data_2YGO # _entry.id 2YGO # _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 2YGO PDBE EBI-48076 WWPDB D_1290048076 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 2YGQ unspecified ;WIF DOMAIN-EPIDERMAL GROWTH FACTOR (EGF)-LIKE DOMAINS 1-3 OF HUMAN WNT INHIBITORY FACTOR 1 IN COMPLEX WITH 1,2-DIPALMITOYLPHOSPHATIDYLCHOLINE ; PDB 2YGP unspecified 'WIF DOMAIN-EGF-LIKE DOMAIN 1 MET77TRP OF HUMAN WNT INHIBITORY FACTOR 1 IN COMPLEX WITH 1,2- DIPALMITOYLPHOSPHATIDYLCHOLINE' PDB 2YGN unspecified 'WIF DOMAIN OF HUMAN WNT INHIBITORY FACTOR 1 IN COMPLEX WITH 1,2-DIPALMITOYLPHOSPHATIDYLCHOLINE' # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 2YGO _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2011-04-19 _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Malinauskas, T.' 1 'Aricescu, A.R.' 2 'Lu, W.' 3 'Siebold, C.' 4 'Jones, E.Y.' 5 # _citation.id primary _citation.title 'Modular Mechanism of Wnt Signaling Inhibition by Wnt Inhibitory Factor 1' _citation.journal_abbrev Nat.Struct.Mol.Biol. _citation.journal_volume 18 _citation.page_first 886 _citation.page_last ? _citation.year 2011 _citation.journal_id_ASTM ? _citation.country US _citation.journal_id_ISSN 1545-9993 _citation.journal_id_CSD ? _citation.book_publisher ? _citation.pdbx_database_id_PubMed 21743455 _citation.pdbx_database_id_DOI 10.1038/NSMB.2081 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Malinauskas, T.' 1 primary 'Aricescu, A.R.' 2 primary 'Lu, W.' 3 primary 'Siebold, C.' 4 primary 'Jones, E.Y.' 5 # _cell.entry_id 2YGO _cell.length_a 50.996 _cell.length_b 134.260 _cell.length_c 60.403 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 8 _cell.pdbx_unique_axis ? # _symmetry.entry_id 2YGO _symmetry.space_group_name_H-M 'C 2 2 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 21 # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man 'WNT INHIBITORY FACTOR 1' 21076.068 1 ? ? 'WIF DOMAIN-EGF-LIKE DOMAIN 1, RESIDUES 35-210' ? 2 non-polymer syn 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE 734.039 1 ? ? ? ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 1 ? ? ? ? 4 non-polymer syn 'SODIUM ION' 22.990 1 ? ? ? ? 5 water nat water 18.015 151 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name WIF-1 # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer yes _entity_poly.pdbx_seq_one_letter_code ;ETGSLYLWIDAHQARVLIGFEEDILIVSEG(MLY)MAPFTHDFR(MLY)AQQRMPAIPVNIHSMNFTWQAAGQAEYFYEF LSLRSLD(MLY)GIMADPTVNVPLLGTVPH(MLY)ASVVQVGFPCLG(MLY)QDGVAAFEVDVIVMNSEGNTIL(MLY)T PQNAIFFKTCQQAECPGGCRNGGFCNERRICECPDGFHGPHCEGTKHHHHHH ; _entity_poly.pdbx_seq_one_letter_code_can ;ETGSLYLWIDAHQARVLIGFEEDILIVSEGKMAPFTHDFRKAQQRMPAIPVNIHSMNFTWQAAGQAEYFYEFLSLRSLDK GIMADPTVNVPLLGTVPHKASVVQVGFPCLGKQDGVAAFEVDVIVMNSEGNTILKTPQNAIFFKTCQQAECPGGCRNGGF CNERRICECPDGFHGPHCEGTKHHHHHH ; _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 GLU n 1 2 THR n 1 3 GLY n 1 4 SER n 1 5 LEU n 1 6 TYR n 1 7 LEU n 1 8 TRP n 1 9 ILE n 1 10 ASP n 1 11 ALA n 1 12 HIS n 1 13 GLN n 1 14 ALA n 1 15 ARG n 1 16 VAL n 1 17 LEU n 1 18 ILE n 1 19 GLY n 1 20 PHE n 1 21 GLU n 1 22 GLU n 1 23 ASP n 1 24 ILE n 1 25 LEU n 1 26 ILE n 1 27 VAL n 1 28 SER n 1 29 GLU n 1 30 GLY n 1 31 MLY n 1 32 MET n 1 33 ALA n 1 34 PRO n 1 35 PHE n 1 36 THR n 1 37 HIS n 1 38 ASP n 1 39 PHE n 1 40 ARG n 1 41 MLY n 1 42 ALA n 1 43 GLN n 1 44 GLN n 1 45 ARG n 1 46 MET n 1 47 PRO n 1 48 ALA n 1 49 ILE n 1 50 PRO n 1 51 VAL n 1 52 ASN n 1 53 ILE n 1 54 HIS n 1 55 SER n 1 56 MET n 1 57 ASN n 1 58 PHE n 1 59 THR n 1 60 TRP n 1 61 GLN n 1 62 ALA n 1 63 ALA n 1 64 GLY n 1 65 GLN n 1 66 ALA n 1 67 GLU n 1 68 TYR n 1 69 PHE n 1 70 TYR n 1 71 GLU n 1 72 PHE n 1 73 LEU n 1 74 SER n 1 75 LEU n 1 76 ARG n 1 77 SER n 1 78 LEU n 1 79 ASP n 1 80 MLY n 1 81 GLY n 1 82 ILE n 1 83 MET n 1 84 ALA n 1 85 ASP n 1 86 PRO n 1 87 THR n 1 88 VAL n 1 89 ASN n 1 90 VAL n 1 91 PRO n 1 92 LEU n 1 93 LEU n 1 94 GLY n 1 95 THR n 1 96 VAL n 1 97 PRO n 1 98 HIS n 1 99 MLY n 1 100 ALA n 1 101 SER n 1 102 VAL n 1 103 VAL n 1 104 GLN n 1 105 VAL n 1 106 GLY n 1 107 PHE n 1 108 PRO n 1 109 CYS n 1 110 LEU n 1 111 GLY n 1 112 MLY n 1 113 GLN n 1 114 ASP n 1 115 GLY n 1 116 VAL n 1 117 ALA n 1 118 ALA n 1 119 PHE n 1 120 GLU n 1 121 VAL n 1 122 ASP n 1 123 VAL n 1 124 ILE n 1 125 VAL n 1 126 MET n 1 127 ASN n 1 128 SER n 1 129 GLU n 1 130 GLY n 1 131 ASN n 1 132 THR n 1 133 ILE n 1 134 LEU n 1 135 MLY n 1 136 THR n 1 137 PRO n 1 138 GLN n 1 139 ASN n 1 140 ALA n 1 141 ILE n 1 142 PHE n 1 143 PHE n 1 144 LYS n 1 145 THR n 1 146 CYS n 1 147 GLN n 1 148 GLN n 1 149 ALA n 1 150 GLU n 1 151 CYS n 1 152 PRO n 1 153 GLY n 1 154 GLY n 1 155 CYS n 1 156 ARG n 1 157 ASN n 1 158 GLY n 1 159 GLY n 1 160 PHE n 1 161 CYS n 1 162 ASN n 1 163 GLU n 1 164 ARG n 1 165 ARG n 1 166 ILE n 1 167 CYS n 1 168 GLU n 1 169 CYS n 1 170 PRO n 1 171 ASP n 1 172 GLY n 1 173 PHE n 1 174 HIS n 1 175 GLY n 1 176 PRO n 1 177 HIS n 1 178 CYS n 1 179 GLU n 1 180 GLY n 1 181 THR n 1 182 LYS n 1 183 HIS n 1 184 HIS n 1 185 HIS n 1 186 HIS n 1 187 HIS n 1 188 HIS n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name HUMAN _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene ? _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'HOMO SAPIENS' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 9606 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name HUMAN _entity_src_gen.pdbx_host_org_scientific_name 'HOMO SAPIENS' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 9606 _entity_src_gen.host_org_genus ? _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line 'N-ACETYLGLUCOSAMINYLTRANSFERASE I-NEGATIVE HEK 293S GNTI(-)CELLS' _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type PLASMID _entity_src_gen.pdbx_host_org_vector PHLSEC _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name ? _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code WIF1_HUMAN _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_align_begin ? _struct_ref.pdbx_db_accession Q9Y5W5 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 2YGO _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 4 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 179 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession Q9Y5W5 _struct_ref_seq.db_align_beg 35 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 210 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 35 _struct_ref_seq.pdbx_auth_seq_align_end 210 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 2YGO GLU A 1 ? UNP Q9Y5W5 ? ? 'expression tag' 32 1 1 2YGO THR A 2 ? UNP Q9Y5W5 ? ? 'expression tag' 33 2 1 2YGO GLY A 3 ? UNP Q9Y5W5 ? ? 'expression tag' 34 3 1 2YGO MLY A 135 ? UNP Q9Y5W5 GLN 166 variant 166 4 1 2YGO GLY A 180 ? UNP Q9Y5W5 ? ? 'expression tag' 211 5 1 2YGO THR A 181 ? UNP Q9Y5W5 ? ? 'expression tag' 212 6 1 2YGO LYS A 182 ? UNP Q9Y5W5 ? ? 'expression tag' 213 7 1 2YGO HIS A 183 ? UNP Q9Y5W5 ? ? 'expression tag' 214 8 1 2YGO HIS A 184 ? UNP Q9Y5W5 ? ? 'expression tag' 215 9 1 2YGO HIS A 185 ? UNP Q9Y5W5 ? ? 'expression tag' 216 10 1 2YGO HIS A 186 ? UNP Q9Y5W5 ? ? 'expression tag' 217 11 1 2YGO HIS A 187 ? UNP Q9Y5W5 ? ? 'expression tag' 218 12 1 2YGO HIS A 188 ? UNP Q9Y5W5 ? ? 'expression tag' 219 13 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 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 MLY 'L-peptide linking' n N-DIMETHYL-LYSINE ? 'C8 H18 N2 O2' 174.241 NA non-polymer . 'SODIUM ION' ? 'Na 1' 22.990 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PCF non-polymer . 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE ? 