 -8.557 3.928 1.00 23.49 ? 82 TRP A C 1 ATOM 654 O O . TRP A 1 82 ? 44.995 -9.180 4.996 1.00 24.68 ? 82 TRP A O 1 ATOM 655 C CB . TRP A 1 82 ? 43.105 -7.467 3.080 1.00 18.98 ? 82 TRP A CB 1 ATOM 656 C CG . TRP A 1 82 ? 42.037 -7.451 2.061 1.00 17.95 ? 82 TRP A CG 1 ATOM 657 C CD1 . TRP A 1 82 ? 40.818 -8.111 2.128 1.00 18.53 ? 82 TRP A CD1 1 ATOM 658 C CD2 . TRP A 1 82 ? 42.117 -6.874 0.763 1.00 18.41 ? 82 TRP A CD2 1 ATOM 659 N NE1 . TRP A 1 82 ? 40.104 -7.897 0.962 1.00 21.53 ? 82 TRP A NE1 1 ATOM 660 C CE2 . TRP A 1 82 ? 40.883 -7.162 0.095 1.00 19.17 ? 82 TRP A CE2 1 ATOM 661 C CE3 . TRP A 1 82 ? 43.109 -6.150 0.070 1.00 20.92 ? 82 TRP A CE3 1 ATOM 662 C CZ2 . TRP A 1 82 ? 40.637 -6.749 -1.234 1.00 19.77 ? 82 TRP A CZ2 1 ATOM 663 C CZ3 . TRP A 1 82 ? 42.841 -5.701 -1.248 1.00 19.04 ? 82 TRP A CZ3 1 ATOM 664 C CH2 . TRP A 1 82 ? 41.611 -6.010 -1.886 1.00 18.97 ? 82 TRP A CH2 1 ATOM 665 N N . GLU A 1 83 ? 46.237 -7.816 3.654 1.00 19.07 ? 83 GLU A N 1 ATOM 666 C CA . GLU A 1 83 ? 47.197 -7.461 4.705 1.00 19.09 ? 83 GLU A CA 1 ATOM 667 C C . GLU A 1 83 ? 47.440 -5.977 4.737 1.00 18.16 ? 83 GLU A C 1 ATOM 668 O O . GLU A 1 83 ? 47.156 -5.296 3.725 1.00 19.29 ? 83 GLU A O 1 ATOM 669 C CB . GLU A 1 83 ? 48.525 -8.170 4.476 1.00 21.50 ? 83 GLU A CB 1 ATOM 670 C CG . GLU A 1 83 ? 48.543 -9.374 5.269 1.00 29.21 ? 83 GLU A CG 1 ATOM 671 C CD . GLU A 1 83 ? 48.738 -9.049 6.805 1.00 30.82 ? 83 GLU A CD 1 ATOM 672 O OE1 . GLU A 1 83 ? 48.638 -7.864 7.328 1.00 30.85 ? 83 GLU A OE1 1 ATOM 673 O OE2 . GLU A 1 83 ? 48.980 -10.016 7.472 1.00 33.31 ? 83 GLU A OE2 1 ATOM 674 N N . VAL A 1 84 ? 47.912 -5.483 5.887 1.00 18.56 ? 84 VAL A N 1 ATOM 675 C CA . VAL A 1 84 ? 48.104 -4.041 6.086 1.00 17.60 ? 84 VAL A CA 1 ATOM 676 C C . VAL A 1 84 ? 49.572 -3.734 6.448 1.00 17.35 ? 84 VAL A C 1 ATOM 677 O O . VAL A 1 84 ? 49.938 -3.654 7.645 1.00 20.26 ? 84 VAL A O 1 ATOM 678 C CB . VAL A 1 84 ? 47.122 -3.498 7.153 1.00 19.64 ? 84 VAL A CB 1 ATOM 679 C CG1 . VAL A 1 84 ? 47.278 -2.008 7.298 1.00 24.64 ? 84 VAL A CG1 1 ATOM 680 C CG2 . VAL A 1 84 ? 45.684 -3.828 6.688 1.00 21.72 ? 84 VAL A CG2 1 ATOM 681 N N . PRO A 1 85 ? 50.426 -3.623 5.412 1.00 16.79 ? 85 PRO A N 1 ATOM 682 C CA . PRO A 1 85 ? 51.849 -3.385 5.687 1.00 16.97 ? 85 PRO A CA 1 ATOM 683 C C . PRO A 1 85 ? 52.068 -2.102 6.470 1.00 18.57 ? 85 PRO A C 1 ATOM 684 O O . PRO A 1 85 ? 51.257 -1.131 6.378 1.00 21.20 ? 85 PRO A O 1 ATOM 685 C CB . PRO A 1 85 ? 52.444 -3.278 4.276 1.00 18.21 ? 85 PRO A CB 1 ATOM 686 C CG . PRO A 1 85 ? 51.513 -4.152 3.371 1.00 17.27 ? 85 PRO A CG 1 ATOM 687 C CD . PRO A 1 85 ? 50.144 -3.854 3.959 1.00 17.56 ? 85 PRO A CD 1 ATOM 688 N N . ILE A 1 86 ? 53.199 -2.055 7.205 1.00 18.24 ? 86 ILE A N 1 ATOM 689 C CA . ILE A 1 86 ? 53.452 -0.957 8.100 1.00 18.49 ? 86 ILE A CA 1 ATOM 690 C C . ILE A 1 86 ? 53.593 0.368 7.338 1.00 18.19 ? 86 ILE A C 1 ATOM 691 O O . ILE A 1 86 ? 53.344 1.427 7.937 1.00 23.30 ? 86 ILE A O 1 ATOM 692 C CB . ILE A 1 86 ? 54.692 -1.229 9.008 1.00 22.98 ? 86 ILE A CB 1 ATOM 693 C CG1 . ILE A 1 86 ? 55.950 -1.298 8.202 1.00 25.58 ? 86 ILE A CG1 1 ATOM 694 C CG2 . ILE A 1 86 ? 54.461 -2.483 9.893 1.00 29.68 ? 86 ILE A CG2 1 ATOM 695 C CD1 . ILE A 1 86 ? 57.219 -1.546 9.102 1.00 28.94 ? 86 ILE A CD1 1 ATOM 696 N N . ASP A 1 87 ? 53.929 0.329 6.030 1.00 18.59 ? 87 ASP A N 1 ATOM 697 C CA . ASP A 1 87 ? 54.060 1.564 5.242 1.00 20.01 ? 87 ASP A CA 1 ATOM 698 C C . ASP A 1 87 ? 52.721 2.124 4.777 1.00 21.99 ? 87 ASP A C 1 ATOM 699 O O . ASP A 1 87 ? 52.681 3.162 4.092 1.00 24.57 ? 87 ASP A O 1 ATOM 700 C CB . ASP A 1 87 ? 55.008 1.367 4.053 1.00 25.03 ? 87 ASP A CB 1 ATOM 701 C CG . ASP A 1 87 ? 54.415 0.528 2.940 1.00 23.51 ? 87 ASP A CG 1 ATOM 702 O OD1 . ASP A 1 87 ? 55.133 0.303 1.983 1.00 30.34 ? 87 ASP A OD1 1 ATOM 703 O OD2 . ASP A 1 87 ? 53.242 0.111 2.959 1.00 22.33 ? 87 ASP A OD2 1 ATOM 704 N N . GLY A 1 88 ? 51.627 1.483 5.178 1.00 19.56 ? 88 GLY A N 1 ATOM 705 C CA . GLY A 1 88 ? 50.276 2.030 4.875 1.00 22.38 ? 88 GLY A CA 1 ATOM 706 C C . GLY A 1 88 ? 49.612 1.507 3.610 1.00 21.13 ? 88 GLY A C 1 ATOM 707 O O . GLY A 1 88 ? 48.520 1.988 3.227 1.00 23.92 ? 88 GLY A O 1 ATOM 708 N N . SER A 1 89 ? 50.215 0.525 2.938 1.00 16.30 ? 89 SER A N 1 ATOM 709 C CA . SER A 1 89 ? 49.503 -0.104 1.808 1.00 17.03 ? 89 SER A CA 1 ATOM 710 C C . SER A 1 89 ? 48.339 -0.980 2.343 1.00 18.53 ? 89 SER A C 1 ATOM 711 O O . SER A 1 89 ? 48.319 -1.375 3.522 1.00 19.20 ? 89 SER A O 1 ATOM 712 C CB . SER A 1 89 ? 50.430 -1.012 1.016 1.00 20.43 ? 89 SER A CB 1 ATOM 713 O OG . SER A 1 89 ? 51.533 -0.285 0.495 1.00 19.89 ? 89 SER A OG 1 ATOM 714 N N . ILE A 1 90 ? 47.427 -1.329 1.462 1.00 17.18 ? 90 ILE A N 1 ATOM 715 C CA . ILE A 1 90 ? 46.450 -2.398 1.739 1.00 17.74 ? 90 ILE A CA 1 ATOM 716 C C . ILE A 1 90 ? 46.599 -3.319 0.529 1.00 16.89 ? 90 ILE A C 1 ATOM 717 O O . ILE A 1 90 ? 46.288 -2.922 -0.624 1.00 17.87 ? 90 ILE A O 1 ATOM 718 C CB . ILE A 1 90 ? 45.018 -1.840 1.945 1.00 16.82 ? 90 ILE A CB 1 ATOM 719 C CG1 . ILE A 1 90 ? 44.964 -0.993 3.226 1.00 17.80 ? 90 ILE A CG1 1 ATOM 720 C CG2 . ILE A 1 90 ? 43.935 -3.048 2.029 1.00 20.09 ? 90 ILE A CG2 1 ATOM 721 C CD1 . ILE A 1 90 ? 43.643 -0.373 3.582 1.00 19.65 ? 90 ILE A CD1 1 ATOM 722 N N . ILE A 1 91 ? 47.118 -4.533 0.802 1.00 16.89 ? 91 ILE A N 1 ATOM 723 C CA . ILE A 1 91 ? 47.496 -5.424 -0.262 1.00 16.48 ? 91 ILE A CA 1 ATOM 724 C C . ILE A 1 91 ? 46.631 -6.670 -0.253 1.00 19.32 ? 91 ILE A C 1 ATOM 725 O O . ILE A 1 91 ? 46.261 -7.174 0.834 1.00 18.54 ? 91 ILE A O 1 ATOM 726 C CB . ILE A 1 91 ? 49.013 -5.849 -0.135 1.00 17.95 ? 91 ILE A CB 1 ATOM 727 C CG1 . ILE A 1 91 ? 49.515 -6.681 -1.350 1.00 18.61 ? 91 ILE A CG1 1 ATOM 728 C CG2 . ILE A 1 91 ? 49.345 -6.574 1.209 1.00 19.97 ? 91 ILE A CG2 1 ATOM 729 C CD1 . ILE A 1 91 ? 51.101 -6.764 -1.422 1.00 20.90 ? 91 ILE A CD1 1 ATOM 730 N N . ASN A 1 92 ? 46.303 -7.155 -1.458 1.00 17.31 ? 92 ASN A N 1 ATOM 731 C CA . ASN A 1 92 ? 45.667 -8.470 -1.606 1.00 18.88 ? 92 ASN A CA 1 ATOM 732 C C . ASN A 1 92 ? 46.811 -9.462 -1.867 1.00 21.67 ? 92 ASN A C 1 ATOM 733 O O . ASN A 1 92 ? 47.476 -9.402 -2.914 1.00 22.85 ? 92 ASN A O 1 ATOM 734 C CB . ASN A 1 92 ? 44.744 -8.428 -2.820 1.00 19.68 ? 92 ASN A CB 1 ATOM 735 C CG . ASN A 1 92 ? 44.207 -9.823 -3.179 1.00 22.87 ? 92 ASN A CG 1 ATOM 736 O OD1 . ASN A 1 92 ? 44.678 -10.426 -4.104 1.00 27.08 ? 92 ASN A OD1 1 ATOM 737 N ND2 . ASN A 1 92 ? 43.268 -10.330 -2.398 1.00 27.75 ? 92 ASN A ND2 1 ATOM 738 N N . PRO A 1 93 ? 47.102 -10.330 -0.887 1.00 20.65 ? 93 PRO A N 1 ATOM 739 C CA . PRO A 1 93 ? 48.291 -11.185 -1.005 1.00 23.74 ? 93 PRO A CA 1 ATOM 740 C C . PRO A 1 93 ? 48.305 -12.088 -2.232 1.00 24.46 ? 93 PRO A C 1 ATOM 741 O O . PRO A 1 93 ? 49.392 -12.318 -2.837 1.00 28.34 ? 93 PRO A O 1 ATOM 742 C CB . PRO A 1 93 ? 48.268 -11.989 0.300 1.00 25.43 ? 93 PRO A CB 1 ATOM 743 C CG . PRO A 1 93 ? 47.571 -11.132 1.284 1.00 25.02 ? 93 PRO A CG 1 ATOM 744 C CD . PRO A 1 93 ? 46.479 -10.434 0.451 1.00 20.76 ? 93 PRO A CD 1 ATOM 745 N N . SER A 1 94 ? 47.135 -12.551 -2.665 1.00 23.95 ? 94 SER A N 1 ATOM 746 C CA . SER A 1 94 ? 47.095 -13.520 -3.782 1.00 26.70 ? 94 SER A CA 1 ATOM 747 C C . SER A 1 94 ? 47.652 -12.905 -5.060 1.00 30.24 ? 94 SER A C 1 ATOM 748 O O . SER A 1 94 ? 48.472 -13.534 -5.738 1.00 34.47 ? 94 SER A O 1 ATOM 749 C CB . SER A 1 94 ? 45.685 -14.028 -3.992 1.00 30.34 ? 94 SER A CB 1 ATOM 750 O OG . SER A 1 94 ? 45.620 -14.802 -5.177 1.00 33.44 ? 94 SER A OG 1 ATOM 751 N N . SER A 1 95 ? 47.213 -11.683 -5.375 1.00 28.56 ? 95 SER A N 1 ATOM 752 C CA . SER A 1 95 ? 47.574 -10.974 -6.595 1.00 29.41 ? 95 SER A CA 1 ATOM 753 C C . SER A 1 95 ? 48.822 -10.107 -6.420 1.00 28.39 ? 95 SER A C 1 ATOM 754 O O . SER A 1 95 ? 49.515 -9.796 -7.406 1.00 29.04 ? 95 SER A O 1 ATOM 755 C CB . SER A 1 95 ? 46.398 -10.108 -7.046 1.00 26.55 ? 95 SER A CB 1 ATOM 756 O OG . SER A 1 95 ? 46.178 -9.023 -6.145 1.00 26.77 ? 95 SER A OG 1 ATOM 757 N N . GLY A 1 96 ? 49.123 -9.728 -5.174 1.00 24.95 ? 96 GLY A N 1 ATOM 758 C CA . GLY A 1 96 ? 50.149 -8.714 -4.937 1.00 24.37 ? 96 GLY A CA 1 ATOM 759 C C . GLY A 1 96 ? 49.786 -7.279 -5.341 1.00 23.34 ? 96 GLY A C 1 ATOM 760 O O . GLY A 1 96 ? 50.589 -6.346 -5.172 1.00 25.65 ? 96 GLY A O 1 ATOM 761 N N . LEU A 1 97 ? 48.528 -7.058 -5.756 1.00 19.75 ? 97 LEU A N 1 ATOM 762 C CA . LEU A 1 97 ? 48.101 -5.715 -6.147 1.00 18.86 ? 97 LEU A CA 1 ATOM 763 C C . LEU A 1 97 ? 47.646 -4.984 -4.879 1.00 18.30 ? 97 LEU A C 1 ATOM 764 O O . LEU A 1 97 ? 47.347 -5.604 -3.847 1.00 18.75 ? 97 LEU A O 1 ATOM 765 C CB . LEU A 1 97 ? 46.933 -5.811 -7.140 1.00 19.85 ? 97 LEU A CB 1 ATOM 766 C CG . LEU A 1 97 ? 47.276 -6.587 -8.435 1.00 20.30 ? 97 LEU A CG 1 ATOM 767 C CD1 . LEU A 1 97 ? 45.994 -6.821 -9.245 1.00 24.46 ? 97 LEU A CD1 1 ATOM 768 C CD2 . LEU A 1 97 ? 48.273 -5.770 -9.247 1.00 21.97 ? 97 LEU A CD2 1 ATOM 769 N N . VAL A 1 98 ? 47.619 -3.656 -4.949 1.00 16.48 ? 98 VAL A N 1 ATOM 770 C CA . VAL A 1 98 ? 47.274 -2.871 -3.759 1.00 15.88 ? 98 VAL A CA 1 ATOM 771 C C . VAL A 1 98 ? 46.093 -1.915 -4.025 1.00 17.42 ? 98 VAL A C 1 ATOM 772 O O . VAL A 1 98 ? 45.884 -1.427 -5.184 1.00 16.13 ? 98 VAL A O 1 ATOM 773 C CB . VAL A 1 98 ? 48.539 -2.025 -3.265 1.00 16.21 ? 98 VAL A CB 1 ATOM 774 C CG1 . VAL A 1 98 ? 49.650 -3.002 -2.947 1.00 19.72 ? 98 VAL A CG1 1 ATOM 775 C CG2 . VAL A 1 98 ? 49.004 -0.964 -4.345 1.00 17.76 ? 98 VAL A CG2 1 ATOM 776 N N A MET A 1 99 ? 45.367 -1.602 -2.944 0.50 15.63 ? 99 MET A N 1 ATOM 777 N N B MET A 1 99 ? 45.329 -1.621 -2.974 0.50 17.43 ? 99 MET A N 1 ATOM 778 C CA A MET A 1 99 ? 44.243 -0.680 -3.002 0.50 15.55 ? 99 MET A CA 1 ATOM 779 C CA B MET A 1 99 ? 44.163 -0.769 -3.120 0.50 18.90 ? 99 MET A CA 1 ATOM 780 C C A MET A 1 99 ? 44.737 0.704 -3.516 0.50 11.45 ? 99 MET A C 1 ATOM 781 C C B MET A 1 99 ? 44.632 0.682 -3.456 0.50 11.36 ? 99 MET A C 1 ATOM 782 O O A MET A 1 99 ? 45.779 1.245 -3.042 0.50 17.40 ? 99 MET A O 1 ATOM 783 O O B MET A 1 99 ? 45.435 1.274 -2.715 0.50 16.22 ? 99 MET A O 1 ATOM 784 C CB A MET A 1 99 ? 43.623 -0.539 -1.589 0.50 11.54 ? 99 MET A CB 1 ATOM 785 C CB B MET A 1 99 ? 43.352 -0.791 -1.813 0.50 16.74 ? 99 MET A CB 1 ATOM 786 C CG A MET A 1 99 ? 42.381 0.366 -1.571 0.50 14.17 ? 99 MET A CG 1 ATOM 787 C CG B MET A 1 99 ? 41.997 -0.053 -1.912 0.50 23.81 ? 99 MET A CG 1 ATOM 788 S SD A MET A 1 99 ? 41.620 0.646 0.019 0.50 13.88 ? 99 MET A SD 1 ATOM 789 S SD B MET A 1 99 ? 40.833 -0.483 -0.611 0.50 26.15 ? 99 MET A SD 1 ATOM 790 C CE A MET A 1 99 ? 40.858 -0.923 0.389 0.50 15.77 ? 99 MET A CE 1 ATOM 791 C CE B MET A 1 99 ? 41.631 0.246 0.776 0.50 18.43 ? 99 MET A CE 1 ATOM 792 N N . THR A 1 100 ? 44.037 1.247 -4.530 1.00 18.71 ? 100 THR A N 1 ATOM 793 C CA . THR A 1 100 ? 44.470 2.538 -5.114 1.00 17.77 ? 100 THR A CA 1 ATOM 794 C C . THR A 1 100 ? 43.270 3.436 -5.330 1.00 17.25 ? 100 THR A C 1 ATOM 795 O O . THR A 1 100 ? 42.206 2.924 -5.788 1.00 17.34 ? 100 THR A O 1 ATOM 796 C CB . THR A 1 100 ? 45.057 2.235 -6.502 1.00 17.08 ? 100 THR A CB 1 ATOM 797 O OG1 . THR A 1 100 ? 46.070 1.228 -6.361 1.00 18.17 ? 100 THR A OG1 1 ATOM 798 C CG2 . THR A 1 100 ? 45.625 3.469 -7.224 1.00 16.72 ? 100 THR A CG2 1 ATOM 799 N N . ALA A 1 101 ? 43.416 4.713 -4.995 1.00 16.27 ? 101 ALA A N 1 ATOM 800 C CA . ALA A 1 101 ? 42.378 5.751 -5.293 1.00 16.11 ? 101 ALA A CA 1 ATOM 801 C C . ALA A 1 101 ? 42.892 6.545 -6.503 1.00 17.88 ? 101 ALA A C 1 ATOM 802 O O . ALA A 1 101 ? 43.795 7.352 -6.351 1.00 19.32 ? 101 ALA A O 1 ATOM 803 C CB . ALA A 1 101 ? 42.199 6.762 -4.100 1.00 16.51 ? 101 ALA A CB 1 ATOM 804 N N . PRO A 1 102 ? 42.383 6.240 -7.714 1.00 21.32 ? 102 PRO A N 1 ATOM 805 C CA . PRO A 1 102 ? 43.039 6.844 -8.943 1.00 23.84 ? 102 PRO A CA 1 ATOM 806 C C . PRO A 1 102 ? 42.792 8.352 -9.128 1.00 18.42 ? 102 PRO A C 1 ATOM 807 O O . PRO A 1 102 ? 43.493 8.990 -9.946 1.00 21.53 ? 102 PRO A O 1 ATOM 808 C CB . PRO A 1 102 ? 42.403 6.075 -10.095 1.00 25.30 ? 102 PRO A CB 1 ATOM 809 C CG . PRO A 1 102 ? 41.847 4.806 -9.477 1.00 30.28 ? 102 PRO A CG 1 ATOM 810 C CD . PRO A 1 102 ? 41.365 5.223 -8.043 1.00 22.95 ? 102 PRO A CD 1 ATOM 811 N N . ARG A 1 103 ? 41.795 8.914 -8.426 1.00 19.69 ? 103 ARG A N 1 ATOM 812 C CA . ARG A 1 103 ? 41.509 10.357 -8.457 1.00 19.97 ? 103 ARG A CA 1 ATOM 813 C C . ARG A 1 103 ? 41.265 10.772 -6.990 1.00 19.45 ? 103 ARG A C 1 ATOM 814 O O . ARG A 1 103 ? 41.030 9.911 -6.110 1.00 20.13 ? 103 ARG A O 1 ATOM 815 C CB . ARG A 1 103 ? 40.231 10.688 -9.254 1.00 21.73 ? 103 ARG A CB 1 ATOM 816 C CG . ARG A 1 103 ? 40.369 10.374 -10.732 1.00 24.96 ? 103 ARG A CG 1 ATOM 817 C CD . ARG A 1 103 ? 39.093 10.736 -11.535 1.00 27.89 ? 103 ARG A CD 1 ATOM 818 N NE . ARG A 1 103 ? 39.058 12.191 -11.797 1.00 43.13 ? 103 ARG A NE 1 ATOM 819 C CZ . ARG A 1 103 ? 38.119 13.066 -11.404 1.00 41.98 ? 103 ARG A CZ 1 ATOM 820 N NH1 . ARG A 1 103 ? 38.278 14.346 -11.745 1.00 46.96 ? 103 ARG A NH1 1 ATOM 821 N NH2 . ARG A 1 103 ? 37.030 12.709 -10.697 1.00 28.92 ? 103 ARG A NH2 1 ATOM 822 N N . ALA A 1 104 ? 41.371 12.068 -6.701 1.00 21.26 ? 104 ALA A N 1 ATOM 823 C CA . ALA A 1 104 ? 41.084 12.553 -5.313 1.00 24.37 ? 104 ALA A CA 1 ATOM 824 C C . ALA A 1 104 ? 39.551 12.796 -5.005 1.00 22.06 ? 104 ALA A C 1 ATOM 825 O O . ALA A 1 104 ? 39.102 12.977 -3.844 1.00 25.13 ? 104 ALA A O 1 ATOM 826 C CB . ALA A 1 104 ? 41.885 13.829 -5.085 1.00 28.69 ? 104 ALA A CB 1 ATOM 827 N N . ALA A 1 105 ? 38.747 12.856 -6.037 1.00 23.53 ? 105 ALA A N 1 ATOM 828 C CA . ALA A 1 105 ? 37.374 13.326 -5.883 1.00 21.86 ? 105 ALA A CA 1 ATOM 829 C C . ALA A 1 105 ? 36.553 12.385 -5.042 1.00 20.29 ? 105 ALA A C 1 ATOM 830 O O . ALA A 1 105 ? 36.771 11.157 -5.117 1.00 20.17 ? 105 ALA A O 1 ATOM 831 C CB . ALA A 1 105 ? 36.729 13.431 -7.293 1.00 23.38 ? 105 ALA A CB 1 ATOM 832 N N A SER A 1 106 ? 35.591 12.915 -4.280 0.50 21.67 ? 106 SER A N 1 ATOM 833 N N B SER A 1 106 ? 35.585 12.935 -4.291 0.50 20.69 ? 106 SER A N 1 ATOM 834 C CA A SER A 1 106 ? 34.556 12.044 -3.718 0.50 21.30 ? 106 SER A CA 1 ATOM 835 C CA B SER A 1 106 ? 34.484 12.116 -3.760 0.50 19.03 ? 106 SER A CA 1 ATOM 836 C C A SER A 1 106 ? 33.899 11.237 -4.846 0.50 19.84 ? 106 SER A C 1 ATOM 837 C C B SER A 1 106 ? 33.926 11.221 -4.880 0.50 19.16 ? 106 SER A C 1 ATOM 838 O O A SER A 1 106 ? 33.751 11.745 -5.981 0.50 20.42 ? 106 SER A O 1 ATOM 839 O O B SER A 1 106 ? 33.875 11.654 -6.055 0.50 19.63 ? 106 SER A O 1 ATOM 840 C CB A SER A 1 106 ? 33.488 12.819 -2.956 0.50 23.22 ? 106 SER A CB 1 ATOM 841 C CB B SER A 1 106 ? 33.330 12.952 -3.197 0.50 21.47 ? 106 SER A CB 1 ATOM 842 O OG A SER A 1 106 ? 32.766 13.648 -3.846 0.50 25.30 ? 106 SER A OG 1 ATOM 843 O OG B SER A 1 106 ? 33.653 13.647 -2.005 0.50 20.76 ? 106 SER A OG 1 ATOM 844 N N . ARG A 1 107 ? 33.516 10.005 -4.516 1.00 17.59 ? 107 ARG A N 1 ATOM 845 C CA . ARG A 1 107 ? 32.937 9.029 -5.454 1.00 18.28 ? 107 ARG A CA 1 ATOM 846 C C . ARG A 1 107 ? 33.933 8.353 -6.411 1.00 16.76 ? 107 ARG A C 1 ATOM 847 O O . ARG A 1 107 ? 33.514 7.562 -7.261 1.00 18.06 ? 107 ARG A O 1 ATOM 848 C CB . ARG A 1 107 ? 31.702 9.568 -6.217 1.00 19.13 ? 107 ARG A CB 1 ATOM 849 C CG . ARG A 1 107 ? 30.638 10.239 -5.365 1.00 18.22 ? 107 ARG A CG 1 ATOM 850 C CD . ARG A 1 107 ? 29.453 10.735 -6.270 1.00 18.88 ? 107 ARG A CD 1 ATOM 851 N NE . ARG A 1 107 ? 28.627 11.765 -5.580 1.00 25.95 ? 107 ARG A NE 1 ATOM 852 C CZ . ARG A 1 107 ? 27.464 11.513 -5.024 1.00 22.97 ? 107 ARG A CZ 1 ATOM 853 N NH1 . ARG A 1 107 ? 26.949 10.305 -5.125 1.00 30.05 ? 107 ARG A NH1 1 ATOM 854 N NH2 . ARG A 1 107 ? 26.778 12.485 -4.423 1.00 23.66 ? 107 ARG A NH2 1 ATOM 855 N N . THR A 1 108 ? 35.250 8.609 -6.233 1.00 16.45 ? 108 THR A N 1 ATOM 856 C CA . THR A 1 108 ? 36.228 7.851 -6.968 1.00 17.28 ? 108 THR A CA 1 ATOM 857 C C . THR A 1 108 ? 36.142 6.393 -6.488 1.00 17.43 ? 108 THR A C 1 ATOM 858 O O . THR A 1 108 ? 36.069 6.119 -5.278 1.00 16.91 ? 108 THR A O 1 ATOM 859 C CB . THR A 1 108 ? 37.627 8.355 -6.645 1.00 18.05 ? 108 THR A CB 1 ATOM 860 O OG1 . THR A 1 108 ? 37.697 9.734 -7.064 1.00 21.09 ? 108 THR A OG1 1 ATOM 861 C CG2 . THR A 1 108 ? 38.625 7.567 -7.414 1.00 18.26 ? 108 THR A CG2 1 ATOM 862 N N . ILE A 1 109 ? 36.121 5.469 -7.448 1.00 15.56 ? 109 ILE A N 1 ATOM 863 C CA . ILE A 1 109 ? 36.040 4.044 -7.195 1.00 15.00 ? 109 ILE A CA 1 ATOM 864 C C . ILE A 1 109 ? 37.424 3.466 -6.957 1.00 19.70 ? 109 ILE A C 1 ATOM 865 O O . ILE A 1 109 ? 38.365 3.757 -7.688 1.00 20.49 ? 109 ILE A O 1 ATOM 866 C CB . ILE A 1 109 ? 35.382 3.356 -8.370 1.00 17.65 ? 109 ILE A CB 1 ATOM 867 C CG1 . ILE A 1 109 ? 33.949 3.787 -8.343 1.00 20.79 ? 109 ILE A CG1 1 ATOM 868 C CG2 . ILE A 1 109 ? 35.513 1.823 -8.336 1.00 23.70 ? 109 ILE A CG2 1 ATOM 869 C CD1 . ILE A 1 109 ? 33.192 3.127 -7.357 1.00 27.93 ? 109 ILE A CD1 1 ATOM 870 N N . LEU A 1 110 ? 37.499 2.591 -5.960 1.00 16.42 ? 110 LEU A N 1 ATOM 871 C CA . LEU A 1 110 ? 38.784 2.068 -5.537 1.00 15.28 ? 110 LEU A CA 1 ATOM 872 C C . LEU A 1 110 ? 39.143 0.823 -6.370 1.00 17.31 ? 110 LEU A C 1 ATOM 873 O O . LEU A 1 110 ? 38.313 -0.098 -6.564 1.00 18.24 ? 110 LEU A O 1 ATOM 874 C CB . LEU A 1 110 ? 38.783 1.759 -4.012 1.00 17.96 ? 110 LEU A CB 1 ATOM 875 C CG . LEU A 1 110 ? 38.495 3.028 -3.169 1.00 15.68 ? 110 LEU A CG 1 ATOM 876 C CD1 . LEU A 1 110 ? 38.604 2.612 -1.653 1.00 18.60 ? 110 LEU A CD1 1 ATOM 877 C CD2 . LEU A 1 110 ? 39.352 4.234 -3.537 1.00 16.51 ? 110 LEU A CD2 1 ATOM 878 N N . LEU A 1 111 ? 40.410 0.724 -6.807 1.00 16.12 ? 111 LEU A N 1 ATOM 879 C CA . LEU A 1 111 ? 40.835 -0.362 -7.694 1.00 16.13 ? 111 LEU A CA 1 ATOM 880 C C . LEU A 1 111 ? 42.058 -1.037 -7.118 1.00 18.11 ? 111 LEU A C 1 ATOM 881 O O . LEU A 1 111 ? 42.807 -0.399 -6.338 1.00 17.95 ? 111 LEU A O 1 ATOM 882 C CB . LEU A 1 111 ? 41.218 0.207 -9.093 1.00 19.45 ? 111 LEU A CB 1 ATOM 883 C CG . LEU A 1 111 ? 40.157 1.004 -9.878 1.00 17.97 ? 111 LEU A CG 1 ATOM 884 C CD1 . LEU A 1 111 ? 40.713 1.384 -11.248 1.00 21.05 ? 111 LEU A CD1 1 ATOM 885 C CD2 . LEU A 1 111 ? 38.921 0.149 -10.037 1.00 19.03 ? 111 LEU A CD2 1 ATOM 886 N N . LEU A 1 112 ? 42.265 -2.273 -7.510 1.00 18.98 ? 112 LEU A N 1 ATOM 887 C CA . LEU A 1 112 ? 43.559 -2.951 -7.294 1.00 17.49 ? 112 LEU A CA 1 ATOM 888 C C . LEU A 1 112 ? 44.495 -2.605 -8.428 1.00 18.01 ? 112 LEU A C 1 ATOM 889 O O . LEU A 1 112 ? 44.152 -2.841 -9.577 1.00 19.82 ? 112 LEU A O 1 ATOM 890 C CB . LEU A 1 112 ? 43.385 -4.468 -7.260 1.00 20.26 ? 112 LEU A CB 1 ATOM 891 C CG . LEU A 1 112 ? 42.910 -5.128 -5.995 1.00 21.80 ? 112 LEU A CG 1 ATOM 892 C CD1 . LEU A 1 112 ? 42.796 -6.651 -6.279 1.00 28.35 ? 112 LEU A CD1 1 ATOM 893 C CD2 . LEU A 1 112 ? 43.869 -4.827 -4.787 1.00 21.91 ? 112 LEU A CD2 1 ATOM 894 N N . GLU A 1 113 ? 45.683 -2.086 -8.121 1.00 18.89 ? 113 GLU A N 1 ATOM 895 C CA . GLU A 1 113 ? 46.637 -1.807 -9.194 1.00 19.85 ? 113 GLU A CA 1 ATOM 896 C C . GLU A 1 113 ? 48.032 -2.195 -8.751 1.00 18.24 ? 113 GLU A C 1 ATOM 897 O O . GLU A 1 113 ? 48.312 -2.432 -7.523 1.00 19.77 ? 113 GLU A O 1 ATOM 898 C CB . GLU A 1 113 ? 46.635 -0.306 -9.590 1.00 21.30 ? 113 GLU A CB 1 ATOM 899 C CG . GLU A 1 113 ? 45.328 0.110 -10.242 1.00 20.16 ? 113 GLU A CG 1 ATOM 900 C CD . GLU A 1 113 ? 45.243 1.536 -10.695 1.00 22.35 ? 113 GLU A CD 1 ATOM 901 O OE1 . GLU A 1 113 ? 46.254 2.261 -10.649 1.00 28.98 ? 113 GLU A OE1 1 ATOM 902 O OE2 . GLU A 1 113 ? 44.140 1.884 -11.187 1.00 32.39 ? 113 GLU A OE2 1 ATOM 903 N N . ASP A 1 114 ? 48.916 -2.265 -9.753 1.00 20.18 ? 114 ASP A N 1 ATOM 904 C CA . ASP A 1 114 ? 50.325 -2.539 -9.470 1.00 17.86 ? 114 ASP A CA 1 ATOM 905 C C . ASP A 1 114 ? 50.854 -1.585 -8.412 1.00 20.31 ? 114 ASP A C 1 ATOM 906 O O . ASP A 1 114 ? 50.625 -0.372 -8.495 1.00 19.14 ? 114 ASP A O 1 ATOM 907 C CB . ASP A 1 114 ? 51.141 -2.358 -10.779 1.00 20.58 ? 114 ASP A CB 1 ATOM 908 C CG . ASP A 1 114 ? 50.757 -3.379 -11.853 1.00 27.22 ? 114 ASP A CG 1 ATOM 909 O OD1 . ASP A 1 114 ? 50.399 -4.536 -11.555 1.00 32.07 ? 114 ASP A OD1 1 ATOM 910 O OD2 . ASP A 1 114 ? 50.897 -3.030 -13.036 1.00 42.31 ? 114 ASP A OD2 1 ATOM 911 N N . ASN A 1 115 ? 51.629 -2.099 -7.448 1.00 18.20 ? 115 ASN A N 1 ATOM 912 C CA . ASN A 1 115 ? 52.157 -1.220 -6.395 1.00 17.61 ? 115 ASN A CA 1 ATOM 913 C C . ASN A 1 115 ? 53.294 -0.385 -6.946 1.00 19.04 ? 115 ASN A C 1 ATOM 914 O O . ASN A 1 115 ? 54.322 -0.929 -7.427 1.00 21.31 ? 115 ASN A O 1 ATOM 915 C CB . ASN A 1 115 ? 52.650 -2.088 -5.240 1.00 18.66 ? 115 ASN A CB 1 ATOM 916 C CG . ASN A 1 115 ? 53.081 -1.291 -4.040 1.00 19.99 ? 115 ASN A CG 1 ATOM 917 O OD1 . ASN A 1 115 ? 52.850 -0.084 -3.938 1.00 18.22 ? 115 ASN A OD1 1 ATOM 918 N ND2 . ASN A 1 115 ? 53.670 -1.991 -3.061 1.00 26.42 ? 115 ASN A ND2 1 ATOM 919 N N . ILE A 1 116 ? 53.111 0.940 -6.899 1.00 17.64 ? 116 ILE A N 1 ATOM 920 C CA . ILE A 1 116 ? 54.169 1.908 -7.263 1.00 19.10 ? 116 ILE A CA 1 ATOM 921 C C . ILE A 1 116 ? 54.525 2.799 -6.073 1.00 19.48 ? 116 ILE A C 1 ATOM 922 O O . ILE A 1 116 ? 55.266 3.828 -6.218 1.00 20.59 ? 116 ILE A O 1 ATOM 923 C CB . ILE A 1 116 ? 53.791 2.705 -8.525 1.00 19.64 ? 116 ILE A CB 1 ATOM 924 C CG1 . ILE A 1 116 ? 52.474 3.466 -8.331 1.00 20.68 ? 116 ILE A CG1 1 ATOM 925 C CG2 . ILE A 1 116 ? 53.775 1.790 -9.754 1.00 21.70 ? 116 ILE A CG2 1 ATOM 926 C CD1 . ILE A 1 116 ? 52.333 4.580 -9.376 1.00 20.71 ? 116 ILE A CD1 1 ATOM 927 N N . TYR A 1 117 ? 54.031 2.388 -4.887 1.00 17.07 ? 117 TYR A N 1 ATOM 928 C CA . TYR A 1 117 ? 54.247 3.155 -3.637 1.00 16.37 ? 117 TYR A CA 1 ATOM 929 C C . TYR A 1 117 ? 53.726 4.598 -3.792 1.00 16.75 ? 117 TYR A C 1 ATOM 930 O O . TYR A 1 117 ? 54.322 5.526 -3.241 1.00 17.62 ? 117 TYR A O 1 ATOM 931 C CB . TYR A 1 117 ? 55.742 3.122 -3.171 1.00 18.97 ? 117 TYR A CB 1 ATOM 932 C CG . TYR A 1 117 ? 56.159 1.689 -2.822 1.00 20.13 ? 117 TYR A CG 1 ATOM 933 C CD1 . TYR A 1 117 ? 56.913 0.965 -3.702 1.00 20.06 ? 117 TYR A CD1 1 ATOM 934 C CD2 . TYR A 1 117 ? 55.838 1.128 -1.593 1.00 23.74 ? 117 TYR A CD2 1 ATOM 935 C CE1 . TYR A 1 117 ? 57.290 -0.367 -3.424 1.00 22.66 ? 117 TYR A CE1 1 ATOM 936 C CE2 . TYR A 1 117 ? 56.221 -0.188 -1.284 1.00 23.43 ? 117 TYR A CE2 1 ATOM 937 C CZ . TYR A 1 117 ? 56.986 -0.906 -2.188 1.00 24.72 ? 117 TYR A CZ 1 ATOM 938 O OH . TYR A 1 117 ? 57.387 -2.174 -1.837 1.00 24.95 ? 117 TYR A OH 1 ATOM 939 N N . ALA A 1 118 ? 52.582 4.787 -4.477 1.00 17.66 ? 118 ALA A N 1 ATOM 940 C CA . ALA A 1 118 ? 52.070 6.126 -4.680 1.00 17.92 ? 118 ALA A CA 1 ATOM 941 C C . ALA A 1 118 ? 51.339 6.595 -3.411 1.00 16.25 ? 118 ALA A C 1 ATOM 942 O O . ALA A 1 118 ? 50.807 5.775 -2.661 1.00 17.59 ? 118 ALA A O 1 ATOM 943 C CB . ALA A 1 118 ? 51.101 6.151 -5.876 1.00 17.19 ? 118 ALA A CB 1 ATOM 944 N N . ALA A 1 119 ? 51.241 7.900 -3.202 1.00 15.54 ? 119 ALA A N 1 ATOM 945 C CA . ALA A 1 119 ? 50.360 8.405 -2.138 1.00 16.68 ? 119 ALA A CA 1 ATOM 946 C C . ALA A 1 119 ? 48.902 8.028 -2.400 1.00 16.99 ? 119 ALA A C 1 ATOM 947 O O . ALA A 1 119 ? 48.115 7.938 -1.434 1.00 18.02 ? 119 ALA A O 1 ATOM 948 C CB . ALA A 1 119 ? 50.462 9.911 -2.039 1.00 17.30 ? 119 ALA A CB 1 ATOM 949 N N . SER A 1 120 ? 48.507 7.810 -3.677 1.00 16.70 ? 120 SER A N 1 ATOM 950 C CA . SER A 1 120 ? 47.156 7.297 -3.967 1.00 15.02 ? 120 SER A CA 1 ATOM 951 C C . SER A 1 120 ? 46.942 5.856 -3.449 1.00 15.86 ? 120 SER A C 1 ATOM 952 O O . SER A 1 120 ? 45.837 5.304 -3.585 1.00 17.33 ? 120 SER A O 1 ATOM 953 C CB . SER A 1 120 ? 46.942 7.302 -5.494 1.00 17.42 ? 120 SER A CB 1 ATOM 954 O OG . SER A 1 120 ? 47.861 6.438 -6.131 1.00 20.10 ? 120 SER A OG 1 ATOM 955 N N . GLN A 1 121 ? 48.021 5.215 -2.973 1.00 15.69 ? 121 GLN A N 1 ATOM 956 C CA . GLN A 1 121 ? 47.979 3.822 -2.483 1.00 13.82 ? 121 GLN A CA 1 ATOM 957 C C . GLN A 1 121 ? 48.319 3.793 -0.967 1.00 14.53 ? 121 GLN A C 1 ATOM 958 O O . GLN A 1 121 ? 48.534 2.709 -0.388 1.00 16.75 ? 121 GLN A O 1 ATOM 959 C CB . GLN A 1 121 ? 49.016 3.002 -3.288 1.00 15.70 ? 121 GLN A CB 1 ATOM 960 C CG . GLN A 1 121 ? 48.641 2.973 -4.808 1.00 16.14 ? 121 GLN A CG 1 ATOM 961 C CD . GLN A 1 121 ? 49.653 2.243 -5.687 1.00 15.74 ? 121 GLN A CD 1 ATOM 962 O OE1 . GLN A 1 121 ? 50.898 2.399 -5.507 1.00 17.41 ? 121 GLN A OE1 1 ATOM 963 N NE2 . GLN A 1 121 ? 49.149 1.498 -6.675 1.00 16.44 ? 121 GLN A NE2 1 ATOM 964 N N . GLY A 1 122 ? 48.314 4.967 -0.314 1.00 14.49 ? 122 GLY A N 1 ATOM 965 C CA . GLY A 1 122 ? 48.557 5.025 1.160 1.00 14.79 ? 122 GLY A CA 1 ATOM 966 C C . GLY A 1 122 ? 47.221 5.075 1.910 1.00 16.59 ? 122 GLY A C 1 ATOM 967 O O . GLY A 1 122 ? 46.300 5.814 1.471 1.00 16.53 ? 122 GLY A O 1 ATOM 968 N N . TRP A 1 123 ? 47.111 4.362 3.038 1.00 15.23 ? 123 TRP A N 1 ATOM 969 C CA . TRP A 1 123 ? 45.868 4.328 3.844 1.00 15.21 ? 123 TRP A CA 1 ATOM 970 C C . TRP A 1 123 ? 46.253 4.292 5.339 1.00 14.63 ? 123 TRP A C 1 ATOM 971 O O . TRP A 1 123 ? 47.377 3.848 5.683 1.00 16.63 ? 123 TRP A O 1 ATOM 972 C CB . TRP A 1 123 ? 45.086 3.037 3.519 1.00 16.73 ? 123 TRP A CB 1 ATOM 973 C CG . TRP A 1 123 ? 44.832 2.919 2.027 1.00 14.73 ? 123 TRP A CG 1 ATOM 974 C CD1 . TRP A 1 123 ? 45.650 2.348 1.100 1.00 18.51 ? 123 TRP A CD1 1 ATOM 975 C CD2 . TRP A 1 123 ? 43.718 3.526 1.285 1.00 17.74 ? 123 TRP A CD2 1 ATOM 976 N NE1 . TRP A 1 123 ? 45.125 2.516 -0.186 1.00 17.55 ? 123 TRP A NE1 1 ATOM 977 C CE2 . TRP A 1 123 ? 43.943 3.244 -0.101 1.00 15.39 ? 123 TRP A CE2 1 ATOM 978 C CE3 . TRP A 1 123 ? 42.566 4.276 1.665 1.00 16.41 ? 123 TRP A CE3 1 ATOM 979 C CZ2 . TRP A 1 123 ? 43.050 3.686 -1.122 1.00 16.46 ? 123 TRP A CZ2 1 ATOM 980 C CZ3 . TRP A 1 123 ? 41.690 4.731 0.648 1.00 17.63 ? 123 TRP A CZ3 1 ATOM 981 C CH2 . TRP A 1 123 ? 41.945 4.418 -0.728 1.00 18.17 ? 123 TRP A CH2 1 ATOM 982 N N . THR A 1 124 ? 45.325 4.713 6.209 1.00 15.28 ? 124 THR A N 1 ATOM 983 C CA . THR A 1 124 ? 45.513 4.660 7.651 1.00 16.70 ? 124 THR A CA 1 ATOM 984 C C . THR A 1 124 ? 44.270 4.089 8.286 1.00 16.46 ? 124 THR A C 1 ATOM 985 O O . THR A 1 124 ? 43.149 4.612 8.093 1.00 17.51 ? 124 THR A O 1 ATOM 986 C CB . THR A 1 124 ? 45.839 6.077 8.227 1.00 16.35 ? 124 THR A CB 1 ATOM 987 O OG1 . THR A 1 124 ? 47.057 6.547 7.604 1.00 18.77 ? 124 THR A OG1 1 ATOM 988 C CG2 . THR A 1 124 ? 46.103 6.007 9.778 1.00 20.58 ? 124 THR A CG2 1 ATOM 989 N N . VAL A 1 125 ? 44.455 3.005 9.058 1.00 17.12 ? 125 VAL A N 1 ATOM 990 C CA . VAL A 1 125 ? 43.354 2.347 9.755 1.00 18.20 ? 125 VAL A CA 1 ATOM 991 C C . VAL A 1 125 ? 43.254 3.006 11.126 1.00 18.06 ? 125 VAL A C 1 ATOM 992 O O . VAL A 1 125 ? 44.185 2.892 11.950 1.00 21.50 ? 125 VAL A O 1 ATOM 993 C CB . VAL A 1 125 ? 43.616 0.788 9.849 1.00 16.50 ? 125 VAL A CB 1 ATOM 994 C CG1 . VAL A 1 125 ? 42.519 0.071 10.689 1.00 20.69 ? 125 VAL A CG1 1 ATOM 995 C CG2 . VAL A 1 125 ? 43.793 0.170 8.448 1.00 17.65 ? 125 VAL A CG2 1 ATOM 996 N N . THR A 1 126 ? 42.151 3.715 11.385 1.00 18.64 ? 126 THR A N 1 ATOM 997 C CA . THR A 1 126 ? 42.095 4.556 12.574 1.00 19.97 ? 126 THR A CA 1 ATOM 998 C C . THR A 1 126 ? 40.662 4.972 12.897 1.00 17.28 ? 126 THR A C 1 ATOM 999 O O . THR A 1 126 ? 39.812 4.985 11.973 1.00 19.70 ? 126 THR A O 1 ATOM 1000 C CB . THR A 1 126 ? 42.959 5.837 12.365 1.00 19.02 ? 126 THR A CB 1 ATOM 1001 O OG1 . THR A 1 126 ? 42.940 6.652 13.546 1.00 19.93 ? 126 THR A OG1 1 ATOM 1002 C CG2 . THR A 1 126 ? 42.474 6.666 11.151 1.00 18.50 ? 126 THR A CG2 1 ATOM 1003 N N . ASN A 1 127 ? 40.389 5.342 14.170 1.00 18.52 ? 127 ASN A N 1 ATOM 1004 C CA . ASN A 1 127 ? 39.101 5.942 14.512 1.00 17.67 ? 127 ASN A CA 1 ATOM 1005 C C . ASN A 1 127 ? 39.123 7.464 14.441 1.00 21.29 ? 127 ASN A C 1 ATOM 1006 O O . ASN A 1 127 ? 38.065 8.091 14.425 1.00 24.12 ? 127 ASN A O 1 ATOM 1007 C CB . ASN A 1 127 ? 38.713 5.609 15.955 1.00 22.05 ? 127 ASN A CB 1 ATOM 1008 C CG . ASN A 1 127 ? 37.928 4.308 16.100 1.00 20.42 ? 127 ASN A CG 1 ATOM 1009 O OD1 . ASN A 1 127 ? 37.456 3.685 15.109 1.00 20.38 ? 127 ASN A OD1 1 ATOM 1010 N ND2 . ASN A 1 127 ? 37.775 3.879 17.364 1.00 27.08 ? 127 ASN A ND2 1 ATOM 1011 N N . ASN A 1 128 ? 40.329 8.055 14.422 1.00 19.80 ? 128 ASN A N 1 ATOM 1012 C CA . ASN A 1 128 ? 40.444 9.524 14.266 1.00 20.15 ? 128 ASN A CA 1 ATOM 1013 C C . ASN A 1 128 ? 40.417 9.879 12.784 1.00 19.88 ? 128 ASN A C 1 ATOM 1014 O O . ASN A 1 128 ? 41.397 9.659 12.066 1.00 22.05 ? 128 ASN A O 1 ATOM 1015 C CB . ASN A 1 128 ? 41.736 10.101 14.887 1.00 23.17 ? 128 ASN A CB 1 ATOM 1016 C CG . ASN A 1 128 ? 41.793 11.656 14.784 1.00 21.74 ? 128 ASN A CG 1 ATOM 1017 O OD1 . ASN A 1 128 ? 40.909 12.283 14.163 1.00 23.16 ? 128 ASN A OD1 1 ATOM 1018 N ND2 . ASN A 1 128 ? 42.800 12.287 15.461 1.00 24.30 ? 128 ASN A ND2 1 ATOM 1019 N N . VAL A 1 129 ? 39.315 10.442 12.330 1.00 20.16 ? 129 VAL A N 1 ATOM 1020 C CA . VAL A 1 129 ? 39.191 10.684 10.865 1.00 18.36 ? 129 VAL A CA 1 ATOM 1021 C C . VAL A 1 129 ? 39.680 12.101 10.466 1.00 20.50 ? 129 VAL A C 1 ATOM 1022 O O . VAL A 1 129 ? 39.480 12.541 9.311 1.00 21.70 ? 129 VAL A O 1 ATOM 1023 C CB . VAL A 1 129 ? 37.750 10.503 10.373 1.00 22.66 ? 129 VAL A CB 1 ATOM 1024 C CG1 . VAL A 1 129 ? 37.247 9.058 10.624 1.00 25.38 ? 129 VAL A CG1 1 ATOM 1025 C CG2 . VAL A 1 129 ? 36.842 11.565 10.912 1.00 23.00 ? 129 VAL A CG2 1 ATOM 1026 N N . LYS A 1 130 ? 40.332 12.808 11.389 1.00 18.49 ? 130 LYS A N 1 ATOM 1027 C CA . LYS A 1 130 ? 40.959 14.101 11.033 1.00 19.12 ? 130 LYS A CA 1 ATOM 1028 C C . LYS A 1 130 ? 42.491 13.946 11.005 1.00 21.73 ? 130 LYS A C 1 ATOM 1029 O O . LYS A 1 130 ? 43.047 13.141 11.751 1.00 22.32 ? 130 LYS A O 1 ATOM 1030 C CB . LYS A 1 130 ? 40.598 15.182 12.037 1.00 21.85 ? 130 LYS A CB 1 ATOM 1031 C CG . LYS A 1 130 ? 39.109 15.363 12.141 1.00 26.81 ? 130 LYS A CG 1 ATOM 1032 C CD . LYS A 1 130 ? 38.686 16.656 12.716 1.00 42.17 ? 130 LYS A CD 1 ATOM 1033 C CE . LYS A 1 130 ? 37.170 16.806 12.424 1.00 51.10 ? 130 LYS A CE 1 ATOM 1034 N NZ . LYS A 1 130 ? 36.859 16.719 10.951 1.00 53.50 ? 130 LYS A NZ 1 ATOM 1035 N N . PRO A 1 131 ? 43.155 14.670 10.101 1.00 20.73 ? 131 PRO A N 1 ATOM 1036 C CA . PRO A 1 131 ? 44.630 14.615 10.018 1.00 20.62 ? 131 PRO A CA 1 ATOM 1037 C C . PRO A 1 131 ? 45.207 14.986 11.364 1.00 20.88 ? 131 PRO A C 1 ATOM 1038 O O . PRO A 1 131 ? 44.625 15.788 12.062 1.00 20.95 ? 131 PRO A O 1 ATOM 1039 C CB . PRO A 1 131 ? 44.950 15.724 9.044 1.00 21.27 ? 131 PRO A CB 1 ATOM 1040 C CG . PRO A 1 131 ? 43.727 15.866 8.165 1.00 25.86 ? 131 PRO A CG 1 ATOM 1041 C CD . PRO A 1 131 ? 42.550 15.568 9.082 1.00 22.16 ? 131 PRO A CD 1 ATOM 1042 N N A ILE A 1 132 ? 46.318 14.370 11.768 0.50 20.03 ? 132 ILE A N 1 ATOM 1043 N N B ILE A 1 132 ? 46.345 14.395 11.692 0.50 20.72 ? 132 ILE A N 1 ATOM 1044 C CA A ILE A 1 132 ? 46.957 14.747 13.031 0.50 20.16 ? 132 ILE A CA 1 ATOM 1045 C CA B ILE A 1 132 ? 47.054 14.686 12.916 0.50 21.26 ? 132 ILE A CA 1 ATOM 1046 C C A ILE A 1 132 ? 47.920 15.905 12.737 0.50 15.65 ? 132 ILE A C 1 ATOM 1047 C C B ILE A 1 132 ? 47.864 15.973 12.636 0.50 18.69 ? 132 ILE A C 1 ATOM 1048 O O A ILE A 1 132 ? 48.755 15.821 11.811 0.50 18.42 ? 132 ILE A O 1 ATOM 1049 O O B ILE A 1 132 ? 48.509 16.067 11.577 0.50 21.30 ? 132 ILE A O 1 ATOM 1050 C CB A ILE A 1 132 ? 47.786 13.624 13.663 0.50 23.33 ? 132 ILE A CB 1 ATOM 1051 C CB B ILE A 1 132 ? 47.962 13.482 13.272 0.50 21.28 ? 132 ILE A CB 1 ATOM 1052 C CG1 A ILE A 1 132 ? 46.962 12.328 13.809 0.50 28.09 ? 132 ILE A CG1 1 ATOM 1053 C CG1 B ILE A 1 132 ? 47.099 12.215 13.528 0.50 24.66 ? 132 ILE A CG1 1 ATOM 1054 C CG2 A ILE A 1 132 ? 48.413 14.120 15.013 0.50 19.67 ? 132 ILE A CG2 1 ATOM 1055 C CG2 B ILE A 1 132 ? 48.923 13.832 14.432 0.50 22.91 ? 132 ILE A CG2 1 ATOM 1056 C CD1 A ILE A 1 132 ? 47.844 11.081 13.768 0.50 31.32 ? 132 ILE A CD1 1 ATOM 1057 C CD1 B ILE A 1 132 ? 45.840 12.460 14.344 0.50 23.73 ? 132 ILE A CD1 1 ATOM 1058 N N . VAL A 1 133 ? 47.794 16.971 13.529 1.00 18.92 ? 133 VAL A N 1 ATOM 1059 C CA . VAL A 1 133 ? 48.563 18.216 13.321 1.00 18.82 ? 133 VAL A CA 1 ATOM 1060 C C . VAL A 1 133 ? 49.711 18.311 14.329 1.00 19.25 ? 133 VAL A C 1 ATOM 1061 O O . VAL A 1 133 ? 49.485 18.262 15.552 1.00 21.06 ? 133 VAL A O 1 ATOM 1062 C CB . VAL A 1 133 ? 47.714 19.456 13.356 1.00 21.92 ? 133 VAL A CB 1 ATOM 1063 C CG1 . VAL A 1 133 ? 48.540 20.675 12.893 1.00 23.81 ? 133 VAL A CG1 1 ATOM 1064 C CG2 . VAL A 1 133 ? 46.475 19.310 12.380 1.00 22.67 ? 133 VAL A CG2 1 ATOM 1065 N N . ALA A 1 134 ? 50.944 18.428 13.807 1.00 15.47 ? 134 ALA A N 1 ATOM 1066 C CA . ALA A 1 134 ? 52.136 18.258 14.622 1.00 16.42 ? 134 ALA A CA 1 ATOM 1067 C C . ALA A 1 134 ? 53.311 19.079 14.073 1.00 16.81 ? 134 ALA A C 1 ATOM 1068 O O . ALA A 1 134 ? 53.385 19.341 12.848 1.00 19.09 ? 134 ALA A O 1 ATOM 1069 C CB . ALA A 1 134 ? 52.544 16.812 14.643 1.00 18.65 ? 134 ALA A CB 1 ATOM 1070 N N A SER A 1 135 ? 54.253 19.435 14.947 0.50 18.18 ? 135 SER A N 1 ATOM 1071 N N B SER A 1 135 ? 54.230 19.458 14.970 0.50 15.54 ? 135 SER A N 1 ATOM 1072 C CA A SER A 1 135 ? 55.564 19.876 14.490 0.50 17.62 ? 135 SER A CA 1 ATOM 1073 C CA B SER A 1 135 ? 55.576 19.870 14.581 0.50 11.87 ? 135 SER A CA 1 ATOM 1074 C C A SER A 1 135 ? 56.463 18.648 14.308 0.50 17.20 ? 135 SER A C 1 ATOM 1075 C C B SER A 1 135 ? 56.352 18.586 14.194 0.50 11.65 ? 135 SER A C 1 ATOM 1076 O O A SER A 1 135 ? 56.312 17.618 15.003 0.50 20.24 ? 135 SER A O 1 ATOM 1077 O O B SER A 1 135 ? 55.999 17.455 14.642 0.50 13.29 ? 135 SER A O 1 ATOM 1078 C CB A SER A 1 135 ? 56.181 20.843 15.488 0.50 22.67 ? 135 SER A CB 1 ATOM 1079 C CB B SER A 1 135 ? 56.275 20.605 15.745 0.50 12.22 ? 135 SER A CB 1 ATOM 1080 O OG A SER A 1 135 ? 56.164 20.269 16.773 0.50 27.33 ? 135 SER A OG 1 ATOM 1081 O OG B SER A 1 135 ? 55.563 21.750 16.205 0.50 15.31 ? 135 SER A OG 1 ATOM 1082 N N . ILE A 1 136 ? 57.386 18.743 13.355 1.00 16.32 ? 136 ILE A N 1 ATOM 1083 C CA . ILE A 1 136 ? 58.302 17.651 13.082 1.00 14.84 ? 136 ILE A CA 1 ATOM 1084 C C . ILE A 1 136 ? 59.658 18.140 13.546 1.00 17.33 ? 136 ILE A C 1 ATOM 1085 O O . ILE A 1 136 ? 60.237 19.086 12.957 1.00 17.84 ? 136 ILE A O 1 ATOM 1086 C CB . ILE A 1 136 ? 58.269 17.250 11.576 1.00 16.11 ? 136 ILE A CB 1 ATOM 1087 C CG1 . ILE A 1 136 ? 56.915 16.647 11.200 1.00 17.84 ? 136 ILE A CG1 1 ATOM 1088 C CG2 . ILE A 1 136 ? 59.448 16.301 11.245 1.00 18.41 ? 136 ILE A CG2 1 ATOM 1089 C CD1 . ILE A 1 136 ? 56.786 16.421 9.659 1.00 19.11 ? 136 ILE A CD1 1 ATOM 1090 N N . VAL A 1 137 ? 60.131 17.565 14.661 1.00 15.38 ? 137 VAL A N 1 ATOM 1091 C CA . VAL A 1 137 ? 61.376 18.047 15.265 1.00 15.81 ? 137 VAL A CA 1 ATOM 1092 C C . VAL A 1 137 ? 62.521 17.097 14.875 1.00 16.70 ? 137 VAL A C 1 ATOM 1093 O O . VAL A 1 137 ? 62.380 15.859 14.985 1.00 18.63 ? 137 VAL A O 1 ATOM 1094 C CB . VAL A 1 137 ? 61.235 18.035 16.814 1.00 16.81 ? 137 VAL A CB 1 ATOM 1095 C CG1 . VAL A 1 137 ? 62.555 18.481 17.488 1.00 21.33 ? 137 VAL A CG1 1 ATOM 1096 C CG2 . VAL A 1 137 ? 59.983 18.857 17.288 1.00 19.80 ? 137 VAL A CG2 1 ATOM 1097 N N . GLY A 1 138 ? 63.653 17.678 14.475 1.00 16.70 ? 138 GLY A N 1 ATOM 1098 C CA . GLY A 1 138 ? 64.766 16.903 13.980 1.00 18.62 ? 138 GLY A CA 1 ATOM 1099 C C . GLY A 1 138 ? 66.092 17.318 14.557 1.00 17.56 ? 138 GLY A C 1 ATOM 1100 O O . GLY A 1 138 ? 66.195 17.697 15.741 1.00 19.63 ? 138 GLY A O 1 ATOM 1101 N N . TYR A 1 139 ? 67.072 17.347 13.651 1.00 18.69 ? 139 TYR A N 1 ATOM 1102 C CA . TYR A 1 139 ? 68.444 17.618 13.966 1.00 18.85 ? 139 TYR A CA 1 ATOM 1103 C C . TYR A 1 139 ? 68.582 18.885 14.815 1.00 18.09 ? 139 TYR A C 1 ATOM 1104 O O . TYR A 1 139 ? 67.954 19.905 14.506 1.00 18.82 ? 139 TYR A O 1 ATOM 1105 C CB . TYR A 1 139 ? 69.212 17.724 12.652 1.00 20.93 ? 139 TYR A CB 1 ATOM 1106 C CG . TYR A 1 139 ? 70.680 17.926 12.829 1.00 18.20 ? 139 TYR A CG 1 ATOM 1107 C CD1 . TYR A 1 139 ? 71.321 19.048 12.277 1.00 20.69 ? 139 TYR A CD1 1 ATOM 1108 C CD2 . TYR A 1 139 ? 71.457 16.973 13.534 1.00 20.68 ? 139 TYR A CD2 1 ATOM 1109 C CE1 . TYR A 1 139 ? 72.716 19.246 12.447 1.00 23.34 ? 139 TYR A CE1 1 ATOM 1110 C CE2 . TYR A 1 139 ? 72.849 17.179 13.707 1.00 20.17 ? 139 TYR A CE2 1 ATOM 1111 C CZ . TYR A 1 139 ? 73.444 18.305 13.126 1.00 20.33 ? 139 TYR A CZ 1 ATOM 1112 O OH . TYR A 1 139 ? 74.820 18.561 13.258 1.00 26.49 ? 139 TYR A OH 1 ATOM 1113 N N . LYS A 1 140 ? 69.418 18.803 15.884 1.00 20.17 ? 140 LYS A N 1 ATOM 1114 C CA . LYS A 1 140 ? 69.633 19.953 16.808 1.00 20.97 ? 140 LYS A CA 1 ATOM 1115 C C . LYS A 1 140 ? 68.374 20.436 17.515 1.00 19.49 ? 140 LYS A C 1 ATOM 1116 O O . LYS A 1 140 ? 68.334 21.584 18.009 1.00 21.17 ? 140 LYS A O 1 ATOM 1117 C CB . LYS A 1 140 ? 70.377 21.091 16.090 1.00 22.17 ? 140 LYS A CB 1 ATOM 1118 C CG . LYS A 1 140 ? 71.782 20.672 15.665 1.00 24.97 ? 140 LYS A CG 1 ATOM 1119 C CD . LYS A 1 140 ? 72.510 21.859 15.116 1.00 27.31 ? 140 LYS A CD 1 ATOM 1120 C CE . LYS A 1 140 ? 74.014 21.580 14.886 1.00 38.52 ? 140 LYS A CE 1 ATOM 1121 N NZ . LYS A 1 140 ? 74.657 21.147 16.165 1.00 48.95 ? 140 LYS A NZ 1 ATOM 1122 N N . GLU A 1 141 ? 67.340 19.571 17.561 1.00 18.40 ? 141 GLU A N 1 ATOM 1123 C CA . GLU A 1 141 ? 66.043 19.910 18.160 1.00 17.85 ? 141 GLU A CA 1 ATOM 1124 C C . GLU A 1 141 ? 65.376 21.073 17.422 1.00 18.91 ? 141 GLU A C 1 ATOM 1125 O O . GLU A 1 141 ? 64.506 21.773 17.975 1.00 21.23 ? 141 GLU A O 1 ATOM 1126 C CB . GLU A 1 141 ? 66.068 20.102 19.687 1.00 20.96 ? 141 GLU A CB 1 ATOM 1127 C CG . GLU A 1 141 ? 66.744 18.976 20.468 1.00 22.05 ? 141 GLU A CG 1 ATOM 1128 C CD . GLU A 1 141 ? 66.182 17.601 20.187 1.00 34.50 ? 141 GLU A CD 1 ATOM 1129 O OE1 . GLU A 1 141 ? 66.973 16.689 19.784 1.00 42.96 ? 141 GLU A OE1 1 ATOM 1130 O OE2 . GLU A 1 141 ? 64.952 17.436 20.343 1.00 35.98 ? 141 GLU A OE2 1 ATOM 1131 N N A MET A 1 142 ? 65.740 21.222 16.147 0.50 17.87 ? 142 MET A N 1 ATOM 1132 N N B MET A 1 142 ? 65.728 21.232 16.146 0.50 15.59 ? 142 MET A N 1 ATOM 1133 C CA A MET A 1 142 ? 65.116 22.222 15.270 0.50 20.88 ? 142 MET A CA 1 ATOM 1134 C CA B MET A 1 142 ? 65.061 22.252 15.317 0.50 15.89 ? 142 MET A CA 1 ATOM 1135 C C A MET A 1 142 ? 63.787 21.671 14.756 0.50 17.59 ? 142 MET A C 1 ATOM 1136 C C B MET A 1 142 ? 63.859 21.642 14.608 0.50 16.55 ? 142 MET A C 1 ATOM 1137 O O A MET A 1 142 ? 63.483 20.500 14.969 0.50 17.75 ? 142 MET A O 1 ATOM 1138 O O B MET A 1 142 ? 63.715 20.414 14.533 0.50 15.36 ? 142 MET A O 1 ATOM 1139 C CB A MET A 1 142 ? 66.049 22.529 14.087 0.50 24.14 ? 142 MET A CB 1 ATOM 1140 C CB B MET A 1 142 ? 66.042 22.886 14.315 0.50 13.88 ? 142 MET A CB 1 ATOM 1141 C CG A MET A 1 142 ? 67.418 22.966 14.504 0.50 33.53 ? 142 MET A CG 1 ATOM 1142 C CG B MET A 1 142 ? 67.201 23.484 15.028 0.50 13.02 ? 142 MET A CG 1 ATOM 1143 S SD A MET A 1 142 ? 67.524 24.740 14.620 0.50 44.42 ? 142 MET A SD 1 ATOM 1144 S SD B MET A 1 142 ? 68.485 24.137 13.917 0.50 13.98 ? 142 MET A SD 1 ATOM 1145 C CE A MET A 1 142 ? 67.811 25.195 12.914 0.50 41.27 ? 142 MET A CE 1 ATOM 1146 C CE B MET A 1 142 ? 67.548 25.468 13.146 0.50 13.14 ? 142 MET A CE 1 ATOM 1147 N N . CYS A 1 143 ? 63.011 22.501 14.064 1.00 17.57 ? 143 CYS A N 1 ATOM 1148 C CA . CYS A 1 143 ? 61.733 22.102 13.455 1.00 16.54 ? 143 CYS A CA 1 ATOM 1149 C C . CYS A 1 143 ? 61.780 22.209 11.940 1.00 17.66 ? 143 CYS A C 1 ATOM 1150 O O . CYS A 1 143 ? 62.301 23.177 11.368 1.00 17.94 ? 143 CYS A O 1 ATOM 1151 C CB . CYS A 1 143 ? 60.612 23.000 13.990 1.00 19.02 ? 143 CYS A CB 1 ATOM 1152 S SG . CYS A 1 143 ? 59.890 22.457 15.587 1.00 19.94 ? 143 CYS A SG 1 ATOM 1153 N N . LEU A 1 144 ? 61.217 21.199 11.283 1.00 17.53 ? 144 LEU A N 1 ATOM 1154 C CA . LEU A 1 144 ? 61.068 21.237 9.840 1.00 16.50 ? 144 LEU A CA 1 ATOM 1155 C C . LEU A 1 144 ? 60.027 22.321 9.480 1.00 15.73 ? 144 LEU A C 1 ATOM 1156 O O . LEU A 1 144 ? 58.933 22.396 10.076 1.00 17.58 ? 144 LEU A O 1 ATOM 1157 C CB . LEU A 1 144 ? 60.538 19.876 9.338 1.00 17.03 ? 144 LEU A CB 1 ATOM 1158 C CG . LEU A 1 144 ? 60.502 19.660 7.796 1.00 16.57 ? 144 LEU A CG 1 ATOM 1159 C CD1 . LEU A 1 144 ? 61.970 19.672 7.265 1.00 20.02 ? 144 LEU A CD1 1 ATOM 1160 C CD2 . LEU A 1 144 ? 59.774 18.371 7.423 1.00 19.44 ? 144 LEU A CD2 1 ATOM 1161 N N . GLN A 1 145 ? 60.343 23.132 8.470 1.00 19.12 ? 145 GLN A N 1 ATOM 1162 C CA . GLN A 1 145 ? 59.467 24.245 8.144 1.00 18.73 ? 145 GLN A CA 1 ATOM 1163 C C . GLN A 1 145 ? 59.235 24.353 6.648 1.00 19.44 ? 145 GLN A C 1 ATOM 1164 O O . GLN A 1 145 ? 60.152 24.151 5.842 1.00 18.40 ? 145 GLN A O 1 ATOM 1165 C CB . GLN A 1 145 ? 60.149 25.547 8.640 1.00 21.00 ? 145 GLN A CB 1 ATOM 1166 C CG . GLN A 1 145 ? 59.225 26.746 8.455 1.00 21.99 ? 145 GLN A CG 1 ATOM 1167 C CD . GLN A 1 145 ? 59.909 27.956 8.912 1.00 26.15 ? 145 GLN A CD 1 ATOM 1168 O OE1 . GLN A 1 145 ? 60.117 28.166 10.144 1.00 22.56 ? 145 GLN A OE1 1 ATOM 1169 N NE2 . GLN A 1 145 ? 60.364 28.793 7.914 1.00 28.47 ? 145 GLN A NE2 1 ATOM 1170 N N A SER A 1 146 ? 58.009 24.712 6.311 0.50 19.60 ? 146 SER A N 1 ATOM 1171 N N B SER A 1 146 ? 57.999 24.657 6.253 0.50 17.30 ? 146 SER A N 1 ATOM 1172 C CA A SER A 1 146 ? 57.620 25.020 4.961 0.50 21.85 ? 146 SER A CA 1 ATOM 1173 C CA B SER A 1 146 ? 57.708 24.950 4.845 0.50 16.48 ? 146 SER A CA 1 ATOM 1174 C C A SER A 1 146 ? 58.086 26.427 4.585 0.50 19.52 ? 146 SER A C 1 ATOM 1175 C C B SER A 1 146 ? 57.894 26.430 4.541 0.50 18.58 ? 146 SER A C 1 ATOM 1176 O O A SER A 1 146 ? 58.308 27.256 5.473 0.50 21.04 ? 146 SER A O 1 ATOM 1177 O O B SER A 1 146 ? 57.700 27.298 5.399 0.50 19.07 ? 146 SER A O 1 ATOM 1178 C CB A SER A 1 146 ? 56.108 24.966 4.903 0.50 24.66 ? 146 SER A CB 1 ATOM 1179 C CB B SER A 1 146 ? 56.289 24.517 4.432 0.50 13.98 ? 146 SER A CB 1 ATOM 1180 O OG A SER A 1 146 ? 55.660 25.453 3.670 0.50 30.58 ? 146 SER A OG 1 ATOM 1181 O OG B SER A 1 146 ? 55.285 25.194 5.190 0.50 17.65 ? 146 SER A OG 1 ATOM 1182 N N . ASN A 1 147 ? 58.201 26.691 3.270 1.00 23.01 ? 147 ASN A N 1 ATOM 1183 C CA . ASN A 1 147 ? 58.535 28.036 2.771 1.00 22.15 ? 147 ASN A CA 1 ATOM 1184 C C . ASN A 1 147 ? 57.841 28.351 1.462 1.00 25.56 ? 147 ASN A C 1 ATOM 1185 O O . ASN A 1 147 ? 58.366 29.134 0.650 1.00 24.51 ? 147 ASN A O 1 ATOM 1186 C CB . ASN A 1 147 ? 60.059 28.123 2.629 1.00 26.99 ? 147 ASN A CB 1 ATOM 1187 C CG . ASN A 1 147 ? 60.742 27.849 3.936 1.00 28.75 ? 147 ASN A CG 1 ATOM 1188 O OD1 . ASN A 1 147 ? 60.714 28.686 4.863 1.00 26.36 ? 147 ASN A OD1 1 ATOM 1189 N ND2 . ASN A 1 147 ? 61.285 26.638 4.073 1.00 24.02 ? 147 ASN A ND2 1 ATOM 1190 N N . GLY A 1 148 ? 56.645 27.789 1.294 1.00 25.16 ? 148 GLY A N 1 ATOM 1191 C CA . GLY A 1 148 ? 55.795 28.059 0.139 1.00 30.12 ? 148 GLY A CA 1 ATOM 1192 C C . GLY A 1 148 ? 55.923 27.021 -0.960 1.00 26.93 ? 148 GLY A C 1 ATOM 1193 O O . GLY A 1 148 ? 56.934 26.332 -1.036 1.00 25.46 ? 148 GLY A O 1 ATOM 1194 N N . GLU A 1 149 ? 54.915 26.968 -1.832 1.00 26.31 ? 149 GLU A N 1 ATOM 1195 C CA . GLU A 1 149 ? 54.851 26.064 -2.983 1.00 25.80 ? 149 GLU A CA 1 ATOM 1196 C C . GLU A 1 149 ? 56.061 26.262 -3.878 1.00 20.84 ? 149 GLU A C 1 ATOM 1197 O O . GLU A 1 149 ? 56.526 27.410 -4.064 1.00 25.44 ? 149 GLU A O 1 ATOM 1198 C CB . GLU A 1 149 ? 53.529 26.248 -3.757 1.00 22.35 ? 149 GLU A CB 1 ATOM 1199 C CG . GLU A 1 149 ? 53.249 25.261 -4.853 1.00 25.44 ? 149 GLU A CG 1 ATOM 1200 C CD . GLU A 1 149 ? 51.909 25.563 -5.580 1.00 24.30 ? 149 GLU A CD 1 ATOM 1201 O OE1 . GLU A 1 149 ? 51.139 26.454 -5.131 1.00 35.77 ? 149 GLU A OE1 1 ATOM 1202 O OE2 . GLU A 1 149 ? 51.663 24.922 -6.604 1.00 36.64 ? 149 GLU A OE2 1 ATOM 1203 N N . ASN A 1 150 ? 56.590 25.127 -4.349 1.00 22.00 ? 150 ASN A N 1 ATOM 1204 C CA . ASN A 1 150 ? 57.795 25.074 -5.214 1.00 19.81 ? 150 ASN A CA 1 ATOM 1205 C C . ASN A 1 150 ? 59.117 25.399 -4.526 1.00 23.50 ? 150 ASN A C 1 ATOM 1206 O O . ASN A 1 150 ? 60.149 25.330 -5.180 1.00 27.23 ? 150 ASN A O 1 ATOM 1207 C CB . ASN A 1 150 ? 57.634 25.935 -6.499 1.00 25.03 ? 150 ASN A CB 1 ATOM 1208 C CG . ASN A 1 150 ? 56.417 25.495 -7.358 1.00 23.72 ? 150 ASN A CG 1 ATOM 1209 O OD1 . ASN A 1 150 ? 55.449 26.249 -7.460 1.00 34.76 ? 150 ASN A OD1 1 ATOM 1210 N ND2 . ASN A 1 150 ? 56.469 24.269 -7.936 1.00 30.59 ? 150 ASN A ND2 1 ATOM 1211 N N A ASN A 1 151 ? 59.077 25.664 -3.216 0.50 19.09 ? 151 ASN A N 1 ATOM 1212 N N B ASN A 1 151 ? 59.102 25.788 -3.244 0.50 20.46 ? 151 ASN A N 1 ATOM 1213 C CA A ASN A 1 151 ? 60.259 25.986 -2.438 0.50 16.79 ? 151 ASN A CA 1 ATOM 1214 C CA B ASN A 1 151 ? 60.348 26.012 -2.506 0.50 21.25 ? 151 ASN A CA 1 ATOM 1215 C C A ASN A 1 151 ? 60.735 24.909 -1.475 0.50 14.82 ? 151 ASN A C 1 ATOM 1216 C C B ASN A 1 151 ? 60.799 24.803 -1.701 0.50 21.35 ? 151 ASN A C 1 ATOM 1217 O O A ASN A 1 151 ? 59.930 24.104 -0.998 0.50 17.52 ? 151 ASN A O 1 ATOM 1218 O O B ASN A 1 151 ? 60.038 23.828 -1.552 0.50 17.34 ? 151 ASN A O 1 ATOM 1219 C CB A ASN A 1 151 ? 59.960 27.197 -1.588 0.50 18.33 ? 151 ASN A CB 1 ATOM 1220 C CB B ASN A 1 151 ? 60.241 27.219 -1.556 0.50 22.00 ? 151 ASN A CB 1 ATOM 1221 C CG A ASN A 1 151 ? 61.139 28.083 -1.420 0.50 17.03 ? 151 ASN A CG 1 ATOM 1222 C CG B ASN A 1 151 ? 59.986 28.530 -2.290 0.50 26.53 ? 151 ASN A CG 1 ATOM 1223 O OD1 A ASN A 1 151 ? 62.282 27.714 -1.747 0.50 20.24 ? 151 ASN A OD1 1 ATOM 1224 O OD1 B ASN A 1 151 ? 60.413 28.715 -3.432 0.50 25.47 ? 151 ASN A OD1 1 ATOM 1225 N ND2 A ASN A 1 151 ? 60.890 29.265 -0.871 0.50 20.13 ? 151 ASN A ND2 1 ATOM 1226 N ND2 B ASN A 1 151 ? 59.292 29.446 -1.638 0.50 26.32 ? 151 ASN A ND2 1 ATOM 1227 N N . GLY A 1 152 ? 62.047 24.851 -1.222 1.00 19.04 ? 152 GLY A N 1 ATOM 1228 C CA . GLY A 1 152 ? 62.556 23.807 -0.311 1.00 19.21 ? 152 GLY A CA 1 ATOM 1229 C C . GLY A 1 152 ? 61.948 23.900 1.086 1.00 21.32 ? 152 GLY A C 1 ATOM 1230 O O . GLY A 1 152 ? 61.548 24.987 1.579 1.00 25.47 ? 152 GLY A O 1 ATOM 1231 N N . VAL A 1 153 ? 61.909 22.758 1.761 1.00 18.03 ? 153 VAL A N 1 ATOM 1232 C CA . VAL A 1 153 ? 61.657 22.803 3.215 1.00 16.98 ? 153 VAL A CA 1 ATOM 1233 C C . VAL A 1 153 ? 63.030 22.958 3.892 1.00 20.63 ? 153 VAL A C 1 ATOM 1234 O O . VAL A 1 153 ? 64.050 22.593 3.296 1.00 21.33 ? 153 VAL A O 1 ATOM 1235 C CB . VAL A 1 153 ? 60.913 21.540 3.706 1.00 19.10 ? 153 VAL A CB 1 ATOM 1236 C CG1 . VAL A 1 153 ? 59.501 21.459 3.077 1.00 17.71 ? 153 VAL A CG1 1 ATOM 1237 C CG2 . VAL A 1 153 ? 61.725 20.262 3.399 1.00 19.56 ? 153 VAL A CG2 1 ATOM 1238 N N . TRP A 1 154 ? 63.077 23.408 5.138 1.00 18.52 ? 154 TRP A N 1 ATOM 1239 C CA . TRP A 1 154 ? 64.349 23.487 5.863 1.00 17.48 ? 154 TRP A CA 1 ATOM 1240 C C . TRP A 1 154 ? 64.135 23.613 7.379 1.00 18.16 ? 154 TRP A C 1 ATOM 1241 O O . TRP A 1 154 ? 63.000 23.672 7.854 1.00 18.43 ? 154 TRP A O 1 ATOM 1242 C CB . TRP A 1 154 ? 65.314 24.554 5.323 1.00 23.89 ? 154 TRP A CB 1 ATOM 1243 C CG . TRP A 1 154 ? 64.808 25.898 5.163 1.00 24.33 ? 154 TRP A CG 1 ATOM 1244 C CD1 . TRP A 1 154 ? 64.643 26.833 6.136 1.00 28.80 ? 154 TRP A CD1 1 ATOM 1245 C CD2 . TRP A 1 154 ? 64.469 26.542 3.912 1.00 28.21 ? 154 TRP A CD2 1 ATOM 1246 N NE1 . TRP A 1 154 ? 64.193 28.010 5.576 1.00 30.65 ? 154 TRP A NE1 1 ATOM 1247 C CE2 . TRP A 1 154 ? 64.083 27.859 4.218 1.00 31.59 ? 154 TRP A CE2 1 ATOM 1248 C CE3 . TRP A 1 154 ? 64.420 26.118 2.578 1.00 26.17 ? 154 TRP A CE3 1 ATOM 1249 C CZ2 . TRP A 1 154 ? 63.685 28.784 3.228 1.00 35.42 ? 154 TRP A CZ2 1 ATOM 1250 C CZ3 . TRP A 1 154 ? 64.027 27.038 1.582 1.00 31.63 ? 154 TRP A CZ3 1 ATOM 1251 C CH2 . TRP A 1 154 ? 63.649 28.343 1.913 1.00 30.55 ? 154 TRP A CH2 1 ATOM 1252 N N . MET A 1 155 ? 65.234 23.556 8.141 1.00 17.11 ? 155 MET A N 1 ATOM 1253 C CA . MET A 1 155 ? 65.147 23.574 9.610 1.00 17.21 ? 155 MET A CA 1 ATOM 1254 C C . MET A 1 155 ? 65.175 24.987 10.149 1.00 19.11 ? 155 MET A C 1 ATOM 1255 O O . MET A 1 155 ? 65.922 25.831 9.609 1.00 21.95 ? 155 MET A O 1 ATOM 1256 C CB . MET A 1 155 ? 66.332 22.829 10.231 1.00 19.11 ? 155 MET A CB 1 ATOM 1257 C CG . MET A 1 155 ? 66.521 21.393 9.728 1.00 17.83 ? 155 MET A CG 1 ATOM 1258 S SD . MET A 1 155 ? 64.993 20.388 9.899 1.00 19.52 ? 155 MET A SD 1 ATOM 1259 C CE . MET A 1 155 ? 64.947 20.263 11.703 1.00 20.60 ? 155 MET A CE 1 ATOM 1260 N N A GLU A 1 156 ? 64.389 25.217 11.208 0.50 18.71 ? 156 GLU A N 1 ATOM 1261 N N B GLU A 1 156 ? 64.326 25.273 11.159 0.50 17.74 ? 156 GLU A N 1 ATOM 1262 C CA A GLU A 1 156 ? 64.423 26.499 11.891 0.50 17.74 ? 156 GLU A CA 1 ATOM 1263 C CA B GLU A 1 156 ? 64.338 26.591 11.848 0.50 17.67 ? 156 GLU A CA 1 ATOM 1264 C C A GLU A 1 156 ? 64.265 26.246 13.393 0.50 23.52 ? 156 GLU A C 1 ATOM 1265 C C B GLU A 1 156 ? 64.047 26.373 13.329 0.50 19.39 ? 156 GLU A C 1 ATOM 1266 O O A GLU A 1 156 ? 63.894 25.159 13.808 0.50 15.37 ? 156 GLU A O 1 ATOM 1267 O O B GLU A 1 156 ? 63.440 25.356 13.673 0.50 12.75 ? 156 GLU A O 1 ATOM 1268 C CB A GLU A 1 156 ? 63.322 27.420 11.312 0.50 17.26 ? 156 GLU A CB 1 ATOM 1269 C CB B GLU A 1 156 ? 63.275 27.536 11.257 0.50 19.91 ? 156 GLU A CB 1 ATOM 1270 C CG A GLU A 1 156 ? 63.250 28.825 11.942 0.50 14.82 ? 156 GLU A CG 1 ATOM 1271 C CG B GLU A 1 156 ? 63.438 27.936 9.814 0.50 21.20 ? 156 GLU A CG 1 ATOM 1272 C CD A GLU A 1 156 ? 64.597 29.548 11.844 0.50 23.57 ? 156 GLU A CD 1 ATOM 1273 C CD B GLU A 1 156 ? 64.648 28.852 9.538 0.50 27.17 ? 156 GLU A CD 1 ATOM 1274 O OE1 A GLU A 1 156 ? 65.478 29.456 12.777 0.50 19.64 ? 156 GLU A OE1 1 ATOM 1275 O OE1 B GLU A 1 156 ? 65.017 28.988 8.345 0.50 26.43 ? 156 GLU A OE1 1 ATOM 1276 O OE2 A GLU A 1 156 ? 64.746 30.196 10.794 0.50 22.76 ? 156 GLU A OE2 1 ATOM 1277 O OE2 B GLU A 1 156 ? 65.220 29.439 10.485 0.50 25.65 ? 156 GLU A OE2 1 ATOM 1278 N N . ASP A 1 157 ? 64.527 27.242 14.232 1.00 18.02 ? 157 ASP A N 1 ATOM 1279 C CA . ASP A 1 157 ? 64.267 27.075 15.689 1.00 17.83 ? 157 ASP A CA 1 ATOM 1280 C C . ASP A 1 157 ? 62.762 26.866 15.862 1.00 18.37 ? 157 ASP A C 1 ATOM 1281 O O . ASP A 1 157 ? 61.967 27.588 15.242 1.00 20.48 ? 157 ASP A O 1 ATOM 1282 C CB . ASP A 1 157 ? 64.708 28.299 16.499 1.00 20.42 ? 157 ASP A CB 1 ATOM 1283 C CG . ASP A 1 157 ? 66.211 28.496 16.477 1.00 23.22 ? 157 ASP A CG 1 ATOM 1284 O OD1 . ASP A 1 157 ? 66.961 27.503 16.353 1.00 24.45 ? 157 ASP A OD1 1 ATOM 1285 O OD2 . ASP A 1 157 ? 66.645 29.649 16.665 1.00 29.39 ? 157 ASP A OD2 1 ATOM 1286 N N . CYS A 1 158 ? 62.361 25.885 16.673 1.00 17.30 ? 158 CYS A N 1 ATOM 1287 C CA . CYS A 1 158 ? 60.913 25.637 16.860 1.00 17.74 ? 158 CYS A CA 1 ATOM 1288 C C . CYS A 1 158 ? 60.219 26.820 17.518 1.00 21.18 ? 158 CYS A C 1 ATOM 1289 O O . CYS A 1 158 ? 60.755 27.356 18.512 1.00 24.38 ? 158 CYS A O 1 ATOM 1290 C CB . CYS A 1 158 ? 60.710 24.444 17.791 1.00 18.37 ? 158 CYS A CB 1 ATOM 1291 S SG . CYS A 1 158 ? 61.340 22.874 17.025 1.00 18.83 ? 158 CYS A SG 1 ATOM 1292 N N . GLU A 1 159 ? 59.013 27.148 17.035 1.00 22.40 ? 159 GLU A N 1 ATOM 1293 C CA . GLU A 1 159 ? 58.269 28.275 17.589 1.00 23.71 ? 159 GLU A CA 1 ATOM 1294 C C . GLU A 1 159 ? 56.806 27.824 17.572 1.00 22.22 ? 159 GLU A C 1 ATOM 1295 O O . GLU A 1 159 ? 56.277 27.512 16.514 1.00 24.46 ? 159 GLU A O 1 ATOM 1296 C CB . GLU A 1 159 ? 58.478 29.593 16.744 1.00 29.78 ? 159 GLU A CB 1 ATOM 1297 N N . ALA A 1 160 ? 56.177 27.826 18.739 1.00 26.00 ? 160 ALA A N 1 ATOM 1298 C CA . ALA A 1 160 ? 54.777 27.415 18.867 1.00 29.22 ? 160 ALA A CA 1 ATOM 1299 C C . ALA A 1 160 ? 53.835 28.165 17.886 1.00 27.91 ? 160 ALA A C 1 ATOM 1300 O O . ALA A 1 160 ? 52.817 27.584 17.421 1.00 30.95 ? 160 ALA A O 1 ATOM 1301 C CB . ALA A 1 160 ? 54.308 27.630 20.306 1.00 32.39 ? 160 ALA A CB 1 ATOM 1302 N N . THR A 1 161 ? 54.153 29.443 17.608 1.00 30.03 ? 161 THR A N 1 ATOM 1303 C CA . THR A 1 161 ? 53.424 30.335 16.674 1.00 28.29 ? 161 THR A CA 1 ATOM 1304 C C . THR A 1 161 ? 53.758 30.265 15.227 1.00 25.70 ? 161 THR A C 1 ATOM 1305 O O . THR A 1 161 ? 53.127 30.985 14.471 1.00 30.03 ? 161 THR A O 1 ATOM 1306 C CB . THR A 1 161 ? 53.594 31.884 17.056 1.00 30.53 ? 161 THR A CB 1 ATOM 1307 O OG1 . THR A 1 161 ? 54.969 32.325 16.865 1.00 32.40 ? 161 THR A OG1 1 ATOM 1308 C CG2 . THR A 1 161 ? 53.287 32.040 18.406 1.00 31.26 ? 161 THR A CG2 1 ATOM 1309 N N . SER A 1 162 ? 54.749 29.446 14.792 1.00 23.16 ? 162 SER A N 1 ATOM 1310 C CA . SER A 1 162 ? 55.097 29.446 13.369 1.00 25.49 ? 162 SER A CA 1 ATOM 1311 C C . SER A 1 162 ? 54.156 28.508 12.678 1.00 21.76 ? 162 SER A C 1 ATOM 1312 O O . SER A 1 162 ? 54.267 27.272 12.834 1.00 20.64 ? 162 SER A O 1 ATOM 1313 C CB . SER A 1 162 ? 56.563 29.000 13.067 1.00 22.12 ? 162 SER A CB 1 ATOM 1314 O OG . SER A 1 162 ? 56.661 28.750 11.636 1.00 28.57 ? 162 SER A OG 1 ATOM 1315 N N . LEU A 1 163 ? 53.230 29.056 11.887 1.00 24.55 ? 163 LEU A N 1 ATOM 1316 C CA . LEU A 1 163 ? 52.297 28.200 11.162 1.00 22.33 ? 163 LEU A CA 1 ATOM 1317 C C . LEU A 1 163 ? 53.013 27.347 10.111 1.00 21.06 ? 163 LEU A C 1 ATOM 1318 O O . LEU A 1 163 ? 52.533 26.254 9.789 1.00 22.31 ? 163 LEU A O 1 ATOM 1319 C CB . LEU A 1 163 ? 51.141 29.000 10.519 1.00 27.90 ? 163 LEU A CB 1 ATOM 1320 C CG . LEU A 1 163 ? 50.192 29.831 11.418 1.00 35.02 ? 163 LEU A CG 1 ATOM 1321 C CD1 . LEU A 1 163 ? 48.960 30.202 10.553 1.00 37.67 ? 163 LEU A CD1 1 ATOM 1322 C CD2 . LEU A 1 163 ? 49.729 29.110 12.577 1.00 30.67 ? 163 LEU A CD2 1 ATOM 1323 N N . GLN A 1 164 ? 54.135 27.836 9.557 1.00 24.23 ? 164 GLN A N 1 ATOM 1324 C CA . GLN A 1 164 ? 54.833 27.046 8.525 1.00 24.19 ? 164 GLN A CA 1 ATOM 1325 C C . GLN A 1 164 ? 55.632 25.876 9.132 1.00 20.33 ? 164 GLN A C 1 ATOM 1326 O O . GLN A 1 164 ? 56.071 25.027 8.387 1.00 22.82 ? 164 GLN A O 1 ATOM 1327 C CB . GLN A 1 164 ? 55.707 27.944 7.633 1.00 29.03 ? 164 GLN A CB 1 ATOM 1328 C CG . GLN A 1 164 ? 54.840 28.669 6.569 1.00 32.51 ? 164 GLN A CG 1 ATOM 1329 C CD . GLN A 1 164 ? 55.689 29.502 5.578 1.00 31.88 ? 164 GLN A CD 1 ATOM 1330 O OE1 . GLN A 1 164 ? 56.582 30.291 5.983 1.00 38.01 ? 164 GLN A OE1 1 ATOM 1331 N NE2 . GLN A 1 164 ? 55.426 29.314 4.277 1.00 28.10 ? 164 GLN A NE2 1 ATOM 1332 N N . GLN A 1 165 ? 55.623 25.771 10.464 1.00 19.98 ? 165 GLN A N 1 ATOM 1333 C CA . GLN A 1 165 ? 56.166 24.574 11.154 1.00 18.02 ? 165 GLN A CA 1 ATOM 1334 C C . GLN A 1 165 ? 55.080 23.571 11.498 1.00 18.71 ? 165 GLN A C 1 ATOM 1335 O O . GLN A 1 165 ? 55.371 22.557 12.173 1.00 18.09 ? 165 GLN A O 1 ATOM 1336 C CB . GLN A 1 165 ? 56.904 24.971 12.450 1.00 16.97 ? 165 GLN A CB 1 ATOM 1337 C CG . GLN A 1 165 ? 58.234 25.720 12.075 1.00 18.90 ? 165 GLN A CG 1 ATOM 1338 C CD . GLN A 1 165 ? 58.965 26.216 13.292 1.00 21.59 ? 165 GLN A CD 1 ATOM 1339 O OE1 . GLN A 1 165 ? 58.624 25.842 14.436 1.00 18.86 ? 165 GLN A OE1 1 ATOM 1340 N NE2 . GLN A 1 165 ? 59.921 27.110 13.081 1.00 21.47 ? 165 GLN A NE2 1 ATOM 1341 N N . GLN A 1 166 ? 53.852 23.841 11.081 1.00 17.96 ? 166 GLN A N 1 ATOM 1342 C CA . GLN A 1 166 ? 52.731 22.976 11.449 1.00 16.17 ? 166 GLN A CA 1 ATOM 1343 C C . GLN A 1 166 ? 52.368 22.081 10.290 1.00 17.28 ? 166 GLN A C 1 ATOM 1344 O O . GLN A 1 166 ? 52.025 22.586 9.202 1.00 18.88 ? 166 GLN A O 1 ATOM 1345 C CB . GLN A 1 166 ? 51.524 23.794 11.938 1.00 19.41 ? 166 GLN A CB 1 ATOM 1346 C CG . GLN A 1 166 ? 51.913 24.815 13.055 1.00 16.81 ? 166 GLN A CG 1 ATOM 1347 C CD . GLN A 1 166 ? 50.803 25.606 13.674 1.00 20.84 ? 166 GLN A CD 1 ATOM 1348 O OE1 . GLN A 1 166 ? 49.711 25.731 13.104 1.00 25.91 ? 166 GLN A OE1 1 ATOM 1349 N NE2 . GLN A 1 166 ? 51.083 26.156 14.880 1.00 23.30 ? 166 GLN A NE2 1 ATOM 1350 N N . TRP A 1 167 ? 52.352 20.757 10.548 1.00 15.35 ? 167 TRP A N 1 ATOM 1351 C CA . TRP A 1 167 ? 52.138 19.750 9.465 1.00 16.25 ? 167 TRP A CA 1 ATOM 1352 C C . TRP A 1 167 ? 50.908 18.905 9.722 1.00 18.10 ? 167 TRP A C 1 ATOM 1353 O O . TRP A 1 167 ? 50.662 18.468 10.857 1.00 20.69 ? 167 TRP A O 1 ATOM 1354 C CB . TRP A 1 167 ? 53.330 18.806 9.448 1.00 18.05 ? 167 TRP A CB 1 ATOM 1355 C CG . TRP A 1 167 ? 54.618 19.557 9.154 1.00 17.52 ? 167 TRP A CG 1 ATOM 1356 C CD1 . TRP A 1 167 ? 55.574 19.948 10.072 1.00 17.15 ? 167 TRP A CD1 1 ATOM 1357 C CD2 . TRP A 1 167 ? 55.048 20.075 7.883 1.00 15.70 ? 167 TRP A CD2 1 ATOM 1358 N NE1 . TRP A 1 167 ? 56.589 20.633 9.455 1.00 17.66 ? 167 TRP A NE1 1 ATOM 1359 C CE2 . TRP A 1 167 ? 56.317 20.712 8.099 1.00 16.71 ? 167 TRP A CE2 1 ATOM 1360 C CE3 . TRP A 1 167 ? 54.529 20.003 6.580 1.00 16.29 ? 167 TRP A CE3 1 ATOM 1361 C CZ2 . TRP A 1 167 ? 57.057 21.312 7.038 1.00 19.69 ? 167 TRP A CZ2 1 ATOM 1362 C CZ3 . TRP A 1 167 ? 55.268 20.626 5.511 1.00 18.20 ? 167 TRP A CZ3 1 ATOM 1363 C CH2 . TRP A 1 167 ? 56.526 21.250 5.775 1.00 16.93 ? 167 TRP A CH2 1 ATOM 1364 N N . ALA A 1 168 ? 50.103 18.722 8.683 1.00 17.42 ? 168 ALA A N 1 ATOM 1365 C CA . ALA A 1 168 ? 48.957 17.828 8.783 1.00 19.14 ? 168 ALA A CA 1 ATOM 1366 C C . ALA A 1 168 ? 49.359 16.470 8.259 1.00 17.83 ? 168 ALA A C 1 ATOM 1367 O O . ALA A 1 168 ? 49.717 16.317 7.059 1.00 17.89 ? 168 ALA A O 1 ATOM 1368 C CB . ALA A 1 168 ? 47.753 18.377 7.932 1.00 17.36 ? 168 ALA A CB 1 ATOM 1369 N N . LEU A 1 169 ? 49.345 15.471 9.134 1.00 18.22 ? 169 LEU A N 1 ATOM 1370 C CA . LEU A 1 169 ? 49.734 14.151 8.720 1.00 17.19 ? 169 LEU A CA 1 ATOM 1371 C C . LEU A 1 169 ? 48.483 13.442 8.262 1.00 16.98 ? 169 LEU A C 1 ATOM 1372 O O . LEU A 1 169 ? 47.652 13.040 9.105 1.00 18.96 ? 169 LEU A O 1 ATOM 1373 C CB . LEU A 1 169 ? 50.373 13.419 9.886 1.00 17.93 ? 169 LEU A CB 1 ATOM 1374 C CG . LEU A 1 169 ? 51.503 14.183 10.605 1.00 20.36 ? 169 LEU A CG 1 ATOM 1375 C CD1 . LEU A 1 169 ? 52.019 13.397 11.824 1.00 23.93 ? 169 LEU A CD1 1 ATOM 1376 C CD2 . LEU A 1 169 ? 52.651 14.558 9.615 1.00 21.60 ? 169 LEU A CD2 1 ATOM 1377 N N . TYR A 1 170 ? 48.323 13.340 6.931 1.00 16.61 ? 170 TYR A N 1 ATOM 1378 C CA . TYR A 1 170 ? 47.106 12.797 6.324 1.00 14.49 ? 170 TYR A CA 1 ATOM 1379 C C . TYR A 1 170 ? 47.071 11.264 6.260 1.00 15.73 ? 170 TYR A C 1 ATOM 1380 O O . TYR A 1 170 ? 48.122 10.597 6.251 1.00 17.89 ? 170 TYR A O 1 ATOM 1381 C CB . TYR A 1 170 ? 46.956 13.402 4.879 1.00 16.35 ? 170 TYR A CB 1 ATOM 1382 C CG . TYR A 1 170 ? 46.060 14.615 4.828 1.00 16.78 ? 170 TYR A CG 1 ATOM 1383 C CD1 . TYR A 1 170 ? 46.414 15.826 5.474 1.00 17.89 ? 170 TYR A CD1 1 ATOM 1384 C CD2 . TYR A 1 170 ? 44.841 14.570 4.150 1.00 20.68 ? 170 TYR A CD2 1 ATOM 1385 C CE1 . TYR A 1 170 ? 45.609 16.954 5.435 1.00 17.45 ? 170 TYR A CE1 1 ATOM 1386 C CE2 . TYR A 1 170 ? 43.993 15.701 4.134 1.00 24.27 ? 170 TYR A CE2 1 ATOM 1387 C CZ . TYR A 1 170 ? 44.385 16.882 4.764 1.00 19.79 ? 170 TYR A CZ 1 ATOM 1388 O OH . TYR A 1 170 ? 43.550 17.972 4.704 1.00 24.27 ? 170 TYR A OH 1 ATOM 1389 N N . GLY A 1 171 ? 45.856 10.703 6.184 1.00 18.64 ? 171 GLY A N 1 ATOM 1390 C CA . GLY A 1 171 ? 45.724 9.230 6.162 1.00 17.16 ? 171 GLY A CA 1 ATOM 1391 C C . GLY A 1 171 ? 46.362 8.541 4.966 1.00 15.69 ? 171 GLY A C 1 ATOM 1392 O O . GLY A 1 171 ? 46.664 7.327 5.046 1.00 16.55 ? 171 GLY A O 1 ATOM 1393 N N . ASP A 1 172 ? 46.489 9.266 3.852 1.00 16.70 ? 172 ASP A N 1 ATOM 1394 C CA . ASP A 1 172 ? 47.133 8.730 2.649 1.00 15.99 ? 172 ASP A CA 1 ATOM 1395 C C . ASP A 1 172 ? 48.668 8.780 2.765 1.00 15.27 ? 172 ASP A C 1 ATOM 1396 O O . ASP A 1 172 ? 49.364 8.553 1.781 1.00 16.87 ? 172 ASP A O 1 ATOM 1397 C CB . ASP A 1 172 ? 46.688 9.505 1.366 1.00 16.94 ? 172 ASP A CB 1 ATOM 1398 C CG . ASP A 1 172 ? 46.932 10.995 1.456 1.00 16.42 ? 172 ASP A CG 1 ATOM 1399 O OD1 . ASP A 1 172 ? 47.583 11.460 2.451 1.00 16.84 ? 172 ASP A OD1 1 ATOM 1400 O OD2 . ASP A 1 172 ? 46.529 11.729 0.473 1.00 17.57 ? 172 ASP A OD2 1 ATOM 1401 N N . ARG A 1 173 ? 49.194 9.069 3.970 1.00 13.50 ? 173 ARG A N 1 ATOM 1402 C CA . ARG A 1 173 ? 50.660 9.006 4.175 1.00 15.07 ? 173 ARG A CA 1 ATOM 1403 C C . ARG A 1 173 ? 51.408 10.190 3.538 1.00 17.25 ? 173 ARG A C 1 ATOM 1404 O O . ARG A 1 173 ? 52.597 10.133 3.310 1.00 18.17 ? 173 ARG A O 1 ATOM 1405 C CB . ARG A 1 173 ? 51.288 7.632 3.808 1.00 16.46 ? 173 ARG A CB 1 ATOM 1406 C CG . ARG A 1 173 ? 50.567 6.451 4.421 1.00 16.75 ? 173 ARG A CG 1 ATOM 1407 C CD . ARG A 1 173 ? 50.616 6.446 5.956 1.00 17.72 ? 173 ARG A CD 1 ATOM 1408 N NE . ARG A 1 173 ? 49.852 5.307 6.495 1.00 17.95 ? 173 ARG A NE 1 ATOM 1409 C CZ . ARG A 1 173 ? 50.194 4.595 7.557 1.00 24.77 ? 173 ARG A CZ 1 ATOM 1410 N NH1 . ARG A 1 173 ? 49.411 3.581 7.954 1.00 23.21 ? 173 ARG A NH1 1 ATOM 1411 N NH2 . ARG A 1 173 ? 51.377 4.831 8.160 1.00 27.34 ? 173 ARG A NH2 1 ATOM 1412 N N . THR A 1 174 ? 50.654 11.241 3.230 1.00 15.42 ? 174 THR A N 1 ATOM 1413 C CA . THR A 1 174 ? 51.224 12.530 2.821 1.00 16.21 ? 174 THR A CA 1 ATOM 1414 C C . THR A 1 174 ? 51.464 13.415 4.048 1.00 15.41 ? 174 THR A C 1 ATOM 1415 O O . THR A 1 174 ? 50.798 13.281 5.124 1.00 17.76 ? 174 THR A O 1 ATOM 1416 C CB . THR A 1 174 ? 50.356 13.270 1.781 1.00 14.19 ? 174 THR A CB 1 ATOM 1417 O OG1 . THR A 1 174 ? 49.060 13.545 2.323 1.00 15.43 ? 174 THR A OG1 1 ATOM 1418 C CG2 . THR A 1 174 ? 50.169 12.382 0.512 1.00 16.00 ? 174 THR A CG2 1 ATOM 1419 N N . ILE A 1 175 ? 52.434 14.336 3.906 1.00 16.13 ? 175 ILE A N 1 ATOM 1420 C CA . ILE A 1 175 ? 52.733 15.271 4.983 1.00 14.24 ? 175 ILE A CA 1 ATOM 1421 C C . ILE A 1 175 ? 52.409 16.622 4.369 1.00 16.66 ? 175 ILE A C 1 ATOM 1422 O O . ILE A 1 175 ? 53.046 17.031 3.398 1.00 16.66 ? 175 ILE A O 1 ATOM 1423 C CB . ILE A 1 175 ? 54.230 15.243 5.446 1.00 13.84 ? 175 ILE A CB 1 ATOM 1424 C CG1 . ILE A 1 175 ? 54.536 13.839 5.939 1.00 14.65 ? 175 ILE A CG1 1 ATOM 1425 C CG2 . ILE A 1 175 ? 54.496 16.314 6.557 1.00 17.13 ? 175 ILE A CG2 1 ATOM 1426 C CD1 . ILE A 1 175 ? 56.028 13.584 6.194 1.00 18.02 ? 175 ILE A CD1 1 ATOM 1427 N N . ARG A 1 176 ? 51.353 17.255 4.866 1.00 16.53 ? 176 ARG A N 1 ATOM 1428 C CA . ARG A 1 176 ? 50.843 18.471 4.220 1.00 15.76 ? 176 ARG A CA 1 ATOM 1429 C C . ARG A 1 176 ? 51.044 19.753 4.999 1.00 18.23 ? 176 ARG A C 1 ATOM 1430 O O . ARG A 1 176 ? 51.101 19.744 6.242 1.00 17.17 ? 176 ARG A O 1 ATOM 1431 C CB . ARG A 1 176 ? 49.332 18.252 3.936 1.00 16.46 ? 176 ARG A CB 1 ATOM 1432 C CG . ARG A 1 176 ? 49.032 16.995 3.164 1.00 16.44 ? 176 ARG A CG 1 ATOM 1433 C CD . ARG A 1 176 ? 47.799 17.077 2.347 1.00 18.49 ? 176 ARG A CD 1 ATOM 1434 N NE . ARG A 1 176 ? 47.540 15.843 1.603 1.00 16.89 ? 176 ARG A NE 1 ATOM 1435 C CZ . ARG A 1 176 ? 46.599 15.736 0.631 1.00 17.68 ? 176 ARG A CZ 1 ATOM 1436 N NH1 . ARG A 1 176 ? 46.427 14.558 0.011 1.00 16.54 ? 176 ARG A NH1 1 ATOM 1437 N NH2 . ARG A 1 176 ? 45.867 16.806 0.262 1.00 17.14 ? 176 ARG A NH2 1 ATOM 1438 N N . VAL A 1 177 ? 51.083 20.881 4.279 1.00 15.97 ? 177 VAL A N 1 ATOM 1439 C CA . VAL A 1 177 ? 51.176 22.197 4.947 1.00 18.10 ? 177 VAL A CA 1 ATOM 1440 C C . VAL A 1 177 ? 49.849 22.424 5.688 1.00 18.86 ? 177 VAL A C 1 ATOM 1441 O O . VAL A 1 177 ? 48.783 22.404 5.054 1.00 19.26 ? 177 VAL A O 1 ATOM 1442 C CB . VAL A 1 177 ? 51.411 23.293 3.892 1.00 19.48 ? 177 VAL A CB 1 ATOM 1443 C CG1 . VAL A 1 177 ? 51.379 24.693 4.527 1.00 22.68 ? 177 VAL A CG1 1 ATOM 1444 C CG2 . VAL A 1 177 ? 52.758 23.043 3.136 1.00 19.70 ? 177 VAL A CG2 1 ATOM 1445 N N . ASN A 1 178 ? 49.875 22.583 7.027 1.00 18.90 ? 178 ASN A N 1 ATOM 1446 C CA . ASN A 1 178 ? 48.593 22.549 7.742 1.00 18.54 ? 178 ASN A CA 1 ATOM 1447 C C . ASN A 1 178 ? 47.645 23.667 7.288 1.00 22.10 ? 178 ASN A C 1 ATOM 1448 O O . ASN A 1 178 ? 46.414 23.464 7.211 1.00 24.25 ? 178 ASN A O 1 ATOM 1449 C CB . ASN A 1 178 ? 48.733 22.635 9.253 1.00 20.78 ? 178 ASN A CB 1 ATOM 1450 C CG . ASN A 1 178 ? 47.406 22.440 9.936 1.00 23.01 ? 178 ASN A CG 1 ATOM 1451 O OD1 . ASN A 1 178 ? 46.768 21.381 9.746 1.00 21.60 ? 178 ASN A OD1 1 ATOM 1452 N ND2 . ASN A 1 178 ? 46.960 23.477 10.682 1.00 24.95 ? 178 ASN A ND2 1 ATOM 1453 N N . SER A 1 179 ? 48.220 24.836 7.005 1.00 20.42 ? 179 SER A N 1 ATOM 1454 C CA . SER A 1 179 ? 47.400 25.979 6.652 1.00 23.14 ? 179 SER A CA 1 ATOM 1455 C C . SER A 1 179 ? 47.019 25.998 5.165 1.00 22.31 ? 179 SER A C 1 ATOM 1456 O O . SER A 1 179 ? 46.227 26.857 4.754 1.00 25.75 ? 179 SER A O 1 ATOM 1457 C CB . SER A 1 179 ? 48.079 27.287 7.058 1.00 29.29 ? 179 SER A CB 1 ATOM 1458 O OG . SER A 1 179 ? 49.252 27.493 6.324 1.00 38.72 ? 179 SER A OG 1 ATOM 1459 N N . THR A 1 180 ? 47.626 25.113 4.364 1.00 21.98 ? 180 THR A N 1 ATOM 1460 C CA . THR A 1 180 ? 47.362 25.046 2.914 1.00 21.34 ? 180 THR A CA 1 ATOM 1461 C C . THR A 1 180 ? 47.339 23.574 2.473 1.00 22.43 ? 180 THR A C 1 ATOM 1462 O O . THR A 1 180 ? 48.326 23.060 1.919 1.00 20.96 ? 180 THR A O 1 ATOM 1463 C CB . THR A 1 180 ? 48.425 25.833 2.156 1.00 22.68 ? 180 THR A CB 1 ATOM 1464 O OG1 . THR A 1 180 ? 48.483 27.157 2.709 1.00 27.05 ? 180 THR A OG1 1 ATOM 1465 C CG2 . THR A 1 180 ? 47.985 25.997 0.688 1.00 25.80 ? 180 THR A CG2 1 ATOM 1466 N N . ARG A 1 181 ? 46.232 22.884 2.743 1.00 19.11 ? 181 ARG A N 1 ATOM 1467 C CA . ARG A 1 181 ? 46.263 21.416 2.770 1.00 16.83 ? 181 ARG A CA 1 ATOM 1468 C C . ARG A 1 181 ? 46.248 20.770 1.369 1.00 20.43 ? 181 ARG A C 1 ATOM 1469 O O . ARG A 1 181 ? 46.193 19.539 1.259 1.00 20.17 ? 181 ARG A O 1 ATOM 1470 C CB . ARG A 1 181 ? 45.130 20.882 3.690 1.00 20.74 ? 181 ARG A CB 1 ATOM 1471 C CG . ARG A 1 181 ? 45.462 21.067 5.198 1.00 21.33 ? 181 ARG A CG 1 ATOM 1472 C CD . ARG A 1 181 ? 44.218 20.942 6.050 1.00 25.40 ? 181 ARG A CD 1 ATOM 1473 N NE . ARG A 1 181 ? 44.593 20.911 7.456 1.00 21.77 ? 181 ARG A NE 1 ATOM 1474 C CZ . ARG A 1 181 ? 43.876 20.278 8.381 1.00 23.41 ? 181 ARG A CZ 1 ATOM 1475 N NH1 . ARG A 1 181 ? 44.273 20.286 9.646 1.00 24.21 ? 181 ARG A NH1 1 ATOM 1476 N NH2 . ARG A 1 181 ? 42.768 19.603 8.014 1.00 25.76 ? 181 ARG A NH2 1 ATOM 1477 N N . GLY A 1 182 ? 46.250 21.586 0.304 1.00 19.46 ? 182 GLY A N 1 ATOM 1478 C CA . GLY A 1 182 ? 46.443 21.073 -1.033 1.00 18.31 ? 182 GLY A CA 1 ATOM 1479 C C . GLY A 1 182 ? 47.933 20.886 -1.376 1.00 17.86 ? 182 GLY A C 1 ATOM 1480 O O . GLY A 1 182 ? 48.241 20.442 -2.514 1.00 21.82 ? 182 GLY A O 1 ATOM 1481 N N . LEU A 1 183 ? 48.843 21.224 -0.454 1.00 18.09 ? 183 LEU A N 1 ATOM 1482 C CA . LEU A 1 183 ? 50.310 21.207 -0.694 1.00 20.59 ? 183 LEU A CA 1 ATOM 1483 C C . LEU A 1 183 ? 50.983 20.123 0.144 1.00 17.47 ? 183 LEU A C 1 ATOM 1484 O O . LEU A 1 183 ? 50.646 19.974 1.341 1.00 18.29 ? 183 LEU A O 1 ATOM 1485 C CB . LEU A 1 183 ? 50.967 22.580 -0.333 1.00 19.16 ? 183 LEU A CB 1 ATOM 1486 C CG . LEU A 1 183 ? 50.457 23.818 -1.119 1.00 18.95 ? 183 LEU A CG 1 ATOM 1487 C CD1 . LEU A 1 183 ? 51.156 25.072 -0.700 1.00 19.50 ? 183 LEU A CD1 1 ATOM 1488 C CD2 . LEU A 1 183 ? 50.606 23.552 -2.635 1.00 25.16 ? 183 LEU A CD2 1 ATOM 1489 N N . CYS A 1 184 ? 51.929 19.391 -0.493 1.00 18.46 ? 184 CYS A N 1 ATOM 1490 C CA . CYS A 1 184 ? 52.501 18.171 0.090 1.00 18.16 ? 184 CYS A CA 1 ATOM 1491 C C . CYS A 1 184 ? 54.024 18.278 0.075 1.00 17.92 ? 184 CYS A C 1 ATOM 1492 O O . CYS A 1 184 ? 54.601 18.770 -0.896 1.00 17.98 ? 184 CYS A O 1 ATOM 1493 C CB . CYS A 1 184 ? 52.165 16.960 -0.806 1.00 18.91 ? 184 CYS A CB 1 ATOM 1494 S SG . CYS A 1 184 ? 50.571 16.220 -0.472 1.00 20.36 ? 184 CYS A SG 1 ATOM 1495 N N . VAL A 1 185 ? 54.661 17.731 1.105 1.00 15.18 ? 185 VAL A N 1 ATOM 1496 C CA . VAL A 1 185 ? 56.108 17.566 1.108 1.00 16.55 ? 185 VAL A CA 1 ATOM 1497 C C . VAL A 1 185 ? 56.412 16.533 0.024 1.00 15.15 ? 185 VAL A C 1 ATOM 1498 O O . VAL A 1 185 ? 55.844 15.392 0.012 1.00 17.33 ? 185 VAL A O 1 ATOM 1499 C CB . VAL A 1 185 ? 56.567 17.005 2.480 1.00 15.96 ? 185 VAL A CB 1 ATOM 1500 C CG1 . VAL A 1 185 ? 58.048 16.643 2.473 1.00 18.50 ? 185 VAL A CG1 1 ATOM 1501 C CG2 . VAL A 1 185 ? 56.305 18.004 3.577 1.00 18.69 ? 185 VAL A CG2 1 ATOM 1502 N N . THR A 1 186 ? 57.345 16.883 -0.876 1.00 16.94 ? 186 THR A N 1 ATOM 1503 C CA . THR A 1 186 ? 57.592 16.127 -2.114 1.00 15.69 ? 186 THR A CA 1 ATOM 1504 C C . THR A 1 186 ? 59.078 16.022 -2.392 1.00 17.22 ? 186 THR A C 1 ATOM 1505 O O . THR A 1 186 ? 59.783 17.060 -2.321 1.00 18.57 ? 186 THR A O 1 ATOM 1506 C CB . THR A 1 186 ? 56.966 16.863 -3.310 1.00 17.02 ? 186 THR A CB 1 ATOM 1507 O OG1 . THR A 1 186 ? 55.572 17.105 -3.020 1.00 17.10 ? 186 THR A OG1 1 ATOM 1508 C CG2 . THR A 1 186 ? 57.094 16.078 -4.577 1.00 18.20 ? 186 THR A CG2 1 ATOM 1509 N N . THR A 1 187 ? 59.571 14.801 -2.666 1.00 16.51 ? 187 THR A N 1 ATOM 1510 C CA . THR A 1 187 ? 60.962 14.703 -3.095 1.00 16.02 ? 187 THR A CA 1 ATOM 1511 C C . THR A 1 187 ? 61.050 15.039 -4.604 1.00 20.09 ? 187 THR A C 1 ATOM 1512 O O . THR A 1 187 ? 60.190 14.613 -5.373 1.00 23.27 ? 187 THR A O 1 ATOM 1513 C CB . THR A 1 187 ? 61.652 13.413 -2.678 1.00 18.99 ? 187 THR A CB 1 ATOM 1514 O OG1 . THR A 1 187 ? 62.999 13.406 -3.200 1.00 22.91 ? 187 THR A OG1 1 ATOM 1515 C CG2 . THR A 1 187 ? 60.946 12.241 -3.128 1.00 23.04 ? 187 THR A CG2 1 ATOM 1516 N N . ASN A 1 188 ? 62.043 15.837 -5.001 1.00 20.11 ? 188 ASN A N 1 ATOM 1517 C CA . ASN A 1 188 ? 62.175 16.252 -6.402 1.00 19.29 ? 188 ASN A CA 1 ATOM 1518 C C . ASN A 1 188 ? 63.033 15.212 -7.078 1.00 26.57 ? 188 ASN A C 1 ATOM 1519 O O . ASN A 1 188 ? 64.188 15.512 -7.456 1.00 35.05 ? 188 ASN A O 1 ATOM 1520 C CB . ASN A 1 188 ? 62.891 17.619 -6.458 1.00 23.81 ? 188 ASN A CB 1 ATOM 1521 C CG . ASN A 1 188 ? 62.774 18.294 -7.810 1.00 38.58 ? 188 ASN A CG 1 ATOM 1522 O OD1 . ASN A 1 188 ? 63.668 19.028 -8.206 1.00 49.96 ? 188 ASN A OD1 1 ATOM 1523 N ND2 . ASN A 1 188 ? 61.687 18.023 -8.540 1.00 41.83 ? 188 ASN A ND2 1 ATOM 1524 N N . GLY A 1 189 ? 62.570 13.968 -7.075 1.00 26.59 ? 189 GLY A N 1 ATOM 1525 C CA . GLY A 1 189 ? 63.256 12.836 -7.689 1.00 22.83 ? 189 GLY A CA 1 ATOM 1526 C C . GLY A 1 189 ? 63.454 11.698 -6.689 1.00 21.41 ? 189 GLY A C 1 ATOM 1527 O O . GLY A 1 189 ? 63.204 11.844 -5.483 1.00 24.05 ? 189 GLY A O 1 ATOM 1528 N N . TYR A 1 190 ? 63.928 10.562 -7.178 1.00 19.29 ? 190 TYR A N 1 ATOM 1529 C CA . TYR A 1 190 ? 64.102 9.385 -6.328 1.00 21.95 ? 190 TYR A CA 1 ATOM 1530 C C . TYR A 1 190 ? 65.547 8.994 -6.096 1.00 20.84 ? 190 TYR A C 1 ATOM 1531 O O . TYR A 1 190 ? 65.791 7.898 -5.581 1.00 23.60 ? 190 TYR A O 1 ATOM 1532 C CB . TYR A 1 190 ? 63.299 8.185 -6.901 1.00 24.10 ? 190 TYR A CB 1 ATOM 1533 C CG . TYR A 1 190 ? 61.839 8.529 -7.101 1.00 24.96 ? 190 TYR A CG 1 ATOM 1534 C CD1 . TYR A 1 190 ? 60.983 8.659 -6.043 1.00 23.60 ? 190 TYR A CD1 1 ATOM 1535 C CD2 . TYR A 1 190 ? 61.320 8.709 -8.367 1.00 24.63 ? 190 TYR A CD2 1 ATOM 1536 C CE1 . TYR A 1 190 ? 59.634 9.004 -6.239 1.00 24.02 ? 190 TYR A CE1 1 ATOM 1537 C CE2 . TYR A 1 190 ? 59.969 9.036 -8.560 1.00 26.90 ? 190 TYR A CE2 1 ATOM 1538 C CZ . TYR A 1 190 ? 59.138 9.172 -7.492 1.00 27.30 ? 190 TYR A CZ 1 ATOM 1539 O OH . TYR A 1 190 ? 57.783 9.478 -7.690 1.00 26.83 ? 190 TYR A OH 1 ATOM 1540 N N . ASN A 1 191 ? 66.463 9.893 -6.443 1.00 20.83 ? 191 ASN A N 1 ATOM 1541 C CA . ASN A 1 191 ? 67.877 9.628 -6.282 1.00 19.67 ? 191 ASN A CA 1 ATOM 1542 C C . ASN A 1 191 ? 68.474 10.275 -5.035 1.00 20.16 ? 191 ASN A C 1 ATOM 1543 O O . ASN A 1 191 ? 67.969 11.295 -4.516 1.00 21.45 ? 191 ASN A O 1 ATOM 1544 C CB . ASN A 1 191 ? 68.642 10.179 -7.476 1.00 22.89 ? 191 ASN A CB 1 ATOM 1545 C CG . ASN A 1 191 ? 68.299 9.451 -8.749 1.00 27.98 ? 191 ASN A CG 1 ATOM 1546 O OD1 . ASN A 1 191 ? 68.285 8.225 -8.790 1.00 36.75 ? 191 ASN A OD1 1 ATOM 1547 N ND2 . ASN A 1 191 ? 67.991 10.199 -9.778 1.00 32.65 ? 191 ASN A ND2 1 ATOM 1548 N N . SER A 1 192 ? 69.541 9.666 -4.536 1.00 20.90 ? 192 SER A N 1 ATOM 1549 C CA . SER A 1 192 ? 70.229 10.240 -3.380 1.00 20.27 ? 192 SER A CA 1 ATOM 1550 C C . SER A 1 192 ? 70.590 11.712 -3.680 1.00 19.58 ? 192 SER A C 1 ATOM 1551 O O . SER A 1 192 ? 71.073 12.076 -4.801 1.00 22.43 ? 192 SER A O 1 ATOM 1552 C CB . SER A 1 192 ? 71.461 9.372 -3.069 1.00 25.92 ? 192 SER A CB 1 ATOM 1553 O OG . SER A 1 192 ? 72.108 9.830 -1.909 1.00 30.45 ? 192 SER A OG 1 ATOM 1554 N N . LYS A 1 193 ? 70.369 12.554 -2.655 1.00 20.62 ? 193 LYS A N 1 ATOM 1555 C CA . LYS A 1 193 ? 70.602 14.019 -2.652 1.00 21.33 ? 193 LYS A CA 1 ATOM 1556 C C . LYS A 1 193 ? 69.562 14.827 -3.397 1.00 22.07 ? 193 LYS A C 1 ATOM 1557 O O . LYS A 1 193 ? 69.690 16.087 -3.497 1.00 24.01 ? 193 LYS A O 1 ATOM 1558 C CB . LYS A 1 193 ? 72.020 14.411 -3.160 1.00 24.86 ? 193 LYS A CB 1 ATOM 1559 C CG . LYS A 1 193 ? 73.094 14.123 -2.178 1.00 28.77 ? 193 LYS A CG 1 ATOM 1560 C CD . LYS A 1 193 ? 74.414 14.854 -2.536 1.00 31.89 ? 193 LYS A CD 1 ATOM 1561 C CE . LYS A 1 193 ? 74.853 14.586 -3.938 1.00 37.63 ? 193 LYS A CE 1 ATOM 1562 N NZ . LYS A 1 193 ? 76.027 15.483 -4.267 1.00 47.44 ? 193 LYS A NZ 1 ATOM 1563 N N . ASP A 1 194 ? 68.517 14.184 -3.924 1.00 21.06 ? 194 ASP A N 1 ATOM 1564 C CA . ASP A 1 194 ? 67.428 15.003 -4.482 1.00 18.97 ? 194 ASP A CA 1 ATOM 1565 C C . ASP A 1 194 ? 66.783 15.833 -3.356 1.00 17.95 ? 194 ASP A C 1 ATOM 1566 O O . ASP A 1 194 ? 66.677 15.360 -2.182 1.00 19.28 ? 194 ASP A O 1 ATOM 1567 C CB . ASP A 1 194 ? 66.417 14.138 -5.197 1.00 18.21 ? 194 ASP A CB 1 ATOM 1568 C CG . ASP A 1 194 ? 66.916 13.646 -6.581 1.00 23.38 ? 194 ASP A CG 1 ATOM 1569 O OD1 . ASP A 1 194 ? 66.356 12.654 -7.095 1.00 23.50 ? 194 ASP A OD1 1 ATOM 1570 O OD2 . ASP A 1 194 ? 67.862 14.241 -7.152 1.00 23.71 ? 194 ASP A OD2 1 ATOM 1571 N N . LEU A 1 195 ? 66.316 17.035 -3.709 1.00 18.24 ? 195 LEU A N 1 ATOM 1572 C CA . LEU A 1 195 ? 65.877 18.003 -2.711 1.00 17.76 ? 195 LEU A CA 1 ATOM 1573 C C . LEU A 1 195 ? 64.404 17.778 -2.347 1.00 18.61 ? 195 LEU A C 1 ATOM 1574 O O . LEU A 1 195 ? 63.615 17.384 -3.228 1.00 20.39 ? 195 LEU A O 1 ATOM 1575 C CB . LEU A 1 195 ? 66.001 19.403 -3.330 1.00 21.32 ? 195 LEU A CB 1 ATOM 1576 C CG . LEU A 1 195 ? 65.933 20.539 -2.337 1.00 25.20 ? 195 LEU A CG 1 ATOM 1577 C CD1 . LEU A 1 195 ? 67.353 20.584 -1.605 1.00 28.84 ? 195 LEU A CD1 1 ATOM 1578 C CD2 . LEU A 1 195 ? 65.684 21.850 -3.122 1.00 32.17 ? 195 LEU A CD2 1 ATOM 1579 N N . ILE A 1 196 ? 64.054 18.019 -1.067 1.00 16.90 ? 196 ILE A N 1 ATOM 1580 C CA . ILE A 1 196 ? 62.656 17.898 -0.629 1.00 17.78 ? 196 ILE A CA 1 ATOM 1581 C C . ILE A 1 196 ? 62.032 19.304 -0.630 1.00 18.17 ? 196 ILE A C 1 ATOM 1582 O O . ILE A 1 196 ? 62.638 20.256 -0.081 1.00 16.64 ? 196 ILE A O 1 ATOM 1583 C CB . ILE A 1 196 ? 62.567 17.248 0.745 1.00 18.10 ? 196 ILE A CB 1 ATOM 1584 C CG1 . ILE A 1 196 ? 63.147 15.812 0.640 1.00 18.67 ? 196 ILE A CG1 1 ATOM 1585 C CG2 . ILE A 1 196 ? 61.122 17.200 1.266 1.00 17.40 ? 196 ILE A CG2 1 ATOM 1586 C CD1 . ILE A 1 196 ? 63.201 15.066 1.956 1.00 21.15 ? 196 ILE A CD1 1 ATOM 1587 N N . ILE A 1 197 ? 60.893 19.436 -1.335 1.00 17.34 ? 197 ILE A N 1 ATOM 1588 C CA . ILE A 1 197 ? 60.266 20.728 -1.576 1.00 16.95 ? 197 ILE A CA 1 ATOM 1589 C C . ILE A 1 197 ? 58.785 20.603 -1.221 1.00 17.90 ? 197 ILE A C 1 ATOM 1590 O O . ILE A 1 197 ? 58.323 19.546 -0.759 1.00 18.26 ? 197 ILE A O 1 ATOM 1591 C CB . ILE A 1 197 ? 60.404 21.151 -3.076 1.00 18.00 ? 197 ILE A CB 1 ATOM 1592 C CG1 . ILE A 1 197 ? 59.751 20.107 -4.031 1.00 19.90 ? 197 ILE A CG1 1 ATOM 1593 C CG2 . ILE A 1 197 ? 61.857 21.318 -3.374 1.00 18.44 ? 197 ILE A CG2 1 ATOM 1594 C CD1 . ILE A 1 197 ? 59.615 20.648 -5.487 1.00 25.30 ? 197 ILE A CD1 1 ATOM 1595 N N . ILE A 1 198 ? 58.042 21.677 -1.420 1.00 18.49 ? 198 ILE A N 1 ATOM 1596 C CA . ILE A 1 198 ? 56.586 21.610 -1.316 1.00 19.32 ? 198 ILE A CA 1 ATOM 1597 C C . ILE A 1 198 ? 55.989 21.717 -2.728 1.00 20.25 ? 198 ILE A C 1 ATOM 1598 O O . ILE A 1 198 ? 56.389 22.608 -3.500 1.00 22.13 ? 198 ILE A O 1 ATOM 1599 C CB . ILE A 1 198 ? 56.075 22.794 -0.467 1.00 19.72 ? 198 ILE A CB 1 ATOM 1600 C CG1 . ILE A 1 198 ? 56.574 22.684 1.010 1.00 21.10 ? 198 ILE A CG1 1 ATOM 1601 C CG2 . ILE A 1 198 ? 54.563 22.795 -0.508 1.00 18.51 ? 198 ILE A CG2 1 ATOM 1602 C CD1 . ILE A 1 198 ? 56.128 21.367 1.664 1.00 20.45 ? 198 ILE A CD1 1 ATOM 1603 N N . LEU A 1 199 ? 55.114 20.796 -3.100 1.00 18.38 ? 199 LEU A N 1 ATOM 1604 C CA . LEU A 1 199 ? 54.411 20.891 -4.369 1.00 18.50 ? 199 LEU A CA 1 ATOM 1605 C C . LEU A 1 199 ? 52.945 20.492 -4.175 1.00 19.39 ? 199 LEU A C 1 ATOM 1606 O O . LEU A 1 199 ? 52.598 19.724 -3.233 1.00 21.34 ? 199 LEU A O 1 ATOM 1607 C CB . LEU A 1 199 ? 54.959 19.857 -5.365 1.00 23.37 ? 199 LEU A CB 1 ATOM 1608 C CG . LEU A 1 199 ? 56.118 20.036 -6.314 1.00 36.80 ? 199 LEU A CG 1 ATOM 1609 C CD1 . LEU A 1 199 ? 55.982 18.817 -7.231 1.00 35.94 ? 199 LEU A CD1 1 ATOM 1610 C CD2 . LEU A 1 199 ? 55.998 21.321 -7.120 1.00 32.44 ? 199 LEU A CD2 1 ATOM 1611 N N . LYS A 1 200 ? 52.098 20.910 -5.130 1.00 22.03 ? 200 LYS A N 1 ATOM 1612 C CA . LYS A 1 200 ? 50.689 20.516 -5.110 1.00 20.39 ? 200 LYS A CA 1 ATOM 1613 C C . LYS A 1 200 ? 50.529 19.001 -4.950 1.00 22.23 ? 200 LYS A C 1 ATOM 1614 O O . LYS A 1 200 ? 51.153 18.243 -5.683 1.00 20.67 ? 200 LYS A O 1 ATOM 1615 C CB . LYS A 1 200 ? 49.994 20.972 -6.401 1.00 21.99 ? 200 LYS A CB 1 ATOM 1616 C CG . LYS A 1 200 ? 48.597 20.490 -6.561 1.00 32.89 ? 200 LYS A CG 1 ATOM 1617 C CD . LYS A 1 200 ? 47.896 21.271 -7.679 1.00 43.52 ? 200 LYS A CD 1 ATOM 1618 C CE . LYS A 1 200 ? 47.094 20.344 -8.572 1.00 51.96 ? 200 LYS A CE 1 ATOM 1619 N NZ . LYS A 1 200 ? 47.839 20.058 -9.830 1.00 60.01 ? 200 LYS A NZ 1 ATOM 1620 N N . CYS A 1 201 ? 49.684 18.568 -4.012 1.00 20.16 ? 201 CYS A N 1 ATOM 1621 C CA . CYS A 1 201 ? 49.437 17.143 -3.826 1.00 18.61 ? 201 CYS A CA 1 ATOM 1622 C C . CYS A 1 201 ? 48.819 16.520 -5.106 1.00 18.72 ? 201 CYS A C 1 ATOM 1623 O O . CYS A 1 201 ? 47.781 17.013 -5.605 1.00 23.23 ? 201 CYS A O 1 ATOM 1624 C CB . CYS A 1 201 ? 48.496 16.955 -2.648 1.00 21.18 ? 201 CYS A CB 1 ATOM 1625 S SG . CYS A 1 201 ? 49.106 17.575 -1.087 1.00 20.70 ? 201 CYS A SG 1 ATOM 1626 N N . GLN A 1 202 ? 49.461 15.475 -5.622 1.00 19.56 ? 202 GLN A N 1 ATOM 1627 C CA . GLN A 1 202 ? 49.080 14.866 -6.910 1.00 21.13 ? 202 GLN A CA 1 ATOM 1628 C C . GLN A 1 202 ? 49.009 13.326 -6.813 1.00 16.23 ? 202 GLN A C 1 ATOM 1629 O O . GLN A 1 202 ? 48.923 12.627 -7.835 1.00 21.22 ? 202 GLN A O 1 ATOM 1630 C CB . GLN A 1 202 ? 50.031 15.338 -8.064 1.00 25.09 ? 202 GLN A CB 1 ATOM 1631 C CG . GLN A 1 202 ? 49.993 16.824 -8.278 1.00 31.12 ? 202 GLN A CG 1 ATOM 1632 C CD . GLN A 1 202 ? 51.248 17.345 -9.015 1.00 32.43 ? 202 GLN A CD 1 ATOM 1633 O OE1 . GLN A 1 202 ? 52.084 18.188 -8.493 1.00 32.61 ? 202 GLN A OE1 1 ATOM 1634 N NE2 . GLN A 1 202 ? 51.409 16.830 -10.230 1.00 36.78 ? 202 GLN A NE2 1 ATOM 1635 N N . GLY A 1 203 ? 49.073 12.792 -5.569 1.00 17.27 ? 203 GLY A N 1 ATOM 1636 C CA . GLY A 1 203 ? 48.959 11.361 -5.330 1.00 18.94 ? 203 GLY A CA 1 ATOM 1637 C C . GLY A 1 203 ? 50.251 10.579 -5.692 1.00 18.16 ? 203 GLY A C 1 ATOM 1638 O O . GLY A 1 203 ? 50.218 9.323 -5.793 1.00 18.94 ? 203 GLY A O 1 ATOM 1639 N N . LEU A 1 204 ? 51.386 11.274 -5.891 1.00 17.93 ? 204 LEU A N 1 ATOM 1640 C CA . LEU A 1 204 ? 52.596 10.640 -6.511 1.00 18.72 ? 204 LEU A CA 1 ATOM 1641 C C . LEU A 1 204 ? 53.432 9.857 -5.480 1.00 16.61 ? 204 LEU A C 1 ATOM 1642 O O . LEU A 1 204 ? 53.369 10.129 -4.253 1.00 16.30 ? 204 LEU A O 1 ATOM 1643 C CB . LEU A 1 204 ? 53.466 11.751 -7.094 1.00 19.38 ? 204 LEU A CB 1 ATOM 1644 C CG . LEU A 1 204 ? 52.791 12.613 -8.197 1.00 21.79 ? 204 LEU A CG 1 ATOM 1645 C CD1 . LEU A 1 204 ? 53.698 13.803 -8.476 1.00 26.47 ? 204 LEU A CD1 1 ATOM 1646 C CD2 . LEU A 1 204 ? 52.494 11.762 -9.431 1.00 25.65 ? 204 LEU A CD2 1 ATOM 1647 N N . PRO A 1 205 ? 54.266 8.906 -5.977 1.00 16.49 ? 205 PRO A N 1 ATOM 1648 C CA . PRO A 1 205 ? 55.210 8.216 -5.071 1.00 17.47 ? 205 PRO A CA 1 ATOM 1649 C C . PRO A 1 205 ? 56.178 9.169 -4.366 1.00 15.94 ? 205 PRO A C 1 ATOM 1650 O O . PRO A 1 205 ? 56.658 8.863 -3.244 1.00 18.64 ? 205 PRO A O 1 ATOM 1651 C CB . PRO A 1 205 ? 55.928 7.207 -5.998 1.00 18.28 ? 205 PRO A CB 1 ATOM 1652 C CG . PRO A 1 205 ? 54.905 6.972 -7.158 1.00 18.98 ? 205 PRO A CG 1 ATOM 1653 C CD . PRO A 1 205 ? 54.297 8.338 -7.358 1.00 21.61 ? 205 PRO A CD 1 ATOM 1654 N N . SER A 1 206 ? 56.504 10.290 -5.006 1.00 16.57 ? 206 SER A N 1 ATOM 1655 C CA . SER A 1 206 ? 57.375 11.319 -4.427 1.00 17.44 ? 206 SER A CA 1 ATOM 1656 C C . SER A 1 206 ? 56.756 12.047 -3.224 1.00 16.81 ? 206 SER A C 1 ATOM 1657 O O . SER A 1 206 ? 57.431 12.878 -2.597 1.00 16.29 ? 206 SER A O 1 ATOM 1658 C CB . SER A 1 206 ? 57.714 12.347 -5.509 1.00 19.00 ? 206 SER A CB 1 ATOM 1659 O OG . SER A 1 206 ? 56.526 12.862 -6.082 1.00 19.98 ? 206 SER A OG 1 ATOM 1660 N N . GLN A 1 207 ? 55.458 11.826 -2.989 1.00 15.44 ? 207 GLN A N 1 ATOM 1661 C CA . GLN A 1 207 ? 54.704 12.517 -1.906 1.00 14.84 ? 207 GLN A CA 1 ATOM 1662 C C . GLN A 1 207 ? 54.279 11.576 -0.779 1.00 18.63 ? 207 GLN A C 1 ATOM 1663 O O . GLN A 1 207 ? 53.536 11.993 0.122 1.00 17.41 ? 207 GLN A O 1 ATOM 1664 C CB . GLN A 1 207 ? 53.487 13.239 -2.530 1.00 16.43 ? 207 GLN A CB 1 ATOM 1665 C CG . GLN A 1 207 ? 54.024 14.241 -3.591 1.00 17.78 ? 207 GLN A CG 1 ATOM 1666 C CD . GLN A 1 207 ? 52.891 14.962 -4.348 1.00 18.86 ? 207 GLN A CD 1 ATOM 1667 O OE1 . GLN A 1 207 ? 51.908 14.336 -4.826 1.00 18.50 ? 207 GLN A OE1 1 ATOM 1668 N NE2 . GLN A 1 207 ? 53.055 16.261 -4.474 1.00 19.20 ? 207 GLN A NE2 1 ATOM 1669 N N . ARG A 1 208 ? 54.755 10.334 -0.843 1.00 15.25 ? 208 ARG A N 1 ATOM 1670 C CA . ARG A 1 208 ? 54.395 9.318 0.180 1.00 16.85 ? 208 ARG A CA 1 ATOM 1671 C C . ARG A 1 208 ? 55.538 9.156 1.185 1.00 14.83 ? 208 ARG A C 1 ATOM 1672 O O . ARG A 1 208 ? 56.727 9.052 0.767 1.00 15.96 ? 208 ARG A O 1 ATOM 1673 C CB . ARG A 1 208 ? 54.058 7.993 -0.487 1.00 18.33 ? 208 ARG A CB 1 ATOM 1674 C CG . ARG A 1 208 ? 53.719 6.934 0.511 1.00 22.82 ? 208 ARG A CG 1 ATOM 1675 C CD . ARG A 1 208 ? 52.684 6.086 0.000 1.00 23.12 ? 208 ARG A CD 1 ATOM 1676 N NE . ARG A 1 208 ? 52.559 4.865 0.823 1.00 20.09 ? 208 ARG A NE 1 ATOM 1677 C CZ . ARG A 1 208 ? 52.193 3.695 0.362 1.00 20.82 ? 208 ARG A CZ 1 ATOM 1678 N NH1 . ARG A 1 208 ? 51.838 3.591 -0.932 1.00 18.88 ? 208 ARG A NH1 1 ATOM 1679 N NH2 . ARG A 1 208 ? 52.167 2.640 1.203 1.00 21.27 ? 208 ARG A NH2 1 ATOM 1680 N N . TRP A 1 209 ? 55.198 9.098 2.479 1.00 14.47 ? 209 TRP A N 1 ATOM 1681 C CA . TRP A 1 209 ? 56.209 9.045 3.545 1.00 15.10 ? 209 TRP A CA 1 ATOM 1682 C C . TRP A 1 209 ? 55.736 8.084 4.622 1.00 13.67 ? 209 TRP A C 1 ATOM 1683 O O . TRP A 1 209 ? 54.523 7.883 4.818 1.00 15.84 ? 209 TRP A O 1 ATOM 1684 C CB . TRP A 1 209 ? 56.458 10.456 4.187 1.00 16.64 ? 209 TRP A CB 1 ATOM 1685 C CG . TRP A 1 209 ? 56.884 11.437 3.148 1.00 15.61 ? 209 TRP A CG 1 ATOM 1686 C CD1 . TRP A 1 209 ? 56.099 12.318 2.468 1.00 15.60 ? 209 TRP A CD1 1 ATOM 1687 C CD2 . TRP A 1 209 ? 58.223 11.623 2.654 1.00 16.57 ? 209 TRP A CD2 1 ATOM 1688 N NE1 . TRP A 1 209 ? 56.839 13.019 1.550 1.00 18.41 ? 209 TRP A NE1 1 ATOM 1689 C CE2 . TRP A 1 209 ? 58.160 12.611 1.643 1.00 17.53 ? 209 TRP A CE2 1 ATOM 1690 C CE3 . TRP A 1 209 ? 59.451 11.039 2.956 1.00 14.38 ? 209 TRP A CE3 1 ATOM 1691 C CZ2 . TRP A 1 209 ? 59.288 13.058 0.957 1.00 14.66 ? 209 TRP A CZ2 1 ATOM 1692 C CZ3 . TRP A 1 209 ? 60.589 11.456 2.267 1.00 16.34 ? 209 TRP A CZ3 1 ATOM 1693 C CH2 . TRP A 1 209 ? 60.501 12.454 1.236 1.00 16.45 ? 209 TRP A CH2 1 ATOM 1694 N N . PHE A 1 210 ? 56.696 7.504 5.319 1.00 18.03 ? 210 PHE A N 1 ATOM 1695 C CA . PHE A 1 210 ? 56.438 6.519 6.379 1.00 22.20 ? 210 PHE A CA 1 ATOM 1696 C C . PHE A 1 210 ? 57.329 6.881 7.610 1.00 16.80 ? 210 PHE A C 1 ATOM 1697 O O . PHE A 1 210 ? 58.549 7.043 7.437 1.00 17.95 ? 210 PHE A O 1 ATOM 1698 C CB . PHE A 1 210 ? 56.833 5.086 5.810 1.00 23.14 ? 210 PHE A CB 1 ATOM 1699 C CG . PHE A 1 210 ? 56.897 4.003 6.877 1.00 22.36 ? 210 PHE A CG 1 ATOM 1700 C CD1 . PHE A 1 210 ? 57.984 3.128 6.937 1.00 24.86 ? 210 PHE A CD1 1 ATOM 1701 C CD2 . PHE A 1 210 ? 55.857 3.900 7.829 1.00 31.86 ? 210 PHE A CD2 1 ATOM 1702 C CE1 . PHE A 1 210 ? 58.041 2.137 7.901 1.00 33.87 ? 210 PHE A CE1 1 ATOM 1703 C CE2 . PHE A 1 210 ? 55.895 2.914 8.838 1.00 34.82 ? 210 PHE A CE2 1 ATOM 1704 C CZ . PHE A 1 210 ? 57.000 2.040 8.867 1.00 35.81 ? 210 PHE A CZ 1 ATOM 1705 N N . PHE A 1 211 ? 56.751 6.979 8.829 1.00 19.18 ? 211 PHE A N 1 ATOM 1706 C CA . PHE A 1 211 ? 57.545 7.186 10.046 1.00 19.54 ? 211 PHE A CA 1 ATOM 1707 C C . PHE A 1 211 ? 57.880 5.844 10.662 1.00 19.79 ? 211 PHE A C 1 ATOM 1708 O O . PHE A 1 211 ? 56.947 5.132 11.161 1.00 25.65 ? 211 PHE A O 1 ATOM 1709 C CB . PHE A 1 211 ? 56.772 8.018 11.076 1.00 21.81 ? 211 PHE A CB 1 ATOM 1710 C CG . PHE A 1 211 ? 56.519 9.461 10.646 1.00 22.95 ? 211 PHE A CG 1 ATOM 1711 C CD1 . PHE A 1 211 ? 55.528 9.763 9.688 1.00 24.94 ? 211 PHE A CD1 1 ATOM 1712 C CD2 . PHE A 1 211 ? 57.287 10.514 11.175 1.00 24.37 ? 211 PHE A CD2 1 ATOM 1713 C CE1 . PHE A 1 211 ? 55.295 11.120 9.279 1.00 26.05 ? 211 PHE A CE1 1 ATOM 1714 C CE2 . PHE A 1 211 ? 57.042 11.893 10.775 1.00 24.25 ? 211 PHE A CE2 1 ATOM 1715 C CZ . PHE A 1 211 ? 56.055 12.158 9.834 1.00 24.78 ? 211 PHE A CZ 1 ATOM 1716 N N . ASN A 1 212 ? 59.154 5.459 10.539 1.00 21.75 ? 212 ASN A N 1 ATOM 1717 C CA . ASN A 1 212 ? 59.563 4.098 10.908 1.00 22.71 ? 212 ASN A CA 1 ATOM 1718 C C . ASN A 1 212 ? 60.029 4.041 12.383 1.00 29.58 ? 212 ASN A C 1 ATOM 1719 O O . ASN A 1 212 ? 60.112 5.063 13.075 1.00 29.28 ? 212 ASN A O 1 ATOM 1720 C CB . ASN A 1 212 ? 60.594 3.497 9.920 1.00 22.33 ? 212 ASN A CB 1 ATOM 1721 C CG . ASN A 1 212 ? 62.049 3.926 10.207 1.00 23.65 ? 212 ASN A CG 1 ATOM 1722 O OD1 . ASN A 1 212 ? 62.321 4.623 11.210 1.00 27.41 ? 212 ASN A OD1 1 ATOM 1723 N ND2 . ASN A 1 212 ? 62.976 3.563 9.299 1.00 25.52 ? 212 ASN A ND2 1 ATOM 1724 N N . SER A 1 213 ? 60.366 2.855 12.850 1.00 31.19 ? 213 SER A N 1 ATOM 1725 C CA . SER A 1 213 ? 60.703 2.686 14.264 1.00 34.96 ? 213 SER A CA 1 ATOM 1726 C C . SER A 1 213 ? 62.092 3.288 14.657 1.00 38.45 ? 213 SER A C 1 ATOM 1727 O O . SER A 1 213 ? 62.365 3.481 15.839 1.00 46.02 ? 213 SER A O 1 ATOM 1728 C CB . SER A 1 213 ? 60.633 1.197 14.587 1.00 34.44 ? 213 SER A CB 1 ATOM 1729 O OG . SER A 1 213 ? 61.671 0.554 13.867 1.00 41.15 ? 213 SER A OG 1 ATOM 1730 N N . ASP A 1 214 ? 62.961 3.562 13.684 1.00 32.92 ? 214 ASP A N 1 ATOM 1731 C CA . ASP A 1 214 ? 64.269 4.152 13.953 1.00 26.85 ? 214 ASP A CA 1 ATOM 1732 C C . ASP A 1 214 ? 64.269 5.687 13.985 1.00 29.84 ? 214 ASP A C 1 ATOM 1733 O O . ASP A 1 214 ? 65.356 6.276 13.927 1.00 34.00 ? 214 ASP A O 1 ATOM 1734 C CB . ASP A 1 214 ? 65.277 3.741 12.846 1.00 31.68 ? 214 ASP A CB 1 ATOM 1735 C CG . ASP A 1 214 ? 65.641 2.279 12.894 1.00 41.24 ? 214 ASP A CG 1 ATOM 1736 O OD1 . ASP A 1 214 ? 65.626 1.699 14.010 1.00 42.27 ? 214 ASP A OD1 1 ATOM 1737 O OD2 . ASP A 1 214 ? 65.924 1.721 11.798 1.00 47.66 ? 214 ASP A OD2 1 ATOM 1738 N N . GLY A 1 215 ? 63.095 6.350 14.043 1.00 24.20 ? 215 GLY A N 1 ATOM 1739 C CA . GLY A 1 215 ? 63.080 7.825 14.014 1.00 21.82 ? 215 GLY A CA 1 ATOM 1740 C C . GLY A 1 215 ? 63.300 8.367 12.591 1.00 18.00 ? 215 GLY A C 1 ATOM 1741 O O . GLY A 1 215 ? 63.429 9.559 12.423 1.00 21.09 ? 215 GLY A O 1 ATOM 1742 N N . ALA A 1 216 ? 63.324 7.508 11.560 1.00 19.11 ? 216 ALA A N 1 ATOM 1743 C CA . ALA A 1 216 ? 63.465 7.990 10.172 1.00 17.41 ? 216 ALA A CA 1 ATOM 1744 C C . ALA A 1 216 ? 62.108 8.319 9.530 1.00 18.99 ? 216 ALA A C 1 ATOM 1745 O O . ALA A 1 216 ? 61.067 7.756 9.926 1.00 18.67 ? 216 ALA A O 1 ATOM 1746 C CB . ALA A 1 216 ? 64.192 6.958 9.280 1.00 18.34 ? 216 ALA A CB 1 ATOM 1747 N N . ILE A 1 217 ? 62.152 9.229 8.533 1.00 16.77 ? 217 ILE A N 1 ATOM 1748 C CA . ILE A 1 217 ? 60.990 9.510 7.691 1.00 16.18 ? 217 ILE A CA 1 ATOM 1749 C C . ILE A 1 217 ? 61.367 9.010 6.301 1.00 15.17 ? 217 ILE A C 1 ATOM 1750 O O . ILE A 1 217 ? 62.216 9.586 5.629 1.00 16.83 ? 217 ILE A O 1 ATOM 1751 C CB . ILE A 1 217 ? 60.593 11.003 7.702 1.00 15.29 ? 217 ILE A CB 1 ATOM 1752 C CG1 . ILE A 1 217 ? 60.304 11.454 9.169 1.00 17.30 ? 217 ILE A CG1 1 ATOM 1753 C CG2 . ILE A 1 217 ? 59.303 11.178 6.833 1.00 16.37 ? 217 ILE A CG2 1 ATOM 1754 C CD1 . ILE A 1 217 ? 60.016 12.948 9.301 1.00 19.50 ? 217 ILE A CD1 1 ATOM 1755 N N . VAL A 1 218 ? 60.732 7.897 5.923 1.00 16.83 ? 218 VAL A N 1 ATOM 1756 C CA . VAL A 1 218 ? 61.135 7.119 4.763 1.00 15.98 ? 218 VAL A CA 1 ATOM 1757 C C . VAL A 1 218 ? 60.240 7.394 3.554 1.00 15.89 ? 218 VAL A C 1 ATOM 1758 O O . VAL A 1 218 ? 59.000 7.429 3.701 1.00 15.85 ? 218 VAL A O 1 ATOM 1759 C CB . VAL A 1 218 ? 61.032 5.603 5.101 1.00 15.39 ? 218 VAL A CB 1 ATOM 1760 C CG1 . VAL A 1 218 ? 61.536 4.778 3.927 1.00 19.96 ? 218 VAL A CG1 1 ATOM 1761 C CG2 . VAL A 1 218 ? 61.752 5.301 6.408 1.00 18.35 ? 218 VAL A CG2 1 ATOM 1762 N N . ASN A 1 219 ? 60.849 7.544 2.358 1.00 15.92 ? 219 ASN A N 1 ATOM 1763 C CA . ASN A 1 219 ? 60.053 7.584 1.088 1.00 15.84 ? 219 ASN A CA 1 ATOM 1764 C C . ASN A 1 219 ? 60.074 6.160 0.547 1.00 16.54 ? 219 ASN A C 1 ATOM 1765 O O . ASN A 1 219 ? 61.128 5.695 0.122 1.00 17.24 ? 219 ASN A O 1 ATOM 1766 C CB . ASN A 1 219 ? 60.733 8.548 0.099 1.00 15.70 ? 219 ASN A CB 1 ATOM 1767 C CG . ASN A 1 219 ? 60.096 8.506 -1.264 1.00 16.00 ? 219 ASN A CG 1 ATOM 1768 O OD1 . ASN A 1 219 ? 60.741 8.071 -2.256 1.00 17.09 ? 219 ASN A OD1 1 ATOM 1769 N ND2 . ASN A 1 219 ? 58.816 8.956 -1.344 1.00 16.08 ? 219 ASN A ND2 1 ATOM 1770 N N . PRO A 1 220 ? 58.920 5.433 0.608 1.00 15.74 ? 220 PRO A N 1 ATOM 1771 C CA . PRO A 1 220 ? 58.989 3.994 0.257 1.00 16.60 ? 220 PRO A CA 1 ATOM 1772 C C . PRO A 1 220 ? 59.517 3.705 -1.165 1.00 17.06 ? 220 PRO A C 1 ATOM 1773 O O . PRO A 1 220 ? 60.254 2.721 -1.326 1.00 18.04 ? 220 PRO A O 1 ATOM 1774 C CB . PRO A 1 220 ? 57.528 3.486 0.432 1.00 17.65 ? 220 PRO A CB 1 ATOM 1775 C CG . PRO A 1 220 ? 56.957 4.372 1.446 1.00 19.56 ? 220 PRO A CG 1 ATOM 1776 C CD . PRO A 1 220 ? 57.601 5.797 1.190 1.00 15.54 ? 220 PRO A CD 1 ATOM 1777 N N . LYS A 1 221 ? 59.113 4.484 -2.185 1.00 14.84 ? 221 LYS A N 1 ATOM 1778 C CA . LYS A 1 221 ? 59.604 4.146 -3.578 1.00 16.36 ? 221 LYS A CA 1 ATOM 1779 C C . LYS A 1 221 ? 61.138 4.167 -3.629 1.00 17.00 ? 221 LYS A C 1 ATOM 1780 O O . LYS A 1 221 ? 61.774 3.210 -4.121 1.00 22.23 ? 221 LYS A O 1 ATOM 1781 C CB . LYS A 1 221 ? 59.026 5.089 -4.656 1.00 19.51 ? 221 LYS A CB 1 ATOM 1782 C CG . LYS A 1 221 ? 59.635 4.932 -6.103 1.00 23.67 ? 221 LYS A CG 1 ATOM 1783 C CD . LYS A 1 221 ? 59.306 3.549 -6.686 1.00 31.71 ? 221 LYS A CD 1 ATOM 1784 C CE . LYS A 1 221 ? 59.978 3.367 -8.114 1.00 34.89 ? 221 LYS A CE 1 ATOM 1785 N NZ . LYS A 1 221 ? 59.877 4.639 -8.814 1.00 42.46 ? 221 LYS A NZ 1 ATOM 1786 N N . SER A 1 222 ? 61.728 5.273 -3.162 1.00 14.80 ? 222 SER A N 1 ATOM 1787 C CA . SER A 1 222 ? 63.182 5.400 -3.333 1.00 16.55 ? 222 SER A CA 1 ATOM 1788 C C . SER A 1 222 ? 63.931 4.555 -2.325 1.00 17.92 ? 222 SER A C 1 ATOM 1789 O O . SER A 1 222 ? 65.087 4.173 -2.604 1.00 20.28 ? 222 SER A O 1 ATOM 1790 C CB . SER A 1 222 ? 63.630 6.863 -3.186 1.00 17.58 ? 222 SER A CB 1 ATOM 1791 O OG . SER A 1 222 ? 63.398 7.336 -1.854 1.00 16.66 ? 222 SER A OG 1 ATOM 1792 N N . ARG A 1 223 ? 63.278 4.267 -1.193 1.00 16.54 ? 223 ARG A N 1 ATOM 1793 C CA . ARG A 1 223 ? 63.863 3.639 0.045 1.00 16.99 ? 223 ARG A CA 1 ATOM 1794 C C . ARG A 1 223 ? 64.605 4.644 0.914 1.00 16.38 ? 223 ARG A C 1 ATOM 1795 O O . ARG A 1 223 ? 65.019 4.297 2.031 1.00 18.92 ? 223 ARG A O 1 ATOM 1796 C CB . ARG A 1 223 ? 64.854 2.520 -0.283 1.00 17.69 ? 223 ARG A CB 1 ATOM 1797 C CG . ARG A 1 223 ? 64.303 1.433 -1.260 1.00 17.99 ? 223 ARG A CG 1 ATOM 1798 C CD . ARG A 1 223 ? 65.541 0.654 -1.815 1.00 18.43 ? 223 ARG A CD 1 ATOM 1799 N NE . ARG A 1 223 ? 65.170 -0.222 -2.931 1.00 19.58 ? 223 ARG A NE 1 ATOM 1800 C CZ . ARG A 1 223 ? 64.993 0.186 -4.187 1.00 19.76 ? 223 ARG A CZ 1 ATOM 1801 N NH1 . ARG A 1 223 ? 64.637 -0.700 -5.130 1.00 23.15 ? 223 ARG A NH1 1 ATOM 1802 N NH2 . ARG A 1 223 ? 65.106 1.481 -4.485 1.00 22.61 ? 223 ARG A NH2 1 ATOM 1803 N N . LEU A 1 224 ? 64.755 5.864 0.424 1.00 15.02 ? 224 LEU A N 1 ATOM 1804 C CA . LEU A 1 224 ? 65.643 6.836 1.042 1.00 16.10 ? 224 LEU A CA 1 ATOM 1805 C C . LEU A 1 224 ? 64.860 7.634 2.091 1.00 18.10 ? 224 LEU A C 1 ATOM 1806 O O . LEU A 1 224 ? 63.583 7.595 2.149 1.00 17.29 ? 224 LEU A O 1 ATOM 1807 C CB . LEU A 1 224 ? 66.254 7.725 -0.052 1.00 19.05 ? 224 LEU A CB 1 ATOM 1808 C CG . LEU A 1 224 ? 67.022 6.929 -1.133 1.00 16.60 ? 224 LEU A CG 1 ATOM 1809 C CD1 . LEU A 1 224 ? 67.810 7.961 -2.010 1.00 20.81 ? 224 LEU A CD1 1 ATOM 1810 C CD2 . LEU A 1 224 ? 67.973 5.892 -0.526 1.00 17.67 ? 224 LEU A CD2 1 ATOM 1811 N N . VAL A 1 225 ? 65.598 8.321 2.945 1.00 15.88 ? 225 VAL A N 1 ATOM 1812 C CA . VAL A 1 225 ? 64.956 8.958 4.124 1.00 15.34 ? 225 VAL A CA 1 ATOM 1813 C C . VAL A 1 225 ? 65.298 10.459 4.197 1.00 16.05 ? 225 VAL A C 1 ATOM 1814 O O . VAL A 1 225 ? 66.331 10.925 3.616 1.00 17.24 ? 225 VAL A O 1 ATOM 1815 C CB . VAL A 1 225 ? 65.362 8.263 5.456 1.00 15.23 ? 225 VAL A CB 1 ATOM 1816 C CG1 . VAL A 1 225 ? 65.239 6.739 5.368 1.00 17.40 ? 225 VAL A CG1 1 ATOM 1817 C CG2 . VAL A 1 225 ? 66.877 8.607 5.832 1.00 17.63 ? 225 VAL A CG2 1 ATOM 1818 N N A MET A 1 226 ? 64.436 11.259 4.839 0.50 16.61 ? 226 MET A N 1 ATOM 1819 N N B MET A 1 226 ? 64.490 11.204 4.958 0.50 15.87 ? 226 MET A N 1 ATOM 1820 C CA A MET A 1 226 ? 64.730 12.719 4.941 0.50 15.57 ? 226 MET A CA 1 ATOM 1821 C CA B MET A 1 226 ? 64.711 12.661 5.160 0.50 14.27 ? 226 MET A CA 1 ATOM 1822 C C A MET A 1 226 ? 66.023 12.891 5.722 0.50 17.03 ? 226 MET A C 1 ATOM 1823 C C B MET A 1 226 ? 66.012 12.960 5.882 0.50 15.75 ? 226 MET A C 1 ATOM 1824 O O A MET A 1 226 ? 66.287 12.154 6.681 0.50 18.49 ? 226 MET A O 1 ATOM 1825 O O B MET A 1 226 ? 66.255 12.399 6.968 0.50 13.81 ? 226 MET A O 1 ATOM 1826 C CB A MET A 1 226 ? 63.585 13.498 5.618 0.50 18.96 ? 226 MET A CB 1 ATOM 1827 C CB B MET A 1 226 ? 63.551 13.223 5.984 0.50 13.83 ? 226 MET A CB 1 ATOM 1828 C CG A MET A 1 226 ? 62.244 13.299 4.931 0.50 20.51 ? 226 MET A CG 1 ATOM 1829 C CG B MET A 1 226 ? 62.326 13.314 5.159 0.50 18.12 ? 226 MET A CG 1 ATOM 1830 S SD A MET A 1 226 ? 61.021 14.580 5.352 0.50 25.66 ? 226 MET A SD 1 ATOM 1831 S SD B MET A 1 226 ? 61.203 14.542 5.843 0.50 15.40 ? 226 MET A SD 1 ATOM 1832 C CE A MET A 1 226 ? 61.827 15.421 6.690 0.50 16.63 ? 226 MET A CE 1 ATOM 1833 C CE B MET A 1 226 ? 59.817 14.339 4.689 0.50 15.37 ? 226 MET A CE 1 ATOM 1834 N N . ASP A 1 227 ? 66.799 13.890 5.324 1.00 15.56 ? 227 ASP A N 1 ATOM 1835 C CA . ASP A 1 227 ? 68.190 14.065 5.801 1.00 17.09 ? 227 ASP A CA 1 ATOM 1836 C C . ASP A 1 227 ? 68.562 15.533 5.763 1.00 16.24 ? 227 ASP A C 1 ATOM 1837 O O . ASP A 1 227 ? 68.350 16.180 4.749 1.00 17.47 ? 227 ASP A O 1 ATOM 1838 C CB . ASP A 1 227 ? 69.067 13.182 4.871 1.00 18.47 ? 227 ASP A CB 1 ATOM 1839 C CG . ASP A 1 227 ? 70.563 13.364 5.070 1.00 17.01 ? 227 ASP A CG 1 ATOM 1840 O OD1 . ASP A 1 227 ? 71.235 12.312 5.192 1.00 18.85 ? 227 ASP A OD1 1 ATOM 1841 O OD2 . ASP A 1 227 ? 71.100 14.483 4.968 1.00 20.33 ? 227 ASP A OD2 1 ATOM 1842 N N . VAL A 1 228 ? 69.005 16.103 6.897 1.00 17.58 ? 228 VAL A N 1 ATOM 1843 C CA . VAL A 1 228 ? 69.456 17.491 6.887 1.00 17.34 ? 228 VAL A CA 1 ATOM 1844 C C . VAL A 1 228 ? 70.868 17.492 6.250 1.00 19.77 ? 228 VAL A C 1 ATOM 1845 O O . VAL A 1 228 ? 71.818 16.963 6.849 1.00 21.13 ? 228 VAL A O 1 ATOM 1846 C CB . VAL A 1 228 ? 69.541 18.049 8.336 1.00 18.57 ? 228 VAL A CB 1 ATOM 1847 C CG1 . VAL A 1 228 ? 70.034 19.477 8.329 1.00 21.69 ? 228 VAL A CG1 1 ATOM 1848 C CG2 . VAL A 1 228 ? 68.140 17.992 8.999 1.00 18.57 ? 228 VAL A CG2 1 ATOM 1849 N N . ARG A 1 229 ? 70.960 18.023 5.024 1.00 19.64 ? 229 ARG A N 1 ATOM 1850 C CA . ARG A 1 229 ? 72.135 17.861 4.177 1.00 22.08 ? 229 ARG A CA 1 ATOM 1851 C C . ARG A 1 229 ? 73.421 18.240 4.899 1.00 23.09 ? 229 ARG A C 1 ATOM 1852 O O . ARG A 1 229 ? 73.536 19.368 5.446 1.00 24.26 ? 229 ARG A O 1 ATOM 1853 C CB . ARG A 1 229 ? 71.993 18.658 2.874 1.00 19.83 ? 229 ARG A CB 1 ATOM 1854 C CG . ARG A 1 229 ? 73.199 18.410 1.900 1.00 23.13 ? 229 ARG A CG 1 ATOM 1855 C CD . ARG A 1 229 ? 72.966 19.103 0.550 1.00 24.73 ? 229 ARG A CD 1 ATOM 1856 N NE . ARG A 1 229 ? 74.181 18.978 -0.282 1.00 30.06 ? 229 ARG A NE 1 ATOM 1857 C CZ . ARG A 1 229 ? 74.192 19.100 -1.606 1.00 39.85 ? 229 ARG A CZ 1 ATOM 1858 N NH1 . ARG A 1 229 ? 73.076 19.349 -2.274 1.00 38.10 ? 229 ARG A NH1 1 ATOM 1859 N NH2 . ARG A 1 229 ? 75.336 18.939 -2.260 1.00 46.98 ? 229 ARG A NH2 1 ATOM 1860 N N . ALA A 1 230 ? 74.355 17.280 4.936 1.00 22.42 ? 230 ALA A N 1 ATOM 1861 C CA . ALA A 1 230 ? 75.688 17.497 5.551 1.00 24.05 ? 230 ALA A CA 1 ATOM 1862 C C . ALA A 1 230 ? 75.646 17.939 7.009 1.00 24.91 ? 230 ALA A C 1 ATOM 1863 O O . ALA A 1 230 ? 76.586 18.601 7.508 1.00 27.66 ? 230 ALA A O 1 ATOM 1864 C CB . ALA A 1 230 ? 76.565 18.481 4.680 1.00 25.79 ? 230 ALA A CB 1 ATOM 1865 N N . SER A 1 231 ? 74.568 17.578 7.699 1.00 22.99 ? 231 SER A N 1 ATOM 1866 C CA . SER A 1 231 ? 74.369 18.015 9.078 1.00 24.20 ? 231 SER A CA 1 ATOM 1867 C C . SER A 1 231 ? 74.649 19.515 9.216 1.00 26.72 ? 231 SER A C 1 ATOM 1868 O O . SER A 1 231 ? 75.205 19.977 10.249 1.00 28.67 ? 231 SER A O 1 ATOM 1869 C CB . SER A 1 231 ? 75.227 17.237 10.075 1.00 26.05 ? 231 SER A CB 1 ATOM 1870 O OG . SER A 1 231 ? 75.059 15.820 9.992 1.00 27.52 ? 231 SER A OG 1 ATOM 1871 N N . ASN A 1 232 ? 74.227 20.265 8.205 1.00 24.25 ? 232 ASN A N 1 ATOM 1872 C CA . ASN A 1 232 ? 74.470 21.695 8.148 1.00 28.57 ? 232 ASN A CA 1 ATOM 1873 C C . ASN A 1 232 ? 73.163 22.447 7.955 1.00 24.36 ? 232 ASN A C 1 ATOM 1874 O O . ASN A 1 232 ? 72.637 22.552 6.830 1.00 25.49 ? 232 ASN A O 1 ATOM 1875 C CB . ASN A 1 232 ? 75.445 22.003 7.006 1.00 30.00 ? 232 ASN A CB 1 ATOM 1876 C CG . ASN A 1 232 ? 75.872 23.430 6.999 1.00 30.75 ? 232 ASN A CG 1 ATOM 1877 O OD1 . ASN A 1 232 ? 75.169 24.296 7.529 1.00 33.11 ? 232 ASN A OD1 1 ATOM 1878 N ND2 . ASN A 1 232 ? 77.030 23.701 6.402 1.00 35.01 ? 232 ASN A ND2 1 ATOM 1879 N N . VAL A 1 233 ? 72.586 22.895 9.078 1.00 25.33 ? 233 VAL A N 1 ATOM 1880 C CA . VAL A 1 233 ? 71.284 23.571 9.000 1.00 24.42 ? 