'C40 H80 N O8 P' 734.039 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 2YGO _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.45 _exptl_crystal.density_percent_sol 50 _exptl_crystal.description NONE # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 7.0 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '1.3 M DIAMMONIUM TARTRATE, 100 MM BIS-TRIS PROPANE PH 7.0' # _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 MARRESEARCH _diffrn_detector.pdbx_collection_date ? _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 'HORIZONTALLY SIDE DIFFRACTING SILICON 111 CRYSTAL' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.873 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'ESRF BEAMLINE ID23-2' _diffrn_source.pdbx_synchrotron_site ESRF _diffrn_source.pdbx_synchrotron_beamline ID23-2 _diffrn_source.pdbx_wavelength 0.873 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 2YGO _reflns.observed_criterion_sigma_I 0.0 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 40.00 _reflns.d_resolution_high 1.85 _reflns.number_obs 18293 _reflns.number_all ? _reflns.percent_possible_obs 100.0 _reflns.pdbx_Rmerge_I_obs 0.14 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 15.50 _reflns.B_iso_Wilson_estimate 17.56 _reflns.pdbx_redundancy 7.3 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 1.85 _reflns_shell.d_res_low 1.99 _reflns_shell.percent_possible_all 100.0 _reflns_shell.Rmerge_I_obs 0.94 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 1.90 _reflns_shell.pdbx_redundancy 7.2 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 2YGO _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 17107 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 0.00 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 37.422 _refine.ls_d_res_high 1.850 _refine.ls_percent_reflns_obs 94.26 _refine.ls_R_factor_obs 0.1856 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.1839 _refine.ls_R_factor_R_free 0.2168 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.2 _refine.ls_number_reflns_R_free 886 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean 36.27 _refine.aniso_B[1][1] 5.9344 _refine.aniso_B[2][2] -4.8759 _refine.aniso_B[3][3] -1.0585 _refine.aniso_B[1][2] 0.0000 _refine.aniso_B[1][3] 0.0000 _refine.aniso_B[2][3] 0.0000 _refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' _refine.solvent_model_param_ksol 0.346 _refine.solvent_model_param_bsol 44.411 _refine.pdbx_solvent_vdw_probe_radii 1.00 _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii 0.72 _refine.pdbx_ls_cross_valid_method ? _refine.details ? _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ML _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML 0.24 _refine.pdbx_overall_phase_error 20.04 _refine.overall_SU_B ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 1400 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 65 _refine_hist.number_atoms_solvent 151 _refine_hist.number_atoms_total 1616 _refine_hist.d_res_high 1.850 _refine_hist.d_res_low 37.422 # 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 f_bond_d 0.015 ? ? 1508 'X-RAY DIFFRACTION' ? f_angle_d 2.069 ? ? 2025 'X-RAY DIFFRACTION' ? f_dihedral_angle_d 18.794 ? ? 584 'X-RAY DIFFRACTION' ? f_chiral_restr 0.152 ? ? 216 'X-RAY DIFFRACTION' ? f_plane_restr 0.008 ? ? 255 'X-RAY DIFFRACTION' ? # loop_ _refine_ls_shell.pdbx_refine_id _refine_ls_shell.pdbx_total_number_of_bins_used _refine_ls_shell.d_res_high _refine_ls_shell.d_res_low _refine_ls_shell.number_reflns_R_work _refine_ls_shell.R_factor_R_work _refine_ls_shell.percent_reflns_obs _refine_ls_shell.R_factor_R_free _refine_ls_shell.R_factor_R_free_error _refine_ls_shell.percent_reflns_R_free _refine_ls_shell.number_reflns_R_free _refine_ls_shell.number_reflns_all _refine_ls_shell.R_factor_all 'X-RAY DIFFRACTION' . 1.8500 1.9659 2360 0.2364 85.00 0.2787 . . 147 . . 'X-RAY DIFFRACTION' . 1.9659 2.1177 2576 0.1931 91.00 0.2638 . . 134 . . 'X-RAY DIFFRACTION' . 2.1177 2.3308 2681 0.1866 95.00 0.2320 . . 160 . . 'X-RAY DIFFRACTION' . 2.3308 2.6680 2736 0.1853 96.00 0.2269 . . 149 . . 'X-RAY DIFFRACTION' . 2.6680 3.3610 2856 0.1726 99.00 0.2168 . . 151 . . 'X-RAY DIFFRACTION' . 3.3610 37.4294 3012 0.1772 100.00 0.1831 . . 145 . . # _struct.entry_id 2YGO _struct.title 'WIF domain-EGF-like domain 1 of human Wnt inhibitory factor 1 in complex with 1,2-dipalmitoylphosphatidylcholine' _struct.pdbx_descriptor 'WNT INHIBITORY FACTOR 1' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 2YGO _struct_keywords.pdbx_keywords 'SIGNALING PROTEIN' _struct_keywords.text 'SIGNALING PROTEIN, WNT SIGNALING PATHWAY, WNT ANTAGONIST, MORPHOGEN, CANCER, GLYCOSAMINOGLYCAN' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 4 ? E N N 5 ? # _struct_biol.id 1 # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 ASP A 10 ? GLY A 19 ? ASP A 41 GLY A 50 1 ? 10 HELX_P HELX_P2 2 PRO A 34 ? HIS A 37 ? PRO A 65 HIS A 68 5 ? 4 HELX_P HELX_P3 3 ASP A 38 ? ARG A 45 ? ASP A 69 ARG A 76 1 ? 8 # _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 109 SG ? ? ? 1_555 A CYS 146 SG ? ? A CYS 140 A CYS 177 1_555 ? ? ? ? ? ? ? 2.041 ? disulf2 disulf ? ? A CYS 151 SG ? ? ? 1_555 A CYS 161 SG ? ? A CYS 182 A CYS 192 1_555 ? ? ? ? ? ? ? 2.037 ? disulf3 disulf ? ? A CYS 155 SG ? ? ? 1_555 A CYS 167 SG ? ? A CYS 186 A CYS 198 1_555 ? ? ? ? ? ? ? 2.037 ? disulf4 disulf ? ? A CYS 169 SG ? ? ? 1_555 A CYS 178 SG ? ? A CYS 200 A CYS 209 1_555 ? ? ? ? ? ? ? 2.029 ? covale1 covale ? ? A GLY 30 C ? ? ? 1_555 A MLY 31 N ? ? A GLY 61 A MLY 62 1_555 ? ? ? ? ? ? ? 1.338 ? covale2 covale ? ? A MLY 31 C ? ? ? 1_555 A MET 32 N ? ? A MLY 62 A MET 63 1_555 ? ? ? ? ? ? ? 1.343 ? covale3 covale ? ? A ARG 40 C ? ? ? 1_555 A MLY 41 N ? ? A ARG 71 A MLY 72 1_555 ? ? ? ? ? ? ? 1.335 ? covale4 covale ? ? A MLY 41 C ? ? ? 1_555 A ALA 42 N ? ? A MLY 72 A ALA 73 1_555 ? ? ? ? ? ? ? 1.348 ? covale5 covale ? ? A ASN 57 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 88 A NAG 1214 1_555 ? ? ? ? ? ? ? 1.404 ? covale6 covale ? ? A ASP 79 C ? ? ? 1_555 A MLY 80 N ? ? A ASP 110 A MLY 111 1_555 ? ? ? ? ? ? ? 1.345 ? covale7 covale ? ? A MLY 80 C ? ? ? 1_555 A GLY 81 N ? ? A MLY 111 A GLY 112 1_555 ? ? ? ? ? ? ? 1.335 ? covale8 covale ? ? A HIS 98 C ? ? ? 1_555 A MLY 99 N ? ? A HIS 129 A MLY 130 1_555 ? ? ? ? ? ? ? 1.323 ? covale9 covale ? ? A MLY 99 C ? ? ? 1_555 A ALA 100 N ? ? A MLY 130 A ALA 131 1_555 ? ? ? ? ? ? ? 1.358 ? covale10 covale ? ? A GLY 111 C ? ? ? 1_555 A MLY 112 N ? ? A GLY 142 A MLY 143 1_555 ? ? ? ? ? ? ? 1.343 ? covale11 covale ? ? A MLY 112 C ? ? ? 1_555 A GLN 113 N ? ? A MLY 143 A GLN 144 1_555 ? ? ? ? ? ? ? 1.367 ? covale12 covale ? ? A LEU 134 C ? ? ? 1_555 A MLY 135 N ? ? A LEU 165 A MLY 166 1_555 ? ? ? ? ? ? ? 1.341 ? covale13 covale ? ? A MLY 135 C ? ? ? 1_555 A THR 136 N ? ? A MLY 166 A THR 167 1_555 ? ? ? ? ? ? ? 1.345 ? metalc1 metalc ? ? D NA . NA ? ? ? 1_555 E HOH . O ? ? A NA 1215 A HOH 2151 1_555 ? ? ? ? ? ? ? 2.396 ? metalc2 metalc ? ? D NA . NA ? ? ? 1_555 E HOH . O ? ? A NA 1215 A HOH 2137 1_555 ? ? ? ? ? ? ? 2.454 ? metalc3 metalc ? ? D NA . NA ? ? ? 1_555 E HOH . O ? ? A NA 1215 A HOH 2138 1_555 ? ? ? ? ? ? ? 2.704 ? metalc4 metalc ? ? D NA . NA ? ? ? 1_555 A CYS 155 O ? ? A NA 1215 A CYS 186 1_555 ? ? ? ? ? ? ? 2.395 ? metalc5 metalc ? ? D NA . NA ? ? ? 1_555 A GLY 159 O ? ? A NA 1215 A GLY 190 1_555 ? ? ? ? ? ? ? 2.729 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA ? 6 ? AB ? 4 ? AC ? 4 ? AD ? 2 ? AE ? 