233 VAL A CA 1 ATOM 1881 C C . VAL A 1 233 ? 71.335 24.873 8.193 1.00 26.77 ? 233 VAL A C 1 ATOM 1882 O O . VAL A 1 233 ? 70.360 25.269 7.638 1.00 25.24 ? 233 VAL A O 1 ATOM 1883 C CB . VAL A 1 233 ? 70.606 23.811 10.403 1.00 27.76 ? 233 VAL A CB 1 ATOM 1884 C CG1 . VAL A 1 233 ? 70.472 22.520 11.222 1.00 24.55 ? 233 VAL A CG1 1 ATOM 1885 C CG2 . VAL A 1 233 ? 71.344 24.825 11.161 1.00 27.39 ? 233 VAL A CG2 1 ATOM 1886 N N A SER A 1 234 ? 72.484 25.548 8.131 0.50 29.62 ? 234 SER A N 1 ATOM 1887 N N B SER A 1 234 ? 72.514 25.498 8.145 0.50 28.19 ? 234 SER A N 1 ATOM 1888 C CA A SER A 1 234 ? 72.531 26.822 7.391 0.50 30.81 ? 234 SER A CA 1 ATOM 1889 C CA B SER A 1 234 ? 72.693 26.759 7.422 0.50 28.07 ? 234 SER A CA 1 ATOM 1890 C C A SER A 1 234 ? 72.581 26.643 5.863 0.50 28.76 ? 234 SER A C 1 ATOM 1891 C C B SER A 1 234 ? 72.513 26.616 5.909 0.50 27.26 ? 234 SER A C 1 ATOM 1892 O O A SER A 1 234 ? 72.529 27.611 5.125 0.50 30.49 ? 234 SER A O 1 ATOM 1893 O O B SER A 1 234 ? 72.200 27.580 5.233 0.50 28.71 ? 234 SER A O 1 ATOM 1894 C CB A SER A 1 234 ? 73.696 27.705 7.864 0.50 33.49 ? 234 SER A CB 1 ATOM 1895 C CB B SER A 1 234 ? 74.072 27.370 7.741 0.50 26.41 ? 234 SER A CB 1 ATOM 1896 O OG A SER A 1 234 ? 74.927 27.156 7.460 0.50 35.46 ? 234 SER A OG 1 ATOM 1897 O OG B SER A 1 234 ? 74.188 27.594 9.137 0.50 30.42 ? 234 SER A OG 1 ATOM 1898 N N . LEU A 1 235 ? 72.723 25.404 5.388 1.00 27.07 ? 235 LEU A N 1 ATOM 1899 C CA . LEU A 1 235 ? 72.536 25.149 3.961 1.00 24.83 ? 235 LEU A CA 1 ATOM 1900 C C . LEU A 1 235 ? 71.069 25.285 3.564 1.00 26.98 ? 235 LEU A C 1 ATOM 1901 O O . LEU A 1 235 ? 70.783 25.523 2.386 1.00 25.33 ? 235 LEU A O 1 ATOM 1902 C CB . LEU A 1 235 ? 73.020 23.764 3.539 1.00 24.12 ? 235 LEU A CB 1 ATOM 1903 C CG . LEU A 1 235 ? 74.499 23.415 3.590 1.00 33.60 ? 235 LEU A CG 1 ATOM 1904 C CD1 . LEU A 1 235 ? 74.588 21.917 3.304 1.00 31.13 ? 235 LEU A CD1 1 ATOM 1905 C CD2 . LEU A 1 235 ? 75.304 24.282 2.558 1.00 38.19 ? 235 LEU A CD2 1 ATOM 1906 N N . ARG A 1 236 ? 70.148 25.117 4.538 1.00 24.19 ? 236 ARG A N 1 ATOM 1907 C CA . ARG A 1 236 ? 68.707 25.145 4.254 1.00 24.99 ? 236 ARG A CA 1 ATOM 1908 C C . ARG A 1 236 ? 68.332 24.218 3.116 1.00 21.37 ? 236 ARG A C 1 ATOM 1909 O O . ARG A 1 236 ? 67.537 24.586 2.199 1.00 22.19 ? 236 ARG A O 1 ATOM 1910 C CB . ARG A 1 236 ? 68.222 26.576 3.983 1.00 23.47 ? 236 ARG A CB 1 ATOM 1911 C CG . ARG A 1 236 ? 68.243 27.384 5.271 1.00 25.24 ? 236 ARG A CG 1 ATOM 1912 C CD . ARG A 1 236 ? 67.817 28.803 5.132 1.00 27.64 ? 236 ARG A CD 1 ATOM 1913 N NE . ARG A 1 236 ? 67.539 29.328 6.469 1.00 39.13 ? 236 ARG A NE 1 ATOM 1914 C CZ . ARG A 1 236 ? 66.964 30.512 6.647 1.00 37.75 ? 236 ARG A CZ 1 ATOM 1915 N NH1 . ARG A 1 236 ? 66.679 30.968 7.886 1.00 31.80 ? 236 ARG A NH1 1 ATOM 1916 N NH2 . ARG A 1 236 ? 66.646 31.219 5.549 1.00 36.57 ? 236 ARG A NH2 1 ATOM 1917 N N . GLU A 1 237 ? 68.822 22.979 3.244 1.00 21.89 ? 237 GLU A N 1 ATOM 1918 C CA . GLU A 1 237 ? 68.501 21.926 2.277 1.00 20.59 ? 237 GLU A CA 1 ATOM 1919 C C . GLU A 1 237 ? 68.235 20.646 3.021 1.00 19.49 ? 237 GLU A C 1 ATOM 1920 O O . GLU A 1 237 ? 69.073 20.154 3.804 1.00 18.95 ? 237 GLU A O 1 ATOM 1921 C CB . GLU A 1 237 ? 69.666 21.697 1.270 1.00 24.30 ? 237 GLU A CB 1 ATOM 1922 C CG . GLU A 1 237 ? 69.808 22.939 0.339 1.00 26.36 ? 237 GLU A CG 1 ATOM 1923 C CD . GLU A 1 237 ? 70.802 22.737 -0.792 1.00 32.20 ? 237 GLU A CD 1 ATOM 1924 O OE1 . GLU A 1 237 ? 71.497 21.719 -0.777 1.00 33.65 ? 237 GLU A OE1 1 ATOM 1925 O OE2 . GLU A 1 237 ? 70.862 23.614 -1.701 1.00 43.38 ? 237 GLU A OE2 1 ATOM 1926 N N . ILE A 1 238 ? 67.062 20.090 2.753 1.00 20.13 ? 238 ILE A N 1 ATOM 1927 C CA . ILE A 1 238 ? 66.730 18.755 3.266 1.00 17.30 ? 238 ILE A CA 1 ATOM 1928 C C . ILE A 1 238 ? 66.673 17.887 2.025 1.00 19.15 ? 238 ILE A C 1 ATOM 1929 O O . ILE A 1 238 ? 66.037 18.262 1.017 1.00 19.68 ? 238 ILE A O 1 ATOM 1930 C CB . ILE A 1 238 ? 65.323 18.758 3.986 1.00 17.05 ? 238 ILE A CB 1 ATOM 1931 C CG1 . ILE A 1 238 ? 65.194 19.872 5.052 1.00 20.10 ? 238 ILE A CG1 1 ATOM 1932 C CG2 . ILE A 1 238 ? 65.025 17.359 4.571 1.00 20.27 ? 238 ILE A CG2 1 ATOM 1933 C CD1 . ILE A 1 238 ? 66.296 19.852 6.097 1.00 22.03 ? 238 ILE A CD1 1 ATOM 1934 N N . ILE A 1 239 ? 67.303 16.717 2.077 1.00 17.26 ? 239 ILE A N 1 ATOM 1935 C CA . ILE A 1 239 ? 67.404 15.862 0.894 1.00 17.12 ? 239 ILE A CA 1 ATOM 1936 C C . ILE A 1 239 ? 66.888 14.494 1.273 1.00 16.18 ? 239 ILE A C 1 ATOM 1937 O O . ILE A 1 239 ? 66.700 14.224 2.477 1.00 17.17 ? 239 ILE A O 1 ATOM 1938 C CB . ILE A 1 239 ? 68.875 15.719 0.429 1.00 18.80 ? 239 ILE A CB 1 ATOM 1939 C CG1 . ILE A 1 239 ? 69.774 15.231 1.611 1.00 17.89 ? 239 ILE A CG1 1 ATOM 1940 C CG2 . ILE A 1 239 ? 69.359 17.067 -0.149 1.00 20.56 ? 239 ILE A CG2 1 ATOM 1941 C CD1 . ILE A 1 239 ? 71.229 14.805 1.106 1.00 21.48 ? 239 ILE A CD1 1 ATOM 1942 N N . ILE A 1 240 ? 66.675 13.607 0.275 1.00 15.39 ? 240 ILE A N 1 ATOM 1943 C CA . ILE A 1 240 ? 66.561 12.174 0.596 1.00 14.73 ? 240 ILE A CA 1 ATOM 1944 C C . ILE A 1 240 ? 67.958 11.545 0.504 1.00 16.82 ? 240 ILE A C 1 ATOM 1945 O O . ILE A 1 240 ? 68.788 11.949 -0.323 1.00 18.10 ? 240 ILE A O 1 ATOM 1946 C CB . ILE A 1 240 ? 65.536 11.435 -0.305 1.00 16.15 ? 240 ILE A CB 1 ATOM 1947 C CG1 . ILE A 1 240 ? 65.864 11.596 -1.794 1.00 17.70 ? 240 ILE A CG1 1 ATOM 1948 C CG2 . ILE A 1 240 ? 64.050 11.873 -0.006 1.00 18.74 ? 240 ILE A CG2 1 ATOM 1949 C CD1 . ILE A 1 240 ? 65.012 10.709 -2.732 1.00 18.95 ? 240 ILE A CD1 1 ATOM 1950 N N . PHE A 1 241 ? 68.216 10.549 1.352 1.00 16.22 ? 241 PHE A N 1 ATOM 1951 C CA . PHE A 1 241 ? 69.528 9.950 1.422 1.00 16.46 ? 241 PHE A CA 1 ATOM 1952 C C . PHE A 1 241 ? 69.389 8.580 2.045 1.00 17.38 ? 241 PHE A C 1 ATOM 1953 O O . PHE A 1 241 ? 68.465 8.326 2.858 1.00 17.30 ? 241 PHE A O 1 ATOM 1954 C CB . PHE A 1 241 ? 70.435 10.829 2.313 1.00 18.33 ? 241 PHE A CB 1 ATOM 1955 C CG . PHE A 1 241 ? 71.929 10.592 2.088 1.00 18.00 ? 241 PHE A CG 1 ATOM 1956 C CD1 . PHE A 1 241 ? 72.554 11.071 0.934 1.00 19.23 ? 241 PHE A CD1 1 ATOM 1957 C CD2 . PHE A 1 241 ? 72.685 9.842 3.010 1.00 18.61 ? 241 PHE A CD2 1 ATOM 1958 C CE1 . PHE A 1 241 ? 73.960 10.813 0.702 1.00 22.27 ? 241 PHE A CE1 1 ATOM 1959 C CE2 . PHE A 1 241 ? 74.054 9.593 2.790 1.00 20.63 ? 241 PHE A CE2 1 ATOM 1960 C CZ . PHE A 1 241 ? 74.687 10.062 1.651 1.00 23.09 ? 241 PHE A CZ 1 ATOM 1961 N N . PRO A 1 242 ? 70.293 7.655 1.721 1.00 17.12 ? 242 PRO A N 1 ATOM 1962 C CA . PRO A 1 242 ? 70.184 6.362 2.378 1.00 17.35 ? 242 PRO A CA 1 ATOM 1963 C C . PRO A 1 242 ? 70.209 6.438 3.920 1.00 17.95 ? 242 PRO A C 1 ATOM 1964 O O . PRO A 1 242 ? 70.985 7.237 4.491 1.00 18.14 ? 242 PRO A O 1 ATOM 1965 C CB . PRO A 1 242 ? 71.465 5.632 1.905 1.00 20.36 ? 242 PRO A CB 1 ATOM 1966 C CG . PRO A 1 242 ? 71.953 6.371 0.728 1.00 25.33 ? 242 PRO A CG 1 ATOM 1967 C CD . PRO A 1 242 ? 71.328 7.703 0.667 1.00 18.85 ? 242 PRO A CD 1 ATOM 1968 N N . ALA A 1 243 ? 69.443 5.572 4.588 1.00 18.68 ? 243 ALA A N 1 ATOM 1969 C CA . ALA A 1 243 ? 69.356 5.616 6.080 1.00 17.83 ? 243 ALA A CA 1 ATOM 1970 C C . ALA A 1 243 ? 70.711 5.280 6.737 1.00 16.94 ? 243 ALA A C 1 ATOM 1971 O O . ALA A 1 243 ? 71.315 4.241 6.447 1.00 18.07 ? 243 ALA A O 1 ATOM 1972 C CB . ALA A 1 243 ? 68.293 4.674 6.589 1.00 18.27 ? 243 ALA A CB 1 ATOM 1973 N N . THR A 1 244 ? 71.162 6.153 7.640 1.00 18.56 ? 244 THR A N 1 ATOM 1974 C CA . THR A 1 244 ? 72.451 5.960 8.365 1.00 18.33 ? 244 THR A CA 1 ATOM 1975 C C . THR A 1 244 ? 72.267 5.848 9.866 1.00 22.58 ? 244 THR A C 1 ATOM 1976 O O . THR A 1 244 ? 73.202 5.495 10.584 1.00 25.32 ? 244 THR A O 1 ATOM 1977 C CB . THR A 1 244 ? 73.392 7.174 8.179 1.00 18.01 ? 244 THR A CB 1 ATOM 1978 O OG1 . THR A 1 244 ? 72.683 8.318 8.674 1.00 21.58 ? 244 THR A OG1 1 ATOM 1979 C CG2 . THR A 1 244 ? 73.722 7.395 6.713 1.00 18.71 ? 244 THR A CG2 1 ATOM 1980 N N . GLY A 1 245 ? 71.084 6.211 10.363 1.00 19.82 ? 245 GLY A N 1 ATOM 1981 C CA . GLY A 1 245 ? 70.840 6.273 11.826 1.00 23.94 ? 245 GLY A CA 1 ATOM 1982 C C . GLY A 1 245 ? 71.455 7.495 12.522 1.00 23.39 ? 245 GLY A C 1 ATOM 1983 O O . GLY A 1 245 ? 71.432 7.584 13.772 1.00 30.49 ? 245 GLY A O 1 ATOM 1984 N N . ASN A 1 246 ? 72.061 8.389 11.755 1.00 23.79 ? 246 ASN A N 1 ATOM 1985 C CA . ASN A 1 246 ? 72.776 9.564 12.329 1.00 23.49 ? 246 ASN A CA 1 ATOM 1986 C C . ASN A 1 246 ? 71.774 10.656 12.788 1.00 23.59 ? 246 ASN A C 1 ATOM 1987 O O . ASN A 1 246 ? 70.614 10.653 12.349 1.00 22.51 ? 246 ASN A O 1 ATOM 1988 C CB . ASN A 1 246 ? 73.713 10.161 11.313 1.00 25.09 ? 246 ASN A CB 1 ATOM 1989 C CG . ASN A 1 246 ? 74.907 9.239 11.013 1.00 26.87 ? 246 ASN A CG 1 ATOM 1990 O OD1 . ASN A 1 246 ? 75.298 8.389 11.857 1.00 30.87 ? 246 ASN A OD1 1 ATOM 1991 N ND2 . ASN A 1 246 ? 75.503 9.431 9.854 1.00 26.90 ? 246 ASN A ND2 1 ATOM 1992 N N . PRO A 1 247 ? 72.197 11.525 13.712 1.00 22.75 ? 247 PRO A N 1 ATOM 1993 C CA . PRO A 1 247 ? 71.302 12.573 14.228 1.00 21.02 ? 247 PRO A CA 1 ATOM 1994 C C . PRO A 1 247 ? 70.602 13.412 13.132 1.00 20.40 ? 247 PRO A C 1 ATOM 1995 O O . PRO A 1 247 ? 69.459 13.872 13.356 1.00 21.98 ? 247 PRO A O 1 ATOM 1996 C CB . PRO A 1 247 ? 72.247 13.473 15.048 1.00 24.48 ? 247 PRO A CB 1 ATOM 1997 C CG . PRO A 1 247 ? 73.293 12.420 15.605 1.00 26.47 ? 247 PRO A CG 1 ATOM 1998 C CD . PRO A 1 247 ? 73.484 11.462 14.450 1.00 23.92 ? 247 PRO A CD 1 ATOM 1999 N N . ASN A 1 248 ? 71.256 13.617 11.989 1.00 18.64 ? 248 ASN A N 1 ATOM 2000 C CA . ASN A 1 248 ? 70.639 14.487 10.944 1.00 17.67 ? 248 ASN A CA 1 ATOM 2001 C C . ASN A 1 248 ? 69.540 13.763 10.164 1.00 16.38 ? 248 ASN A C 1 ATOM 2002 O O . ASN A 1 248 ? 69.024 14.302 9.177 1.00 18.97 ? 248 ASN A O 1 ATOM 2003 C CB . ASN A 1 248 ? 71.688 15.038 9.972 1.00 21.88 ? 248 ASN A CB 1 ATOM 2004 C CG . ASN A 1 248 ? 72.310 13.945 9.095 1.00 21.08 ? 248 ASN A CG 1 ATOM 2005 O OD1 . ASN A 1 248 ? 72.527 12.827 9.580 1.00 23.21 ? 248 ASN A OD1 1 ATOM 2006 N ND2 . ASN A 1 248 ? 72.569 14.249 7.805 1.00 19.56 ? 248 ASN A ND2 1 ATOM 2007 N N . GLN A 1 249 ? 69.216 12.524 10.580 1.00 17.63 ? 249 GLN A N 1 ATOM 2008 C CA . GLN A 1 249 ? 68.145 11.772 9.957 1.00 18.53 ? 249 GLN A CA 1 ATOM 2009 C C . GLN A 1 249 ? 67.108 11.325 10.998 1.00 18.59 ? 249 GLN A C 1 ATOM 2010 O O . GLN A 1 249 ? 66.226 10.495 10.686 1.00 19.37 ? 249 GLN A O 1 ATOM 2011 C CB . GLN A 1 249 ? 68.699 10.488 9.260 1.00 17.92 ? 249 GLN A CB 1 ATOM 2012 C CG . GLN A 1 249 ? 69.518 10.777 7.986 1.00 18.98 ? 249 GLN A CG 1 ATOM 2013 C CD . GLN A 1 249 ? 69.869 9.495 7.262 1.00 17.53 ? 249 GLN A CD 1 ATOM 2014 O OE1 . GLN A 1 249 ? 69.585 8.411 7.772 1.00 19.55 ? 249 GLN A OE1 1 ATOM 2015 N NE2 . GLN A 1 249 ? 70.484 9.605 6.080 1.00 20.80 ? 249 GLN A NE2 1 ATOM 2016 N N . GLN A 1 250 ? 67.208 11.885 12.225 1.00 18.66 ? 250 GLN A N 1 ATOM 2017 C CA . GLN A 1 250 ? 66.298 11.480 13.307 1.00 20.39 ? 250 GLN A CA 1 ATOM 2018 C C . GLN A 1 250 ? 65.221 12.539 13.477 1.00 17.83 ? 250 GLN A C 1 ATOM 2019 O O . GLN A 1 250 ? 65.523 13.737 13.498 1.00 18.63 ? 250 GLN A O 1 ATOM 2020 C CB . GLN A 1 250 ? 67.083 11.280 14.614 1.00 21.43 ? 250 GLN A CB 1 ATOM 2021 C CG . GLN A 1 250 ? 67.975 10.025 14.608 1.00 27.16 ? 250 GLN A CG 1 ATOM 2022 C CD . GLN A 1 250 ? 67.209 8.771 15.025 1.00 47.42 ? 250 GLN A CD 1 ATOM 2023 O OE1 . GLN A 1 250 ? 66.066 8.840 15.535 1.00 45.49 ? 250 GLN A OE1 1 ATOM 2024 N NE2 . GLN A 1 250 ? 67.845 7.599 14.826 1.00 57.99 ? 250 GLN A NE2 1 ATOM 2025 N N . TRP A 1 251 ? 63.966 12.095 13.583 1.00 18.60 ? 251 TRP A N 1 ATOM 2026 C CA . TRP A 1 251 ? 62.798 12.976 13.649 1.00 18.11 ? 251 TRP A CA 1 ATOM 2027 C C . TRP A 1 251 ? 61.788 12.444 14.630 1.00 17.73 ? 251 TRP A C 1 ATOM 2028 O O . TRP A 1 251 ? 61.713 11.212 14.879 1.00 21.23 ? 251 TRP A O 1 ATOM 2029 C CB . TRP A 1 251 ? 62.113 13.045 12.257 1.00 18.77 ? 251 TRP A CB 1 ATOM 2030 C CG . TRP A 1 251 ? 63.084 13.358 11.103 1.00 15.88 ? 251 TRP A CG 1 ATOM 2031 C CD1 . TRP A 1 251 ? 63.756 12.455 10.366 1.00 17.64 ? 251 TRP A CD1 1 ATOM 2032 C CD2 . TRP A 1 251 ? 63.428 14.663 10.572 1.00 15.82 ? 251 TRP A CD2 1 ATOM 2033 N NE1 . TRP A 1 251 ? 64.509 13.094 9.380 1.00 17.90 ? 251 TRP A NE1 1 ATOM 2034 C CE2 . TRP A 1 251 ? 64.356 14.450 9.497 1.00 16.19 ? 251 TRP A CE2 1 ATOM 2035 C CE3 . TRP A 1 251 ? 63.064 15.994 10.913 1.00 16.76 ? 251 TRP A CE3 1 ATOM 2036 C CZ2 . TRP A 1 251 ? 64.892 15.498 8.738 1.00 16.55 ? 251 TRP A CZ2 1 ATOM 2037 C CZ3 . TRP A 1 251 ? 63.616 17.059 10.160 1.00 17.03 ? 251 TRP A CZ3 1 ATOM 2038 C CH2 . TRP A 1 251 ? 64.533 16.791 9.080 1.00 15.82 ? 251 TRP A CH2 1 ATOM 2039 N N A VAL A 1 252 ? 61.012 13.341 15.229 0.50 17.87 ? 252 VAL A N 1 ATOM 2040 N N B VAL A 1 252 ? 61.039 13.368 15.238 0.50 19.03 ? 252 VAL A N 1 ATOM 2041 C CA A VAL A 1 252 ? 59.878 12.908 16.024 0.50 19.32 ? 252 VAL A CA 1 ATOM 2042 C CA B VAL A 1 252 ? 59.938 13.026 16.129 0.50 21.16 ? 252 VAL A CA 1 ATOM 2043 C C A VAL A 1 252 ? 58.754 13.908 15.880 0.50 19.78 ? 252 VAL A C 1 ATOM 2044 C C B VAL A 1 252 ? 58.750 13.930 15.801 0.50 20.83 ? 252 VAL A C 1 ATOM 2045 O O A VAL A 1 252 ? 59.003 15.128 15.798 0.50 20.43 ? 252 VAL A O 1 ATOM 2046 O O B VAL A 1 252 ? 58.951 15.111 15.477 0.50 20.50 ? 252 VAL A O 1 ATOM 2047 C CB A VAL A 1 252 ? 60.214 12.776 17.530 0.50 17.90 ? 252 VAL A CB 1 ATOM 2048 C CB B VAL A 1 252 ? 60.324 13.198 17.639 0.50 24.99 ? 252 VAL A CB 1 ATOM 2049 C CG1 A VAL A 1 252 ? 61.207 11.649 17.841 0.50 24.46 ? 252 VAL A CG1 1 ATOM 2050 C CG1 B VAL A 1 252 ? 59.358 12.389 18.517 0.50 30.91 ? 252 VAL A CG1 1 ATOM 2051 C CG2 A VAL A 1 252 ? 60.657 14.106 18.089 0.50 15.11 ? 252 VAL A CG2 1 ATOM 2052 C CG2 B VAL A 1 252 ? 61.771 12.767 17.925 0.50 23.17 ? 252 VAL A CG2 1 ATOM 2053 N N . THR A 1 253 ? 57.523 13.412 15.868 1.00 20.50 ? 253 THR A N 1 ATOM 2054 C CA . THR A 1 253 ? 56.346 14.301 15.779 1.00 20.78 ? 253 THR A CA 1 ATOM 2055 C C . THR A 1 253 ? 56.018 14.812 17.165 1.00 18.31 ? 253 THR A C 1 ATOM 2056 O O . THR A 1 253 ? 56.102 14.060 18.175 1.00 24.86 ? 253 THR A O 1 ATOM 2057 C CB . THR A 1 253 ? 55.149 13.647 15.130 1.00 23.28 ? 253 THR A CB 1 ATOM 2058 O OG1 . THR A 1 253 ? 54.885 12.445 15.850 1.00 27.79 ? 253 THR A OG1 1 ATOM 2059 C CG2 . THR A 1 253 ? 55.484 13.291 13.683 1.00 26.86 ? 253 THR A CG2 1 ATOM 2060 N N . GLN A 1 254 ? 55.672 16.103 17.244 1.00 18.00 ? 254 GLN A N 1 ATOM 2061 C CA . GLN A 1 254 ? 55.176 16.655 18.512 1.00 20.08 ? 254 GLN A CA 1 ATOM 2062 C C . GLN A 1 254 ? 53.822 17.316 18.266 1.00 19.20 ? 254 GLN A C 1 ATOM 2063 O O . GLN A 1 254 ? 53.715 18.316 17.545 1.00 21.81 ? 254 GLN A O 1 ATOM 2064 C CB . GLN A 1 254 ? 56.209 17.627 19.137 1.00 23.41 ? 254 GLN A CB 1 ATOM 2065 C CG . GLN A 1 254 ? 57.526 16.929 19.581 1.00 26.33 ? 254 GLN A CG 1 ATOM 2066 C CD . GLN A 1 254 ? 57.348 15.923 20.774 1.00 39.27 ? 254 GLN A CD 1 ATOM 2067 O OE1 . GLN A 1 254 ? 58.114 14.968 20.906 1.00 44.72 ? 254 GLN A OE1 1 ATOM 2068 N NE2 . GLN A 1 254 ? 56.327 16.138 21.614 1.00 45.27 ? 254 GLN A NE2 1 ATOM 2069 N N . VAL A 1 255 ? 52.766 16.687 18.766 1.00 20.13 ? 255 VAL A N 1 ATOM 2070 C CA . VAL A 1 255 ? 51.418 17.164 18.537 1.00 23.02 ? 255 VAL A CA 1 ATOM 2071 C C . VAL A 1 255 ? 51.292 18.582 19.037 1.00 25.13 ? 255 VAL A C 1 ATOM 2072 O O . VAL A 1 255 ? 51.872 18.980 20.092 1.00 23.67 ? 255 VAL A O 1 ATOM 2073 C CB . VAL A 1 255 ? 50.410 16.215 19.193 1.00 31.06 ? 255 VAL A CB 1 ATOM 2074 C CG1 . VAL A 1 255 ? 48.984 16.763 19.061 1.00 34.37 ? 255 VAL A CG1 1 ATOM 2075 C CG2 . VAL A 1 255 ? 50.511 14.867 18.453 1.00 33.94 ? 255 VAL A CG2 1 ATOM 2076 N N . LEU A 1 256 ? 50.530 19.340 18.268 1.00 21.11 ? 256 LEU A N 1 ATOM 2077 C CA . LEU A 1 256 ? 50.271 20.769 18.548 1.00 20.34 ? 256 LEU A CA 1 ATOM 2078 C C . LEU A 1 256 ? 48.943 20.994 19.260 1.00 25.60 ? 256 LEU A C 1 ATOM 2079 O O . LEU A 1 256 ? 48.024 20.213 19.090 1.00 26.14 ? 256 LEU A O 1 ATOM 2080 C CB . LEU A 1 256 ? 50.281 21.563 17.232 1.00 21.23 ? 256 LEU A CB 1 ATOM 2081 C CG . LEU A 1 256 ? 51.716 21.745 16.690 1.00 22.36 ? 256 LEU A CG 1 ATOM 2082 C CD1 . LEU A 1 256 ? 51.666 22.008 15.211 1.00 24.36 ? 256 LEU A CD1 1 ATOM 2083 C CD2 . LEU A 1 256 ? 52.424 22.936 17.414 1.00 28.38 ? 256 LEU A CD2 1 ATOM 2084 N N . PRO A 1 257 ? 48.855 22.055 20.093 1.00 24.28 ? 257 PRO A N 1 ATOM 2085 C CA . PRO A 1 257 ? 47.591 22.307 20.765 1.00 26.32 ? 257 PRO A CA 1 ATOM 2086 C C . PRO A 1 257 ? 46.538 22.878 19.830 1.00 34.85 ? 257 PRO A C 1 ATOM 2087 O O . PRO A 1 257 ? 46.916 23.601 18.875 1.00 32.61 ? 257 PRO A O 1 ATOM 2088 C CB . PRO A 1 257 ? 47.974 23.320 21.845 1.00 27.23 ? 257 PRO A CB 1 ATOM 2089 C CG . PRO A 1 257 ? 49.261 23.997 21.375 1.00 27.24 ? 257 PRO A CG 1 ATOM 2090 C CD . PRO A 1 257 ? 49.909 23.032 20.450 1.00 24.66 ? 257 PRO A CD 1 HETATM 2091 C C1 . NAG B 2 . ? 48.263 -0.497 -14.303 1.00 32.59 ? 258 NAG A C1 1 HETATM 2092 C C2 . NAG B 2 . ? 49.344 -0.308 -15.405 1.00 34.95 ? 258 NAG A C2 1 HETATM 2093 C C3 . NAG B 2 . ? 49.837 1.151 -15.532 1.00 36.81 ? 258 NAG A C3 1 HETATM 2094 C C4 . NAG B 2 . ? 48.661 2.109 -15.534 1.00 38.30 ? 258 NAG A C4 1 HETATM 2095 C C5 . NAG B 2 . ? 47.687 1.802 -14.376 1.00 36.77 ? 258 NAG A C5 1 HETATM 2096 C C6 . NAG B 2 . ? 46.436 2.671 -14.452 1.00 41.27 ? 258 NAG A C6 1 HETATM 2097 C C7 . NAG B 2 . ? 50.784 -2.239 -15.884 1.00 49.76 ? 258 NAG A C7 1 HETATM 2098 C C8 . NAG B 2 . ? 52.079 -2.923 -15.540 1.00 54.83 ? 258 NAG A C8 1 HETATM 2099 N N2 . NAG B 2 . ? 50.458 -1.193 -15.119 1.00 41.54 ? 258 NAG A N2 1 HETATM 2100 O O3 . NAG B 2 . ? 50.599 1.358 -16.740 1.00 39.57 ? 258 NAG A O3 1 HETATM 2101 O O4 . NAG B 2 . ? 49.163 3.417 -15.409 1.00 45.47 ? 258 NAG A O4 1 HETATM 2102 O O5 . NAG B 2 . ? 47.233 0.468 -14.475 1.00 32.93 ? 258 NAG A O5 1 HETATM 2103 O O6 . NAG B 2 . ? 45.776 2.362 -15.683 1.00 39.59 ? 258 NAG A O6 1 HETATM 2104 O O7 . NAG B 2 . ? 50.137 -2.658 -16.841 1.00 55.87 ? 258 NAG A O7 1 HETATM 2105 C C1 . NAG C 2 . ? 48.620 4.309 -16.395 1.00 50.71 ? 259 NAG A C1 1 HETATM 2106 C C2 . NAG C 2 . ? 49.089 5.736 -16.088 1.00 62.77 ? 259 NAG A C2 1 HETATM 2107 C C3 . NAG C 2 . ? 48.564 6.703 -17.140 1.00 61.73 ? 259 NAG A C3 1 HETATM 2108 C C4 . NAG C 2 . ? 48.872 6.178 -18.547 1.00 57.74 ? 259 NAG A C4 1 HETATM 2109 C C5 . NAG C 2 . ? 48.355 4.748 -18.707 1.00 49.70 ? 259 NAG A C5 1 HETATM 2110 C C6 . NAG C 2 . ? 48.691 4.208 -20.094 1.00 46.55 ? 259 NAG A C6 1 HETATM 2111 C C7 . NAG C 2 . ? 49.551 6.324 -13.751 1.00 79.56 ? 259 NAG A C7 1 HETATM 2112 C C8 . NAG C 2 . ? 49.199 7.363 -12.712 1.00 69.63 ? 259 NAG A C8 1 HETATM 2113 N N2 . NAG C 2 . ? 48.685 6.202 -14.769 1.00 61.43 ? 259 NAG A N2 1 HETATM 2114 O O3 . NAG C 2 . ? 49.163 7.962 -16.913 1.00 71.86 ? 259 NAG A O3 1 HETATM 2115 O O4 . NAG C 2 . ? 48.322 7.025 -19.531 1.00 57.56 ? 259 NAG A O4 1 HETATM 2116 O O5 . NAG C 2 . ? 48.968 3.940 -17.717 1.00 49.13 ? 259 NAG A O5 1 HETATM 2117 O O6 . NAG C 2 . ? 48.102 2.935 -20.337 1.00 46.72 ? 259 NAG A O6 1 HETATM 2118 O O7 . NAG C 2 . ? 50.585 5.641 -13.625 1.00 71.42 ? 259 NAG A O7 1 HETATM 2119 C C1 . FUC D 3 . ? 52.069 1.415 -16.553 1.00 42.85 ? 260 FUC A C1 1 HETATM 2120 C C2 . FUC D 3 . ? 52.700 1.115 -17.913 1.00 45.48 ? 260 FUC A C2 1 HETATM 2121 C C3 . FUC D 3 . ? 52.488 2.269 -18.888 1.00 52.12 ? 260 FUC A C3 1 HETATM 2122 C C4 . FUC D 3 . ? 52.973 3.602 -18.320 1.00 53.60 ? 260 FUC A C4 1 HETATM 2123 C C5 . FUC D 3 . ? 52.330 3.784 -16.954 1.00 49.00 ? 260 FUC A C5 1 HETATM 2124 C C6 . FUC D 3 . ? 52.768 5.099 -16.323 1.00 53.53 ? 260 FUC A C6 1 HETATM 2125 O O2 . FUC D 3 . ? 52.123 -0.010 -18.529 1.00 43.82 ? 260 FUC A O2 1 HETATM 2126 O O3 . FUC D 3 . ? 53.125 1.924 -20.102 1.00 59.09 ? 260 FUC A O3 1 HETATM 2127 O O4 . FUC D 3 . ? 54.387 3.614 -18.191 1.00 57.34 ? 260 FUC A O4 1 HETATM 2128 O O5 . FUC D 3 . ? 52.645 2.659 -16.135 1.00 45.87 ? 260 FUC A O5 1 HETATM 2129 C C1 . NAG E 2 . ? 26.097 -15.322 2.678 1.00 27.99 ? 261 NAG A C1 1 HETATM 2130 C C2 . NAG E 2 . ? 25.006 -14.731 3.548 1.00 32.44 ? 261 NAG A C2 1 HETATM 2131 C C3 . NAG E 2 . ? 24.392 -15.865 4.377 1.00 36.92 ? 261 NAG A C3 1 HETATM 2132 C C4 . NAG E 2 . ? 23.936 -17.000 3.466 1.00 36.99 ? 261 NAG A C4 1 HETATM 2133 C C5 . NAG E 2 . ? 25.108 -17.428 2.593 1.00 38.01 ? 261 NAG A C5 1 HETATM 2134 C C6 . NAG E 2 . ? 24.761 -18.580 1.662 1.00 39.07 ? 261 NAG A C6 1 HETATM 2135 C C7 . NAG E 2 . ? 25.169 -12.459 4.462 1.00 29.70 ? 261 NAG A C7 1 HETATM 2136 C C8 . NAG E 2 . ? 25.761 -11.539 5.484 1.00 34.46 ? 261 NAG A C8 1 HETATM 2137 N N2 . NAG E 2 . ? 25.575 -13.733 4.440 1.00 32.73 ? 261 NAG A N2 1 HETATM 2138 O O3 . NAG E 2 . ? 23.339 -15.372 5.200 1.00 39.35 ? 261 NAG A O3 1 HETATM 2139 O O4 . NAG E 2 . ? 23.547 -18.102 4.296 1.00 40.43 ? 261 NAG A O4 1 HETATM 2140 O O5 . NAG E 2 . ? 25.564 -16.320 1.824 1.00 33.71 ? 261 NAG A O5 1 HETATM 2141 O O6 . NAG E 2 . ? 23.871 -18.123 0.671 1.00 43.76 ? 261 NAG A O6 1 HETATM 2142 O O7 . NAG E 2 . ? 24.335 -12.027 3.671 1.00 34.16 ? 261 NAG A O7 1 HETATM 2143 C C1 . NAG F 2 . ? 22.241 -18.560 3.894 1.00 47.20 ? 262 NAG A C1 1 HETATM 2144 C C2 . NAG F 2 . ? 22.006 -19.923 4.547 1.00 50.28 ? 262 NAG A C2 1 HETATM 2145 C C3 . NAG F 2 . ? 20.538 -20.380 4.456 1.00 56.29 ? 262 NAG A C3 1 HETATM 2146 C C4 . NAG F 2 . ? 19.592 -19.214 4.742 1.00 58.50 ? 262 NAG A C4 1 HETATM 2147 C C5 . NAG F 2 . ? 19.956 -18.106 3.744 1.00 54.58 ? 262 NAG A C5 1 HETATM 2148 C C6 . NAG F 2 . ? 18.972 -16.943 3.627 1.00 53.53 ? 262 NAG A C6 1 HETATM 2149 C C7 . NAG F 2 . ? 24.025 -21.233 4.520 1.00 53.31 ? 262 NAG A C7 1 HETATM 2150 C C8 . NAG F 2 . ? 24.929 -22.176 3.778 1.00 56.62 ? 262 NAG A C8 1 HETATM 2151 N N2 . NAG F 2 . ? 22.915 -20.839 3.889 1.00 46.88 ? 262 NAG A N2 1 HETATM 2152 O O3 . NAG F 2 . ? 20.287 -21.436 5.359 1.00 59.12 ? 262 NAG A O3 1 HETATM 2153 O O4 . NAG F 2 . ? 18.243 -19.628 4.652 1.00 63.97 ? 262 NAG A O4 1 HETATM 2154 O O5 . NAG F 2 . ? 21.213 -17.631 4.190 1.00 53.27 ? 262 NAG A O5 1 HETATM 2155 O O6 . NAG F 2 . ? 19.077 -16.187 4.807 1.00 53.74 ? 262 NAG A O6 1 HETATM 2156 O O7 . NAG F 2 . ? 24.317 -20.876 5.671 1.00 58.00 ? 262 NAG A O7 1 HETATM 2157 C C1 . FUC G 3 . ? 23.814 -15.255 6.566 1.00 50.67 ? 263 FUC A C1 1 HETATM 2158 C C2 . FUC G 3 . ? 22.818 -14.437 7.378 1.00 54.02 ? 263 FUC A C2 1 HETATM 2159 C C3 . FUC G 3 . ? 21.481 -15.205 7.428 1.00 58.12 ? 263 FUC A C3 1 HETATM 2160 C C4 . FUC G 3 . ? 21.692 -16.566 8.079 1.00 58.32 ? 263 FUC A C4 1 HETATM 2161 C C5 . FUC G 3 . ? 22.755 -17.288 7.246 1.00 59.51 ? 263 FUC A C5 1 HETATM 2162 C C6 . FUC G 3 . ? 23.041 -18.707 7.715 1.00 63.48 ? 263 FUC A C6 1 HETATM 2163 O O2 . FUC G 3 . ? 22.663 -13.168 6.781 1.00 53.20 ? 263 FUC A O2 1 HETATM 2164 O O3 . FUC G 3 . ? 20.471 -14.493 8.103 1.00 59.76 ? 263 FUC A O3 1 HETATM 2165 O O4 . FUC G 3 . ? 22.143 -16.373 9.406 1.00 58.23 ? 263 FUC A O4 1 HETATM 2166 O O5 . FUC G 3 . ? 23.966 -16.521 7.193 1.00 56.63 ? 263 FUC A O5 1 HETATM 2167 C C1 . NAG H 2 . ? 45.585 23.462 11.141 1.00 25.83 ? 264 NAG A C1 1 HETATM 2168 C C2 . NAG H 2 . ? 45.347 24.476 12.256 1.00 29.74 ? 264 NAG A C2 1 HETATM 2169 C C3 . NAG H 2 . ? 43.874 24.326 12.666 1.00 31.77 ? 264 NAG A C3 1 HETATM 2170 C C4 . NAG H 2 . ? 42.839 24.377 11.509 1.00 33.66 ? 264 NAG A C4 1 HETATM 2171 C C5 . NAG H 2 . ? 43.296 23.443 10.409 1.00 30.11 ? 264 NAG A C5 1 HETATM 2172 C C6 . NAG H 2 . ? 42.450 23.512 9.155 1.00 32.96 ? 264 NAG A C6 1 HETATM 2173 C C7 . NAG H 2 . ? 46.418 23.349 14.171 1.00 28.86 ? 264 NAG A C7 1 HETATM 2174 C C8 . NAG H 2 . ? 47.507 23.333 15.203 1.00 30.57 ? 264 NAG A C8 1 HETATM 2175 N N2 . NAG H 2 . ? 46.331 24.423 13.363 1.00 29.34 ? 264 NAG A N2 1 HETATM 2176 O O3 . NAG H 2 . ? 43.596 25.377 13.557 1.00 39.83 ? 264 NAG A O3 1 HETATM 2177 O O4 . NAG H 2 . ? 41.514 23.931 11.878 1.00 34.62 ? 264 NAG A O4 1 HETATM 2178 O O5 . NAG H 2 . ? 44.662 23.755 10.094 1.00 26.84 ? 264 NAG A O5 1 HETATM 2179 O O6 . NAG H 2 . ? 42.504 24.858 8.758 1.00 31.90 ? 264 NAG A O6 1 HETATM 2180 O O7 . NAG H 2 . ? 45.649 22.385 14.091 1.00 31.52 ? 264 NAG A O7 1 HETATM 2181 C C1 . NAG I 2 . ? 40.415 24.859 11.898 1.00 38.99 ? 265 NAG A C1 1 HETATM 2182 C C2 . NAG I 2 . ? 39.170 23.969 11.851 1.00 44.73 ? 265 NAG A C2 1 HETATM 2183 C C3 . NAG I 2 . ? 37.876 24.735 12.170 1.00 50.33 ? 265 NAG A C3 1 HETATM 2184 C C4 . NAG I 2 . ? 38.043 25.819 13.241 1.00 52.53 ? 265 NAG A C4 1 HETATM 2185 C C5 . NAG I 2 . ? 39.414 26.492 13.226 1.00 47.35 ? 265 NAG A C5 1 HETATM 2186 C C6 . NAG I 2 . ? 39.625 27.282 14.521 1.00 49.74 ? 265 NAG A C6 1 HETATM 2187 C C7 . NAG I 2 . ? 39.185 21.946 10.378 1.00 46.57 ? 265 NAG A C7 1 HETATM 2188 C C8 . NAG I 2 . ? 38.837 21.442 9.014 1.00 47.29 ? 265 NAG A C8 1 HETATM 2189 N N2 . NAG I 2 . ? 39.027 23.268 10.577 1.00 41.78 ? 265 NAG A N2 1 HETATM 2190 O O3 . NAG I 2 . ? 36.893 23.791 12.593 1.00 53.87 ? 265 NAG A O3 1 HETATM 2191 O O4 . NAG I 2 . ? 37.078 26.835 13.067 1.00 58.70 ? 265 NAG A O4 1 HETATM 2192 O O5 . NAG I 2 . ? 40.426 25.512 13.133 1.00 39.47 ? 265 NAG A O5 1 HETATM 2193 O O6 . NAG I 2 . ? 39.792 26.355 15.579 1.00 53.52 ? 265 NAG A O6 1 HETATM 2194 O O7 . NAG I 2 . ? 39.601 21.113 11.205 1.00 44.44 ? 265 NAG A O7 1 HETATM 2195 C C1 . NAG J 2 . ? 77.376 25.113 6.417 1.00 41.33 ? 266 NAG A C1 1 HETATM 2196 C C2 . NAG J 2 . ? 78.905 25.212 6.305 1.00 45.95 ? 266 NAG A C2 1 HETATM 2197 C C3 . NAG J 2 . ? 79.361 26.659 6.148 1.00 52.83 ? 266 NAG A C3 1 HETATM 2198 C C4 . NAG J 2 . ? 78.681 27.277 4.935 1.00 56.34 ? 266 NAG A C4 1 HETATM 2199 C C5 . NAG J 2 . ? 77.173 27.167 5.238 1.00 52.01 ? 266 NAG A C5 1 HETATM 2200 C C6 . NAG J 2 . ? 76.267 27.952 4.298 1.00 47.76 ? 266 NAG A C6 1 HETATM 2201 C C7 . NAG J 2 . ? 80.390 23.633 7.239 1.00 47.47 ? 266 NAG A C7 1 HETATM 2202 C C8 . NAG J 2 . ? 81.008 22.953 8.427 1.00 45.96 ? 266 NAG A C8 1 HETATM 2203 N N2 . NAG J 2 . ? 79.542 24.643 7.466 1.00 45.58 ? 266 NAG A N2 1 HETATM 2204 O O3 . NAG J 2 . ? 80.756 26.752 6.033 1.00 60.18 ? 266 NAG A O3 1 HETATM 2205 O O4 . NAG J 2 . ? 79.117 28.615 4.748 1.00 60.50 ? 266 NAG A O4 1 HETATM 2206 O O5 . NAG J 2 . ? 76.803 25.778 5.306 1.00 47.83 ? 266 NAG A O5 1 HETATM 2207 O O6 . NAG J 2 . ? 76.410 27.468 2.971 1.00 49.56 ? 266 NAG A O6 1 HETATM 2208 O O7 . NAG J 2 . ? 80.661 23.245 6.093 1.00 55.72 ? 266 NAG A O7 1 HETATM 2209 C C1 . AMG K 4 . ? 25.188 8.012 1.205 1.00 22.53 ? 267 AMG A C1 1 HETATM 2210 C C2 . AMG K 4 . ? 25.976 7.207 2.247 1.00 18.94 ? 267 AMG A C2 1 HETATM 2211 C C3 . AMG K 4 . ? 27.449 7.640 2.150 1.00 17.69 ? 267 AMG A C3 1 HETATM 2212 C C4 . AMG K 4 . ? 27.998 7.534 0.711 1.00 17.97 ? 267 AMG A C4 1 HETATM 2213 C C5 . AMG K 4 . ? 27.141 8.414 -0.207 1.00 19.06 ? 267 AMG A C5 1 HETATM 2214 C C6 . AMG K 4 . ? 27.580 8.491 -1.664 1.00 18.87 ? 267 AMG A C6 1 HETATM 2215 C C7 . AMG K 4 . ? 24.233 10.121 0.828 1.00 27.92 ? 267 AMG A C7 1 HETATM 2216 O O1 . AMG K 4 . ? 25.205 9.373 1.592 1.00 24.59 ? 267 AMG A O1 1 HETATM 2217 O O2 . AMG K 4 . ? 25.529 7.448 3.580 1.00 22.65 ? 267 AMG A O2 1 HETATM 2218 O O3 . AMG K 4 . ? 28.239 6.863 3.044 1.00 17.63 ? 267 AMG A O3 1 HETATM 2219 O O4 . AMG K 4 . ? 27.987 6.141 0.303 1.00 16.40 ? 267 AMG A O4 1 HETATM 2220 O O5 . AMG K 4 . ? 25.791 7.914 -0.113 1.00 20.64 ? 267 AMG A O5 1 HETATM 2221 O O6 . AMG K 4 . ? 27.494 7.256 -2.368 1.00 19.90 ? 267 AMG A O6 1 HETATM 2222 C C1 . AMG L 4 . ? 76.936 13.832 5.050 1.00 28.38 ? 268 AMG A C1 1 HETATM 2223 C C2 . AMG L 4 . ? 75.739 13.456 5.906 1.00 24.57 ? 268 AMG A C2 1 HETATM 2224 C C3 . AMG L 4 . ? 74.760 12.609 5.107 1.00 24.75 ? 268 AMG A C3 1 HETATM 2225 C C4 . AMG L 4 . ? 74.278 13.407 3.903 1.00 21.83 ? 268 AMG A C4 1 HETATM 2226 C C5 . AMG L 4 . ? 75.505 13.839 3.101 1.00 24.03 ? 268 AMG A C5 1 HETATM 2227 C C6 . AMG L 4 . ? 75.153 14.708 1.904 1.00 25.80 ? 268 AMG A C6 1 HETATM 2228 C C7 . AMG L 4 . ? 78.962 12.828 4.417 1.00 30.76 ? 268 AMG A C7 1 HETATM 2229 O O1 . AMG L 4 . ? 77.554 12.600 4.698 1.00 32.58 ? 268 AMG A O1 1 HETATM 2230 O O2 . AMG L 4 . ? 76.176 12.622 6.987 1.00 28.31 ? 268 AMG A O2 1 HETATM 2231 O O3 . AMG L 4 . ? 73.689 12.186 5.959 1.00 24.39 ? 268 AMG A O3 1 HETATM 2232 O O4 . AMG L 4 . ? 73.638 14.648 4.290 1.00 21.87 ? 268 AMG A O4 1 HETATM 2233 O O5 . AMG L 4 . ? 76.468 14.570 3.909 1.00 28.16 ? 268 AMG A O5 1 HETATM 2234 O O6 . AMG L 4 . ? 76.339 14.981 1.148 1.00 28.31 ? 268 AMG A O6 1 HETATM 2235 S S . SO4 M 5 . ? 37.466 -20.914 -2.989 1.00 78.34 ? 901 SO4 A S 1 HETATM 2236 O O1 . SO4 M 5 . ? 37.494 -20.044 -4.158 1.00 74.72 ? 901 SO4 A O1 1 HETATM 2237 O O2 . SO4 M 5 . ? 36.357 -20.558 -2.100 1.00 79.58 ? 901 SO4 A O2 1 HETATM 2238 O O3 . SO4 M 5 . ? 37.313 -22.290 -3.456 1.00 81.24 ? 901 SO4 A O3 1 HETATM 2239 O O4 . SO4 M 5 . ? 38.705 -20.814 -2.216 1.00 81.34 ? 901 SO4 A O4 1 HETATM 2240 S S . SO4 N 5 . ? 31.903 0.218 16.235 1.00 38.18 ? 902 SO4 A S 1 HETATM 2241 O O1 . SO4 N 5 . ? 31.322 -1.087 15.826 1.00 41.12 ? 902 SO4 A O1 1 HETATM 2242 O O2 . SO4 N 5 . ? 31.317 0.583 17.552 1.00 42.98 ? 902 SO4 A O2 1 HETATM 2243 O O3 . SO4 N 5 . ? 33.324 0.100 16.400 1.00 31.12 ? 902 SO4 A O3 1 HETATM 2244 O O4 . SO4 N 5 . ? 31.532 1.162 15.134 1.00 34.81 ? 902 SO4 A O4 1 HETATM 2245 S S . SO4 O 5 . ? 28.349 -15.324 6.137 1.00 53.61 ? 903 SO4 A S 1 HETATM 2246 O O1 . SO4 O 5 . ? 27.597 -16.285 5.309 1.00 56.03 ? 903 SO4 A O1 1 HETATM 2247 O O2 . SO4 O 5 . ? 27.603 -14.074 6.237 1.00 56.43 ? 903 SO4 A O2 1 HETATM 2248 O O3 . SO4 O 5 . ? 28.454 -15.923 7.474 1.00 55.07 ? 903 SO4 A O3 1 HETATM 2249 O O4 . SO4 O 5 . ? 29.690 -15.134 5.557 1.00 49.64 ? 903 SO4 A O4 1 HETATM 2250 S S A SO4 P 5 . ? 54.241 31.441 9.583 0.25 30.87 ? 904 SO4 A S 1 HETATM 2251 S S B SO4 P 5 . ? 56.161 31.528 9.489 0.25 20.61 ? 904 SO4 A S 1 HETATM 2252 O O1 A SO4 P 5 . ? 53.712 31.117 8.258 0.25 35.75 ? 904 SO4 A O1 1 HETATM 2253 O O1 B SO4 P 5 . ? 57.007 31.269 10.671 0.25 22.15 ? 904 SO4 A O1 1 HETATM 2254 O O2 A SO4 P 5 . ? 53.110 31.594 10.500 0.25 22.14 ? 904 SO4 A O2 1 HETATM 2255 O O2 B SO4 P 5 . ? 56.917 31.913 8.278 0.25 18.41 ? 904 SO4 A O2 1 HETATM 2256 O O3 A SO4 P 5 . ? 55.110 30.372 10.056 0.25 31.18 ? 904 SO4 A O3 1 HETATM 2257 O O3 B SO4 P 5 . ? 55.371 30.333 9.198 0.25 25.28 ? 904 SO4 A O3 1 HETATM 2258 O O4 A SO4 P 5 . ? 54.967 32.698 9.516 0.25 31.31 ? 904 SO4 A O4 1 HETATM 2259 O O4 B SO4 P 5 . ? 55.167 32.564 9.799 0.25 21.99 ? 904 SO4 A O4 1 HETATM 2260 S S . SO4 Q 5 . ? 26.248 7.271 -7.815 1.00 25.41 ? 905 SO4 A S 1 HETATM 2261 O O1 . SO4 Q 5 . ? 26.734 8.683 -7.664 1.00 31.82 ? 905 SO4 A O1 1 HETATM 2262 O O2 . SO4 Q 5 . ? 24.834 7.428 -8.178 1.00 25.18 ? 905 SO4 A O2 1 HETATM 2263 O O3 . SO4 Q 5 . ? 26.978 6.492 -8.818 1.00 23.45 ? 905 SO4 A O3 1 HETATM 2264 O O4 . SO4 Q 5 . ? 26.458 6.665 -6.483 1.00 26.12 ? 905 SO4 A O4 1 HETATM 2265 C C . ACT R 6 . ? 31.270 -9.831 -11.605 1.00 34.15 ? 910 ACT A C 1 HETATM 2266 O O . ACT R 6 . ? 32.085 -10.528 -10.953 1.00 35.59 ? 910 ACT A O 1 HETATM 2267 O OXT . ACT R 6 . ? 30.289 -10.375 -12.215 1.00 42.12 ? 910 ACT A OXT 1 HETATM 2268 C CH3 . ACT R 6 . ? 31.496 -8.405 -11.623 1.00 21.72 ? 910 ACT A CH3 1 HETATM 2269 O O . HOH S 7 . ? 56.842 6.232 -2.211 1.00 18.61 ? 911 HOH A O 1 HETATM 2270 O O . HOH S 7 . ? 37.101 13.061 5.280 1.00 18.47 ? 912 HOH A O 1 HETATM 2271 O O . HOH S 7 . ? 57.793 21.415 12.503 1.00 16.44 ? 913 HOH A O 1 HETATM 2272 O O . HOH S 7 . ? 36.244 4.208 6.389 1.00 17.67 ? 914 HOH A O 1 HETATM 2273 O O . HOH S 7 . ? 53.983 5.356 3.431 1.00 19.38 ? 915 HOH A O 1 HETATM 2274 O O . HOH S 7 . ? 65.077 21.443 1.117 1.00 19.60 ? 916 HOH A O 1 HETATM 2275 O O . HOH S 7 . ? 43.741 12.246 7.359 1.00 19.73 ? 917 HOH A O 1 HETATM 2276 O O . HOH S 7 . ? 67.593 3.918 3.090 1.00 22.15 ? 918 HOH A O 1 HETATM 2277 O O . HOH S 7 . ? 64.896 10.218 8.221 1.00 16.48 ? 919 HOH A O 1 HETATM 2278 O O . HOH S 7 . ? 44.772 6.656 -0.735 1.00 17.65 ? 920 HOH A O 1 HETATM 2279 O O . HOH S 7 . ? 53.505 14.451 1.219 1.00 18.44 ? 921 HOH A O 1 HETATM 2280 O O . HOH S 7 . ? 47.524 0.281 -0.947 1.00 16.95 ? 922 HOH A O 1 HETATM 2281 O O . HOH S 7 . ? 66.782 15.337 11.601 1.00 18.24 ? 923 HOH A O 1 HETATM 2282 O O . HOH S 7 . ? 56.598 24.250 15.879 1.00 20.21 ? 924 HOH A O 1 HETATM 2283 O O . HOH S 7 . ? 40.975 12.982 7.022 1.00 18.53 ? 925 HOH A O 1 HETATM 2284 O O . HOH S 7 . ? 64.194 24.392 18.374 1.00 18.76 ? 926 HOH A O 1 HETATM 2285 O O . HOH S 7 . ? 37.699 -9.264 3.338 1.00 19.93 ? 927 HOH A O 1 HETATM 2286 O O . HOH S 7 . ? 70.564 2.026 4.844 1.00 21.14 ? 928 HOH A O 1 HETATM 2287 O O . HOH S 7 . ? 51.373 1.026 -2.001 1.00 22.43 ? 929 HOH A O 1 HETATM 2288 O O . HOH S 7 . ? 58.435 25.211 0.932 1.00 23.32 ? 930 HOH A O 1 HETATM 2289 O O . HOH S 7 . ? 36.299 -2.318 17.767 1.00 24.76 ? 931 HOH A O 1 HETATM 2290 O O . HOH S 7 . ? 56.371 31.165 18.807 1.00 27.63 ? 932 HOH A O 1 HETATM 2291 O O . HOH S 7 . ? 45.484 13.927 -3.945 1.00 25.82 ? 933 HOH A O 1 HETATM 2292 O O . HOH S 7 . ? 41.912 -8.391 8.932 1.00 25.35 ? 934 HOH A O 1 HETATM 2293 O O . HOH S 7 . ? 37.277 11.056 14.437 1.00 25.02 ? 935 HOH A O 1 HETATM 2294 O O . HOH S 7 . ? 25.727 1.150 -4.656 1.00 20.28 ? 936 HOH A O 1 HETATM 2295 O O . HOH S 7 . ? 37.353 13.765 8.001 1.00 24.24 ? 937 HOH A O 1 HETATM 2296 O O . HOH S 7 . ? 73.662 10.700 8.054 1.00 25.62 ? 938 HOH A O 1 HETATM 2297 O O . HOH S 7 . ? 37.962 -1.482 -13.625 1.00 23.24 ? 939 HOH A O 1 HETATM 2298 O O . HOH S 7 . ? 50.902 11.239 6.948 1.00 21.21 ? 940 HOH A O 1 HETATM 2299 O O . HOH S 7 . ? 29.595 -2.071 9.256 1.00 22.90 ? 941 HOH A O 1 HETATM 2300 O O . HOH S 7 . ? 54.233 25.734 15.208 1.00 22.04 ? 942 HOH A O 1 HETATM 2301 O O . HOH S 7 . ? 35.704 -0.815 -7.093 1.00 21.95 ? 943 HOH A O 1 HETATM 2302 O O . HOH S 7 . ? 38.775 5.946 19.373 1.00 22.53 ? 944 HOH A O 1 HETATM 2303 O O . HOH S 7 . ? 28.462 7.690 -4.851 1.00 22.84 ? 945 HOH A O 1 HETATM 2304 O O . HOH S 7 . ? 43.463 15.190 14.686 1.00 27.21 ? 946 HOH A O 1 HETATM 2305 O O . HOH S 7 . ? 31.539 8.852 -9.498 0.50 20.71 ? 947 HOH A O 1 HETATM 2306 O O . HOH S 7 . ? 44.676 -12.919 -1.012 1.00 28.33 ? 948 HOH A O 1 HETATM 2307 O O . HOH S 7 . ? 66.079 23.736 -0.085 1.00 26.63 ? 949 HOH A O 1 HETATM 2308 O O . HOH S 7 . ? 29.130 -12.156 4.593 1.00 26.07 ? 950 HOH A O 1 HETATM 2309 O O . HOH S 7 . ? 43.866 24.306 3.728 1.00 25.98 ? 951 HOH A O 1 HETATM 2310 O O . HOH S 7 . ? 53.097 9.298 6.868 1.00 21.95 ? 952 HOH A O 1 HETATM 2311 O O . HOH S 7 . ? 38.944 -5.931 19.886 1.00 25.56 ? 953 HOH A O 1 HETATM 2312 O O . HOH S 7 . ? 68.284 6.931 9.665 1.00 24.50 ? 954 HOH A O 1 HETATM 2313 O O . HOH S 7 . ? 33.692 10.938 -8.724 1.00 22.88 ? 955 HOH A O 1 HETATM 2314 O O . HOH S 7 . ? 30.120 11.268 5.351 1.00 22.81 ? 956 HOH A O 1 HETATM 2315 O O . HOH S 7 . ? 53.614 23.852 7.071 1.00 27.75 ? 957 HOH A O 1 HETATM 2316 O O . HOH S 7 . ? 23.173 -9.555 -2.110 1.00 32.50 ? 958 HOH A O 1 HETATM 2317 O O . HOH S 7 . ? 51.833 -4.862 -7.271 1.00 24.54 ? 959 HOH A O 1 HETATM 2318 O O . HOH S 7 . ? 32.154 -3.484 10.378 1.00 24.12 ? 960 HOH A O 1 HETATM 2319 O O . HOH S 7 . ? 68.084 23.251 7.213 1.00 21.30 ? 961 HOH A O 1 HETATM 2320 O O . HOH S 7 . ? 60.013 7.817 12.549 1.00 25.33 ? 962 HOH A O 1 HETATM 2321 O O . HOH S 7 . ? 54.207 27.185 3.567 1.00 27.31 ? 963 HOH A O 1 HETATM 2322 O O . HOH S 7 . ? 39.724 8.253 17.893 1.00 30.03 ? 964 HOH A O 1 HETATM 2323 O O . HOH S 7 . ? 30.778 -5.839 9.610 1.00 25.58 ? 965 HOH A O 1 HETATM 2324 O O . HOH S 7 . ? 64.176 2.117 3.616 1.00 26.22 ? 966 HOH A O 1 HETATM 2325 O O . HOH S 7 . ? 70.137 21.974 5.696 1.00 22.93 ? 967 HOH A O 1 HETATM 2326 O O . HOH S 7 . ? 24.821 3.681 8.964 1.00 26.40 ? 968 HOH A O 1 HETATM 2327 O O . HOH S 7 . ? 65.122 31.361 18.417 1.00 32.78 ? 969 HOH A O 1 HETATM 2328 O O . HOH S 7 . ? 57.512 28.345 21.290 1.00 34.09 ? 970 HOH A O 1 HETATM 2329 O O . HOH S 7 . ? 52.491 24.644 20.976 1.00 27.12 ? 971 HOH A O 1 HETATM 2330 O O . HOH S 7 . ? 25.218 5.168 4.822 1.00 25.17 ? 972 HOH A O 1 HETATM 2331 O O . HOH S 7 . ? 66.802 7.908 11.696 1.00 24.55 ? 973 HOH A O 1 HETATM 2332 O O . HOH S 7 . ? 70.623 16.475 16.947 1.00 27.49 ? 974 HOH A O 1 HETATM 2333 O O . HOH S 7 . ? 44.148 24.719 6.443 1.00 29.55 ? 975 HOH A O 1 HETATM 2334 O O . HOH S 7 . ? 47.371 11.613 -2.215 1.00 28.82 ? 976 HOH A O 1 HETATM 2335 O O . HOH S 7 . ? 45.250 24.246 -0.289 1.00 29.23 ? 977 HOH A O 1 HETATM 2336 O O . HOH S 7 . ? 66.661 17.893 -6.530 1.00 31.15 ? 978 HOH A O 1 HETATM 2337 O O . HOH S 7 . ? 35.201 15.792 -4.779 1.00 37.73 ? 979 HOH A O 1 HETATM 2338 O O . HOH S 7 . ? 48.580 25.817 10.610 1.00 28.22 ? 980 HOH A O 1 HETATM 2339 O O . HOH S 7 . ? 66.643 25.578 18.139 1.00 22.92 ? 981 HOH A O 1 HETATM 2340 O O . HOH S 7 . ? 35.848 1.217 -11.933 1.00 24.11 ? 982 HOH A O 1 HETATM 2341 O O . HOH S 7 . ? 25.985 -4.979 -6.615 1.00 28.87 ? 983 HOH A O 1 HETATM 2342 O O . HOH S 7 . ? 24.086 -8.163 -6.038 1.00 28.87 ? 984 HOH A O 1 HETATM 2343 O O . HOH S 7 . ? 23.858 7.824 -2.158 1.00 29.47 ? 985 HOH A O 1 HETATM 2344 O O . HOH S 7 . ? 49.030 7.954 8.848 1.00 30.76 ? 986 HOH A O 1 HETATM 2345 O O . HOH S 7 . ? 43.181 18.147 11.694 1.00 30.50 ? 987 HOH A O 1 HETATM 2346 O O . HOH S 7 . ? 51.616 -10.851 -2.997 1.00 25.56 ? 988 HOH A O 1 HETATM 2347 O O . HOH S 7 . ? 40.174 15.747 6.317 1.00 30.92 ? 989 HOH A O 1 HETATM 2348 O O . HOH S 7 . ? 30.228 -4.396 -9.247 1.00 27.04 ? 990 HOH A O 1 HETATM 2349 O O . HOH S 7 . ? 27.150 11.528 3.638 1.00 31.21 ? 991 HOH A O 1 HETATM 2350 O O . HOH S 7 . ? 67.034 -0.560 11.443 1.00 33.44 ? 992 HOH A O 1 HETATM 2351 O O . HOH S 7 . ? 43.908 10.542 11.795 1.00 31.79 ? 993 HOH A O 1 HETATM 2352 O O . HOH S 7 . ? 57.443 10.477 15.613 1.00 31.33 ? 994 HOH A O 1 HETATM 2353 O O . HOH S 7 . ? 40.741 19.970 5.667 1.00 32.32 ? 995 HOH A O 1 HETATM 2354 O O . HOH S 7 . ? 53.649 -1.990 0.415 1.00 32.13 ? 996 HOH A O 1 HETATM 2355 O O . HOH S 7 . ? 63.336 0.022 2.128 0.50 26.64 ? 997 HOH A O 1 HETATM 2356 O O . HOH S 7 . ? 34.795 -13.957 -5.317 1.00 32.07 ? 998 HOH A O 1 HETATM 2357 O O . HOH S 7 . ? 74.493 13.944 12.153 1.00 32.59 ? 999 HOH A O 1 HETATM 2358 O O . HOH S 7 . ? 22.846 7.371 -6.163 1.00 31.22 ? 1000 HOH A O 1 HETATM 2359 O O . HOH S 7 . ? 45.711 -5.019 11.095 1.00 57.79 ? 1001 HOH A O 1 HETATM 2360 O O . HOH S 7 . ? 44.003 -7.715 7.386 1.00 35.72 ? 1002 HOH A O 1 HETATM 2361 O O . HOH S 7 . ? 53.021 22.761 -7.144 1.00 35.65 ? 1003 HOH A O 1 HETATM 2362 O O . HOH S 7 . ? 68.878 14.399 15.978 1.00 29.92 ? 1004 HOH A O 1 HETATM 2363 O O . HOH S 7 . ? 73.529 11.141 -5.699 1.00 29.93 ? 1005 HOH A O 1 HETATM 2364 O O . HOH S 7 . ? 70.823 7.486 -6.131 1.00 33.43 ? 1006 HOH A O 1 HETATM 2365 O O . HOH S 7 . ? 50.990 26.108 19.148 1.00 28.22 ? 1007 HOH A O 1 HETATM 2366 O O . HOH S 7 . ? 28.043 -4.884 10.995 1.00 36.07 ? 1008 HOH A O 1 HETATM 2367 O O . HOH S 7 . ? 53.554 6.816 8.444 1.00 29.75 ? 1009 HOH A O 1 HETATM 2368 O O . HOH S 7 . ? 42.316 13.802 -8.823 1.00 34.16 ? 1010 HOH A O 1 HETATM 2369 O O . HOH S 7 . ? 31.699 -5.881 13.607 1.00 37.84 ? 1011 HOH A O 1 HETATM 2370 O O . HOH S 7 . ? 42.220 4.502 16.254 1.00 33.18 ? 1012 HOH A O 1 HETATM 2371 O O . HOH S 7 . ? 40.979 18.608 10.160 1.00 28.78 ? 1013 HOH A O 1 HETATM 2372 O O . HOH S 7 . ? 74.173 22.714 11.532 1.00 32.98 ? 1014 HOH A O 1 HETATM 2373 O O . HOH S 7 . ? 60.906 1.300 1.034 1.00 29.78 ? 1015 HOH A O 1 HETATM 2374 O O . HOH S 7 . ? 59.805 30.550 11.122 1.00 33.63 ? 1016 HOH A O 1 HETATM 2375 O O . HOH S 7 . ? 29.160 10.930 10.704 1.00 34.13 ? 1017 HOH A O 1 HETATM 2376 O O . HOH S 7 . ? 55.070 31.375 21.195 1.00 39.47 ? 1018 HOH A O 1 HETATM 2377 O O . HOH S 7 . ? 64.155 14.582 17.094 1.00 34.11 ? 1019 HOH A O 1 HETATM 2378 O O . HOH S 7 . ? 49.849 1.252 -10.650 1.00 33.74 ? 1020 HOH A O 1 HETATM 2379 O O . HOH S 7 . ? 45.588 14.884 -6.271 1.00 35.05 ? 1021 HOH A O 1 HETATM 2380 O O . HOH S 7 . ? 38.943 15.319 -2.783 1.00 36.80 ? 1022 HOH A O 1 HETATM 2381 O O . HOH S 7 . ? 24.289 4.837 -8.759 1.00 28.85 ? 1023 HOH A O 1 HETATM 2382 O O . HOH S 7 . ? 49.452 13.892 -2.797 1.00 29.63 ? 1024 HOH A O 1 HETATM 2383 O O . HOH S 7 . ? 47.261 10.287 9.610 1.00 32.44 ? 1025 HOH A O 1 HETATM 2384 O O . HOH S 7 . ? 34.786 9.726 13.878 1.00 31.41 ? 1026 HOH A O 1 HETATM 2385 O O . HOH S 7 . ? 64.222 10.351 -10.008 1.00 28.41 ? 1027 HOH A O 1 HETATM 2386 O O . HOH S 7 . ? 58.929 31.896 -3.236 1.00 39.87 ? 1028 HOH A O 1 HETATM 2387 O O . HOH S 7 . ? 67.933 1.427 4.570 1.00 30.73 ? 1029 HOH A O 1 HETATM 2388 O O . HOH S 7 . ? 59.640 9.487 14.542 1.00 33.48 ? 1030 HOH A O 1 HETATM 2389 O O . HOH S 7 . ? 36.398 -12.371 -7.002 1.00 29.33 ? 1031 HOH A O 1 HETATM 2390 O O . HOH S 7 . ? 57.357 -2.537 0.864 1.00 31.24 ? 1032 HOH A O 1 HETATM 2391 O O . HOH S 7 . ? 26.147 3.651 -7.367 1.00 31.40 ? 1033 HOH A O 1 HETATM 2392 O O . HOH S 7 . ? 47.117 1.755 9.141 1.00 29.54 ? 1034 HOH A O 1 HETATM 2393 O O . HOH S 7 . ? 53.943 18.057 21.785 1.00 31.46 ? 1035 HOH A O 1 HETATM 2394 O O . HOH S 7 . ? 34.932 -5.119 16.306 1.00 31.58 ? 1036 HOH A O 1 HETATM 2395 O O . HOH S 7 . ? 39.532 16.228 3.005 1.00 38.15 ? 1037 HOH A O 1 HETATM 2396 O O . HOH S 7 . ? 52.754 28.969 -2.117 1.00 36.45 ? 1038 HOH A O 1 HETATM 2397 O O . HOH S 7 . ? 31.247 14.801 -1.015 1.00 32.76 ? 1039 HOH A O 1 HETATM 2398 O O . HOH S 7 . ? 33.238 11.089 11.996 1.00 35.94 ? 1040 HOH A O 1 HETATM 2399 O O . HOH S 7 . ? 52.537 30.076 22.267 1.00 32.33 ? 1041 HOH A O 1 HETATM 2400 O O . HOH S 7 . ? 56.856 4.266 -8.666 1.00 34.15 ? 1042 HOH A O 1 HETATM 2401 O O . HOH S 7 . ? 19.839 3.952 -6.197 1.00 30.58 ? 1043 HOH A O 1 HETATM 2402 O O . HOH S 7 . ? 44.960 8.569 13.366 1.00 31.34 ? 1044 HOH A O 1 HETATM 2403 O O . HOH S 7 . ? 44.659 17.943 -2.315 1.00 33.09 ? 1045 HOH A O 1 HETATM 2404 O O B HOH S 7 . ? 52.961 31.192 7.682 0.50 22.32 ? 1046 HOH A O 1 HETATM 2405 O O . HOH S 7 . ? 31.624 -8.239 10.878 1.00 37.60 ? 1047 HOH A O 1 HETATM 2406 O O . HOH S 7 . ? 24.788 -12.365 0.436 1.00 34.77 ? 1048 HOH A O 1 HETATM 2407 O O . HOH S 7 . ? 51.075 25.553 7.722 1.00 35.04 ? 1049 HOH A O 1 HETATM 2408 O O . HOH S 7 . ? 39.691 14.342 -8.716 1.00 37.62 ? 1050 HOH A O 1 HETATM 2409 O O . HOH S 7 . ? 45.982 18.987 -4.471 1.00 39.51 ? 1051 HOH A O 1 HETATM 2410 O O . HOH S 7 . ? 51.103 -12.998 -6.945 1.00 38.78 ? 1052 HOH A O 1 HETATM 2411 O O . HOH S 7 . ? 67.525 3.922 -3.796 1.00 33.24 ? 1053 HOH A O 1 HETATM 2412 O O . HOH S 7 . ? 53.163 -6.628 -4.377 1.00 36.93 ? 1054 HOH A O 1 HETATM 2413 O O . HOH S 7 . ? 34.764 -17.630 1.051 1.00 36.40 ? 1055 HOH A O 1 HETATM 2414 O O . HOH S 7 . ? 77.911 15.749 -1.427 1.00 41.28 ? 1056 HOH A O 1 HETATM 2415 O O . HOH S 7 . ? 54.676 20.945 18.770 1.00 30.91 ? 1057 HOH A O 1 HETATM 2416 O O . HOH S 7 . ? 45.716 11.481 -9.851 1.00 37.78 ? 1058 HOH A O 1 HETATM 2417 O O . HOH S 7 . ? 36.941 -9.172 9.610 1.00 41.91 ? 1059 HOH A O 1 HETATM 2418 O O . HOH S 7 . ? 59.115 31.624 14.313 1.00 38.06 ? 1060 HOH A O 1 HETATM 2419 O O . HOH S 7 . ? 51.342 -7.929 -8.571 1.00 38.21 ? 1061 HOH A O 1 HETATM 2420 O O . HOH S 7 . ? 36.992 15.428 3.746 1.00 33.37 ? 1062 HOH A O 1 HETATM 2421 O O . HOH S 7 . ? 22.730 4.767 -6.452 1.00 32.46 ? 1063 HOH A O 1 HETATM 2422 O O . HOH S 7 . ? 36.067 13.731 14.456 1.00 33.08 ? 1064 HOH A O 1 HETATM 2423 O O . HOH S 7 . ? 47.208 0.886 5.922 1.00 35.72 ? 1065 HOH A O 1 HETATM 2424 O O . HOH S 7 . ? 29.519 13.680 3.877 1.00 37.31 ? 1066 HOH A O 1 HETATM 2425 O O . HOH S 7 . ? 49.352 3.455 11.208 1.00 46.40 ? 1067 HOH A O 1 HETATM 2426 O O . HOH S 7 . ? 35.599 7.105 13.868 1.00 35.42 ? 1068 HOH A O 1 HETATM 2427 O O . HOH S 7 . ? 51.644 27.741 2.316 1.00 34.15 ? 1069 HOH A O 1 HETATM 2428 O O . HOH S 7 . ? 67.823 26.868 0.469 1.00 36.52 ? 1070 HOH A O 1 HETATM 2429 O O . HOH S 7 . ? 75.940 15.633 14.823 1.00 47.58 ? 1071 HOH A O 1 HETATM 2430 O O . HOH S 7 . ? 31.823 -15.857 7.166 1.00 41.61 ? 1072 HOH A O 1 HETATM 2431 O O . HOH S 7 . ? 40.364 -18.641 -3.725 1.00 33.08 ? 1073 HOH A O 1 HETATM 2432 O O . HOH S 7 . ? 57.998 0.174 2.191 1.00 36.46 ? 1074 HOH A O 1 HETATM 2433 O O . HOH S 7 . ? 73.224 15.940 17.237 1.00 36.24 ? 1075 HOH A O 1 HETATM 2434 O O . HOH S 7 . ? 23.916 5.879 7.207 1.00 38.12 ? 1076 HOH A O 1 HETATM 2435 O O . HOH S 7 . ? 70.259 9.269 15.949 1.00 52.41 ? 1077 HOH A O 1 HETATM 2436 O O . HOH S 7 . ? 50.229 -4.915 9.909 1.00 33.44 ? 1078 HOH A O 1 HETATM 2437 O O . HOH S 7 . ? 29.630 14.921 1.172 1.00 37.69 ? 1079 HOH A O 1 HETATM 2438 O O . HOH S 7 . ? 35.764 16.408 1.080 1.00 40.45 ? 1080 HOH A O 1 HETATM 2439 O O . HOH S 7 . ? 48.766 25.293 17.887 1.00 41.19 ? 1081 HOH A O 1 HETATM 2440 O O . HOH S 7 . ? 70.704 13.668 -6.896 1.00 32.76 ? 1082 HOH A O 1 HETATM 2441 O O . HOH S 7 . ? 45.934 16.714 15.782 1.00 35.06 ? 1083 HOH A O 1 HETATM 2442 O O . HOH S 7 . ? 33.026 13.381 -9.919 1.00 35.14 ? 1084 HOH A O 1 HETATM 2443 O O . HOH S 7 . ? 44.191 26.179 1.155 1.00 40.54 ? 1085 HOH A O 1 HETATM 2444 O O . HOH S 7 . ? 53.461 14.177 20.324 1.00 39.38 ? 1086 HOH A O 1 HETATM 2445 O O . HOH S 7 . ? 21.450 -2.704 -0.405 1.00 39.30 ? 1087 HOH A O 1 HETATM 2446 O O . HOH S 7 . ? 33.631 14.530 6.955 1.00 36.23 ? 1088 HOH A O 1 HETATM 2447 O O . HOH S 7 . ? 44.394 25.132 20.394 1.00 53.31 ? 1089 HOH A O 1 HETATM 2448 O O . HOH S 7 . ? 47.412 -0.343 10.502 1.00 41.07 ? 1090 HOH A O 1 HETATM 2449 O O . HOH S 7 . ? 78.518 21.606 5.133 1.00 39.33 ? 1091 HOH A O 1 HETATM 2450 O O . HOH S 7 . ? 42.876 -1.930 -16.371 1.00 38.35 ? 1092 HOH A O 1 HETATM 2451 O O . HOH S 7 . ? 39.375 17.360 8.309 1.00 44.08 ? 1093 HOH A O 1 HETATM 2452 O O . HOH S 7 . ? 65.003 25.413 -2.044 1.00 37.45 ? 1094 HOH A O 1 HETATM 2453 O O . HOH S 7 . ? 35.414 15.583 -1.306 1.00 35.67 ? 1095 HOH A O 1 HETATM 2454 O O . HOH S 7 . ? 34.937 -16.518 4.938 1.00 39.46 ? 1096 HOH A O 1 HETATM 2455 O O . HOH S 7 . ? 52.286 0.416 -12.824 1.00 40.81 ? 1097 HOH A O 1 HETATM 2456 O O . HOH S 7 . ? 50.662 8.042 -8.947 1.00 32.29 ? 1098 HOH A O 1 HETATM 2457 O O . HOH S 7 . ? 32.339 14.053 -6.779 1.00 41.28 ? 1099 HOH A O 1 HETATM 2458 O O . HOH S 7 . ? 59.226 22.956 -8.345 1.00 39.11 ? 1100 HOH A O 1 HETATM 2459 O O . HOH S 7 . ? 49.233 10.335 -9.116 1.00 34.11 ? 1101 HOH A O 1 HETATM 2460 O O . HOH S 7 . ? 74.445 18.800 -5.696 1.00 49.32 ? 1102 HOH A O 1 HETATM 2461 O O . HOH S 7 . ? 47.909 -11.006 9.513 1.00 37.39 ? 1103 HOH A O 1 HETATM 2462 O O . HOH S 7 . ? 26.573 -14.507 -2.422 1.00 32.16 ? 1104 HOH A O 1 HETATM 2463 O O . HOH S 7 . ? 69.596 16.855 19.487 1.00 39.02 ? 1105 HOH A O 1 HETATM 2464 O O . HOH S 7 . ? 58.819 21.775 19.313 1.00 35.45 ? 1106 HOH A O 1 HETATM 2465 O O . HOH S 7 . ? 74.702 25.580 10.295 1.00 42.88 ? 1107 HOH A O 1 HETATM 2466 O O . HOH S 7 . ? 66.509 12.492 -9.908 1.00 43.04 ? 1108 HOH A O 1 HETATM 2467 O O . HOH S 7 . ? 46.710 9.485 -9.339 1.00 35.87 ? 1109 HOH A O 1 HETATM 2468 O O . HOH S 7 . ? 25.954 -12.391 -5.656 1.00 42.82 ? 1110 HOH A O 1 HETATM 2469 O O . HOH S 7 . ? 47.635 6.231 -8.870 1.00 38.44 ? 1111 HOH A O 1 HETATM 2470 O O . HOH S 7 . ? 72.618 8.863 -7.314 1.00 37.09 ? 1112 HOH A O 1 HETATM 2471 O O . HOH S 7 . ? 25.459 9.741 4.749 1.00 36.81 ? 1113 HOH A O 1 HETATM 2472 O O . HOH S 7 . ? 23.622 1.713 4.775 1.00 41.54 ? 1114 HOH A O 1 HETATM 2473 O O . HOH S 7 . ? 56.226 -3.202 -6.047 1.00 42.88 ? 1115 HOH A O 1 HETATM 2474 O O . HOH S 7 . ? 40.967 17.626 4.691 1.00 39.03 ? 1116 HOH A O 1 HETATM 2475 O O . HOH S 7 . ? 64.503 1.399 -7.977 1.00 38.29 ? 1117 HOH A O 1 HETATM 2476 O O . HOH S 7 . ? 62.162 26.769 20.630 1.00 35.31 ? 1118 HOH A O 1 HETATM 2477 O O . HOH S 7 . ? 56.659 18.391 22.491 1.00 46.34 ? 1119 HOH A O 1 HETATM 2478 O O . HOH S 7 . ? 58.884 28.862 -5.210 1.00 38.13 ? 1120 HOH A O 1 HETATM 2479 O O . HOH S 7 . ? 65.650 3.210 9.398 1.00 41.49 ? 1121 HOH A O 1 HETATM 2480 O O . HOH S 7 . ? 38.313 16.979 -4.903 1.00 40.95 ? 1122 HOH A O 1 HETATM 2481 O O . HOH S 7 . ? 30.259 -11.283 8.658 1.00 34.93 ? 1123 HOH A O 1 HETATM 2482 O O . HOH S 7 . ? 77.065 14.988 8.414 1.00 38.34 ? 1124 HOH A O 1 HETATM 2483 O O . HOH S 7 . ? 66.528 14.755 17.435 1.00 38.53 ? 1125 HOH A O 1 HETATM 2484 O O . HOH S 7 . ? 45.627 21.268 23.069 1.00 44.43 ? 1126 HOH A O 1 HETATM 2485 O O . HOH S 7 . ? 28.236 10.905 8.199 1.00 44.70 ? 1127 HOH A O 1 HETATM 2486 O O . HOH S 7 . ? 71.351 11.774 -9.235 1.00 52.99 ? 1128 HOH A O 1 HETATM 2487 O O . HOH S 7 . ? 68.787 13.469 -9.627 1.00 48.78 ? 1129 HOH A O 1 HETATM 2488 O O . HOH S 7 . ? 67.866 31.886 15.853 1.00 42.41 ? 1130 HOH A O 1 HETATM 2489 O O . HOH S 7 . ? 46.908 -7.928 -15.063 1.00 56.42 ? 1131 HOH A O 1 HETATM 2490 O O . HOH S 7 . ? 41.703 22.800 3.287 1.00 44.07 ? 1132 HOH A O 1 HETATM 2491 O O . HOH S 7 . ? 45.768 -15.300 0.076 1.00 35.14 ? 1133 HOH A O 1 HETATM 2492 O O . HOH S 7 . ? 28.597 -1.798 17.098 1.00 39.88 ? 1134 HOH A O 1 HETATM 2493 O O . HOH S 7 . ? 43.804 1.187 14.218 1.00 37.29 ? 1135 HOH A O 1 HETATM 2494 O O . HOH S 7 . ? 23.844 11.867 -3.259 1.00 45.37 ? 1136 HOH A O 1 HETATM 2495 O O . HOH S 7 . ? 47.179 18.766 16.729 1.00 38.03 ? 1137 HOH A O 1 HETATM 2496 O O . HOH S 7 . ? 44.603 -5.169 -16.655 1.00 36.69 ? 1138 HOH A O 1 HETATM 2497 O O . HOH S 7 . ? 42.588 18.169 1.747 1.00 41.53 ? 1139 HOH A O 1 HETATM 2498 O O . HOH S 7 . ? 67.433 4.684 10.201 1.00 39.81 ? 1140 HOH A O 1 HETATM 2499 O O . HOH S 7 . ? 57.070 14.533 -8.163 1.00 41.56 ? 1141 HOH A O 1 HETATM 2500 O O . HOH S 7 . ? 58.965 30.834 19.260 1.00 44.34 ? 1142 HOH A O 1 HETATM 2501 O O . HOH S 7 . ? 66.449 29.418 0.198 1.00 45.98 ? 1143 HOH A O 1 HETATM 2502 O O . HOH S 7 . ? 35.673 -7.697 19.101 1.00 45.66 ? 1144 HOH A O 1 HETATM 2503 O O . HOH S 7 . ? 23.221 -9.380 4.326 1.00 40.78 ? 1145 HOH A O 1 HETATM 2504 O O . HOH S 7 . ? 35.224 -11.863 -9.348 1.00 41.19 ? 1146 HOH A O 1 HETATM 2505 O O . HOH S 7 . ? 44.471 10.325 9.182 1.00 33.16 ? 1147 HOH A O 1 HETATM 2506 O O . HOH S 7 . ? 42.137 -8.760 13.788 1.00 44.66 ? 1148 HOH A O 1 HETATM 2507 O O . HOH S 7 . ? 33.690 6.940 12.832 1.00 34.51 ? 1149 HOH A O 1 HETATM 2508 O O . HOH S 7 . ? 46.606 27.893 10.127 1.00 38.82 ? 1150 HOH A O 1 HETATM 2509 O O . HOH S 7 . ? 63.551 15.171 19.544 1.00 38.99 ? 1151 HOH A O 1 HETATM 2510 O O . HOH S 7 . ? 48.904 27.668 16.260 1.00 40.84 ? 1152 HOH A O 1 HETATM 2511 O O . HOH S 7 . ? 34.557 18.474 13.605 1.00 57.83 ? 1153 HOH A O 1 HETATM 2512 O O . HOH S 7 . ? 36.159 -13.683 10.682 1.00 46.50 ? 1154 HOH A O 1 HETATM 2513 O O . HOH S 7 . ? 35.033 14.804 -10.763 1.00 41.58 ? 1155 HOH A O 1 HETATM 2514 O O . HOH S 7 . ? 50.531 14.165 -11.888 1.00 53.70 ? 1156 HOH A O 1 HETATM 2515 O O . HOH S 7 . ? 61.555 23.166 -7.096 1.00 50.98 ? 1157 HOH A O 1 HETATM 2516 O O . HOH S 7 . ? 25.593 13.378 2.249 1.00 38.04 ? 1158 HOH A O 1 HETATM 2517 O O . HOH S 7 . ? 38.779 -14.180 -7.756 1.00 44.13 ? 1159 HOH A O 1 HETATM 2518 O O . HOH S 7 . ? 63.957 9.993 16.603 1.00 41.22 ? 1160 HOH A O 1 HETATM 2519 O O . HOH S 7 . ? 57.576 1.729 -8.834 1.00 49.53 ? 1161 HOH A O 1 HETATM 2520 O O . HOH S 7 . ? 54.787 -2.144 -9.704 1.00 43.58 ? 1162 HOH A O 1 HETATM 2521 O O . HOH S 7 . ? 21.789 3.247 1.867 1.00 36.81 ? 1163 HOH A O 1 HETATM 2522 O O . HOH S 7 . ? 35.919 -10.243 -11.885 1.00 46.15 ? 1164 HOH A O 1 HETATM 2523 O O . HOH S 7 . ? 62.164 31.184 8.428 1.00 40.24 ? 1165 HOH A O 1 HETATM 2524 O O . HOH S 7 . ? 33.967 -19.723 -1.710 1.00 48.99 ? 1166 HOH A O 1 HETATM 2525 O O . HOH S 7 . ? 22.614 -1.467 3.326 1.00 44.44 ? 1167 HOH A O 1 HETATM 2526 O O . HOH S 7 . ? 47.376 -16.158 7.209 1.00 44.34 ? 1168 HOH A O 1 HETATM 2527 O O . HOH S 7 . ? 36.436 16.437 15.384 1.00 46.85 ? 1169 HOH A O 1 HETATM 2528 O O . HOH S 7 . ? 35.213 16.473 5.552 1.00 53.70 ? 1170 HOH A O 1 HETATM 2529 O O . HOH S 7 . ? 44.005 27.941 6.154 1.00 43.44 ? 1171 HOH A O 1 HETATM 2530 O O . HOH S 7 . ? 65.420 7.735 -10.235 1.00 43.42 ? 1172 HOH A O 1 HETATM 2531 O O . HOH S 7 . ? 56.070 15.972 24.656 1.00 48.89 ? 1173 HOH A O 1 HETATM 2532 O O . HOH S 7 . ? 46.000 28.843 12.609 1.00 38.14 ? 1174 HOH A O 1 HETATM 2533 O O . HOH S 7 . ? 63.561 4.563 -6.996 1.00 36.74 ? 1175 HOH A O 1 HETATM 2534 O O . HOH S 7 . ? 46.838 27.233 20.012 1.00 45.25 ? 1176 HOH A O 1 HETATM 2535 O O . HOH S 7 . ? 47.517 26.971 13.936 1.00 39.90 ? 1177 HOH A O 1 HETATM 2536 O O . HOH S 7 . ? 46.334 -16.694 4.606 1.00 39.40 ? 1178 HOH A O 1 HETATM 2537 O O . HOH S 7 . ? 62.485 21.311 -10.825 1.00 52.19 ? 1179 HOH A O 1 HETATM 2538 O O . HOH S 7 . ? 22.475 -21.339 0.659 1.00 43.81 ? 1180 HOH A O 1 HETATM 2539 O O . HOH S 7 . ? 21.957 5.874 -0.230 1.00 41.49 ? 1181 HOH A O 1 HETATM 2540 O O . HOH S 7 . ? 24.669 -7.350 4.903 1.00 36.00 ? 1182 HOH A O 1 HETATM 2541 O O . HOH S 7 . ? 62.075 1.668 7.342 1.00 50.76 ? 1183 HOH A O 1 HETATM 2542 O O . HOH S 7 . ? 42.889 22.832 20.120 1.00 57.30 ? 1184 HOH A O 1 HETATM 2543 O O . HOH S 7 . ? 55.716 9.258 -10.551 1.00 52.37 ? 1185 HOH A O 1 HETATM 2544 O O . HOH S 7 . ? 31.772 0.480 20.348 1.00 38.20 ? 1186 HOH A O 1 HETATM 2545 O O . HOH S 7 . ? 43.523 13.086 -10.777 1.00 43.73 ? 1187 HOH A O 1 HETATM 2546 O O . HOH S 7 . ? 66.336 5.275 -5.363 1.00 43.69 ? 1188 HOH A O 1 HETATM 2547 O O . HOH S 7 . ? 30.312 12.563 8.244 1.00 45.85 ? 1189 HOH A O 1 HETATM 2548 O O . HOH S 7 . ? 33.417 -1.913 17.479 1.00 42.76 ? 1190 HOH A O 1 HETATM 2549 O O . HOH S 7 . ? 77.102 18.388 0.994 1.00 46.59 ? 1191 HOH A O 1 HETATM 2550 O O . HOH S 7 . ? 54.174 5.213 11.251 1.00 48.46 ? 1192 HOH A O 1 HETATM 2551 O O . HOH S 7 . ? 52.325 7.970 -10.839 1.00 41.53 ? 1193 HOH A O 1 HETATM 2552 O O . HOH S 7 . ? 43.294 27.716 12.964 1.00 49.32 ? 1194 HOH A O 1 HETATM 2553 O O . HOH S 7 . ? 45.853 28.860 2.701 1.00 48.04 ? 1195 HOH A O 1 HETATM 2554 O O . HOH S 7 . ? 46.366 30.209 8.542 1.00 55.47 ? 1196 HOH A O 1 HETATM 2555 O O . HOH S 7 . ? 37.979 -18.103 2.615 1.00 44.48 ? 1197 HOH A O 1 HETATM 2556 O O . HOH S 7 . ? 24.205 -1.014 8.074 1.00 48.93 ? 1198 HOH A O 1 HETATM 2557 O O . HOH S 7 . ? 54.499 9.855 13.789 1.00 54.39 ? 1199 HOH A O 1 HETATM 2558 O O . HOH S 7 . ? 59.233 20.446 -9.429 1.00 50.03 ? 1200 HOH A O 1 HETATM 2559 O O . HOH S 7 . ? 44.014 1.686 16.886 1.00 41.03 ? 1201 HOH A O 1 HETATM 2560 O O . HOH S 7 . ? 51.611 11.770 20.843 1.00 60.24 ? 1202 HOH A O 1 HETATM 2561 O O . HOH S 7 . ? 29.214 15.156 -4.535 1.00 37.51 ? 1203 HOH A O 1 HETATM 2562 O O . HOH S 7 . ? 38.065 -14.114 -10.345 1.00 53.76 ? 1204 HOH A O 1 HETATM 2563 O O . HOH S 7 . ? 28.592 -3.848 15.481 1.00 47.23 ? 1205 HOH A O 1 HETATM 2564 O O . HOH S 7 . ? 74.202 22.576 -1.335 1.00 43.11 ? 1206 HOH A O 1 HETATM 2565 O O . HOH S 7 . ? 49.855 -1.528 9.810 1.00 38.86 ? 1207 HOH A O 1 HETATM 2566 O O . HOH S 7 . ? 50.196 0.669 8.493 1.00 48.91 ? 1208 HOH A O 1 HETATM 2567 O O . HOH S 7 . ? 46.990 24.736 -2.643 1.00 48.43 ? 1209 HOH A O 1 HETATM 2568 O O . HOH S 7 . ? 43.110 22.681 -0.931 1.00 48.87 ? 1210 HOH A O 1 HETATM 2569 O O . HOH S 7 . ? 27.094 12.974 6.367 1.00 44.13 ? 1211 HOH A O 1 HETATM 2570 O O . HOH S 7 . ? 65.253 0.234 9.596 1.00 52.54 ? 1212 HOH A O 1 HETATM 2571 O O . HOH S 7 . ? 45.084 -2.706 10.897 1.00 52.37 ? 1213 HOH A O 1 HETATM 2572 O O . HOH S 7 . ? 63.614 25.291 -4.482 1.00 50.87 ? 1214 HOH A O 1 HETATM 2573 O O . HOH S 7 . ? 49.833 6.287 11.255 1.00 48.53 ? 1215 HOH A O 1 HETATM 2574 O O . HOH S 7 . ? 31.092 15.436 5.723 1.00 45.79 ? 1216 HOH A O 1 HETATM 2575 O O . HOH S 7 . ? 27.302 -16.051 -4.830 1.00 50.07 ? 1217 HOH A O 1 HETATM 2576 O O . HOH S 7 . ? 68.713 3.502 12.398 1.00 40.08 ? 1218 HOH A O 1 HETATM 2577 O O . HOH S 7 . ? 68.580 28.816 18.894 1.00 50.95 ? 1219 HOH A O 1 HETATM 2578 O O . HOH S 7 . ? 78.711 15.651 2.272 1.00 47.72 ? 1220 HOH A O 1 HETATM 2579 O O . HOH S 7 . ? 70.761 25.372 16.420 1.00 45.55 ? 1221 HOH A O 1 HETATM 2580 O O . HOH S 7 . ? 45.113 20.464 15.688 1.00 40.12 ? 1222 HOH A O 1 HETATM 2581 O O . HOH S 7 . ? 50.321 28.201 20.997 1.00 44.34 ? 1223 HOH A O 1 HETATM 2582 O O . HOH S 7 . ? 56.913 -0.343 12.656 1.00 55.86 ? 1224 HOH A O 1 HETATM 2583 O O . HOH S 7 . ? 53.701 12.177 18.454 1.00 49.97 ? 1225 HOH A O 1 HETATM 2584 O O . HOH S 7 . ? 46.389 4.315 13.249 1.00 47.49 ? 1226 HOH A O 1 HETATM 2585 O O . HOH S 7 . ? 43.813 -17.283 -0.298 1.00 47.02 ? 1227 HOH A O 1 HETATM 2586 O O . HOH S 7 . ? 43.050 19.605 14.121 1.00 42.79 ? 1228 HOH A O 1 HETATM 2587 O O . HOH S 7 . ? 50.392 -5.232 -14.600 1.00 48.55 ? 1229 HOH A O 1 HETATM 2588 O O . HOH S 7 . ? 77.524 7.365 9.690 1.00 44.73 ? 1230 HOH A O 1 HETATM 2589 O O . HOH S 7 . ? 17.770 8.784 0.788 1.00 47.25 ? 1231 HOH A O 1 HETATM 2590 O O . HOH S 7 . ? 25.373 -2.302 9.707 1.00 44.35 ? 1232 HOH A O 1 HETATM 2591 O O . HOH S 7 . ? 48.509 26.943 -2.864 1.00 51.94 ? 1233 HOH A O 1 HETATM 2592 O O . HOH S 7 . ? 74.777 21.849 -4.116 1.00 51.50 ? 1234 HOH A O 1 HETATM 2593 O O . HOH S 7 . ? 35.332 14.829 9.616 1.00 47.03 ? 1235 HOH A O 1 HETATM 2594 O O . HOH S 7 . ? 39.790 -16.855 -11.105 1.00 52.36 ? 1236 HOH A O 1 HETATM 2595 O O . HOH S 7 . ? 52.844 26.438 -8.630 1.00 45.29 ? 1237 HOH A O 1 HETATM 2596 O O . HOH S 7 . ? 69.309 31.867 19.975 1.00 52.07 ? 1238 HOH A O 1 HETATM 2597 O O . HOH S 7 . ? 48.294 12.723 -10.450 1.00 47.39 ? 1239 HOH A O 1 HETATM 2598 O O . HOH S 7 . ? 40.850 -12.549 -11.615 1.00 43.31 ? 1240 HOH A O 1 HETATM 2599 O O . HOH S 7 . ? 47.344 -3.175 -17.127 1.00 47.51 ? 1241 HOH A O 1 HETATM 2600 O O . HOH S 7 . ? 55.687 11.242 18.969 1.00 57.99 ? 1242 HOH A O 1 HETATM 2601 O O . HOH S 7 . ? 54.900 13.997 22.579 1.00 54.23 ? 1243 HOH A O 1 HETATM 2602 O O . HOH S 7 . ? 62.000 30.254 14.745 1.00 41.08 ? 1244 HOH A O 1 HETATM 2603 O O . HOH S 7 . ? 35.657 16.608 -8.914 1.00 53.94 ? 1245 HOH A O 1 HETATM 2604 O O . HOH S 7 . ? 51.631 9.877 -12.845 1.00 48.90 ? 1246 HOH A O 1 HETATM 2605 O O . HOH S 7 . ? 39.045 9.732 -15.109 1.00 50.05 ? 1247 HOH A O 1 HETATM 2606 O O . HOH S 7 . ? 54.320 -1.359 -12.191 1.00 49.26 ? 1248 HOH A O 1 HETATM 2607 O O . HOH S 7 . ? 33.341 -7.808 15.536 1.00 49.63 ? 1249 HOH A O 1 HETATM 2608 O O . HOH S 7 . ? 26.762 10.406 -9.339 1.00 28.19 ? 1250 HOH A O 1 HETATM 2609 O O . HOH S 7 . ? 33.028 1.713 18.510 1.00 37.29 ? 1251 HOH A O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . THR A 1 ? 0.7320 0.7024 0.6562 0.0063 0.0085 -0.0002 1 THR A N 2 C CA . THR A 1 ? 0.6852 0.6272 0.6146 0.0283 -0.0113 0.0378 1 THR A CA 3 C C . THR A 1 ? 0.5751 0.5711 0.5334 0.0278 0.0027 0.0005 1 THR A C 4 O O . THR A 1 ? 0.6025 0.5171 0.5252 0.0503 -0.0216 0.0530 1 THR A O 5 C CB . THR A 1 ? 0.6889 0.6416 0.6464 0.0013 -0.0111 -0.0040 1 THR A CB 6 O OG1 . THR A 1 ? 0.7259 0.7115 0.6948 0.0109 0.0015 0.0015 1 THR A OG1 7 C CG2 . THR A 1 ? 0.6486 0.6477 0.6433 -0.0011 0.0049 0.0209 1 THR A CG2 8 N N . SER A 2 ? 0.5624 0.4113 0.3545 0.0114 -0.0395 0.0357 2 SER A N 9 C CA . SER A 2 ? 0.3933 0.3298 0.3357 0.0237 -0.0276 0.0115 2 SER A CA 10 C C . SER A 2 ? 0.3597 0.3128 0.3100 -0.0304 -0.0004 0.0280 2 SER A C 11 O O . SER A 2 ? 0.3690 0.3830 0.3109 -0.0155 0.0286 0.0671 2 SER A O 12 C CB . SER A 2 ? 0.4225 0.4503 0.4161 -0.0097 -0.0173 -0.0139 2 SER A CB 13 O OG . SER A 2 ? 0.4355 0.4776 0.4839 -0.0341 0.0063 0.0013 2 SER A OG 14 N N . PHE A 3 ? 0.2205 0.2801 0.2487 -0.0413 -0.0272 0.0307 3 PHE A N 15 C CA . PHE A 3 ? 0.2483 0.2503 0.2293 0.0094 -0.0530 0.0482 3 PHE A CA 16 C C . PHE A 3 ? 0.1993 0.2006 0.2079 -0.0001 -0.0289 0.0159 3 PHE A C 17 O O . PHE A 3 ? 0.2353 0.3214 0.2182 -0.0022 -0.0379 -0.0027 3 PHE A O 18 C CB . PHE A 3 ? 0.1988 0.3047 0.2461 0.0152 -0.0039 0.0209 3 PHE A CB 19 C CG . PHE A 3 ? 0.2257 0.2453 0.2109 -0.0141 -0.0383 -0.0078 3 PHE A CG 20 C CD1 . PHE A 3 ? 0.3050 0.2739 0.2885 0.0149 0.0111 -0.0230 3 PHE A CD1 21 C CD2 . PHE A 3 ? 0.2282 0.3086 0.2146 -0.0179 -0.0195 0.0236 3 PHE A CD2 22 C CE1 . PHE A 3 ? 0.2009 0.2941 0.3006 -0.0368 -0.0623 -0.0091 3 PHE A CE1 23 C CE2 . PHE A 3 ? 0.2635 0.2922 0.2571 -0.0175 -0.0023 0.0235 3 PHE A CE2 24 C CZ . PHE A 3 ? 0.2182 0.3375 0.2168 0.0045 0.0166 0.0212 3 PHE A CZ 25 N N . THR A 4 ? 0.2297 0.1977 0.2202 0.0085 -0.0278 0.0288 4 THR A N 26 C CA . THR A 4 ? 0.1938 0.2543 0.1636 -0.0093 -0.0234 0.0273 4 THR A CA 27 C C . THR A 4 ? 0.2515 0.2542 0.2003 -0.0195 -0.0103 0.0249 4 THR A C 28 O O . THR A 4 ? 0.2167 0.2874 0.2153 -0.0184 -0.0008 0.0472 4 THR A O 29 C CB . THR A 4 ? 0.2273 0.3136 0.2473 0.0229 -0.0431 0.0315 4 THR A CB 30 O OG1 . THR A 4 ? 0.2439 0.3035 0.2330 -0.0103 -0.0133 0.0536 4 THR A OG1 31 C CG2 . THR A 4 ? 0.2191 0.2770 0.2189 0.0119 -0.0254 0.0533 4 THR A CG2 32 N N . ARG A 5 ? 0.2220 0.2678 0.2044 -0.0180 -0.0181 0.0376 5 ARG A N 33 C CA . ARG A 5 ? 0.1814 0.2515 0.2364 -0.0129 -0.0213 0.0446 5 ARG A CA 34 C C . ARG A 5 ? 0.2406 0.2824 0.2427 -0.0080 -0.0081 0.0233 5 ARG A C 35 O O . ARG A 5 ? 0.2244 0.2823 0.2235 -0.0292 -0.0275 0.0195 5 ARG A O 36 C CB . ARG A 5 ? 0.1934 0.2678 0.2326 0.0026 -0.0332 0.0293 5 ARG A CB 37 C CG . ARG A 5 ? 0.2244 0.3086 0.1945 -0.0016 -0.0581 0.0193 5 ARG A CG 38 C CD . ARG A 5 ? 0.2272 0.2723 0.2103 -0.0194 -0.0219 0.0376 5 ARG A CD 39 N NE . ARG A 5 ? 0.2939 0.3274 0.1865 -0.0254 -0.0421 0.0433 5 ARG A NE 40 C CZ . ARG A 5 ? 0.2189 0.2717 0.2120 -0.0092 -0.0114 0.0263 5 ARG A CZ 41 N NH1 . ARG A 5 ? 0.2255 0.2774 0.2089 -0.0287 -0.0110 0.0108 5 ARG A NH1 42 N NH2 . ARG A 5 ? 0.2767 0.3339 0.2341 0.0074 -0.0552 0.0201 5 ARG A NH2 43 N N . ASN A 6 ? 0.1905 0.2675 0.1837 0.0062 -0.0136 0.0430 6 ASN A N 44 C CA . ASN A 6 ? 0.1823 0.1904 0.1643 0.0047 0.0146 0.0379 6 ASN A CA 45 C C . ASN A 6 ? 0.1603 0.2492 0.1604 0.0160 0.0033 0.0195 6 ASN A C 46 O O . ASN A 6 ? 0.1869 0.2599 0.2139 0.0122 -0.0279 0.0234 6 ASN A O 47 C CB . ASN A 6 ? 0.1649 0.1855 0.2110 -0.0105 0.0033 0.0048 6 ASN A CB 48 C CG . ASN A 6 ? 0.1851 0.2384 0.2066 0.0070 0.0044 0.0048 6 ASN A CG 49 O OD1 . ASN A 6 ? 0.2226 0.3104 0.2261 0.0128 0.0220 0.0264 6 ASN A OD1 50 N ND2 . ASN A 6 ? 0.2290 0.2626 0.1966 -0.0299 -0.0206 -0.0041 6 ASN A ND2 51 N N . ILE A 7 ? 0.1983 0.2255 0.1587 -0.0142 0.0222 0.0090 7 ILE A N 52 C CA . ILE A 7 ? 0.1820 0.2114 0.2027 0.0170 0.0148 -0.0091 7 ILE A CA 53 C C . ILE A 7 ? 0.1572 0.2058 0.2016 0.0048 -0.0076 -0.0046 7 ILE A C 54 O O . ILE A 7 ? 0.1969 0.2639 0.1924 -0.0224 -0.0129 0.0438 7 ILE A O 55 C CB . ILE A 7 ? 0.1903 0.1817 0.2151 0.0111 -0.0006 -0.0010 7 ILE A CB 56 C CG1 . ILE A 7 ? 0.1679 0.2212 0.2246 -0.0230 -0.0208 0.0228 7 ILE A CG1 57 C CG2 . ILE A 7 ? 0.1682 0.2783 0.2074 0.0026 -0.0065 0.0246 7 ILE A CG2 58 C CD1 . ILE A 7 ? 0.1762 0.2194 0.2447 -0.0395 0.0162 0.0000 7 ILE A CD1 59 N N . VAL A 8 ? 0.1648 0.1907 0.2061 -0.0226 0.0005 0.0340 8 VAL A N 60 C CA . VAL A 8 ? 0.1885 0.1815 0.2002 -0.0174 0.0184 -0.0151 8 VAL A CA 61 C C . VAL A 8 ? 0.1847 0.2426 0.2047 0.0456 0.0217 0.0251 8 VAL A C 62 O O . VAL A 8 ? 0.2023 0.2893 0.2049 0.0483 -0.0099 0.0355 8 VAL A O 63 C CB . VAL A 8 ? 0.2016 0.1892 0.1981 -0.0288 0.0073 0.0192 8 VAL A CB 64 C CG1 . VAL A 8 ? 0.2135 0.1729 0.2578 -0.0039 -0.0171 0.0463 8 VAL A CG1 65 C CG2 . VAL A 8 ? 0.1677 0.2388 0.2021 -0.0042 -0.0004 0.0188 8 VAL A CG2 66 N N . GLY A 9 ? 0.1809 0.2742 0.1573 -0.0148 -0.0088 0.0052 9 GLY A N 67 C CA . GLY A 9 ? 0.2112 0.2417 0.1904 -0.0126 0.0109 0.0581 9 GLY A CA 68 C C . GLY A 9 ? 0.1655 0.2082 0.1991 0.0311 0.0139 0.0102 9 GLY A C 69 O O . GLY A 9 ? 0.1841 0.2522 0.2202 0.0001 0.0222 0.0091 9 GLY A O 70 N N . ARG A 10 ? 0.1578 0.2225 0.2105 -0.0136 -0.0130 0.0363 10 ARG A N 71 C CA . ARG A 10 ? 0.1859 0.2117 0.2165 -0.0006 0.0005 0.0227 10 ARG A CA 72 C C . ARG A 10 ? 0.1990 0.2362 0.1656 0.0001 0.0064 0.0033 10 ARG A C 73 O O . ARG A 10 ? 0.1825 0.2522 0.2283 -0.0071 -0.0122 0.0059 10 ARG A O 74 C CB . ARG A 10 ? 0.1857 0.2540 0.1878 0.0000 -0.0139 0.0234 10 ARG A CB 75 C CG . ARG A 10 ? 0.2522 0.3035 0.1940 -0.0174 0.0089 0.0364 10 ARG A CG 76 C CD . ARG A 10 ? 0.2247 0.2603 0.2046 0.0217 0.0344 0.0322 10 ARG A CD 77 N NE . ARG A 10 ? 0.1810 0.2545 0.2140 0.0018 0.0026 0.0226 10 ARG A NE 78 C CZ . ARG A 10 ? 0.2041 0.2773 0.2136 0.0039 -0.0144 0.0138 10 ARG A CZ 79 N NH1 . ARG A 10 ? 0.2119 0.2579 0.2566 0.0363 -0.0020 0.0317 10 ARG A NH1 80 N NH2 . ARG A 10 ? 0.2152 0.3497 0.2747 -0.0211 0.0149 0.0688 10 ARG A NH2 81 N N . ASP A 11 ? 0.2087 0.2264 0.2097 0.0103 0.0175 -0.0005 11 ASP A N 82 C CA . ASP A 11 ? 0.2142 0.2386 0.1773 0.0387 -0.0127 0.0277 11 ASP A CA 83 C C . ASP A 11 ? 0.2238 0.2516 0.2159 -0.0023 0.0016 0.0262 11 ASP A C 84 O O . ASP A 11 ? 0.2324 0.2839 0.2958 0.0008 -0.0173 0.0433 11 ASP A O 85 C CB . ASP A 11 ? 0.2008 0.3179 0.2087 0.0389 -0.0276 0.0220 11 ASP A CB 86 C CG . ASP A 11 ? 0.1953 0.3482 0.3784 0.0323 -0.0256 0.0914 11 ASP A CG 87 O OD1 . ASP A 11 ? 0.3245 0.3190 0.3639 -0.0122 -0.0979 0.0449 11 ASP A OD1 88 O OD2 . ASP A 11 ? 0.2342 0.3465 0.3154 -0.0194 -0.0396 0.0555 11 ASP A OD2 89 N N . GLY A 12 ? 0.1620 0.2327 0.2051 -0.0044 0.0039 0.0264 12 GLY A N 90 C CA . GLY A 12 ? 0.1794 0.2661 0.2397 -0.0229 0.0278 -0.0161 12 GLY A CA 91 C C . GLY A 12 ? 0.1973 0.1997 0.1944 -0.0095 -0.0156 -0.0237 12 GLY A C 92 O O . GLY A 12 ? 0.1795 0.2661 0.2358 -0.0169 -0.0083 -0.0167 12 GLY A O 93 N N . LEU A 13 ? 0.1656 0.2338 0.2069 -0.0073 -0.0340 -0.0256 13 LEU A N 94 C CA . LEU A 13 ? 0.1619 0.2064 0.2031 -0.0187 -0.0446 0.0192 13 LEU A CA 95 C C . LEU A 13 ? 0.2225 0.2041 0.2365 -0.0032 -0.0119 0.0200 13 LEU A C 96 O O . LEU A 13 ? 0.1724 0.2529 0.2512 0.0147 0.0035 0.0247 13 LEU A O 97 C CB . LEU A 13 ? 0.1989 0.2252 0.1651 0.0190 -0.0279 0.0425 13 LEU A CB 98 C CG . LEU A 13 ? 0.3144 0.2887 0.1534 0.0497 -0.0443 0.0504 13 LEU A CG 99 C CD1 . LEU A 13 ? 0.4902 0.3139 0.2168 0.0087 -0.0542 0.0156 13 LEU A CD1 100 C CD2 . LEU A 13 ? 0.3114 0.4205 0.3905 0.0483 0.0079 0.0127 13 LEU A CD2 101 N N . CYS A 14 ? 0.2115 0.2142 0.1834 0.0113 -0.0120 -0.0052 14 CYS A N 102 C CA . CYS A 14 ? 0.1764 0.1842 0.2281 -0.0162 0.0143 -0.0114 14 CYS A CA 103 C C . CYS A 14 ? 0.2092 0.2154 0.1858 -0.0027 0.0047 -0.0052 14 CYS A C 104 O O . CYS A 14 ? 0.2048 0.2507 0.1740 -0.0044 -0.0345 0.0172 14 CYS A O 105 C CB . CYS A 14 ? 0.2177 0.2709 0.1536 -0.0202 -0.0117 -0.0152 14 CYS A CB 106 S SG . CYS A 14 ? 0.2140 0.2681 0.1899 -0.0059 -0.0150 0.0069 14 CYS A SG 107 N N . VAL A 15 ? 0.1732 0.2056 0.1890 0.0021 0.0047 -0.0049 15 VAL A N 108 C CA . VAL A 15 ? 0.1844 0.1606 0.2216 0.0056 0.0082 -0.0124 15 VAL A CA 109 C C . VAL A 15 ? 0.2015 0.2480 0.1973 -0.0232 0.0004 0.0282 15 VAL A C 110 O O . VAL A 15 ? 0.1929 0.2668 0.1835 -0.0010 0.0029 0.0097 15 VAL A O 111 C CB . VAL A 15 ? 0.1403 0.1921 0.2337 0.0016 0.0121 0.0040 15 VAL A CB 112 C CG1 . VAL A 15 ? 0.2391 0.2469 0.1978 -0.0379 -0.0242 -0.0146 15 VAL A CG1 113 C CG2 . VAL A 15 ? 0.1309 0.2172 0.2259 0.0161 0.0158 0.0013 15 VAL A CG2 114 N N . ASP A 16 ? 0.1748 0.2820 0.1872 0.0126 -0.0261 0.0096 16 ASP A N 115 C CA . ASP A 16 ? 0.1720 0.2272 0.2120 -0.0091 -0.0005 -0.0044 16 ASP A CA 116 C C . ASP A 16 ? 0.2037 0.2465 0.2172 0.0080 0.0074 0.0050 16 ASP A C 117 O O . ASP A 16 ? 0.1780 0.2658 0.1998 0.0037 -0.0138 0.0044 16 ASP A O 118 C CB . ASP A 16 ? 0.1473 0.2204 0.1938 0.0391 -0.0026 -0.0046 16 ASP A CB 119 C CG . ASP A 16 ? 0.1575 0.2359 0.2321 0.0340 0.0118 -0.0312 16 ASP A CG 120 O OD1 . ASP A 16 ? 0.1809 0.2724 0.1867 0.0219 -0.0178 -0.0280 16 ASP A OD1 121 O OD2 . ASP A 16 ? 0.2203 0.2825 0.2239 -0.0372 -0.0254 0.0188 16 ASP A OD2 122 N N . VAL A 17 ? 0.1786 0.1888 0.2310 -0.0292 -0.0125 -0.0118 17 VAL A N 123 C CA . VAL A 17 ? 0.1533 0.1971 0.2156 -0.0398 -0.0290 0.0122 17 VAL A CA 124 C C . VAL A 17 ? 0.2250 0.2198 0.1910 0.0219 -0.0096 -0.0130 17 VAL A C 125 O O . VAL A 17 ? 0.1758 0.2572 0.2010 -0.0154 0.0022 -0.0014 17 VAL A O 126 C CB . VAL A 17 ? 0.1992 0.2133 0.2302 -0.0365 -0.0297 0.0176 17 VAL A CB 127 C CG1 . VAL A 17 ? 0.2899 0.2960 0.2021 -0.0063 -0.0375 -0.0232 17 VAL A CG1 128 C CG2 . VAL A 17 ? 0.2070 0.2234 0.2280 -0.0013 -0.0462 0.0310 17 VAL A CG2 129 N N . ARG A 18 ? 0.1810 0.2188 0.1819 0.0034 -0.0327 0.0308 18 ARG A N 130 C CA . ARG A 18 ? 0.1707 0.2638 0.1709 0.0277 0.0346 0.0320 18 ARG A CA 131 C C . ARG A 18 ? 0.1772 0.2402 0.1874 -0.0331 -0.0060 -0.0203 18 ARG A C 132 O O . ARG A 18 ? 0.1819 0.2735 0.2205 -0.0216 -0.0123 0.0038 18 ARG A O 133 C CB . ARG A 18 ? 0.2305 0.2239 0.1469 0.0218 0.0084 0.0121 18 ARG A CB 134 C CG . ARG A 18 ? 0.1965 0.2670 0.1344 0.0099 -0.0199 0.0291 18 ARG A CG 135 C CD . ARG A 18 ? 0.2623 0.2755 0.1651 0.0366 0.0135 0.0139 18 ARG A CD 136 N NE . ARG A 18 ? 0.1976 0.2367 0.1996 -0.0108 -0.0170 0.0171 18 ARG A NE 137 C CZ . ARG A 18 ? 0.1786 0.1855 0.2364 0.0091 -0.0165 0.0134 18 ARG A CZ 138 N NH1 . ARG A 18 ? 0.2636 0.2579 0.2071 0.0259 -0.0331 0.0030 18 ARG A NH1 139 N NH2 . ARG A 18 ? 0.1604 0.2417 0.2430 0.0375 -0.0242 0.0144 18 ARG A NH2 140 N N . ASN A 19 ? 0.1559 0.2863 0.1851 0.0051 -0.0151 0.0143 19 ASN A N 141 C CA . ASN A 19 ? 0.1452 0.3294 0.1948 -0.0041 0.0174 0.0009 19 ASN A CA 142 C C . ASN A 19 ? 0.1774 0.2667 0.1692 0.0505 0.0173 0.0282 19 ASN A C 143 O O . ASN A 19 ? 0.1783 0.3474 0.2587 0.0162 0.0190 -0.0014 19 ASN A O 144 C CB . ASN A 19 ? 0.2174 0.2980 0.2237 0.0181 -0.0044 0.0026 19 ASN A CB 145 C CG . ASN A 19 ? 0.2401 0.2980 0.2973 0.0037 -0.0280 0.0272 19 ASN A CG 146 O OD1 . ASN A 19 ? 0.3234 0.3335 0.3747 0.0146 -0.0359 0.0889 19 ASN A OD1 147 N ND2 . ASN A 19 ? 0.2814 0.3963 0.2775 0.0081 -0.0219 0.0199 19 ASN A ND2 148 N N . GLY A 20 ? 0.1988 0.2420 0.2032 -0.0045 -0.0242 0.0393 20 GLY A N 149 C CA . GLY A 20 ? 0.2403 0.2402 0.2464 -0.0220 0.0049 0.0487 20 GLY A CA 150 C C . GLY A 20 ? 0.2569 0.2789 0.2122 0.0036 -0.0269 0.0204 20 GLY A C 151 O O . GLY A 20 ? 0.2580 0.3671 0.2569 -0.0023 -0.0325 0.0264 20 GLY A O 152 N N . TYR A 21 ? 0.2055 0.2535 0.2332 0.0029 -0.0117 -0.0333 21 TYR A N 153 C CA . TYR A 21 ? 0.2835 0.2372 0.2332 0.0028 -0.0105 -0.0011 21 TYR A CA 154 C C . TYR A 21 ? 0.2006 0.2557 0.2777 -0.0022 -0.0119 0.0176 21 TYR A C 155 O O . TYR A 21 ? 0.1746 0.2879 0.2985 -0.0009 -0.0301 0.0140 21 TYR A O 156 C CB . TYR A 21 ? 0.2023 0.3552 0.2535 0.0003 -0.0306 -0.0006 21 TYR A CB 157 C CG . TYR A 21 ? 0.1984 0.2959 0.2501 0.0004 0.0036 -0.0145 21 TYR A CG 158 C CD1 . TYR A 21 ? 0.2555 0.3960 0.2861 0.0031 -0.0043 0.0354 21 TYR A CD1 159 C CD2 . TYR A 21 ? 0.2461 0.3292 0.2752 0.0021 -0.0117 0.0026 21 TYR A CD2 160 C CE1 . TYR A 21 ? 0.2421 0.3028 0.3242 0.0035 0.0035 0.0042 21 TYR A CE1 161 C CE2 . TYR A 21 ? 0.2482 0.4019 0.2910 0.0168 -0.0270 0.0077 21 TYR A CE2 162 C CZ . TYR A 21 ? 0.2943 0.3472 0.2853 0.0371 0.0067 0.0107 21 TYR A CZ 163 O OH . TYR A 21 ? 0.3337 0.4229 0.3180 0.0690 -0.0176 0.0314 21 TYR A OH 164 N N . ASP A 22 ? 0.2972 0.2851 0.3380 -0.0308 -0.0010 0.0433 22 ASP A N 165 C CA . ASP A 22 ? 0.2476 0.3402 0.2721 0.0031 -0.0200 0.0323 22 ASP A CA 166 C C . ASP A 22 ? 0.2171 0.3009 0.2878 -0.0028 0.0033 0.0292 22 ASP A C 167 O O . ASP A 22 ? 0.2753 0.3154 0.2746 -0.0037 -0.0256 0.0470 22 ASP A O 168 C CB . ASP A 22 ? 0.2781 0.3626 0.2905 -0.0438 0.0232 0.0136 22 ASP A CB 169 C CG . ASP A 22 ? 0.3223 0.4354 0.3436 -0.0224 0.0125 0.0079 22 ASP A CG 170 O OD1 . ASP A 22 ? 0.3902 0.5071 0.3766 -0.0105 0.0041 0.0836 22 ASP A OD1 171 O OD2 . ASP A 22 ? 0.3168 0.3594 0.3730 -0.0195 -0.0056 0.0064 22 ASP A OD2 172 N N A THR A 23 ? 0.2176 0.3376 0.3046 0.0197 -0.0165 0.0035 23 THR A N 173 N N B THR A 23 ? 0.1694 0.3185 0.2875 0.0216 -0.0139 -0.0043 23 THR A N 174 C CA A THR A 23 ? 0.2805 0.3437 0.2601 -0.0094 -0.0227 0.0070 23 THR A CA 175 C CA B THR A 23 ? 0.2206 0.3227 0.2168 -0.0094 -0.0532 0.0126 23 THR A CA 176 C C A THR A 23 ? 0.3004 0.2965 0.2686 -0.0068 -0.0204 0.0001 23 THR A C 177 C C B THR A 23 ? 0.2835 0.2869 0.2176 0.0041 -0.0243 0.0000 23 THR A C 178 O O A THR A 23 ? 0.2005 0.2916 0.2563 -0.0265 -0.0198 0.0229 23 THR A O 179 O O B THR A 23 ? 0.2298 0.3017 0.2478 -0.0229 -0.0238 0.0077 23 THR A O 180 C CB A THR A 23 ? 0.3067 0.3528 0.3172 0.0199 -0.0277 0.0143 23 THR A CB 181 C CB B THR A 23 ? 0.1897 0.3073 0.1879 0.0173 -0.0157 0.0145 23 THR A CB 182 O OG1 A THR A 23 ? 0.3245 0.4260 0.3390 -0.0256 -0.0081 0.0014 23 THR A OG1 183 O OG1 B THR A 23 ? 0.3705 0.2889 0.2794 -0.0026 -0.0258 0.0238 23 THR A OG1 184 C CG2 A THR A 23 ? 0.3119 0.3548 0.2088 0.0025 -0.0620 -0.0188 23 THR A CG2 185 C CG2 B THR A 23 ? 0.1688 0.2663 0.2930 0.0606 -0.0103 0.0627 23 THR A CG2 186 N N . ASP A 24 ? 0.2533 0.2895 0.2438 0.0278 0.0028 0.0281 24 ASP A N 187 C CA . ASP A 24 ? 0.2329 0.2710 0.2594 -0.0122 0.0074 0.0129 24 ASP A CA 188 C C . ASP A 24 ? 0.2555 0.3534 0.2830 -0.0174 -0.0252 0.0280 24 ASP A C 189 O O . ASP A 24 ? 0.2349 0.3348 0.3041 -0.0414 -0.0366 0.0515 24 ASP A O 190 C CB . ASP A 24 ? 0.2982 0.2628 0.3095 -0.0282 -0.0576 0.0385 24 ASP A CB 191 C CG . ASP A 24 ? 0.3227 0.2828 0.2375 -0.0366 -0.0156 0.0031 24 ASP A CG 192 O OD1 . ASP A 24 ? 0.3136 0.3274 0.3725 -0.0628 -0.0589 0.0179 24 ASP A OD1 193 O OD2 . ASP A 24 ? 0.2373 0.3184 0.2725 -0.0389 -0.0365 0.0195 24 ASP A OD2 194 N N . GLY A 25 ? 0.2295 0.2687 0.2497 -0.0268 -0.0089 0.0334 25 GLY A N 195 C CA . GLY A 25 ? 0.2048 0.2606 0.2875 -0.0031 -0.0158 0.0359 25 GLY A CA 196 C C . GLY A 25 ? 0.2257 0.2604 0.1971 -0.0193 -0.0479 -0.0460 25 GLY A C 197 O O . GLY A 25 ? 0.2334 0.2899 0.2534 -0.0199 -0.0373 -0.0071 25 GLY A O 198 N N . THR A 26 ? 0.1721 0.2487 0.2023 0.0057 -0.0525 -0.0268 26 THR A N 199 C CA . THR A 26 ? 0.2096 0.2550 0.2326 -0.0176 0.0095 -0.0189 26 THR A CA 200 C C . THR A 26 ? 0.2025 0.2608 0.1636 -0.0049 0.0164 -0.0275 26 THR A C 201 O O . THR A 26 ? 0.1830 0.2867 0.2599 -0.0257 -0.0303 -0.0040 26 THR A O 202 C CB . THR A 26 ? 0.1889 0.3117 0.2358 -0.0102 -0.0027 -0.0376 26 THR A CB 203 O OG1 . THR A 26 ? 0.1752 0.2917 0.2423 -0.0213 0.0105 0.0149 26 THR A OG1 204 C CG2 . THR A 26 ? 0.1727 0.2932 0.2573 -0.0077 -0.0496 0.0075 26 THR A CG2 205 N N A PRO A 27 ? 0.1902 0.2354 0.1759 -0.0276 -0.0118 -0.0125 27 PRO A N 206 N N B PRO A 27 ? 0.1640 0.2282 0.1942 -0.0088 -0.0073 -0.0125 27 PRO A N 207 C CA A PRO A 27 ? 0.1637 0.2391 0.2106 -0.0416 0.0061 0.0031 27 PRO A CA 208 C CA B PRO A 27 ? 0.1538 0.2487 0.2195 -0.0341 0.0023 -0.0023 27 PRO A CA 209 C C A PRO A 27 ? 0.1736 0.2569 0.1897 0.0157 0.0150 0.0044 27 PRO A C 210 C C B PRO A 27 ? 0.1690 0.2459 0.1807 0.0049 0.0022 0.0177 27 PRO A C 211 O O A PRO A 27 ? 0.1237 0.1721 0.1806 0.0031 -0.0036 0.0349 27 PRO A O 212 O O B PRO A 27 ? 0.1916 0.2408 0.1956 -0.0045 -0.0180 -0.0096 27 PRO A O 213 C CB A PRO A 27 ? 0.2138 0.3009 0.1734 -0.0130 -0.0223 -0.0040 27 PRO A CB 214 C CB B PRO A 27 ? 0.2262 0.3058 0.2080 -0.0040 -0.0197 -0.0006 27 PRO A CB 215 C CG A PRO A 27 ? 0.1759 0.2206 0.1788 -0.0262 -0.0060 0.0031 27 PRO A CG 216 C CG B PRO A 27 ? 0.2296 0.1826 0.2296 0.0086 0.0284 0.0227 27 PRO A CG 217 C CD A PRO A 27 ? 0.1564 0.1937 0.1482 0.0115 0.0178 0.0005 27 PRO A CD 218 C CD B PRO A 27 ? 0.2562 0.2020 0.2468 -0.0189 -0.0018 0.0276 27 PRO A CD 219 N N . LEU A 28 ? 0.1816 0.2360 0.1967 0.0009 -0.0292 -0.0066 28 LEU A N 220 C CA . LEU A 28 ? 0.1856 0.1939 0.2234 0.0140 -0.0342 -0.0139 28 LEU A CA 221 C C . LEU A 28 ? 0.1828 0.2239 0.1938 0.0098 -0.0310 -0.0003 28 LEU A C 222 O O . LEU A 28 ? 0.1729 0.2614 0.1949 -0.0110 -0.0372 0.0037 28 LEU A O 223 C CB . LEU A 28 ? 0.2007 0.1914 0.2093 0.0606 -0.0160 0.0305 28 LEU A CB 224 C CG . LEU A 28 ? 0.2113 0.2953 0.2786 0.0869 -0.0203 0.0917 28 LEU A CG 225 C CD1 . LEU A 28 ? 0.2305 0.3018 0.2304 0.0185 -0.0500 0.0204 28 LEU A CD1 226 C CD2 . LEU A 28 ? 0.2792 0.3386 0.2693 0.0027 -0.0099 0.0289 28 LEU A CD2 227 N N . GLN A 29 ? 0.1730 0.2243 0.1736 0.0354 -0.0062 -0.0007 29 GLN A N 228 C CA . GLN A 29 ? 0.1784 0.2126 0.2041 0.0030 -0.0391 -0.0029 29 GLN A CA 229 C C . GLN A 29 ? 0.1640 0.2129 0.2145 -0.0152 -0.0036 0.0107 29 GLN A C 230 O O . GLN A 29 ? 0.2060 0.2280 0.2050 -0.0003 -0.0228 -0.0117 29 GLN A O 231 C CB . GLN A 29 ? 0.1424 0.2600 0.1929 0.0099 0.0221 0.0094 29 GLN A CB 232 C CG . GLN A 29 ? 0.1301 0.2478 0.1921 0.0222 -0.0159 -0.0173 29 GLN A CG 233 C CD . GLN A 29 ? 0.1750 0.2371 0.2029 0.0070 -0.0258 0.0006 29 GLN A CD 234 O OE1 . GLN A 29 ? 0.1725 0.2804 0.2439 0.0095 0.0220 0.0231 29 GLN A OE1 235 N NE2 . GLN A 29 ? 0.2327 0.2372 0.2036 0.0058 -0.0127 0.0096 29 GLN A NE2 236 N N . LEU A 30 ? 0.1671 0.1816 0.2159 0.0117 0.0117 0.0046 30 LEU A N 237 C CA . LEU A 30 ? 0.1696 0.2149 0.2202 0.0165 -0.0017 -0.0220 30 LEU A CA 238 C C . LEU A 30 ? 0.1726 0.3034 0.1840 0.0134 0.0106 -0.0172 30 LEU A C 239 O O . LEU A 30 ? 0.1854 0.2606 0.2107 0.0298 -0.0025 0.0015 30 LEU A O 240 C CB . LEU A 30 ? 0.1846 0.2919 0.2507 0.0211 0.0233 0.0020 30 LEU A CB 241 C CG . LEU A 30 ? 0.2068 0.2899 0.2416 0.0332 0.0063 0.0253 30 LEU A CG 242 C CD1 . LEU A 30 ? 0.2169 0.2767 0.2600 -0.0166 0.0300 -0.0354 30 LEU A CD1 243 C CD2 . LEU A 30 ? 0.2148 0.3164 0.2306 0.0590 0.0024 -0.0235 30 LEU A CD2 244 N N . TRP A 31 ? 0.1774 0.2874 0.1798 0.0238 0.0238 -0.0107 31 TRP A N 245 C CA . TRP A 31 ? 0.1895 0.2365 0.1982 0.0219 0.0062 -0.0163 31 TRP A CA 246 C C . TRP A 31 ? 0.2287 0.2307 0.1959 0.0252 -0.0043 0.0085 31 TRP A C 247 O O . TRP A 31 ? 0.2120 0.2420 0.2080 0.0131 -0.0142 0.0208 31 TRP A O 248 C CB . TRP A 31 ? 0.1980 0.2705 0.2235 0.0222 -0.0101 -0.0269 31 TRP A CB 249 C CG . TRP A 31 ? 0.2049 0.2705 0.1751 0.0440 -0.0126 0.0147 31 TRP A CG 250 C CD1 . TRP A 31 ? 0.1881 0.3154 0.2077 0.0471 0.0065 -0.0340 31 TRP A CD1 251 C CD2 . TRP A 31 ? 0.1750 0.2408 0.1983 0.0000 -0.0232 -0.0177 31 TRP A CD2 252 N NE1 . TRP A 31 ? 0.1916 0.2803 0.2419 0.0424 -0.0208 -0.0118 31 TRP A NE1 253 C CE2 . TRP A 31 ? 0.1734 0.2587 0.2465 0.0118 -0.0009 0.0123 31 TRP A CE2 254 C CE3 . TRP A 31 ? 0.2581 0.2582 0.2314 0.0196 0.0040 0.0298 31 TRP A CE3 255 C CZ2 . TRP A 31 ? 0.2745 0.2813 0.2294 0.0334 -0.0119 0.0234 31 TRP A CZ2 256 C CZ3 . TRP A 31 ? 0.2268 0.2672 0.2512 0.0208 -0.0225 -0.0007 31 TRP A CZ3 257 C CH2 . TRP A 31 ? 0.2161 0.3068 0.2211 0.0074 -0.0243 0.0032 31 TRP A CH2 258 N N . PRO A 32 ? 0.1703 0.2207 0.1953 0.0171 -0.0026 -0.0086 32 PRO A N 259 C CA . PRO A 32 ? 0.2390 0.2000 0.2031 0.0108 0.0216 -0.0019 32 PRO A CA 260 C C . PRO A 32 ? 0.1963 0.2290 0.2009 0.0004 0.0203 0.0010 32 PRO A C 261 O O . PRO A 32 ? 0.1884 0.2709 0.2170 0.0182 -0.0162 -0.0139 32 PRO A O 262 C CB . PRO A 32 ? 0.2426 0.2251 0.2128 0.0445 0.0044 0.0153 32 PRO A CB 263 C CG . PRO A 32 ? 0.2465 0.2250 0.2117 0.0458 -0.0144 -0.0178 32 PRO A CG 264 C CD . PRO A 32 ? 0.1844 0.2246 0.2477 0.0731 0.0008 -0.0270 32 PRO A CD 265 N N . CYS A 33 ? 0.2068 0.2416 0.1670 0.0215 -0.0009 0.0009 33 CYS A N 266 C CA . CYS A 33 ? 0.1727 0.2773 0.1835 0.0112 0.0033 0.0201 33 CYS A CA 267 C C . CYS A 33 ? 0.1957 0.2417 0.2257 -0.0061 0.0179 0.0009 33 CYS A C 268 O O . CYS A 33 ? 0.2484 0.2704 0.2445 0.0322 0.0342 -0.0017 33 CYS A O 269 C CB . CYS A 33 ? 0.1600 0.2893 0.2051 0.0244 -0.0276 -0.0171 33 CYS A CB 270 S SG . CYS A 33 ? 0.1849 0.2641 0.2251 -0.0088 -0.0041 -0.0005 33 CYS A SG 271 N N . GLY A 34 ? 0.2003 0.2730 0.1792 -0.0035 -0.0009 0.0000 34 GLY A N 272 C CA . GLY A 34 ? 0.2112 0.2835 0.2180 -0.0472 0.0113 0.0212 34 GLY A CA 273 C C . GLY A 34 ? 0.2801 0.2875 0.2221 -0.0238 0.0238 -0.0018 34 GLY A C 274 O O . GLY A 34 ? 0.2245 0.3384 0.2242 -0.0374 -0.0066 0.0322 34 GLY A O 275 N N . THR A 35 ? 0.2102 0.3389 0.2374 -0.0517 0.0276 -0.0280 35 THR A N 276 C CA . THR A 35 ? 0.2650 0.3262 0.2420 -0.0521 0.0220 -0.0063 35 THR A CA 277 C C . THR A 35 ? 0.2468 0.2717 0.1625 -0.0093 0.0133 0.0115 35 THR A C 278 O O . THR A 35 ? 0.2513 0.3005 0.2083 -0.0242 -0.0011 0.0265 35 THR A O 279 C CB . THR A 35 ? 0.2842 0.2903 0.2253 -0.0071 0.0255 -0.0335 35 THR A CB 280 O OG1 . THR A 35 ? 0.3724 0.4659 0.3106 0.0196 0.0625 -0.0378 35 THR A OG1 281 C CG2 . THR A 35 ? 0.4492 0.3898 0.3385 -0.0289 -0.0031 -0.0147 35 THR A CG2 282 N N . GLN A 36 ? 0.2042 0.3276 0.1740 -0.0091 -0.0151 -0.0166 36 GLN A N 283 C CA . GLN A 36 ? 0.2077 0.2815 0.2121 -0.0031 0.0034 -0.0006 36 GLN A CA 284 C C . GLN A 36 ? 0.1997 0.2247 0.1734 -0.0314 -0.0049 0.0187 36 GLN A C 285 O O . GLN A 36 ? 0.1712 0.3235 0.1926 -0.0141 0.0185 0.0040 36 GLN A O 286 C CB . GLN A 36 ? 0.2419 0.3037 0.1896 -0.0020 -0.0015 0.0210 36 GLN A CB 287 C CG . GLN A 36 ? 0.2272 0.2553 0.1913 -0.0298 0.0247 0.0094 36 GLN A CG 288 C CD . GLN A 36 ? 0.2058 0.2595 0.2412 -0.0116 0.0125 -0.0171 36 GLN A CD 289 O OE1 . GLN A 36 ? 0.2916 0.3400 0.2776 0.0341 0.0054 0.0352 36 GLN A OE1 290 N NE2 . GLN A 36 ? 0.2515 0.2821 0.2244 -0.0397 0.0119 -0.0352 36 GLN A NE2 291 N N . ARG A 37 ? 0.2374 0.2536 0.1971 -0.0519 0.0084 -0.0073 37 ARG A N 292 C CA . ARG A 37 ? 0.2213 0.3376 0.2252 0.0092 0.0131 0.0048 37 ARG A CA 293 C C . ARG A 37 ? 0.1941 0.2598 0.2317 -0.0179 0.0177 0.0001 37 ARG A C 294 O O . ARG A 37 ? 0.2363 0.2743 0.2128 -0.0003 -0.0025 0.0169 37 ARG A O 295 C CB . ARG A 37 ? 0.2557 0.3700 0.3155 -0.0009 0.0098 0.0299 37 ARG A CB 296 C CG . ARG A 37 ? 0.3641 0.4176 0.3124 0.0259 0.0322 0.0239 37 ARG A CG 297 C CD . ARG A 37 ? 0.4340 0.4994 0.3644 0.0367 0.0288 0.0125 37 ARG A CD 298 N NE . ARG A 37 ? 0.4552 0.5380 0.3701 0.0059 -0.0198 0.0407 37 ARG A NE 299 C CZ . ARG A 37 ? 0.3352 0.3478 0.3403 -0.0225 -0.0376 -0.0017 37 ARG A CZ 300 N NH1 . ARG A 37 ? 0.4189 0.4473 0.4223 0.0015 0.0250 0.0074 37 ARG A NH1 301 N NH2 . ARG A 37 ? 0.5036 0.4673 0.3980 -0.0307 0.0217 -0.0109 37 ARG A NH2 302 N N . ASN A 38 ? 0.2077 0.2903 0.1952 0.0087 -0.0026 -0.0060 38 ASN A N 303 C CA . ASN A 38 ? 0.1507 0.2974 0.1747 0.0136 -0.0375 -0.0116 38 ASN A CA 304 C C . ASN A 38 ? 0.1872 0.2748 0.2083 -0.0121 -0.0174 -0.0167 38 ASN A C 305 O O . ASN A 38 ? 0.1817 0.2690 0.2033 -0.0121 0.0113 0.0054 38 ASN A O 306 C CB . ASN A 38 ? 0.1781 0.2519 0.1937 0.0624 -0.0331 0.0121 38 ASN A CB 307 C CG . ASN A 38 ? 0.1965 0.2378 0.2325 0.0066 -0.0057 -0.0009 38 ASN A CG 308 O OD1 . ASN A 38 ? 0.2230 0.2895 0.2059 -0.0079 0.0067 -0.0141 38 ASN A OD1 309 N ND2 . ASN A 38 ? 0.2156 0.2752 0.2360 0.0122 0.0084 0.0341 38 ASN A ND2 310 N N . GLN A 39 ? 0.1493 0.2608 0.2081 -0.0188 -0.0049 0.0049 39 GLN A N 311 C CA . GLN A 39 ? 0.1723 0.2214 0.2131 -0.0145 -0.0118 0.0451 39 GLN A CA 312 C C . GLN A 39 ? 0.2061 0.2672 0.1761 -0.0306 -0.0604 0.0188 39 GLN A C 313 O O . GLN A 39 ? 0.1569 0.2685 0.2037 -0.0139 -0.0033 0.0167 39 GLN A O 314 C CB . GLN A 39 ? 0.2217 0.2331 0.2035 -0.0113 0.0037 0.0255 39 GLN A CB 315 C CG . GLN A 39 ? 0.2117 0.2446 0.2049 -0.0149 0.0242 0.0167 39 GLN A CG 316 C CD . GLN A 39 ? 0.2258 0.2247 0.1978 0.0216 0.0043 -0.0063 39 GLN A CD 317 O OE1 . GLN A 39 ? 0.2095 0.2571 0.2011 -0.0411 -0.0373 0.0088 39 GLN A OE1 318 N NE2 . GLN A 39 ? 0.1954 0.2881 0.1931 -0.0031 0.0044 0.0138 39 GLN A NE2 319 N N . ARG A 40 ? 0.2170 0.2559 0.2153 0.0037 -0.0188 0.0376 40 ARG A N 320 C CA . ARG A 40 ? 0.1579 0.2480 0.2055 -0.0066 0.0211 0.0151 40 ARG A CA 321 C C . ARG A 40 ? 0.1772 0.2328 0.2168 -0.0049 -0.0040 0.0225 40 ARG A C 322 O O . ARG A 40 ? 0.1890 0.2328 0.2655 -0.0180 -0.0060 0.0094 40 ARG A O 323 C CB . ARG A 40 ? 0.1743 0.2677 0.2042 -0.0277 -0.0021 0.0220 40 ARG A CB 324 C CG . ARG A 40 ? 0.1911 0.3083 0.2777 -0.0111 0.0132 -0.0107 40 ARG A CG 325 C CD . ARG A 40 ? 0.2260 0.2837 0.2275 0.0092 -0.0236 0.0353 40 ARG A CD 326 N NE . ARG A 40 ? 0.2082 0.3317 0.1929 -0.0196 -0.0291 0.0282 40 ARG A NE 327 C CZ . ARG A 40 ? 0.1988 0.2740 0.2452 -0.0290 -0.0322 0.0117 40 ARG A CZ 328 N NH1 . ARG A 40 ? 0.1953 0.3256 0.2421 0.0055 -0.0022 0.0257 40 ARG A NH1 329 N NH2 . ARG A 40 ? 0.2649 0.2671 0.2318 -0.0203 -0.0205 0.0275 40 ARG A NH2 330 N N . TRP A 41 ? 0.1679 0.2754 0.2271 -0.0059 0.0006 0.0287 41 TRP A N 331 C CA . TRP A 41 ? 0.2027 0.2634 0.1620 -0.0070 -0.0194 0.0337 41 TRP A CA 332 C C . TRP A 41 ? 0.1969 0.2109 0.2003 -0.0129 0.0002 0.0312 41 TRP A C 333 O O . TRP A 41 ? 0.2190 0.2611 0.1869 -0.0182 -0.0373 0.0218 41 TRP A O 334 C CB . TRP A 41 ? 0.1774 0.2778 0.2078 0.0028 -0.0123 0.0485 41 TRP A CB 335 C CG . TRP A 41 ? 0.2309 0.2418 0.2069 -0.0150 -0.0266 0.0116 41 TRP A CG 336 C CD1 . TRP A 41 ? 0.1501 0.2623 0.1975 0.0139 -0.0108 0.0333 41 TRP A CD1 337 C CD2 . TRP A 41 ? 0.1998 0.2284 0.2348 0.0101 -0.0087 -0.0013 41 TRP A CD2 338 N NE1 . TRP A 41 ? 0.1970 0.2513 0.1894 0.0066 -0.0263 0.0355 41 TRP A NE1 339 C CE2 . TRP A 41 ? 0.1693 0.2484 0.2107 -0.0043 -0.0013 -0.0050 41 TRP A CE2 340 C CE3 . TRP A 41 ? 0.1541 0.2586 0.2058 -0.0297 -0.0163 0.0031 41 TRP A CE3 341 C CZ2 . TRP A 41 ? 0.1770 0.2616 0.2226 0.0145 -0.0237 -0.0064 41 TRP A CZ2 342 C CZ3 . TRP A 41 ? 0.1934 0.2607 0.2002 0.0258 -0.0170 0.0113 41 TRP A CZ3 343 C CH2 . TRP A 41 ? 0.1668 0.2696 0.2087 0.0183 0.0170 0.0195 41 TRP A CH2 344 N N . THR A 42 ? 0.2405 0.2415 0.2160 0.0043 -0.0146 0.0192 42 THR A N 345 C CA . THR A 42 ? 0.2280 0.2164 0.2270 -0.0250 -0.0098 0.0706 42 THR A CA 346 C C . THR A 42 ? 0.2436 0.2419 0.2303 -0.0073 -0.0037 0.0391 42 THR A C 347 O O . THR A 42 ? 0.2558 0.2598 0.2499 -0.0216 -0.0393 0.0324 42 THR A O 348 C CB . THR A 42 ? 0.2461 0.2971 0.2186 -0.0058 -0.0051 0.0687 42 THR A CB 349 O OG1 . THR A 42 ? 0.2149 0.3143 0.2393 -0.0175 0.0063 0.0371 42 THR A OG1 350 C CG2 . THR A 42 ? 0.2725 0.2822 0.2092 -0.0330 -0.0208 0.0449 42 THR A CG2 351 N N . PHE A 43 ? 0.2042 0.3324 0.2177 -0.0129 -0.0063 -0.0034 43 PHE A N 352 C CA . PHE A 43 ? 0.1853 0.2698 0.3077 0.0020 -0.0093 0.0222 43 PHE A CA 353 C C . PHE A 43 ? 0.2731 0.3282 0.2923 -0.0189 0.0157 0.0291 43 PHE A C 354 O O . PHE A 43 ? 0.3316 0.3251 0.2799 -0.0089 -0.0731 0.0593 43 PHE A O 355 C CB . PHE A 43 ? 0.2712 0.2937 0.2947 -0.0301 -0.0083 0.0081 43 PHE A CB 356 C CG . PHE A 43 ? 0.1633 0.3264 0.2643 0.0032 -0.0474 0.0210 43 PHE A CG 357 C CD1 . PHE A 43 ? 0.1934 0.2815 0.2979 -0.0190 -0.0144 0.0073 43 PHE A CD1 358 C CD2 . PHE A 43 ? 0.2631 0.2411 0.2514 0.0122 -0.0369 0.0138 43 PHE A CD2 359 C CE1 . PHE A 43 ? 0.2189 0.2974 0.2796 -0.0363 -0.0371 -0.0136 43 PHE A CE1 360 C CE2 . PHE A 43 ? 0.2235 0.2622 0.2701 -0.0312 -0.0025 0.0036 43 PHE A CE2 361 C CZ . PHE A 43 ? 0.2205 0.2990 0.2883 -0.0140 -0.0299 -0.0241 43 PHE A CZ 362 N N A ASP A 44 ? 0.3580 0.3075 0.2990 -0.0014 -0.0042 0.0313 44 ASP A N 363 N N B ASP A 44 ? 0.4107 0.3815 0.4072 -0.0071 0.0056 -0.0031 44 ASP A N 364 C CA A ASP A 44 ? 0.3062 0.2991 0.2962 0.0295 -0.0104 0.0245 44 ASP A CA 365 C CA B ASP A 44 ? 0.4841 0.4520 0.4721 0.0083 0.0041 0.0249 44 ASP A CA 366 C C A ASP A 44 ? 0.2975 0.2387 0.3065 0.0315 -0.0015 0.0080 44 ASP A C 367 C C B ASP A 44 ? 0.4683 0.4693 0.4731 0.0123 0.0010 0.0170 44 ASP A C 368 O O A ASP A 44 ? 0.2815 0.2877 0.3015 0.0055 -0.0304 0.0208 44 ASP A O 369 O O B ASP A 44 ? 0.4909 0.5021 0.4844 0.0054 0.0078 0.0010 44 ASP A O 370 C CB A ASP A 44 ? 0.3542 0.2992 0.3443 -0.0218 0.0165 0.0330 44 ASP A CB 371 C CB B ASP A 44 ? 0.4467 0.4750 0.4753 0.0019 -0.0024 0.0040 44 ASP A CB 372 C CG A ASP A 44 ? 0.3597 0.3259 0.3276 -0.0040 -0.0099 0.0089 44 ASP A CG 373 C CG B ASP A 44 ? 0.5104 0.4832 0.4813 -0.0019 0.0040 -0.0021 44 ASP A CG 374 O OD1 A ASP A 44 ? 0.3926 0.2935 0.3632 0.0282 0.0317 0.0340 44 ASP A OD1 375 O OD1 B ASP A 44 ? 0.4966 0.4874 0.4899 0.0083 0.0194 -0.0255 44 ASP A OD1 376 O OD2 A ASP A 44 ? 0.3383 0.4456 0.4267 -0.0281 -0.0098 0.0160 44 ASP A OD2 377 O OD2 B ASP A 44 ? 0.4555 0.5170 0.4607 0.0203 0.0227 -0.0050 44 ASP A OD2 378 N N A SER A 45 ? 0.3583 0.3541 0.2879 0.0042 -0.0054 0.0570 45 SER A N 379 N N B SER A 45 ? 0.5077 0.4919 0.4567 0.0115 -0.0078 0.0166 45 SER A N 380 C CA A SER A 45 ? 0.3644 0.3569 0.3286 0.0227 -0.0302 0.0245 45 SER A CA 381 C CA B SER A 45 ? 0.4564 0.4496 0.4093 -0.0032 -0.0057 0.0070 45 SER A CA 382 C C A SER A 45 ? 0.3546 0.3694 0.3561 0.0038 0.0131 0.0191 45 SER A C 383 C C B SER A 45 ? 0.3892 0.4125 0.3956 -0.0027 0.0003 0.0278 45 SER A C 384 O O A SER A 45 ? 0.3186 0.4025 0.4140 0.0079 -0.0121 0.0179 45 SER A O 385 O O B SER A 45 ? 0.4103 0.4196 0.4426 0.0403 -0.0144 0.0212 45 SER A O 386 C CB A SER A 45 ? 0.4598 0.4017 0.3795 -0.0065 -0.0048 0.0406 45 SER A CB 387 C CB B SER A 45 ? 0.4846 0.4626 0.4357 -0.0118 -0.0084 0.0201 45 SER A CB 388 O OG A SER A 45 ? 0.4701 0.4355 0.3972 0.0247 -0.0023 0.0329 45 SER A OG 389 O OG B SER A 45 ? 0.4490 0.4793 0.3997 0.0117 0.0412 0.0111 45 SER A OG 390 N N . ASP A 46 ? 0.3670 0.2827 0.3365 0.0014 0.0001 0.0381 46 ASP A N 391 C CA . ASP A 46 ? 0.3124 0.2670 0.3175 -0.0047 -0.0166 0.0519 46 ASP A CA 392 C C . ASP A 46 ? 0.3098 0.2972 0.2993 0.0252 0.0088 0.0207 46 ASP A C 393 O O . ASP A 46 ? 0.2975 0.3103 0.3194 0.0267 -0.0288 0.0291 46 ASP A O 394 C CB . ASP A 46 ? 0.2721 0.3296 0.3979 -0.0162 0.0024 0.0471 46 ASP A CB 395 C CG . ASP A 46 ? 0.3323 0.3166 0.4047 -0.0068 0.0010 0.0184 46 ASP A CG 396 O OD1 . ASP A 46 ? 0.3334 0.2972 0.3334 0.0133 0.0105 0.0647 46 ASP A OD1 397 O OD2 . ASP A 46 ? 0.3516 0.3759 0.4815 -0.0181 -0.0044 0.0664 46 ASP A OD2 398 N N . ASP A 47 ? 0.2147 0.2916 0.2841 0.0029 -0.0190 0.0608 47 ASP A N 399 C CA . ASP A 47 ? 0.2512 0.3203 0.2788 0.0040 -0.0007 0.0497 47 ASP A CA 400 C C . ASP A 47 ? 0.2283 0.3167 0.2734 0.0034 -0.0184 0.0356 47 ASP A C 401 O O . ASP A 47 ? 0.2170 0.3644 0.2699 -0.0275 -0.0220 0.0710 47 ASP A O 402 C CB . ASP A 47 ? 0.2822 0.3747 0.3425 0.0113 0.0237 0.0180 47 ASP A CB 403 C CG . ASP A 47 ? 0.4329 0.5645 0.5071 0.0144 -0.0329 -0.0213 47 ASP A CG 404 O OD1 . ASP A 47 ? 0.3538 0.5886 0.4494 -0.0027 -0.0061 -0.0322 47 ASP A OD1 405 O OD2 . ASP A 47 ? 0.5765 0.5874 0.5687 0.0292 0.0106 0.0499 47 ASP A OD2 406 N N . THR A 48 ? 0.2015 0.2927 0.2952 0.0052 -0.0211 0.0182 48 THR A N 407 C CA . THR A 48 ? 0.2106 0.2579 0.3002 -0.0104 -0.0384 0.0513 48 THR A CA 408 C C . THR A 48 ? 0.2576 0.2903 0.2466 0.0011 -0.0289 0.0197 48 THR A C 409 O O . THR A 48 ? 0.2258 0.2739 0.2471 0.0217 -0.0354 0.0008 48 THR A O 410 C CB . THR A 48 ? 0.2620 0.2560 0.2405 -0.0207 -0.0194 0.0130 48 THR A CB 411 O OG1 . THR A 48 ? 0.2437 0.3336 0.2786 0.0087 -0.0251 0.0570 48 THR A OG1 412 C CG2 . THR A 48 ? 0.2636 0.2747 0.2930 0.0034 -0.0118 -0.0362 48 THR A CG2 413 N N . ILE A 49 ? 0.1984 0.2356 0.2829 -0.0164 -0.0087 0.0289 49 ILE A N 414 C CA . ILE A 49 ? 0.1860 0.2741 0.2692 0.0112 -0.0063 0.0158 49 ILE A CA 415 C C . ILE A 49 ? 0.1824 0.2689 0.2363 -0.0097 -0.0066 -0.0020 49 ILE A C 416 O O . ILE A 49 ? 0.2140 0.2706 0.2487 -0.0335 -0.0406 0.0167 49 ILE A O 417 C CB . ILE A 49 ? 0.1716 0.2189 0.2215 0.0333 -0.0220 0.0201 49 ILE A CB 418 C CG1 . ILE A 49 ? 0.1800 0.2773 0.2843 0.0163 -0.0332 0.0540 49 ILE A CG1 419 C CG2 . ILE A 49 ? 0.1948 0.2539 0.2421 0.0180 -0.0084 -0.0130 49 ILE A CG2 420 C CD1 . ILE A 49 ? 0.2172 0.2452 0.2873 -0.0443 -0.0355 0.0150 49 ILE A CD1 421 N N . ARG A 50 ? 0.1533 0.2554 0.2405 -0.0155 -0.0143 0.0153 50 ARG A N 422 C CA . ARG A 50 ? 0.1610 0.2331 0.2832 -0.0202 -0.0160 0.0144 50 ARG A CA 423 C C . ARG A 50 ? 0.2503 0.2456 0.2711 0.0041 -0.0259 -0.0001 50 ARG A C 424 O O . ARG A 50 ? 0.2210 0.2775 0.2513 -0.0109 -0.0346 0.0312 50 ARG A O 425 C CB . ARG A 50 ? 0.3067 0.2393 0.3033 -0.0161 0.0055 0.0534 50 ARG A CB 426 C CG . ARG A 50 ? 0.2807 0.2880 0.3656 -0.0206 0.0052 0.0460 50 ARG A CG 427 C CD . ARG A 50 ? 0.3111 0.2506 0.3509 -0.0295 0.0248 0.0374 50 ARG A CD 428 N NE . ARG A 50 ? 0.3545 0.2434 0.3189 -0.0103 0.0005 0.0043 50 ARG A NE 429 C CZ . ARG A 50 ? 0.2484 0.2947 0.3174 -0.0131 -0.0192 0.0148 50 ARG A CZ 430 N NH1 . ARG A 50 ? 0.3279 0.3461 0.3702 0.0114 -0.0064 0.0344 50 ARG A NH1 431 N NH2 . ARG A 50 ? 0.2302 0.3691 0.3236 -0.0198 -0.0193 0.0686 50 ARG A NH2 432 N N . SER A 51 ? 0.2118 0.2748 0.2616 0.0218 -0.0421 0.0144 51 SER A N 433 C CA . SER A 51 ? 0.1730 0.2335 0.2815 -0.0148 -0.0172 0.0237 51 SER A CA 434 C C . SER A 51 ? 0.2111 0.2906 0.2586 -0.0143 -0.0208 -0.0326 51 SER A C 435 O O . SER A 51 ? 0.2275 0.3310 0.2351 -0.0295 -0.0297 0.0030 51 SER A O 436 C CB . SER A 51 ? 0.2536 0.2036 0.2507 -0.0071 -0.0075 0.0021 51 SER A CB 437 O OG . SER A 51 ? 0.2172 0.2718 0.2409 -0.0051 0.0092 0.0064 51 SER A OG 438 N N . MET A 52 ? 0.1587 0.3012 0.2904 -0.0053 -0.0190 0.0119 52 MET A N 439 C CA . MET A 52 ? 0.1900 0.3088 0.3144 -0.0325 -0.0168 0.0424 52 MET A CA 440 C C . MET A 52 ? 0.2393 0.3093 0.2968 -0.0296 0.0091 0.0134 52 MET A C 441 O O . MET A 52 ? 0.2629 0.3555 0.3899 -0.0108 -0.0136 -0.0040 52 MET A O 442 C CB . MET A 52 ? 0.2113 0.2511 0.3070 -0.0226 -0.0254 0.0282 52 MET A CB 443 C CG . MET A 52 ? 0.2487 0.2860 0.2650 -0.0224 0.0052 0.0184 52 MET A CG 444 S SD . MET A 52 ? 0.2281 0.3567 0.2999 -0.0216 -0.0157 0.0260 52 MET A SD 445 C CE . MET A 52 ? 0.3090 0.3224 0.2748 -0.0350 0.0110 -0.0219 52 MET A CE 446 N N . GLY A 53 ? 0.2556 0.2926 0.3099 -0.0125 0.0111 0.0227 53 GLY A N 447 C CA . GLY A 53 ? 0.2993 0.2937 0.2562 -0.0171 0.0344 0.0178 53 GLY A CA 448 C C . GLY A 53 ? 0.2371 0.2434 0.2773 -0.0104 -0.0036 -0.0041 53 GLY A C 449 O O . GLY A 53 ? 0.3582 0.2660 0.3137 -0.0308 0.0078 0.0019 53 GLY A O 450 N N . LYS A 54 ? 0.2227 0.3060 0.2465 -0.0199 0.0059 0.0283 54 LYS A N 451 C CA . LYS A 54 ? 0.2276 0.3062 0.2640 -0.0191 -0.0190 -0.0063 54 LYS A CA 452 C C . LYS A 54 ? 0.2387 0.3170 0.2896 0.0000 -0.0184 -0.0027 54 LYS A C 453 O O . LYS A 54 ? 0.2123 0.3030 0.3641 -0.0232 -0.0113 -0.0219 54 LYS A O 454 C CB . LYS A 54 ? 0.1741 0.3205 0.3057 -0.0466 -0.0405 -0.0004 54 LYS A CB 455 C CG . LYS A 54 ? 0.2062 0.3629 0.2744 -0.0215 -0.0021 -0.0039 54 LYS A CG 456 C CD . LYS A 54 ? 0.1910 0.3728 0.3251 -0.0426 -0.0263 0.0192 54 LYS A CD 457 C CE . LYS A 54 ? 0.2469 0.3479 0.3438 -0.0574 -0.0264 0.0093 54 LYS A CE 458 N NZ . LYS A 54 ? 0.2760 0.3618 0.3002 -0.0184 -0.0340 0.0458 54 LYS A NZ 459 N N . CYS A 55 ? 0.1677 0.2376 0.2692 -0.0079 -0.0041 0.0299 55 CYS A N 460 C CA . CYS A 55 ? 0.1774 0.2559 0.2980 -0.0109 -0.0035 0.0344 55 CYS A CA 461 C C . CYS A 55 ? 0.2468 0.2874 0.2355 -0.0009 0.0115 0.0191 55 CYS A C 462 O O . CYS A 55 ? 0.1871 0.2763 0.2481 -0.0343 -0.0530 0.0304 55 CYS A O 463 C CB . CYS A 55 ? 0.1940 0.2744 0.2608 0.0215 -0.0275 0.0034 55 CYS A CB 464 S SG . CYS A 55 ? 0.2556 0.3035 0.3081 -0.0039 -0.0434 0.0406 55 CYS A SG 465 N N . MET A 56 ? 0.2050 0.2714 0.2541 -0.0066 -0.0049 0.0412 56 MET A N 466 C CA . MET A 56 ? 0.2146 0.2497 0.2437 -0.0087 -0.0235 0.0205 56 MET A CA 467 C C . MET A 56 ? 0.2210 0.2329 0.2183 -0.0365 -0.0077 0.0077 56 MET A C 468 O O . MET A 56 ? 0.2365 0.2995 0.2522 0.0166 -0.0281 0.0141 56 MET A O 469 C CB . MET A 56 ? 0.1707 0.2614 0.2438 -0.0311 -0.0417 0.0219 56 MET A CB 470 C CG . MET A 56 ? 0.1731 0.2728 0.2760 -0.0610 -0.0255 0.0137 56 MET A CG 471 S SD . MET A 56 ? 0.2037 0.2866 0.2712 -0.0035 -0.0251 0.0260 56 MET A SD 472 C CE . MET A 56 ? 0.2544 0.2843 0.2714 0.0156 0.0136 -0.0212 56 MET A CE 473 N N . THR A 57 ? 0.2309 0.2709 0.2334 -0.0214 -0.0331 0.0209 57 THR A N 474 C CA . THR A 57 ? 0.1834 0.2896 0.2631 -0.0082 -0.0626 0.0037 57 THR A CA 475 C C . THR A 57 ? 0.2186 0.2766 0.2511 0.0049 -0.0241 -0.0006 57 THR A C 476 O O . THR A 57 ? 0.2159 0.2750 0.2542 0.0532 -0.0250 0.0090 57 THR A O 477 C CB . THR A 57 ? 0.2282 0.2364 0.2504 -0.0526 -0.0312 -0.0092 57 THR A CB 478 O OG1 . THR A 57 ? 0.2305 0.2836 0.2540 -0.0072 -0.0309 0.0178 57 THR A OG1 479 C CG2 . THR A 57 ? 0.2585 0.2557 0.2740 -0.0494 -0.0079 -0.0295 57 THR A CG2 480 N N . ALA A 58 ? 0.2380 0.3065 0.1943 -0.0287 -0.0008 -0.0094 58 ALA A N 481 C CA . ALA A 58 ? 0.2473 0.2772 0.2111 -0.0257 -0.0179 -0.0075 58 ALA A CA 482 C C . ALA A 58 ? 0.2525 0.2950 0.2483 -0.0102 -0.0297 0.0006 58 ALA A C 483 O O . ALA A 58 ? 0.3059 0.3128 0.3137 -0.0229 -0.0350 0.0091 58 ALA A O 484 C CB . ALA A 58 ? 0.2579 0.3057 0.2263 -0.0292 0.0014 0.0267 58 ALA A CB 485 N N . ASN A 59 ? 0.3487 0.3302 0.3368 -0.0228 -0.0957 -0.0078 59 ASN A N 486 C CA . ASN A 59 ? 0.3362 0.3702 0.3516 0.0191 -0.0553 -0.0290 59 ASN A CA 487 C C . ASN A 59 ? 0.3748 0.4003 0.4083 -0.0474 -0.0172 -0.0090 59 ASN A C 488 O O . ASN A 59 ? 0.3943 0.4472 0.4023 0.0023 -0.0139 0.0110 59 ASN A O 489 C CB . ASN A 59 ? 0.2327 0.3727 0.3366 0.0220 -0.0420 -0.0309 59 ASN A CB 490 C CG . ASN A 59 ? 0.2928 0.3343 0.3855 -0.0314 -0.0064 0.0033 59 ASN A CG 491 O OD1 . ASN A 59 ? 0.3584 0.3729 0.3527 0.0157 -0.0440 -0.0060 59 ASN A OD1 492 N ND2 . ASN A 59 ? 0.3121 0.4395 0.3519 0.0053 -0.0120 0.0223 59 ASN A ND2 493 N N . GLY A 60 ? 0.4223 0.4329 0.4012 0.0119 -0.0073 0.0018 60 GLY A N 494 C CA . GLY A 60 ? 0.4232 0.4837 0.4330 0.0167 -0.0043 -0.0068 60 GLY A CA 495 C C . GLY A 60 ? 0.4425 0.3845 0.3992 0.0031 0.0010 -0.0117 60 GLY A C 496 O O . GLY A 60 ? 0.3293 0.4341 0.3583 0.0579 0.0025 -0.0116 60 GLY A O 497 N N . LEU A 61 ? 0.4024 0.3971 0.3972 0.0115 -0.0180 0.0071 61 LEU A N 498 C CA . LEU A 61 ? 0.3895 0.4328 0.4725 -0.0322 -0.0166 0.0370 61 LEU A CA 499 C C . LEU A 61 ? 0.4088 0.4272 0.3842 0.0170 0.0132 0.0027 61 LEU A C 500 O O . LEU A 61 ? 0.3928 0.4441 0.4567 0.0692 -0.0184 -0.0530 61 LEU A O 501 C CB . LEU A 61 ? 0.4187 0.4587 0.4454 -0.0021 -0.0175 0.0163 61 LEU A CB 502 C CG . LEU A 61 ? 0.5264 0.5034 0.4496 -0.0154 -0.0010 -0.0047 61 LEU A CG 503 C CD1 . LEU A 61 ? 0.5834 0.5337 0.5815 0.0215 -0.0070 0.0014 61 LEU A CD1 504 C CD2 . LEU A 61 ? 0.2447 0.4235 0.3954 -0.0231 -0.0290 -0.0138 61 LEU A CD2 505 N N . ASN A 62 ? 0.4443 0.4297 0.4261 0.0124 -0.0481 0.0122 62 ASN A N 506 C CA . ASN A 62 ? 0.3570 0.4472 0.4000 0.0327 -0.0400 -0.0052 62 ASN A CA 507 C C . ASN A 62 ? 