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 AA 1 2 ? anti-parallel AA 2 3 ? anti-parallel AA 3 4 ? anti-parallel AA 4 5 ? anti-parallel AA 5 6 ? anti-parallel AB 1 2 ? anti-parallel AB 2 3 ? anti-parallel AB 3 4 ? anti-parallel AC 1 2 ? anti-parallel AC 2 3 ? anti-parallel AC 3 4 ? anti-parallel AD 1 2 ? anti-parallel AE 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 AA 1 MLY A 31 ? MET A 32 ? MLY A 62 MET A 63 AA 2 ILE A 24 ? SER A 28 ? ILE A 55 SER A 59 AA 3 LEU A 5 ? ILE A 9 ? LEU A 36 ILE A 40 AA 4 SER A 55 ? ALA A 62 ? SER A 86 ALA A 93 AA 5 SER A 101 ? GLY A 106 ? SER A 132 GLY A 137 AA 6 THR A 87 ? VAL A 88 ? THR A 118 VAL A 119 AB 1 LEU A 93 ? THR A 95 ? LEU A 124 THR A 126 AB 2 PHE A 69 ? SER A 77 ? PHE A 100 SER A 108 AB 3 GLY A 115 ? MET A 126 ? GLY A 146 MET A 157 AB 4 THR A 132 ? MLY A 135 ? THR A 163 MLY A 166 AC 1 LEU A 93 ? THR A 95 ? LEU A 124 THR A 126 AC 2 PHE A 69 ? SER A 77 ? PHE A 100 SER A 108 AC 3 GLY A 115 ? MET A 126 ? GLY A 146 MET A 157 AC 4 PHE A 142 ? CYS A 146 ? PHE A 173 CYS A 177 AD 1 THR A 132 ? MLY A 135 ? THR A 163 MLY A 166 AD 2 GLY A 115 ? MET A 126 ? GLY A 146 MET A 157 AE 1 PHE A 160 ? CYS A 161 ? PHE A 191 CYS A 192 AE 2 CYS A 167 ? GLU A 168 ? CYS A 198 GLU A 199 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id AA 1 2 N MLY A 31 ? N MLY A 62 O SER A 28 ? O SER A 59 AA 2 3 N ILE A 26 ? N ILE A 57 O LEU A 7 ? O LEU A 38 AA 3 4 N TRP A 8 ? N TRP A 39 O THR A 59 ? O THR A 90 AA 4 5 N TRP A 60 ? N TRP A 91 O SER A 101 ? O SER A 132 AA 5 6 N GLY A 106 ? N GLY A 137 O THR A 87 ? O THR A 118 AB 1 2 N GLY A 94 ? N GLY A 125 O TYR A 70 ? O TYR A 101 AB 2 3 N ARG A 76 ? N ARG A 107 O GLU A 120 ? O GLU A 151 AB 3 4 O VAL A 125 ? O VAL A 156 N ILE A 133 ? N ILE A 164 AC 1 2 N GLY A 94 ? N GLY A 125 O TYR A 70 ? O TYR A 101 AC 2 3 N ARG A 76 ? N ARG A 107 O GLU A 120 ? O GLU A 151 AC 3 4 N PHE A 119 ? N PHE A 150 O PHE A 142 ? O PHE A 173 AD 1 2 N ILE A 133 ? N ILE A 164 O VAL A 125 ? O VAL A 156 AE 1 2 N PHE A 160 ? N PHE A 191 O GLU A 168 ? O GLU A 199 # 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 ? ? ? ? 10 'BINDING SITE FOR RESIDUE PCF A 1213' AC2 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG A 1214' AC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NA A 1215' # 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 10 LEU A 17 ? LEU A 48 . ? 1_555 ? 2 AC1 10 ILE A 18 ? ILE A 49 . ? 1_555 ? 3 AC1 10 ILE A 24 ? ILE A 55 . ? 1_555 ? 4 AC1 10 ARG A 45 ? ARG A 76 . ? 1_555 ? 5 AC1 10 MET A 46 ? MET A 77 . ? 1_555 ? 6 AC1 10 PRO A 47 ? PRO A 78 . ? 1_555 ? 7 AC1 10 PHE A 58 ? PHE A 89 . ? 1_555 ? 8 AC1 10 VAL A 125 ? VAL A 156 . ? 1_555 ? 9 AC1 10 PHE A 142 ? PHE A 173 . ? 1_555 ? 10 AC1 10 ARG A 165 ? ARG A 196 . ? 2_555 ? 11 AC2 7 HIS A 12 ? HIS A 43 . ? 1_555 ? 12 AC2 7 GLN A 13 ? GLN A 44 . ? 1_555 ? 13 AC2 7 GLU A 21 ? GLU A 52 . ? 3_555 ? 14 AC2 7 ASN A 57 ? ASN A 88 . ? 1_555 ? 15 AC2 7 HOH E . ? HOH A 2008 . ? 1_555 ? 16 AC2 7 HOH E . ? HOH A 2149 . ? 1_555 ? 17 AC2 7 HOH E . ? HOH A 2150 . ? 1_555 ? 18 AC3 5 CYS A 155 ? CYS A 186 . ? 1_555 ? 19 AC3 5 GLY A 159 ? GLY A 190 . ? 1_555 ? 20 AC3 5 HOH E . ? HOH A 2137 . ? 1_555 ? 21 AC3 5 HOH E . ? HOH A 2138 . ? 1_555 ? 22 AC3 5 HOH E . ? HOH A 2151 . ? 1_555 ? # _database_PDB_matrix.entry_id 2YGO _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 2YGO _atom_sites.fract_transf_matrix[1][1] 0.019609 _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] 0.007448 _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] 0.016555 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N NA O P 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 2 ? 9.042 -35.559 6.808 1.00 77.82 ? 33 THR A N 1 ATOM 2 C CA . THR A 1 2 ? 8.082 -36.350 7.585 1.00 84.94 ? 33 THR A CA 1 ATOM 3 C C . THR A 1 2 ? 6.783 -35.595 7.918 1.00 67.38 ? 33 THR A C 1 ATOM 4 O O . THR A 1 2 ? 5.720 -36.010 7.452 1.00 68.95 ? 33 THR A O 1 ATOM 5 C CB . THR A 1 2 ? 8.752 -37.129 8.737 1.00 87.83 ? 33 THR A CB 1 ATOM 6 O OG1 . THR A 1 2 ? 7.751 -37.828 9.481 1.00 82.11 ? 33 THR A OG1 1 ATOM 7 C CG2 . THR A 1 2 ? 9.583 -36.238 9.669 1.00 81.95 ? 33 THR A CG2 1 ATOM 8 N N . GLY A 1 3 ? 6.882 -34.511 8.701 1.00 47.23 ? 34 GLY A N 1 ATOM 9 C CA . GLY A 1 3 ? 5.747 -33.667 9.074 1.00 38.68 ? 34 GLY A CA 1 ATOM 10 C C . GLY A 1 3 ? 5.286 -32.826 7.896 1.00 34.18 ? 34 GLY A C 1 ATOM 11 O O . GLY A 1 3 ? 6.097 -32.510 7.021 1.00 40.00 ? 34 GLY A O 1 ATOM 12 N N . SER A 1 4 ? 3.984 -32.482 7.828 1.00 31.35 ? 35 SER A N 1 ATOM 13 C CA . SER A 1 4 ? 3.465 -31.735 6.674 1.00 26.70 ? 35 SER A CA 1 ATOM 14 C C . SER A 1 4 ? 2.667 -30.475 6.990 1.00 25.42 ? 35 SER A C 1 ATOM 15 O O . SER A 1 4 ? 2.329 -29.743 6.060 1.00 23.57 ? 35 SER A O 1 ATOM 16 C CB . SER A 1 4 ? 2.655 -32.656 5.761 1.00 36.33 ? 35 SER A CB 1 ATOM 17 O OG . SER A 1 4 ? 1.527 -33.174 6.447 1.00 30.47 ? 35 SER A OG 1 ATOM 18 N N . LEU A 1 5 ? 2.320 -30.237 8.269 1.00 19.70 ? 36 LEU A N 1 ATOM 19 C CA . LEU A 1 5 ? 1.530 -29.057 8.612 1.00 18.23 ? 36 LEU A CA 1 ATOM 20 C C . LEU A 1 5 ? 2.344 -27.785 8.598 1.00 17.16 ? 36 LEU A C 1 ATOM 21 O O . LEU A 1 5 ? 3.468 -27.765 9.108 1.00 15.30 ? 36 LEU A O 1 ATOM 22 C CB . LEU A 1 5 ? 0.859 -29.195 9.989 1.00 24.44 ? 36 LEU A CB 1 ATOM 23 C CG . LEU A 1 5 ? -0.301 -30.174 10.081 1.00 25.70 ? 36 LEU A CG 1 ATOM 24 C CD1 . LEU A 1 5 ? -0.430 -30.676 11.489 1.00 29.15 ? 36 LEU A CD1 1 ATOM 25 C CD2 . LEU A 1 5 ? -1.619 -29.512 9.623 1.00 26.88 ? 36 LEU A CD2 1 ATOM 26 N N . TYR A 1 6 ? 1.742 -26.708 8.079 1.00 13.72 ? 37 TYR A N 1 ATOM 27 C CA . TYR A 1 6 ? 2.391 -25.383 8.070 1.00 11.45 ? 37 TYR A CA 1 ATOM 28 C C . TYR A 1 6 ? 1.390 -24.340 8.504 1.00 10.85 ? 37 TYR A C 1 ATOM 29 O O . TYR A 1 6 ? 0.226 -24.411 8.117 1.00 10.97 ? 37 TYR A O 1 ATOM 30 C CB . TYR A 1 6 ? 2.902 -25.002 6.668 1.00 14.69 ? 37 TYR A CB 1 ATOM 31 C CG . TYR A 1 6 ? 4.092 -25.794 6.174 1.00 17.23 ? 37 TYR A CG 1 ATOM 32 C CD1 . TYR A 1 6 ? 3.919 -26.987 5.475 1.00 20.72 ? 37 TYR A CD1 1 ATOM 33 C CD2 . TYR A 1 6 ? 5.389 -25.327 6.360 1.00 16.84 ? 37 TYR A CD2 1 ATOM 34 C CE1 . TYR A 1 6 ? 5.010 -27.717 5.011 1.00 25.97 ? 37 TYR A CE1 1 ATOM 35 C CE2 . TYR A 1 6 ? 6.489 -26.037 5.880 1.00 26.05 ? 37 TYR A CE2 1 ATOM 36 C CZ . TYR A 1 6 ? 6.292 -27.234 5.210 1.00 27.41 ? 37 TYR A CZ 1 ATOM 37 O OH . TYR A 1 6 ? 7.361 -27.937 4.728 1.00 43.21 ? 37 TYR A OH 1 ATOM 38 N N . LEU A 1 7 ? 1.844 -23.354 9.288 1.00 9.89 ? 38 LEU A N 1 ATOM 39 C CA . LEU A 1 7 ? 1.062 -22.193 9.685 1.00 7.93 ? 38 LEU A CA 1 ATOM 40 C C . LEU A 1 7 ? 2.024 -21.007 9.643 1.00 14.98 ? 38 LEU A C 1 ATOM 41 O O . LEU A 1 7 ? 3.126 -21.078 10.219 1.00 12.21 ? 38 LEU A O 1 ATOM 42 C CB . LEU A 1 7 ? 0.450 -22.349 11.094 1.00 9.94 ? 38 LEU A CB 1 ATOM 43 C CG . LEU A 1 7 ? -0.243 -21.115 11.669 1.00 12.19 ? 38 LEU A CG 1 ATOM 44 C CD1 . LEU A 1 7 ? -1.578 -20.801 10.941 1.00 13.98 ? 38 LEU A CD1 1 ATOM 45 C CD2 . LEU A 1 7 ? -0.418 -21.243 13.180 1.00 16.42 ? 38 LEU A CD2 1 ATOM 46 N N . TRP A 1 8 ? 1.634 -19.948 8.919 1.00 11.26 ? 39 TRP A N 1 ATOM 47 C CA . TRP A 1 8 ? 2.474 -18.752 8.807 1.00 13.56 ? 39 TRP A CA 1 ATOM 48 C C . TRP A 1 8 ? 1.646 -17.497 8.608 1.00 14.19 ? 39 TRP A C 1 ATOM 49 O O . TRP A 1 8 ? 0.446 -17.570 8.308 1.00 13.31 ? 39 TRP A O 1 ATOM 50 C CB . TRP A 1 8 ? 3.547 -18.912 7.694 1.00 11.66 ? 39 TRP A CB 1 ATOM 51 C CG . TRP A 1 8 ? 3.073 -18.876 6.259 1.00 11.17 ? 39 TRP A CG 1 ATOM 52 C CD1 . TRP A 1 8 ? 3.152 -17.817 5.398 1.00 13.53 ? 39 TRP A CD1 1 ATOM 53 C CD2 . TRP A 1 8 ? 2.547 -19.979 5.489 1.00 15.34 ? 39 TRP A CD2 1 ATOM 54 N NE1 . TRP A 1 8 ? 2.625 -18.164 4.173 1.00 14.47 ? 39 TRP A NE1 1 ATOM 55 C CE2 . TRP A 1 8 ? 2.324 -19.505 4.177 1.00 10.15 ? 39 TRP A CE2 1 ATOM 56 C CE3 . TRP A 1 8 ? 2.265 -21.331 5.776 1.00 19.06 ? 39 TRP A CE3 1 ATOM 57 C CZ2 . TRP A 1 8 ? 1.836 -20.332 3.151 1.00 17.69 ? 39 TRP A CZ2 1 ATOM 58 C CZ3 . TRP A 1 8 ? 1.793 -22.153 4.752 1.00 18.67 ? 39 TRP A CZ3 1 ATOM 59 C CH2 . TRP A 1 8 ? 1.563 -21.647 3.465 1.00 20.92 ? 39 TRP A CH2 1 ATOM 60 N N . ILE A 1 9 ? 2.288 -16.344 8.765 1.00 10.08 ? 40 ILE A N 1 ATOM 61 C CA . ILE A 1 9 ? 1.686 -15.055 8.466 1.00 9.98 ? 40 ILE A CA 1 ATOM 62 C C . ILE A 1 9 ? 2.359 -14.599 7.158 1.00 14.98 ? 40 ILE A C 1 ATOM 63 O O . ILE A 1 9 ? 3.582 -14.453 7.139 1.00 14.77 ? 40 ILE A O 1 ATOM 64 C CB . ILE A 1 9 ? 1.863 -14.019 9.599 1.00 11.46 ? 40 ILE A CB 1 ATOM 65 C CG1 . ILE A 1 9 ? 1.160 -14.464 10.900 1.00 15.29 ? 40 ILE A CG1 1 ATOM 66 C CG2 . ILE A 1 9 ? 1.296 -12.662 9.120 1.00 10.72 ? 40 ILE A CG2 1 ATOM 67 C CD1 . ILE A 1 9 ? 1.713 -13.746 12.183 1.00 21.79 ? 40 ILE A CD1 1 ATOM 68 N N . ASP A 1 10 ? 1.578 -14.375 6.086 1.00 11.06 ? 41 ASP A N 1 ATOM 69 C CA . ASP A 1 10 ? 2.130 -13.975 4.782 1.00 13.60 ? 41 ASP A CA 1 ATOM 70 C C . ASP A 1 10 ? 2.901 -12.657 4.869 1.00 20.09 ? 41 ASP A C 1 ATOM 71 O O . ASP A 1 10 ? 2.587 -11.816 5.722 1.00 14.66 ? 41 ASP A O 1 ATOM 72 C CB . ASP A 1 10 ? 1.055 -13.922 3.681 1.00 16.93 ? 41 ASP A CB 1 ATOM 73 C CG . ASP A 1 10 ? 0.057 -12.783 3.808 1.00 30.62 ? 41 ASP A CG 1 ATOM 74 O OD1 . ASP A 1 10 ? 0.392 -11.662 3.402 1.00 23.60 ? 41 ASP A OD1 1 ATOM 75 O OD2 . ASP A 1 10 ? -1.078 -13.032 4.281 1.00 22.52 ? 41 ASP A OD2 1 ATOM 76 N N . ALA A 1 11 ? 3.910 -12.500 3.996 1.00 15.55 ? 42 ALA A N 1 ATOM 77 C CA . ALA A 1 11 ? 4.777 -11.308 3.933 1.00 16.48 ? 42 ALA A CA 1 ATOM 78 C C . ALA A 1 11 ? 4.023 -9.972 3.923 1.00 20.31 ? 42 ALA A C 1 ATOM 79 O O . ALA A 1 11 ? 4.442 -9.044 4.622 1.00 21.92 ? 42 ALA A O 1 ATOM 80 C CB . ALA A 1 11 ? 5.709 -11.402 2.725 1.00 18.42 ? 42 ALA A CB 1 ATOM 81 N N . HIS A 1 12 ? 2.909 -9.878 3.167 1.00 15.76 ? 43 HIS A N 1 ATOM 82 C CA . HIS A 1 12 ? 2.113 -8.648 3.105 1.00 20.13 ? 43 HIS A CA 1 ATOM 83 C C . HIS A 1 12 ? 1.445 -8.336 4.452 1.00 21.45 ? 43 HIS A C 1 ATOM 84 O O . HIS A 1 12 ? 1.506 -7.195 4.910 1.00 17.55 ? 43 HIS A O 1 ATOM 85 C CB . HIS A 1 12 ? 1.065 -8.691 1.973 1.00 21.92 ? 43 HIS A CB 1 ATOM 86 C CG . HIS A 1 12 ? 0.313 -7.406 1.841 1.00 29.57 ? 43 HIS A CG 1 ATOM 87 N ND1 . HIS A 1 12 ? -1.039 -7.327 2.118 1.00 42.82 ? 43 HIS A ND1 1 ATOM 88 C CD2 . HIS A 1 12 ? 0.761 -6.174 1.511 1.00 32.91 ? 43 HIS A CD2 1 ATOM 89 C CE1 . HIS A 1 12 ? -1.372 -6.060 1.940 1.00 26.93 ? 43 HIS A CE1 1 ATOM 90 N NE2 . HIS A 1 12 ? -0.327 -5.331 1.565 1.00 40.77 ? 43 HIS A NE2 1 ATOM 91 N N . GLN A 1 13 ? 0.803 -9.342 5.080 1.00 16.95 ? 44 GLN A N 1 ATOM 92 C CA . GLN A 1 13 ? 0.179 -9.157 6.396 1.00 16.61 ? 44 GLN A CA 1 ATOM 93 C C . GLN A 1 13 ? 1.235 -8.806 7.469 1.00 21.48 ? 44 GLN A C 1 ATOM 94 O O . GLN A 1 13 ? 0.976 -7.960 8.334 1.00 15.75 ? 44 GLN A O 1 ATOM 95 C CB . GLN A 1 13 ? -0.613 -10.432 6.801 1.00 15.09 ? 44 GLN A CB 1 ATOM 96 C CG . GLN A 1 13 ? -1.250 -10.375 8.200 1.00 16.11 ? 44 GLN A CG 1 ATOM 97 C CD . GLN A 1 13 ? -2.365 -9.372 8.267 1.00 20.26 ? 44 GLN A CD 1 ATOM 98 O OE1 . GLN A 1 13 ? -3.508 -9.672 7.924 1.00 18.98 ? 44 GLN A OE1 1 ATOM 99 N NE2 . GLN A 1 13 ? -2.043 -8.145 8.662 1.00 21.03 ? 44 GLN A NE2 1 ATOM 100 N N . ALA A 1 14 ? 2.411 -9.459 7.414 1.00 13.53 ? 45 ALA A N 1 ATOM 101 C CA . ALA A 1 14 ? 3.512 -9.220 8.352 1.00 12.91 ? 45 ALA A CA 1 ATOM 102 C C . ALA A 1 14 ? 3.995 -7.763 8.250 1.00 13.84 ? 45 ALA A C 1 ATOM 103 O O . ALA A 1 14 ? 4.277 -7.147 9.269 1.00 20.54 ? 45 ALA A O 1 ATOM 104 C CB . ALA A 1 14 ? 4.661 -10.160 8.053 1.00 16.18 ? 45 ALA A CB 1 ATOM 105 N N . ARG A 1 15 ? 4.059 -7.214 7.024 1.00 18.90 ? 46 ARG A N 1 ATOM 106 C CA . ARG A 1 15 ? 4.465 -5.826 6.797 1.00 27.58 ? 46 ARG A CA 1 ATOM 107 C C . ARG A 1 15 ? 3.510 -4.839 7.488 1.00 26.44 ? 46 ARG A C 1 ATOM 108 O O . ARG A 1 15 ? 3.987 -3.973 8.204 1.00 20.69 ? 46 ARG A O 1 ATOM 109 C CB . ARG A 1 15 ? 4.617 -5.532 5.299 1.00 18.11 ? 46 ARG A CB 1 ATOM 110 C CG . ARG A 1 15 ? 5.247 -4.162 5.003 1.00 33.12 ? 46 ARG A CG 1 ATOM 111 C CD . ARG A 1 15 ? 5.152 -3.841 3.526 1.00 41.44 ? 46 ARG A CD 1 ATOM 112 N NE . ARG A 1 15 ? 4.693 -2.472 3.288 1.00 81.88 ? 46 ARG A NE 1 ATOM 113 C CZ . ARG A 1 15 ? 3.424 -2.124 3.087 1.00 91.61 ? 46 ARG A CZ 1 ATOM 114 N NH1 . ARG A 1 15 ? 2.465 -3.043 3.098 1.00 94.98 ? 46 ARG A NH1 1 ATOM 115 N NH2 . ARG A 1 15 ? 3.104 -0.855 2.876 1.00 80.26 ? 46 ARG A NH2 1 ATOM 116 N N . VAL A 1 16 ? 2.175 -4.995 7.314 1.00 26.90 ? 47 VAL A N 1 ATOM 117 C CA . VAL A 1 16 ? 1.194 -4.103 7.977 1.00 28.29 ? 47 VAL A CA 1 ATOM 118 C C . VAL A 1 16 ? 1.253 -4.190 9.511 1.00 27.03 ? 47 VAL A C 1 ATOM 119 O O . VAL A 1 16 ? 1.037 -3.196 10.197 1.00 24.15 ? 47 VAL A O 1 ATOM 120 C CB . VAL A 1 16 ? -0.263 -4.127 7.398 1.00 36.79 ? 47 VAL A CB 1 ATOM 121 C CG1 . VAL A 1 16 ? -0.339 -4.771 6.011 1.00 37.68 ? 47 VAL A CG1 1 ATOM 122 C CG2 . VAL A 1 16 ? -1.274 -4.754 8.352 1.00 27.72 ? 47 VAL A CG2 1 ATOM 123 N N . LEU A 1 17 ? 1.585 -5.371 10.037 1.00 21.88 ? 48 LEU A N 1 ATOM 124 C CA . LEU A 1 17 ? 1.639 -5.612 11.459 1.00 22.92 ? 48 LEU A CA 1 ATOM 125 C C . LEU A 1 17 ? 2.929 -5.168 12.148 1.00 29.63 ? 48 LEU A C 1 ATOM 126 O O . LEU A 1 17 ? 2.849 -4.488 13.166 1.00 34.14 ? 48 LEU A O 1 ATOM 127 C CB . LEU A 1 17 ? 1.335 -7.102 11.721 1.00 23.07 ? 48 LEU A CB 1 ATOM 128 C CG . LEU A 1 17 ? 1.183 -7.560 13.163 1.00 38.75 ? 48 LEU A CG 1 ATOM 129 C CD1 . LEU A 1 17 ? -0.113 -7.037 13.779 1.00 42.16 ? 48 LEU A CD1 1 ATOM 130 C CD2 . LEU A 1 17 ? 1.195 -9.070 13.231 1.00 36.86 ? 48 LEU A CD2 1 ATOM 131 N N . ILE A 1 18 ? 4.103 -5.575 11.629 1.00 22.75 ? 49 ILE A N 1 ATOM 132 C CA . ILE A 1 18 ? 5.405 -5.292 12.254 1.00 28.96 ? 49 ILE A CA 1 ATOM 133 C C . ILE A 1 18 ? 6.378 -4.432 11.441 1.00 19.74 ? 49 ILE A C 1 ATOM 134 O O . ILE A 1 18 ? 7.410 -4.041 11.977 1.00 36.61 ? 49 ILE A O 1 ATOM 135 C CB . ILE A 1 18 ? 6.103 -6.576 12.811 1.00 33.65 ? 49 ILE A CB 1 ATOM 136 C CG1 . ILE A 1 18 ? 6.439 -7.563 11.694 1.00 33.19 ? 49 ILE A CG1 1 ATOM 137 C CG2 . ILE A 1 18 ? 5.295 -7.236 13.925 1.00 57.31 ? 49 ILE A CG2 1 ATOM 138 C CD1 . ILE A 1 18 ? 7.894 -7.965 11.639 1.00 58.61 ? 49 ILE A CD1 1 ATOM 139 N N . GLY A 1 19 ? 6.073 -4.170 10.175 1.00 23.36 ? 50 GLY A N 1 ATOM 140 C CA . GLY A 1 19 ? 6.932 -3.335 9.340 1.00 27.88 ? 50 GLY A CA 1 ATOM 141 C C . GLY A 1 19 ? 7.910 -4.060 8.439 1.00 43.87 ? 50 GLY A C 1 ATOM 142 O O . GLY A 1 19 ? 8.534 -3.421 7.585 1.00 46.78 ? 50 GLY A O 1 ATOM 143 N N . PHE A 1 20 ? 8.051 -5.387 8.607 1.00 33.17 ? 51 PHE A N 1 ATOM 144 C CA . PHE A 1 20 ? 8.967 -6.188 7.791 1.00 42.42 ? 51 PHE A CA 1 ATOM 145 C C . PHE A 1 20 ? 8.235 -7.141 6.861 1.00 25.75 ? 51 PHE A C 1 ATOM 146 O O . PHE A 1 20 ? 7.420 -7.946 7.311 1.00 22.56 ? 51 PHE A O 1 ATOM 147 C CB . PHE A 1 20 ? 10.050 -6.876 8.645 1.00 32.44 ? 51 PHE A CB 1 ATOM 148 C CG . PHE A 1 20 ? 10.902 -5.853 9.366 1.00 62.67 ? 51 PHE A CG 1 ATOM 149 C CD1 . PHE A 1 20 ? 11.871 -5.121 8.681 1.00 45.33 ? 51 PHE A CD1 1 ATOM 150 C CD2 . PHE A 1 20 ? 10.674 -5.554 10.709 1.00 59.22 ? 51 PHE A CD2 1 ATOM 151 C CE1 . PHE A 1 20 ? 12.611 -4.126 9.331 1.00 53.19 ? 51 PHE A CE1 1 ATOM 152 C CE2 . PHE A 1 20 ? 11.416 -4.559 11.360 1.00 44.38 ? 51 PHE A CE2 1 ATOM 153 C CZ . PHE A 1 20 ? 12.377 -3.850 10.665 1.00 62.50 ? 51 PHE A CZ 1 ATOM 154 N N . GLU A 1 21 ? 8.490 -7.003 5.556 1.00 25.48 ? 52 GLU A N 1 ATOM 155 C CA . GLU A 1 21 ? 7.842 -7.806 4.530 1.00 30.13 ? 52 GLU A CA 1 ATOM 156 C C . GLU A 1 21 ? 8.557 -9.141 4.313 1.00 43.37 ? 52 GLU A C 1 ATOM 157 O O . GLU A 1 21 ? 9.276 -9.339 3.335 1.00 28.05 ? 52 GLU A O 1 ATOM 158 C CB . GLU A 1 21 ? 7.618 -6.998 3.238 1.00 29.67 ? 52 GLU A CB 1 ATOM 159 C CG . GLU A 1 21 ? 6.618 -7.644 2.288 1.00 43.08 ? 52 GLU A CG 1 ATOM 160 C CD . GLU A 1 21 ? 5.858 -6.718 1.354 1.00 66.57 ? 52 GLU A CD 1 ATOM 161 O OE1 . GLU A 1 21 ? 6.431 -5.691 0.921 1.00 54.17 ? 52 GLU A OE1 1 ATOM 162 O OE2 . GLU A 1 21 ? 