0.3878 0.4560 0.3820 0.0041 -0.0410 -0.0084 62 ASN A C 508 O O . ASN A 62 ? 0.2890 0.4079 0.4572 0.0545 -0.0432 0.0085 62 ASN A O 509 C CB . ASN A 62 ? 0.4985 0.4868 0.4258 0.0315 -0.0474 -0.0053 62 ASN A CB 510 C CG . ASN A 62 ? 0.6943 0.5799 0.6332 -0.0004 0.0019 -0.0383 62 ASN A CG 511 O OD1 . ASN A 62 ? 0.7188 0.6336 0.6802 -0.0125 -0.0022 -0.0150 62 ASN A OD1 512 N ND2 . ASN A 62 ? 0.7017 0.6975 0.7000 0.0151 0.0335 -0.0044 62 ASN A ND2 513 N N . ASN A 63 ? 0.3379 0.3780 0.3217 0.0601 -0.0336 -0.0246 63 ASN A N 514 C CA . ASN A 63 ? 0.2890 0.4254 0.3351 0.0083 -0.0426 -0.0006 63 ASN A CA 515 C C . ASN A 63 ? 0.3433 0.3725 0.3310 0.0497 -0.0093 -0.0304 63 ASN A C 516 O O . ASN A 63 ? 0.2652 0.4189 0.3365 0.0854 0.0165 -0.0638 63 ASN A O 517 C CB . ASN A 63 ? 0.2956 0.4368 0.2672 0.0018 -0.0105 -0.0402 63 ASN A CB 518 C CG . ASN A 63 ? 0.3388 0.4407 0.3294 0.0217 0.0025 0.0079 63 ASN A CG 519 O OD1 . ASN A 63 ? 0.2675 0.4685 0.3175 -0.0031 0.0141 -0.0205 63 ASN A OD1 520 N ND2 . ASN A 63 ? 0.3412 0.4698 0.2774 0.0043 -0.0004 -0.0183 63 ASN A ND2 521 N N . GLY A 64 ? 0.2101 0.3397 0.2626 0.0621 -0.0308 -0.0313 64 GLY A N 522 C CA . GLY A 64 ? 0.2330 0.3273 0.2688 0.0535 -0.0033 0.0156 64 GLY A CA 523 C C . GLY A 64 ? 0.2734 0.2934 0.2308 0.0222 0.0012 -0.0449 64 GLY A C 524 O O . GLY A 64 ? 0.2525 0.3356 0.2722 0.0601 -0.0339 -0.0411 64 GLY A O 525 N N . SER A 65 ? 0.2788 0.3296 0.2272 0.0293 -0.0140 -0.0157 65 SER A N 526 C CA . SER A 65 ? 0.2763 0.2700 0.2253 0.0152 -0.0054 -0.0196 65 SER A CA 527 C C . SER A 65 ? 0.2021 0.2823 0.2223 -0.0127 0.0158 -0.0204 65 SER A C 528 O O . SER A 65 ? 0.2281 0.2988 0.2879 0.0250 -0.0499 -0.0645 65 SER A O 529 C CB . SER A 65 ? 0.3744 0.2705 0.2661 0.0144 -0.0166 -0.0206 65 SER A CB 530 O OG . SER A 65 ? 0.3568 0.3327 0.3481 0.0440 -0.0462 -0.0483 65 SER A OG 531 N N . ASN A 66 ? 0.2011 0.3167 0.2476 0.0013 -0.0133 -0.0003 66 ASN A N 532 C CA . ASN A 66 ? 0.1776 0.3063 0.1915 -0.0058 -0.0373 0.0105 66 ASN A CA 533 C C . ASN A 66 ? 0.2396 0.2450 0.2130 -0.0078 -0.0045 0.0244 66 ASN A C 534 O O . ASN A 66 ? 0.3411 0.2914 0.2147 -0.0333 -0.0452 -0.0096 66 ASN A O 535 C CB . ASN A 66 ? 0.2099 0.2764 0.2743 -0.0218 -0.0655 0.0264 66 ASN A CB 536 C CG . ASN A 66 ? 0.2200 0.3197 0.3063 0.0405 -0.0395 0.0154 66 ASN A CG 537 O OD1 . ASN A 66 ? 0.3008 0.3540 0.3162 0.0462 -0.0331 -0.0586 66 ASN A OD1 538 N ND2 . ASN A 66 ? 0.2146 0.3207 0.2721 0.0120 -0.0192 0.0291 66 ASN A ND2 539 N N . ILE A 67 ? 0.2294 0.2458 0.2194 -0.0239 0.0000 -0.0028 67 ILE A N 540 C CA . ILE A 67 ? 0.1618 0.3010 0.2002 -0.0257 0.0065 -0.0019 67 ILE A CA 541 C C . ILE A 67 ? 0.2084 0.2191 0.2360 0.0032 0.0141 0.0123 67 ILE A C 542 O O . ILE A 67 ? 0.1778 0.2573 0.2174 0.0251 -0.0024 0.0108 67 ILE A O 543 C CB . ILE A 67 ? 0.2172 0.2362 0.2168 0.0031 0.0110 -0.0143 67 ILE A CB 544 C CG1 . ILE A 67 ? 0.1549 0.2621 0.2594 -0.0074 -0.0006 0.0135 67 ILE A CG1 545 C CG2 . ILE A 67 ? 0.2203 0.2597 0.1997 0.0261 0.0163 0.0124 67 ILE A CG2 546 C CD1 . ILE A 67 ? 0.2308 0.3116 0.2744 -0.0315 -0.0205 -0.0287 67 ILE A CD1 547 N N . VAL A 68 ? 0.1772 0.2646 0.2143 0.0080 -0.0162 0.0067 68 VAL A N 548 C CA . VAL A 68 ? 0.1522 0.3000 0.2055 -0.0210 -0.0401 0.0093 68 VAL A CA 549 C C . VAL A 68 ? 0.2077 0.2422 0.2413 -0.0127 0.0082 0.0137 68 VAL A C 550 O O . VAL A 68 ? 0.1845 0.2941 0.2520 -0.0107 -0.0225 0.0371 68 VAL A O 551 C CB . VAL A 68 ? 0.2048 0.2609 0.2207 -0.0283 -0.0025 0.0297 68 VAL A CB 552 C CG1 . VAL A 68 ? 0.2194 0.2854 0.1986 -0.0123 -0.0014 0.0293 68 VAL A CG1 553 C CG2 . VAL A 68 ? 0.2450 0.2604 0.3017 0.0328 -0.0444 -0.0122 68 VAL A CG2 554 N N . ILE A 69 ? 0.1913 0.2746 0.2158 -0.0167 -0.0075 0.0073 69 ILE A N 555 C CA . ILE A 69 ? 0.2248 0.2549 0.2260 -0.0110 -0.0137 -0.0138 69 ILE A CA 556 C C . ILE A 69 ? 0.2210 0.2362 0.2737 -0.0013 0.0125 0.0043 69 ILE A C 557 O O . ILE A 69 ? 0.2084 0.3098 0.2641 -0.0314 -0.0247 0.0377 69 ILE A O 558 C CB . ILE A 69 ? 0.2781 0.3279 0.2233 -0.0166 0.0429 -0.0303 69 ILE A CB 559 C CG1 . ILE A 69 ? 0.2729 0.3402 0.3268 -0.0264 -0.0555 0.0498 69 ILE A CG1 560 C CG2 . ILE A 69 ? 0.2813 0.2957 0.3593 -0.0098 0.0014 0.0141 69 ILE A CG2 561 C CD1 . ILE A 69 ? 0.2288 0.3076 0.4350 -0.0653 -0.0439 -0.0195 69 ILE A CD1 562 N N . PHE A 70 ? 0.2169 0.2752 0.2570 -0.0140 -0.0434 -0.0028 70 PHE A N 563 C CA . PHE A 70 ? 0.2725 0.2570 0.2177 -0.0087 -0.0057 -0.0020 70 PHE A CA 564 C C . PHE A 70 ? 0.3092 0.2917 0.2914 -0.0273 -0.0056 0.0321 70 PHE A C 565 O O . PHE A 70 ? 0.2678 0.2757 0.2645 -0.0256 -0.0125 0.0455 70 PHE A O 566 C CB . PHE A 70 ? 0.2878 0.3177 0.2364 0.0033 -0.0267 -0.0265 70 PHE A CB 567 C CG . PHE A 70 ? 0.2756 0.2792 0.2805 -0.0296 0.0042 -0.0093 70 PHE A CG 568 C CD1 . PHE A 70 ? 0.2877 0.3521 0.2589 -0.0546 -0.0078 0.0121 70 PHE A CD1 569 C CD2 . PHE A 70 ? 0.3070 0.3204 0.3158 -0.0192 -0.0142 -0.0085 70 PHE A CD2 570 C CE1 . PHE A 70 ? 0.3402 0.3801 0.3844 -0.0118 -0.0257 -0.0324 70 PHE A CE1 571 C CE2 . PHE A 70 ? 0.3342 0.3534 0.3284 -0.0229 -0.0186 0.0058 70 PHE A CE2 572 C CZ . PHE A 70 ? 0.3246 0.3727 0.3235 -0.0416 -0.0388 -0.0043 70 PHE A CZ 573 N N . ASN A 71 ? 0.2584 0.2795 0.2721 0.0000 -0.0007 0.0267 71 ASN A N 574 C CA . ASN A 71 ? 0.2110 0.2373 0.3334 -0.0625 0.0038 0.0150 71 ASN A CA 575 C C . ASN A 71 ? 0.2977 0.2837 0.2989 -0.0152 -0.0220 0.0129 71 ASN A C 576 O O . ASN A 71 ? 0.2441 0.3001 0.3333 -0.0302 -0.0543 0.0018 71 ASN A O 577 C CB . ASN A 71 ? 0.2708 0.2452 0.3658 -0.0566 -0.0036 0.0041 71 ASN A CB 578 C CG . ASN A 71 ? 0.3777 0.3474 0.4091 -0.0267 -0.0076 0.0080 71 ASN A CG 579 O OD1 . ASN A 71 ? 0.3072 0.3117 0.4078 -0.0346 0.0026 0.0236 71 ASN A OD1 580 N ND2 . ASN A 71 ? 0.3075 0.3079 0.4136 -0.0677 0.0144 0.0014 71 ASN A ND2 581 N N . CYS A 72 ? 0.2756 0.2796 0.2992 -0.0055 -0.0247 0.0453 72 CYS A N 582 C CA . CYS A 72 ? 0.2824 0.2456 0.3001 -0.0060 -0.0178 0.0007 72 CYS A CA 583 C C . CYS A 72 ? 0.3520 0.2902 0.3855 -0.0118 -0.0050 -0.0058 72 CYS A C 584 O O . CYS A 72 ? 0.3253 0.3194 0.4366 -0.0351 -0.0104 0.0000 72 CYS A O 585 C CB . CYS A 72 ? 0.3667 0.3149 0.3025 0.0172 -0.0181 -0.0077 72 CYS A CB 586 S SG . CYS A 72 ? 0.2949 0.3142 0.3194 -0.0407 -0.0265 0.0285 72 CYS A SG 587 N N A SER A 73 ? 0.3029 0.2993 0.3761 -0.0028 -0.0279 -0.0017 73 SER A N 588 N N B SER A 73 ? 0.2941 0.2837 0.3661 0.0009 -0.0290 -0.0029 73 SER A N 589 C CA A SER A 73 ? 0.3202 0.3074 0.3940 -0.0092 0.0055 -0.0053 73 SER A CA 590 C CA B SER A 73 ? 0.3113 0.2927 0.3815 -0.0126 0.0060 -0.0034 73 SER A CA 591 C C A SER A 73 ? 0.3537 0.3540 0.3935 -0.0046 0.0075 0.0044 73 SER A C 592 C C B SER A 73 ? 0.3383 0.3302 0.3858 -0.0121 0.0079 0.0021 73 SER A C 593 O O A SER A 73 ? 0.4181 0.3907 0.4955 0.0074 0.0094 -0.0052 73 SER A O 594 O O B SER A 73 ? 0.3636 0.3750 0.4619 0.0036 0.0154 -0.0004 73 SER A O 595 C CB A SER A 73 ? 0.3968 0.3782 0.3890 -0.0147 0.0186 0.0061 73 SER A CB 596 C CB B SER A 73 ? 0.3585 0.3487 0.3781 -0.0128 0.0212 0.0096 73 SER A CB 597 O OG A SER A 73 ? 0.4011 0.3897 0.4165 -0.0385 0.0020 0.0452 73 SER A OG 598 O OG B SER A 73 ? 0.3859 0.4075 0.3679 -0.0209 -0.0237 0.0208 73 SER A OG 599 N N . THR A 74 ? 0.2824 0.2744 0.3851 -0.0319 0.0097 -0.0203 74 THR A N 600 C CA . THR A 74 ? 0.3363 0.3697 0.3720 -0.0217 0.0054 -0.0072 74 THR A CA 601 C C . THR A 74 ? 0.3844 0.3615 0.4164 -0.0371 0.0107 -0.0269 74 THR A C 602 O O . THR A 74 ? 0.3939 0.3482 0.3919 -0.0646 -0.0147 -0.0475 74 THR A O 603 C CB . THR A 74 ? 0.3309 0.3732 0.3772 -0.0111 -0.0047 0.0092 74 THR A CB 604 O OG1 . THR A 74 ? 0.3441 0.3893 0.4109 -0.0144 -0.0233 -0.0115 74 THR A OG1 605 C CG2 . THR A 74 ? 0.3794 0.4308 0.4799 -0.0186 0.0552 0.0102 74 THR A CG2 606 N N . ALA A 75 ? 0.2764 0.3168 0.3727 -0.0413 -0.0203 0.0082 75 ALA A N 607 C CA . ALA A 75 ? 0.3058 0.2998 0.3685 -0.0298 -0.0215 -0.0072 75 ALA A CA 608 C C . ALA A 75 ? 0.3190 0.3733 0.3697 -0.0150 0.0053 -0.0255 75 ALA A C 609 O O . ALA A 75 ? 0.2854 0.3600 0.4365 -0.0280 0.0427 0.0198 75 ALA A O 610 C CB . ALA A 75 ? 0.3165 0.2998 0.4111 -0.0435 -0.0306 -0.0102 75 ALA A CB 611 N N . ALA A 76 ? 0.3086 0.3432 0.3422 -0.0481 -0.0314 -0.0248 76 ALA A N 612 C CA . ALA A 76 ? 0.3306 0.3387 0.3630 0.0032 0.0042 -0.0329 76 ALA A CA 613 C C . ALA A 76 ? 0.3340 0.3375 0.3618 0.0062 0.0032 0.0072 76 ALA A C 614 O O . ALA A 76 ? 0.2972 0.3255 0.3477 0.0053 0.0077 0.0191 76 ALA A O 615 C CB . ALA A 76 ? 0.3558 0.4061 0.3892 -0.0206 -0.0034 -0.0002 76 ALA A CB 616 N N . GLU A 77 ? 0.3162 0.3183 0.3860 -0.0230 -0.0068 -0.0058 77 GLU A N 617 C CA . GLU A 77 ? 0.2864 0.3218 0.3771 0.0051 -0.0055 0.0236 77 GLU A CA 618 C C . GLU A 77 ? 0.2524 0.2946 0.3681 -0.0028 -0.0275 0.0140 77 GLU A C 619 O O . GLU A 77 ? 0.3607 0.4029 0.3718 0.0579 -0.0520 -0.0528 77 GLU A O 620 C CB . GLU A 77 ? 0.3696 0.3399 0.4717 0.0108 -0.0088 0.0397 77 GLU A CB 621 N N . ASN A 78 ? 0.3335 0.3187 0.3614 0.0177 0.0220 0.0044 78 ASN A N 622 C CA . ASN A 78 ? 0.3440 0.2905 0.3711 0.0103 -0.0199 -0.0077 78 ASN A CA 623 C C . ASN A 78 ? 0.3052 0.3077 0.3881 0.0036 0.0186 -0.0005 78 ASN A C 624 O O . ASN A 78 ? 0.2332 0.3217 0.4184 0.0231 -0.0189 -0.0373 78 ASN A O 625 C CB . ASN A 78 ? 0.4068 0.3430 0.4382 0.0140 0.0689 -0.0151 78 ASN A CB 626 C CG . ASN A 78 ? 0.4786 0.4474 0.5108 0.0340 -0.0151 0.0155 78 ASN A CG 627 O OD1 . ASN A 78 ? 0.5707 0.6103 0.5719 0.0035 0.0329 -0.0279 78 ASN A OD1 628 N ND2 . ASN A 78 ? 0.4421 0.3874 0.4855 -0.0161 0.0024 0.0179 78 ASN A ND2 629 N N . ALA A 79 ? 0.2761 0.2451 0.3456 0.0136 -0.0240 -0.0352 79 ALA A N 630 C CA . ALA A 79 ? 0.2707 0.2780 0.2859 0.0062 -0.0242 -0.0071 79 ALA A CA 631 C C . ALA A 79 ? 0.2374 0.2340 0.2426 -0.0227 -0.0168 0.0081 79 ALA A C 632 O O . ALA A 79 ? 0.2343 0.2548 0.2718 -0.0200 -0.0278 0.0171 79 ALA A O 633 C CB . ALA A 79 ? 0.2257 0.3695 0.2965 -0.0383 -0.0295 -0.0269 79 ALA A CB 634 N N . ILE A 80 ? 0.2590 0.2548 0.2526 -0.0185 0.0140 0.0102 80 ILE A N 635 C CA . ILE A 80 ? 0.2060 0.2964 0.2792 -0.0184 0.0036 0.0019 80 ILE A CA 636 C C . ILE A 80 ? 0.2827 0.2965 0.2751 -0.0115 -0.0195 0.0080 80 ILE A C 637 O O . ILE A 80 ? 0.2538 0.2814 0.2721 -0.0013 -0.0568 0.0279 80 ILE A O 638 C CB . ILE A 80 ? 0.2024 0.2691 0.3119 0.0025 -0.0101 0.0419 80 ILE A CB 639 C CG1 . ILE A 80 ? 0.2152 0.2780 0.3121 -0.0180 0.0045 0.0263 80 ILE A CG1 640 C CG2 . ILE A 80 ? 0.2561 0.4109 0.2758 0.0041 -0.0291 -0.0393 80 ILE A CG2 641 C CD1 . ILE A 80 ? 0.2515 0.2855 0.2784 -0.0164 0.0087 0.0620 80 ILE A CD1 642 N N . LYS A 81 ? 0.2279 0.2520 0.2937 -0.0231 -0.0521 0.0091 81 LYS A N 643 C CA . LYS A 81 ? 0.2202 0.2533 0.3052 -0.0037 -0.0366 -0.0042 81 LYS A CA 644 C C . LYS A 81 ? 0.2438 0.2754 0.2695 -0.0183 -0.0251 -0.0077 81 LYS A C 645 O O . LYS A 81 ? 0.2247 0.3211 0.3105 -0.0204 -0.0201 0.0162 81 LYS A O 646 C CB . LYS A 81 ? 0.2707 0.2961 0.3697 0.0109 -0.0407 0.0295 81 LYS A CB 647 C CG . LYS A 81 ? 0.4221 0.2912 0.4520 -0.0242 -0.0203 0.0353 81 LYS A CG 648 C CD . LYS A 81 ? 0.4075 0.4665 0.5833 0.0232 0.0066 0.0037 81 LYS A CD 649 C CE . LYS A 81 ? 0.6476 0.5836 0.6275 -0.0292 0.0061 0.0403 81 LYS A CE 650 N NZ . LYS A 81 ? 0.7351 0.6212 0.6783 -0.0024 0.0007 -0.0037 81 LYS A NZ 651 N N . TRP A 82 ? 0.2188 0.2187 0.2539 -0.0065 -0.0167 0.0061 82 TRP A N 652 C CA . TRP A 82 ? 0.2214 0.2252 0.2902 0.0031 -0.0586 0.0086 82 TRP A CA 653 C C . TRP A 82 ? 0.2616 0.3417 0.2889 0.0095 -0.0350 0.0198 82 TRP A C 654 O O . TRP A 82 ? 0.2555 0.4094 0.2728 -0.0507 -0.0762 0.0724 82 TRP A O 655 C CB . TRP A 82 ? 0.1833 0.2517 0.2860 0.0089 -0.0504 0.0043 82 TRP A CB 656 C CG . TRP A 82 ? 0.1767 0.2371 0.2680 -0.0259 -0.0524 0.0122 82 TRP A CG 657 C CD1 . TRP A 82 ? 0.1616 0.2618 0.2805 -0.0084 -0.0114 0.0330 82 TRP A CD1 658 C CD2 . TRP A 82 ? 0.1590 0.2772 0.2630 0.0085 -0.0346 0.0247 82 TRP A CD2 659 N NE1 . TRP A 82 ? 0.2303 0.2907 0.2968 -0.0084 -0.0306 0.0330 82 TRP A NE1 660 C CE2 . TRP A 82 ? 0.1757 0.2636 0.2889 -0.0041 -0.0282 0.0215 82 TRP A CE2 661 C CE3 . TRP A 82 ? 0.2571 0.2610 0.2767 0.0197 0.0124 0.0243 82 TRP A CE3 662 C CZ2 . TRP A 82 ? 0.1853 0.2804 0.2854 0.0005 -0.0074 0.0187 82 TRP A CZ2 663 C CZ3 . TRP A 82 ? 0.1901 0.2673 0.2660 -0.0203 -0.0316 -0.0002 82 TRP A CZ3 664 C CH2 . TRP A 82 ? 0.2000 0.2823 0.2384 -0.0185 -0.0142 -0.0012 82 TRP A CH2 665 N N . GLU A 83 ? 0.2318 0.2359 0.2567 0.0005 -0.0310 0.0282 83 GLU A N 666 C CA . GLU A 83 ? 0.2061 0.2393 0.2798 -0.0080 0.0118 -0.0039 83 GLU A CA 667 C C . GLU A 83 ? 0.2392 0.2202 0.2303 0.0067 0.0079 0.0094 83 GLU A C 668 O O . GLU A 83 ? 0.1828 0.2891 0.2608 -0.0010 -0.0211 0.0411 83 GLU A O 669 C CB . GLU A 83 ? 0.2118 0.2945 0.3104 0.0315 0.0226 0.0014 83 GLU A CB 670 C CG . GLU A 83 ? 0.3789 0.4084 0.3225 0.0254 -0.0102 0.0072 83 GLU A CG 671 C CD . GLU A 83 ? 0.3747 0.4639 0.3324 0.0023 0.0121 0.0033 83 GLU A CD 672 O OE1 . GLU A 83 ? 0.2989 0.4319 0.4412 -0.0368 -0.0383 0.0562 83 GLU A OE1 673 O OE2 . GLU A 83 ? 0.3609 0.4432 0.4614 0.0406 0.0107 0.0470 83 GLU A OE2 674 N N . VAL A 84 ? 0.1955 0.2281 0.2813 -0.0101 0.0152 -0.0257 84 VAL A N 675 C CA . VAL A 84 ? 0.1901 0.2273 0.2510 -0.0052 0.0107 -0.0302 84 VAL A CA 676 C C . VAL A 84 ? 0.1993 0.2449 0.2150 0.0105 0.0125 0.0071 84 VAL A C 677 O O . VAL A 84 ? 0.2332 0.3062 0.2300 -0.0207 -0.0225 0.0000 84 VAL A O 678 C CB . VAL A 84 ? 0.1856 0.2810 0.2793 0.0211 0.0058 -0.0379 84 VAL A CB 679 C CG1 . VAL A 84 ? 0.3086 0.3040 0.3233 0.0148 -0.0181 -0.0332 84 VAL A CG1 680 C CG2 . VAL A 84 ? 0.1929 0.3241 0.3083 0.0054 0.0060 -0.0078 84 VAL A CG2 681 N N . PRO A 85 ? 0.1832 0.2500 0.2047 0.0019 0.0022 0.0087 85 PRO A N 682 C CA . PRO A 85 ? 0.1870 0.2360 0.2218 -0.0228 -0.0083 0.0135 85 PRO A CA 683 C C . PRO A 85 ? 0.1976 0.2717 0.2360 0.0012 -0.0193 0.0289 85 PRO A C 684 O O . PRO A 85 ? 0.2246 0.2895 0.2911 0.0376 -0.0122 0.0205 85 PRO A O 685 C CB . PRO A 85 ? 0.2356 0.2153 0.2406 -0.0228 0.0219 -0.0023 85 PRO A CB 686 C CG . PRO A 85 ? 0.1817 0.2427 0.2315 0.0168 0.0294 0.0115 85 PRO A CG 687 C CD . PRO A 85 ? 0.1747 0.2799 0.2126 0.0004 0.0229 -0.0019 85 PRO A CD 688 N N . ILE A 86 ? 0.2133 0.2660 0.2137 0.0032 -0.0300 -0.0040 86 ILE A N 689 C CA . ILE A 86 ? 0.2066 0.2654 0.2303 -0.0020 -0.0515 0.0036 86 ILE A CA 690 C C . ILE A 86 ? 0.2223 0.2293 0.2393 0.0012 -0.0266 -0.0348 86 ILE A C 691 O O . ILE A 86 ? 0.3331 0.2378 0.3144 0.0674 -0.0625 -0.0811 86 ILE A O 692 C CB . ILE A 86 ? 0.2734 0.2978 0.3019 -0.0101 -0.0896 -0.0247 86 ILE A CB 693 C CG1 . ILE A 86 ? 0.3083 0.3626 0.3007 -0.0142 -0.0539 -0.0243 86 ILE A CG1 694 C CG2 . ILE A 86 ? 0.3897 0.3562 0.3815 0.0047 -0.0464 0.0371 86 ILE A CG2 695 C CD1 . ILE A 86 ? 0.2736 0.4038 0.4219 0.0454 -0.0774 -0.0418 86 ILE A CD1 696 N N . ASP A 87 ? 0.2614 0.2034 0.2412 -0.0083 -0.0091 0.0195 87 ASP A N 697 C CA . ASP A 87 ? 0.2231 0.2194 0.3176 -0.0317 -0.0484 0.0282 87 ASP A CA 698 C C . ASP A 87 ? 0.2604 0.2600 0.3150 0.0028 -0.0348 0.0261 87 ASP A C 699 O O . ASP A 87 ? 0.3301 0.2443 0.3589 -0.0091 -0.0797 0.0598 87 ASP A O 700 C CB . ASP A 87 ? 0.3175 0.2992 0.3342 -0.0572 -0.0035 0.0447 87 ASP A CB 701 C CG . ASP A 87 ? 0.3072 0.2791 0.3067 0.0303 0.0101 0.0032 87 ASP A CG 702 O OD1 . ASP A 87 ? 0.3539 0.4385 0.3601 0.0159 0.0502 -0.0427 87 ASP A OD1 703 O OD2 . ASP A 87 ? 0.2857 0.2886 0.2740 -0.0002 -0.0248 0.0000 87 ASP A OD2 704 N N . GLY A 88 ? 0.2371 0.2376 0.2684 -0.0103 -0.0511 -0.0081 88 GLY A N 705 C CA . GLY A 88 ? 0.2815 0.2823 0.2865 0.0305 -0.0703 -0.0008 88 GLY A CA 706 C C . GLY A 88 ? 0.2675 0.2256 0.3096 0.0127 -0.0294 -0.0304 88 GLY A C 707 O O . GLY A 88 ? 0.2847 0.3632 0.2606 0.0289 -0.0304 0.0088 88 GLY A O 708 N N . SER A 89 ? 0.1963 0.2012 0.2218 0.0062 -0.0429 -0.0113 89 SER A N 709 C CA . SER A 89 ? 0.2117 0.2324 0.2027 0.0040 -0.0124 -0.0090 89 SER A CA 710 C C . SER A 89 ? 0.2125 0.2713 0.2200 -0.0131 0.0076 0.0025 89 SER A C 711 O O . SER A 89 ? 0.2191 0.2747 0.2356 -0.0449 -0.0210 0.0127 89 SER A O 712 C CB . SER A 89 ? 0.2404 0.2712 0.2645 -0.0090 0.0274 -0.0028 89 SER A CB 713 O OG . SER A 89 ? 0.2183 0.2713 0.2660 0.0153 0.0174 0.0345 89 SER A OG 714 N N . ILE A 90 ? 0.1964 0.2016 0.2545 0.0085 -0.0147 -0.0094 90 ILE A N 715 C CA . ILE A 90 ? 0.1882 0.2431 0.2428 0.0010 0.0096 -0.0447 90 ILE A CA 716 C C . ILE A 90 ? 0.2129 0.2213 0.2076 0.0004 0.0079 0.0230 90 ILE A C 717 O O . ILE A 90 ? 0.2125 0.2346 0.2319 0.0192 -0.0108 -0.0144 90 ILE A O 718 C CB . ILE A 90 ? 0.1747 0.2362 0.2279 0.0043 -0.0150 -0.0207 90 ILE A CB 719 C CG1 . ILE A 90 ? 0.1781 0.2731 0.2248 0.0274 0.0277 -0.0364 90 ILE A CG1 720 C CG2 . ILE A 90 ? 0.2070 0.2429 0.3132 -0.0235 0.0285 0.0102 90 ILE A CG2 721 C CD1 . ILE A 90 ? 0.2025 0.2548 0.2889 0.0586 -0.0072 -0.0095 90 ILE A CD1 722 N N . ILE A 91 ? 0.2141 0.1914 0.2360 0.0122 -0.0196 -0.0181 91 ILE A N 723 C CA . ILE A 91 ? 0.1834 0.2003 0.2422 0.0144 -0.0173 -0.0149 91 ILE A CA 724 C C . ILE A 91 ? 0.2090 0.2644 0.2606 -0.0142 -0.0062 -0.0029 91 ILE A C 725 O O . ILE A 91 ? 0.2157 0.2465 0.2422 -0.0112 -0.0284 0.0206 91 ILE A O 726 C CB . ILE A 91 ? 0.1692 0.2885 0.2242 0.0659 -0.0227 -0.0007 91 ILE A CB 727 C CG1 . ILE A 91 ? 0.1763 0.3141 0.2165 0.0282 0.0063 -0.0125 91 ILE A CG1 728 C CG2 . ILE A 91 ? 0.2148 0.2841 0.2596 0.0374 -0.0179 0.0248 91 ILE A CG2 729 C CD1 . ILE A 91 ? 0.1750 0.3254 0.2937 -0.0063 -0.0257 0.0017 91 ILE A CD1 730 N N . ASN A 92 ? 0.1956 0.2113 0.2507 0.0109 -0.0194 -0.0037 92 ASN A N 731 C CA . ASN A 92 ? 0.2054 0.2330 0.2788 0.0058 -0.0193 -0.0238 92 ASN A CA 732 C C . ASN A 92 ? 0.2666 0.2844 0.2723 0.0000 -0.0053 0.0008 92 ASN A C 733 O O . ASN A 92 ? 0.3030 0.2529 0.3120 -0.0033 0.0298 -0.0178 92 ASN A O 734 C CB . ASN A 92 ? 0.2626 0.2246 0.2605 -0.0130 -0.0182 -0.0249 92 ASN A CB 735 C CG . ASN A 92 ? 0.3195 0.2431 0.3063 -0.0246 -0.0332 -0.0044 92 ASN A CG 736 O OD1 . ASN A 92 ? 0.3549 0.2982 0.3755 -0.0822 0.0108 -0.0403 92 ASN A OD1 737 N ND2 . ASN A 92 ? 0.3440 0.3456 0.3647 -0.0146 0.0331 -0.0127 92 ASN A ND2 738 N N . PRO A 93 ? 0.2265 0.2607 0.2971 0.0150 -0.0280 0.0059 93 PRO A N 739 C CA . PRO A 93 ? 0.2894 0.2821 0.3303 0.0388 -0.0208 -0.0005 93 PRO A CA 740 C C . PRO A 93 ? 0.2860 0.2780 0.3655 0.0123 -0.0092 -0.0223 93 PRO A C 741 O O . PRO A 93 ? 0.3205 0.3489 0.4072 -0.0379 0.0480 -0.0448 93 PRO A O 742 C CB . PRO A 93 ? 0.3519 0.3010 0.3133 0.0193 0.0016 0.0022 93 PRO A CB 743 C CG . PRO A 93 ? 0.3240 0.3160 0.3105 0.0825 -0.0322 0.0226 93 PRO A CG 744 C CD . PRO A 93 ? 0.2156 0.2924 0.2808 -0.0023 -0.0310 0.0591 93 PRO A CD 745 N N . SER A 94 ? 0.2985 0.2944 0.3170 0.0016 0.0073 -0.0231 94 SER A N 746 C CA . SER A 94 ? 0.3615 0.3215 0.3312 0.0071 0.0147 -0.0339 94 SER A CA 747 C C . SER A 94 ? 0.4045 0.3528 0.3914 0.0164 0.0350 0.0000 94 SER A C 748 O O . SER A 94 ? 0.4482 0.3823 0.4791 0.0013 0.0379 -0.0330 94 SER A O 749 C CB . SER A 94 ? 0.3888 0.3778 0.3861 -0.0163 -0.0248 -0.0541 94 SER A CB 750 O OG . SER A 94 ? 0.4696 0.4052 0.3956 -0.0166 0.0143 -0.0495 94 SER A OG 751 N N . SER A 95 ? 0.4245 0.3008 0.3599 -0.0192 0.0358 -0.0185 95 SER A N 752 C CA . SER A 95 ? 0.3917 0.3630 0.3624 -0.0085 0.0084 -0.0227 95 SER A CA 753 C C . SER A 95 ? 0.3765 0.3480 0.3540 -0.0078 0.0053 -0.0164 95 SER A C 754 O O . SER A 95 ? 0.4155 0.2892 0.3986 0.0475 0.0487 -0.0208 95 SER A O 755 C CB . SER A 95 ? 0.3871 0.3079 0.3135 -0.0194 0.0132 -0.0174 95 SER A CB 756 O OG . SER A 95 ? 0.3854 0.2830 0.3486 -0.0335 0.0172 -0.0305 95 SER A OG 757 N N . GLY A 96 ? 0.3234 0.2666 0.3579 0.0673 0.0092 -0.0129 96 GLY A N 758 C CA . GLY A 96 ? 0.2797 0.3086 0.3375 0.0394 0.0004 -0.0051 96 GLY A CA 759 C C . GLY A 96 ? 0.2431 0.3088 0.3347 0.0292 -0.0058 0.0235 96 GLY A C 760 O O . GLY A 96 ? 0.2039 0.4046 0.3661 0.0316 -0.0155 -0.0069 96 GLY A O 761 N N . LEU A 97 ? 0.2304 0.2862 0.2336 0.0273 -0.0346 -0.0228 97 LEU A N 762 C CA . LEU A 97 ? 0.2427 0.2676 0.2060 0.0266 -0.0050 -0.0116 97 LEU A CA 763 C C . LEU A 97 ? 0.2200 0.2306 0.2444 0.0045 -0.0377 -0.0187 97 LEU A C 764 O O . LEU A 97 ? 0.1917 0.2602 0.2603 0.0039 -0.0044 -0.0242 97 LEU A O 765 C CB . LEU A 97 ? 0.2441 0.2735 0.2364 0.0264 -0.0367 -0.0524 97 LEU A CB 766 C CG . LEU A 97 ? 0.2768 0.2420 0.2525 0.0085 -0.0030 -0.0037 97 LEU A CG 767 C CD1 . LEU A 97 ? 0.2642 0.3344 0.3307 0.0174 -0.0382 -0.0593 97 LEU A CD1 768 C CD2 . LEU A 97 ? 0.2761 0.2699 0.2886 -0.0107 0.0499 -0.0232 97 LEU A CD2 769 N N . VAL A 98 ? 0.1689 0.1857 0.2713 0.0091 -0.0261 -0.0398 98 VAL A N 770 C CA . VAL A 98 ? 0.1794 0.1922 0.2317 -0.0018 -0.0210 -0.0441 98 VAL A CA 771 C C . VAL A 98 ? 0.2116 0.2291 0.2210 0.0197 -0.0140 0.0366 98 VAL A C 772 O O . VAL A 98 ? 0.1740 0.2432 0.1955 0.0008 0.0268 -0.0083 98 VAL A O 773 C CB . VAL A 98 ? 0.1741 0.1821 0.2594 -0.0152 -0.0101 0.0095 98 VAL A CB 774 C CG1 . VAL A 98 ? 0.1767 0.2742 0.2980 0.0456 -0.0339 0.0374 98 VAL A CG1 775 C CG2 . VAL A 98 ? 0.1902 0.2409 0.2434 -0.0410 0.0013 0.0340 98 VAL A CG2 776 N N A MET A 99 ? 0.1651 0.1836 0.2451 0.0121 -0.0031 -0.0018 99 MET A N 777 N N B MET A 99 ? 0.1998 0.2014 0.2609 0.0066 0.0095 -0.0009 99 MET A N 778 C CA A MET A 99 ? 0.1666 0.2434 0.1806 0.0276 0.0167 0.0298 99 MET A CA 779 C CA B MET A 99 ? 0.2433 0.2455 0.2291 0.0222 -0.0073 0.0252 99 MET A CA 780 C C A MET A 99 ? 0.0780 0.2080 0.1487 -0.0532 -0.0504 -0.0073 99 MET A C 781 C C B MET A 99 ? 0.0674 0.2055 0.1585 -0.0478 -0.0591 -0.0121 99 MET A C 782 O O A MET A 99 ? 0.1858 0.2351 0.2400 0.0088 -0.0003 0.0057 99 MET A O 783 O O B MET A 99 ? 0.1856 0.2234 0.2072 0.0133 0.0034 -0.0147 99 MET A O 784 C CB A MET A 99 ? 0.0995 0.1866 0.1523 0.0295 0.0176 -0.0049 99 MET A CB 785 C CB B MET A 99 ? 0.1865 0.2401 0.2095 -0.0063 0.0219 -0.0110 99 MET A CB 786 C CG A MET A 99 ? 0.1180 0.2168 0.2035 0.0072 0.0087 -0.0122 99 MET A CG 787 C CG B MET A 99 ? 0.2674 0.2924 0.3449 0.0183 0.0012 0.0184 99 MET A CG 788 S SD A MET A 99 ? 0.1651 0.2048 0.1572 -0.0117 0.0085 0.0064 99 MET A SD 789 S SD B MET A 99 ? 0.3427 0.3403 0.3105 0.0270 0.0287 -0.0163 99 MET A SD 790 C CE A MET A 99 ? 0.1819 0.2385 0.1787 -0.0047 -0.0260 0.0382 99 MET A CE 791 C CE B MET A 99 ? 0.1766 0.2415 0.2821 0.0221 0.0111 0.0015 99 MET A CE 792 N N . THR A 100 ? 0.2511 0.2642 0.1957 0.0086 0.0027 0.0116 100 THR A N 793 C CA . THR A 100 ? 0.2122 0.2601 0.2029 0.0243 0.0199 0.0390 100 THR A CA 794 C C . THR A 100 ? 0.2195 0.2363 0.1994 -0.0084 0.0097 0.0130 100 THR A C 795 O O . THR A 100 ? 0.1981 0.2286 0.2320 -0.0078 -0.0198 0.0150 100 THR A O 796 C CB . THR A 100 ? 0.2223 0.2327 0.1938 0.0037 0.0205 -0.0105 100 THR A CB 797 O OG1 . THR A 100 ? 0.2066 0.2476 0.2360 0.0364 0.0110 -0.0355 100 THR A OG1 798 C CG2 . THR A 100 ? 0.2315 0.2151 0.1886 -0.0390 -0.0058 0.0080 100 THR A CG2 799 N N . ALA A 101 ? 0.2116 0.1962 0.2103 0.0655 0.0095 -0.0072 101 ALA A N 800 C CA . ALA A 101 ? 0.2164 0.1792 0.2164 0.0320 0.0016 0.0233 101 ALA A CA 801 C C . ALA A 101 ? 0.2235 0.2440 0.2118 0.0173 -0.0164 0.0201 101 ALA A C 802 O O . ALA A 101 ? 0.2101 0.2677 0.2561 0.0060 -0.0035 0.0280 101 ALA A O 803 C CB . ALA A 101 ? 0.1803 0.2307 0.2162 0.0312 -0.0012 -0.0329 101 ALA A CB 804 N N . PRO A 102 ? 0.2740 0.3139 0.2222 0.0434 0.0126 0.0269 102 PRO A N 805 C CA . PRO A 102 ? 0.3370 0.3129 0.2556 -0.0223 -0.0074 0.0256 102 PRO A CA 806 C C . PRO A 102 ? 0.1945 0.2650 0.2404 0.0002 0.0097 0.0245 102 PRO A C 807 O O . PRO A 102 ? 0.2793 0.3152 0.2234 0.0161 0.0077 0.0354 102 PRO A O 808 C CB . PRO A 102 ? 0.3819 0.3266 0.2525 -0.0095 -0.0229 -0.0206 102 PRO A CB 809 C CG . PRO A 102 ? 0.5043 0.3726 0.2734 0.0021 0.0280 0.0005 102 PRO A CG 810 C CD . PRO A 102 ? 0.3529 0.3034 0.2158 0.0362 -0.0141 0.0175 102 PRO A CD 811 N N . ARG A 103 ? 0.2330 0.2705 0.2444 0.0454 0.0098 0.0471 103 ARG A N 812 C CA . ARG A 103 ? 0.2211 0.2747 0.2629 0.0488 -0.0184 0.0243 103 ARG A CA 813 C C . ARG A 103 ? 0.2162 0.2759 0.2467 0.0416 -0.0324 0.0010 103 ARG A C 814 O O . ARG A 103 ? 0.2496 0.2702 0.2451 -0.0016 -0.0042 0.0083 103 ARG A O 815 C CB . ARG A 103 ? 0.2309 0.3442 0.2503 -0.0037 -0.0453 0.0243 103 ARG A CB 816 C CG . ARG A 103 ? 0.3050 0.3606 0.2824 0.0039 -0.0415 0.0072 103 ARG A CG 817 C CD . ARG A 103 ? 0.3280 0.4363 0.2953 0.0439 -0.0459 0.0402 103 ARG A CD 818 N NE . ARG A 103 ? 0.5683 0.5063 0.5639 0.0027 -0.0092 0.0207 103 ARG A NE 819 C CZ . ARG A 103 ? 0.5183 0.5448 0.5316 -0.0133 0.0074 0.0124 103 ARG A CZ 820 N NH1 . ARG A 103 ? 0.6180 0.5494 0.6167 -0.0140 -0.0286 0.0213 103 ARG A NH1 821 N NH2 . ARG A 103 ? 0.3878 0.4592 0.2517 0.0361 -0.0448 -0.0025 103 ARG A NH2 822 N N . ALA A 104 ? 0.2122 0.2631 0.3324 0.0470 -0.0369 -0.0252 104 ALA A N 823 C CA . ALA A 104 ? 0.2719 0.3142 0.3396 0.0129 -0.0017 -0.0319 104 ALA A CA 824 C C . ALA A 104 ? 0.2702 0.2926 0.2753 0.0023 0.0105 0.0157 104 ALA A C 825 O O . ALA A 104 ? 0.2970 0.3719 0.2857 -0.0083 -0.0003 0.0135 104 ALA A O 826 C CB . ALA A 104 ? 0.3247 0.3557 0.4096 -0.0005 -0.0589 -0.0314 104 ALA A CB 827 N N . ALA A 105 ? 0.2931 0.3139 0.2868 -0.0054 -0.0115 -0.0249 105 ALA A N 828 C CA . ALA A 105 ? 0.2671 0.3198 0.2435 -0.0026 -0.0174 0.0449 105 ALA A CA 829 C C . ALA A 105 ? 0.2522 0.2760 0.2424 0.0006 -0.0044 -0.0029 105 ALA A C 830 O O . ALA A 105 ? 0.2340 0.2984 0.2337 0.0094 -0.0219 -0.0054 105 ALA A O 831 C CB . ALA A 105 ? 0.3129 0.3412 0.2340 -0.0245 -0.0227 0.0279 105 ALA A CB 832 N N A SER A 106 ? 0.2755 0.3174 0.2302 0.0197 -0.0081 0.0137 106 SER A N 833 N N B SER A 106 ? 0.2619 0.3086 0.2156 0.0188 -0.0104 0.0184 106 SER A N 834 C CA A SER A 106 ? 0.2606 0.3076 0.2412 0.0044 0.0051 -0.0061 106 SER A CA 835 C CA B SER A 106 ? 0.2444 0.2687 0.2097 0.0080 0.0018 -0.0025 106 SER A CA 836 C C A SER A 106 ? 0.2583 0.2656 0.2299 0.0191 0.0156 -0.0022 106 SER A C 837 C C B SER A 106 ? 0.2549 0.2535 0.2195 0.0211 0.0135 -0.0107 106 SER A C 838 O O A SER A 106 ? 0.2534 0.3196 0.2026 0.0200 0.0052 0.0166 106 SER A O 839 O O B SER A 106 ? 0.2575 0.2815 0.2069 0.0142 0.0066 0.0215 106 SER A O 840 C CB A SER A 106 ? 0.2763 0.3112 0.2944 0.0318 -0.0144 -0.0101 106 SER A CB 841 C CB B SER A 106 ? 0.2580 0.3084 0.2493 0.0285 -0.0071 -0.0079 106 SER A CB 842 O OG A SER A 106 ? 0.3042 0.3627 0.2941 0.0578 0.0265 0.0090 106 SER A OG 843 O OG B SER A 106 ? 0.2549 0.2655 0.2683 0.0092 -0.0163 -0.0163 106 SER A OG 844 N N . ARG A 107 ? 0.2130 0.2474 0.2077 0.0388 -0.0038 -0.0127 107 ARG A N 845 C CA . ARG A 107 ? 0.1840 0.2641 0.2464 0.0318 -0.0179 -0.0206 107 ARG A CA 846 C C . ARG A 107 ? 0.1792 0.2454 0.2122 -0.0030 -0.0301 -0.0163 107 ARG A C 847 O O . ARG A 107 ? 0.1799 0.2843 0.2218 0.0197 -0.0263 -0.0196 107 ARG A O 848 C CB . ARG A 107 ? 0.1929 0.3006 0.2331 0.0218 -0.0046 0.0020 107 ARG A CB 849 C CG . ARG A 107 ? 0.1870 0.3022 0.2030 0.0645 -0.0218 0.0225 107 ARG A CG 850 C CD . ARG A 107 ? 0.2012 0.2696 0.2466 0.0560 -0.0359 0.0156 107 ARG A CD 851 N NE . ARG A 107 ? 0.2780 0.3953 0.3126 0.0684 -0.0170 -0.0183 107 ARG A NE 852 C CZ . ARG A 107 ? 0.2992 0.2797 0.2938 0.0262 0.0084 -0.0374 107 ARG A CZ 853 N NH1 . ARG A 107 ? 0.4615 0.3256 0.3546 0.0025 -0.0048 0.0327 107 ARG A NH1 854 N NH2 . ARG A 107 ? 0.2839 0.3548 0.2601 0.0758 -0.0441 -0.0467 107 ARG A NH2 855 N N . THR A 108 ? 0.1784 0.2663 0.1803 0.0285 -0.0263 0.0182 108 THR A N 856 C CA . THR A 108 ? 0.1807 0.2407 0.2350 0.0001 0.0114 -0.0073 108 THR A CA 857 C C . THR A 108 ? 0.1942 0.2429 0.2250 -0.0096 0.0099 -0.0083 108 THR A C 858 O O . THR A 108 ? 0.1627 0.2675 0.2122 0.0158 0.0139 0.0030 108 THR A O 859 C CB . THR A 108 ? 0.1975 0.2033 0.2849 -0.0348 0.0381 -0.0100 108 THR A CB 860 O OG1 . THR A 108 ? 0.2165 0.3057 0.2791 -0.0160 -0.0242 0.0368 108 THR A OG1 861 C CG2 . THR A 108 ? 0.1919 0.2072 0.2944 0.0297 -0.0004 -0.0176 108 THR A CG2 862 N N . ILE A 109 ? 0.1682 0.2302 0.1926 0.0152 -0.0090 -0.0211 109 ILE A N 863 C CA . ILE A 109 ? 0.1559 0.2128 0.2010 0.0130 -0.0312 -0.0329 109 ILE A CA 864 C C . ILE A 109 ? 0.1795 0.3190 0.2499 0.0355 0.0165 0.0140 109 ILE A C 865 O O . ILE A 109 ? 0.1838 0.3622 0.2323 0.0309 -0.0091 0.0561 109 ILE A O 866 C CB . ILE A 109 ? 0.1675 0.2666 0.2363 0.0387 -0.0549 -0.0196 109 ILE A CB 867 C CG1 . ILE A 109 ? 0.1844 0.3154 0.2897 0.0309 -0.0322 -0.0083 109 ILE A CG1 868 C CG2 . ILE A 109 ? 0.2798 0.2984 0.3220 0.0329 -0.0455 -0.0240 109 ILE A CG2 869 C CD1 . ILE A 109 ? 0.2887 0.4340 0.3385 -0.0019 0.0123 0.0218 109 ILE A CD1 870 N N . LEU A 110 ? 0.1584 0.2449 0.2206 0.0431 -0.0237 -0.0058 110 LEU A N 871 C CA . LEU A 110 ? 0.1654 0.2460 0.1691 0.0492 -0.0289 -0.0123 110 LEU A CA 872 C C . LEU A 110 ? 0.2211 0.2380 0.1983 0.0149 0.0158 -0.0023 110 LEU A C 873 O O . LEU A 110 ? 0.2011 0.2615 0.2305 -0.0235 -0.0104 -0.0014 110 LEU A O 874 C CB . LEU A 110 ? 0.2274 0.2689 0.1858 0.0084 -0.0243 -0.0164 110 LEU A CB 875 C CG . LEU A 110 ? 0.1810 0.2164 0.1982 0.0000 -0.0110 0.0143 110 LEU A CG 876 C CD1 . LEU A 110 ? 0.2237 0.2757 0.2069 0.0440 -0.0363 0.0378 110 LEU A CD1 877 C CD2 . LEU A 110 ? 0.1906 0.2117 0.2248 -0.0106 -0.0030 0.0162 110 LEU A CD2 878 N N . LEU A 111 ? 0.1501 0.2604 0.2017 -0.0032 0.0254 -0.0132 111 LEU A N 879 C CA . LEU A 111 ? 0.1853 0.2169 0.2104 0.0537 -0.0346 0.0180 111 LEU A CA 880 C C . LEU A 111 ? 0.1923 0.2432 0.2523 0.0258 -0.0270 -0.0111 111 LEU A C 881 O O . LEU A 111 ? 0.1826 0.2740 0.2251 -0.0054 -0.0228 -0.0161 111 LEU A O 882 C CB . LEU A 111 ? 0.2485 0.2702 0.2200 0.0027 -0.0185 0.0280 111 LEU A CB 883 C CG . LEU A 111 ? 0.2139 0.2402 0.2287 -0.0114 -0.0154 0.0210 111 LEU A CG 884 C CD1 . LEU A 111 ? 0.3081 0.3286 0.1630 -0.0394 0.0107 0.0011 111 LEU A CD1 885 C CD2 . LEU A 111 ? 0.1676 0.3033 0.2522 -0.0180 -0.0298 -0.0109 111 LEU A CD2 886 N N . LEU A 112 ? 0.1954 0.2538 0.2719 0.0353 -0.0088 0.0035 112 LEU A N 887 C CA . LEU A 112 ? 0.1689 0.2526 0.2427 -0.0047 0.0035 0.0042 112 LEU A CA 888 C C . LEU A 112 ? 0.1976 0.2672 0.2194 0.0205 0.0106 0.0105 112 LEU A C 889 O O . LEU A 112 ? 0.1696 0.3049 0.2785 0.0075 -0.0246 -0.0031 112 LEU A O 890 C CB . LEU A 112 ? 0.2837 0.2554 0.2307 -0.0066 0.0045 -0.0200 112 LEU A CB 891 C CG . LEU A 112 ? 0.2930 0.2837 0.2514 -0.0489 -0.0394 -0.0068 112 LEU A CG 892 C CD1 . LEU A 112 ? 0.4155 0.3030 0.3584 -0.0272 -0.0317 -0.0007 112 LEU A CD1 893 C CD2 . LEU A 112 ? 0.2348 0.3865 0.2110 -0.0066 -0.0459 0.0184 112 LEU A CD2 894 N N . GLU A 113 ? 0.2004 0.2723 0.2447 -0.0157 0.0035 -0.0077 113 GLU A N 895 C CA . GLU A 113 ? 0.1762 0.3069 0.2710 -0.0014 -0.0213 0.0053 113 GLU A CA 896 C C . GLU A 113 ? 0.1848 0.2692 0.2389 0.0027 -0.0128 -0.0160 113 GLU A C 897 O O . GLU A 113 ? 0.2034 0.3064 0.2410 0.0039 -0.0066 -0.0064 113 GLU A O 898 C CB . GLU A 113 ? 0.2323 0.3027 0.2740 0.0043 0.0052 0.0128 113 GLU A CB 899 C CG . GLU A 113 ? 0.2094 0.2787 0.2778 0.0481 0.0201 0.0205 113 GLU A CG 900 C CD . GLU A 113 ? 0.2252 0.3433 0.2807 -0.0261 -0.0215 0.0655 113 GLU A CD 901 O OE1 . GLU A 113 ? 0.4702 0.3387 0.2921 -0.0941 -0.0252 -0.0085 113 GLU A OE1 902 O OE2 . GLU A 113 ? 0.3000 0.4426 0.4881 0.0447 0.0342 0.0618 113 GLU A OE2 903 N N . ASP A 114 ? 0.1640 0.3343 0.2683 0.0148 0.0080 -0.0136 114 ASP A N 904 C CA . ASP A 114 ? 0.1655 0.2816 0.2313 0.0371 0.0060 -0.0084 114 ASP A CA 905 C C . ASP A 114 ? 0.2367 0.2792 0.2555 0.0041 0.0101 0.0035 114 ASP A C 906 O O . ASP A 114 ? 0.1893 0.2997 0.2382 0.0297 0.0058 -0.0055 114 ASP A O 907 C CB . ASP A 114 ? 0.2229 0.3337 0.2253 -0.0125 0.0154 -0.0309 114 ASP A CB 908 C CG . ASP A 114 ? 0.3276 0.3525 0.3540 0.0183 0.0098 -0.0319 114 ASP A CG 909 O OD1 . ASP A 114 ? 0.4440 0.3967 0.3775 -0.0177 0.0366 -0.0598 114 ASP A OD1 910 O OD2 . ASP A 114 ? 0.5923 0.5621 0.4529 0.0396 -0.0077 0.0103 114 ASP A OD2 911 N N . ASN A 115 ? 0.1999 0.2713 0.2203 0.0055 -0.0162 -0.0287 115 ASN A N 912 C CA . ASN A 115 ? 0.1931 0.2498 0.2262 -0.0165 -0.0268 -0.0094 115 ASN A CA 913 C C . ASN A 115 ? 0.2480 0.2195 0.2557 0.0205 0.0318 -0.0137 115 ASN A C 914 O O . ASN A 115 ? 0.2060 0.2806 0.3229 0.0326 0.0271 -0.0064 115 ASN A O 915 C CB . ASN A 115 ? 0.1965 0.2661 0.2464 0.0203 -0.0249 -0.0068 115 ASN A CB 916 C CG . ASN A 115 ? 0.2747 0.1971 0.2875 0.0167 -0.0250 -0.0346 115 ASN A CG 917 O OD1 . ASN A 115 ? 0.1842 0.2471 0.2608 -0.0044 -0.0437 0.0104 115 ASN A OD1 918 N ND2 . ASN A 115 ? 0.3201 0.3341 0.3493 0.0374 -0.0254 0.0018 115 ASN A ND2 919 N N . ILE A 116 ? 0.1900 0.2218 0.2584 0.0070 -0.0167 -0.0336 116 ILE A N 920 C CA . ILE A 116 ? 0.2551 0.2305 0.2401 0.0117 0.0056 -0.0125 116 ILE A CA 921 C C . ILE A 116 ? 0.2262 0.2444 0.2692 0.0177 0.0062 -0.0096 116 ILE A C 922 O O . ILE A 116 ? 0.2248 0.2910 0.2665 -0.0039 0.0190 -0.0025 116 ILE A O 923 C CB . ILE A 116 ? 0.2485 0.2467 0.2509 0.0228 0.0335 -0.0358 116 ILE A CB 924 C CG1 . ILE A 116 ? 0.2679 0.2287 0.2891 0.0420 0.0243 0.0138 116 ILE A CG1 925 C CG2 . ILE A 116 ? 0.2780 0.2907 0.2558 -0.0380 0.0194 -0.0517 116 ILE A CG2 926 C CD1 . ILE A 116 ? 0.2627 0.2665 0.2576 0.0004 -0.0109 0.0120 116 ILE A CD1 927 N N . TYR A 117 ? 0.2172 0.2255 0.2059 0.0195 -0.0425 0.0060 117 TYR A N 928 C CA . TYR A 117 ? 0.1361 0.2272 0.2587 0.0127 -0.0169 -0.0360 117 TYR A CA 929 C C . TYR A 117 ? 0.1691 0.2294 0.2376 0.0054 0.0011 0.0140 117 TYR A C 930 O O . TYR A 117 ? 0.1904 0.2544 0.2245 0.0072 -0.0220 0.0173 117 TYR A O 931 C CB . TYR A 117 ? 0.1617 0.2173 0.3415 -0.0032 -0.0533 0.0221 117 TYR A CB 932 C CG . TYR A 117 ? 0.2119 0.2444 0.3082 0.0065 -0.0209 0.0060 117 TYR A CG 933 C CD1 . TYR A 117 ? 0.2195 0.2234 0.3189 -0.0124 -0.0271 -0.0130 117 TYR A CD1 934 C CD2 . TYR A 117 ? 0.3020 0.2611 0.3387 -0.0009 -0.0334 0.0211 117 TYR A CD2 935 C CE1 . TYR A 117 ? 0.2695 0.2079 0.3835 0.0110 0.0257 -0.0067 117 TYR A CE1 936 C CE2 . TYR A 117 ? 0.2873 0.2989 0.3040 0.0201 -0.0346 0.0003 117 TYR A CE2 937 C CZ . TYR A 117 ? 0.3105 0.2574 0.3710 0.0061 0.0167 0.0126 117 TYR A CZ 938 O OH . TYR A 117 ? 0.3460 0.2463 0.3557 0.0292 0.0118 0.0002 117 TYR A OH 939 N N . ALA A 118 ? 0.1698 0.2530 0.2481 0.0282 -0.0092 0.0127 118 ALA A N 940 C CA . ALA A 118 ? 0.2545 0.2389 0.1874 0.0077 -0.0307 0.0218 118 ALA A CA 941 C C . ALA A 118 ? 0.1998 0.2245 0.1927 -0.0033 -0.0288 0.0034 118 ALA A C 942 O O . ALA A 118 ? 0.2142 0.2484 0.2056 0.0032 -0.0126 0.0243 118 ALA A O 943 C CB . ALA A 118 ? 0.1992 0.2654 0.1882 -0.0146 -0.0183 0.0088 118 ALA A CB 944 N N . ALA A 119 ? 0.1563 0.2112 0.2227 0.0253 -0.0253 0.0010 119 ALA A N 945 C CA . ALA A 119 ? 0.1786 0.2146 0.2403 0.0046 0.0054 0.0112 119 ALA A CA 946 C C . ALA A 119 ? 0.2034 0.2517 0.1901 0.0054 -0.0421 -0.0010 119 ALA A C 947 O O . ALA A 119 ? 0.1800 0.2851 0.2195 0.0224 -0.0095 -0.0167 119 ALA A O 948 C CB . ALA A 119 ? 0.1936 0.2128 0.2506 -0.0151 -0.0367 0.0157 119 ALA A CB 949 N N . SER A 120 ? 0.1844 0.2267 0.2234 -0.0176 -0.0298 -0.0003 120 SER A N 950 C CA . SER A 120 ? 0.1572 0.2142 0.1992 -0.0290 -0.0329 0.0018 120 SER A CA 951 C C . SER A 120 ? 0.1866 0.2208 0.1951 -0.0276 -0.0307 -0.0011 120 SER A C 952 O O . SER A 120 ? 0.1981 0.2074 0.2529 0.0058 -0.0077 0.0144 120 SER A O 953 C CB . SER A 120 ? 0.2073 0.2446 0.2099 -0.0069 -0.0222 0.0160 120 SER A CB 954 O OG . SER A 120 ? 0.2151 0.3154 0.2329 -0.0028 -0.0223 -0.0139 120 SER A OG 955 N N . GLN A 121 ? 0.1958 0.1871 0.2131 0.0204 -0.0286 -0.0096 121 GLN A N 956 C CA . GLN A 121 ? 0.1687 0.1684 0.1877 0.0249 -0.0207 -0.0266 121 GLN A CA 957 C C . GLN A 121 ? 0.1594 0.1874 0.2050 0.0175 0.0074 0.0005 121 GLN A C 958 O O . GLN A 121 ? 0.2200 0.1973 0.2188 0.0006 0.0004 0.0281 121 GLN A O 959 C CB . GLN A 121 ? 0.2116 0.2094 0.1753 0.0081 0.0211 -0.0227 121 GLN A CB 960 C CG . GLN A 121 ? 0.2485 0.2283 0.1362 -0.0167 0.0190 -0.0448 121 GLN A CG 961 C CD . GLN A 121 ? 0.1841 0.2061 0.2078 -0.0177 -0.0033 0.0021 121 GLN A CD 962 O OE1 . GLN A 121 ? 0.1373 0.3009 0.2233 0.0163 0.0181 0.0022 121 GLN A OE1 963 N NE2 . GLN A 121 ? 0.1779 0.2276 0.2190 0.0105 -0.0370 -0.0035 121 GLN A NE2 964 N N . GLY A 122 ? 0.1379 0.2175 0.1948 -0.0246 0.0251 -0.0305 122 GLY A N 965 C CA . GLY A 122 ? 0.1790 0.2109 0.1719 -0.0403 0.0289 -0.0123 122 GLY A CA 966 C C . GLY A 122 ? 0.2066 0.1976 0.2262 -0.0130 0.0262 0.0324 122 GLY A C 967 O O . GLY A 122 ? 0.1825 0.2357 0.2097 0.0182 -0.0157 0.0044 122 GLY A O 968 N N . TRP A 123 ? 0.1796 0.2304 0.1685 -0.0177 -0.0035 0.0286 123 TRP A N 969 C CA . TRP A 123 ? 0.1819 0.2314 0.1643 -0.0001 0.0311 -0.0064 123 TRP A CA 970 C C . TRP A 123 ? 0.1628 0.1983 0.1947 -0.0095 0.0041 0.0411 123 TRP A C 971 O O . TRP A 123 ? 0.1761 0.2537 0.2020 0.0120 -0.0216 0.0149 123 TRP A O 972 C CB . TRP A 123 ? 0.2028 0.2322 0.2006 -0.0289 -0.0280 -0.0135 123 TRP A CB 973 C CG . TRP A 123 ? 0.1242 0.2393 0.1962 0.0178 0.0037 -0.0135 123 TRP A CG 974 C CD1 . TRP A 123 ? 0.2324 0.2811 0.1896 0.0023 0.0209 -0.0037 123 TRP A CD1 975 C CD2 . TRP A 123 ? 0.1702 0.2744 0.2292 0.0369 -0.0142 0.0025 123 TRP A CD2 976 N NE1 . TRP A 123 ? 0.1857 0.2605 0.2204 0.0100 -0.0378 -0.0040 123 TRP A NE1 977 C CE2 . TRP A 123 ? 0.1487 0.2539 0.1821 0.0294 -0.0303 0.0376 123 TRP A CE2 978 C CE3 . TRP A 123 ? 0.1690 0.2617 0.1927 0.0132 0.0097 0.0239 123 TRP A CE3 979 C CZ2 . TRP A 123 ? 0.1607 0.2434 0.2213 0.0235 -0.0365 0.0211 123 TRP A CZ2 980 C CZ3 . TRP A 123 ? 0.2303 0.2448 0.1947 -0.0084 -0.0183 -0.0096 123 TRP A CZ3 981 C CH2 . TRP A 123 ? 0.1930 0.2694 0.2278 0.0112 -0.0210 -0.0198 123 TRP A CH2 982 N N . THR A 124 ? 0.1894 0.2091 0.1819 -0.0083 -0.0015 -0.0163 124 THR A N 983 C CA . THR A 124 ? 0.1909 0.2317 0.2116 -0.0350 0.0119 0.0046 124 THR A CA 984 C C . THR A 124 ? 0.1860 0.2425 0.1966 0.0217 -0.0093 0.0430 124 THR A C 985 O O . THR A 124 ? 0.1909 0.2665 0.2078 0.0165 -0.0252 0.0062 124 THR A O 986 C CB . THR A 124 ? 0.1847 0.2492 0.1869 -0.0205 0.0074 -0.0106 124 THR A CB 987 O OG1 . THR A 124 ? 0.1538 0.3091 0.2500 -0.0139 -0.0123 0.0288 124 THR A OG1 988 C CG2 . THR A 124 ? 0.2766 0.2921 0.2129 -0.0147 -0.0211 0.0016 124 THR A CG2 989 N N . VAL A 125 ? 0.2251 0.2081 0.2170 -0.0022 -0.0027 0.0415 125 VAL A N 990 C CA . VAL A 125 ? 0.2345 0.2123 0.2444 -0.0100 0.0022 0.0199 125 VAL A CA 991 C C . VAL A 125 ? 0.2323 0.2111 0.2426 0.0118 -0.0264 0.0274 125 VAL A C 992 O O . VAL A 125 ? 0.2289 0.3202 0.2677 0.0169 -0.0693 0.0353 125 VAL A O 993 C CB . VAL A 125 ? 0.1799 0.2197 0.2274 -0.0174 -0.0073 0.0159 125 VAL A CB 994 C CG1 . VAL A 125 ? 0.2214 0.2842 0.2804 -0.0612 0.0256 0.0134 125 VAL A CG1 995 C CG2 . VAL A 125 ? 0.1794 0.2382 0.2527 0.0190 0.0039 -0.0132 125 VAL A CG2 996 N N . THR A 126 ? 0.2187 0.2597 0.2298 -0.0190 -0.0147 0.0019 126 THR A N 997 C CA . THR A 126 ? 0.2594 0.2760 0.2232 -0.0151 0.0227 0.0009 126 THR A CA 998 C C . THR A 126 ? 0.2106 0.2756 0.1704 -0.0182 -0.0079 0.0158 126 THR A C 999 O O . THR A 126 ? 0.2354 0.2859 0.2273 -0.0403 -0.0493 0.0277 126 THR A O 1000 C CB . THR A 126 ? 0.2507 0.2464 0.2255 -0.0123 -0.0221 0.0142 126 THR A CB 1001 O OG1 . THR A 126 ? 0.2246 0.2940 0.2384 -0.0461 0.0021 -0.0104 126 THR A OG1 1002 C CG2 . THR A 126 ? 0.2481 0.2487 0.2061 0.0165 -0.0031 0.0310 126 THR A CG2 1003 N N . ASN A 127 ? 0.2338 0.2478 0.2219 -0.0604 0.0229 0.0187 127 ASN A N 1004 C CA . ASN A 127 ? 0.2300 0.2431 0.1983 -0.0413 -0.0040 -0.0033 127 ASN A CA 1005 C C . ASN A 127 ? 0.2542 0.2615 0.2930 -0.0098 -0.0144 -0.0241 127 ASN A C 1006 O O . ASN A 127 ? 0.2687 0.3015 0.3460 -0.0167 0.0061 -0.0311 127 ASN A O 1007 C CB . ASN A 127 ? 0.3050 0.2848 0.2479 -0.0794 0.0133 0.0197 127 ASN A CB 1008 C CG . ASN A 127 ? 0.2229 0.2710 0.2817 -0.0359 -0.0001 0.0031 127 ASN A CG 1009 O OD1 . ASN A 127 ? 0.2308 0.2677 0.2757 -0.0359 -0.0394 0.0172 127 ASN A OD1 1010 N ND2 . ASN A 127 ? 0.3425 0.4128 0.2737 -0.0497 -0.0278 0.0661 127 ASN A ND2 1011 N N . ASN A 128 ? 0.2082 0.2925 0.2516 -0.0487 -0.0240 0.0121 128 ASN A N 1012 C CA . ASN A 128 ? 0.2196 0.2874 0.2584 -0.0375 -0.0475 0.0171 128 ASN A CA 1013 C C . ASN A 128 ? 0.2499 0.2611 0.2441 -0.0066 -0.0160 -0.0131 128 ASN A C 1014 O O . ASN A 128 ? 0.2769 0.2541 0.3065 -0.0022 0.0205 0.0191 128 ASN A O 1015 C CB . ASN A 128 ? 0.2688 0.2986 0.3127 -0.0312 -0.0658 -0.0257 128 ASN A CB 1016 C CG . ASN A 128 ? 0.2557 0.2998 0.2706 0.0016 -0.0272 0.0128 128 ASN A CG 1017 O OD1 . ASN A 128 ? 0.3043 0.3025 0.2729 -0.0010 -0.0494 0.0005 128 ASN A OD1 1018 N ND2 . ASN A 128 ? 0.3369 0.3120 0.2742 -0.0322 -0.0370 -0.0015 128 ASN A ND2 1019 N N . VAL A 129 ? 0.2592 0.2788 0.2279 -0.0427 -0.0517 0.0153 129 VAL A N 1020 C CA . VAL A 129 ? 0.2368 0.2598 0.2009 -0.0195 -0.0281 0.0341 129 VAL A CA 1021 C C . VAL A 129 ? 0.2783 0.2589 0.2416 -0.0196 -0.0056 0.0154 129 VAL A C 1022 O O . VAL A 129 ? 0.2409 0.3474 0.2362 -0.0189 -0.0045 0.0258 129 VAL A O 1023 C CB . VAL A 129 ? 0.2663 0.3140 0.2807 -0.0314 -0.0185 -0.0003 129 VAL A CB 1024 C CG1 . VAL A 129 ? 0.3346 0.3387 0.2908 -0.0366 -0.0227 0.0472 129 VAL A CG1 1025 C CG2 . VAL A 129 ? 0.2681 0.3375 0.2681 -0.0332 -0.0083 0.0048 129 VAL A CG2 1026 N N . LYS A 130 ? 0.1953 0.2668 0.2402 -0.0216 0.0107 -0.0025 130 LYS A N 1027 C CA . LYS A 130 ? 0.1960 0.2397 0.2908 -0.0093 0.0294 0.0095 130 LYS A CA 1028 C C . LYS A 130 ? 0.2290 0.3071 0.2892 -0.0019 0.0114 0.0075 130 LYS A C 1029 O O . LYS A 130 ? 0.2045 0.3183 0.3251 -0.0233 0.0146 0.0304 130 LYS A O 1030 C CB . LYS A 130 ? 0.2373 0.2683 0.3244 -0.0052 0.0148 -0.0159 130 LYS A CB 1031 C CG . LYS A 130 ? 0.1985 0.4526 0.3675 -0.0224 0.0630 -0.0105 130 LYS A CG 1032 C CD . LYS A 130 ? 0.5610 0.4980 0.5429 0.0156 0.0122 -0.0017 130 LYS A CD 1033 C CE . LYS A 130 ? 0.5907 0.6711 0.6796 0.0136 -0.0079 0.0034 130 LYS A CE 1034 N NZ . LYS A 130 ? 0.6379 0.7176 0.6769 -0.0040 0.0003 -0.0183 130 LYS A NZ 1035 N N . PRO A 131 ? 0.2184 0.2737 0.2954 -0.0096 0.0021 0.0114 131 PRO A N 1036 C CA . PRO A 131 ? 0.2159 0.2835 0.2840 -0.0431 -0.0106 -0.0038 131 PRO A CA 1037 C C . PRO A 131 ? 0.2218 0.2881 0.2832 -0.0046 0.0058 0.0195 131 PRO A C 1038 O O . PRO A 131 ? 0.2346 0.2808 0.2803 -0.0071 0.0130 -0.0042 131 PRO A O 1039 C CB . PRO A 131 ? 0.2699 0.2993 0.2388 -0.0593 0.0146 0.0108 131 PRO A CB 1040 C CG . PRO A 131 ? 0.2929 0.3345 0.3550 -0.0223 0.0078 0.0218 131 PRO A CG 1041 C CD . PRO A 131 ? 0.2563 0.2981 0.2876 -0.0386 0.0036 0.0392 131 PRO A CD 1042 N N A ILE A 132 ? 0.2218 0.2555 0.2838 -0.0005 -0.0153 0.0174 132 ILE A N 1043 N N B ILE A 132 ? 0.2253 0.2724 0.2895 0.0035 -0.0139 0.0207 132 ILE A N 1044 C CA A ILE A 132 ? 0.2356 0.2656 0.2646 -0.0349 -0.0060 0.0176 132 ILE A CA 1045 C CA B ILE A 132 ? 0.2656 0.2718 0.2701 -0.0215 -0.0058 0.0140 132 ILE A CA 1046 C C A ILE A 132 ? 0.1731 0.2285 0.1928 -0.0220 -0.0196 -0.0029 132 ILE A C 1047 C C B ILE A 132 ? 0.2243 0.2533 0.2323 -0.0169 -0.0021 -0.0111 132 ILE A C 1048 O O A ILE A 132 ? 0.2375 0.2373 0.2249 -0.0016 0.0139 0.0092 132 ILE A O 1049 O O B ILE A 132 ? 0.2847 0.2779 0.2467 -0.0321 0.0309 0.0342 132 ILE A O 1050 C CB A ILE A 132 ? 0.3140 0.2970 0.2752 -0.0056 -0.0059 0.0126 132 ILE A CB 1051 C CB B ILE A 132 ? 0.2533 0.2869 0.2683 -0.0264 0.0134 0.0262 132 ILE A CB 1052 C CG1 A ILE A 132 ? 0.3489 0.3642 0.3542 -0.0268 0.0054 0.0086 132 ILE A CG1 1053 C CG1 B ILE A 132 ? 0.3239 0.2990 0.3139 -0.0136 0.0046 0.0034 132 ILE A CG1 1054 C CG2 A ILE A 132 ? 0.1798 0.3011 0.2665 0.0058 -0.0110 0.0041 132 ILE A CG2 1055 C CG2 B ILE A 132 ? 0.2744 0.3371 0.2589 -0.0015 -0.0024 -0.0020 132 ILE A CG2 1056 C CD1 A ILE A 132 ? 0.4341 0.3572 0.3983 -0.0152 -0.0075 0.0204 132 ILE A CD1 1057 C CD1 B ILE A 132 ? 0.2892 0.3309 0.2813 0.0045 -0.0260 0.0130 132 ILE A CD1 1058 N N . VAL A 133 ? 0.2369 0.2408 0.2410 -0.0122 0.0021 -0.0113 133 VAL A N 1059 C CA . VAL A 133 ? 0.2534 0.2491 0.2125 -0.0273 -0.0011 0.0209 133 VAL A CA 1060 C C . VAL A 133 ? 0.2042 0.2878 0.2392 -0.0249 0.0024 0.0092 133 VAL A C 1061 O O . VAL A 133 ? 0.2289 0.3446 0.2264 -0.0252 0.0127 -0.0133 133 VAL A O 1062 C CB . VAL A 133 ? 0.2676 0.2958 0.2694 -0.0019 -0.0070 0.0460 133 VAL A CB 1063 C CG1 . VAL A 133 ? 0.2602 0.2854 0.3591 -0.0434 -0.0053 -0.0192 133 VAL A CG1 1064 C CG2 . VAL A 133 ? 0.2522 0.2940 0.3152 -0.0117 -0.0050 0.0130 133 VAL A CG2 1065 N N . ALA A 134 ? 0.1864 0.2075 0.1939 -0.0295 0.0016 0.0033 134 ALA A N 1066 C CA . ALA A 134 ? 0.2026 0.2037 0.2175 0.0051 -0.0213 0.0168 134 ALA A CA 1067 C C . ALA A 134 ? 0.2164 0.2179 0.2041 0.0108 0.0077 -0.0125 134 ALA A C 1068 O O . ALA A 134 ? 0.2512 0.2819 0.1921 -0.0220 -0.0055 0.0134 134 ALA A O 1069 C CB . ALA A 134 ? 0.2773 0.2024 0.2288 0.0135 -0.0021 0.0238 134 ALA A CB 1070 N N A SER A 135 ? 0.2234 0.2319 0.2354 -0.0107 0.0011 -0.0075 135 SER A N 1071 N N B SER A 135 ? 0.1818 0.1946 0.2139 -0.0129 0.0122 -0.0031 135 SER A N 1072 C CA A SER A 135 ? 0.2215 0.2080 0.2398 -0.0037 0.0176 -0.0091 135 SER A CA 1073 C CA B SER A 135 ? 0.1596 0.1136 0.1777 -0.0062 0.0142 -0.0231 135 SER A CA 1074 C C A SER A 135 ? 0.2389 0.2146 0.1997 -0.0043 0.0206 0.0062 135 SER A C 1075 C C B SER A 135 ? 0.1848 0.0917 0.1661 0.0048 0.0131 0.0269 135 SER A C 1076 O O A SER A 135 ? 0.3017 0.2399 0.2274 0.0258 -0.0271 0.0154 135 SER A O 1077 O O B SER A 135 ? 0.1869 0.1531 0.1648 -0.0291 0.0286 0.0107 135 SER A O 1078 C CB A SER A 135 ? 0.2976 0.2749 0.2886 -0.0069 -0.0004 -0.0088 135 SER A CB 1079 C CB B SER A 135 ? 0.1666 0.1519 0.1457 0.0176 -0.0153 0.0441 135 SER A CB 1080 O OG A SER A 135 ? 0.3527 0.3891 0.2966 -0.0258 -0.0355 0.0059 135 SER A OG 1081 O OG B SER A 135 ? 0.1771 0.2101 0.1945 -0.0074 0.0174 -0.0388 135 SER A OG 1082 N N . ILE A 136 ? 0.1987 0.2194 0.2019 0.0261 0.0338 -0.0325 136 ILE A N 1083 C CA . ILE A 136 ? 0.1904 0.1858 0.1876 0.0064 -0.0071 0.0054 136 ILE A CA 1084 C C . ILE A 136 ? 0.2237 0.2253 0.2092 -0.0003 -0.0033 0.0308 136 ILE A C 1085 O O . ILE A 136 ? 0.2290 0.2119 0.2369 -0.0252 0.0045 0.0024 136 ILE A O 1086 C CB . ILE A 136 ? 0.1859 0.2164 0.2097 -0.0075 -0.0120 -0.0491 136 ILE A CB 1087 C CG1 . ILE A 136 ? 0.2353 0.2269 0.2155 -0.0471 -0.0564 0.0096 136 ILE A CG1 1088 C CG2 . ILE A 136 ? 0.2271 0.2444 0.2277 0.0435 0.0221 -0.0144 136 ILE A CG2 1089 C CD1 . ILE A 136 ? 0.2601 0.2568 0.2089 -0.0002 -0.0234 -0.0162 136 ILE A CD1 1090 N N . VAL A 137 ? 0.1762 0.1972 0.2108 0.0112 -0.0178 -0.0078 137 VAL A N 1091 C CA . VAL A 137 ? 0.2112 0.2139 0.1753 0.0127 -0.0362 -0.0163 137 VAL A CA 1092 C C . VAL A 137 ? 0.2201 0.1821 0.2323 0.0040 -0.0054 0.0224 137 VAL A C 1093 O O . VAL A 137 ? 0.2465 0.1915 0.2698 0.0113 0.0072 0.0074 137 VAL A O 1094 C CB . VAL A 137 ? 0.2589 0.2067 0.1730 0.0057 0.0058 -0.0062 137 VAL A CB 1095 C CG1 . VAL A 137 ? 0.2539 0.3168 0.2395 -0.0123 -0.0437 -0.0128 137 VAL A CG1 1096 C CG2 . VAL A 137 ? 0.2722 0.2634 0.2166 0.0091 0.0390 0.0022 137 VAL A CG2 1097 N N . GLY A 138 ? 0.2217 0.2145 0.1982 0.0081 -0.0007 -0.0276 138 GLY A N 1098 C CA . GLY A 138 ? 0.1957 0.2395 0.2722 -0.0062 0.0002 -0.0278 138 GLY A CA 1099 C C . GLY A 138 ? 0.2240 0.2197 0.2234 -0.0042 0.0099 -0.0006 138 GLY A C 1100 O O . GLY A 138 ? 0.2295 0.2999 0.2163 0.0057 -0.0138 -0.0350 138 GLY A O 1101 N N . TYR A 139 ? 0.1884 0.2768 0.2447 -0.0318 0.0089 -0.0424 139 TYR A N 1102 C CA . TYR A 139 ? 0.2082 0.2541 0.2539 0.0180 -0.0133 -0.0427 139 TYR A CA 1103 C C . TYR A 139 ? 0.2213 0.2352 0.2309 0.0066 -0.0250 -0.0238 139 TYR A C 1104 O O . TYR A 139 ? 0.2352 0.2261 0.2536 0.0056 -0.0027 -0.0403 139 TYR A O 1105 C CB . TYR A 139 ? 0.1900 0.3322 0.2729 0.0201 0.0062 -0.0338 139 TYR A CB 1106 C CG . TYR A 139 ? 0.2105 0.2318 0.2491 0.0155 -0.0047 -0.0284 139 TYR A CG 1107 C CD1 . TYR A 139 ? 0.2209 0.2984 0.2666 -0.0288 0.0083 -0.0284 139 TYR A CD1 1108 C CD2 . TYR A 139 ? 0.2604 0.2564 0.2688 0.0198 0.0101 -0.0043 139 TYR A CD2 1109 C CE1 . TYR A 139 ? 0.2201 0.3354 0.3311 -0.0103 -0.0175 -0.0143 139 TYR A CE1 1110 C CE2 . TYR A 139 ? 0.2323 0.2724 0.2614 0.0040 0.0081 -0.0674 139 TYR A CE2 1111 C CZ . TYR A 139 ? 0.2108 0.2948 0.2666 -0.0177 -0.0170 -0.0261 139 TYR A CZ 1112 O OH . TYR A 139 ? 0.2399 0.3947 0.3719 -0.0074 -0.0306 -0.0821 139 TYR A OH 1113 N N . LYS A 140 ? 0.2398 0.2853 0.2412 -0.0033 -0.0334 -0.0574 140 LYS A N 1114 C CA . LYS A 140 ? 0.2644 0.2605 0.2717 0.0090 -0.0198 -0.0332 140 LYS A CA 1115 C C . LYS A 140 ? 0.2088 0.2628 0.2686 -0.0369 -0.0176 -0.0405 140 LYS A C 1116 O O . LYS A 140 ? 0.2803 0.2550 0.2688 -0.0025 0.0012 -0.0454 140 LYS A O 1117 C CB . LYS A 140 ? 0.2831 0.2958 0.2631 -0.0088 -0.0151 -0.0618 140 LYS A CB 1118 C CG . LYS A 140 ? 0.3100 0.3086 0.3301 -0.0180 0.0409 -0.0270 140 LYS A CG 1119 C CD . LYS A 140 ? 0.3215 0.2798 0.4364 -0.0408 0.0371 -0.0546 140 LYS A CD 1120 C CE . LYS A 140 ? 0.4133 0.5029 0.5470 0.0271 0.0114 -0.0141 140 LYS A CE 1121 N NZ . LYS A 140 ? 