4.689 -7.036 1.038 1.00 72.83 ? 52 GLU A OE2 1 ATOM 163 N N . GLU A 1 22 ? 8.339 -10.057 5.260 1.00 25.95 ? 53 GLU A N 1 ATOM 164 C CA . GLU A 1 22 ? 8.887 -11.402 5.286 1.00 22.30 ? 53 GLU A CA 1 ATOM 165 C C . GLU A 1 22 ? 7.838 -12.316 5.940 1.00 19.12 ? 53 GLU A C 1 ATOM 166 O O . GLU A 1 22 ? 7.183 -11.903 6.912 1.00 18.06 ? 53 GLU A O 1 ATOM 167 C CB . GLU A 1 22 ? 10.157 -11.419 6.145 1.00 30.11 ? 53 GLU A CB 1 ATOM 168 C CG . GLU A 1 22 ? 11.448 -11.269 5.352 1.00 72.49 ? 53 GLU A CG 1 ATOM 169 C CD . GLU A 1 22 ? 12.057 -9.878 5.313 1.00 103.82 ? 53 GLU A CD 1 ATOM 170 O OE1 . GLU A 1 22 ? 12.471 -9.376 6.384 1.00 96.32 ? 53 GLU A OE1 1 ATOM 171 O OE2 . GLU A 1 22 ? 12.162 -9.310 4.201 1.00 109.90 ? 53 GLU A OE2 1 ATOM 172 N N . ASP A 1 23 ? 7.683 -13.543 5.428 1.00 17.03 ? 54 ASP A N 1 ATOM 173 C CA . ASP A 1 23 ? 6.738 -14.501 6.026 1.00 15.99 ? 54 ASP A CA 1 ATOM 174 C C . ASP A 1 23 ? 7.183 -14.755 7.473 1.00 17.34 ? 54 ASP A C 1 ATOM 175 O O . ASP A 1 23 ? 8.387 -14.854 7.726 1.00 21.12 ? 54 ASP A O 1 ATOM 176 C CB . ASP A 1 23 ? 6.770 -15.858 5.282 1.00 17.88 ? 54 ASP A CB 1 ATOM 177 C CG . ASP A 1 23 ? 6.191 -15.906 3.891 1.00 24.79 ? 54 ASP A CG 1 ATOM 178 O OD1 . ASP A 1 23 ? 5.374 -15.020 3.551 1.00 23.89 ? 54 ASP A OD1 1 ATOM 179 O OD2 . ASP A 1 23 ? 6.538 -16.845 3.138 1.00 31.50 ? 54 ASP A OD2 1 ATOM 180 N N . ILE A 1 24 ? 6.227 -14.828 8.420 1.00 13.64 ? 55 ILE A N 1 ATOM 181 C CA . ILE A 1 24 ? 6.531 -15.168 9.815 1.00 15.52 ? 55 ILE A CA 1 ATOM 182 C C . ILE A 1 24 ? 6.092 -16.611 9.966 1.00 16.37 ? 55 ILE A C 1 ATOM 183 O O . ILE A 1 24 ? 4.896 -16.881 9.896 1.00 16.77 ? 55 ILE A O 1 ATOM 184 C CB . ILE A 1 24 ? 5.799 -14.251 10.833 1.00 14.55 ? 55 ILE A CB 1 ATOM 185 C CG1 . ILE A 1 24 ? 6.266 -12.777 10.695 1.00 17.98 ? 55 ILE A CG1 1 ATOM 186 C CG2 . ILE A 1 24 ? 5.980 -14.787 12.295 1.00 17.75 ? 55 ILE A CG2 1 ATOM 187 C CD1 . ILE A 1 24 ? 5.312 -11.751 11.436 1.00 22.20 ? 55 ILE A CD1 1 ATOM 188 N N . LEU A 1 25 ? 7.041 -17.530 10.155 1.00 18.36 ? 56 LEU A N 1 ATOM 189 C CA . LEU A 1 25 ? 6.758 -18.952 10.282 1.00 17.17 ? 56 LEU A CA 1 ATOM 190 C C . LEU A 1 25 ? 6.354 -19.282 11.714 1.00 18.76 ? 56 LEU A C 1 ATOM 191 O O . LEU A 1 25 ? 7.047 -18.899 12.651 1.00 20.61 ? 56 LEU A O 1 ATOM 192 C CB . LEU A 1 25 ? 7.970 -19.820 9.826 1.00 17.11 ? 56 LEU A CB 1 ATOM 193 C CG . LEU A 1 25 ? 8.684 -19.404 8.512 1.00 32.01 ? 56 LEU A CG 1 ATOM 194 C CD1 . LEU A 1 25 ? 9.804 -20.388 8.166 1.00 42.35 ? 56 LEU A CD1 1 ATOM 195 C CD2 . LEU A 1 25 ? 7.706 -19.289 7.332 1.00 29.41 ? 56 LEU A CD2 1 ATOM 196 N N . ILE A 1 26 ? 5.225 -19.959 11.881 1.00 13.83 ? 57 ILE A N 1 ATOM 197 C CA . ILE A 1 26 ? 4.715 -20.347 13.216 1.00 15.74 ? 57 ILE A CA 1 ATOM 198 C C . ILE A 1 26 ? 4.829 -21.852 13.399 1.00 14.44 ? 57 ILE A C 1 ATOM 199 O O . ILE A 1 26 ? 5.308 -22.319 14.438 1.00 15.20 ? 57 ILE A O 1 ATOM 200 C CB . ILE A 1 26 ? 3.313 -19.783 13.520 1.00 12.95 ? 57 ILE A CB 1 ATOM 201 C CG1 . ILE A 1 26 ? 3.296 -18.241 13.339 1.00 15.46 ? 57 ILE A CG1 1 ATOM 202 C CG2 . ILE A 1 26 ? 2.864 -20.196 14.945 1.00 13.03 ? 57 ILE A CG2 1 ATOM 203 C CD1 . ILE A 1 26 ? 1.918 -17.611 13.267 1.00 17.75 ? 57 ILE A CD1 1 ATOM 204 N N . VAL A 1 27 ? 4.396 -22.624 12.387 1.00 10.90 ? 58 VAL A N 1 ATOM 205 C CA . VAL A 1 27 ? 4.556 -24.082 12.401 1.00 12.05 ? 58 VAL A CA 1 ATOM 206 C C . VAL A 1 27 ? 5.187 -24.467 11.054 1.00 15.18 ? 58 VAL A C 1 ATOM 207 O O . VAL A 1 27 ? 4.738 -23.978 10.015 1.00 15.37 ? 58 VAL A O 1 ATOM 208 C CB . VAL A 1 27 ? 3.207 -24.832 12.649 1.00 14.43 ? 58 VAL A CB 1 ATOM 209 C CG1 . VAL A 1 27 ? 3.350 -26.340 12.469 1.00 15.83 ? 58 VAL A CG1 1 ATOM 210 C CG2 . VAL A 1 27 ? 2.634 -24.516 14.031 1.00 16.08 ? 58 VAL A CG2 1 ATOM 211 N N . SER A 1 28 ? 6.225 -25.310 11.070 1.00 12.98 ? 59 SER A N 1 ATOM 212 C CA . SER A 1 28 ? 6.855 -25.780 9.828 1.00 25.14 ? 59 SER A CA 1 ATOM 213 C C . SER A 1 28 ? 7.072 -27.271 9.954 1.00 27.38 ? 59 SER A C 1 ATOM 214 O O . SER A 1 28 ? 7.657 -27.734 10.948 1.00 22.27 ? 59 SER A O 1 ATOM 215 C CB . SER A 1 28 ? 8.176 -25.053 9.545 1.00 33.94 ? 59 SER A CB 1 ATOM 216 O OG . SER A 1 28 ? 7.966 -23.673 9.289 1.00 31.96 ? 59 SER A OG 1 ATOM 217 N N . GLU A 1 29 ? 6.525 -28.034 8.979 1.00 19.23 ? 60 GLU A N 1 ATOM 218 C CA . GLU A 1 29 ? 6.600 -29.495 8.924 1.00 21.16 ? 60 GLU A CA 1 ATOM 219 C C . GLU A 1 29 ? 6.103 -30.128 10.230 1.00 23.40 ? 60 GLU A C 1 ATOM 220 O O . GLU A 1 29 ? 6.755 -31.027 10.778 1.00 24.45 ? 60 GLU A O 1 ATOM 221 C CB . GLU A 1 29 ? 8.033 -29.967 8.568 1.00 22.78 ? 60 GLU A CB 1 ATOM 222 C CG . GLU A 1 29 ? 8.597 -29.387 7.283 1.00 31.41 ? 60 GLU A CG 1 ATOM 223 C CD . GLU A 1 29 ? 10.101 -29.515 7.116 1.00 63.18 ? 60 GLU A CD 1 ATOM 224 O OE1 . GLU A 1 29 ? 10.620 -30.652 7.207 1.00 60.67 ? 60 GLU A OE1 1 ATOM 225 O OE2 . GLU A 1 29 ? 10.760 -28.475 6.886 1.00 60.84 ? 60 GLU A OE2 1 ATOM 226 N N . GLY A 1 30 ? 4.983 -29.602 10.745 1.00 19.96 ? 61 GLY A N 1 ATOM 227 C CA . GLY A 1 30 ? 4.342 -30.077 11.964 1.00 20.53 ? 61 GLY A CA 1 ATOM 228 C C . GLY A 1 30 ? 5.048 -29.718 13.258 1.00 23.49 ? 61 GLY A C 1 ATOM 229 O O . GLY A 1 30 ? 4.667 -30.217 14.305 1.00 23.61 ? 61 GLY A O 1 HETATM 230 N N . MLY A 1 31 ? 6.064 -28.849 13.217 1.00 18.70 ? 62 MLY A N 1 HETATM 231 C CA . MLY A 1 31 ? 6.786 -28.473 14.436 1.00 19.58 ? 62 MLY A CA 1 HETATM 232 C CB . MLY A 1 31 ? 8.302 -28.716 14.209 1.00 27.59 ? 62 MLY A CB 1 HETATM 233 C CG . MLY A 1 31 ? 8.570 -30.187 13.809 1.00 44.60 ? 62 MLY A CG 1 HETATM 234 C CD . MLY A 1 31 ? 8.758 -31.072 15.051 1.00 69.32 ? 62 MLY A CD 1 HETATM 235 C CE . MLY A 1 31 ? 7.953 -32.387 14.865 1.00 74.53 ? 62 MLY A CE 1 HETATM 236 N NZ . MLY A 1 31 ? 8.077 -33.299 16.040 1.00 83.69 ? 62 MLY A NZ 1 HETATM 237 C CH1 . MLY A 1 31 ? 7.352 -34.550 15.703 1.00 88.85 ? 62 MLY A CH1 1 HETATM 238 C CH2 . MLY A 1 31 ? 7.378 -32.694 17.194 1.00 70.39 ? 62 MLY A CH2 1 HETATM 239 C C . MLY A 1 31 ? 6.683 -26.978 14.719 1.00 22.51 ? 62 MLY A C 1 HETATM 240 O O . MLY A 1 31 ? 6.913 -26.164 13.823 1.00 18.93 ? 62 MLY A O 1 ATOM 241 N N . MET A 1 32 ? 6.391 -26.617 15.979 1.00 20.28 ? 63 MET A N 1 ATOM 242 C CA . MET A 1 32 ? 6.302 -25.218 16.422 1.00 16.44 ? 63 MET A CA 1 ATOM 243 C C . MET A 1 32 ? 7.631 -24.510 16.164 1.00 19.26 ? 63 MET A C 1 ATOM 244 O O . MET A 1 32 ? 8.684 -25.097 16.414 1.00 20.46 ? 63 MET A O 1 ATOM 245 C CB . MET A 1 32 ? 5.980 -25.147 17.932 1.00 23.01 ? 63 MET A CB 1 ATOM 246 C CG . MET A 1 32 ? 4.645 -25.758 18.320 1.00 31.24 ? 63 MET A CG 1 ATOM 247 S SD . MET A 1 32 ? 3.220 -24.790 17.767 1.00 32.09 ? 63 MET A SD 1 ATOM 248 C CE . MET A 1 32 ? 3.322 -23.371 18.847 1.00 35.63 ? 63 MET A CE 1 ATOM 249 N N . ALA A 1 33 ? 7.589 -23.265 15.680 1.00 13.15 ? 64 ALA A N 1 ATOM 250 C CA . ALA A 1 33 ? 8.799 -22.480 15.390 1.00 20.85 ? 64 ALA A CA 1 ATOM 251 C C . ALA A 1 33 ? 9.634 -22.243 16.676 1.00 24.59 ? 64 ALA A C 1 ATOM 252 O O . ALA A 1 33 ? 9.041 -22.163 17.761 1.00 21.38 ? 64 ALA A O 1 ATOM 253 C CB . ALA A 1 33 ? 8.435 -21.148 14.751 1.00 22.57 ? 64 ALA A CB 1 ATOM 254 N N . PRO A 1 34 ? 10.991 -22.168 16.565 1.00 30.80 ? 65 PRO A N 1 ATOM 255 C CA . PRO A 1 34 ? 11.832 -21.992 17.766 1.00 26.39 ? 65 PRO A CA 1 ATOM 256 C C . PRO A 1 34 ? 11.456 -20.835 18.685 1.00 32.99 ? 65 PRO A C 1 ATOM 257 O O . PRO A 1 34 ? 11.479 -21.044 19.900 1.00 39.48 ? 65 PRO A O 1 ATOM 258 C CB . PRO A 1 34 ? 13.243 -21.842 17.187 1.00 35.72 ? 65 PRO A CB 1 ATOM 259 C CG . PRO A 1 34 ? 13.193 -22.641 15.910 1.00 34.36 ? 65 PRO A CG 1 ATOM 260 C CD . PRO A 1 34 ? 11.835 -22.317 15.353 1.00 39.13 ? 65 PRO A CD 1 ATOM 261 N N . PHE A 1 35 ? 11.044 -19.657 18.133 1.00 27.37 ? 