0.6292 0.6566 0.5740 -0.0200 -0.0292 0.0064 140 LYS A NZ 1122 N N . GLU A 141 ? 0.2241 0.2516 0.2234 -0.0048 0.0038 -0.0199 141 GLU A N 1123 C CA . GLU A 141 ? 0.2398 0.2563 0.1820 0.0302 0.0065 0.0084 141 GLU A CA 1124 C C . GLU A 141 ? 0.2637 0.2195 0.2351 -0.0097 0.0101 0.0172 141 GLU A C 1125 O O . GLU A 141 ? 0.2744 0.2642 0.2680 0.0180 0.0364 -0.0003 141 GLU A O 1126 C CB . GLU A 141 ? 0.3510 0.2344 0.2109 0.0100 -0.0457 -0.0429 141 GLU A CB 1127 C CG . GLU A 141 ? 0.3348 0.2395 0.2633 0.0494 -0.0198 -0.0045 141 GLU A CG 1128 C CD . GLU A 141 ? 0.4490 0.4060 0.4556 -0.0271 -0.0133 0.0080 141 GLU A CD 1129 O OE1 . GLU A 141 ? 0.5609 0.4867 0.5845 0.0226 -0.0047 0.0133 141 GLU A OE1 1130 O OE2 . GLU A 141 ? 0.4538 0.4649 0.4484 -0.0158 0.0359 0.0421 141 GLU A OE2 1131 N N A MET A 142 ? 0.2373 0.2349 0.2064 -0.0005 0.0180 -0.0084 142 MET A N 1132 N N B MET A 142 ? 0.1992 0.2039 0.1890 0.0062 0.0150 -0.0081 142 MET A N 1133 C CA A MET A 142 ? 0.2832 0.2706 0.2394 0.0057 0.0026 0.0142 142 MET A CA 1134 C CA B MET A 142 ? 0.2203 0.2066 0.1769 -0.0065 0.0234 0.0163 142 MET A CA 1135 C C A MET A 142 ? 0.2462 0.2019 0.2202 0.0171 0.0255 -0.0169 142 MET A C 1136 C C B MET A 142 ? 0.2319 0.1822 0.2146 -0.0007 0.0118 -0.0173 142 MET A C 1137 O O A MET A 142 ? 0.2177 0.2237 0.2328 -0.0153 0.0412 0.0197 142 MET A O 1138 O O B MET A 142 ? 0.2285 0.1496 0.2054 0.0007 0.0007 0.0001 142 MET A O 1139 C CB A MET A 142 ? 0.3527 0.3289 0.2356 -0.0139 0.0091 0.0181 142 MET A CB 1140 C CB B MET A 142 ? 0.1839 0.1596 0.1837 -0.0380 0.0108 -0.0335 142 MET A CB 1141 C CG A MET A 142 ? 0.3990 0.4511 0.4235 -0.0059 -0.0112 -0.0060 142 MET A CG 1142 C CG B MET A 142 ? 0.1417 0.1417 0.2112 -0.0358 0.0006 -0.0237 142 MET A CG 1143 S SD A MET A 142 ? 0.6248 0.4830 0.5798 -0.0106 -0.0389 -0.0027 142 MET A SD 1144 S SD B MET A 142 ? 0.1634 0.1717 0.1959 -0.0088 0.0306 -0.0320 142 MET A SD 1145 C CE A MET A 142 ? 0.5216 0.5135 0.5329 -0.0129 -0.0060 -0.0131 142 MET A CE 1146 C CE B MET A 142 ? 0.1952 0.1801 0.1240 -0.0143 0.0147 0.0105 142 MET A CE 1147 N N . CYS A 143 ? 0.2254 0.2379 0.2041 -0.0169 -0.0364 -0.0228 143 CYS A N 1148 C CA . CYS A 143 ? 0.2048 0.2137 0.2097 0.0131 -0.0204 -0.0291 143 CYS A CA 1149 C C . CYS A 143 ? 0.2271 0.2301 0.2137 -0.0312 -0.0008 0.0083 143 CYS A C 1150 O O . CYS A 143 ? 0.2370 0.2146 0.2298 -0.0181 0.0209 0.0197 143 CYS A O 1151 C CB . CYS A 143 ? 0.2286 0.2548 0.2393 0.0295 0.0699 0.0086 143 CYS A CB 1152 S SG . CYS A 143 ? 0.2602 0.2388 0.2584 0.0000 0.0339 -0.0118 143 CYS A SG 1153 N N . LEU A 144 ? 0.2294 0.2266 0.2098 -0.0275 -0.0093 -0.0095 144 LEU A N 1154 C CA . LEU A 144 ? 0.2361 0.1807 0.2099 0.0095 -0.0164 -0.0133 144 LEU A CA 1155 C C . LEU A 144 ? 0.1829 0.1737 0.2410 -0.0178 0.0175 0.0030 144 LEU A C 1156 O O . LEU A 144 ? 0.1990 0.2249 0.2437 0.0200 0.0311 0.0289 144 LEU A O 1157 C CB . LEU A 144 ? 0.2437 0.1907 0.2125 -0.0065 0.0088 -0.0285 144 LEU A CB 1158 C CG . LEU A 144 ? 0.2190 0.2195 0.1909 -0.0189 0.0117 -0.0234 144 LEU A CG 1159 C CD1 . LEU A 144 ? 0.2128 0.2874 0.2601 0.0099 0.0265 0.0055 144 LEU A CD1 1160 C CD2 . LEU A 144 ? 0.2492 0.2552 0.2341 -0.0113 0.0012 -0.0211 144 LEU A CD2 1161 N N . GLN A 145 ? 0.2411 0.2217 0.2634 0.0170 0.0207 0.0595 145 GLN A N 1162 C CA . GLN A 145 ? 0.2668 0.2023 0.2424 -0.0080 -0.0088 0.0288 145 GLN A CA 1163 C C . GLN A 145 ? 0.2351 0.2476 0.2557 0.0126 0.0126 0.0298 145 GLN A C 1164 O O . GLN A 145 ? 0.2461 0.2221 0.2306 0.0096 0.0272 0.0226 145 GLN A O 1165 C CB . GLN A 145 ? 0.3189 0.2192 0.2595 0.0172 0.0123 0.0012 145 GLN A CB 1166 C CG . GLN A 145 ? 0.3288 0.2603 0.2462 0.0286 0.0207 -0.0049 145 GLN A CG 1167 C CD . GLN A 145 ? 0.4096 0.2249 0.3589 0.0020 0.0250 0.0166 145 GLN A CD 1168 O OE1 . GLN A 145 ? 0.2899 0.2069 0.3602 -0.0077 0.0175 0.0083 145 GLN A OE1 1169 N NE2 . GLN A 145 ? 0.4611 0.2776 0.3427 0.0027 0.0522 0.0148 145 GLN A NE2 1170 N N A SER A 146 ? 0.2335 0.2675 0.2433 -0.0003 -0.0090 0.0298 146 SER A N 1171 N N B SER A 146 ? 0.2173 0.2386 0.2012 0.0001 -0.0032 0.0342 146 SER A N 1172 C CA A SER A 146 ? 0.3009 0.2560 0.2731 0.0045 -0.0239 0.0245 146 SER A CA 1173 C CA B SER A 146 ? 0.2079 0.1914 0.2269 0.0128 -0.0346 0.0295 146 SER A CA 1174 C C A SER A 146 ? 0.2502 0.2605 0.2309 0.0097 -0.0069 0.0251 146 SER A C 1175 C C B SER A 146 ? 0.2634 0.2214 0.2210 -0.0070 0.0045 0.0232 146 SER A C 1176 O O A SER A 146 ? 0.2506 0.2596 0.2891 -0.0223 -0.0019 0.0307 146 SER A O 1177 O O B SER A 146 ? 0.2440 0.2222 0.2580 -0.0261 0.0339 0.0183 146 SER A O 1178 C CB A SER A 146 ? 0.2947 0.3028 0.3393 0.0023 0.0055 0.0259 146 SER A CB 1179 C CB B SER A 146 ? 0.1759 0.1640 0.1910 0.0000 -0.0114 0.0329 146 SER A CB 1180 O OG A SER A 146 ? 0.4095 0.4102 0.3421 -0.0252 -0.0086 0.0028 146 SER A OG 1181 O OG B SER A 146 ? 0.2430 0.1994 0.2282 0.0299 0.0304 0.0431 146 SER A OG 1182 N N . ASN A 147 ? 0.4139 0.1973 0.2627 -0.0137 0.0488 0.0554 147 ASN A N 1183 C CA . ASN A 147 ? 0.3379 0.2038 0.2997 -0.0132 0.0417 0.0279 147 ASN A CA 1184 C C . ASN A 147 ? 0.3561 0.2725 0.3422 0.0173 0.0129 -0.0028 147 ASN A C 1185 O O . ASN A 147 ? 0.2959 0.2953 0.3400 -0.0054 0.0556 0.0031 147 ASN A O 1186 C CB . ASN A 147 ? 0.3302 0.3164 0.3787 0.0144 0.0062 0.0316 147 ASN A CB 1187 C CG . ASN A 147 ? 0.3914 0.3351 0.3655 0.0289 0.0041 -0.0089 147 ASN A CG 1188 O OD1 . ASN A 147 ? 0.3501 0.2786 0.3726 -0.0422 0.0315 0.0262 147 ASN A OD1 1189 N ND2 . ASN A 147 ? 0.3422 0.2761 0.2941 0.0238 0.0177 0.0363 147 ASN A ND2 1190 N N . GLY A 148 ? 0.3659 0.2374 0.3525 -0.0057 0.0365 -0.0024 148 GLY A N 1191 C CA . GLY A 148 ? 0.3913 0.3601 0.3928 0.0149 0.0142 -0.0104 148 GLY A CA 1192 C C . GLY A 148 ? 0.3545 0.3252 0.3435 0.0006 -0.0008 0.0099 148 GLY A C 1193 O O . GLY A 148 ? 0.3647 0.2794 0.3232 -0.0233 0.0342 0.0181 148 GLY A O 1194 N N . GLU A 149 ? 0.3397 0.2816 0.3780 -0.0067 0.0197 0.0208 149 GLU A N 1195 C CA . GLU A 149 ? 0.2915 0.3694 0.3193 -0.0174 0.0104 0.0325 149 GLU A CA 1196 C C . GLU A 149 ? 0.2799 0.2480 0.2638 -0.0199 0.0339 -0.0021 149 GLU A C 1197 O O . GLU A 149 ? 0.3012 0.2486 0.4166 0.0089 0.0179 0.0714 149 GLU A O 1198 C CB . GLU A 149 ? 0.2798 0.2620 0.3072 0.0075 0.0128 0.0587 149 GLU A CB 1199 C CG . GLU A 149 ? 0.2505 0.3843 0.3318 0.0253 -0.0087 0.0150 149 GLU A CG 1200 C CD . GLU A 149 ? 0.3007 0.2915 0.3309 -0.0133 -0.0165 0.0490 149 GLU A CD 1201 O OE1 . GLU A 149 ? 0.4424 0.4299 0.4865 0.0262 0.0337 0.0564 149 GLU A OE1 1202 O OE2 . GLU A 149 ? 0.4744 0.4223 0.4953 -0.0119 -0.0461 -0.0035 149 GLU A OE2 1203 N N . ASN A 150 ? 0.2838 0.2819 0.2700 0.0178 0.0131 0.0408 150 ASN A N 1204 C CA . ASN A 150 ? 0.2645 0.2617 0.2261 0.0125 0.0135 0.0643 150 ASN A CA 1205 C C . ASN A 150 ? 0.3146 0.3373 0.2410 -0.0009 -0.0110 0.0275 150 ASN A C 1206 O O . ASN A 150 ? 0.3258 0.4845 0.2243 0.0289 -0.0082 -0.0033 150 ASN A O 1207 C CB . ASN A 150 ? 0.3448 0.3459 0.2600 -0.0071 -0.0218 0.0838 150 ASN A CB 1208 C CG . ASN A 150 ? 0.3349 0.2969 0.2693 0.0174 -0.0287 0.0362 150 ASN A CG 1209 O OD1 . ASN A 150 ? 0.4335 0.4750 0.4121 0.0281 0.0249 0.0788 150 ASN A OD1 1210 N ND2 . ASN A 150 ? 0.4243 0.3968 0.3411 -0.0407 -0.0577 0.0421 150 ASN A ND2 1211 N N A ASN A 151 ? 0.2956 0.2185 0.2110 0.0004 0.0077 0.0174 151 ASN A N 1212 N N B ASN A 151 ? 0.3025 0.2383 0.2366 -0.0019 0.0084 0.0103 151 ASN A N 1213 C CA A ASN A 151 ? 0.2482 0.1828 0.2069 0.0195 0.0157 0.0326 151 ASN A CA 1214 C CA B ASN A 151 ? 0.2957 0.2433 0.2682 0.0111 0.0024 0.0216 151 ASN A CA 1215 C C A ASN A 151 ? 0.2306 0.1363 0.1961 0.0401 0.0300 -0.0054 151 ASN A C 1216 C C B ASN A 151 ? 0.2845 0.2327 0.2939 -0.0089 0.0033 0.0214 151 ASN A C 1217 O O A ASN A 151 ? 0.2361 0.2196 0.2098 0.0168 0.0575 -0.0088 151 ASN A O 1218 O O B ASN A 151 ? 0.2272 0.1962 0.2352 -0.0059 0.0164 0.0200 151 ASN A O 1219 C CB A ASN A 151 ? 0.2472 0.1693 0.2797 -0.0022 0.0036 0.0011 151 ASN A CB 1220 C CB B ASN A 151 ? 0.2716 0.2574 0.3067 0.0169 -0.0148 -0.0057 151 ASN A CB 1221 C CG A ASN A 151 ? 0.2467 0.1841 0.2160 -0.0279 -0.0124 0.0224 151 ASN A CG 1222 C CG B ASN A 151 ? 0.3754 0.3017 0.3307 -0.0037 0.0076 0.0290 151 ASN A CG 1223 O OD1 A ASN A 151 ? 0.3064 0.1954 0.2672 0.0045 0.0099 0.0086 151 ASN A OD1 1224 O OD1 B ASN A 151 ? 0.3382 0.3266 0.3027 0.0145 0.0117 0.0117 151 ASN A OD1 1225 N ND2 A ASN A 151 ? 0.2707 0.2176 0.2764 0.0249 0.0081 -0.0190 151 ASN A ND2 1226 N ND2 B ASN A 151 ? 0.3694 0.3274 0.3030 -0.0176 0.0312 0.0266 151 ASN A ND2 1227 N N . GLY A 152 ? 0.2750 0.2136 0.2347 0.0015 -0.0007 0.0272 152 GLY A N 1228 C CA . GLY A 152 ? 0.2933 0.2234 0.2132 0.0420 0.0418 0.0128 152 GLY A CA 1229 C C . GLY A 152 ? 0.3088 0.2589 0.2421 0.0197 0.0318 0.0393 152 GLY A C 1230 O O . GLY A 152 ? 0.4438 0.2315 0.2922 0.0312 0.0374 0.0406 152 GLY A O 1231 N N . VAL A 153 ? 0.2639 0.2265 0.1945 -0.0126 0.0427 0.0285 153 VAL A N 1232 C CA . VAL A 153 ? 0.2416 0.2289 0.1747 0.0031 0.0252 0.0086 153 VAL A CA 1233 C C . VAL A 153 ? 0.2894 0.2357 0.2586 0.0076 -0.0020 0.0017 153 VAL A C 1234 O O . VAL A 153 ? 0.2751 0.2904 0.2446 0.0222 0.0251 0.0075 153 VAL A O 1235 C CB . VAL A 153 ? 0.2064 0.2474 0.2718 -0.0016 -0.0099 0.0078 153 VAL A CB 1236 C CG1 . VAL A 153 ? 0.2022 0.2352 0.2354 -0.0246 -0.0081 0.0291 153 VAL A CG1 1237 C CG2 . VAL A 153 ? 0.2655 0.2196 0.2578 0.0178 0.0286 0.0089 153 VAL A CG2 1238 N N . TRP A 154 ? 0.2309 0.2433 0.2295 -0.0270 -0.0222 0.0121 154 TRP A N 1239 C CA . TRP A 154 ? 0.1831 0.2766 0.2043 -0.0330 -0.0100 0.0015 154 TRP A CA 1240 C C . TRP A 154 ? 0.2415 0.2427 0.2055 -0.0078 -0.0018 -0.0255 154 TRP A C 1241 O O . TRP A 154 ? 0.2263 0.2315 0.2424 -0.0028 0.0096 0.0064 154 TRP A O 1242 C CB . TRP A 154 ? 0.3044 0.3404 0.2626 -0.0295 0.0323 0.0171 154 TRP A CB 1243 C CG . TRP A 154 ? 0.2863 0.3271 0.3111 -0.0402 0.0184 0.0018 154 TRP A CG 1244 C CD1 . TRP A 154 ? 0.3455 0.3407 0.4080 -0.0035 0.0017 0.0030 154 TRP A CD1 1245 C CD2 . TRP A 154 ? 0.4060 0.3601 0.3056 -0.0106 0.0205 0.0024 154 TRP A CD2 1246 N NE1 . TRP A 154 ? 0.4323 0.3311 0.4009 0.0031 0.0283 0.0329 154 TRP A NE1 1247 C CE2 . TRP A 154 ? 0.4078 0.3659 0.4264 0.0103 -0.0224 0.0116 154 TRP A CE2 1248 C CE3 . TRP A 154 ? 0.2280 0.4285 0.3379 -0.0176 0.0048 0.0129 154 TRP A CE3 1249 C CZ2 . TRP A 154 ? 0.5204 0.4134 0.4117 -0.0074 -0.0103 0.0232 154 TRP A CZ2 1250 C CZ3 . TRP A 154 ? 0.4210 0.3919 0.3888 0.0257 0.0327 0.0264 154 TRP A CZ3 1251 C CH2 . TRP A 154 ? 0.4205 0.3584 0.3817 0.0007 0.0488 0.0541 154 TRP A CH2 1252 N N . MET A 155 ? 0.2349 0.1979 0.2171 -0.0117 -0.0024 0.0024 155 MET A N 1253 C CA . MET A 155 ? 0.2643 0.1819 0.2076 -0.0067 0.0036 -0.0293 155 MET A CA 1254 C C . MET A 155 ? 0.2499 0.2201 0.2559 -0.0132 0.0381 -0.0505 155 MET A C 1255 O O . MET A 155 ? 0.2681 0.2775 0.2880 -0.0240 0.0495 -0.0233 155 MET A O 1256 C CB . MET A 155 ? 0.2342 0.2007 0.2910 0.0212 -0.0149 -0.0152 155 MET A CB 1257 C CG . MET A 155 ? 0.2013 0.1913 0.2847 0.0263 0.0344 -0.0100 155 MET A CG 1258 S SD . MET A 155 ? 0.2614 0.2233 0.2570 -0.0050 0.0285 -0.0292 155 MET A SD 1259 C CE . MET A 155 ? 0.3214 0.2357 0.2254 0.0146 0.0181 -0.0128 155 MET A CE 1260 N N A GLU A 156 ? 0.2546 0.2064 0.2496 0.0176 0.0343 -0.0154 156 GLU A N 1261 N N B GLU A 156 ? 0.2330 0.1948 0.2460 0.0252 0.0358 -0.0172 156 GLU A N 1262 C CA A GLU A 156 ? 0.2369 0.2313 0.2058 0.0146 -0.0021 -0.0286 156 GLU A CA 1263 C CA B GLU A 156 ? 0.2445 0.2223 0.2045 0.0070 0.0076 -0.0269 156 GLU A CA 1264 C C A GLU A 156 ? 0.3019 0.3029 0.2886 0.0233 0.0096 -0.0035 156 GLU A C 1265 C C B GLU A 156 ? 0.2383 0.2390 0.2593 0.0040 0.0068 0.0117 156 GLU A C 1266 O O A GLU A 156 ? 0.2164 0.1271 0.2405 0.0149 -0.0099 -0.0026 156 GLU A O 1267 O O B GLU A 156 ? 0.1814 0.0865 0.2163 -0.0368 0.0107 -0.0442 156 GLU A O 1268 C CB A GLU A 156 ? 0.2601 0.1946 0.2010 -0.0099 0.0093 -0.0213 156 GLU A CB 1269 C CB B GLU A 156 ? 0.2825 0.2353 0.2383 -0.0104 0.0003 -0.0051 156 GLU A CB 1270 C CG A GLU A 156 ? 0.2383 0.2141 0.1107 0.0132 -0.0095 -0.0454 156 GLU A CG 1271 C CG B GLU A 156 ? 0.2697 0.2912 0.2443 0.0093 -0.0084 0.0081 156 GLU A CG 1272 C CD A GLU A 156 ? 0.3008 0.2881 0.3067 -0.0215 0.0135 -0.0121 156 GLU A CD 1273 C CD B GLU A 156 ? 0.3578 0.3495 0.3250 -0.0406 0.0075 -0.0005 156 GLU A CD 1274 O OE1 A GLU A 156 ? 0.2874 0.1781 0.2804 -0.0232 0.0458 0.0215 156 GLU A OE1 1275 O OE1 B GLU A 156 ? 0.3838 0.2928 0.3274 -0.0079 0.0219 0.0314 156 GLU A OE1 1276 O OE2 A GLU A 156 ? 0.2970 0.2753 0.2925 -0.0302 -0.0094 0.0080 156 GLU A OE2 1277 O OE2 B GLU A 156 ? 0.3483 0.2939 0.3321 0.0066 0.0019 -0.0268 156 GLU A OE2 1278 N N . ASP A 157 ? 0.2674 0.2119 0.2054 0.0079 -0.0305 -0.0280 157 ASP A N 1279 C CA . ASP A 157 ? 0.2334 0.2064 0.2377 -0.0015 0.0175 -0.0455 157 ASP A CA 1280 C C . ASP A 157 ? 0.2320 0.2255 0.2401 -0.0230 -0.0155 -0.0054 157 ASP A C 1281 O O . ASP A 157 ? 0.2360 0.2404 0.3018 0.0055 0.0018 -0.0155 157 ASP A O 1282 C CB . ASP A 157 ? 0.2550 0.1994 0.3214 -0.0362 -0.0054 -0.0407 157 ASP A CB 1283 C CG . ASP A 157 ? 0.2751 0.2932 0.3138 -0.0198 -0.0148 0.0075 157 ASP A CG 1284 O OD1 . ASP A 157 ? 0.2784 0.3315 0.3189 -0.0168 -0.0249 -0.0434 157 ASP A OD1 1285 O OD2 . ASP A 157 ? 0.3896 0.2671 0.4599 -0.0211 -0.0101 0.0025 157 ASP A OD2 1286 N N . CYS A 158 ? 0.2361 0.2015 0.2194 -0.0085 0.0068 -0.0144 158 CYS A N 1287 C CA . CYS A 158 ? 0.2080 0.1689 0.2968 0.0009 0.0283 -0.0147 158 CYS A CA 1288 C C . CYS A 158 ? 0.2825 0.1879 0.3341 0.0042 -0.0055 0.0030 158 CYS A C 1289 O O . CYS A 158 ? 0.2924 0.2434 0.3901 0.0553 0.0067 -0.0690 158 CYS A O 1290 C CB . CYS A 158 ? 0.2620 0.1931 0.2426 0.0306 0.0081 0.0190 158 CYS A CB 1291 S SG . CYS A 158 ? 0.2601 0.2148 0.2405 0.0157 0.0201 0.0003 158 CYS A SG 1292 N N . GLU A 159 ? 0.2576 0.2484 0.3449 0.0438 0.0150 -0.0221 159 GLU A N 1293 C CA . GLU A 159 ? 0.1829 0.2763 0.4415 0.0342 0.0226 0.0092 159 GLU A CA 1294 C C . GLU A 159 ? 0.2333 0.2424 0.3684 0.0124 0.0135 -0.0495 159 GLU A C 1295 O O . GLU A 159 ? 0.3081 0.2478 0.3733 -0.0207 0.0250 -0.0374 159 GLU A O 1296 C CB . GLU A 159 ? 0.4063 0.2933 0.4319 0.0171 0.0201 -0.0128 159 GLU A CB 1297 N N . ALA A 160 ? 0.3158 0.2688 0.4031 -0.0170 0.0291 -0.0125 160 ALA A N 1298 C CA . ALA A 160 ? 0.3313 0.3772 0.4017 -0.0041 0.0366 -0.0360 160 ALA A CA 1299 C C . ALA A 160 ? 0.2936 0.4028 0.3640 -0.0144 0.0441 -0.0347 160 ALA A C 1300 O O . ALA A 160 ? 0.3272 0.4335 0.4151 -0.0189 0.0302 -0.1202 160 ALA A O 1301 C CB . ALA A 160 ? 0.4403 0.3999 0.3905 -0.0005 0.0223 -0.0127 160 ALA A CB 1302 N N . THR A 161 ? 0.3847 0.3297 0.4265 0.0242 0.0021 -0.0357 161 THR A N 1303 C CA . THR A 161 ? 0.3786 0.2914 0.4046 0.0071 -0.0109 -0.0667 161 THR A CA 1304 C C . THR A 161 ? 0.3153 0.2795 0.3816 0.0141 -0.0390 -0.0201 161 THR A C 1305 O O . THR A 161 ? 0.4047 0.2918 0.4444 0.0730 -0.0431 -0.0965 161 THR A O 1306 C CB . THR A 161 ? 0.4048 0.2920 0.4632 0.0224 0.0196 -0.0156 161 THR A CB 1307 O OG1 . THR A 161 ? 0.4505 0.3599 0.4205 -0.0121 -0.0009 0.0169 161 THR A OG1 1308 C CG2 . THR A 161 ? 0.4654 0.3691 0.3531 0.0298 -0.0195 0.0083 161 THR A CG2 1309 N N . SER A 162 ? 0.2718 0.2035 0.4044 0.0389 0.0007 -0.0507 162 SER A N 1310 C CA . SER A 162 ? 0.3013 0.2553 0.4116 0.0074 0.0212 -0.0242 162 SER A CA 1311 C C . SER A 162 ? 0.2551 0.2716 0.2999 -0.0021 0.0029 0.0285 162 SER A C 1312 O O . SER A 162 ? 0.2554 0.2218 0.3067 0.0180 0.0218 -0.0046 162 SER A O 1313 C CB . SER A 162 ? 0.2947 0.1717 0.3738 -0.0316 -0.0040 -0.0271 162 SER A CB 1314 O OG . SER A 162 ? 0.3506 0.3502 0.3846 0.0008 -0.0224 -0.0133 162 SER A OG 1315 N N . LEU A 163 ? 0.3161 0.2518 0.3649 0.0430 0.0094 0.0440 163 LEU A N 1316 C CA . LEU A 163 ? 0.2597 0.2996 0.2889 0.0563 0.0088 0.0504 163 LEU A CA 1317 C C . LEU A 163 ? 0.2528 0.2791 0.2681 -0.0283 -0.0177 -0.0055 163 LEU A C 1318 O O . LEU A 163 ? 0.2648 0.2974 0.2854 0.0156 0.0448 0.0238 163 LEU A O 1319 C CB . LEU A 163 ? 0.3119 0.3860 0.3620 0.0488 -0.0135 0.0434 163 LEU A CB 1320 C CG . LEU A 163 ? 0.4351 0.4516 0.4438 0.0689 0.0199 0.0166 163 LEU A CG 1321 C CD1 . LEU A 163 ? 0.4185 0.5199 0.4928 0.0436 0.0004 0.0120 163 LEU A CD1 1322 C CD2 . LEU A 163 ? 0.3149 0.3988 0.4514 0.0301 0.0119 0.0125 163 LEU A CD2 1323 N N . GLN A 164 ? 0.3024 0.3052 0.3128 0.0387 0.0446 0.0426 164 GLN A N 1324 C CA . GLN A 164 ? 0.2853 0.2998 0.3339 0.0763 0.0288 0.0599 164 GLN A CA 1325 C C . GLN A 164 ? 0.2413 0.2471 0.2838 0.0296 0.0165 0.0539 164 GLN A C 1326 O O . GLN A 164 ? 0.2960 0.2910 0.2799 0.0128 0.0538 0.0677 164 GLN A O 1327 C CB . GLN A 164 ? 0.3604 0.3753 0.3672 0.0069 0.0396 0.0514 164 GLN A CB 1328 C CG . GLN A 164 ? 0.4572 0.3930 0.3847 0.0372 0.0347 0.0447 164 GLN A CG 1329 C CD . GLN A 164 ? 0.4368 0.4247 0.3497 -0.0016 0.0077 0.0404 164 GLN A CD 1330 O OE1 . GLN A 164 ? 0.5479 0.3533 0.5429 -0.0211 0.0377 -0.0345 164 GLN A OE1 1331 N NE2 . GLN A 164 ? 0.3999 0.3719 0.2957 -0.0580 -0.0005 0.0442 164 GLN A NE2 1332 N N . GLN A 165 ? 0.2364 0.2687 0.2541 0.0201 -0.0152 0.0487 165 GLN A N 1333 C CA . GLN A 165 ? 0.2192 0.2526 0.2127 -0.0094 -0.0224 0.0216 165 GLN A CA 1334 C C . GLN A 165 ? 0.2466 0.2106 0.2536 0.0008 0.0082 0.0148 165 GLN A C 1335 O O . GLN A 165 ? 0.2124 0.2186 0.2561 -0.0155 0.0129 0.0455 165 GLN A O 1336 C CB . GLN A 165 ? 0.2003 0.1939 0.2506 -0.0062 -0.0134 -0.0185 165 GLN A CB 1337 C CG . GLN A 165 ? 0.2240 0.2044 0.2897 -0.0272 -0.0156 0.0180 165 GLN A CG 1338 C CD . GLN A 165 ? 0.2831 0.2713 0.2659 -0.0057 -0.0037 0.0038 165 GLN A CD 1339 O OE1 . GLN A 165 ? 0.2539 0.1809 0.2814 -0.0147 0.0064 0.0085 165 GLN A OE1 1340 N NE2 . GLN A 165 ? 0.2478 0.2387 0.3292 -0.0041 0.0197 -0.0139 165 GLN A NE2 1341 N N . GLN A 166 ? 0.2133 0.2300 0.2391 -0.0143 0.0411 -0.0005 166 GLN A N 1342 C CA . GLN A 166 ? 0.1982 0.2004 0.2156 0.0000 0.0058 0.0085 166 GLN A CA 1343 C C . GLN A 166 ? 0.1778 0.2254 0.2533 -0.0348 -0.0054 0.0026 166 GLN A C 1344 O O . GLN A 166 ? 0.2290 0.2438 0.2443 0.0181 -0.0032 0.0296 166 GLN A O 1345 C CB . GLN A 166 ? 0.2326 0.2558 0.2489 0.0347 0.0135 -0.0231 166 GLN A CB 1346 C CG . GLN A 166 ? 0.1985 0.1970 0.2429 0.0336 0.0329 -0.0026 166 GLN A CG 1347 C CD . GLN A 166 ? 0.2612 0.2751 0.2555 0.0248 0.0490 0.0106 166 GLN A CD 1348 O OE1 . GLN A 166 ? 0.3140 0.3395 0.3308 0.0438 0.0070 -0.0047 166 GLN A OE1 1349 N NE2 . GLN A 166 ? 0.3282 0.2342 0.3227 0.0012 -0.0186 0.0192 166 GLN A NE2 1350 N N . TRP A 167 ? 0.1894 0.1814 0.2121 -0.0260 0.0166 -0.0005 167 TRP A N 1351 C CA . TRP A 167 ? 0.1366 0.2460 0.2346 -0.0080 0.0058 -0.0245 167 TRP A CA 1352 C C . TRP A 167 ? 0.2158 0.2466 0.2252 -0.0297 -0.0036 0.0000 167 TRP A C 1353 O O . TRP A 167 ? 0.2534 0.3177 0.2148 -0.0171 0.0111 0.0217 167 TRP A O 1354 C CB . TRP A 167 ? 0.1919 0.2408 0.2532 0.0280 0.0051 0.0557 167 TRP A CB 1355 C CG . TRP A 167 ? 0.2253 0.2185 0.2217 0.0009 0.0062 0.0225 167 TRP A CG 1356 C CD1 . TRP A 167 ? 0.1944 0.2125 0.2444 -0.0013 0.0066 -0.0064 167 TRP A CD1 1357 C CD2 . TRP A 167 ? 0.2116 0.1872 0.1974 -0.0037 -0.0034 0.0042 167 TRP A CD2 1358 N NE1 . TRP A 167 ? 0.1909 0.2451 0.2348 -0.0058 0.0162 0.0073 167 TRP A NE1 1359 C CE2 . TRP A 167 ? 0.2332 0.1929 0.2088 0.0020 0.0024 0.0346 167 TRP A CE2 1360 C CE3 . TRP A 167 ? 0.2052 0.2100 0.2036 -0.0110 0.0108 0.0317 167 TRP A CE3 1361 C CZ2 . TRP A 167 ? 0.2191 0.2907 0.2384 -0.0012 0.0145 0.0320 167 TRP A CZ2 1362 C CZ3 . TRP A 167 ? 0.2188 0.2206 0.2522 -0.0252 0.0089 0.0196 167 TRP A CZ3 1363 C CH2 . TRP A 167 ? 0.2002 0.1817 0.2610 -0.0032 0.0129 -0.0020 167 TRP A CH2 1364 N N . ALA A 168 ? 0.1987 0.2401 0.2230 -0.0138 -0.0107 0.0226 168 ALA A N 1365 C CA . ALA A 168 ? 0.1924 0.2470 0.2879 -0.0130 -0.0132 0.0092 168 ALA A CA 1366 C C . ALA A 168 ? 0.2025 0.2599 0.2149 0.0206 -0.0238 0.0142 168 ALA A C 1367 O O . ALA A 168 ? 0.2176 0.2480 0.2140 -0.0310 0.0058 -0.0034 168 ALA A O 1368 C CB . ALA A 168 ? 0.1606 0.2314 0.2674 0.0261 -0.0094 -0.0082 168 ALA A CB 1369 N N . LEU A 169 ? 0.2143 0.2315 0.2463 0.0057 -0.0132 0.0178 169 LEU A N 1370 C CA . LEU A 169 ? 0.2205 0.2075 0.2252 0.0047 -0.0308 -0.0148 169 LEU A CA 1371 C C . LEU A 169 ? 0.2057 0.2483 0.1911 -0.0013 0.0053 0.0017 169 LEU A C 1372 O O . LEU A 169 ? 0.2221 0.3020 0.1961 -0.0399 -0.0045 0.0227 169 LEU A O 1373 C CB . LEU A 169 ? 0.2118 0.2142 0.2550 -0.0118 -0.0231 0.0104 169 LEU A CB 1374 C CG . LEU A 169 ? 0.2398 0.2963 0.2374 -0.0437 -0.0153 0.0277 169 LEU A CG 1375 C CD1 . LEU A 169 ? 0.3347 0.3057 0.2687 0.0228 -0.0648 -0.0005 169 LEU A CD1 1376 C CD2 . LEU A 169 ? 0.2520 0.2830 0.2854 0.0068 0.0469 0.0336 169 LEU A CD2 1377 N N . TYR A 170 ? 0.1872 0.2237 0.2199 -0.0015 -0.0399 -0.0037 170 TYR A N 1378 C CA . TYR A 170 ? 0.1806 0.1841 0.1855 -0.0229 -0.0072 0.0133 170 TYR A CA 1379 C C . TYR A 170 ? 0.2058 0.2042 0.1875 -0.0072 0.0073 0.0072 170 TYR A C 1380 O O . TYR A 170 ? 0.1926 0.2596 0.2275 0.0105 0.0210 0.0004 170 TYR A O 1381 C CB . TYR A 170 ? 0.1969 0.2103 0.2138 -0.0057 -0.0176 0.0372 170 TYR A CB 1382 C CG . TYR A 170 ? 0.1825 0.2289 0.2261 0.0128 0.0100 0.0196 170 TYR A CG 1383 C CD1 . TYR A 170 ? 0.2239 0.2021 0.2536 0.0000 -0.0052 0.0402 170 TYR A CD1 1384 C CD2 . TYR A 170 ? 0.2527 0.2828 0.2501 -0.0198 -0.0041 -0.0273 170 TYR A CD2 1385 C CE1 . TYR A 170 ? 0.1989 0.2241 0.2399 0.0010 -0.0275 0.0079 170 TYR A CE1 1386 C CE2 . TYR A 170 ? 0.3220 0.2797 0.3201 0.0195 -0.0232 -0.0172 170 TYR A CE2 1387 C CZ . TYR A 170 ? 0.1868 0.2564 0.3085 -0.0009 -0.0112 0.0172 170 TYR A CZ 1388 O OH . TYR A 170 ? 0.2727 0.2680 0.3814 0.0235 -0.0348 0.0147 170 TYR A OH 1389 N N . GLY A 171 ? 0.2375 0.2221 0.2486 -0.0370 0.0172 0.0120 171 GLY A N 1390 C CA . GLY A 171 ? 0.1957 0.2347 0.2216 0.0043 -0.0028 -0.0319 171 GLY A CA 1391 C C . GLY A 171 ? 0.1774 0.2020 0.2164 -0.0358 0.0097 -0.0070 171 GLY A C 1392 O O . GLY A 171 ? 0.1911 0.1861 0.2513 0.0000 -0.0165 0.0117 171 GLY A O 1393 N N . ASP A 172 ? 0.1844 0.2383 0.2118 -0.0145 -0.0050 0.0131 172 ASP A N 1394 C CA . ASP A 172 ? 0.1646 0.2533 0.1895 -0.0014 -0.0303 -0.0184 172 ASP A CA 1395 C C . ASP A 172 ? 0.1629 0.2318 0.1854 -0.0021 -0.0081 -0.0110 172 ASP A C 1396 O O . ASP A 172 ? 0.1782 0.2551 0.2074 0.0072 -0.0030 0.0031 172 ASP A O 1397 C CB . ASP A 172 ? 0.2281 0.2182 0.1970 0.0240 -0.0179 -0.0094 172 ASP A CB 1398 C CG . ASP A 172 ? 0.1555 0.2398 0.2286 0.0297 -0.0035 -0.0052 172 ASP A CG 1399 O OD1 . ASP A 172 ? 0.1805 0.2480 0.2111 -0.0005 -0.0194 0.0151 172 ASP A OD1 1400 O OD2 . ASP A 172 ? 0.1761 0.2471 0.2444 -0.0073 -0.0152 0.0396 172 ASP A OD2 1401 N N . ARG A 173 ? 0.1476 0.1783 0.1869 -0.0116 -0.0221 -0.0061 173 ARG A N 1402 C CA . ARG A 173 ? 0.1529 0.1641 0.2552 0.0109 -0.0219 0.0321 173 ARG A CA 1403 C C . ARG A 173 ? 0.2035 0.2196 0.2323 -0.0044 0.0196 0.0216 173 ARG A C 1404 O O . ARG A 173 ? 0.2034 0.2160 0.2709 0.0172 0.0393 0.0167 173 ARG A O 1405 C CB . ARG A 173 ? 0.1999 0.1643 0.2611 -0.0008 -0.0221 0.0300 173 ARG A CB 1406 C CG . ARG A 173 ? 0.2245 0.1740 0.2379 -0.0118 0.0056 0.0330 173 ARG A CG 1407 C CD . ARG A 173 ? 0.2140 0.2265 0.2328 -0.0471 -0.0192 0.0627 173 ARG A CD 1408 N NE . ARG A 173 ? 0.2150 0.2067 0.2602 -0.0185 0.0170 0.0316 173 ARG A NE 1409 C CZ . ARG A 173 ? 0.2788 0.3393 0.3227 -0.0145 -0.0315 0.0521 173 ARG A CZ 1410 N NH1 . ARG A 173 ? 0.2968 0.3230 0.2620 -0.0623 -0.0618 0.0129 173 ARG A NH1 1411 N NH2 . ARG A 173 ? 0.3251 0.3533 0.3603 -0.0572 -0.0896 0.0957 173 ARG A NH2 1412 N N . THR A 174 ? 0.1699 0.2000 0.2159 -0.0010 -0.0117 0.0098 174 THR A N 1413 C CA . THR A 174 ? 0.2050 0.1730 0.2379 -0.0042 -0.0253 0.0268 174 THR A CA 1414 C C . THR A 174 ? 0.1435 0.2119 0.2300 0.0512 0.0078 0.0069 174 THR A C 1415 O O . THR A 174 ? 0.2309 0.2175 0.2262 -0.0246 0.0200 0.0232 174 THR A O 1416 C CB . THR A 174 ? 0.1449 0.1921 0.2018 0.0293 0.0257 0.0071 174 THR A CB 1417 O OG1 . THR A 174 ? 0.1923 0.2095 0.1845 0.0310 0.0365 0.0243 174 THR A OG1 1418 C CG2 . THR A 174 ? 0.1890 0.2016 0.2172 0.0088 -0.0262 -0.0140 174 THR A CG2 1419 N N . ILE A 175 ? 0.1631 0.2249 0.2248 -0.0095 -0.0028 0.0070 175 ILE A N 1420 C CA . ILE A 175 ? 0.1475 0.1957 0.1978 0.0110 0.0098 0.0046 175 ILE A CA 1421 C C . ILE A 175 ? 0.2021 0.2082 0.2227 0.0042 0.0021 0.0145 175 ILE A C 1422 O O . ILE A 175 ? 0.1986 0.2100 0.2241 0.0159 0.0096 0.0270 175 ILE A O 1423 C CB . ILE A 175 ? 0.1476 0.1986 0.1796 -0.0001 0.0037 0.0068 175 ILE A CB 1424 C CG1 . ILE A 175 ? 0.1488 0.1835 0.2243 0.0246 -0.0168 0.0106 175 ILE A CG1 1425 C CG2 . ILE A 175 ? 0.2188 0.2170 0.2150 0.0290 -0.0317 -0.0249 175 ILE A CG2 1426 C CD1 . ILE A 175 ? 0.1905 0.2385 0.2554 0.0469 -0.0245 -0.0081 175 ILE A CD1 1427 N N . ARG A 176 ? 0.2040 0.2113 0.2124 0.0390 0.0051 0.0391 176 ARG A N 1428 C CA . ARG A 176 ? 0.1612 0.2041 0.2334 0.0173 -0.0264 0.0169 176 ARG A CA 1429 C C . ARG A 176 ? 0.2275 0.2297 0.2354 -0.0132 -0.0091 0.0276 176 ARG A C 1430 O O . ARG A 176 ? 0.2127 0.2071 0.2325 0.0102 -0.0022 0.0041 176 ARG A O 1431 C CB . ARG A 176 ? 0.1633 0.2304 0.2316 -0.0136 -0.0375 -0.0091 176 ARG A CB 1432 C CG . ARG A 176 ? 0.1878 0.2509 0.1858 0.0179 -0.0265 -0.0202 176 ARG A CG 1433 C CD . ARG A 176 ? 0.2252 0.2575 0.2195 0.0112 -0.0562 -0.0037 176 ARG A CD 1434 N NE . ARG A 176 ? 0.1687 0.2587 0.2143 0.0149 0.0050 -0.0143 176 ARG A NE 1435 C CZ . ARG A 176 ? 0.2134 0.2056 0.2525 0.0038 -0.0277 -0.0123 176 ARG A CZ 1436 N NH1 . ARG A 176 ? 0.1724 0.2363 0.2197 -0.0222 -0.0018 -0.0069 176 ARG A NH1 1437 N NH2 . ARG A 176 ? 0.2013 0.2137 0.2361 0.0283 -0.0038 0.0368 176 ARG A NH2 1438 N N . VAL A 177 ? 0.1716 0.1840 0.2509 0.0141 -0.0166 0.0544 177 VAL A N 1439 C CA . VAL A 177 ? 0.2566 0.2042 0.2267 0.0112 0.0288 0.0384 177 VAL A CA 1440 C C . VAL A 177 ? 0.2547 0.2298 0.2320 0.0103 -0.0063 0.0273 177 VAL A C 1441 O O . VAL A 177 ? 0.2343 0.2455 0.2520 0.0036 0.0049 0.0183 177 VAL A O 1442 C CB . VAL A 177 ? 0.2341 0.2373 0.2686 0.0068 0.0353 0.0310 177 VAL A CB 1443 C CG1 . VAL A 177 ? 0.2464 0.2370 0.3782 0.0461 0.0148 0.0307 177 VAL A CG1 1444 C CG2 . VAL A 177 ? 0.2287 0.2188 0.3010 0.0061 0.0260 0.0560 177 VAL A CG2 1445 N N . ASN A 178 ? 0.2311 0.2128 0.2741 0.0356 0.0136 -0.0029 178 ASN A N 1446 C CA . ASN A 178 ? 0.2103 0.2578 0.2361 0.0289 0.0233 0.0299 178 ASN A CA 1447 C C . ASN A 178 ? 0.2953 0.2805 0.2639 0.0226 -0.0108 -0.0072 178 ASN A C 1448 O O . ASN A 178 ? 0.2950 0.3244 0.3019 0.0619 0.0291 -0.0169 178 ASN A O 1449 C CB . ASN A 178 ? 0.1870 0.3116 0.2909 0.0216 0.0204 0.0201 178 ASN A CB 1450 C CG . ASN A 178 ? 0.2701 0.3460 0.2579 0.0031 0.0162 0.0200 178 ASN A CG 1451 O OD1 . ASN A 178 ? 0.2475 0.3267 0.2462 0.0372 0.0308 0.0142 178 ASN A OD1 1452 N ND2 . ASN A 178 ? 0.2784 0.3336 0.3357 0.0357 0.0057 0.0162 178 ASN A ND2 1453 N N . SER A 179 ? 0.2680 0.2376 0.2703 0.0627 0.0203 0.0223 179 SER A N 1454 C CA . SER A 179 ? 0.2935 0.2841 0.3014 0.0550 -0.0251 0.0196 179 SER A CA 1455 C C . SER A 179 ? 0.2768 0.2993 0.2714 0.0300 0.0283 0.0061 179 SER A C 1456 O O . SER A 179 ? 0.3535 0.2941 0.3307 0.0843 -0.0113 0.0313 179 SER A O 1457 C CB . SER A 179 ? 0.4284 0.2482 0.4361 0.0428 0.0107 0.0272 179 SER A CB 1458 O OG . SER A 179 ? 0.4978 0.3900 0.5832 0.0184 0.0321 0.0349 179 SER A OG 1459 N N . THR A 180 ? 0.2726 0.2824 0.2801 0.0557 0.0085 -0.0003 180 THR A N 1460 C CA . THR A 180 ? 0.2873 0.2497 0.2737 0.0306 0.0255 0.0054 180 THR A CA 1461 C C . THR A 180 ? 0.2821 0.2861 0.2840 0.0102 0.0091 0.0077 180 THR A C 1462 O O . THR A 180 ? 0.2408 0.2795 0.2760 0.0155 0.0105 0.0551 180 THR A O 1463 C CB . THR A 180 ? 0.3705 0.2143 0.2768 0.0092 0.0378 0.0334 180 THR A CB 1464 O OG1 . THR A 180 ? 0.3406 0.2741 0.4127 0.0105 0.0631 -0.0078 180 THR A OG1 1465 C CG2 . THR A 180 ? 0.2976 0.3390 0.3438 0.0460 0.0154 0.0567 180 THR A CG2 1466 N N . ARG A 181 ? 0.2633 0.1850 0.2778 0.0050 0.0147 0.0210 181 ARG A N 1467 C CA . ARG A 181 ? 0.2154 0.1894 0.2344 -0.0158 0.0371 -0.0108 181 ARG A CA 1468 C C . ARG A 181 ? 0.2613 0.2379 0.2768 0.0227 0.0122 -0.0053 181 ARG A C 1469 O O . ARG A 181 ? 0.2534 0.2320 0.2808 0.0325 -0.0097 0.0154 181 ARG A O 1470 C CB . ARG A 181 ? 0.2789 0.2695 0.2396 -0.0024 0.0091 0.0330 181 ARG A CB 1471 C CG . ARG A 181 ? 0.2748 0.2995 0.2359 0.0309 0.0424 0.0218 181 ARG A CG 1472 C CD . ARG A 181 ? 0.2964 0.3544 0.3143 0.0362 0.0257 0.0216 181 ARG A CD 1473 N NE . ARG A 181 ? 0.2553 0.2883 0.2835 0.0227 0.0441 0.0292 181 ARG A NE 1474 C CZ . ARG A 181 ? 0.2547 0.3386 0.2959 0.0069 0.0117 0.0472 181 ARG A CZ 1475 N NH1 . ARG A 181 ? 0.2669 0.3737 0.2793 -0.0122 0.0329 0.0076 181 ARG A NH1 1476 N NH2 . ARG A 181 ? 0.3128 0.3199 0.3460 0.0041 -0.0127 0.0046 181 ARG A NH2 1477 N N . GLY A 182 ? 0.2311 0.2744 0.2335 0.0407 0.0032 0.0152 182 GLY A N 1478 C CA . GLY A 182 ? 0.1894 0.2604 0.2459 0.0331 -0.0017 0.0209 182 GLY A CA 1479 C C . GLY A 182 ? 0.2016 0.2309 0.2459 0.0390 -0.0001 0.0094 182 GLY A C 1480 O O . GLY A 182 ? 0.2497 0.3100 0.2691 0.0491 -0.0005 0.0135 182 GLY A O 1481 N N . LEU A 183 ? 0.2148 0.2144 0.2579 0.0247 0.0171 0.0461 183 LEU A N 1482 C CA . LEU A 183 ? 0.2074 0.2952 0.2796 0.0377 -0.0006 0.0528 183 LEU A CA 1483 C C . LEU A 183 ? 0.2277 0.2489 0.1871 0.0463 -0.0058 0.0265 183 LEU A C 1484 O O . LEU A 183 ? 0.2384 0.2476 0.2088 0.0373 0.0222 0.0214 183 LEU A O 1485 C CB . LEU A 183 ? 0.2616 0.2366 0.2296 0.0491 0.0131 0.0562 183 LEU A CB 1486 C CG . LEU A 183 ? 0.2362 0.1987 0.2849 0.0152 -0.0143 0.0259 183 LEU A CG 1487 C CD1 . LEU A 183 ? 0.2706 0.1989 0.2712 -0.0039 -0.0094 0.0037 183 LEU A CD1 1488 C CD2 . LEU A 183 ? 0.3641 0.3170 0.2747 0.0589 -0.0106 0.0325 183 LEU A CD2 1489 N N . CYS A 184 ? 0.2328 0.2699 0.1986 0.0607 -0.0147 0.0553 184 CYS A N 1490 C CA . CYS A 184 ? 0.1929 0.2284 0.2684 0.0272 -0.0126 0.0362 184 CYS A CA 1491 C C . CYS A 184 ? 0.1981 0.2646 0.2178 0.0318 0.0018 0.0305 184 CYS A C 1492 O O . CYS A 184 ? 0.2139 0.2361 0.2331 0.0182 0.0029 0.0240 184 CYS A O 1493 C CB . CYS A 184 ? 0.1916 0.2689 0.2577 0.0067 -0.0014 0.0215 184 CYS A CB 1494 S SG . CYS A 184 ? 0.2260 0.2864 0.2611 0.0182 -0.0191 0.0344 184 CYS A SG 1495 N N . VAL A 185 ? 0.1518 0.2227 0.2021 0.0095 -0.0087 0.0250 185 VAL A N 1496 C CA . VAL A 185 ? 0.1612 0.2741 0.1934 0.0346 -0.0320 0.0104 185 VAL A CA 1497 C C . VAL A 185 ? 0.2098 0.1733 0.1924 0.0113 -0.0249 0.0394 185 VAL A C 1498 O O . VAL A 185 ? 0.2119 0.2107 0.2358 0.0012 0.0241 0.0241 185 VAL A O 1499 C CB . VAL A 185 ? 0.1652 0.2380 0.2033 0.0078 -0.0212 0.0146 185 VAL A CB 1500 C CG1 . VAL A 185 ? 0.1610 0.2824 0.2593 0.0086 -0.0142 0.0017 185 VAL A CG1 1501 C CG2 . VAL A 185 ? 0.2546 0.2718 0.1837 0.0173 -0.0213 0.0108 185 VAL A CG2 1502 N N . THR A 186 ? 0.2112 0.2318 0.2006 0.0055 0.0075 0.0294 186 THR A N 1503 C CA . THR A 186 ? 0.1922 0.2147 0.1891 0.0162 0.0058 0.0189 186 THR A CA 1504 C C . THR A 186 ? 0.2095 0.2185 0.2262 0.0046 0.0018 -0.0008 186 THR A C 1505 O O . THR A 186 ? 0.2128 0.2411 0.2517 0.0054 0.0115 0.0057 186 THR A O 1506 C CB . THR A 186 ? 0.1702 0.2556 0.2206 0.0365 -0.0114 0.0128 186 THR A CB 1507 O OG1 . THR A 186 ? 0.1761 0.2377 0.2359 0.0198 -0.0008 0.0279 186 THR A OG1 1508 C CG2 . THR A 186 ? 0.2100 0.2934 0.1880 0.0121 0.0252 0.0292 186 THR A CG2 1509 N N . THR A 187 ? 0.1441 0.2468 0.2363 0.0157 0.0221 0.0134 187 THR A N 1510 C CA . THR A 187 ? 0.1534 0.2360 0.2191 0.0339 0.0036 0.0326 187 THR A CA 1511 C C . THR A 187 ? 0.2862 0.2547 0.2222 0.0071 0.0031 0.0137 187 THR A C 1512 O O . THR A 187 ? 0.2568 0.3559 0.2713 -0.0303 0.0209 0.0070 187 THR A O 1513 C CB . THR A 187 ? 0.2042 0.2220 0.2950 0.0135 0.0152 -0.0090 187 THR A CB 1514 O OG1 . THR A 187 ? 0.2574 0.3138 0.2992 -0.0100 0.0312 -0.0308 187 THR A OG1 1515 C CG2 . THR A 187 ? 0.1621 0.2971 0.4160 -0.0188 0.0226 -0.0457 187 THR A CG2 1516 N N . ASN A 188 ? 0.2816 0.2732 0.2092 0.0073 0.0104 0.0267 188 ASN A N 1517 C CA . ASN A 188 ? 0.2462 0.2491 0.2376 -0.0038 0.0061 0.0016 188 ASN A CA 1518 C C . ASN A 188 ? 0.3224 0.3459 0.3412 -0.0039 0.0524 -0.0369 188 ASN A C 1519 O O . ASN A 188 ? 0.4070 0.4899 0.4346 -0.0461 0.0634 0.0273 188 ASN A O 1520 C CB . ASN A 188 ? 0.3156 0.3224 0.2666 -0.0726 0.0050 0.0450 188 ASN A CB 1521 C CG . ASN A 188 ? 0.5496 0.4912 0.4251 0.0050 -0.0098 0.0634 188 ASN A CG 1522 O OD1 . ASN A 188 ? 0.6159 0.6068 0.6754 -0.0406 0.0083 0.0157 188 ASN A OD1 1523 N ND2 . ASN A 188 ? 0.5970 0.5696 0.4225 -0.0132 -0.0018 0.0506 188 ASN A ND2 1524 N N . GLY A 189 ? 0.3334 0.3500 0.3266 0.0090 0.0452 -0.0362 189 GLY A N 1525 C CA . GLY A 189 ? 0.2815 0.3173 0.2686 0.0390 0.0225 0.0044 189 GLY A CA 1526 C C . GLY A 189 ? 0.2643 0.2546 0.2945 0.0229 0.0054 -0.0111 189 GLY A C 1527 O O . GLY A 189 ? 0.3026 0.3227 0.2884 0.0382 0.0039 -0.0030 189 GLY A O 1528 N N . TYR A 190 ? 0.2201 0.2423 0.2705 0.0256 0.0161 -0.0199 190 TYR A N 1529 C CA . TYR A 190 ? 0.2299 0.3061 0.2978 0.0141 0.0091 0.0179 190 TYR A CA 1530 C C . TYR A 190 ? 0.2355 0.2991 0.2572 -0.0004 -0.0061 -0.0158 190 TYR A C 1531 O O . TYR A 190 ? 0.2291 0.3550 0.3123 0.0255 0.0154 0.0097 190 TYR A O 1532 C CB . TYR A 190 ? 0.3130 0.3109 0.2918 -0.0021 0.0068 -0.0208 190 TYR A CB 1533 C CG . TYR A 190 ? 0.3211 0.3295 0.2977 -0.0185 -0.0153 -0.0086 190 TYR A CG 1534 C CD1 . TYR A 190 ? 0.2856 0.2687 0.3424 0.0108 -0.0237 -0.0132 190 TYR A CD1 1535 C CD2 . TYR A 190 ? 0.2637 0.3488 0.3230 -0.0438 -0.0227 0.0200 190 TYR A CD2 1536 C CE1 . TYR A 190 ? 0.2484 0.3243 0.3400 0.0155 -0.0023 0.0093 190 TYR A CE1 1537 C CE2 . TYR A 190 ? 0.2746 0.3989 0.3482 -0.0015 -0.0109 -0.0268 190 TYR A CE2 1538 C CZ . TYR A 190 ? 0.3157 0.3903 0.3311 -0.0284 0.0080 0.0088 190 TYR A CZ 1539 O OH . TYR A 190 ? 0.3301 0.4062 0.2832 -0.0231 0.0475 0.0326 190 TYR A OH 1540 N N . ASN A 191 ? 0.2429 0.3017 0.2468 0.0176 -0.0056 -0.0230 191 ASN A N 1541 C CA . ASN A 191 ? 0.2001 0.2905 0.2567 0.0003 0.0008 0.0009 191 ASN A CA 1542 C C . ASN A 191 ? 0.2220 0.2809 0.2628 -0.0065 -0.0111 0.0004 191 ASN A C 1543 O O . ASN A 191 ? 0.2243 0.3158 0.2749 -0.0231 0.0167 -0.0123 191 ASN A O 1544 C CB . ASN A 191 ? 0.2904 0.3184 0.2606 0.0087 0.0372 -0.0156 191 ASN A CB 1545 C CG . ASN A 191 ? 0.3498 0.3955 0.3175 0.0083 0.0184 -0.0236 191 ASN A CG 1546 O OD1 . ASN A 191 ? 0.5220 0.4703 0.4038 -0.0080 0.0603 -0.0582 191 ASN A OD1 1547 N ND2 . ASN A 191 ? 0.3835 0.5194 0.3376 0.0026 -0.0107 -0.0018 191 ASN A ND2 1548 N N . SER A 192 ? 0.2223 0.3059 0.2659 0.0137 0.0012 -0.0037 192 SER A N 1549 C CA . SER A 192 ? 0.2405 0.2541 0.2756 0.0305 0.0118 -0.0080 192 SER A CA 1550 C C . SER A 192 ? 0.1935 0.2882 0.2619 0.0251 0.0130 -0.0008 192 SER A C 1551 O O . SER A 192 ? 0.2607 0.3283 0.2631 0.0126 0.0200 -0.0142 192 SER A O 1552 C CB . SER A 192 ? 0.2560 0.4053 0.3232 0.0442 -0.0453 -0.0357 192 SER A CB 1553 O OG . SER A 192 ? 0.3432 0.4264 0.3873 0.0369 -0.0031 -0.0410 192 SER A OG 1554 N N . LYS A 193 ? 0.2330 0.2879 0.2624 0.0202 0.0233 -0.0134 193 LYS A N 1555 C CA . LYS A 193 ? 0.2285 0.3008 0.2811 -0.0011 0.0293 0.0042 193 LYS A CA 1556 C C . LYS A 193 ? 0.2657 0.2857 0.2869 -0.0180 -0.0085 -0.0048 193 LYS A C 1557 O O . LYS A 193 ? 0.2949 0.2772 0.3399 -0.0146 -0.0104 -0.0037 193 LYS A O 1558 C CB . LYS A 193 ? 0.2196 0.3624 0.3622 0.0047 0.0154 0.0466 193 LYS A CB 1559 C CG . LYS A 193 ? 0.2785 0.4251 0.3892 -0.0216 0.0070 0.0263 193 LYS A CG 1560 C CD . LYS A 193 ? 0.2732 0.4510 0.4874 -0.0415 -0.0030 -0.0389 193 LYS A CD 1561 C CE . LYS A 193 ? 0.4814 0.5102 0.4379 -0.0103 0.0036 0.0404 193 LYS A CE 1562 N NZ . LYS A 193 ? 0.5195 0.6318 0.6510 -0.0275 0.0441 -0.0076 193 LYS A NZ 1563 N N . ASP A 194 ? 0.2634 0.2969 0.2396 0.0024 0.0208 -0.0133 194 ASP A N 1564 C CA . ASP A 194 ? 0.2068 0.2631 0.2508 0.0178 -0.0091 -0.0681 194 ASP A CA 1565 C C . ASP A 194 ? 0.2382 0.2613 0.1825 0.0508 0.0028 0.0049 194 ASP A C 1566 O O . ASP A 194 ? 0.2412 0.2599 0.2314 0.0163 0.0111 0.0167 194 ASP A O 1567 C CB . ASP A 194 ? 0.1816 0.2773 0.2330 -0.0240 0.0011 -0.0134 194 ASP A CB 1568 C CG . ASP A 194 ? 0.2919 0.3218 0.2745 -0.0079 0.0249 -0.0189 194 ASP A CG 1569 O OD1 . ASP A 194 ? 0.2602 0.3444 0.2882 -0.0004 0.0050 -0.0118 194 ASP A OD1 1570 O OD2 . ASP A 194 ? 0.3023 0.3301 0.2686 -0.0159 0.0245 0.0070 194 ASP A OD2 1571 N N . LEU A 195 ? 0.1997 0.2263 0.2671 0.0073 0.0314 -0.0004 195 LEU A N 1572 C CA . LEU A 195 ? 0.1984 0.2270 0.2490 0.0161 0.0576 0.0135 195 LEU A CA 1573 C C . LEU A 195 ? 0.2119 0.2722 0.2228 -0.0029 0.0168 -0.0142 195 LEU A C 1574 O O . LEU A 195 ? 0.2431 0.2736 0.2579 -0.0042 0.0216 0.0197 195 LEU A O 1575 C CB . LEU A 195 ? 0.3456 0.2221 0.2424 0.0086 0.0394 0.0217 195 LEU A CB 1576 C CG . LEU A 195 ? 0.2911 0.3261 0.3401 0.0031 0.0195 -0.0090 195 LEU A CG 1577 C CD1 . LEU A 195 ? 0.3414 0.3318 0.4223 -0.0578 -0.0608 0.0095 195 LEU A CD1 1578 C CD2 . LEU A 195 ? 0.4280 0.3791 0.4151 0.0157 -0.0019 0.0363 195 LEU A CD2 1579 N N . ILE A 196 ? 0.2018 0.2202 0.2199 -0.0151 0.0298 -0.0089 196 ILE A N 1580 C CA . ILE A 196 ? 0.1894 0.2539 0.2322 0.0040 -0.0036 0.0325 196 ILE A CA 1581 C C . ILE A 196 ? 0.2026 0.2258 0.2618 -0.0353 0.0152 0.0168 196 ILE A C 1582 O O . ILE A 196 ? 0.1861 0.1904 0.2556 -0.0069 0.0003 0.0111 196 ILE A O 1583 C CB . ILE A 196 ? 0.1842 0.2421 0.2613 -0.0070 0.0299 0.0617 196 ILE A CB 1584 C CG1 . ILE A 196 ? 0.2323 0.2140 0.2630 0.0285 0.0082 0.0299 196 ILE A CG1 1585 C CG2 . ILE A 196 ? 0.1485 0.2310 0.2815 -0.0042 0.0133 0.0161 196 ILE A CG2 1586 C CD1 . ILE A 196 ? 0.2597 0.2944 0.2494 -0.0106 0.0036 0.0388 196 ILE A CD1 1587 N N . ILE A 197 ? 0.2244 0.2101 0.2242 0.0043 0.0053 0.0453 197 ILE A N 1588 C CA . ILE A 197 ? 0.2346 0.2317 0.1776 0.0316 0.0255 0.0332 197 ILE A CA 1589 C C . ILE A 197 ? 0.2207 0.2319 0.2275 0.0189 0.0291 0.0216 197 ILE A C 1590 O O . ILE A 197 ? 0.2074 0.2259 0.2602 0.0222 0.0069 0.0457 197 ILE A O 1591 C CB . ILE A 197 ? 0.1971 0.2932 0.1936 -0.0185 0.0009 0.0094 197 ILE A CB 1592 C CG1 . ILE A 197 ? 0.2529 0.3333 0.1697 -0.0141 -0.0292 0.0305 197 ILE A CG1 1593 C CG2 . ILE A 197 ? 0.1898 0.2658 0.2448 0.0047 0.0287 0.0153 197 ILE A CG2 1594 C CD1 . ILE A 197 ? 0.3657 0.3887 0.2067 0.0100 -0.0275 0.0130 197 ILE A CD1 1595 N N . ILE A 198 ? 0.2075 0.2255 0.2693 0.0369 0.0179 0.0535 198 ILE A N 1596 C CA . ILE A 198 ? 0.2367 0.2750 0.2220 0.0240 -0.0126 0.0057 198 ILE A CA 1597 C C . ILE A 198 ? 0.2375 0.2574 0.2745 0.0446 0.0039 0.0097 198 ILE A C 1598 O O . ILE A 198 ? 0.2781 0.2558 0.3066 0.0365 0.0357 0.0744 198 ILE A O 1599 C CB . ILE A 198 ? 0.2298 0.2856 0.2336 0.0027 -0.0014 -0.0140 198 ILE A CB 1600 C CG1 . ILE A 198 ? 0.2942 0.2790 0.2285 -0.0027 0.0241 0.0411 198 ILE A CG1 1601 C CG2 . ILE A 198 ? 0.1618 0.2584 0.2829 0.0062 0.0125 0.0323 198 ILE A CG2 1602 C CD1 . ILE A 198 ? 0.2773 0.2802 0.2195 0.0150 -0.0007 0.0566 198 ILE A CD1 1603 N N . LEU A 199 ? 0.2284 0.2602 0.2098 0.0239 -0.0248 0.0459 199 LEU A N 1604 C CA . LEU A 199 ? 0.2012 0.2818 0.2198 0.0154 -0.0343 0.0213 199 LEU A CA 1605 C C . LEU A 199 ? 0.2455 0.2189 0.2722 -0.0292 -0.0135 0.0181 199 LEU A C 1606 O O . LEU A 199 ? 0.2521 0.3291 0.2297 0.0154 0.0149 0.0538 199 LEU A O 1607 C CB . LEU A 199 ? 0.3084 0.2936 0.2859 0.0236 0.0107 0.0394 199 LEU A CB 1608 C CG . LEU A 199 ? 0.5063 0.4385 0.4531 0.0079 0.0506 0.0258 199 LEU A CG 1609 C CD1 . LEU A 199 ? 0.5722 0.4501 0.3431 0.0348 0.0296 0.0143 199 LEU A CD1 1610 C CD2 . LEU A 199 ? 0.4474 0.4062 0.3790 0.0260 0.0466 0.0590 199 LEU A CD2 1611 N N . LYS A 200 ? 0.2501 0.2952 0.2916 0.0323 -0.0056 0.0379 200 LYS A N 1612 C CA . LYS A 200 ? 0.2475 0.2632 0.2638 0.0094 -0.0343 0.0557 200 LYS A CA 1613 C C . LYS A 200 ? 0.2976 0.2788 0.2681 -0.0057 0.0139 0.0344 200 LYS A C 1614 O O . LYS A 200 ? 0.2661 0.2837 0.2354 0.0172 -0.0010 0.0363 200 LYS A O 1615 C CB . LYS A 200 ? 0.2736 0.2990 0.2626 0.0388 -0.0613 0.0705 200 LYS A CB 1616 C CG . LYS A 200 ? 0.3563 0.4904 0.4027 -0.0217 -0.0079 0.0251 200 LYS A CG 1617 C CD . LYS A 200 ? 0.5484 0.5828 0.5221 0.0400 -0.0296 0.0608 200 LYS A CD 1618 C CE . LYS A 200 ? 0.6681 0.6422 0.6637 -0.0061 -0.0238 -0.0182 200 LYS A CE 1619 N NZ . LYS A 200 ? 0.7594 0.7729 0.7478 -0.0003 0.0163 -0.0133 200 LYS A NZ 1620 N N . CYS A 201 ? 0.2184 0.2752 0.2723 0.0319 -0.0248 0.0600 201 CYS A N 1621 C CA . CYS A 201 ? 0.2165 0.2827 0.2079 -0.0177 -0.0356 0.0074 201 CYS A CA 1622 C C . CYS A 201 ? 0.2481 0.2689 0.1940 0.0109 -0.0052 0.0158 201 CYS A C 1623 O O . CYS A 201 ? 0.2550 0.3687 0.2587 0.0762 -0.0485 0.0262 201 CYS A O 1624 C CB . CYS A 201 ? 0.2168 0.3288 0.2591 0.0269 0.0112 0.0076 201 CYS A CB 1625 S SG . CYS A 201 ? 0.2385 0.2905 0.2572 0.0374 0.0004 0.0335 201 CYS A SG 1626 N N . GLN A 202 ? 0.2613 0.2664 0.2151 0.0119 0.0135 0.0101 202 GLN A N 1627 C CA . GLN A 202 ? 0.2564 0.2909 0.2552 0.0318 -0.0069 -0.0166 202 GLN A CA 1628 C C . GLN A 202 ? 0.1584 0.2682 0.1900 -0.0084 -0.0026 0.0255 202 GLN A C 1629 O O . GLN A 202 ? 0.2821 0.2927 0.2312 -0.0016 -0.0283 0.0103 202 GLN A O 1630 C CB . GLN A 202 ? 0.3691 0.3238 0.2602 0.0121 0.0164 0.0164 202 GLN A CB 1631 C CG . GLN A 202 ? 0.4270 0.3737 0.3817 -0.0016 0.0102 0.0157 202 GLN A CG 1632 C CD . GLN A 202 ? 0.4173 0.3952 0.4196 -0.0273 0.0242 0.0148 202 GLN A CD 1633 O OE1 . GLN A 202 ? 0.4749 0.4126 0.3513 -0.0021 0.0085 -0.0105 202 GLN A OE1 1634 N NE2 . GLN A 202 ? 0.4980 0.5018 0.3974 -0.0071 -0.0074 0.0265 202 GLN A NE2 1635 N N . GLY A 203 ? 0.1604 0.2836 0.2121 0.0533 -0.0037 0.0643 203 GLY A N 1636 C CA . GLY A 203 ? 0.1965 0.2336 0.2892 0.0374 -0.0104 0.0339 203 GLY A CA 1637 C C . GLY A 203 ? 0.2286 0.2457 0.2155 0.0083 0.0064 0.0031 203 GLY A C 1638 O O . GLY A 203 ? 0.2145 0.2344 0.2705 0.0185 -0.0008 0.0244 203 GLY A O 1639 N N . LEU A 204 ? 0.1911 0.2739 0.2161 0.0399 -0.0137 0.0156 204 LEU A N 1640 C CA . LEU A 204 ? 0.1892 0.2400 0.2820 0.0400 -0.0021 0.0472 204 LEU A CA 1641 C C . LEU A 204 ? 0.1950 0.2525 0.1833 0.0230 0.0060 0.0019 204 LEU A C 1642 O O . LEU A 204 ? 0.1823 0.2414 0.1956 -0.0042 -0.0067 0.0231 204 LEU A O 1643 C CB . LEU A 204 ? 0.2101 0.2821 0.2441 0.0020 -0.0018 0.0561 204 LEU A CB 1644 C CG . LEU A 204 ? 0.2328 0.2900 0.3052 0.0129 -0.0096 0.0269 204 LEU A CG 1645 C CD1 . LEU A 204 ? 0.3698 0.2843 0.3513 -0.0017 0.0277 0.0811 204 LEU A CD1 1646 C CD2 . LEU A 204 ? 0.3543 0.3163 0.3039 0.0106 -0.0120 0.0271 204 LEU A CD2 1647 N N . PRO A 205 ? 0.1865 0.2238 0.2161 0.0264 0.0142 0.0129 205 PRO A N 1648 C CA . PRO A 205 ? 0.2108 0.2479 0.2050 0.0103 -0.0219 0.0105 205 PRO A CA 1649 C C . PRO A 205 ? 0.1994 0.2100 0.1963 -0.0029 0.0160 0.0293 205 PRO A C 1650 O O . PRO A 205 ? 0.2106 0.2644 0.2332 0.0044 0.0142 0.0282 205 PRO A O 1651 C CB . PRO A 205 ? 0.2017 0.2428 0.2498 0.0135 -0.0138 0.0114 205 PRO A CB 1652 C CG . PRO A 205 ? 0.2418 0.2693 0.2101 -0.0225 0.0090 0.0187 205 PRO A CG 1653 C CD . PRO A 205 ? 0.3114 0.2813 0.2281 0.0080 0.0308 -0.0062 205 PRO A CD 1654 N N . SER A 206 ? 0.2064 0.2046 0.2186 -0.0091 0.0085 0.0392 206 SER A N 1655 C CA . SER A 206 ? 0.2498 0.2244 0.1882 -0.0234 0.0235 -0.0039 206 SER A CA 1656 C C . SER A 206 ? 0.1944 0.2270 0.2171 0.0157 0.0089 0.0128 206 SER A C 1657 O O . SER A 206 ? 0.1992 0.2032 0.2163 0.0058 0.0129 0.0030 206 SER A O 1658 C CB . SER A 206 ? 0.1994 0.2919 0.2305 -0.0438 -0.0104 0.0144 206 SER A CB 1659 O OG . SER A 206 ? 0.2056 0.3023 0.2510 0.0043 -0.0077 0.0346 206 SER A OG 1660 N N . GLN A 207 ? 0.1519 0.2288 0.2058 0.0345 -0.0133 0.0214 207 GLN A N 1661 C CA . GLN A 207 ? 0.1487 0.2210 0.1941 0.0083 -0.0095 0.0393 207 GLN A CA 1662 C C . GLN A 207 ? 0.2352 0.2500 0.2224 0.0268 0.0286 0.0470 207 GLN A C 1663 O O . GLN A 207 ? 0.1979 0.2556 0.2077 0.0295 0.0074 0.0034 207 GLN A O 1664 C CB . GLN A 207 ? 0.2228 0.1938 0.2074 0.0373 -0.0151 0.0500 207 GLN A CB 1665 C CG . GLN A 207 ? 0.1898 0.2371 0.2483 0.0448 -0.0037 0.0684 207 GLN A CG 1666 C CD . GLN A 207 ? 0.1997 0.2611 0.2557 0.0244 -0.0186 0.0326 207 GLN A CD 1667 O OE1 . GLN A 207 ? 0.2039 0.2635 0.2353 0.0280 -0.0291 0.0665 207 GLN A OE1 1668 N NE2 . GLN A 207 ? 0.2126 0.2628 0.2541 0.0331 0.0370 0.0350 207 GLN A NE2 1669 N N . ARG A 208 ? 0.1638 0.2241 0.1915 -0.0030 -0.0044 0.0326 208 ARG A N 1670 C CA . ARG A 208 ? 0.1749 0.2251 0.2400 0.0261 -0.0301 0.0401 208 ARG A CA 1671 C C . ARG A 208 ? 0.1728 0.2170 0.1734 0.0029 -0.0155 0.0204 208 ARG A C 1672 O O . ARG A 208 ? 0.1842 0.2143 0.2079 -0.0162 0.0052 0.0091 208 ARG A O 1673 C CB . ARG A 208 ? 0.2021 0.2404 0.2540 -0.0101 -0.0120 0.0244 208 ARG A CB 1674 C CG . ARG A 208 ? 0.3211 0.2556 0.2903 -0.0320 -0.0243 0.0655 208 ARG A CG 1675 C CD . ARG A 208 ? 0.3410 0.2271 0.3103 -0.0386 -0.0276 0.0455 208 ARG A CD 1676 N NE . ARG A 208 ? 0.2037 0.2646 0.2950 -0.0156 -0.0237 0.0557 208 ARG A NE 1677 C CZ . ARG A 208 ? 0.2083 0.3085 0.2739 -0.0160 0.0023 0.0151 208 ARG A CZ 1678 N NH1 . ARG A 208 ? 0.1746 0.2957 0.2470 0.0236 -0.0129 0.0230 208 ARG A NH1 1679 N NH2 . ARG A 208 ? 0.2226 0.2618 0.3238 -0.0209 -0.0714 0.0530 208 ARG A NH2 1680 N N . TRP A 209 ? 0.1811 0.2128 0.1556 -0.0132 -0.0295 0.0175 209 TRP A N 1681 C CA . TRP A 209 ? 0.1850 0.2155 0.1733 -0.0053 -0.0328 0.0182 209 TRP A CA 1682 C C . TRP A 209 ? 0.1537 0.1919 0.1735 -0.0262 -0.0072 0.0453 209 TRP A C 1683 O O . TRP A 209 ? 0.1517 0.2304 0.2197 -0.0155 0.0042 0.0219 209 TRP A O 1684 C CB . TRP A 209 ? 0.1970 0.1961 0.2389 -0.0314 0.0123 0.0047 209 TRP A CB 1685 C CG . TRP A 209 ? 0.1992 0.1910 0.2026 0.0068 -0.0161 0.0016 209 TRP A CG 1686 C CD1 . TRP A 209 ? 0.1983 0.1978 0.1966 0.0103 -0.0180 0.0350 209 TRP A CD1 1687 C CD2 . TRP A 209 ? 0.1636 0.2419 0.2239 0.0217 -0.0003 0.0131 209 TRP A CD2 1688 N NE1 . TRP A 209 ? 0.2188 0.2244 0.2562 -0.0095 0.0139 0.0219 209 TRP A NE1 1689 C CE2 . TRP A 209 ? 0.1963 0.2317 0.2380 -0.0303 0.0119 0.0032 209 TRP A CE2 1690 C CE3 . TRP A 209 ? 0.1520 0.1881 0.2061 -0.0099 -0.0063 0.0041 209 TRP A CE3 1691 C CZ2 . TRP A 209 ? 0.1683 0.1766 0.2121 0.0091 -0.0051 0.0194 209 TRP A CZ2 1692 C CZ3 . TRP A 209 ? 0.2019 0.2063 0.2126 -0.0279 0.0159 0.0000 209 TRP A CZ3 1693 C CH2 . TRP A 209 ? 0.1740 0.2168 0.2342 0.0299 -0.0235 0.0206 209 TRP A CH2 1694 N N . PHE A 210 ? 0.2288 0.2378 0.2184 0.0188 -0.0211 0.0192 210 PHE A N 1695 C CA . PHE A 210 ? 0.3187 0.2783 0.2463 0.0019 -0.0764 0.0302 210 PHE A CA 1696 C C . PHE A 210 ? 0.1932 0.2243 0.2209 0.0147 -0.0066 0.0239 210 PHE A C 1697 O O . PHE A 210 ? 0.1960 0.2300 0.2559 -0.0068 -0.0214 0.0124 210 PHE A O 1698 C CB . PHE A 210 ? 0.2647 0.3054 0.3088 -0.0259 -0.0769 -0.0177 210 PHE A CB 1699 C CG . PHE A 210 ? 0.1747 0.2711 0.4036 0.0096 0.0233 -0.0179 210 PHE A CG 1700 C CD1 . PHE A 210 ? 0.2866 0.3145 0.3434 0.0094 -0.1065 0.0905 210 PHE A CD1 1701 C CD2 . PHE A 210 ? 0.4018 0.4284 0.3801 -0.0110 0.0090 0.0275 210 PHE A CD2 1702 C CE1 . PHE A 210 ? 0.4909 0.4037 0.3920 -0.0178 -0.0370 0.0586 210 PHE A CE1 1703 C CE2 . PHE A 210 ? 0.4603 0.4203 0.4421 -0.0233 -0.0459 0.0250 210 PHE A CE2 1704 C CZ . PHE A 210 ? 0.4947 0.4125 0.4533 -0.0013 -0.0041 0.0261 210 PHE A CZ 1705 N N . PHE A 211 ? 0.2561 0.2667 0.2058 0.0115 -0.0205 0.0050 211 PHE A N 1706 C CA . PHE A 211 ? 0.2940 0.2263 0.2220 0.0203 -0.0112 -0.0129 211 PHE A CA 1707 C C . PHE A 211 ? 0.2375 0.2513 0.2630 -0.0249 -0.0063 -0.0032 211 PHE A C 1708 O O . PHE A 211 ? 0.3325 0.3172 0.3250 -0.0457 0.0381 0.0355 211 PHE A O 1709 C CB . PHE A 211 ? 0.2539 0.2805 0.2941 -0.0061 0.0268 -0.0261 211 PHE A CB 1710 C CG . PHE A 211 ? 0.2774 0.3063 0.2883 0.0210 -0.0060 -0.0262 211 PHE A CG 1711 C CD1 . PHE A 211 ? 0.2959 0.3073 0.3443 0.0502 0.0219 0.0040 211 PHE A CD1 1712 C CD2 . PHE A 211 ? 0.3392 0.2592 0.3273 -0.0160 0.0489 -0.0173 211 PHE A CD2 1713 C CE1 . PHE A 211 ? 0.2794 0.3240 0.3864 0.0412 -0.0060 0.0133 211 PHE A CE1 1714 C CE2 . PHE A 211 ? 0.2740 0.3106 0.3367 0.0249 0.0282 0.0328 211 PHE A CE2 1715 C CZ . PHE A 211 ? 0.3169 0.2766 0.3476 0.0280 0.0440 -0.0013 211 PHE A CZ 1716 N N . ASN A 212 ? 0.2873 0.2662 0.2728 0.0196 -0.0123 0.0083 212 ASN A N 1717 C CA . ASN A 212 ? 0.3394 0.2506 0.2726 0.0028 0.0046 -0.0041 212 ASN A CA 1718 C C . ASN A 212 ? 0.4499 0.3585 0.3154 0.0061 -0.0173 -0.0001 212 ASN A C 1719 O O . ASN A 212 ? 0.4395 0.3400 0.3331 0.0083 0.0193 -0.0022 212 ASN A O 1720 C CB . ASN A 212 ? 0.3035 0.2126 0.3324 0.0073 -0.0162 0.0107 212 ASN A CB 1721 C CG . ASN A 212 ? 0.2870 0.3067 0.3047 0.0156 -0.0085 0.0145 212 ASN A CG 1722 O OD1 . ASN A 212 ? 0.4148 0.2599 0.3665 -0.0194 -0.0402 0.0227 212 ASN A OD1 1723 N ND2 . ASN A 212 ? 0.3081 0.2925 0.3690 0.0142 -0.0204 0.0312 212 ASN A ND2 1724 N N . SER A 213 ? 0.4626 0.3790 0.3435 0.0013 -0.0338 0.0245 213 SER A N 1725 C CA . SER A 213 ? 0.4810 0.4457 0.4015 -0.0062 -0.0143 0.0352 213 SER A CA 1726 C C . SER A 213 ? 0.5053 0.5036 0.4520 -0.0210 -0.0031 0.0094 213 SER A C 1727 O O . SER A 213 ? 0.6164 0.6102 0.5217 -0.0178 -0.0487 -0.0306 213 SER A O 1728 C CB . SER A 213 ? 0.5167 0.4060 0.3856 0.0176 -0.0146 0.0354 213 SER A CB 1729 O OG . SER A 213 ? 0.5408 0.5197 0.5026 0.0368 0.0033 0.0294 213 SER A OG 1730 N N . ASP A 214 ? 0.4161 0.3688 0.4657 -0.0043 0.0054 0.0106 214 ASP A N 1731 C CA . ASP A 214 ? 0.3774 0.3485 0.2941 0.0204 -0.0300 0.0329 214 ASP A CA 1732 C C . ASP A 214 ? 0.3791 0.3561 0.3983 0.0129 -0.0214 0.0251 214 ASP A C 1733 O O . ASP A 214 ? 0.3716 0.4386 0.4814 0.0080 -0.0500 0.0584 214 ASP A O 1734 C CB . ASP A 214 ? 0.3981 0.3555 0.4499 0.0261 0.0258 -0.0189 214 ASP A CB 1735 C CG . ASP A 214 ? 0.5464 0.4592 0.5613 0.0341 -0.0005 0.0043 214 ASP A CG 1736 O OD1 . ASP A 214 ? 0.5531 0.4978 0.5552 0.0338 -0.0150 -0.0058 214 ASP A OD1 1737 O OD2 . ASP A 214 ? 0.6264 0.5842 0.6000 0.0260 0.0167 -0.0219 214 ASP A OD2 1738 N N . GLY A 215 ? 0.4038 0.2462 0.2694 0.0155 -0.0382 0.0246 215 GLY A N 1739 C CA . GLY A 215 ? 0.3356 0.2497 0.2438 -0.0106 -0.0251 0.0461 215 GLY A CA 1740 C C . GLY A 215 ? 0.2015 0.2468 0.2357 0.0145 0.0017 0.0141 215 GLY A C 1741 O O . GLY A 215 ? 0.3046 0.2129 0.2839 -0.0233 0.0193 -0.0008 215 GLY A O 1742 N N . ALA A 216 ? 0.2418 0.2673 0.2170 0.0229 -0.0022 -0.0174 216 ALA A N 1743 C CA . ALA A 216 ? 0.2187 0.2160 0.2266 0.0479 -0.0224 -0.0259 216 ALA A CA 1744 C C . ALA A 216 ? 0.2229 0.2353 0.2633 0.0174 -0.0078 0.0133 216 ALA A C 1745 O O . ALA A 216 ? 0.2186 0.2249 0.2659 0.0180 -0.0225 0.0315 216 ALA A O 1746 C CB . ALA A 216 ? 0.2199 0.2135 0.2635 0.0222 -0.0313 -0.0635 216 ALA A CB 1747 N N . ILE A 217 ? 0.2054 0.2358 0.1959 0.0326 -0.0336 0.0120 217 ILE A N 1748 C CA . ILE A 217 ? 0.1917 0.2133 0.2097 0.0520 -0.0120 -0.0121 217 ILE A CA 1749 C C . ILE A 217 ? 0.1849 0.2129 0.1783 0.0088 -0.0096 0.0302 217 ILE A C 1750 O O . ILE A 217 ? 0.2162 0.1918 0.2315 -0.0212 0.0196 -0.0120 217 ILE A O 1751 C CB . ILE A 217 ? 0.1931 0.1960 0.1917 0.0437 -0.0359 -0.0187 217 ILE A CB 1752 C CG1 . ILE A 217 ? 0.2586 0.1817 0.2170 0.0296 0.0153 -0.0081 217 ILE A CG1 1753 C CG2 . ILE A 217 ? 0.1736 0.2269 0.2214 0.0089 -0.0416 -0.0031 217 ILE A CG2 1754 C CD1 . ILE A 217 ? 0.2636 0.2092 0.2681 0.0323 0.0137 0.0041 217 ILE A CD1 1755 N N . VAL A 218 ? 0.1911 0.2317 0.2165 0.0014 -0.0239 -0.0406 218 VAL A N 1756 C CA . VAL A 218 ? 0.2217 0.1884 0.1971 0.0300 -0.0240 -0.0075 218 VAL A CA 1757 C C . VAL A 218 ? 0.1929 0.2144 0.1963 -0.0201 -0.0067 -0.0014 218 VAL A C 1758 O O . VAL A 218 ? 0.1842 0.2089 0.2091 0.0128 -0.0102 0.0160 218 VAL A O 1759 C CB . VAL A 218 ? 0.1957 0.1976 0.1912 0.0400 -0.0246 -0.0284 218 VAL A CB 1760 C CG1 . VAL A 218 ? 0.2423 0.3126 0.2032 0.0401 0.0097 -0.0496 218 VAL A CG1 1761 C CG2 . VAL A 218 ? 0.2414 0.2563 0.1995 0.0182 -0.0384 0.0348 218 VAL A CG2 1762 N N . ASN A 219 ? 0.2392 0.2062 0.1595 0.0080 -0.0031 -0.0088 219 ASN A N 1763 C CA . ASN A 219 ? 0.2110 0.1749 0.2157 0.0046 0.0041 0.0140 219 ASN A CA 1764 C C . ASN A 219 ? 0.1875 0.2100 0.2307 -0.0060 0.0063 -0.0081 219 ASN A C 1765 O O . ASN A 219 ? 0.2203 0.2545 0.1799 0.0235 0.0102 -0.0097 219 ASN A O 1766 C CB . ASN A 219 ? 0.2090 0.2104 0.1769 -0.0110 -0.0187 0.0158 219 ASN A CB 1767 C CG . ASN A 219 ? 0.1856 0.2211 0.2010 0.0023 -0.0317 -0.0094 219 ASN A CG 1768 O OD1 . ASN A 219 ? 0.1811 0.2506 0.2174 0.0099 0.0060 -0.0173 219 ASN A OD1 1769 N ND2 . ASN A 219 ? 0.1696 0.2061 0.2351 0.0101 -0.0151 0.0227 219 ASN A ND2 1770 N N . PRO A 220 ? 0.1596 0.1976 0.2407 0.0286 0.0080 0.0068 220 PRO A N 1771 C CA . PRO A 220 ? 0.2234 0.1993 0.2079 0.0046 0.0188 0.0032 220 PRO A CA 1772 C C . PRO A 220 ? 0.2033 0.2509 0.1939 0.0340 0.0038 0.0179 220 PRO A C 1773 O O . PRO A 220 ? 0.2387 0.2291 0.2176 0.0197 -0.0089 -0.0172 220 PRO A O 1774 C CB . PRO A 220 ? 0.1910 0.2340 0.2454 -0.0086 0.0317 0.0177 220 PRO A CB 1775 C CG . PRO A 220 ? 0.2569 0.1744 0.3119 -0.0012 0.0253 -0.0008 220 PRO A CG 1776 C CD . PRO A 220 ? 0.1342 0.1904 0.2658 0.0316 0.0283 0.0048 220 PRO A CD 1777 N N . LYS A 221 ? 0.1765 0.2006 0.1868 -0.0072 0.0118 0.0140 221 LYS A N 1778 C CA . LYS A 221 ? 0.1721 0.2503 0.1992 -0.0245 -0.0008 0.0041 221 LYS A CA 1779 C C . LYS A 221 ? 0.1950 0.2272 0.2234 -0.0141 -0.0041 0.0096 221 LYS A C 1780 O O . LYS A 221 ? 0.2595 0.3177 0.2674 -0.0035 -0.0124 -0.0559 221 LYS A O 1781 C CB . LYS A 221 ? 0.2522 0.3000 0.1889 -0.0052 -0.0166 0.0447 221 LYS A CB 1782 C CG . LYS A 221 ? 0.3451 0.3374 0.2168 0.0148 0.0275 -0.0201 221 LYS A CG 1783 C CD . LYS A 221 ? 0.4669 0.4062 0.3316 -0.0108 0.0178 -0.0414 221 LYS A CD 1784 C CE . LYS A 221 ? 0.4445 0.5084 0.3727 0.0083 0.0307 -0.0215 221 LYS A CE 1785 N NZ . LYS A 221 ? 0.5610 0.5938 0.4585 0.0028 0.0328 0.0594 221 LYS A NZ 1786 N N . SER A 222 ? 0.1483 0.2110 0.2030 -0.0291 0.0042 -0.0111 222 SER A N 1787 C CA . SER A 222 ? 0.1589 0.2280 0.2417 -0.0017 0.0137 0.0007 222 SER A CA 1788 C C . SER A 222 ? 0.2490 0.2061 0.2255 0.0103 -0.0030 -0.0270 222 SER A C 1789 O O . SER A 222 ? 0.2110 0.3024 0.2569 0.0300 0.0090 -0.0245 222 SER A O 1790 C CB . SER A 222 ? 0.2055 0.2408 0.2214 0.0006 0.0130 -0.0192 222 SER A CB 1791 O OG . SER A 222 ? 0.2064 0.2244 0.2022 0.0102 -0.0131 0.0091 222 SER A OG 1792 N N . ARG A 223 ? 0.1907 0.2110 0.2268 -0.0017 -0.0185 -0.0182 223 ARG A N 1793 C CA . ARG A 223 ? 0.2084 0.2146 0.2221 0.0276 -0.0047 -0.0261 223 ARG A CA 1794 C C . ARG A 223 ? 0.1678 0.2001 0.2542 0.0043 -0.0154 -0.0057 223 ARG A C 1795 O O . ARG A 223 ? 0.2138 0.2641 0.2409 -0.0038 -0.0060 -0.0076 223 ARG A O 1796 C CB . ARG A 223 ? 0.1973 0.2288 0.2458 0.0362 -0.0176 -0.0399 223 ARG A CB 1797 C CG . ARG A 223 ? 0.2427 0.1580 0.2826 0.0379 0.0067 -0.0536 223 ARG A CG 1798 C CD . ARG A 223 ? 0.2548 0.2190 0.2264 0.0472 0.0094 -0.0648 223 ARG A CD 1799 N NE . ARG A 223 ? 0.2620 0.2606 0.2212 0.0040 0.0013 -0.0163 223 ARG A NE 1800 C CZ . ARG A 223 ? 0.2806 0.2509 0.2193 -0.0272 0.0247 0.0264 223 ARG A CZ 1801 N NH1 . ARG A 223 ? 0.3130 0.2857 0.2808 0.0120 0.0108 -0.0262 223 ARG A NH1 1802 N NH2 . ARG A 223 ? 0.3418 0.2362 0.2811 -0.0080 0.0121 0.0080 223 ARG A NH2 1803 N N . LEU A 224 ? 0.1488 0.2144 0.2074 -0.0008 -0.0154 -0.0398 224 LEU A N 1804 C CA . LEU A 224 ? 0.1398 0.2337 0.2383 0.0278 -0.0306 -0.0346 224 LEU A CA 1805 C C . LEU A 224 ? 0.2224 0.2374 0.2278 -0.0010 0.0174 -0.0339 224 LEU A C 1806 O O . LEU A 224 ? 0.1991 0.2029 0.2546 -0.0197 -0.0125 -0.0358 224 LEU A O 1807 C CB . LEU A 224 ? 0.2077 0.2478 0.2680 -0.0069 0.0282 -0.0430 224 LEU A CB 1808 C CG . LEU A 224 ? 0.2159 0.2016 0.2130 0.0269 0.0090 0.0064 224 LEU A CG 1809 C CD1 . LEU A 224 ? 0.2934 0.2325 0.2647 -0.0208 0.0479 -0.0062 224 LEU A CD1 1810 C CD2 . LEU A 224 ? 0.1807 0.2386 0.2521 0.0714 0.0272 -0.0367 224 LEU A CD2 1811 N N . VAL A 225 ? 0.1898 0.2033 0.2101 0.0330 -0.0085 -0.0125 225 VAL A N 1812 C CA . VAL A 225 ? 0.2244 0.2099 0.1484 0.0216 -0.0159 -0.0445 225 VAL A CA 1813 C C . VAL A 225 ? 0.1619 0.2124 0.2355 0.0339 -0.0194 -0.0177 225 VAL A C 1814 O O . VAL A 225 ? 0.2131 0.2195 0.2224 0.0137 0.0107 -0.0250 225 VAL A O 1815 C CB . VAL A 225 ? 0.1719 0.1982 0.2084 -0.0110 -0.0070 -0.0185 225 VAL A CB 1816 C CG1 . VAL A 225 ? 0.2352 0.1706 0.2550 0.0033 -0.0033 -0.0266 225 VAL A CG1 1817 C CG2 . VAL A 225 ? 0.1907 0.2253 0.2538 0.0090 -0.0175 0.0119 225 VAL A CG2 1818 N N A MET A 226 ? 0.2040 0.1820 0.2448 0.0297 -0.0038 -0.0432 226 MET A N 1819 N N B MET A 226 ? 0.1982 0.1721 0.2326 0.0291 -0.0054 -0.0356 226 MET A N 1820 C CA A MET A 226 ? 0.1807 0.2057 0.2048 -0.0082 0.0251 -0.0212 226 MET A CA 1821 C CA B MET A 226 ? 0.1334 0.1828 0.2260 0.0161 0.0205 -0.0362 226 MET A CA 1822 C C A MET A 226 ? 0.2251 0.2019 0.2200 -0.0030 0.0002 -0.0111 226 MET A C 1823 C C B MET A 226 ? 0.2029 0.1749 0.2205 0.0127 -0.0147 0.0050 226 MET A C 1824 O O A MET A 226 ? 0.2144 0.2256 0.2624 -0.0092 -0.0167 0.0071 226 MET A O 1825 O O B MET A 226 ? 0.1649 0.1731 0.1864 -0.0420 0.0008 0.0008 226 MET A O 1826 C CB A MET A 226 ? 0.1899 0.3065 0.2239 0.0329 0.0384 0.0212 226 MET A CB 1827 C CB B MET A 226 ? 0.1713 0.1531 0.2011 0.0583 0.0312 -0.0225 226 MET A CB 1828 C CG A MET A 226 ? 0.2398 0.2654 0.2741 0.0034 0.0159 0.0037 226 MET A CG 1829 C CG B MET A 226 ? 0.2040 0.2148 0.2696 0.0148 0.0129 -0.0091 226 MET A CG 1830 S SD A MET A 226 ? 0.3080 0.3241 0.3426 0.0444 0.0211 -0.0140 226 MET A SD 1831 S SD B MET A 226 ? 0.1885 0.2055 0.1910 0.0281 0.0073 0.0134 226 MET A SD 1832 C CE A MET A 226 ? 0.2000 0.2034 0.2285 0.0166 0.0277 0.0395 226 MET A CE 1833 C CE B MET A 226 ? 0.1527 0.2268 0.2042 0.0010 -0.0228 0.0245 226 MET A CE 1834 N N . ASP A 227 ? 0.1721 0.1994 0.2196 -0.0155 -0.0043 -0.0136 227 ASP A N 1835 C CA . ASP A 227 ? 0.1792 0.2134 0.2567 -0.0068 0.0102 -0.0015 227 ASP A CA 1836 C C . ASP A 227 ? 0.1560 0.2337 0.2271 0.0274 0.0020 -0.0125 227 ASP A C 1837 O O . ASP A 227 ? 0.2197 0.2251 0.2186 0.0020 0.0042 -0.0002 227 ASP A O 1838 C CB . ASP A 227 ? 0.1570 0.2573 0.2874 -0.0199 0.0561 -0.0101 227 ASP A CB 1839 C CG . ASP A 227 ? 0.1974 0.2329 0.2157 0.0101 0.0296 -0.0332 227 ASP A CG 1840 O OD1 . ASP A 227 ? 0.2169 0.2437 0.2555 0.0132 -0.0372 -0.0048 227 ASP A OD1 1841 O OD2 . ASP A 227 ? 0.2007 0.2663 0.3051 0.0028 0.0324 -0.0370 227 ASP A OD2 1842 N N . VAL A 228 ? 0.1773 0.2235 0.2670 0.0168 0.0051 -0.0651 228 VAL A N 1843 C CA . VAL A 228 ? 0.1998 0.2078 0.2512 -0.0010 0.0232 -0.0303 228 VAL A CA 1844 C C . VAL A 228 ? 0.2467 0.2527 0.2517 -0.0001 0.0065 -0.0343 228 VAL A C 1845 O O . VAL A 228 ? 0.2291 0.2701 0.3035 -0.0191 -0.0261 -0.0172 228 VAL A O 1846 C CB . VAL A 228 ? 0.2458 0.2159 0.2436 -0.0062 0.0012 -0.0397 228 VAL A CB 1847 C CG1 . VAL A 228 ? 0.2718 0.2480 0.3042 -0.0676 0.0051 -0.0286 228 VAL A CG1 1848 C CG2 . VAL A 228 ? 0.1931 0.2634 0.2492 0.0086 0.0117 -0.0270 228 VAL A CG2 1849 N N . ARG A 229 ? 0.2442 0.2389 0.2632 -0.0018 0.0256 -0.0251 229 ARG A N 1850 C CA . ARG A 229 ? 0.2310 0.3289 0.2787 -0.0108 -0.0019 -0.0338 229 ARG A CA 1851 C C . ARG A 229 ? 0.2423 0.3029 0.3321 -0.0128 0.0025 -0.0250 229 ARG A C 1852 O O . ARG A 229 ? 0.2760 0.3017 0.3438 -0.0198 0.0264 -0.0757 229 ARG A O 1853 C CB . ARG A 229 ? 0.2304 0.2411 0.2817 -0.0407 0.0344 -0.0320 229 ARG A CB 1854 C CG . ARG A 229 ? 0.2292 0.3676 0.2818 0.0033 0.0483 0.0049 229 ARG A CG 1855 C CD . ARG A 229 ? 0.2501 0.3616 0.3278 0.0070 0.0384 0.0115 229 ARG A CD 1856 N NE . ARG A 229 ? 0.3433 0.3929 0.4056 0.0075 0.0902 -0.0178 229 ARG A NE 1857 C CZ . ARG A 229 ? 0.5118 0.5454 0.4567 -0.0070 0.0018 0.0186 229 ARG A CZ 1858 N NH1 . ARG A 229 ? 0.5261 0.4562 0.4652 -0.0015 -0.0008 0.0316 229 ARG A NH1 1859 N NH2 . ARG A 229 ? 0.5783 0.6379 0.5686 0.0077 0.0574 -0.0161 229 ARG A NH2 1860 N N . ALA A 230 ? 0.2059 0.3288 0.3170 -0.0077 0.0100 -0.0445 230 ALA A N 1861 C CA . ALA A 230 ? 0.2349 0.3824 0.2964 -0.0065 -0.0044 -0.0262 230 ALA A CA 1862 C C . ALA A 230 ? 0.2506 0.3735 0.3221 -0.0134 0.0242 -0.0469 230 ALA A C 1863 O O . ALA A 230 ? 0.2496 0.4352 0.3659 -0.0359 0.0186 -0.0506 230 ALA A O 1864 C CB . ALA A 230 ? 0.3053 0.3452 0.3293 -0.0183 0.0314 -0.0562 230 ALA A CB 1865 N N . SER A 231 ? 0.2077 0.3632 0.3027 -0.0126 0.0068 -0.0319 231 SER A N 1866 C CA . SER A 231 ? 0.2829 0.3403 0.2960 0.0221 0.0350 -0.0358 231 SER A CA 1867 C C . SER A 231 ? 0.3038 0.3611 0.3503 -0.0167 0.0191 -0.0105 231 SER A C 1868 O O . SER A 231 ? 0.2752 0.4038 0.4103 -0.0095 0.0040 -0.0686 231 SER A O 1869 C CB . SER A 231 ? 0.2868 0.3807 0.3223 -0.0221 -0.0012 0.0038 231 SER A CB 1870 O OG . SER A 231 ? 0.2814 0.3918 0.3725 0.0249 0.0044 -0.0461 231 SER A OG 1871 N N . ASN A 232 ? 0.2514 0.3123 0.3576 -0.0500 0.0313 -0.0276 232 ASN A N 1872 C CA . ASN A 232 ? 0.3318 0.3424 0.4114 -0.0087 0.0281 -0.0100 232 ASN A CA 1873 C C . ASN A 232 ? 0.3365 0.2705 0.3184 -0.0062 0.0086 -0.0312 232 ASN A C 1874 O O . ASN A 232 ? 0.3134 0.3226 0.3324 -0.0132 0.0378 -0.0342 232 ASN A O 1875 C CB . ASN A 232 ? 0.3667 0.3613 0.4117 -0.0497 0.0394 -0.0308 232 ASN A CB 1876 C CG . ASN A 232 ? 0.3745 0.3309 0.4629 0.0088 0.0292 -0.0228 232 ASN A CG 1877 O OD1 . ASN A 232 ? 0.3418 0.3869 0.5293 -0.0322 0.0193 -0.0919 232 ASN A OD1 1878 N ND2 . ASN A 232 ? 0.3653 0.4554 0.5092 -0.0482 0.0416 -0.0043 232 ASN A ND2 1879 N N . VAL A 233 ? 0.2379 0.3722 0.3521 -0.0209 0.0201 -0.0652 233 VAL A N 1880 C CA . VAL A 233 ? 0.2876 0.3253 0.3148 -0.0106 0.0196 -0.0176 233 VAL A CA 1881 C C . VAL A 233 ? 0.3527 0.3299 0.3344 0.0086 0.0155 -0.0419 233 VAL A C 1882 O O . VAL A 233 ? 0.2796 0.3325 0.3469 -0.0775 0.0007 -0.0535 233 VAL A O 1883 C CB . VAL A 233 ? 0.4032 0.3302 0.3212 -0.0067 0.0202 -0.0122 233 VAL A CB 1884 C CG1 . VAL A 233 ? 0.3529 0.3051 0.2746 0.0127 0.0228 -0.0173 233 VAL A CG1 1885 C CG2 . VAL A 233 ? 0.3078 0.3454 0.3872 0.0049 0.0108 -0.0587 233 VAL A CG2 1886 N N A SER A 234 ? 0.3619 0.3991 0.3643 -0.0281 0.0109 -0.0168 234 SER A N 1887 N N B SER A 234 ? 0.3471 0.3823 0.3414 -0.0273 0.0106 -0.0167 234 SER A N 1888 C CA A SER A 234 ? 0.3880 0.3864 0.3960 -0.0210 0.0014 -0.0156 234 SER A CA 1889 C CA B SER A 234 ? 0.3449 0.3526 0.3689 -0.0427 -0.0042 -0.0234 234 SER A CA 1890 C C A SER A 234 ? 0.3459 0.3513 0.3953 -0.0092 -0.0081 -0.0044 234 SER A C 1891 C C B SER A 234 ? 0.3175 0.3448 0.3735 -0.0149 -0.0045 -0.0040 234 SER A C 1892 O O A SER A 234 ? 0.3895 0.3567 0.4122 -0.0163 -0.0045 -0.0019 234 SER A O 1893 O O B SER A 234 ? 0.3525 0.3309 0.4074 -0.0337 -0.0028 -0.0093 234 SER A O 1894 C CB A SER A 234 ? 0.4183 0.4145 0.4395 -0.0243 -0.0098 -0.0126 234 SER A CB 1895 C CB B SER A 234 ? 0.2849 0.3523 0.3660 -0.0010 0.0059 -0.0084 234 SER A CB 1896 O OG A SER A 234 ? 0.4202 0.4461 0.4810 -0.0209 -0.0077 -0.0044 234 SER A OG 1897 O OG B SER A 234 ? 0.3700 0.3950 0.3907 -0.0484 -0.0142 -0.0168 234 SER A OG 1898 N N . LEU A 235 ? 0.2785 0.3503 0.3994 -0.0618 0.0116 -0.0486 235 LEU A N 1899 C CA . LEU A 235 ? 0.3335 0.2517 0.3581 -0.0015 0.0044 -0.0056 235 LEU A CA 1900 C C . LEU A 235 ? 0.3402 0.3409 0.3437 -0.0021 0.0341 -0.0072 235 LEU A C 1901 O O . LEU A 235 ? 0.3358 0.2811 0.3454 -0.0352 0.0299 -0.0345 235 LEU A O 1902 C CB . LEU A 235 ? 0.2950 0.2534 0.3680 0.0162 0.0254 0.0129 235 LEU A CB 1903 C CG . LEU A 235 ? 0.3718 0.4371 0.4676 0.0069 0.0090 0.0058 235 LEU A CG 1904 C CD1 . LEU A 235 ? 0.3022 0.4056 0.4747 -0.0471 0.0360 -0.0001 235 LEU A CD1 1905 C CD2 . LEU A 235 ? 0.4811 0.4527 0.5172 -0.0154 0.0276 0.0101 235 LEU A CD2 1906 N N . ARG A 236 ? 0.2979 0.2828 0.3384 -0.0199 0.0459 -0.0360 236 ARG A N 1907 C CA . ARG A 236 ? 0.3189 0.2935 0.3368 -0.0156 0.0134 -0.0132 236 ARG A CA 1908 C C . ARG A 236 ? 0.2593 0.2654 0.2873 -0.0178 0.0452 0.0224 236 ARG A C 1909 O O . ARG A 236 ? 0.2970 0.2314 0.3146 -0.0261 0.0286 0.0253 236 ARG A O 1910 C CB . ARG A 236 ? 0.3386 0.2786 0.2744 -0.0168 0.0379 0.0044 236 ARG A CB 1911 C CG . ARG A 236 ? 0.3517 0.2916 0.3157 0.0424 0.0276 -0.0255 236 ARG A CG 1912 C CD . ARG A 236 ? 0.3779 0.2995 0.3726 0.0479 -0.0066 -0.0631 236 ARG A CD 1913 N NE . ARG A 236 ? 0.5526 0.4753 0.4586 0.0356 0.0332 -0.0295 236 ARG A NE 1914 C CZ . ARG A 236 ? 0.5407 0.4552 0.4385 0.0456 0.0200 -0.0148 236 ARG A CZ 1915 N NH1 . ARG A 236 ? 0.4498 0.3934 0.3647 -0.0361 -0.0167 0.0127 236 ARG A NH1 1916 N NH2 . ARG A 236 ? 0.5373 0.3892 0.4628 0.0368 -0.0027 0.0213 236 ARG A NH2 1917 N N . GLU A 237 ? 0.2792 0.2445 0.3079 0.0121 0.0418 -0.0300 237 GLU A N 1918 C CA . GLU A 237 ? 0.2725 0.2372 0.2725 -0.0409 0.0334 -0.0221 237 GLU A CA 1919 C C . GLU A 237 ? 0.2308 0.2200 0.2896 -0.0109 -0.0144 -0.0101 237 GLU A C 1920 O O . GLU A 237 ? 0.2300 0.2143 0.2754 -0.0279 0.0210 0.0038 237 GLU A O 1921 C CB . GLU A 237 ? 0.2999 0.3185 0.3047 0.0152 0.0527 0.0240 237 GLU A CB 1922 C CG . GLU A 237 ? 0.3761 0.3079 0.3173 0.0108 0.0487 0.0106 237 GLU A CG 1923 C CD . GLU A 237 ? 0.4128 0.4150 0.3954 0.0119 0.0755 0.0230 237 GLU A CD 1924 O OE1 . GLU A 237 ? 0.4061 0.4605 0.4118 0.0676 0.0736 0.0468 237 GLU A OE1 1925 O OE2 . GLU A 237 ? 0.5937 0.5794 0.4750 0.0087 0.0774 0.0721 237 GLU A OE2 1926 N N . ILE A 238 ? 0.2494 0.2474 0.2679 -0.0388 0.0101 -0.0285 238 ILE A N 1927 C CA . ILE A 238 ? 0.1756 0.2247 0.2568 -0.0244 0.0266 -0.0071 238 ILE A CA 1928 C C . ILE A 238 ? 0.2328 0.2368 0.2577 -0.0055 0.0201 0.0095 238 ILE A C 1929 O O . ILE A 238 ? 0.2427 0.2332 0.2718 0.0221 0.0172 -0.0012 238 ILE A O 1930 C CB . ILE A 238 ? 0.2055 0.2124 0.2298 -0.0082 0.0493 -0.0271 238 ILE A CB 1931 C CG1 . ILE A 238 ? 0.2936 0.2158 0.2540 0.0122 -0.0050 -0.0170 238 ILE A CG1 1932 C CG2 . ILE A 238 ? 0.2478 0.2326 0.2895 -0.0366 0.0537 0.0437 238 ILE A CG2 1933 C CD1 . ILE A 238 ? 0.2274 0.3249 0.2845 -0.0107 -0.0251 -0.0100 238 ILE A CD1 1934 N N . ILE A 239 ? 0.2149 0.2152 0.2255 0.0107 0.0163 -0.0036 239 ILE A N 1935 C CA . ILE A 239 ? 0.1911 0.2082 0.2512 -0.0009 0.0389 -0.0124 239 ILE A CA 1936 C C . ILE A 239 ? 0.1788 0.2109 0.2249 0.0117 -0.0161 0.0053 239 ILE A C 1937 O O . ILE A 239 ? 0.1932 0.2371 0.2221 -0.0099 -0.0007 -0.0143 239 ILE A O 1938 C CB . ILE A 239 ? 0.2118 0.2436 0.2587 0.0204 0.0051 0.0220 239 ILE A CB 1939 C CG1 . ILE A 239 ? 0.1693 0.2285 0.2820 -0.0101 0.0134 0.0243 239 ILE A CG1 1940 C CG2 . ILE A 239 ? 0.2569 0.2760 0.2481 -0.0407 0.0265 0.0064 239 ILE A CG2 1941 C CD1 . ILE A 239 ? 0.1941 0.2992 0.3229 0.0062 0.0158 0.0002 239 ILE A CD1 1942 N N . ILE A 240 ? 0.1741 0.1977 0.2129 -0.0121 0.0145 -0.0172 240 ILE A N 1943 C CA . ILE A 240 ? 0.1670 0.1730 0.2195 0.0217 -0.0198 -0.0289 240 ILE A CA 1944 C C . ILE A 240 ? 0.2171 0.1846 0.2373 0.0183 0.0357 0.0097 240 ILE A C 1945 O O . ILE A 240 ? 0.1926 0.2529 0.2421 0.0093 0.0115 0.0138 240 ILE A O 1946 C CB . ILE A 240 ? 0.1600 0.2463 0.2070 -0.0058 -0.0039 -0.0329 240 ILE A CB 1947 C CG1 . ILE A 240 ? 0.2554 0.2018 0.2153 0.0037 -0.0155 0.0027 240 ILE A CG1 1948 C CG2 . ILE A 240 ? 0.1570 0.2937 0.2611 0.0094 0.0319 0.0107 240 ILE A CG2 1949 C CD1 . ILE A 240 ? 0.2490 0.2561 0.2147 -0.0059 -0.0296 -0.0586 240 ILE A CD1 1950 N N . PHE A 241 ? 0.1614 0.2313 0.2236 0.0211 -0.0066 0.0056 241 PHE A N 1951 C CA . PHE A 241 ? 0.1723 0.2258 0.2272 0.0146 -0.0316 0.0114 241 PHE A CA 1952 C C . PHE A 241 ? 0.2270 0.1867 0.2465 0.0395 0.0282 -0.0113 241 PHE A C 1953 O O . PHE A 241 ? 0.1926 0.2361 0.2285 0.0171 0.0172 -0.0077 241 PHE A O 1954 C CB . PHE A 241 ? 0.1672 0.2566 0.2723 -0.0213 -0.0160 -0.0321 241 PHE A CB 1955 C CG . PHE A 241 ? 0.1756 0.2860 0.2221 0.0025 -0.0103 0.0084 241 PHE A CG 1956 C CD1 . PHE A 241 ? 0.1965 0.2762 0.2576 0.0181 0.0081 -0.0095 241 PHE A CD1 1957 C CD2 . PHE A 241 ? 0.1444 0.3013 0.2615 0.0033 -0.0284 -0.0095 241 PHE A CD2 1958 C CE1 . PHE A 241 ? 0.2180 0.3228 0.3053 0.0141 0.0147 0.0034 241 PHE A CE1 1959 C CE2 . PHE A 241 ? 0.1804 0.3453 0.2579 0.0073 -0.0155 -0.0126 241 PHE A CE2 1960 C CZ . PHE A 241 ? 0.2560 0.3520 0.2691 0.0331 0.0191 -0.0216 241 PHE A CZ 1961 N N . PRO A 242 ? 0.1533 0.2528 0.2442 0.0178 0.0183 -0.0134 242 PRO A N 1962 C CA . PRO A 242 ? 0.2074 0.2524 0.1994 0.0507 0.0148 -0.0164 242 PRO A CA 1963 C C . PRO A 242 ? 0.1856 0.2594 0.2367 0.0436 -0.0075 -0.0228 242 PRO A C 1964 O O . PRO A 242 ? 0.1894 0.2509 0.2489 0.0056 0.0203 -0.0318 242 PRO A O 1965 C CB . PRO A 242 ? 0.2390 0.3260 0.2084 0.0745 0.0240 -0.0297 242 PRO A CB 1966 C CG . PRO A 242 ? 0.2969 0.2642 0.4011 0.0235 0.0449 0.0206 242 PRO A CG 1967 C CD . PRO A 242 ? 0.1944 0.2486 0.2731 0.0476 0.0329 -0.0196 242 PRO A CD 1968 N N . ALA A 243 ? 0.2144 0.2672 0.2279 0.0452 0.0004 -0.0063 243 ALA A N 1969 C CA . ALA A 243 ? 0.2053 0.2391 0.2328 0.0314 0.0153 0.0141 243 ALA A CA 1970 C C . ALA A 243 ? 0.2011 0.2329 0.2097 0.0148 -0.0191 -0.0218 243 ALA A C 1971 O O . ALA A 243 ? 0.2127 0.2277 0.2460 0.0383 -0.0009 -0.0237 243 ALA A O 1972 C CB . ALA A 243 ? 0.2308 0.1898 0.2732 0.0357 0.0392 0.0067 243 ALA A CB 1973 N N . THR A 244 ? 0.1952 0.2640 0.2460 -0.0043 -0.0037 -0.0515 244 THR A N 1974 C CA . THR A 244 ? 0.1953 0.2487 0.2524 0.0013 -0.0225 -0.0024 244 THR A CA 1975 C C . THR A 244 ? 0.2781 0.2955 0.2842 0.0911 0.0070 -0.0517 244 THR A C 1976 O O . THR A 244 ? 0.3613 0.3102 0.2904 0.0702 -0.0625 -0.0244 244 THR A O 1977 C CB . THR A 244 ? 0.2718 0.2081 0.2042 0.0194 0.0044 -0.0479 244 THR A CB 1978 O OG1 . THR A 244 ? 0.2420 0.2420 0.3359 0.0454 -0.0442 -0.0434 244 THR A OG1 1979 C CG2 . THR A 244 ? 0.2040 0.2612 0.2454 0.0434 0.0127 0.0052 244 THR A CG2 1980 N N . GLY A 245 ? 0.2543 0.2749 0.2237 0.0483 0.0268 -0.0211 245 GLY A N 1981 C CA . GLY A 245 ? 0.3853 0.3034 0.2207 -0.0041 0.0233 -0.0213 245 GLY A CA 1982 C C . GLY A 245 ? 0.3114 0.3122 0.2649 0.0000 -0.0112 -0.0073 245 GLY A C 1983 O O . GLY A 245 ? 0.4632 0.4197 0.2756 0.0316 0.0154 -0.0542 245 GLY A O 1984 N N . ASN A 246 ? 0.3058 0.2505 0.3476 0.0353 -0.0424 0.0088 246 ASN A N 1985 C CA . ASN A 246 ? 0.2807 0.2819 0.3296 0.0517 -0.0309 -0.0355 246 ASN A CA 1986 C C . ASN A 246 ? 0.2822 0.2848 0.3292 0.0522 -0.0390 -0.0505 246 ASN A C 1987 O O . ASN A 246 ? 0.2972 0.2988 0.2594 0.0532 -0.0415 -0.0442 246 ASN A O 1988 C CB . ASN A 246 ? 0.2389 0.3529 0.3613 0.0520 -0.0226 -0.0403 246 ASN A CB 1989 C CG . ASN A 246 ? 0.2957 0.3410 0.3839 0.0341 -0.0181 -0.0034 246 ASN A CG 1990 O OD1 . ASN A 246 ? 0.3514 0.3585 0.4631 0.0799 -0.0448 0.0148 246 ASN A OD1 1991 N ND2 . ASN A 246 ? 0.2679 0.3790 0.3751 0.0529 -0.0187 -0.0754 246 ASN A ND2 1992 N N . PRO A 247 ? 0.2769 0.2717 0.3157 0.0759 -0.0452 -0.0299 247 PRO A N 1993 C CA . PRO A 247 ? 0.2649 0.2430 0.2906 0.0804 -0.0780 -0.0186 247 PRO A CA 1994 C C . PRO A 247 ? 0.2744 0.2843 0.2161 0.0252 -0.0338 0.0169 247 PRO A C 1995 O O . PRO A 247 ? 0.2567 0.2907 0.2877 0.0103 -0.0353 -0.0412 247 PRO A O 1996 C CB . PRO A 247 ? 0.3488 0.2681 0.3131 0.0274 -0.0589 -0.0353 247 PRO A CB 1997 C CG . PRO A 247 ? 0.3672 0.3554 0.2829 0.0560 -0.0631 -0.0473 247 PRO A CG 1998 C CD . PRO A 247 ? 0.2751 0.3029 0.3306 0.0381 -0.0653 -0.0814 247 PRO A CD 1999 N N . ASN A 248 ? 0.2552 0.2331 0.2196 0.0359 -0.0262 -0.0203 248 ASN A N 2000 C CA . ASN A 248 ? 0.2501 0.1849 0.2363 -0.0010 -0.0286 -0.0255 248 ASN A CA 2001 C C . ASN A 248 ? 0.2108 0.1869 0.2245 0.0084 -0.0401 -0.0115 248 ASN A C 2002 O O . ASN A 248 ? 0.2152 0.2639 0.2414 0.0169 -0.0063 -0.0227 248 ASN A O 2003 C CB . ASN A 248 ? 0.2435 0.2774 0.3104 0.0145 0.0361 -0.0268 248 ASN A CB 2004 C CG . ASN A 248 ? 0.2342 0.2841 0.2825 -0.0024 0.0283 -0.0127 248 ASN A CG 2005 O OD1 . ASN A 248 ? 0.2814 0.2824 0.3178 0.0546 0.0049 -0.0515 248 ASN A OD1 2006 N ND2 . ASN A 248 ? 0.2021 0.2708 0.2702 0.0295 -0.0272 -0.0260 248 ASN A ND2 2007 N N . GLN A 249 ? 0.2321 0.2118 0.2259 -0.0037 0.0057 -0.0103 249 GLN A N 2008 C CA . GLN A 249 ? 0.2503 0.2192 0.2343 -0.0070 0.0254 -0.0484 249 GLN A CA 2009 C C . GLN A 249 ? 0.2437 0.2336 0.2289 0.0300 -0.0071 -0.0038 249 GLN A C 2010 O O . GLN A 249 ? 0.2439 0.2552 0.2369 0.0240 -0.0022 -0.0246 249 GLN A O 2011 C CB . GLN A 249 ? 0.2457 0.2237 0.2114 0.0327 0.0172 -0.0385 249 GLN A CB 2012 C CG . GLN A 249 ? 0.2371 0.2173 0.2667 0.0170 0.0605 -0.0189 249 GLN A CG 2013 C CD . GLN A 249 ? 0.2077 0.2460 0.2122 0.0312 -0.0225 -0.0117 249 GLN A CD 2014 O OE1 . GLN A 249 ? 0.2185 0.2517 0.2725 0.0138 -0.0280 -0.0172 249 GLN A OE1 2015 N NE2 . GLN A 249 ? 0.2077 0.3354 0.2471 0.0231 0.0089 -0.0003 249 GLN A NE2 2016 N N . GLN A 250 ? 0.2297 0.2681 0.2111 0.0281 0.0044 -0.0504 250 GLN A N 2017 C CA . GLN A 250 ? 0.2693 0.2908 0.2143 0.0319 -0.0205 -0.0042 250 GLN A CA 2018 C C . GLN A 250 ? 0.2382 0.2356 0.2036 -0.0068 0.0047 0.0121 250 GLN A C 2019 O O . GLN A 250 ? 0.2309 0.2054 0.2715 0.0203 0.0136 -0.0331 250 GLN A O 2020 C CB . GLN A 250 ? 0.3128 0.2909 0.2102 0.0785 -0.0260 -0.0062 250 GLN A CB 2021 C CG . GLN A 250 ? 0.3290 0.3275 0.3751 0.0961 -0.0331 -0.0105 250 GLN A CG 2022 C CD . GLN A 250 ? 0.6194 0.5836 0.5986 -0.0357 0.0140 0.0264 250 GLN A CD 2023 O OE1 . GLN A 250 ? 0.5506 0.5958 0.5819 0.0025 -0.0545 0.0041 250 GLN A OE1 2024 N NE2 . GLN A 250 ? 0.7467 0.7143 0.7420 0.0396 0.0048 -0.0205 250 GLN A NE2 2025 N N . TRP A 251 ? 0.2353 0.2492 0.2221 0.0093 0.0017 -0.0002 251 TRP A N 2026 C CA . TRP A 251 ? 0.1960 0.2582 0.2339 0.0073 0.0035 0.0308 251 TRP A CA 2027 C C . TRP A 251 ? 0.2546 0.1984 0.2204 0.0230 0.0304 0.0157 251 TRP A C 2028 O O . TRP A 251 ? 0.2865 0.2156 0.3043 0.0324 0.0283 0.0134 251 TRP A O 2029 C CB . TRP A 251 ? 0.2335 0.2679 0.2116 -0.0068 0.0035 0.0167 251 TRP A CB 2030 C CG . TRP A 251 ? 0.1929 0.2171 0.1934 0.0224 0.0149 0.0047 251 TRP A CG 2031 C CD1 . TRP A 251 ? 0.2348 0.2592 0.1760 0.0154 -0.0027 -0.0246 251 TRP A CD1 2032 C CD2 . TRP A 251 ? 0.2319 0.1875 0.1815 0.0200 0.0259 -0.0233 251 TRP A CD2 2033 N NE1 . TRP A 251 ? 0.2234 0.2179 0.2387 0.0040 -0.0161 0.0106 251 TRP A NE1 2034 C CE2 . TRP A 251 ? 0.2261 0.2037 0.1853 -0.0189 -0.0002 -0.0134 251 TRP A CE2 2035 C CE3 . TRP A 251 ? 0.2228 0.1888 0.2253 0.0049 -0.0262 -0.0423 251 TRP A CE3 2036 C CZ2 . TRP A 251 ? 0.1967 0.1993 0.2328 -0.0064 -0.0322 -0.0078 251 TRP A CZ2 2037 C CZ3 . TRP A 251 ? 0.1862 0.2381 0.2225 0.0031 0.0185 -0.0185 251 TRP A CZ3 2038 C CH2 . TRP A 251 ? 0.2051 0.2106 0.1854 0.0221 0.0048 -0.0146 251 TRP A CH2 2039 N N A VAL A 252 ? 0.2231 0.2371 0.2184 0.0081 0.0081 -0.0054 252 VAL A N 2040 N N B VAL A 252 ? 0.2442 0.2448 0.2340 0.0120 0.0086 -0.0085 252 VAL A N 2041 C CA A VAL A 252 ? 0.2532 0.2552 0.2255 -0.0028 0.0109 -0.0095 252 VAL A CA 2042 C CA B VAL A 252 ? 0.2794 0.2478 0.2767 -0.0049 0.0193 -0.0115 252 VAL A CA 2043 C C A VAL A 252 ? 0.2564 0.2407 0.2543 -0.0149 0.0043 -0.0112 252 VAL A C 2044 C C B VAL A 252 ? 0.2655 0.2576 0.2682 -0.0173 0.0077 -0.0124 252 VAL A C 2045 O O A VAL A 252 ? 0.2795 0.2202 0.2765 0.0015 0.0320 0.0165 252 VAL A O 2046 O O B VAL A 252 ? 0.2479 0.2526 0.2785 0.0005 0.0240 0.0192 252 VAL A O 2047 C CB A VAL A 252 ? 0.2199 0.2488 0.2114 0.0265 0.0133 -0.0120 252 VAL A CB 2048 C CB B VAL A 252 ? 0.2960 0.3482 0.3052 0.0028 -0.0161 0.0196 252 VAL A CB 2049 C CG1 A VAL A 252 ? 0.3207 0.2857 0.3228 0.0395 -0.0135 0.0107 252 VAL A CG1 2050 C CG1 B VAL A 252 ? 0.3810 0.4329 0.3604 -0.0030 0.0367 0.0235 252 VAL A CG1 2051 C CG2 A VAL A 252 ? 0.2204 0.1977 0.1560 0.0260 -0.0310 -0.0134 252 VAL A CG2 2052 C CG2 B VAL A 252 ? 0.2925 0.3133 0.2746 -0.0075 0.0004 0.0154 252 VAL A CG2 2053 N N . THR A 253 ? 0.2185 0.2882 0.2721 0.0068 0.0204 -0.0096 253 THR A N 2054 C CA . THR A 253 ? 0.2717 0.2664 0.2514 0.0101 0.0118 -0.0262 253 THR A CA 2055 C C . THR A 253 ? 0.2625 0.2012 0.2317 0.0117 0.0222 0.0041 253 THR A C 2056 O O . THR A 253 ? 0.3984 0.2877 0.2584 0.0403 0.0689 0.0406 253 THR A O 2057 C CB . THR A 253 ? 0.3057 0.2899 0.2886 -0.0376 0.0276 0.0225 253 THR A CB 2058 O OG1 . THR A 253 ? 0.3529 0.3090 0.3938 -0.0289 0.0061 0.0444 253 THR A OG1 2059 C CG2 . THR A 253 ? 0.3372 0.3617 0.3216 0.0004 0.0190 -0.0115 253 THR A CG2 2060 N N . GLN A 254 ? 0.2888 0.1914 0.2035 0.0236 0.0341 0.0008 254 GLN A N 2061 C CA . GLN A 254 ? 0.2552 0.2977 0.2097 0.0152 0.0354 -0.0157 254 GLN A CA 2062 C C . GLN A 254 ? 0.2356 0.2448 0.2489 0.0000 0.0644 0.0217 254 GLN A C 2063 O O . GLN A 254 ? 0.3095 0.2569 0.2621 0.0310 0.0390 0.0479 254 GLN A O 2064 C CB . GLN A 254 ? 0.2917 0.3530 0.2447 0.0112 -0.0188 -0.0131 254 GLN A CB 2065 C CG . GLN A 254 ? 0.3036 0.3699 0.3265 0.0241 0.0133 -0.0236 254 GLN A CG 2066 C CD . GLN A 254 ? 0.5362 0.5224 0.4333 0.0201 -0.0124 0.0306 254 GLN A CD 2067 O OE1 . GLN A 254 ? 0.6039 0.5623 0.5329 0.0648 -0.0042 -0.0063 254 GLN A OE1 2068 N NE2 . GLN A 254 ? 0.5663 0.6288 0.5246 -0.0039 0.0170 0.0016 254 GLN A NE2 2069 N N . VAL A 255 ? 0.2422 0.2738 0.2487 -0.0175 0.0538 0.0164 255 VAL A N 2070 C CA . VAL A 255 ? 0.2965 0.3194 0.2588 -0.0042 0.0237 0.0037 255 VAL A CA 2071 C C . VAL A 255 ? 0.2931 0.3427 0.3189 0.0069 0.0285 0.0048 255 VAL A C 2072 O O . VAL A 255 ? 0.3130 0.3088 0.2774 0.0274 0.0310 -0.0053 255 VAL A O 2073 C CB . VAL A 255 ? 0.3694 0.3507 0.4599 -0.0244 0.0152 0.0065 255 VAL A CB 2074 C CG1 . VAL A 255 ? 0.3869 0.4243 0.4947 -0.0080 0.0346 0.0163 255 VAL A CG1 2075 C CG2 . VAL A 255 ? 0.4823 0.3432 0.4640 -0.0206 0.0205 0.0110 255 VAL A CG2 2076 N N . LEU A 256 ? 0.2903 0.2645 0.2472 0.0128 0.0352 0.0041 256 LEU A N 2077 C CA . LEU A 256 ? 0.2911 0.2084 0.2733 0.0490 0.0026 0.0151 256 LEU A CA 2078 C C . LEU A 256 ? 0.3355 0.3529 0.2840 -0.0140 0.0123 -0.0068 256 LEU A C 2079 O O . LEU A 256 ? 0.3139 0.3122 0.3669 -0.0335 -0.0007 -0.0145 256 LEU A O 2080 C CB . LEU A 256 ? 0.2442 0.2945 0.2678 0.0153 -0.0115 0.0273 256 LEU A CB 2081 C CG . LEU A 256 ? 0.2808 0.2960 0.2727 -0.0292 0.0113 -0.0492 256 LEU A CG 2082 C CD1 . LEU A 256 ? 0.3582 0.2805 0.2869 0.0166 0.0164 0.0329 256 LEU A CD1 2083 C CD2 . LEU A 256 ? 0.3306 0.3432 0.4045 -0.0473 -0.0067 -0.0416 256 LEU A CD2 2084 N N . PRO A 257 ? 0.2996 0.3028 0.3201 0.0132 0.0389 -0.0066 257 PRO A N 2085 C CA . PRO A 257 ? 0.3440 0.3277 0.3282 0.0397 0.0193 0.0210 257 PRO A CA 2086 C C . PRO A 257 ? 0.3890 0.5064 0.4286 0.0069 -0.0239 0.0240 257 PRO A C 2087 O O . PRO A 257 ? 0.4045 0.4353 0.3991 0.0147 0.0059 -0.0085 257 PRO A O 2088 C CB . PRO A 257 ? 0.3936 0.3059 0.3351 -0.0019 0.0607 -0.0476 257 PRO A CB 2089 C CG . PRO A 257 ? 0.3747 0.3173 0.3428 0.0226 0.0140 -0.0366 257 PRO A CG 2090 C CD . PRO A 257 ? 0.3544 0.2683 0.3142 0.0107 0.0129 -0.0300 257 PRO A CD 2091 C C1 . NAG B . ? 0.3979 0.4668 0.3733 0.0106 0.0238 0.0343 258 NAG A C1 2092 C C2 . NAG B . ? 0.4183 0.5208 0.3889 0.0082 0.0368 0.0149 258 NAG A C2 2093 C C3 . NAG B . ? 0.4651 0.5299 0.4033 0.0136 0.0342 0.0195 258 NAG A C3 2094 C C4 . NAG B . ? 0.4464 0.5324 0.4764 -0.0045 0.0389 -0.0050 258 NAG A C4 2095 C C5 . NAG B . ? 0.4625 0.5066 0.4278 -0.0157 0.0169 0.0162 258 NAG A C5 2096 C C6 . NAG B . ? 0.5265 0.5170 0.5246 0.0211 0.0069 -0.0131 258 NAG A C6 2097 C C7 . NAG B . ? 0.6210 0.6206 0.6490 0.0070 0.0081 -0.0105 258 NAG A C7 2098 C C8 . NAG B . ? 0.6652 0.7082 0.7096 0.0292 -0.0036 0.0051 258 NAG A C8 2099 N N2 . NAG B . ? 0.4587 0.6019 0.5175 0.0336 0.0066 0.0389 258 NAG A N2 2100 O O3 . NAG B . ? 0.4316 0.6424 0.4293 -0.0380 0.0546 0.0404 258 NAG A O3 2101 O O4 . NAG B . ? 0.5201 0.5906 0.6169 -0.0272 0.0181 -0.0123 258 NAG A O4 2102 O O5 . NAG B . ? 0.4139 0.4885 0.3485 0.0224 0.0320 0.0285 258 NAG A O5 2103 O O6 . NAG B . ? 0.4247 0.5779 0.5015 0.0088 0.0143 0.0201 258 NAG A O6 2104 O O7 . NAG B . ? 0.6701 0.7334 0.7190 -0.0091 -0.0042 0.0002 258 NAG A O7 2105 C C1 . NAG C . ? 0.6399 0.6732 0.6135 0.0110 0.0009 0.0029 259 NAG A C1 2106 C C2 . NAG C . ? 0.7648 0.7450 0.8748 -0.0308 -0.0050 -0.0034 259 NAG A C2 2107 C C3 . NAG C . ? 0.8077 0.7848 0.7527 0.0190 0.0000 0.0074 259 NAG A C3 2108 C C4 . NAG C . ? 0.7192 0.7145 0.7601 -0.0162 -0.0034 0.0072 259 NAG A C4 2109 C C5 . NAG C . ? 0.6307 0.6426 0.6149 0.0197 -0.0004 -0.0079 259 NAG A C5 2110 C C6 . NAG C . ? 0.6090 0.5688 0.5908 0.0097 -0.0114 0.0257 259 NAG A C6 2111 C C7 . NAG C . ? 1.0256 1.0307 0.9666 -0.0601 -0.0033 0.0299 259 NAG A C7 2112 C C8 . NAG C . ? 0.9235 0.8636 0.8585 0.0215 0.0084 -0.0354 259 NAG A C8 2113 N N2 . NAG C . ? 0.7746 0.8242 0.7351 -0.0063 -0.0047 -0.0250 259 NAG A N2 2114 O O3 . NAG C . ? 0.9150 0.8780 0.9374 -0.0195 0.0021 -0.0085 259 NAG A O3 2115 O O4 . NAG C . ? 0.6892 0.7318 0.7658 0.0048 -0.0059 0.0097 259 NAG A O4 2116 O O5 . NAG C . ? 0.6022 0.6582 0.6060 -0.0117 0.0070 -0.0032 259 NAG A O5 2117 O O6 . NAG C . ? 0.5781 0.6243 0.5724 -0.0221 0.0033 0.0038 259 NAG A O6 2118 O O7 . NAG C . ? 0.8576 0.8889 0.9672 0.0453 -0.0117 -0.0074 259 NAG A O7 2119 C C1 . FUC D . ? 0.4840 0.5956 0.5484 0.0025 0.0033 -0.0136 260 FUC A C1 2120 C C2 . FUC D . ? 0.5375 0.6174 0.5728 -0.0008 0.0303 -0.0140 260 FUC A C2 2121 C C3 . FUC D . ? 0.6710 0.6552 0.6539 0.0016 -0.0015 0.0078 260 FUC A C3 2122 C C4 . FUC D . ? 0.6970 0.6818 0.6578 -0.0068 0.0132 -0.0001 260 FUC A C4 2123 C C5 . FUC D . ? 0.6090 0.6266 0.6261 -0.0117 0.0012 0.0017 260 FUC A C5 2124 C C6 . FUC D . ? 0.6900 0.6735 0.6700 -0.0111 0.0027 -0.0059 260 FUC A C6 2125 O O2 . FUC D . ? 0.5161 0.6220 0.5268 0.0104 0.0491 -0.0175 260 FUC A O2 2126 O O3 . FUC D . ? 0.7375 0.7997 0.7078 -0.0142 0.0438 0.0093 260 FUC A O3 2127 O O4 . FUC D . ? 0.7038 0.7515 0.7231 -0.0108 -0.0201 -0.0092 260 FUC A O4 2128 O O5 . FUC D . ? 0.5440 0.6267 0.5718 -0.0084 0.0030 -0.0081 260 FUC A O5 2129 C C1 . NAG E . ? 0.3408 0.3487 0.3736 -0.0465 0.0228 0.0195 261 NAG A C1 2130 C C2 . NAG E . ? 0.4184 0.3853 0.4288 -0.0040 0.0228 0.0128 261 NAG A C2 2131 C C3 . NAG E . ? 0.4780 0.4320 0.4928 -0.0283 0.0224 0.0180 261 NAG A C3 2132 C C4 . NAG E . ? 0.4981 0.4294 0.4779 -0.0229 0.0125 0.0384 261 NAG A C4 2133 C C5 . NAG E . ? 0.5119 0.4503 0.4818 -0.0230 0.0193 0.0209 261 NAG A C5 2134 C C6 . NAG E . ? 0.4844 0.4426 0.5573 -0.0115 0.0207 -0.0138 261 NAG A C6 2135 C C7 . NAG E . ? 0.3346 0.4088 0.3847 -0.0216 0.0217 0.0278 261 NAG A C7 2136 C C8 . NAG E . ? 0.4627 0.4299 0.4167 -0.0141 0.0055 0.0198 261 NAG A C8 2137 N N2 . NAG E . ? 0.3833 0.4158 0.4443 -0.0072 0.0066 0.0060 261 NAG A N2 2138 O O3 . NAG E . ? 0.4913 0.4510 0.5528 -0.0214 0.0399 0.0369 261 NAG A O3 2139 O O4 . NAG E . ? 0.5036 0.4779 0.5546 -0.0265 0.0505 0.0558 261 NAG A O4 2140 O O5 . NAG E . ? 0.3858 0.4216 0.4735 -0.0078 0.0311 -0.0056 261 NAG A O5 2141 O O6 . NAG E . ? 0.5788 0.5224 0.5614 -0.0384 0.0041 -0.0098 261 NAG A O6 2142 O O7 . NAG E . ? 0.3994 0.4319 0.4665 0.0310 -0.0063 0.0574 261 NAG A O7 2143 C C1 . NAG F . ? 0.5657 0.5794 0.6483 -0.0288 -0.0063 0.0054 262 NAG A C1 2144 C C2 . NAG F . ? 0.6454 0.5815 0.6832 -0.0008 0.0151 0.0251 262 NAG A C2 2145 C C3 . NAG F . ? 0.6756 0.7168 0.7460 -0.0023 -0.0039 0.0124 262 NAG A C3 2146 C C4 . NAG F . ? 0.7478 0.7202 0.7544 0.0104 0.0155 0.0085 262 NAG A C4 2147 C C5 . NAG F . ? 0.6600 0.6849 0.7288 -0.0022 -0.0004 -0.0028 262 NAG A C5 2148 C C6 . NAG F . ? 0.6446 0.6846 0.7046 -0.0085 0.0097 0.0000 262 NAG A C6 2149 C C7 . NAG F . ? 0.6508 0.6640 0.7107 -0.0197 0.0011 0.0101 262 NAG A C7 2150 C C8 . NAG F . ? 0.7053 0.7071 0.7386 -0.0005 0.0185 -0.0037 262 NAG A C8 2151 N N2 . NAG F . ? 0.6183 0.5324 0.6302 -0.0247 0.0230 0.0320 262 NAG A N2 2152 O O3 . NAG F . ? 0.7490 0.7390 0.7582 -0.0230 0.0026 0.0167 262 NAG A O3 2153 O O4 . NAG F . ? 0.7930 0.7873 0.8500 -0.0121 -0.0169 -0.0080 262 NAG A O4 2154 O O5 . NAG F . ? 0.6360 0.6641 0.7239 0.0186 0.0235 0.0079 262 NAG A O5 2155 O O6 . NAG F . ? 0.6467 0.6575 0.7376 0.0130 0.0080 -0.0220 262 NAG A O6 2156 O O7 . NAG F . ? 0.7437 0.7282 0.7315 -0.0263 -0.0011 0.0099 262 NAG A O7 2157 C C1 . FUC G . ? 0.6467 0.6638 0.6146 -0.0076 -0.0048 -0.0013 263 FUC A C1 2158 C C2 . FUC G . ? 0.6942 0.6654 0.6926 0.0218 0.0082 0.0000 263 FUC A C2 2159 C C3 . FUC G . ? 0.7209 0.7247 0.7626 0.0010 0.0041 0.0047 263 FUC A C3 2160 C C4 . FUC G . ? 0.7344 0.7430 0.7385 -0.0086 0.0032 0.0109 263 FUC A C4 2161 C C5 . FUC G . ? 0.7425 0.7561 0.7623 -0.0020 0.0073 0.0024 263 FUC A C5 2162 C C6 . FUC G . ? 0.8073 0.7842 0.8205 -0.0057 0.0038 0.0199 263 FUC A C6 2163 O O2 . FUC G . ? 0.6614 0.6639 0.6959 -0.0197 0.0382 0.0067 263 FUC A O2 2164 O O3 . FUC G . ? 0.7288 0.7802 0.7617 -0.0078 0.0275 -0.0090 263 FUC A O3 2165 O O4 . FUC G . ? 0.7236 0.7735 0.7150 -0.0061 0.0102 0.0150 263 FUC A O4 2166 O O5 . FUC G . ? 0.7308 0.7035 0.7172 0.0067 -0.0077 0.0266 263 FUC A O5 2167 C C1 . NAG H . ? 0.2926 0.3712 0.3175 0.0379 0.0038 -0.0027 264 NAG A C1 2168 C C2 . NAG H . ? 0.3647 0.4101 0.3551 0.0082 -0.0017 -0.0124 264 NAG A C2 2169 C C3 . NAG H . ? 0.3186 0.4719 0.4166 0.0540 0.0178 -0.0365 264 NAG A C3 2170 C C4 . NAG H . ? 0.3586 0.4896 0.4306 -0.0006 0.0011 0.0340 264 NAG A C4 2171 C C5 . NAG H . ? 0.3297 0.4704 0.3440 -0.0127 0.0081 0.0378 264 NAG A C5 2172 C C6 . NAG H . ? 0.3558 0.4309 0.4654 -0.0098 -0.0198 0.0246 264 NAG A C6 2173 C C7 . NAG H . ? 0.3924 0.3660 0.3380 0.0438 0.0253 -0.0341 264 NAG A C7 2174 C C8 . NAG H . ? 0.3864 0.4448 0.3301 0.0122 0.0000 0.0034 264 NAG A C8 2175 N N2 . NAG H . ? 0.4002 0.4015 0.3129 0.0637 0.0398 -0.0110 264 NAG A N2 2176 O O3 . NAG H . ? 0.5453 0.4877 0.4802 0.0705 0.0255 -0.0413 264 NAG A O3 2177 O O4 . NAG H . ? 0.2655 0.5702 0.4795 0.0857 0.0876 0.0120 264 NAG A O4 2178 O O5 . NAG H . ? 0.2445 0.4356 0.3397 0.0719 0.0301 0.0179 264 NAG A O5 2179 O O6 . NAG H . ? 0.3427 0.4144 0.4550 0.0912 0.0417 0.0213 264 NAG A O6 2180 O O7 . NAG H . ? 0.3653 0.4448 0.3872 0.0135 0.0398 0.0041 264 NAG A O7 2181 C C1 . NAG I . ? 0.4754 0.4707 0.5354 0.0528 0.0029 -0.0305 265 NAG A C1 2182 C C2 . NAG I . ? 0.4795 0.6285 0.5916 -0.0081 0.0017 -0.0165 265 NAG A C2 2183 C C3 . NAG I . ? 0.6136 0.6250 0.6735 0.0358 0.0139 -0.0159 265 NAG A C3 2184 C C4 . NAG I . ? 0.6405 0.6605 0.6946 -0.0191 -0.0146 -0.0166 265 NAG A C4 2185 C C5 . NAG I . ? 0.5616 0.5874 0.6498 0.0508 -0.0038 -0.0067 265 NAG A C5 2186 C C6 . NAG I . ? 0.6148 0.6545 0.6205 0.0225 0.0084 -0.0113 265 NAG A C6 2187 C C7 . NAG I . ? 0.5867 0.5936 0.5890 0.0029 0.0030 0.0050 265 NAG A C7 2188 C C8 . NAG I . ? 0.5737 0.6434 0.5796 0.0046 -0.0097 0.0175 265 NAG A C8 2189 N N2 . NAG I . ? 0.4039 0.5919 0.5913 0.0276 0.0197 -0.0078 265 NAG A N2 2190 O O3 . NAG I . ? 0.6238 0.7049 0.7180 0.0020 0.0271 -0.0055 265 NAG A O3 2191 O O4 . NAG I . ? 0.7105 0.7497 0.7701 0.0353 -0.0309 -0.0109 265 NAG A O4 2192 O O5 . NAG I . ? 0.4896 0.5209 0.4889 0.0448 0.0391 -0.0289 265 NAG A O5 2193 O O6 . NAG I . ? 0.6760 0.6988 0.6585 0.0241 0.0310 0.0084 265 NAG A O6 2194 O O7 . NAG I . ? 0.5312 0.6232 0.5338 0.0131 0.0185 0.0082 265 NAG A O7 2195 C C1 . NAG J . ? 0.5360 0.4697 0.5645 -0.0194 0.0156 -0.0200 266 NAG A C1 2196 C C2 . NAG J . ? 0.5420 0.5902 0.6134 0.0058 0.0056 -0.0010 266 NAG A C2 2197 C C3 . NAG J . ? 0.6701 0.6293 0.7079 -0.0082 -0.0017 -0.0047 266 NAG A C3 2198 C C4 . NAG J . ? 0.7114 0.7229 0.7063 -0.0105 0.0048 0.0082 266 NAG A C4 2199 C C5 . NAG J . ? 0.6768 0.6169 0.6824 -0.0124 -0.0130 0.0015 266 NAG A C5 2200 C C6 . NAG J . ? 0.6287 0.5596 0.6261 -0.0280 0.0165 0.0137 266 NAG A C6 2201 C C7 . NAG J . ? 0.5893 0.5934 0.6209 -0.0075 -0.0013 0.0069 266 NAG A C7 2202 C C8 . NAG J . ? 0.5582 0.5699 0.6182 -0.0264 0.0074 -0.0003 266 NAG A C8 2203 N N2 . NAG J . ? 0.5222 0.5794 0.6302 -0.0222 -0.0012 0.0045 266 NAG A N2 2204 O O3 . NAG J . ? 0.7108 0.7784 0.7973 -0.0056 0.0223 -0.0186 266 NAG A O3 2205 O O4 . NAG J . ? 0.7840 0.7470 0.7676 -0.0434 0.0067 -0.0100 266 NAG A O4 2206 O O5 . NAG J . ? 0.5865 0.5803 0.6506 -0.0148 0.0040 0.0252 266 NAG A O5 2207 O O6 . NAG J . ? 0.6634 0.5540 0.6655 -0.0405 0.0243 -0.0016 266 NAG A O6 2208 O O7 . NAG J . ? 0.6842 0.7183 0.7145 -0.0311 0.0135 -0.0151 266 NAG A O7 2209 C C1 . AMG K . ? 0.2586 0.3423 0.2551 0.0603 -0.0136 0.0265 267 AMG A C1 2210 C C2 . AMG K . ? 0.1839 0.3431 0.1924 0.0215 0.0412 0.0148 267 AMG A C2 2211 C C3 . AMG K . ? 0.1978 0.2771 0.1970 0.0064 0.0154 0.0444 267 AMG A C3 2212 C C4 . AMG K . ? 0.2393 0.2227 0.2207 0.0340 0.0138 -0.0021 267 AMG A C4 2213 C C5 . AMG K . ? 0.1762 0.3036 0.2441 -0.0147 0.0260 0.0627 267 AMG A C5 2214 C C6 . AMG K . ? 0.2556 0.2369 0.2243 0.0249 -0.0180 0.0212 267 AMG A C6 2215 C C7 . AMG K . ? 0.3562 0.3738 0.3306 0.0718 -0.0419 0.0148 267 AMG A C7 2216 O O1 . AMG K . ? 0.2807 0.3810 0.2724 0.0748 -0.0395 -0.0227 267 AMG A O1 2217 O O2 . AMG K . ? 0.2305 0.3913 0.2384 0.0597 0.0461 -0.0111 267 AMG A O2 2218 O O3 . AMG K . ? 0.2170 0.2876 0.1652 0.0438 -0.0019 0.0000 267 AMG A O3 2219 O O4 . AMG K . ? 0.1882 0.2394 0.1954 0.0168 -0.0050 -0.0287 267 AMG A O4 2220 O O5 . AMG K . ? 0.1888 0.3226 0.2728 0.0229 0.0193 0.0146 267 AMG A O5 2221 O O6 . AMG K . ? 0.1879 0.3244 0.2436 -0.0093 -0.0191 -0.0121 267 AMG A O6 2222 C C1 . AMG L . ? 0.3450 0.3734 0.3597 -0.0162 0.0304 -0.0228 268 AMG A C1 2223 C C2 . AMG L . ? 0.2511 0.3494 0.3328 -0.0248 0.0306 -0.0387 268 AMG A C2 2224 C C3 . AMG L . ? 0.2518 0.3897 0.2988 -0.0112 0.0050 -0.0203 268 AMG A C3 2225 C C4 . AMG L . ? 0.2338 0.2874 0.3081 0.0160 0.0385 -0.0019 268 AMG A C4 2226 C C5 . AMG L . ? 0.2633 0.3655 0.2839 -0.0195 0.0375 -0.0453 268 AMG A C5 2227 C C6 . AMG L . ? 0.2734 0.3397 0.3671 0.0333 0.0270 -0.0152 268 AMG A C6 2228 C C7 . AMG L . ? 0.3255 0.4787 0.3643 0.0272 0.0204 -0.0677 268 AMG A C7 2229 O O1 . AMG L . ? 0.3314 0.4747 0.4315 0.0438 0.0020 -0.0714 268 AMG A O1 2230 O O2 . AMG L . ? 0.2526 0.4465 0.3762 0.0615 -0.0165 -0.0662 268 AMG A O2 2231 O O3 . AMG L . ? 0.2402 0.3828 0.3036 -0.0047 0.0203 -0.0503 268 AMG A O3 2232 O O4 . AMG L . ? 0.2526 0.2865 0.2917 0.0000 0.0030 -0.0577 268 AMG A O4 2233 O O5 . AMG L . ? 0.2954 0.4211 0.3534 0.0151 0.0135 -0.0469 268 AMG A O5 2234 O O6 . AMG L . ? 0.2660 0.4142 0.3951 0.0119 0.0485 -0.0701 268 AMG A O6 2235 S S . SO4 M . ? 0.9930 0.9731 1.0105 -0.0093 0.0036 0.0096 901 SO4 A S 2236 O O1 . SO4 M . ? 0.9516 0.9367 0.9507 -0.0042 0.0001 -0.0183 901 SO4 A O1 2237 O O2 . SO4 M . ? 1.0082 0.9848 1.0304 -0.0021 0.0007 -0.0084 901 SO4 A O2 2238 O O3 . SO4 M . ? 1.0388 1.0182 1.0296 0.0001 0.0029 -0.0080 901 SO4 A O3 2239 O O4 . SO4 M . ? 1.0212 1.0241 1.0452 -0.0035 -0.0035 -0.0037 901 SO4 A O4 2240 S S . SO4 N . ? 0.4551 0.5496 0.4458 0.0534 0.0220 0.0405 902 SO4 A S 2241 O O1 . SO4 N . ? 0.5002 0.5311 0.5308 0.0064 -0.0036 -0.0209 902 SO4 A O1 2242 O O2 . SO4 N . ? 0.6083 0.5438 0.4808 0.0149 0.0289 0.0126 902 SO4 A O2 2243 O O3 . SO4 N . ? 0.3620 0.4084 0.4120 -0.0126 0.0184 0.0583 902 SO4 A O3 2244 O O4 . SO4 N . ? 0.3744 0.4474 0.5006 -0.0029 0.0624 0.1369 902 SO4 A O4 2245 S S . SO4 O . ? 0.6910 0.6869 0.6589 -0.0015 -0.0061 0.0058 903 SO4 A S 2246 O O1 . SO4 O . ? 0.7209 0.7165 0.6913 -0.0071 -0.0172 -0.0010 903 SO4 A O1 2247 O O2 . SO4 O . ? 0.7230 0.6899 0.7310 0.0010 -0.0184 -0.0107 903 SO4 A O2 2248 O O3 . SO4 O . ? 0.7128 0.7027 0.6769 -0.0083 -0.0200 -0.0120 903 SO4 A O3 2249 O O4 . SO4 O . ? 0.6335 0.5931 0.6595 -0.0146 -0.0083 0.0156 903 SO4 A O4 2250 S S A SO4 P . ? 0.3845 0.3955 0.3927 0.0023 0.0259 -0.0120 904 SO4 A S 2251 S S B SO4 P . ? 0.2833 0.2634 0.2361 0.0019 0.0099 0.0050 904 SO4 A S 2252 O O1 A SO4 P . ? 0.4643 0.4604 0.4335 -0.0073 -0.0106 0.0005 904 SO4 A O1 2253 O O1 B SO4 P . ? 0.2704 0.2764 0.2947 0.0251 -0.0247 0.0074 904 SO4 A O1 2254 O O2 A SO4 P . ? 0.3044 0.2407 0.2958 -0.0191 -0.0115 0.0109 904 SO4 A O2 2255 O O2 B SO4 P . ? 0.2148 0.2340 0.2507 -0.0302 0.0206 0.0064 904 SO4 A O2 2256 O O3 A SO4 P . ? 0.4009 0.3735 0.4100 -0.0098 0.0104 0.0021 904 SO4 A O3 2257 O O3 B SO4 P . ? 0.3414 0.2766 0.3423 -0.0252 0.0040 0.0170 904 SO4 A O3 2258 O O4 A SO4 P . ? 0.3908 0.3798 0.4188 0.0024 -0.0028 0.0115 904 SO4 A O4 2259 O O4 B SO4 P . ? 0.2787 0.2556 0.3010 0.0080 0.0020 0.0247 904 SO4 A O4 2260 S S . SO4 Q . ? 0.2747 0.3881 0.3026 0.0469 0.0019 0.0069 905 SO4 A S 2261 O O1 . SO4 Q . ? 0.4326 0.3629 0.4133 0.0163 -0.0402 -0.0622 905 SO4 A O1 2262 O O2 . SO4 Q . ? 0.2912 0.3811 0.2845 0.0161 -0.0235 -0.0390 905 SO4 A O2 2263 O O3 . SO4 Q . ? 0.2310 0.4242 0.2359 0.0245 -0.0214 -0.0287 905 SO4 A O3 2264 O O4 . SO4 Q . ? 0.2249 0.4619 0.3054 0.0450 0.0060 0.0378 905 SO4 A O4 2265 C C . ACT R . ? 0.4753 0.4004 0.4216 0.0121 -0.0031 -0.0058 910 ACT A C 2266 O O . ACT R . ? 0.4540 0.4618 0.4364 0.0200 -0.0320 0.0130 910 ACT A O 2267 O OXT . ACT R . ? 0.4907 0.5498 0.5598 -0.0209 -0.0253 0.0016 910 ACT A OXT 2268 C CH3 . ACT R . ? 0.2023 0.3375 0.2852 -0.0105 -0.0280 0.0244 910 ACT A CH3 2269 O O . HOH S . ? 0.2057 0.2447 0.2563 0.0166 0.0124 0.0132 911 HOH A O 2270 O O . HOH S . ? 0.1834 0.2729 0.2454 0.0002 -0.0102 0.0117 912 HOH A O 2271 O O . HOH S . ? 0.2097 0.1906 0.2243 -0.0182 0.0041 0.0118 913 HOH A O 2272 O O . HOH S . ? 0.1740 0.2782 0.2188 0.0143 -0.0065 0.0272 914 HOH A O 2273 O O . HOH S . ? 0.2035 0.2387 0.2940 -0.0040 -0.0291 -0.0005 915 HOH A O 2274 O O . HOH S . ? 0.2515 0.2190 0.2739 -0.0029 0.0262 0.0177 916 HOH A O 2275 O O . HOH S . ? 0.1760 0.2872 0.2864 0.0113 0.0007 -0.0159 917 HOH A O 2276 O O . HOH S . ? 0.2403 0.2775 0.3237 0.0324 -0.0607 -0.0277 918 HOH A O 2277 O O . HOH S . ? 0.2022 0.2163 0.2077 0.0099 0.0032 -0.0205 919 HOH A O 2278 O O . HOH S . ? 0.1854 0.2768 0.2081 0.0094 -0.0116 0.0136 920 HOH A O 2279 O O . HOH S . ? 0.1929 0.2562 0.2514 -0.0037 -0.0094 0.0345 921 HOH A O 2280 O O . HOH S . ? 0.1942 0.2273 0.2225 0.0114 -0.0215 -0.0008 922 HOH A O 2281 O O . HOH S . ? 0.2304 0.2408 0.2218 0.0193 -0.0338 -0.0530 923 HOH A O 2282 O O . HOH S . ? 0.2366 0.2562 0.2747 -0.0134 0.0298 -0.0016 924 HOH A O 2283 O O . HOH S . ? 0.1946 0.2945 0.2147 -0.0106 -0.0146 -0.0235 925 HOH A O 2284 O O . HOH S . ? 0.2564 0.2357 0.2206 0.0009 0.0128 0.0036 926 HOH A O 2285 O O . HOH S . ? 0.2254 0.2889 0.2428 -0.0213 -0.0363 0.0382 927 HOH A O 2286 O O . HOH S . ? 0.2339 0.2723 0.2970 -0.0037 -0.0164 -0.0062 928 HOH A O 2287 O O . HOH S . ? 0.2775 0.2531 0.3216 -0.0078 0.0298 0.0333 929 HOH A O 2288 O O . HOH S . ? 0.3108 0.2594 0.3157 0.0083 0.0767 0.0403 930 HOH A O 2289 O O . HOH S . ? 0.3091 0.3545 0.2771 -0.0129 0.0032 0.0407 931 HOH A O 2290 O O . HOH S . ? 0.4394 0.2062 0.4041 -0.0026 0.0149 0.0030 932 HOH A O 2291 O O . HOH S . ? 0.2072 0.3313 0.4422 -0.0401 -0.0125 -0.0079 933 HOH A O 2292 O O . HOH S . ? 0.2387 0.3745 0.3497 -0.0166 -0.0264 0.0124 934 HOH A O 2293 O O . HOH S . ? 0.2351 0.4375 0.2779 0.0398 -0.0187 0.0267 935 HOH A O 2294 O O . HOH S . ? 0.2133 0.2826 0.2744 0.0130 -0.0392 -0.0282 936 HOH A O 2295 O O . HOH S . ? 0.2974 0.3246 0.2988 -0.0234 -0.0390 -0.0144 937 HOH A O 2296 O O . HOH S . ? 0.2615 0.3187 0.3931 0.0263 -0.0427 -0.0596 938 HOH A O 2297 O O . HOH S . ? 0.2526 0.3459 0.2844 0.0198 -0.0138 -0.0029 939 HOH A O 2298 O O . HOH S . ? 0.2609 0.2726 0.2722 0.0297 0.0061 0.0621 940 HOH A O 2299 O O . HOH S . ? 0.2853 0.3185 0.2660 -0.0378 -0.0066 0.0189 941 HOH A O 2300 O O . HOH S . ? 0.3115 0.2075 0.3184 -0.0360 0.0082 -0.0019 942 HOH A O 2301 O O . HOH S . ? 0.2405 0.3112 0.2821 -0.0164 -0.0177 -0.0050 943 HOH A O 2302 O O . HOH S . ? 0.2520 0.3393 0.2647 -0.0024 -0.0326 0.0240 944 HOH A O 2303 O O . HOH S . ? 0.2556 0.3542 0.2578 0.0080 -0.0220 -0.0212 945 HOH A O 2304 O O . HOH S . ? 0.3142 0.3565 0.3632 -0.0266 0.0134 -0.0141 946 HOH A O 2305 O O . HOH S . ? 0.2344 0.3036 0.2487 0.0012 0.0288 -0.0003 947 HOH A O 2306 O O . HOH S . ? 0.3557 0.3956 0.3251 -0.0586 -0.0098 -0.0477 948 HOH A O 2307 O O . HOH S . ? 0.3305 0.2734 0.4078 -0.0296 0.0588 0.0661 949 HOH A O 2308 O O . HOH S . ? 0.3354 0.3058 0.3493 -0.0429 -0.0287 0.0306 950 HOH A O 2309 O O . HOH S . ? 0.2964 0.3348 0.3559 0.0766 0.0560 0.0223 951 HOH A O 2310 O O . HOH S . ? 0.2539 0.3091 0.2710 0.0100 0.0014 0.0070 952 HOH A O 2311 O O . HOH S . ? 0.2629 0.3695 0.3387 -0.0065 0.0017 0.0054 953 HOH A O 2312 O O . HOH S . ? 0.2957 0.3204 0.3145 0.0775 0.0266 0.0130 954 HOH A O 2313 O O . HOH S . ? 0.2965 0.3221 0.2504 0.0055 -0.0260 0.0051 955 HOH A O 2314 O O . HOH S . ? 0.1872 0.3593 0.3198 -0.0066 -0.0165 -0.0196 956 HOH A O 2315 O O . HOH S . ? 0.3864 0.3315 0.3364 -0.0524 0.0238 0.1011 957 HOH A O 2316 O O . HOH S . ? 0.4341 0.2886 0.5118 0.0148 -0.0811 0.0393 958 HOH A O 2317 O O . HOH S . ? 0.2790 0.2916 0.3617 0.0259 -0.0328 0.0052 959 HOH A O 2318 O O . HOH S . ? 0.2984 0.3600 0.2577 -0.0285 0.0080 0.0521 960 HOH A O 2319 O O . HOH S . ? 0.2423 0.3131 0.2538 -0.0300 0.0136 -0.0028 961 HOH A O 2320 O O . HOH S . ? 0.3453 0.3532 0.2638 -0.0250 0.0396 -0.0628 962 HOH A O 2321 O O . HOH S . ? 0.3571 0.2721 0.4085 -0.0255 -0.0750 0.0883 963 HOH A O 2322 O O . HOH S . ? 0.4547 0.3388 0.3475 0.0048 -0.0600 0.0048 964 HOH A O 2323 O O . HOH S . ? 0.3249 0.3371 0.3099 -0.0360 -0.0199 0.0095 965 HOH A O 2324 O O . HOH S . ? 0.3370 0.3252 0.3341 0.0113 0.0028 0.0058 966 HOH A O 2325 O O . HOH S . ? 0.2760 0.2901 0.3049 -0.0358 0.0389 -0.0261 967 HOH A O 2326 O O . HOH S . ? 0.2162 0.3963 0.3904 0.0291 0.0209 0.0100 968 HOH A O 2327 O O . HOH S . ? 0.3871 0.4258 0.4325 -0.0073 -0.0099 -0.0273 969 HOH A O 2328 O O . HOH S . ? 0.4101 0.3520 0.5332 -0.0024 -0.0302 -0.0575 970 HOH A O 2329 O O . HOH S . ? 0.3505 0.3333 0.3466 0.0129 -0.0289 -0.0175 971 HOH A O 2330 O O . HOH S . ? 0.2815 0.3831 0.2915 0.0752 0.0123 0.0079 972 HOH A O 2331 O O . HOH S . ? 0.3238 0.2886 0.3204 0.0542 -0.0262 -0.0166 973 HOH A O 2332 O O . HOH S . ? 0.3724 0.3140 0.3578 0.0519 -0.0268 -0.0621 974 HOH A O 2333 O O . HOH S . ? 0.3332 0.4063 0.3834 0.0642 0.0168 0.0215 975 HOH A O 2334 O O . HOH S . ? 