66 PHE A N 1 ATOM 262 C CA . PHE A 1 35 ? 10.652 -18.491 18.945 1.00 34.65 ? 66 PHE A CA 1 ATOM 263 C C . PHE A 1 35 ? 9.478 -18.771 19.909 1.00 29.51 ? 66 PHE A C 1 ATOM 264 O O . PHE A 1 35 ? 9.331 -18.072 20.910 1.00 32.08 ? 66 PHE A O 1 ATOM 265 C CB . PHE A 1 35 ? 10.385 -17.232 18.074 1.00 37.67 ? 66 PHE A CB 1 ATOM 266 C CG . PHE A 1 35 ? 8.994 -17.099 17.479 1.00 40.74 ? 66 PHE A CG 1 ATOM 267 C CD1 . PHE A 1 35 ? 8.648 -17.779 16.314 1.00 30.85 ? 66 PHE A CD1 1 ATOM 268 C CD2 . PHE A 1 35 ? 8.036 -16.283 18.079 1.00 30.40 ? 66 PHE A CD2 1 ATOM 269 C CE1 . PHE A 1 35 ? 7.365 -17.657 15.763 1.00 26.29 ? 66 PHE A CE1 1 ATOM 270 C CE2 . PHE A 1 35 ? 6.755 -16.154 17.524 1.00 34.27 ? 66 PHE A CE2 1 ATOM 271 C CZ . PHE A 1 35 ? 6.424 -16.848 16.371 1.00 29.96 ? 66 PHE A CZ 1 ATOM 272 N N . THR A 1 36 ? 8.668 -19.806 19.615 1.00 24.13 ? 67 THR A N 1 ATOM 273 C CA . THR A 1 36 ? 7.486 -20.173 20.399 1.00 24.54 ? 67 THR A CA 1 ATOM 274 C C . THR A 1 36 ? 7.770 -21.063 21.616 1.00 30.41 ? 67 THR A C 1 ATOM 275 O O . THR A 1 36 ? 6.893 -21.173 22.469 1.00 33.41 ? 67 THR A O 1 ATOM 276 C CB . THR A 1 36 ? 6.402 -20.831 19.511 1.00 25.27 ? 67 THR A CB 1 ATOM 277 O OG1 . THR A 1 36 ? 6.844 -22.128 19.098 1.00 27.53 ? 67 THR A OG1 1 ATOM 278 C CG2 . THR A 1 36 ? 5.998 -19.977 18.312 1.00 30.21 ? 67 THR A CG2 1 ATOM 279 N N . HIS A 1 37 ? 8.949 -21.734 21.683 1.00 30.74 ? 68 HIS A N 1 ATOM 280 C CA . HIS A 1 37 ? 9.288 -22.653 22.790 1.00 24.04 ? 68 HIS A CA 1 ATOM 281 C C . HIS A 1 37 ? 9.237 -21.962 24.162 1.00 36.89 ? 68 HIS A C 1 ATOM 282 O O . HIS A 1 37 ? 8.582 -22.472 25.073 1.00 39.86 ? 68 HIS A O 1 ATOM 283 C CB . HIS A 1 37 ? 10.641 -23.355 22.550 1.00 36.00 ? 68 HIS A CB 1 ATOM 284 C CG . HIS A 1 37 ? 10.692 -24.213 21.311 1.00 53.23 ? 68 HIS A CG 1 ATOM 285 N ND1 . HIS A 1 37 ? 11.875 -24.821 20.904 1.00 59.07 ? 68 HIS A ND1 1 ATOM 286 C CD2 . HIS A 1 37 ? 9.714 -24.542 20.431 1.00 51.77 ? 68 HIS A CD2 1 ATOM 287 C CE1 . HIS A 1 37 ? 11.579 -25.486 19.798 1.00 62.96 ? 68 HIS A CE1 1 ATOM 288 N NE2 . HIS A 1 37 ? 10.290 -25.351 19.474 1.00 55.26 ? 68 HIS A NE2 1 ATOM 289 N N . ASP A 1 38 ? 9.879 -20.785 24.290 1.00 19.88 ? 69 ASP A N 1 ATOM 290 C CA . ASP A 1 38 ? 9.822 -19.991 25.525 1.00 15.39 ? 69 ASP A CA 1 ATOM 291 C C . ASP A 1 38 ? 8.715 -18.991 25.229 1.00 14.80 ? 69 ASP A C 1 ATOM 292 O O . ASP A 1 38 ? 8.985 -17.861 24.800 1.00 16.92 ? 69 ASP A O 1 ATOM 293 C CB . ASP A 1 38 ? 11.158 -19.289 25.815 1.00 16.45 ? 69 ASP A CB 1 ATOM 294 C CG . ASP A 1 38 ? 11.216 -18.535 27.150 1.00 32.24 ? 69 ASP A CG 1 ATOM 295 O OD1 . ASP A 1 38 ? 10.137 -18.195 27.700 1.00 23.36 ? 69 ASP A OD1 1 ATOM 296 O OD2 . ASP A 1 38 ? 12.327 -18.255 27.619 1.00 27.63 ? 69 ASP A OD2 1 ATOM 297 N N . PHE A 1 39 ? 7.467 -19.432 25.400 1.00 13.44 ? 70 PHE A N 1 ATOM 298 C CA . PHE A 1 39 ? 6.310 -18.606 25.063 1.00 17.79 ? 70 PHE A CA 1 ATOM 299 C C . PHE A 1 39 ? 6.181 -17.289 25.817 1.00 21.78 ? 70 PHE A C 1 ATOM 300 O O . PHE A 1 39 ? 5.800 -16.285 25.207 1.00 15.28 ? 70 PHE A O 1 ATOM 301 C CB . PHE A 1 39 ? 5.000 -19.397 25.062 1.00 24.55 ? 70 PHE A CB 1 ATOM 302 C CG . PHE A 1 39 ? 3.935 -18.699 24.255 1.00 25.49 ? 70 PHE A CG 1 ATOM 303 C CD1 . PHE A 1 39 ? 4.053 -18.580 22.870 1.00 28.28 ? 70 PHE A CD1 1 ATOM 304 C CD2 . PHE A 1 39 ? 2.856 -18.095 24.880 1.00 26.91 ? 70 PHE A CD2 1 ATOM 305 C CE1 . PHE A 1 39 ? 3.079 -17.912 22.126 1.00 37.45 ? 70 PHE A CE1 1 ATOM 306 C CE2 . PHE A 1 39 ? 1.883 -17.433 24.131 1.00 28.57 ? 70 PHE A CE2 1 ATOM 307 C CZ . PHE A 1 39 ? 2.008 -17.335 22.763 1.00 30.39 ? 70 PHE A CZ 1 ATOM 308 N N . ARG A 1 40 ? 6.503 -17.275 27.123 1.00 14.90 ? 71 ARG A N 1 ATOM 309 C CA . ARG A 1 40 ? 6.402 -16.017 27.899 1.00 15.08 ? 71 ARG A CA 1 ATOM 310 C C . ARG A 1 40 ? 7.358 -14.961 27.383 1.00 17.20 ? 71 ARG A C 1 ATOM 311 O O . ARG A 1 40 ? 7.012 -13.778 27.357 1.00 16.37 ? 71 ARG A O 1 ATOM 312 C CB . ARG A 1 40 ? 6.596 -16.259 29.395 1.00 15.58 ? 71 ARG A CB 1 ATOM 313 C CG . ARG A 1 40 ? 5.379 -16.950 29.996 1.00 18.50 ? 71 ARG A CG 1 ATOM 314 C CD . ARG A 1 40 ? 5.620 -17.406 31.415 1.00 20.11 ? 71 ARG A CD 1 ATOM 315 N NE . ARG A 1 40 ? 6.473 -18.592 31.458 1.00 18.96 ? 71 ARG A NE 1 ATOM 316 C CZ . ARG A 1 40 ? 6.702 -19.295 32.557 1.00 25.41 ? 71 ARG A CZ 1 ATOM 317 N NH1 . ARG A 1 40 ? 6.103 -18.972 33.695 1.00 15.55 ? 71 ARG A NH1 1 ATOM 318 N NH2 . ARG A 1 40 ? 7.511 -20.343 32.522 1.00 16.97 ? 71 ARG A NH2 1 HETATM 319 N N . MLY A 1 41 ? 8.540 -15.389 26.933 1.00 14.43 ? 72 MLY A N 1 HETATM 320 C CA . MLY A 1 41 ? 9.519 -14.459 26.353 1.00 23.10 ? 72 MLY A CA 1 HETATM 321 C CB . MLY A 1 41 ? 10.896 -15.123 26.267 1.00 21.52 ? 72 MLY A CB 1 HETATM 322 C CG . MLY A 1 41 ? 11.839 -14.295 25.419 1.00 31.05 ? 72 MLY A CG 1 HETATM 323 C CD . MLY A 1 41 ? 13.279 -14.605 25.802 1.00 42.85 ? 72 MLY A CD 1 HETATM 324 C CE . MLY A 1 41 ? 14.165 -13.363 25.540 1.00 74.06 ? 72 MLY A CE 1 HETATM 325 N NZ . MLY A 1 41 ? 13.543 -12.377 24.617 1.00 83.52 ? 72 MLY A NZ 1 HETATM 326 C CH1 . MLY A 1 41 ? 13.839 -12.786 23.216 1.00 79.38 ? 72 MLY A CH1 1 HETATM 327 C CH2 . MLY A 1 41 ? 14.105 -11.034 24.889 1.00 68.98 ? 72 MLY A CH2 1 HETATM 328 C C . MLY A 1 41 ? 8.995 -13.963 24.984 1.00 29.61 ? 72 MLY A C 1 HETATM 329 O O . MLY A 1 41 ? 9.119 -12.776 24.685 1.00 23.52 ? 72 MLY A O 1 ATOM 330 N N . ALA A 1 42 ? 8.383 -14.860 24.185 1.00 20.86 ? 73 ALA A N 1 ATOM 331 C CA . ALA A 1 42 ? 7.797 -14.506 22.889 1.00 21.19 ? 73 ALA A CA 1 ATOM 332 C C . ALA A 1 42 ? 6.643 -13.513 23.077 1.00 25.41 ? 73 ALA A C 1 ATOM 333 O O . ALA A 1 42 ? 6.577 -12.548 22.324 1.00 22.49 ? 73 ALA A O 1 ATOM 334 C CB . ALA A 1 42 ? 7.301 -15.753 22.168 1.00 15.55 ? 73 ALA A CB 1 ATOM 335 N N . GLN A 1 43 ? 5.759 -13.737 24.087 1.00 18.24 ? 74 GLN A N 1 ATOM 336 C CA . GLN A 1 43 ? 4.611 -12.870 24.397 1.00 20.09 ? 74 GLN A CA 1 ATOM 337 C C . GLN A 1 43 ? 5.016 -11.465 24.765 1.00 32.14 ? 74 GLN A C 1 ATOM 338 O O . GLN A 1 43 ? 4.321 -10.511 24.401 1.00 29.76 ? 74 GLN A O 1 ATOM 339 C CB . GLN A 1 43 ? 3.776 -13.435 25.535 1.00 20.86 ? 74 GLN A CB 1 ATOM 340 C CG . GLN A 1 43 ? 2.714 -14.386 25.067 1.00 33.41 ? 74 GLN A CG 1 ATOM 341 C CD . GLN A 1 43 ? 1.783 -14.817 26.168 1.00 55.02 ? 74 GLN A CD 1 ATOM 342 O OE1 . GLN A 1 43 ? 0.564 -14.717 26.035 1.00 66.63 ? 74 GLN A OE1 1 ATOM 343 N NE2 . GLN A 1 43 ? 2.320 -15.389 27.244 1.00 79.27 ? 74 GLN A NE2 1 ATOM 344 N N . GLN A 1 44 ? 6.130 -11.319 25.500 1.00 35.93 ? 75 GLN A N 1 ATOM 345 C CA . GLN A 1 44 ? 6.586 -9.988 25.898 1.00 35.47 ? 75 GLN A CA 1 ATOM 346 C C . GLN A 1 44 ? 7.173 -9.152 24.739 1.00 29.48 ? 75 GLN A C 1 ATOM 347 O O . GLN A 1 44 ? 7.274 -7.935 24.857 1.00 47.48 ? 75 GLN A O 1 ATOM 348 C CB . GLN A 1 44 ? 7.412 -10.018 27.205 1.00 39.37 ? 75 GLN A CB 1 ATOM 349 C CG . GLN A 1 44 ? 6.617 -10.554 28.416 1.00 27.92 ? 75 GLN A CG 1 ATOM 350 C CD . GLN A 1 44 ? 5.435 -9.702 28.864 1.00 44.67 ? 75 GLN A CD 1 ATOM 351 O OE1 . GLN A 1 44 ? 5.584 -8.580 29.348 1.00 37.99 ? 75 GLN A OE1 1 ATOM 352 N NE2 . GLN A 1 44 ? 4.222 -10.240 28.766 1.00 39.74 ? 75 GLN A NE2 1 ATOM 353 N N . ARG A 1 45 ? 7.453 -9.797 23.591 1.00 29.87 ? 76 ARG A N 1 ATOM 354 C CA . ARG A 1 45 ? 7.885 -9.187 22.336 1.00 26.03 ? 76 ARG A CA 1 ATOM 355 C C . ARG A 1 45 ? 6.678 -8.948 21.376 1.00 43.81 ? 76 ARG A C 1 ATOM 356 O O . ARG A 1 45 ? 6.877 -8.454 20.264 1.00 40.42 ? 76 ARG A O 1 ATOM 357 C CB . ARG A 1 45 ? 8.911 -10.075 21.618 1.00 33.06 ? 76 ARG A CB 1 ATOM 358 C CG . ARG A 1 45 ? 10.320 -10.008 22.182 1.00 66.41 ? 76 ARG A CG 1 ATOM 359 C CD . ARG A 1 45 ? 11.334 -10.586 21.206 1.00 78.79 ? 76 ARG A CD 1 ATOM 360 N NE . ARG A 1 45 ? 11.707 -9.625 20.162 1.00 94.43 ? 76 ARG A NE 1 ATOM 361 C CZ . ARG A 1 45 ? 11.262 -9.657 18.908 1.00 92.32 ? 76 ARG A CZ 1 ATOM 362 N NH1 . ARG A 1 45 ? 10.423 -10.609 18.517 1.00 80.22 ? 76 ARG A NH1 1 ATOM 363 N NH2 . ARG A 1 45 ? 11.657 -8.739 18.035 1.00 72.30 ? 76 ARG A NH2 1 ATOM 364 N N . MET A 1 46 ? 5.450 -9.334 21.785 1.00 30.53 ? 77 MET A N 1 ATOM 365 C CA . MET A 1 46 ? 4.235 -9.174 20.980 1.00 20.31 ? 77 MET A CA 1 ATOM 366 C C . MET A 1 46 ? 3.516 -7.892 21.419 1.00 22.24 ? 77 MET A C 1 ATOM 367 O O . MET A 1 46 ? 2.929 -7.882 22.494 1.00 35.23 ? 77 MET A O 1 ATOM 368 C CB . MET A 1 46 ? 3.288 -10.387 21.168 1.00 20.12 ? 77 MET A CB 1 ATOM 369 C CG . MET A 1 46 ? 3.668 -11.600 20.373 1.00 30.47 ? 77 MET A CG 1 ATOM 370 S SD . MET A 1 46 ? 2.510 -12.958 20.730 1.00 31.34 ? 77 MET A SD 1 ATOM 371 C CE . MET A 1 46 ? 3.567 -14.357 20.451 1.00 27.26 ? 77 MET A CE 1 ATOM 372 N N . PRO A 1 47 ? 3.536 -6.784 20.647 1.00 40.53 ? 78 PRO A N 1 ATOM 373 C CA . PRO A 1 47 ? 2.816 -5.582 21.111 1.00 32.44 ? 78 PRO A CA 1 ATOM 374 C C . PRO A 1 47 ? 1.304 -5.726 20.889 1.00 22.18 ? 78 PRO A C 1 ATOM 375 O O . PRO A 1 47 ? 0.894 -6.572 20.103 1.00 25.62 ? 78 PRO A O 1 ATOM 376 C CB . PRO A 1 47 ? 3.418 -4.460 20.260 1.00 29.63 ? 78 PRO A CB 1 ATOM 377 C CG . PRO A 1 47 ? 3.800 -5.134 18.979 1.00 45.56 ? 78 PRO A CG 1 ATOM 378 C CD . PRO A 1 47 ? 4.176 -6.565 19.333 1.00 56.59 ? 78 PRO A CD 1 ATOM 379 N N . ALA A 1 48 ? 0.493 -4.926 21.598 1.00 25.18 ? 79 ALA A N 1 ATOM 380 C CA . ALA A 1 48 ? -0.962 -4.902 21.443 1.00 23.56 ? 79 ALA A CA 1 ATOM 381 C C . ALA A 1 48 ? -1.282 -4.538 20.001 1.00 37.71 ? 79 ALA A C 1 ATOM 382 O O . ALA A 1 48 ? -0.675 -3.585 19.469 1.00 27.06 ? 79 ALA A O 1 ATOM 383 C CB . ALA A 1 48 ? -1.575 -3.885 22.387 1.00 25.21 ? 79 ALA A CB 1 ATOM 384 N N . ILE A 1 49 ? -2.177 -5.341 19.336 1.00 19.40 ? 80 ILE A N 1 ATOM 385 C CA . ILE A 1 49 ? -2.604 -5.142 17.932 1.00 17.15 ? 80 ILE A CA 1 ATOM 386 C C . ILE A 1 49 ? -3.104 -3.691 17.785 1.00 18.44 ? 80 ILE A C 1 ATOM 387 O O . ILE A 1 49 ? -3.939 -3.275 18.576 1.00 19.57 ? 80 ILE A O 1 ATOM 388 C CB . ILE A 1 49 ? -3.683 -6.184 17.487 1.00 14.03 ? 80 ILE A CB 1 ATOM 389 C CG1 . ILE A 1 49 ? -3.125 -7.618 17.573 1.00 19.76 ? 80 ILE A CG1 1 ATOM 390 C CG2 . ILE A 1 49 ? -4.194 -5.898 16.071 1.00 15.61 ? 80 ILE A CG2 1 ATOM 391 C CD1 . ILE A 1 49 ? -4.204 -8.662 17.899 1.00 27.86 ? 80 ILE A CD1 1 ATOM 392 N N . PRO A 1 50 ? -2.542 -2.890 16.853 1.00 19.67 ? 81 PRO A N 1 ATOM 393 C CA . PRO A 1 50 ? -2.949 -1.477 16.764 1.00 17.07 ? 81 PRO A CA 1 ATOM 394 C C . PRO A 1 50 ? -4.377 -1.197 16.311 1.00 20.12 ? 81 PRO A C 1 ATOM 395 O O . PRO A 1 50 ? -5.047 -2.047 15.729 1.00 19.49 ? 81 PRO A O 1 ATOM 396 C CB . PRO A 1 50 ? -1.899 -0.846 15.841 1.00 21.31 ? 81 PRO A CB 1 ATOM 397 C CG . PRO A 1 50 ? -1.337 -1.945 15.069 1.00 32.38 ? 81 PRO A CG 1 ATOM 398 C CD . PRO A 1 50 ? -1.505 -3.226 15.852 1.00 28.80 ? 81 PRO A CD 1 ATOM 399 N N . VAL A 1 51 ? -4.833 0.028 16.578 1.00 18.08 ? 82 VAL A N 1 ATOM 400 C CA . VAL A 1 51 ? -6.183 0.505 16.237 1.00 16.42 ? 82 VAL A CA 1 ATOM 401 C C . VAL A 1 51 ? -6.559 0.385 14.742 1.00 24.82 ? 82 VAL A C 1 ATOM 402 O O . VAL A 1 51 ? -7.727 0.187 14.439 1.00 30.30 ? 82 VAL A O 1 ATOM 403 C CB . VAL A 1 51 ? -6.430 1.952 16.755 1.00 17.97 ? 82 VAL A CB 1 ATOM 404 C CG1 . VAL A 1 51 ? -6.397 2.016 18.276 1.00 21.11 ? 82 VAL A CG1 1 ATOM 405 C CG2 . VAL A 1 51 ? -5.439 2.946 16.141 1.00 30.62 ? 82 VAL A CG2 1 ATOM 406 N N . ASN A 1 52 ? -5.592 0.533 13.825 1.00 22.79 ? 83 ASN A N 1 ATOM 407 C CA . ASN A 1 52 ? -5.834 0.490 12.376 1.00 26.35 ? 83 ASN A CA 1 ATOM 408 C C . ASN A 1 52 ? -6.040 -0.930 11.826 1.00 23.40 ? 83 ASN A C 1 ATOM 409 O O . ASN A 1 52 ? -6.410 -1.089 10.662 1.00 32.02 ? 83 ASN A O 1 ATOM 410 C CB . ASN A 1 52 ? -4.691 1.194 11.620 1.00 27.85 ? 83 ASN A CB 1 ATOM 411 C CG . ASN A 1 52 ? -3.342 0.571 11.836 1.00 30.94 ? 83 ASN A CG 1 ATOM 412 O OD1 . ASN A 1 52 ? -2.800 0.577 12.936 1.00 36.03 ? 83 ASN A OD1 1 ATOM 413 N ND2 . ASN A 1 52 ? -2.766 0.022 10.783 1.00 40.40 ? 83 ASN A ND2 1 ATOM 414 N N . ILE A 1 53 ? -5.750 -1.949 12.637 1.00 23.47 ? 84 ILE A N 1 ATOM 415 C CA . ILE A 1 53 ? -5.890 -3.357 12.231 1.00 15.74 ? 84 ILE A CA 1 ATOM 416 C C . ILE A 1 53 ? -7.174 -3.918 12.864 1.00 24.39 ? 84 ILE A C 1 ATOM 417 O O . ILE A 1 53 ? -7.234 -4.019 14.078 1.00 30.05 ? 84 ILE A O 1 ATOM 418 C CB . ILE A 1 53 ? -4.596 -4.153 12.591 1.00 20.49 ? 84 ILE A CB 1 ATOM 419 C CG1 . ILE A 1 53 ? -3.390 -3.619 11.751 1.00 31.02 ? 84 ILE A CG1 1 ATOM 420 C CG2 . ILE A 1 53 ? -4.781 -5.669 12.385 1.00 23.52 ? 84 ILE A CG2 1 ATOM 421 C CD1 . ILE A 1 53 ? -2.018 -4.162 12.090 1.00 40.24 ? 84 ILE A CD1 1 ATOM 422 N N . HIS A 1 54 ? -8.179 -4.287 12.048 1.00 16.65 ? 85 HIS A N 1 ATOM 423 C CA . HIS A 1 54 ? -9.453 -4.832 12.530 1.00 19.91 ? 85 HIS A CA 1 ATOM 424 C C . HIS A 1 54 ? -9.487 -6.375 12.454 1.00 18.79 ? 85 HIS A C 1 ATOM 425 O O . HIS A 1 54 ? -10.362 -7.002 13.044 1.00 15.42 ? 85 HIS A O 1 ATOM 426 C CB . HIS A 1 54 ? -10.648 -4.237 11.744 1.00 20.81 ? 85 HIS A CB 1 ATOM 427 C CG . HIS A 1 54 ? -10.661 -2.735 11.682 1.00 40.48 ? 85 HIS A CG 1 ATOM 428 N ND1 . HIS A 1 54 ? -10.738 -1.960 12.830 1.00 44.74 ? 85 HIS A ND1 1 ATOM 429 C CD2 . HIS A 1 54 ? -10.598 -1.915 10.610 1.00 52.04 ? 85 HIS A CD2 1 ATOM 430 C CE1 . HIS A 1 54 ? -10.712 -0.701 12.421 1.00 31.69 ? 85 HIS A CE1 1 ATOM 431 N NE2 . HIS A 1 54 ? -10.647 -0.623 11.093 1.00 44.79 ? 85 HIS A NE2 1 ATOM 432 N N . SER A 1 55 ? -8.542 -6.973 11.711 1.00 17.30 ? 86 SER A N 1 ATOM 433 C CA . SER A 1 55 ? -8.449 -8.418 11.526 1.00 16.95 ? 86 SER A CA 1 ATOM 434 C C . SER A 1 55 ? -7.059 -8.790 11.052 1.00 24.45 ? 86 SER A C 1 ATOM 435 O O . SER A 1 55 ? -6.316 -7.927 10.567 1.00 21.95 ? 86 SER A O 1 ATOM 436 C CB . SER A 1 55 ? -9.498 -8.915 10.527 1.00 19.67 ? 86 SER A CB 1 ATOM 437 O OG . SER A 1 55 ? -9.276 -8.351 9.248 1.00 27.68 ? 86 SER A OG 1 ATOM 438 N N . MET A 1 56 ? -6.714 -10.067 11.177 1.00 16.38 ? 87 MET A N 1 ATOM 439 C CA . MET A 1 56 ? -5.392 -10.561 10.799 1.00 16.10 ? 87 MET A CA 1 ATOM 440 C C . MET A 1 56 ? -5.528 -11.854 9.980 1.00 13.81 ? 87 MET A C 1 ATOM 441 O O . MET A 1 56 ? -6.314 -12.718 10.346 1.00 14.52 ? 87 MET A O 1 ATOM 442 C CB . MET A 1 56 ? -4.631 -10.862 12.078 1.00 19.10 ? 87 MET A CB 1 ATOM 443 C CG . MET A 1 56 ? -3.187 -11.119 11.886 1.00 31.35 ? 87 MET A CG 1 ATOM 444 S SD . MET A 1 56 ? -2.559 -11.238 13.543 1.00 33.83 ? 87 MET A SD 1 ATOM 445 C CE . MET A 1 56 ? -1.010 -11.905 13.209 1.00 40.46 ? 87 MET A CE 1 ATOM 446 N N . ASN A 1 57 ? -4.704 -12.003 8.937 1.00 14.95 ? 88 ASN A N 1 ATOM 447 C CA . ASN A 1 57 ? -4.734 -13.178 8.072 1.00 12.86 ? 88 ASN A CA 1 ATOM 448 C C . ASN A 1 57 ? -3.645 -14.153 8.432 1.00 12.82 ? 88 ASN A C 1 ATOM 449 O O . ASN A 1 57 ? -2.475 -13.778 8.422 1.00 14.61 ? 88 ASN A O 1 ATOM 450 C CB . ASN A 1 57 ? -4.507 -12.757 6.625 1.00 15.68 ? 88 ASN A CB 1 ATOM 451 C CG . ASN A 1 57 ? -5.647 -12.039 5.968 1.00 21.62 ? 88 ASN A CG 1 ATOM 452 O OD1 . ASN A 1 57 ? -6.778 -11.990 6.458 1.00 21.23 ? 88 ASN A OD1 1 ATOM 453 N ND2 . ASN A 1 57 ? -5.355 -11.456 4.834 1.00 29.25 ? 88 ASN A ND2 1 ATOM 454 N N . PHE A 1 58 ? -4.012 -15.414 8.695 1.00 9.33 ? 89 PHE A N 1 ATOM 455 C CA . PHE A 1 58 ? -3.059 -16.498 8.918 1.00 8.21 ? 89 PHE A CA 1 ATOM 456 C C . PHE A 1 58 ? -3.209 -17.435 7.732 1.00 14.69 ? 89 PHE A C 1 ATOM 457 O O . PHE A 1 58 ? -4.308 -17.561 7.201 1.00 12.83 ? 89 PHE A O 1 ATOM 458 C CB . PHE A 1 58 ? -3.363 -17.301 10.207 1.00 11.67 ? 89 PHE A CB 1 ATOM 459 C CG . PHE A 1 58 ? -3.016 -16.557 11.473 1.00 11.50 ? 89 PHE A CG 1 ATOM 460 C CD1 . PHE A 1 58 ? -3.922 -15.674 12.047 1.00 19.76 ? 