0.1398 0.6511 0.3040 0.1304 -0.0842 -0.0990 976 HOH A O 2335 O O . HOH S . ? 0.3699 0.2887 0.4519 0.0786 -0.0343 0.0600 977 HOH A O 2336 O O . HOH S . ? 0.4341 0.4351 0.3142 0.0559 0.0544 -0.0161 978 HOH A O 2337 O O . HOH S . ? 0.4462 0.4342 0.5533 0.0192 0.0330 0.0129 979 HOH A O 2338 O O . HOH S . ? 0.3198 0.3604 0.3919 0.0037 -0.0089 -0.0514 980 HOH A O 2339 O O . HOH S . ? 0.3272 0.3125 0.2310 -0.0068 0.0121 -0.0320 981 HOH A O 2340 O O . HOH S . ? 0.2624 0.3941 0.2595 -0.0006 -0.0134 0.0322 982 HOH A O 2341 O O . HOH S . ? 0.2961 0.3732 0.4275 -0.0533 -0.1039 0.0612 983 HOH A O 2342 O O . HOH S . ? 0.3000 0.4001 0.3967 -0.0410 -0.0412 0.0386 984 HOH A O 2343 O O . HOH S . ? 0.3398 0.4219 0.3577 0.0211 -0.0536 -0.0146 985 HOH A O 2344 O O . HOH S . ? 0.3361 0.4321 0.4003 -0.0777 -0.0407 -0.0146 986 HOH A O 2345 O O . HOH S . ? 0.2994 0.3977 0.4616 0.0071 0.0026 0.0083 987 HOH A O 2346 O O . HOH S . ? 0.3280 0.3523 0.2907 -0.0033 -0.0265 0.0404 988 HOH A O 2347 O O . HOH S . ? 0.3763 0.3414 0.4571 0.0187 -0.0401 0.0132 989 HOH A O 2348 O O . HOH S . ? 0.2485 0.4851 0.2935 -0.0099 0.0254 0.0155 990 HOH A O 2349 O O . HOH S . ? 0.3030 0.5158 0.3671 0.0887 0.0464 -0.0105 991 HOH A O 2350 O O . HOH S . ? 0.4627 0.3371 0.4707 -0.0234 0.0264 -0.0305 992 HOH A O 2351 O O . HOH S . ? 0.3977 0.4107 0.3995 -0.0285 0.0291 0.0313 993 HOH A O 2352 O O . HOH S . ? 0.4014 0.2988 0.4902 0.0455 0.0424 0.0149 994 HOH A O 2353 O O . HOH S . ? 0.3328 0.4827 0.4125 0.0402 0.0008 0.0157 995 HOH A O 2354 O O . HOH S . ? 0.3510 0.4833 0.3862 0.0941 -0.0671 0.0351 996 HOH A O 2355 O O . HOH S . ? 0.3503 0.3087 0.3531 0.0075 0.0090 -0.0250 997 HOH A O 2356 O O . HOH S . ? 0.3899 0.4218 0.4067 -0.0613 -0.0378 0.0306 998 HOH A O 2357 O O . HOH S . ? 0.3826 0.4295 0.4262 0.0226 -0.0423 -0.0253 999 HOH A O 2358 O O . HOH S . ? 0.3507 0.5080 0.3274 0.0623 -0.0392 0.0122 1000 HOH A O 2359 O O . HOH S . ? 0.7206 0.7477 0.7273 0.0265 0.0043 0.0113 1001 HOH A O 2360 O O . HOH S . ? 0.4339 0.5004 0.4229 -0.0469 0.0709 0.0082 1002 HOH A O 2361 O O . HOH S . ? 0.4113 0.4981 0.4450 0.0542 -0.0184 0.1043 1003 HOH A O 2362 O O . HOH S . ? 0.4415 0.3046 0.3907 -0.0092 -0.0284 -0.0346 1004 HOH A O 2363 O O . HOH S . ? 0.3768 0.4068 0.3535 0.0226 0.0566 0.0049 1005 HOH A O 2364 O O . HOH S . ? 0.4287 0.4398 0.4017 0.0266 -0.0275 -0.0031 1006 HOH A O 2365 O O . HOH S . ? 0.3218 0.3487 0.4015 -0.0150 -0.0070 -0.0361 1007 HOH A O 2366 O O . HOH S . ? 0.4002 0.5253 0.4451 -0.0384 0.0250 0.0871 1008 HOH A O 2367 O O . HOH S . ? 0.3375 0.3776 0.4150 -0.0810 0.0341 -0.0251 1009 HOH A O 2368 O O . HOH S . ? 0.4552 0.3758 0.4666 -0.0747 0.0133 0.0298 1010 HOH A O 2369 O O . HOH S . ? 0.4104 0.5912 0.4359 -0.0332 0.0422 0.0300 1011 HOH A O 2370 O O . HOH S . ? 0.4213 0.4571 0.3821 -0.0296 0.0004 0.0181 1012 HOH A O 2371 O O . HOH S . ? 0.3486 0.3924 0.3526 0.0251 0.0506 0.0619 1013 HOH A O 2372 O O . HOH S . ? 0.3509 0.4413 0.4606 -0.0531 -0.0459 -0.0521 1014 HOH A O 2373 O O . HOH S . ? 0.4523 0.3305 0.3486 0.0272 -0.0008 -0.0011 1015 HOH A O 2374 O O . HOH S . ? 0.4626 0.3550 0.4601 -0.0017 0.0434 -0.0272 1016 HOH A O 2375 O O . HOH S . ? 0.3644 0.4984 0.4340 0.0251 0.0074 -0.0403 1017 HOH A O 2376 O O . HOH S . ? 0.5729 0.5332 0.3934 -0.0484 -0.0147 0.0085 1018 HOH A O 2377 O O . HOH S . ? 0.4804 0.3626 0.4530 0.0612 -0.0088 -0.0051 1019 HOH A O 2378 O O . HOH S . ? 0.3728 0.4417 0.4674 -0.0103 -0.0191 0.0656 1020 HOH A O 2379 O O . HOH S . ? 0.4223 0.5385 0.3709 -0.0956 0.0690 0.0270 1021 HOH A O 2380 O O . HOH S . ? 0.6533 0.3449 0.3996 -0.0070 -0.0252 -0.0132 1022 HOH A O 2381 O O . HOH S . ? 0.3020 0.4683 0.3255 -0.0589 -0.0248 0.0055 1023 HOH A O 2382 O O . HOH S . ? 0.4700 0.4238 0.2318 0.0138 0.0309 0.0536 1024 HOH A O 2383 O O . HOH S . ? 0.4889 0.3556 0.3880 -0.0467 0.0202 0.0406 1025 HOH A O 2384 O O . HOH S . ? 0.3632 0.4104 0.4195 -0.0626 -0.0014 0.0670 1026 HOH A O 2385 O O . HOH S . ? 0.4157 0.3869 0.2765 0.0443 0.0000 -0.0252 1027 HOH A O 2386 O O . HOH S . ? 0.4591 0.5667 0.4890 -0.0161 -0.0129 0.0504 1028 HOH A O 2387 O O . HOH S . ? 0.2952 0.3729 0.4994 -0.0046 -0.0362 -0.0043 1029 HOH A O 2388 O O . HOH S . ? 0.4190 0.3522 0.5009 -0.0168 0.0475 -0.0376 1030 HOH A O 2389 O O . HOH S . ? 0.4124 0.3489 0.3529 -0.0621 -0.0375 0.0056 1031 HOH A O 2390 O O . HOH S . ? 0.3399 0.4029 0.4441 0.0299 -0.0400 0.0487 1032 HOH A O 2391 O O . HOH S . ? 0.3472 0.3902 0.4555 0.0198 0.0465 0.0166 1033 HOH A O 2392 O O . HOH S . ? 0.2812 0.3093 0.5316 0.0046 0.0006 0.0839 1034 HOH A O 2393 O O . HOH S . ? 0.4417 0.4141 0.3392 0.0056 -0.0371 -0.0269 1035 HOH A O 2394 O O . HOH S . ? 0.3642 0.4548 0.3807 -0.0320 -0.0399 0.0375 1036 HOH A O 2395 O O . HOH S . ? 0.4216 0.4236 0.6042 0.0276 0.0317 -0.0322 1037 HOH A O 2396 O O . HOH S . ? 0.5925 0.3631 0.4294 0.0416 0.0123 -0.0320 1038 HOH A O 2397 O O . HOH S . ? 0.3793 0.4866 0.3786 0.0034 -0.0268 -0.0290 1039 HOH A O 2398 O O . HOH S . ? 0.4024 0.5992 0.3637 -0.0881 -0.0362 -0.0173 1040 HOH A O 2399 O O . HOH S . ? 0.4900 0.3165 0.4216 -0.0119 -0.0053 -0.0773 1041 HOH A O 2400 O O . HOH S . ? 0.4128 0.4714 0.4133 0.0149 0.0264 -0.0215 1042 HOH A O 2401 O O . HOH S . ? 0.4153 0.3717 0.3749 -0.0252 0.0194 0.0130 1043 HOH A O 2402 O O . HOH S . ? 0.3471 0.4308 0.4128 -0.0051 -0.0205 0.0164 1044 HOH A O 2403 O O . HOH S . ? 0.4072 0.4230 0.4268 0.0104 -0.0200 -0.0210 1045 HOH A O 2404 O O B HOH S . ? 0.2874 0.2348 0.3256 -0.0373 -0.0387 0.0230 1046 HOH A O 2405 O O . HOH S . ? 0.5074 0.5027 0.4183 0.0376 0.0026 0.0247 1047 HOH A O 2406 O O . HOH S . ? 0.3097 0.4145 0.5968 -0.0023 -0.0240 0.0417 1048 HOH A O 2407 O O . HOH S . ? 0.4849 0.3525 0.4936 -0.0301 -0.0479 0.0216 1049 HOH A O 2408 O O . HOH S . ? 0.5027 0.4824 0.4440 0.0389 0.0007 -0.0049 1050 HOH A O 2409 O O . HOH S . ? 0.4828 0.5327 0.4855 0.0816 0.0255 0.0453 1051 HOH A O 2410 O O . HOH S . ? 0.4785 0.4966 0.4983 0.0182 -0.0190 -0.0044 1052 HOH A O 2411 O O . HOH S . ? 0.3371 0.4610 0.4646 0.0060 0.0429 -0.0346 1053 HOH A O 2412 O O . HOH S . ? 0.3288 0.5468 0.5274 0.0042 -0.0284 0.0001 1054 HOH A O 2413 O O . HOH S . ? 0.5085 0.3977 0.4767 -0.0143 -0.0087 -0.0195 1055 HOH A O 2414 O O . HOH S . ? 0.4601 0.5551 0.5530 -0.0097 -0.0303 -0.0438 1056 HOH A O 2415 O O . HOH S . ? 0.3657 0.4153 0.3931 0.0149 -0.0158 0.0246 1057 HOH A O 2416 O O . HOH S . ? 0.5023 0.5343 0.3987 -0.0229 0.0101 -0.0197 1058 HOH A O 2417 O O . HOH S . ? 0.5413 0.5327 0.5184 -0.0084 0.0128 0.0160 1059 HOH A O 2418 O O . HOH S . ? 0.4888 0.4525 0.5049 -0.0059 -0.0794 0.0052 1060 HOH A O 2419 O O . HOH S . ? 0.4039 0.5644 0.4832 0.0068 0.0284 0.0443 1061 HOH A O 2420 O O . HOH S . ? 0.4496 0.3916 0.4264 0.0668 0.0420 0.0103 1062 HOH A O 2421 O O . HOH S . ? 0.3724 0.4941 0.3666 -0.0367 -0.0261 0.0000 1063 HOH A O 2422 O O . HOH S . ? 0.3780 0.4399 0.4388 0.0125 -0.0147 0.0245 1064 HOH A O 2423 O O . HOH S . ? 0.4548 0.3666 0.5355 0.0597 -0.0323 0.0788 1065 HOH A O 2424 O O . HOH S . ? 0.4290 0.4787 0.5099 0.0593 -0.0372 0.0133 1066 HOH A O 2425 O O . HOH S . ? 0.6511 0.5834 0.5285 -0.0044 0.0253 0.0661 1067 HOH A O 2426 O O . HOH S . ? 0.2839 0.4946 0.5670 -0.0450 -0.0268 0.0338 1068 HOH A O 2427 O O . HOH S . ? 0.4632 0.3844 0.4497 -0.0402 -0.0107 0.0729 1069 HOH A O 2428 O O . HOH S . ? 0.5291 0.4279 0.4303 -0.0297 0.0426 0.0058 1070 HOH A O 2429 O O . HOH S . ? 0.5026 0.6531 0.6521 0.0664 -0.0230 0.0081 1071 HOH A O 2430 O O . HOH S . ? 0.5105 0.5399 0.5304 -0.1100 -0.0026 0.0415 1072 HOH A O 2431 O O . HOH S . ? 0.4082 0.3772 0.4714 -0.0046 0.0376 -0.0357 1073 HOH A O 2432 O O . HOH S . ? 0.5504 0.4074 0.4272 0.0271 -0.0108 0.0251 1074 HOH A O 2433 O O . HOH S . ? 0.3888 0.5230 0.4651 -0.0134 -0.0203 -0.0232 1075 HOH A O 2434 O O . HOH S . ? 0.4193 0.6057 0.4231 0.0385 0.0396 0.0168 1076 HOH A O 2435 O O . HOH S . ? 0.7300 0.6446 0.6167 -0.0021 0.0087 0.0044 1077 HOH A O 2436 O O . HOH S . ? 0.4017 0.4848 0.3839 0.1236 0.0236 0.0083 1078 HOH A O 2437 O O . HOH S . ? 0.4318 0.4451 0.5552 0.0228 0.0014 -0.0183 1079 HOH A O 2438 O O . HOH S . ? 0.4775 0.5169 0.5423 -0.0093 -0.0062 -0.0183 1080 HOH A O 2439 O O . HOH S . ? 0.5406 0.5040 0.5202 -0.0273 -0.0441 0.0507 1081 HOH A O 2440 O O . HOH S . ? 0.3980 0.4741 0.3724 -0.0014 0.0472 0.0380 1082 HOH A O 2441 O O . HOH S . ? 0.4622 0.4852 0.3844 -0.0403 0.0808 -0.0207 1083 HOH A O 2442 O O . HOH S . ? 0.4766 0.4344 0.4238 0.0149 -0.0394 0.0022 1084 HOH A O 2443 O O . HOH S . ? 0.4076 0.5105 0.6222 0.0023 -0.0168 -0.0188 1085 HOH A O 2444 O O . HOH S . ? 0.5097 0.5052 0.4813 0.0269 0.0492 0.0711 1086 HOH A O 2445 O O . HOH S . ? 0.4470 0.5602 0.4859 -0.0149 0.0155 0.0424 1087 HOH A O 2446 O O . HOH S . ? 0.4764 0.4505 0.4495 -0.0038 0.0359 -0.0067 1088 HOH A O 2447 O O . HOH S . ? 0.6644 0.6654 0.6954 0.0269 0.0097 0.0061 1089 HOH A O 2448 O O . HOH S . ? 0.5263 0.5039 0.5301 0.0577 -0.0665 0.0441 1090 HOH A O 2449 O O . HOH S . ? 0.3786 0.4813 0.6344 -0.0279 0.0638 -0.0653 1091 HOH A O 2450 O O . HOH S . ? 0.5341 0.4758 0.4469 0.0512 -0.0294 -0.0188 1092 HOH A O 2451 O O . HOH S . ? 0.5389 0.5488 0.5870 0.0272 0.0081 0.0081 1093 HOH A O 2452 O O . HOH S . ? 0.4336 0.5031 0.4860 -0.0512 0.0222 0.0259 1094 HOH A O 2453 O O . HOH S . ? 0.4705 0.3857 0.4990 0.0228 -0.0413 -0.0178 1095 HOH A O 2454 O O . HOH S . ? 0.4572 0.5315 0.5104 -0.0100 -0.0383 0.0430 1096 HOH A O 2455 O O . HOH S . ? 0.5403 0.5693 0.4409 -0.0123 -0.0367 0.0142 1097 HOH A O 2456 O O . HOH S . ? 0.5020 0.3720 0.3527 -0.0026 -0.0419 -0.0024 1098 HOH A O 2457 O O . HOH S . ? 0.5624 0.5686 0.4374 0.0613 0.0191 0.0719 1099 HOH A O 2458 O O . HOH S . ? 0.5424 0.4836 0.4598 0.0276 0.0302 0.0608 1100 HOH A O 2459 O O . HOH S . ? 0.4019 0.4414 0.4525 -0.0390 -0.0033 -0.0066 1101 HOH A O 2460 O O . HOH S . ? 0.6437 0.6827 0.5473 -0.0027 0.0256 -0.0032 1102 HOH A O 2461 O O . HOH S . ? 0.3986 0.6039 0.4180 0.0330 -0.0532 0.0391 1103 HOH A O 2462 O O . HOH S . ? 0.3520 0.3663 0.5036 -0.0320 -0.0324 0.0398 1104 HOH A O 2463 O O . HOH S . ? 0.5508 0.5572 0.3746 0.0195 -0.0397 -0.0028 1105 HOH A O 2464 O O . HOH S . ? 0.5206 0.4248 0.4013 0.0548 0.0611 -0.0115 1106 HOH A O 2465 O O . HOH S . ? 0.5234 0.5451 0.5607 -0.0024 0.0232 -0.0450 1107 HOH A O 2466 O O . HOH S . ? 0.5834 0.5315 0.5204 -0.0032 0.0382 -0.0647 1108 HOH A O 2467 O O . HOH S . ? 0.4352 0.5277 0.4000 -0.0087 0.0255 -0.0397 1109 HOH A O 2468 O O . HOH S . ? 0.5344 0.5047 0.5876 -0.0367 -0.0241 -0.0103 1110 HOH A O 2469 O O . HOH S . ? 0.5758 0.5345 0.3502 -0.0423 0.0202 0.0197 1111 HOH A O 2470 O O . HOH S . ? 0.3452 0.5884 0.4754 0.0188 0.0341 -0.0389 1112 HOH A O 2471 O O . HOH S . ? 0.4834 0.4724 0.4426 -0.0051 0.0439 -0.0464 1113 HOH A O 2472 O O . HOH S . ? 0.5294 0.5719 0.4770 -0.0033 0.0329 -0.0234 1114 HOH A O 2473 O O . HOH S . ? 0.4617 0.5549 0.6127 0.0221 -0.0282 -0.0346 1115 HOH A O 2474 O O . HOH S . ? 0.3971 0.5298 0.5558 0.0418 -0.0240 -0.0144 1116 HOH A O 2475 O O . HOH S . ? 0.5660 0.3994 0.4891 0.0562 -0.0149 0.0859 1117 HOH A O 2476 O O . HOH S . ? 0.5594 0.3706 0.4113 -0.0140 -0.0214 0.0084 1118 HOH A O 2477 O O . HOH S . ? 0.6375 0.4926 0.6304 -0.0072 0.0335 -0.0208 1119 HOH A O 2478 O O . HOH S . ? 0.5230 0.5721 0.3533 0.0088 -0.0295 0.0035 1120 HOH A O 2479 O O . HOH S . ? 0.4732 0.5143 0.5887 0.0427 0.0124 0.0376 1121 HOH A O 2480 O O . HOH S . ? 0.5448 0.4446 0.5664 -0.0005 -0.0264 0.0209 1122 HOH A O 2481 O O . HOH S . ? 0.4156 0.4688 0.4426 -0.0022 0.0644 0.0533 1123 HOH A O 2482 O O . HOH S . ? 0.4466 0.5282 0.4819 0.0062 -0.0031 -0.0657 1124 HOH A O 2483 O O . HOH S . ? 0.4473 0.5155 0.5011 0.0221 -0.0064 0.0137 1125 HOH A O 2484 O O . HOH S . ? 0.5537 0.5935 0.5409 0.0142 0.0246 0.0408 1126 HOH A O 2485 O O . HOH S . ? 0.5716 0.5601 0.5666 0.0561 0.0060 -0.0230 1127 HOH A O 2486 O O . HOH S . ? 0.6524 0.6964 0.6645 -0.0289 0.0073 -0.0020 1128 HOH A O 2487 O O . HOH S . ? 0.6532 0.5761 0.6241 0.0029 0.0210 -0.0207 1129 HOH A O 2488 O O . HOH S . ? 0.5311 0.5185 0.5615 -0.0360 0.0121 -0.0454 1130 HOH A O 2489 O O . HOH S . ? 0.7182 0.6885 0.7371 0.0334 0.0012 0.0103 1131 HOH A O 2490 O O . HOH S . ? 0.4513 0.5970 0.6259 -0.0258 -0.0693 -0.0034 1132 HOH A O 2491 O O . HOH S . ? 0.3999 0.4918 0.4435 0.0052 -0.0104 0.0150 1133 HOH A O 2492 O O . HOH S . ? 0.4364 0.5025 0.5762 0.0897 -0.0039 -0.0245 1134 HOH A O 2493 O O . HOH S . ? 0.4282 0.5782 0.4105 -0.0111 -0.0203 0.0813 1135 HOH A O 2494 O O . HOH S . ? 0.5540 0.6227 0.5471 0.0247 -0.0119 0.0148 1136 HOH A O 2495 O O . HOH S . ? 0.4494 0.5775 0.4180 -0.0065 0.0317 0.0394 1137 HOH A O 2496 O O . HOH S . ? 0.4863 0.5190 0.3885 0.0058 0.0012 -0.0608 1138 HOH A O 2497 O O . HOH S . ? 0.4079 0.5640 0.6058 -0.0140 -0.0208 -0.0184 1139 HOH A O 2498 O O . HOH S . ? 0.6106 0.4425 0.4594 -0.0043 0.0376 0.0394 1140 HOH A O 2499 O O . HOH S . ? 0.5673 0.5722 0.4394 -0.0381 0.0559 0.0703 1141 HOH A O 2500 O O . HOH S . ? 0.5705 0.4752 0.6389 -0.0143 0.0260 0.0302 1142 HOH A O 2501 O O . HOH S . ? 0.6308 0.5482 0.5677 -0.0067 0.0104 0.0241 1143 HOH A O 2502 O O . HOH S . ? 0.5679 0.6190 0.5479 -0.0405 0.0176 0.0047 1144 HOH A O 2503 O O . HOH S . ? 0.4494 0.5896 0.5104 -0.0188 -0.0019 0.0306 1145 HOH A O 2504 O O . HOH S . ? 0.4910 0.5141 0.5599 -0.0250 -0.0105 0.0063 1146 HOH A O 2505 O O . HOH S . ? 0.4643 0.4097 0.3858 -0.0235 -0.0624 -0.0026 1147 HOH A O 2506 O O . HOH S . ? 0.5718 0.5797 0.5450 0.0127 -0.0393 -0.0132 1148 HOH A O 2507 O O . HOH S . ? 0.4158 0.4498 0.4453 -0.0019 -0.0163 0.0269 1149 HOH A O 2508 O O . HOH S . ? 0.4769 0.4684 0.5297 0.0391 0.0175 -0.0166 1150 HOH A O 2509 O O . HOH S . ? 0.5532 0.4590 0.4688 -0.0321 -0.0209 -0.0254 1151 HOH A O 2510 O O . HOH S . ? 0.5350 0.5215 0.4950 0.0668 0.0026 -0.0146 1152 HOH A O 2511 O O . HOH S . ? 0.7472 0.7169 0.7331 0.0078 0.0018 -0.0118 1153 HOH A O 2512 O O . HOH S . ? 0.5961 0.5994 0.5710 0.0104 -0.0203 0.0127 1154 HOH A O 2513 O O . HOH S . ? 0.4816 0.5590 0.5390 0.0391 -0.0086 -0.0197 1155 HOH A O 2514 O O . HOH S . ? 0.7063 0.7218 0.6120 0.0106 0.0124 0.0266 1156 HOH A O 2515 O O . HOH S . ? 0.7004 0.5933 0.6431 -0.0427 0.0003 0.0307 1157 HOH A O 2516 O O . HOH S . ? 0.3921 0.4971 0.5560 0.0197 0.0296 0.0131 1158 HOH A O 2517 O O . HOH S . ? 0.6073 0.5330 0.5363 0.0191 0.0170 -0.0152 1159 HOH A O 2518 O O . HOH S . ? 0.6298 0.5210 0.4153 -0.0019 -0.0137 0.0254 1160 HOH A O 2519 O O . HOH S . ? 0.5727 0.6424 0.6664 0.0014 0.0117 -0.0097 1161 HOH A O 2520 O O . HOH S . ? 0.5678 0.5575 0.5303 0.0292 0.0243 -0.0670 1162 HOH A O 2521 O O . HOH S . ? 0.3915 0.5635 0.4436 -0.0305 0.0632 -0.0369 1163 HOH A O 2522 O O . HOH S . ? 0.5748 0.6021 0.5762 -0.0170 -0.0129 -0.0127 1164 HOH A O 2523 O O . HOH S . ? 0.5525 0.4356 0.5409 -0.0457 -0.0012 0.0123 1165 HOH A O 2524 O O . HOH S . ? 0.6044 0.5903 0.6665 -0.0405 -0.0023 -0.0318 1166 HOH A O 2525 O O . HOH S . ? 0.5373 0.5883 0.5627 -0.0405 0.0546 0.0649 1167 HOH A O 2526 O O . HOH S . ? 0.4958 0.6136 0.5751 -0.0100 0.0006 0.0293 1168 HOH A O 2527 O O . HOH S . ? 0.5912 0.5983 0.5905 0.0280 -0.0224 0.0129 1169 HOH A O 2528 O O . HOH S . ? 0.6969 0.6235 0.7197 0.0098 -0.0094 -0.0022 1170 HOH A O 2529 O O . HOH S . ? 0.5247 0.5026 0.6229 0.0537 0.0349 -0.0171 1171 HOH A O 2530 O O . HOH S . ? 0.5853 0.5934 0.4710 0.0002 0.0383 -0.0108 1172 HOH A O 2531 O O . HOH S . ? 0.6657 0.6358 0.5558 0.0218 0.0012 -0.0318 1173 HOH A O 2532 O O . HOH S . ? 0.4387 0.4937 0.5166 -0.0203 0.0223 -0.0387 1174 HOH A O 2533 O O . HOH S . ? 0.5275 0.4406 0.4279 0.0121 0.0058 -0.0135 1175 HOH A O 2534 O O . HOH S . ? 0.5516 0.6192 0.5484 0.0227 -0.0060 -0.0068 1176 HOH A O 2535 O O . HOH S . ? 0.4961 0.5059 0.5138 0.0042 0.0036 0.0087 1177 HOH A O 2536 O O . HOH S . ? 0.4291 0.5595 0.5082 0.0118 -0.0084 0.0378 1178 HOH A O 2537 O O . HOH S . ? 0.6977 0.6323 0.6527 0.0139 0.0359 -0.0113 1179 HOH A O 2538 O O . HOH S . ? 0.5478 0.5251 0.5915 -0.0458 -0.0106 0.0167 1180 HOH A O 2539 O O . HOH S . ? 0.4662 0.5261 0.5839 0.0383 -0.0072 0.0149 1181 HOH A O 2540 O O . HOH S . ? 0.3630 0.4920 0.5125 -0.0726 -0.0457 0.0084 1182 HOH A O 2541 O O . HOH S . ? 0.6626 0.5631 0.7027 0.0421 0.0060 -0.0294 1183 HOH A O 2542 O O . HOH S . ? 0.6927 0.7420 0.7421 0.0029 -0.0175 -0.0158 1184 HOH A O 2543 O O . HOH S . ? 0.7310 0.7149 0.5439 0.0262 0.0227 0.0001 1185 HOH A O 2544 O O . HOH S . ? 0.5038 0.5513 0.3961 0.0110 -0.0254 -0.0244 1186 HOH A O 2545 O O . HOH S . ? 0.5078 0.6152 0.5385 -0.0428 0.0308 0.0390 1187 HOH A O 2546 O O . HOH S . ? 0.5088 0.5264 0.6245 -0.0090 0.0260 -0.0066 1188 HOH A O 2547 O O . HOH S . ? 0.6117 0.5488 0.5814 0.0232 0.0435 0.0222 1189 HOH A O 2548 O O . HOH S . ? 0.5277 0.5817 0.5152 -0.0152 0.0076 0.0141 1190 HOH A O 2549 O O . HOH S . ? 0.5750 0.6115 0.5835 0.0041 0.0503 0.0031 1191 HOH A O 2550 O O . HOH S . ? 0.5144 0.6380 0.6888 -0.0283 -0.0095 0.0163 1192 HOH A O 2551 O O . HOH S . ? 0.5886 0.4983 0.4909 0.0182 0.0020 0.0002 1193 HOH A O 2552 O O . HOH S . ? 0.6233 0.5995 0.6510 0.0186 0.0149 -0.0281 1194 HOH A O 2553 O O . HOH S . ? 0.6441 0.5399 0.6412 0.0255 0.0175 0.0247 1195 HOH A O 2554 O O . HOH S . ? 0.7175 0.6791 0.7108 -0.0066 0.0282 -0.0028 1196 HOH A O 2555 O O . HOH S . ? 0.6427 0.4978 0.5493 0.0069 0.0074 0.0168 1197 HOH A O 2556 O O . HOH S . ? 0.4950 0.7230 0.6409 0.0149 0.0522 0.0082 1198 HOH A O 2557 O O . HOH S . ? 0.6887 0.6865 0.6910 -0.0061 0.0487 -0.0154 1199 HOH A O 2558 O O . HOH S . ? 0.6641 0.6083 0.6286 -0.0035 0.0083 -0.0029 1200 HOH A O 2559 O O . HOH S . ? 0.4667 0.6660 0.4260 -0.0545 -0.0426 0.0025 1201 HOH A O 2560 O O . HOH S . ? 0.7417 0.7597 0.7871 0.0196 -0.0083 -0.0191 1202 HOH A O 2561 O O . HOH S . ? 0.4580 0.4585 0.5085 -0.0443 -0.0114 -0.0209 1203 HOH A O 2562 O O . HOH S . ? 0.7004 0.6992 0.6429 -0.0061 0.0293 0.0130 1204 HOH A O 2563 O O . HOH S . ? 0.6172 0.6207 0.5564 0.0130 0.0136 0.0238 1205 HOH A O 2564 O O . HOH S . ? 0.4773 0.5527 0.6079 -0.0429 0.0679 0.0177 1206 HOH A O 2565 O O . HOH S . ? 0.4452 0.4920 0.5393 0.0203 -0.0130 -0.0693 1207 HOH A O 2566 O O . HOH S . ? 0.5847 0.6214 0.6521 0.0350 0.0142 -0.0132 1208 HOH A O 2567 O O . HOH S . ? 0.5862 0.6463 0.6076 0.0230 -0.0104 -0.0145 1209 HOH A O 2568 O O . HOH S . ? 0.5708 0.6280 0.6580 0.0181 -0.0158 -0.0174 1210 HOH A O 2569 O O . HOH S . ? 0.5385 0.6197 0.5184 0.0296 -0.0372 0.0069 1211 HOH A O 2570 O O . HOH S . ? 0.6894 0.6172 0.6895 -0.0088 -0.0123 0.0304 1212 HOH A O 2571 O O . HOH S . ? 0.6956 0.6698 0.6244 0.0041 0.0392 0.0205 1213 HOH A O 2572 O O . HOH S . ? 0.6132 0.6739 0.6454 0.0208 0.0260 0.0061 1214 HOH A O 2573 O O . HOH S . ? 0.6011 0.6224 0.6205 -0.0364 -0.0095 -0.0127 1215 HOH A O 2574 O O . HOH S . ? 0.5910 0.5608 0.5879 0.0218 -0.0216 -0.0124 1216 HOH A O 2575 O O . HOH S . ? 0.6912 0.5616 0.6494 -0.0477 -0.0106 -0.0051 1217 HOH A O 2576 O O . HOH S . ? 0.4745 0.5765 0.4716 0.0129 0.0417 0.0019 1218 HOH A O 2577 O O . HOH S . ? 0.6089 0.6920 0.6349 -0.0148 -0.0269 -0.0035 1219 HOH A O 2578 O O . HOH S . ? 0.5346 0.6585 0.6200 -0.0145 -0.0002 -0.0210 1220 HOH A O 2579 O O . HOH S . ? 0.5585 0.5808 0.5911 -0.0171 0.0328 -0.0029 1221 HOH A O 2580 O O . HOH S . ? 0.4757 0.5664 0.4819 0.0105 0.0737 -0.0261 1222 HOH A O 2581 O O . HOH S . ? 0.5324 0.5441 0.6082 0.0420 0.0439 0.0038 1223 HOH A O 2582 O O . HOH S . ? 0.6973 0.7366 0.6883 -0.0013 -0.0026 -0.0351 1224 HOH A O 2583 O O . HOH S . ? 0.6518 0.6413 0.6055 -0.0340 0.0445 0.0330 1225 HOH A O 2584 O O . HOH S . ? 0.5037 0.6794 0.6211 0.0155 -0.0672 0.0043 1226 HOH A O 2585 O O . HOH S . ? 0.5713 0.6005 0.6145 0.0079 -0.0160 -0.0145 1227 HOH A O 2586 O O . HOH S . ? 0.5549 0.5681 0.5028 0.0193 0.0159 -0.0176 1228 HOH A O 2587 O O . HOH S . ? 0.5987 0.6172 0.6287 0.0360 -0.0031 -0.0496 1229 HOH A O 2588 O O . HOH S . ? 0.5367 0.5441 0.6187 -0.0057 0.0046 0.0234 1230 HOH A O 2589 O O . HOH S . ? 0.5789 0.5781 0.6383 -0.0062 -0.0092 -0.0458 1231 HOH A O 2590 O O . HOH S . ? 0.5031 0.6316 0.5502 0.0008 0.0517 0.0139 1232 HOH A O 2591 O O . HOH S . ? 0.6633 0.6582 0.6518 0.0321 0.0002 0.0405 1233 HOH A O 2592 O O . HOH S . ? 0.6596 0.6824 0.6145 0.0054 0.0077 0.0000 1234 HOH A O 2593 O O . HOH S . ? 0.5934 0.6089 0.5845 0.0164 0.0283 0.0479 1235 HOH A O 2594 O O . HOH S . ? 0.7116 0.6191 0.6585 0.0195 0.0026 -0.0266 1236 HOH A O 2595 O O . HOH S . ? 0.5928 0.5558 0.5721 0.0240 -0.0107 0.0814 1237 HOH A O 2596 O O . HOH S . ? 0.7074 0.6603 0.6106 0.0030 -0.0057 -0.0109 1238 HOH A O 2597 O O . HOH S . ? 0.6073 0.6567 0.5364 -0.0422 0.0180 0.0382 1239 HOH A O 2598 O O . HOH S . ? 0.5391 0.5516 0.5547 0.0368 -0.0306 -0.0472 1240 HOH A O 2599 O O . HOH S . ? 0.5994 0.6588 0.5468 0.0170 0.0091 -0.0305 1241 HOH A O 2600 O O . HOH S . ? 0.7512 0.7096 0.7426 -0.0018 -0.0037 0.0129 1242 HOH A O 2601 O O . HOH S . ? 0.6783 0.7331 0.6487 -0.0039 0.0075 0.0008 1243 HOH A O 2602 O O . HOH S . ? 0.5193 0.4139 0.6275 -0.0033 -0.0063 0.0344 1244 HOH A O 2603 O O . HOH S . ? 0.7073 0.6410 0.7011 0.0084 -0.0160 0.0313 1245 HOH A O 2604 O O . HOH S . ? 0.6686 0.6179 0.5713 0.0199 -0.0057 0.0249 1246 HOH A O 2605 O O . HOH S . ? 0.6222 0.6647 0.6144 -0.0109 0.0048 -0.0127 1247 HOH A O 2606 O O . HOH S . ? 0.6226 0.6364 0.6124 0.0038 0.0191 -0.0219 1248 HOH A O 2607 O O . HOH S . ? 0.6123 0.6677 0.6057 -0.0307 0.0401 0.0513 1249 HOH A O 2608 O O . HOH S . ? 0.3078 0.3741 0.3889 -0.0353 -0.0120 0.0038 1250 HOH A O 2609 O O . HOH S . ? 0.3667 0.5968 0.4533 -0.0436 -0.0850 -0.0494 1251 HOH A O # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 THR 1 1 1 THR THR A . n A 1 2 SER 2 2 2 SER SER A . n A 1 3 PHE 3 3 3 PHE PHE A . n A 1 4 THR 4 4 4 THR THR A . n A 1 5 ARG 5 5 5 ARG ARG A . n A 1 6 ASN 6 6 6 ASN ASN A . n A 1 7 ILE 7 7 7 ILE ILE A . n A 1 8 VAL 8 8 8 VAL VAL A . n A 1 9 GLY 9 9 9 GLY GLY A . n A 1 10 ARG 10 10 10 ARG ARG A . n A 1 11 ASP 11 11 11 ASP ASP A . n A 1 12 GLY 12 12 12 GLY GLY A . n A 1 13 LEU 13 13 13 LEU LEU A . n A 1 14 CYS 14 14 14 CYS CYS A . n A 1 15 VAL 15 15 15 VAL VAL A . n A 1 16 ASP 16 16 16 ASP ASP A . n A 1 17 VAL 17 17 17 VAL VAL A . n A 1 18 ARG 18 18 18 ARG ARG A . n A 1 19 ASN 19 19 19 ASN ASN A . n A 1 20 GLY 20 20 20 GLY GLY A . n A 1 21 TYR 21 21 21 TYR TYR A . n A 1 22 ASP 22 22 22 ASP ASP A . n A 1 23 THR 23 23 23 THR THR A . n A 1 24 ASP 24 24 24 ASP ASP A . n A 1 25 GLY 25 25 25 GLY GLY A . n A 1 26 THR 26 26 26 THR THR A . n A 1 27 PRO 27 27 27 PRO PRO A . n A 1 28 LEU 28 28 28 LEU LEU A . n A 1 29 GLN 29 29 29 GLN GLN A . n A 1 30 LEU 30 30 30 LEU LEU A . n A 1 31 TRP 31 31 31 TRP TRP A . n A 1 32 PRO 32 32 32 PRO PRO A . n A 1 33 CYS 33 33 33 CYS CYS A . n A 1 34 GLY 34 34 34 GLY GLY A . n A 1 35 THR 35 35 35 THR THR A . n A 1 36 GLN 36 36 36 GLN GLN A . n A 1 37 ARG 37 37 37 ARG ARG A . n A 1 38 ASN 38 38 38 ASN ASN A . n A 1 39 GLN 39 39 39 GLN GLN A . n A 1 40 ARG 40 40 40 ARG ARG A . n A 1 41 TRP 41 41 41 TRP TRP A . n A 1 42 THR 42 42 42 THR THR A . n A 1 43 PHE 43 43 43 PHE PHE A . n A 1 44 ASP 44 44 44 ASP ASP A . n A 1 45 SER 45 45 45 SER SER A . n A 1 46 ASP 46 46 46 ASP ASP A . n A 1 47 ASP 47 47 47 ASP ASP A . n A 1 48 THR 48 48 48 THR THR A . n A 1 49 ILE 49 49 49 ILE ILE A . n A 1 50 ARG 50 50 50 ARG ARG A . n A 1 51 SER 51 51 51 SER SER A . n A 1 52 MET 52 52 52 MET MET A . n A 1 53 GLY 53 53 53 GLY GLY A . n A 1 54 LYS 54 54 54 LYS LYS A . n A 1 55 CYS 55 55 55 CYS CYS A . n A 1 56 MET 56 56 56 MET MET A . n A 1 57 THR 57 57 57 THR THR A . n A 1 58 ALA 58 58 58 ALA ALA A . n A 1 59 ASN 59 59 59 ASN ASN A . n A 1 60 GLY 60 60 60 GLY GLY A . n A 1 61 LEU 61 61 61 LEU LEU A . n A 1 62 ASN 62 62 62 ASN ASN A . n A 1 63 ASN 63 63 63 ASN ASN A . n A 1 64 GLY 64 64 64 GLY GLY A . n A 1 65 SER 65 65 65 SER SER A . n A 1 66 ASN 66 66 66 ASN ASN A . n A 1 67 ILE 67 67 67 ILE ILE A . n A 1 68 VAL 68 68 68 VAL VAL A . n A 1 69 ILE 69 69 69 ILE ILE A . n A 1 70 PHE 70 70 70 PHE PHE A . n A 1 71 ASN 71 71 71 ASN ASN A . n A 1 72 CYS 72 72 72 CYS CYS A . n A 1 73 SER 73 73 73 SER SER A . n A 1 74 THR 74 74 74 THR THR A . n A 1 75 ALA 75 75 75 ALA ALA A . n A 1 76 ALA 76 76 76 ALA ALA A . n A 1 77 GLU 77 77 77 GLU GLU A . n A 1 78 ASN 78 78 78 ASN ASN A . n A 1 79 ALA 79 79 79 ALA ALA A . n A 1 80 ILE 80 80 80 ILE ILE A . n A 1 81 LYS 81 81 81 LYS LYS A . n A 1 82 TRP 82 82 82 TRP TRP A . n A 1 83 GLU 83 83 83 GLU GLU A . n A 1 84 VAL 84 84 84 VAL VAL A . n A 1 85 PRO 85 85 85 PRO PRO A . n A 1 86 ILE 86 86 86 ILE ILE A . n A 1 87 ASP 87 87 87 ASP ASP A . n A 1 88 GLY 88 88 88 GLY GLY A . n A 1 89 SER 89 89 89 SER SER A . n A 1 90 ILE 90 90 90 ILE ILE A . n A 1 91 ILE 91 91 91 ILE ILE A . n A 1 92 ASN 92 92 92 ASN ASN A . n A 1 93 PRO 93 93 93 PRO PRO A . n A 1 94 SER 94 94 94 SER SER A . n A 1 95 SER 95 95 95 SER SER A . n A 1 96 GLY 96 96 96 GLY GLY A . n A 1 97 LEU 97 97 97 LEU LEU A . n A 1 98 VAL 98 98 98 VAL VAL A . n A 1 99 MET 99 99 99 MET MET A . n A 1 100 THR 100 100 100 THR THR A . n A 1 101 ALA 101 101 101 ALA ALA A . n A 1 102 PRO 102 102 102 PRO PRO A . n A 1 103 ARG 103 103 103 ARG ARG A . n A 1 104 ALA 104 104 104 ALA ALA A . n A 1 105 ALA 105 105 105 ALA ALA A . n A 1 106 SER 106 106 106 SER SER A . n A 1 107 ARG 107 107 107 ARG ARG A . n A 1 108 THR 108 108 108 THR THR A . n A 1 109 ILE 109 109 109 ILE ILE A . n A 1 110 LEU 110 110 110 LEU LEU A . n A 1 111 LEU 111 111 111 LEU LEU A . n A 1 112 LEU 112 112 112 LEU LEU A . n A 1 113 GLU 113 113 113 GLU GLU A . n A 1 114 ASP 114 114 114 ASP ASP A . n A 1 115 ASN 115 115 115 ASN ASN A . n A 1 116 ILE 116 116 116 ILE ILE A . n A 1 117 TYR 117 117 117 TYR TYR A . n A 1 118 ALA 118 118 118 ALA ALA A . n A 1 119 ALA 119 119 119 ALA ALA A . n A 1 120 SER 120 120 120 SER SER A . n A 1 121 GLN 121 121 121 GLN GLN A . n A 1 122 GLY 122 122 122 GLY GLY A . n A 1 123 TRP 123 123 123 TRP TRP A . n A 1 124 THR 124 124 124 THR THR A . n A 1 125 VAL 125 125 125 VAL VAL A . n A 1 126 THR 126 126 126 THR THR A . n A 1 127 ASN 127 127 127 ASN ASN A . n A 1 128 ASN 128 128 128 ASN ASN A . n A 1 129 VAL 129 129 129 VAL VAL A . n A 1 130 LYS 130 130 130 LYS LYS A . n A 1 131 PRO 131 131 131 PRO PRO A . n A 1 132 ILE 132 132 132 ILE ILE A . n A 1 133 VAL 133 133 133 VAL VAL A . n A 1 134 ALA 134 134 134 ALA ALA A . n A 1 135 SER 135 135 135 SER SER A . n A 1 136 ILE 136 136 136 ILE ILE A . n A 1 137 VAL 137 137 137 VAL VAL A . n A 1 138 GLY 138 138 138 GLY GLY A . n A 1 139 TYR 139 139 139 TYR TYR A . n A 1 140 LYS 140 140 140 LYS LYS A . n A 1 141 GLU 141 141 141 GLU GLU A . n A 1 142 MET 142 142 142 MET MET A . n A 1 143 CYS 143 143 143 CYS CYS A . n A 1 144 LEU 144 144 144 LEU LEU A . n A 1 145 GLN 145 145 145 GLN GLN A . n A 1 146 SER 146 146 146 SER SER A . n A 1 147 ASN 147 147 147 ASN ASN A . n A 1 148 GLY 148 148 148 GLY GLY A . n A 1 149 GLU 149 149 149 GLU GLU A . n A 1 150 ASN 150 150 150 ASN ASN A . n A 1 151 ASN 151 151 151 ASN ASN A . n A 1 152 GLY 152 152 152 GLY GLY A . n A 1 153 VAL 153 153 153 VAL VAL A . n A 1 154 TRP 154 154 154 TRP TRP A . n A 1 155 MET 155 155 155 MET MET A . n A 1 156 GLU 156 156 156 GLU GLU A . n A 1 157 ASP 157 157 157 ASP ASP A . n A 1 158 CYS 158 158 158 CYS CYS A . n A 1 159 GLU 159 159 159 GLU GLU 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 SER 162 162 162 SER SER A . n A 1 163 LEU 163 163 163 LEU LEU A . n A 1 164 GLN 164 164 164 GLN GLN A . n A 1 165 GLN 165 165 165 GLN GLN A . n A 1 166 GLN 166 166 166 GLN GLN A . n A 1 167 TRP 167 167 167 TRP TRP A . n A 1 168 ALA 168 168 168 ALA ALA A . n A 1 169 LEU 169 169 169 LEU LEU A . n A 1 170 TYR 170 170 170 TYR TYR A . n A 1 171 GLY 171 171 171 GLY GLY A . n A 1 172 ASP 172 172 172 ASP ASP A . n A 1 173 ARG 173 173 173 ARG ARG A . n A 1 174 THR 174 174 174 THR THR A . n A 1 175 ILE 175 175 175 ILE ILE A . n A 1 176 ARG 176 176 176 ARG ARG A . n A 1 177 VAL 177 177 177 VAL VAL A . n A 1 178 ASN 178 178 178 ASN ASN A . n A 1 179 SER 179 179 179 SER SER A . n A 1 180 THR 180 180 180 THR THR A . n A 1 181 ARG 181 181 181 ARG ARG A . n A 1 182 GLY 182 182 182 GLY GLY A . n A 1 183 LEU 183 183 183 LEU LEU A . n A 1 184 CYS 184 184 184 CYS CYS A . n A 1 185 VAL 185 185 185 VAL VAL A . n A 1 186 THR 186 186 186 THR THR A . n A 1 187 THR 187 187 187 THR THR A . n A 1 188 ASN 188 188 188 ASN ASN A . n A 1 189 GLY 189 189 189 GLY GLY A . n A 1 190 TYR 190 190 190 TYR TYR A . n A 1 191 ASN 191 191 191 ASN ASN A . n A 1 192 SER 192 192 192 SER SER A . n A 1 193 LYS 193 193 193 LYS LYS A . n A 1 194 ASP 194 194 194 ASP ASP A . n A 1 195 LEU 195 195 195 LEU LEU A . n A 1 196 ILE 196 196 196 ILE ILE A . n A 1 197 ILE 197 197 197 ILE ILE A . n A 1 198 ILE 198 198 198 ILE ILE A . n A 1 199 LEU 199 199 199 LEU LEU A . n A 1 200 LYS 200 200 200 LYS LYS A . n A 1 201 CYS 201 201 201 CYS CYS A . n A 1 202 GLN 202 202 202 GLN GLN A . n A 1 203 GLY 203 203 203 GLY GLY A . n A 1 204 LEU 204 204 204 LEU LEU A . n A 1 205 PRO 205 205 205 PRO PRO A . n A 1 206 SER 206 206 206 SER SER A . n A 1 207 GLN 207 207 207 GLN GLN A . n A 1 208 ARG 208 208 208 ARG ARG A . n A 1 209 TRP 209 209 209 TRP TRP A . n A 1 210 PHE 210 210 210 PHE PHE A . n A 1 211 PHE 211 211 211 PHE PHE A . n A 1 212 ASN 212 212 212 ASN ASN A . n A 1 213 SER 213 213 213 SER SER A . n A 1 214 ASP 214 214 214 ASP ASP A . n A 1 215 GLY 215 215 215 GLY GLY A . n A 1 216 ALA 216 216 216 ALA ALA A . n A 1 217 ILE 217 217 217 ILE ILE A . n A 1 218 VAL 218 218 218 VAL VAL A . n A 1 219 ASN 219 219 219 ASN ASN A . n A 1 220 PRO 220 220 220 PRO PRO A . n A 1 221 LYS 221 221 221 LYS LYS A . n A 1 222 SER 222 222 222 SER SER A . n A 1 223 ARG 223 223 223 ARG ARG A . n A 1 224 LEU 224 224 224 LEU LEU A . n A 1 225 VAL 225 225 225 VAL VAL A . n A 1 226 MET 226 226 226 MET MET A . n A 1 227 ASP 227 227 227 ASP ASP A . n A 1 228 VAL 228 228 228 VAL VAL A . n A 1 229 ARG 229 229 229 ARG ARG A . n A 1 230 ALA 230 230 230 ALA ALA A . n A 1 231 SER 231 231 231 SER SER A . n A 1 232 ASN 232 232 232 ASN ASN A . n A 1 233 VAL 233 233 233 VAL VAL A . n A 1 234 SER 234 234 234 SER SER A . n A 1 235 LEU 235 235 235 LEU LEU A . n A 1 236 ARG 236 236 236 ARG ARG A . n A 1 237 GLU 237 237 237 GLU GLU A . n A 1 238 ILE 238 238 238 ILE ILE A . n A 1 239 ILE 239 239 239 ILE ILE A . n A 1 240 ILE 240 240 240 ILE ILE A . n A 1 241 PHE 241 241 241 PHE PHE A . n A 1 242 PRO 242 242 242 PRO PRO A . n A 1 243 ALA 243 243 243 ALA ALA A . n A 1 244 THR 244 244 244 THR THR A . n A 1 245 GLY 245 245 245 GLY GLY A . n A 1 246 ASN 246 246 246 ASN ASN A . n A 1 247 PRO 247 247 247 PRO PRO A . n A 1 248 ASN 248 248 248 ASN ASN A . n A 1 249 GLN 249 249 249 GLN GLN A . n A 1 250 GLN 250 250 250 GLN GLN A . n A 1 251 TRP 251 251 251 TRP TRP A . n A 1 252 VAL 252 252 252 VAL VAL A . n A 1 253 THR 253 253 253 THR THR A . n A 1 254 GLN 254 254 254 GLN GLN A . n A 1 255 VAL 255 255 255 VAL VAL A . n A 1 256 LEU 256 256 256 LEU LEU A . n A 1 257 PRO 257 257 257 PRO PRO A . n A 1 258 SER 258 258 ? ? ? A . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 NAG 1 258 1 NAG NAG A . C 2 NAG 2 259 2 NAG NAG A . D 3 FUC 3 260 5 FUC FUC A . E 2 NAG 1 261 11 NAG NAG A . F 2 NAG 2 262 12 NAG NAG A . G 3 FUC 3 263 15 FUC FUC A . H 2 NAG 1 264 21 NAG NAG A . I 2 NAG 2 265 22 NAG NAG A . J 2 NAG 1 266 31 NAG NAG A . K 4 AMG 1 267 1 AMG AMG A . L 4 AMG 1 268 2 AMG AMG A . M 5 SO4 1 901 901 SO4 SO4 A . N 5 SO4 1 902 902 SO4 SO4 A . O 5 SO4 1 903 903 SO4 SO4 A . P 5 SO4 1 904 904 SO4 SO4 A . Q 5 SO4 1 905 905 SO4 SO4 A . R 6 ACT 1 910 910 ACT ACT A . S 7 HOH 1 911 1 HOH HOH A . S 7 HOH 2 912 2 HOH HOH A . S 7 HOH 3 913 3 HOH HOH A . S 7 HOH 4 914 4 HOH HOH A . S 7 HOH 5 915 5 HOH HOH A . S 7 HOH 6 916 6 HOH HOH A . S 7 HOH 7 917 7 HOH HOH A . S 7 HOH 8 918 8 HOH HOH A . S 7 HOH 9 919 9 HOH HOH A . S 7 HOH 10 920 10 HOH HOH A . S 7 HOH 11 921 11 HOH HOH A . S 7 HOH 12 922 12 HOH HOH A . S 7 HOH 13 923 13 HOH HOH A . S 7 HOH 14 924 14 HOH HOH A . S 7 HOH 15 925 15 HOH HOH A . S 7 HOH 16 926 16 HOH HOH A . S 7 HOH 17 927 17 HOH HOH A . S 7 HOH 18 928 18 HOH HOH A . S 7 HOH 19 929 19 HOH HOH A . S 7 HOH 20 930 20 HOH HOH A . S 7 HOH 21 931 21 HOH HOH A . S 7 HOH 22 932 22 HOH HOH A . S 7 HOH 23 933 23 HOH HOH A . S 7 HOH 24 934 24 HOH HOH A . S 7 HOH 25 935 25 HOH HOH A . S 7 HOH 26 936 26 HOH HOH A . S 7 HOH 27 937 27 HOH HOH A . S 7 HOH 28 938 28 HOH HOH A . S 7 HOH 29 939 29 HOH HOH A . S 7 HOH 30 940 30 HOH HOH A . S 7 HOH 31 941 31 HOH HOH A . S 7 HOH 32 942 32 HOH HOH A . S 7 HOH 33 943 33 HOH HOH A . S 7 HOH 34 944 34 HOH HOH A . S 7 HOH 35 945 35 HOH HOH A . S 7 HOH 36 946 36 HOH HOH A . S 7 HOH 37 947 37 HOH HOH A . S 7 HOH 38 948 38 HOH HOH A . S 7 HOH 39 949 39 HOH HOH A . S 7 HOH 40 950 40 HOH HOH A . S 7 HOH 41 951 41 HOH HOH A . S 7 HOH 42 952 42 HOH HOH A . S 7 HOH 43 953 43 HOH HOH A . S 7 HOH 44 954 44 HOH HOH A . S 7 HOH 45 955 45 HOH HOH A . S 7 HOH 46 956 46 HOH HOH A . S 7 HOH 47 957 47 HOH HOH A . S 7 HOH 48 958 48 HOH HOH A . S 7 HOH 49 959 49 HOH HOH A . S 7 HOH 50 960 50 HOH HOH A . S 7 HOH 51 961 51 HOH HOH A . S 7 HOH 52 962 52 HOH HOH A . S 7 HOH 53 963 53 HOH HOH A . S 7 HOH 54 964 54 HOH HOH A . S 7 HOH 55 965 55 HOH HOH A . S 7 HOH 56 966 56 HOH HOH A . S 7 HOH 57 967 57 HOH HOH A . S 7 HOH 58 968 58 HOH HOH A . S 7 HOH 59 969 59 HOH HOH A . S 7 HOH 60 970 60 HOH HOH A . S 7 HOH 61 971 61 HOH HOH A . S 7 HOH 62 972 62 HOH HOH A . S 7 HOH 63 973 63 HOH HOH A . S 7 HOH 64 974 64 HOH HOH A . S 7 HOH 65 975 65 HOH HOH A . S 7 HOH 66 976 66 HOH HOH A . S 7 HOH 67 977 67 HOH HOH A . S 7 HOH 68 978 68 HOH HOH A . S 7 HOH 69 979 69 HOH HOH A . S 7 HOH 70 980 70 HOH HOH A . S 7 HOH 71 981 71 HOH HOH A . S 7 HOH 72 982 72 HOH HOH A . S 7 HOH 73 983 73 HOH HOH A . S 7 HOH 74 984 74 HOH HOH A . S 7 HOH 75 985 75 HOH HOH A . S 7 HOH 76 986 76 HOH HOH A . S 7 HOH 77 987 77 HOH HOH A . S 7 HOH 78 988 78 HOH HOH A . S 7 HOH 79 989 79 HOH HOH A . S 7 HOH 80 990 80 HOH HOH A . S 7 HOH 81 991 81 HOH HOH A . S 7 HOH 82 992 82 HOH HOH A . S 7 HOH 83 993 83 HOH HOH A . S 7 HOH 84 994 84 HOH HOH A . S 7 HOH 85 995 85 HOH HOH A . S 7 HOH 86 996 86 HOH HOH A . S 7 HOH 87 997 87 HOH HOH A . S 7 HOH 88 998 88 HOH HOH A . S 7 HOH 89 999 89 HOH HOH A . S 7 HOH 90 1000 90 HOH HOH A . S 7 HOH 91 1001 91 HOH HOH A . S 7 HOH 92 1002 92 HOH HOH A . S 7 HOH 93 1003 93 HOH HOH A . S 7 HOH 94 1004 94 HOH HOH A . S 7 HOH 95 1005 95 HOH HOH A . S 7 HOH 96 1006 96 HOH HOH A . S 7 HOH 97 1007 97 HOH HOH A . S 7 HOH 98 1008 98 HOH HOH A . S 7 HOH 99 1009 99 HOH HOH A . S 7 HOH 100 1010 100 HOH HOH A . S 7 HOH 101 1011 101 HOH HOH A . S 7 HOH 102 1012 102 HOH HOH A . S 7 HOH 103 1013 103 HOH HOH A . S 7 HOH 104 1014 104 HOH HOH A . S 7 HOH 105 1015 105 HOH HOH A . S 7 HOH 106 1016 106 HOH HOH A . S 7 HOH 107 1017 107 HOH HOH A . S 7 HOH 108 1018 108 HOH HOH A . S 7 HOH 109 1019 109 HOH HOH A . S 7 HOH 110 1020 110 HOH HOH A . S 7 HOH 111 1021 111 HOH HOH A . S 7 HOH 112 1022 112 HOH HOH A . S 7 HOH 113 1023 113 HOH HOH A . S 7 HOH 114 1024 114 HOH HOH A . S 7 HOH 115 1025 115 HOH HOH A . S 7 HOH 116 1026 116 HOH HOH A . S 7 HOH 117 1027 117 HOH HOH A . S 7 HOH 118 1028 118 HOH HOH A . S 7 HOH 119 1029 119 HOH HOH A . S 7 HOH 120 1030 120 HOH HOH A . S 7 HOH 121 1031 121 HOH HOH A . S 7 HOH 122 1032 122 HOH HOH A . S 7 HOH 123 1033 123 HOH HOH A . S 7 HOH 124 1034 124 HOH HOH A . S 7 HOH 125 1035 125 HOH HOH A . S 7 HOH 126 1036 126 HOH HOH A . S 7 HOH 127 1037 127 HOH HOH A . S 7 HOH 128 1038 128 HOH HOH A . S 7 HOH 129 1039 129 HOH HOH A . S 7 HOH 130 1040 130 HOH HOH A . S 7 HOH 131 1041 131 HOH HOH A . S 7 HOH 132 1042 132 HOH HOH A . S 7 HOH 133 1043 133 HOH HOH A . S 7 HOH 134 1044 134 HOH HOH A . S 7 HOH 135 1045 135 HOH HOH A . S 7 HOH 136 1046 136 HOH HOH A . S 7 HOH 137 1047 137 HOH HOH A . S 7 HOH 138 1048 138 HOH HOH A . S 7 HOH 139 1049 139 HOH HOH A . S 7 HOH 140 1050 140 HOH HOH A . S 7 HOH 141 1051 141 HOH HOH A . S 7 HOH 142 1052 142 HOH HOH A . S 7 HOH 143 1053 143 HOH HOH A . S 7 HOH 144 1054 144 HOH HOH A . S 7 HOH 145 1055 145 HOH HOH A . S 7 HOH 146 1056 146 HOH HOH A . S 7 HOH 147 1057 147 HOH HOH A . S 7 HOH 148 1058 148 HOH HOH A . S 7 HOH 149 1059 149 HOH HOH A . S 7 HOH 150 1060 150 HOH HOH A . S 7 HOH 151 1061 151 HOH HOH A . S 7 HOH 152 1062 152 HOH HOH A . S 7 HOH 153 1063 153 HOH HOH A . S 7 HOH 154 1064 154 HOH HOH A . S 7 HOH 155 1065 155 HOH HOH A . S 7 HOH 156 1066 156 HOH HOH A . S 7 HOH 157 1067 157 HOH HOH A . S 7 HOH 158 1068 158 HOH HOH A . S 7 HOH 159 1069 159 HOH HOH A . S 7 HOH 160 1070 160 HOH HOH A . S 7 HOH 161 1071 161 HOH HOH A . S 7 HOH 162 1072 162 HOH HOH A . S 7 HOH 163 1073 163 HOH HOH A . S 7 HOH 164 1074 164 HOH HOH A . S 7 HOH 165 1075 165 HOH HOH A . S 7 HOH 166 1076 166 HOH HOH A . S 7 HOH 167 1077 167 HOH HOH A . S 7 HOH 168 1078 168 HOH HOH A . S 7 HOH 169 1079 169 HOH HOH A . S 7 HOH 170 1080 170 HOH HOH A . S 7 HOH 171 1081 171 HOH HOH A . S 7 HOH 172 1082 172 HOH HOH A . S 7 HOH 173 1083 173 HOH HOH A . S 7 HOH 174 1084 174 HOH HOH A . S 7 HOH 175 1085 175 HOH HOH A . S 7 HOH 176 1086 176 HOH HOH A . S 7 HOH 177 1087 177 HOH HOH A . S 7 HOH 178 1088 178 HOH HOH A . S 7 HOH 179 1089 179 HOH HOH A . S 7 HOH 180 1090 180 HOH HOH A . S 7 HOH 181 1091 181 HOH HOH A . S 7 HOH 182 1092 182 HOH HOH A . S 7 HOH 183 1093 183 HOH HOH A . S 7 HOH 184 1094 184 HOH HOH A . S 7 HOH 185 1095 185 HOH HOH A . S 7 HOH 186 1096 186 HOH HOH A . S 7 HOH 187 1097 187 HOH HOH A . S 7 HOH 188 1098 188 HOH HOH A . S 7 HOH 189 1099 189 HOH HOH A . S 7 HOH 190 1100 190 HOH HOH A . S 7 HOH 191 1101 191 HOH HOH A . S 7 HOH 192 1102 192 HOH HOH A . S 7 HOH 193 1103 193 HOH HOH A . S 7 HOH 194 1104 194 HOH HOH A . S 7 HOH 195 1105 195 HOH HOH A . S 7 HOH 196 1106 196 HOH HOH A . S 7 HOH 197 1107 197 HOH HOH A . S 7 HOH 198 1108 198 HOH HOH A . S 7 HOH 199 1109 199 HOH HOH A . S 7 HOH 200 1110 200 HOH HOH A . S 7 HOH 201 1111 201 HOH HOH A . S 7 HOH 202 1112 202 HOH HOH A . S 7 HOH 203 1113 203 HOH HOH A . S 7 HOH 204 1114 204 HOH HOH A . S 7 HOH 205 1115 205 HOH HOH A . S 7 HOH 206 1116 206 HOH HOH A . S 7 HOH 207 1117 207 HOH HOH A . S 7 HOH 208 1118 208 HOH HOH A . S 7 HOH 209 1119 209 HOH HOH A . S 7 HOH 210 1120 210 HOH HOH A . S 7 HOH 211 1121 211 HOH HOH A . S 7 HOH 212 1122 212 HOH HOH A . S 7 HOH 213 1123 213 HOH HOH A . S 7 HOH 214 1124 214 HOH HOH A . S 7 HOH 215 1125 215 HOH HOH A . S 7 HOH 216 1126 216 HOH HOH A . S 7 HOH 217 1127 217 HOH HOH A . S 7 HOH 218 1128 218 HOH HOH A . S 7 HOH 219 1129 219 HOH HOH A . S 7 HOH 220 1130 220 HOH HOH A . S 7 HOH 221 1131 221 HOH HOH A . S 7 HOH 222 1132 222 HOH HOH A . S 7 HOH 223 1133 223 HOH HOH A . S 7 HOH 224 1134 224 HOH HOH A . S 7 HOH 225 1135 225 HOH HOH A . S 7 HOH 226 1136 226 HOH HOH A . S 7 HOH 227 1137 227 HOH HOH A . S 7 HOH 228 1138 228 HOH HOH A . S 7 HOH 229 1139 229 HOH HOH A . S 7 HOH 230 1140 230 HOH HOH A . S 7 HOH 231 1141 231 HOH HOH A . S 7 HOH 232 1142 232 HOH HOH A . S 7 HOH 233 1143 233 HOH HOH A . S 7 HOH 234 1144 234 HOH HOH A . S 7 HOH 235 1145 235 HOH HOH A . S 7 HOH 236 1146 236 HOH HOH A . S 7 HOH 237 1147 237 HOH HOH A . S 7 HOH 238 1148 238 HOH HOH A . S 7 HOH 239 1149 239 HOH HOH A . S 7 HOH 240 1150 240 HOH HOH A . S 7 HOH 241 1151 241 HOH HOH A . S 7 HOH 242 1152 242 HOH HOH A . S 7 HOH 243 1153 243 HOH HOH A . S 7 HOH 244 1154 244 HOH HOH A . S 7 HOH 245 1155 245 HOH HOH A . S 7 HOH 246 1156 246 HOH HOH A . S 7 HOH 247 1157 247 HOH HOH A . S 7 HOH 248 1158 248 HOH HOH A . S 7 HOH 249 1159 249 HOH HOH A . S 7 HOH 250 1160 250 HOH HOH A . S 7 HOH 251 1161 251 HOH HOH A . S 7 HOH 252 1162 252 HOH HOH A . S 7 HOH 253 1163 253 HOH HOH A . S 7 HOH 254 1164 254 HOH HOH A . S 7 HOH 255 1165 255 HOH HOH A . S 7 HOH 256 1166 256 HOH HOH A . S 7 HOH 257 1167 257 HOH HOH A . S 7 HOH 258 1168 258 HOH HOH A . S 7 HOH 259 1169 259 HOH HOH A . S 7 HOH 260 1170 260 HOH HOH A . S 7 HOH 261 1171 261 HOH HOH A . S 7 HOH 262 1172 262 HOH HOH A . S 7 HOH 263 1173 263 HOH HOH A . S 7 HOH 264 1174 264 HOH HOH A . S 7 HOH 265 1175 265 HOH HOH A . S 7 HOH 266 1176 267 HOH HOH A . S 7 HOH 267 1177 268 HOH HOH A . S 7 HOH 268 1178 269 HOH HOH A . S 7 HOH 269 1179 270 HOH HOH A . S 7 HOH 270 1180 271 HOH HOH A . S 7 HOH 271 1181 272 HOH HOH A . S 7 HOH 272 1182 273 HOH HOH A . S 7 HOH 273 1183 274 HOH HOH A . S 7 HOH 274 1184 275 HOH HOH A . S 7 HOH 275 1185 276 HOH HOH A . S 7 HOH 276 1186 277 HOH HOH A . S 7 HOH 277 1187 278 HOH HOH A . S 7 HOH 278 1188 279 HOH HOH A . S 7 HOH 279 1189 280 HOH HOH A . S 7 HOH 280 1190 281 HOH HOH A . S 7 HOH 281 1191 282 HOH HOH A . S 7 HOH 282 1192 283 HOH HOH A . S 7 HOH 283 1193 284 HOH HOH A . S 7 HOH 284 1194 285 HOH HOH A . S 7 HOH 285 1195 286 HOH HOH A . S 7 HOH 286 1196 287 HOH HOH A . S 7 HOH 287 1197 288 HOH HOH A . S 7 HOH 288 1198 289 HOH HOH A . S 7 HOH 289 1199 290 HOH HOH A . S 7 HOH 290 1200 291 HOH HOH A . S 7 HOH 291 1201 292 HOH HOH A . S 7 HOH 292 1202 293 HOH HOH A . S 7 HOH 293 1203 294 HOH HOH A . S 7 HOH 294 1204 295 HOH HOH A . S 7 HOH 295 1205 296 HOH HOH A . S 7 HOH 296 1206 297 HOH HOH A . S 7 HOH 297 1207 298 HOH HOH A . S 7 HOH 298 1208 299 HOH HOH A . S 7 HOH 299 1209 300 HOH HOH A . S 7 HOH 300 1210 301 HOH HOH A . S 7 HOH 301 1211 302 HOH HOH A . S 7 HOH 302 1212 303 HOH HOH A . S 7 HOH 303 1213 304 HOH HOH A . S 7 HOH 304 1214 305 HOH HOH A . S 7 HOH 305 1215 306 HOH HOH A . S 7 HOH 306 1216 307 HOH HOH A . S 7 HOH 307 1217 308 HOH HOH A . S 7 HOH 308 1218 309 HOH HOH A . S 7 HOH 309 1219 310 HOH HOH A . S 7 HOH 310 1220 312 HOH HOH A . S 7 HOH 311 1221 313 HOH HOH A . S 7 HOH 312 1222 314 HOH HOH A . S 7 HOH 313 1223 316 HOH HOH A . S 7 HOH 314 1224 317 HOH HOH A . S 7 HOH 315 1225 318 HOH HOH A . S 7 HOH 316 1226 319 HOH HOH A . S 7 HOH 317 1227 320 HOH HOH A . S 7 HOH 318 1228 321 HOH HOH A . S 7 HOH 319 1229 322 HOH HOH A . S 7 HOH 320 1230 325 HOH HOH A . S 7 HOH 321 1231 326 HOH HOH A . S 7 HOH 322 1232 327 HOH HOH A . S 7 HOH 323 1233 328 HOH HOH A . S 7 HOH 324 1234 329 HOH HOH A . S 7 HOH 325 1235 330 HOH HOH A . S 7 HOH 326 1236 331 HOH HOH A . S 7 HOH 327 1237 332 HOH HOH A . S 7 HOH 328 1238 333 HOH HOH A . S 7 HOH 329 1239 334 HOH HOH A . S 7 HOH 330 1240 335 HOH HOH A . S 7 HOH 331 1241 336 HOH HOH A . S 7 HOH 332 1242 337 HOH HOH A . S 7 HOH 333 1243 338 HOH HOH A . S 7 HOH 334 1244 339 HOH HOH A . S 7 HOH 335 1245 340 HOH HOH A . S 7 HOH 336 1246 341 HOH HOH A . S 7 HOH 337 1247 342 HOH HOH A . S 7 HOH 338 1248 343 HOH HOH A . S 7 HOH 339 1249 344 HOH HOH A . S 7 HOH 340 1250 346 HOH HOH A . S 7 HOH 341 1251 347 HOH HOH A . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 63 A ASN 63 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 71 A ASN 71 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 178 A ASN 178 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 232 A ASN 232 ? ASN 'GLYCOSYLATION SITE' # loop_ _pdbx_struct_assembly.id _pdbx_struct_assembly.details _pdbx_struct_assembly.method_details _pdbx_struct_assembly.oligomeric_details _pdbx_struct_assembly.oligomeric_count 1 author_defined_assembly ? monomeric 1 2 software_defined_assembly PISA dimeric 2 3 software_defined_assembly PISA dimeric 2 4 software_defined_assembly PQS tetrameric 4 # loop_ _pdbx_struct_assembly_gen.assembly_id _pdbx_struct_assembly_gen.oper_expression _pdbx_struct_assembly_gen.asym_id_list 1 1 A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S 2 1,2 A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S 3 1,3 A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S 4 1,4,5,6 A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 2 'ABSA (A^2)' 7720 ? 2 MORE -73 ? 2 'SSA (A^2)' 24480 ? 3 'ABSA (A^2)' 9010 ? 3 MORE -43 ? 3 'SSA (A^2)' 22810 ? # loop_ _pdbx_struct_oper_list.id _pdbx_struct_oper_list.type _pdbx_struct_oper_list.name _pdbx_struct_oper_list.symmetry_operation _pdbx_struct_oper_list.matrix[1][1] _pdbx_struct_oper_list.matrix[1][2] _pdbx_struct_oper_list.matrix[1][3] _pdbx_struct_oper_list.vector[1] _pdbx_struct_oper_list.matrix[2][1] _pdbx_struct_oper_list.matrix[2][2] _pdbx_struct_oper_list.matrix[2][3] _pdbx_struct_oper_list.vector[2] _pdbx_struct_oper_list.matrix[3][1] _pdbx_struct_oper_list.matrix[3][2] _pdbx_struct_oper_list.matrix[3][3] _pdbx_struct_oper_list.vector[3] 1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 2 'crystal symmetry operation' 6_555 x,-y+1/2,-z+1/4 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 63.0620000000 0.0000000000 0.0000000000 -1.0000000000 19.0097500000 3 'crystal symmetry operation' 5_554 -x+1/2,y,-z-1/4 -1.0000000000 0.0000000000 0.0000000000 63.0620000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 -19.0097500000 4 'crystal symmetry operation' 7_545 y+1/2,x-1/2,-z+1/2 0.0000000000 1.0000000000 0.0000000000 63.0620000000 1.0000000000 0.0000000000 0.0000000000 -63.0620000000 0.0000000000 0.0000000000 -1.0000000000 38.0195000000 5 'crystal symmetry operation' 10_655 -x+1,-y,z -1.0000000000 0.0000000000 0.0000000000 126.1240000000 0.0000000000 -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 6 'crystal symmetry operation' 16_555 -y+1/2,-x+1/2,-z+1/2 0.0000000000 -1.0000000000 0.0000000000 63.0620000000 -1.0000000000 0.0000000000 0.0000000000 63.0620000000 0.0000000000 0.0000000000 -1.0000000000 38.0195000000 # loop_ _pdbx_struct_special_symmetry.id _pdbx_struct_special_symmetry.PDB_model_num _pdbx_struct_special_symmetry.auth_asym_id _pdbx_struct_special_symmetry.auth_comp_id _pdbx_struct_special_symmetry.auth_seq_id _pdbx_struct_special_symmetry.PDB_ins_code _pdbx_struct_special_symmetry.label_asym_id _pdbx_struct_special_symmetry.label_comp_id _pdbx_struct_special_symmetry.label_seq_id 1 1 A SO4 904 ? P SO4 . 2 1 A HOH 947 ? S HOH . # 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 2008-11-25 2 'Structure model' 1 1 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' 'Derived calculations' 2 2 'Structure model' 'Version format compliance' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.2.0019 ? 1 DNA 'data collection' . ? 2 MOSFLM 'data reduction' . ? 3 SCALA 'data scaling' . ? 4 REFMAC phasing 5.2.0019 ? 5 # _pdbx_entry_details.entry_id 3CA5 _pdbx_entry_details.sequence_details ;AUTHORS STATE THAT THE ELECTRON DENSITY OF THE STRUCTURE INDICATES CLEARLY THAT THE AMINO ACID AT POSITION 224 IS A LEU AND NOT A HIS. ; _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ? # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 OG1 A THR 1 ? ? OG A SER 45 ? A 2.08 2 1 O A HOH 1068 ? ? O A HOH 1149 ? ? 2.18 # loop_ _pdbx_validate_symm_contact.id _pdbx_validate_symm_contact.PDB_model_num _pdbx_validate_symm_contact.auth_atom_id_1 _pdbx_validate_symm_contact.auth_asym_id_1 _pdbx_validate_symm_contact.auth_comp_id_1 _pdbx_validate_symm_contact.auth_seq_id_1 _pdbx_validate_symm_contact.PDB_ins_code_1 _pdbx_validate_symm_contact.label_alt_id_1 _pdbx_validate_symm_contact.site_symmetry_1 _pdbx_validate_symm_contact.auth_atom_id_2 _pdbx_validate_symm_contact.auth_asym_id_2 _pdbx_validate_symm_contact.auth_comp_id_2 _pdbx_validate_symm_contact.auth_seq_id_2 _pdbx_validate_symm_contact.PDB_ins_code_2 _pdbx_validate_symm_contact.label_alt_id_2 _pdbx_validate_symm_contact.site_symmetry_2 _pdbx_validate_symm_contact.dist 1 1 O A HOH 1180 ? ? 1_555 O A HOH 1180 ? ? 8_555 2.08 2 1 NH2 A ARG 37 ? ? 1_555 OD1 A ASN 151 ? B 12_555 2.11 # 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 ASP A 11 ? ? 59.26 18.78 2 1 ASN A 147 ? ? -145.27 31.69 3 1 ASN A 150 ? ? 71.48 -4.29 4 1 ARG A 223 ? ? 80.28 -6.54 # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 Y 1 A GLU 77 ? CG ? A GLU 77 CG 2 1 Y 1 A GLU 77 ? CD ? A GLU 77 CD 3 1 Y 1 A GLU 77 ? OE1 ? A GLU 77 OE1 4 1 Y 1 A GLU 77 ? OE2 ? A GLU 77 OE2 5 1 Y 1 A GLU 159 ? CG ? A GLU 159 CG 6 1 Y 1 A GLU 159 ? CD ? A GLU 159 CD 7 1 Y 1 A GLU 159 ? OE1 ? A GLU 159 OE1 8 1 Y 1 A GLU 159 ? OE2 ? A GLU 159 OE2 # _pdbx_unobs_or_zero_occ_residues.id 1 _pdbx_unobs_or_zero_occ_residues.PDB_model_num 1 _pdbx_unobs_or_zero_occ_residues.polymer_flag Y _pdbx_unobs_or_zero_occ_residues.occupancy_flag 1 _pdbx_unobs_or_zero_occ_residues.auth_asym_id A _pdbx_unobs_or_zero_occ_residues.auth_comp_id SER _pdbx_unobs_or_zero_occ_residues.auth_seq_id 258 _pdbx_unobs_or_zero_occ_residues.PDB_ins_code ? _pdbx_unobs_or_zero_occ_residues.label_asym_id A _pdbx_unobs_or_zero_occ_residues.label_comp_id SER _pdbx_unobs_or_zero_occ_residues.label_seq_id 258 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 ALPHA-L-FUCOSE FUC 4 ALPHA-METHYL-D-GALACTOSIDE AMG 5 'SULFATE ION' SO4 6 'ACETATE ION' ACT 7 water HOH #