89 PHE A CD1 1 ATOM 461 C CD2 . PHE A 1 58 ? -1.781 -16.740 12.089 1.00 15.35 ? 89 PHE A CD2 1 ATOM 462 C CE1 . PHE A 1 58 ? -3.585 -14.953 13.203 1.00 19.91 ? 89 PHE A CE1 1 ATOM 463 C CE2 . PHE A 1 58 ? -1.458 -16.059 13.267 1.00 17.77 ? 89 PHE A CE2 1 ATOM 464 C CZ . PHE A 1 58 ? -2.366 -15.178 13.820 1.00 19.05 ? 89 PHE A CZ 1 ATOM 465 N N . THR A 1 59 ? -2.132 -18.084 7.325 1.00 9.93 ? 90 THR A N 1 ATOM 466 C CA . THR A 1 59 ? -2.182 -19.034 6.225 1.00 9.03 ? 90 THR A CA 1 ATOM 467 C C . THR A 1 59 ? -1.812 -20.423 6.753 1.00 15.38 ? 90 THR A C 1 ATOM 468 O O . THR A 1 59 ? -0.826 -20.572 7.489 1.00 11.20 ? 90 THR A O 1 ATOM 469 C CB . THR A 1 59 ? -1.292 -18.583 5.046 1.00 11.40 ? 90 THR A CB 1 ATOM 470 O OG1 . THR A 1 59 ? -1.674 -17.255 4.671 1.00 15.15 ? 90 THR A OG1 1 ATOM 471 C CG2 . THR A 1 59 ? -1.451 -19.492 3.824 1.00 12.48 ? 90 THR A CG2 1 ATOM 472 N N . TRP A 1 60 ? -2.585 -21.442 6.358 1.00 10.16 ? 91 TRP A N 1 ATOM 473 C CA . TRP A 1 60 ? -2.251 -22.793 6.783 1.00 7.93 ? 91 TRP A CA 1 ATOM 474 C C . TRP A 1 60 ? -2.432 -23.778 5.671 1.00 11.42 ? 91 TRP A C 1 ATOM 475 O O . TRP A 1 60 ? -3.196 -23.519 4.727 1.00 9.50 ? 91 TRP A O 1 ATOM 476 C CB . TRP A 1 60 ? -3.028 -23.251 8.057 1.00 14.06 ? 91 TRP A CB 1 ATOM 477 C CG . TRP A 1 60 ? -4.535 -23.293 8.016 1.00 12.33 ? 91 TRP A CG 1 ATOM 478 C CD1 . TRP A 1 60 ? -5.353 -23.118 6.935 1.00 13.73 ? 91 TRP A CD1 1 ATOM 479 C CD2 . TRP A 1 60 ? -5.402 -23.473 9.149 1.00 14.63 ? 91 TRP A CD2 1 ATOM 480 N NE1 . TRP A 1 60 ? -6.676 -23.183 7.326 1.00 17.24 ? 91 TRP A NE1 1 ATOM 481 C CE2 . TRP A 1 60 ? -6.731 -23.408 8.680 1.00 14.08 ? 91 TRP A CE2 1 ATOM 482 C CE3 . TRP A 1 60 ? -5.178 -23.679 10.524 1.00 24.49 ? 91 TRP A CE3 1 ATOM 483 C CZ2 . TRP A 1 60 ? -7.841 -23.545 9.541 1.00 22.20 ? 91 TRP A CZ2 1 ATOM 484 C CZ3 . TRP A 1 60 ? -6.280 -23.795 11.379 1.00 24.03 ? 91 TRP A CZ3 1 ATOM 485 C CH2 . TRP A 1 60 ? -7.588 -23.714 10.882 1.00 18.16 ? 91 TRP A CH2 1 ATOM 486 N N . GLN A 1 61 ? -1.770 -24.912 5.819 1.00 10.46 ? 92 GLN A N 1 ATOM 487 C CA . GLN A 1 61 ? -1.882 -26.056 4.934 1.00 7.10 ? 92 GLN A CA 1 ATOM 488 C C . GLN A 1 61 ? -1.419 -27.360 5.540 1.00 8.88 ? 92 GLN A C 1 ATOM 489 O O . GLN A 1 61 ? -0.493 -27.383 6.356 1.00 13.44 ? 92 GLN A O 1 ATOM 490 C CB . GLN A 1 61 ? -1.212 -25.795 3.578 1.00 15.12 ? 92 GLN A CB 1 ATOM 491 C CG . GLN A 1 61 ? 0.281 -25.865 3.534 1.00 31.83 ? 92 GLN A CG 1 ATOM 492 C CD . GLN A 1 61 ? 0.598 -25.934 2.070 1.00 31.22 ? 92 GLN A CD 1 ATOM 493 O OE1 . GLN A 1 61 ? 1.306 -25.106 1.562 1.00 16.92 ? 92 GLN A OE1 1 ATOM 494 N NE2 . GLN A 1 61 ? -0.097 -26.800 1.334 1.00 45.11 ? 92 GLN A NE2 1 ATOM 495 N N . ALA A 1 62 ? -2.028 -28.458 5.080 1.00 13.69 ? 93 ALA A N 1 ATOM 496 C CA . ALA A 1 62 ? -1.692 -29.834 5.461 1.00 16.17 ? 93 ALA A CA 1 ATOM 497 C C . ALA A 1 62 ? -1.270 -30.364 4.101 1.00 23.00 ? 93 ALA A C 1 ATOM 498 O O . ALA A 1 62 ? -2.077 -30.833 3.312 1.00 25.30 ? 93 ALA A O 1 ATOM 499 C CB . ALA A 1 62 ? -2.941 -30.548 5.975 1.00 21.32 ? 93 ALA A CB 1 ATOM 500 N N . ALA A 1 63 ? -0.006 -30.139 3.812 1.00 25.52 ? 94 ALA A N 1 ATOM 501 C CA . ALA A 1 63 ? 0.705 -30.284 2.562 1.00 22.54 ? 94 ALA A CA 1 ATOM 502 C C . ALA A 1 63 ? 0.976 -31.675 2.012 1.00 30.95 ? 94 ALA A C 1 ATOM 503 O O . ALA A 1 63 ? 1.512 -31.765 0.903 1.00 35.35 ? 94 ALA A O 1 ATOM 504 C CB . ALA A 1 63 ? 2.000 -29.472 2.640 1.00 29.39 ? 94 ALA A CB 1 ATOM 505 N N . GLY A 1 64 ? 0.665 -32.725 2.786 1.00 22.75 ? 95 GLY A N 1 ATOM 506 C CA . GLY A 1 64 ? 0.887 -34.114 2.388 1.00 39.46 ? 95 GLY A CA 1 ATOM 507 C C . GLY A 1 64 ? -0.403 -34.865 2.111 1.00 42.69 ? 95 GLY A C 1 ATOM 508 O O . GLY A 1 64 ? -1.386 -34.241 1.714 1.00 44.49 ? 95 GLY A O 1 ATOM 509 N N . GLN A 1 65 ? -0.416 -36.209 2.324 1.00 32.40 ? 96 GLN A N 1 ATOM 510 C CA . GLN A 1 65 ? -1.599 -37.072 2.127 1.00 24.88 ? 96 GLN A CA 1 ATOM 511 C C . GLN A 1 65 ? -2.361 -37.332 3.443 1.00 29.11 ? 96 GLN A C 1 ATOM 512 O O . GLN A 1 65 ? -3.534 -37.718 3.413 1.00 29.67 ? 96 GLN A O 1 ATOM 513 C CB . GLN A 1 65 ? -1.221 -38.418 1.463 1.00 36.09 ? 96 GLN A CB 1 ATOM 514 C CG . GLN A 1 65 ? -2.423 -39.146 0.839 1.00 41.07 ? 96 GLN A CG 1 ATOM 515 C CD . GLN A 1 65 ? -2.063 -40.456 0.182 1.00 78.64 ? 96 GLN A CD 1 ATOM 516 O OE1 . GLN A 1 65 ? -1.399 -40.501 -0.861 1.00 84.73 ? 96 GLN A OE1 1 ATOM 517 N NE2 . GLN A 1 65 ? -2.556 -41.555 0.743 1.00 72.98 ? 96 GLN A NE2 1 ATOM 518 N N . ALA A 1 66 ? -1.699 -37.130 4.587 1.00 35.39 ? 97 ALA A N 1 ATOM 519 C CA . ALA A 1 66 ? -2.317 -37.323 5.904 1.00 31.72 ? 97 ALA A CA 1 ATOM 520 C C . ALA A 1 66 ? -3.392 -36.246 6.141 1.00 25.40 ? 97 ALA A C 1 ATOM 521 O O . ALA A 1 66 ? -3.235 -35.120 5.667 1.00 26.40 ? 97 ALA A O 1 ATOM 522 C CB . ALA A 1 66 ? -1.251 -37.252 6.982 1.00 34.22 ? 97 ALA A CB 1 ATOM 523 N N . GLU A 1 67 ? -4.501 -36.605 6.817 1.00 23.80 ? 98 GLU A N 1 ATOM 524 C CA . GLU A 1 67 ? -5.580 -35.662 7.120 1.00 24.08 ? 98 GLU A CA 1 ATOM 525 C C . GLU A 1 67 ? -5.414 -35.139 8.530 1.00 16.59 ? 98 GLU A C 1 ATOM 526 O O . GLU A 1 67 ? -5.093 -35.904 9.442 1.00 19.67 ? 98 GLU A O 1 ATOM 527 C CB . GLU A 1 67 ? -6.981 -36.302 6.980 1.00 22.47 ? 98 GLU A CB 1 ATOM 528 C CG . GLU A 1 67 ? -7.395 -36.712 5.577 1.00 34.86 ? 98 GLU A CG 1 ATOM 529 C CD . GLU A 1 67 ? -7.433 -35.621 4.523 1.00 59.19 ? 98 GLU A CD 1 ATOM 530 O OE1 . GLU A 1 67 ? -8.018 -34.541 4.780 1.00 38.89 ? 98 GLU A OE1 1 ATOM 531 O OE2 . GLU A 1 67 ? -6.879 -35.859 3.426 1.00 40.48 ? 98 GLU A OE2 1 ATOM 532 N N . TYR A 1 68 ? -5.665 -33.847 8.714 1.00 12.74 ? 99 TYR A N 1 ATOM 533 C CA . TYR A 1 68 ? -5.580 -33.213 10.025 1.00 10.00 ? 99 TYR A CA 1 ATOM 534 C C . TYR A 1 68 ? -6.832 -32.417 10.251 1.00 12.76 ? 99 TYR A C 1 ATOM 535 O O . TYR A 1 68 ? -7.454 -31.934 9.289 1.00 14.32 ? 99 TYR A O 1 ATOM 536 C CB . TYR A 1 68 ? -4.319 -32.324 10.149 1.00 10.61 ? 99 TYR A CB 1 ATOM 537 C CG . TYR A 1 68 ? -3.025 -33.107 10.058 1.00 18.98 ? 99 TYR A CG 1 ATOM 538 C CD1 . TYR A 1 68 ? -2.519 -33.788 11.163 1.00 17.18 ? 99 TYR A CD1 1 ATOM 539 C CD2 . TYR A 1 68 ? -2.293 -33.147 8.874 1.00 26.04 ? 99 TYR A CD2 1 ATOM 540 C CE1 . TYR A 1 68 ? -1.336 -34.517 11.082 1.00 21.28 ? 99 TYR A CE1 1 ATOM 541 C CE2 . TYR A 1 68 ? -1.085 -33.839 8.794 1.00 28.78 ? 99 TYR A CE2 1 ATOM 542 C CZ . TYR A 1 68 ? -0.616 -34.530 9.901 1.00 31.30 ? 99 TYR A CZ 1 ATOM 543 O OH . TYR A 1 68 ? 0.557 -35.236 9.838 1.00 32.46 ? 99 TYR A OH 1 ATOM 544 N N . PHE A 1 69 ? -7.227 -32.303 11.522 1.00 9.67 ? 100 PHE A N 1 ATOM 545 C CA . PHE A 1 69 ? -8.478 -31.638 11.917 1.00 10.25 ? 100 PHE A CA 1 ATOM 546 C C . PHE A 1 69 ? -8.150 -30.562 12.911 1.00 13.76 ? 100 PHE A C 1 ATOM 547 O O . PHE A 1 69 ? -7.408 -30.820 13.851 1.00 14.01 ? 100 PHE A O 1 ATOM 548 C CB . PHE A 1 69 ? -9.445 -32.681 12.560 1.00 10.92 ? 100 PHE A CB 1 ATOM 549 C CG . PHE A 1 69 ? -9.726 -33.820 11.600 1.00 10.08 ? 100 PHE A CG 1 ATOM 550 C CD1 . PHE A 1 69 ? -8.844 -34.890 11.488 1.00 11.84 ? 100 PHE A CD1 1 ATOM 551 C CD2 . PHE A 1 69 ? -10.823 -33.775 10.747 1.00 13.36 ? 100 PHE A CD2 1 ATOM 552 C CE1 . PHE A 1 69 ? -9.055 -35.909 10.541 1.00 12.34 ? 100 PHE A CE1 1 ATOM 553 C CE2 . PHE A 1 69 ? -11.021 -34.788 9.781 1.00 16.20 ? 100 PHE A CE2 1 ATOM 554 C CZ . PHE A 1 69 ? -10.123 -35.832 9.686 1.00 15.43 ? 100 PHE A CZ 1 ATOM 555 N N . TYR A 1 70 ? -8.725 -29.394 12.745 1.00 11.21 ? 101 TYR A N 1 ATOM 556 C CA . TYR A 1 70 ? -8.512 -28.306 13.691 1.00 9.17 ? 101 TYR A CA 1 ATOM 557 C C . TYR A 1 70 ? -9.788 -28.066 14.480 1.00 12.11 ? 101 TYR A C 1 ATOM 558 O O . TYR A 1 70 ? -10.886 -28.384 14.012 1.00 10.97 ? 101 TYR A O 1 ATOM 559 C CB . TYR A 1 70 ? -8.067 -27.014 12.947 1.00 10.39 ? 101 TYR A CB 1 ATOM 560 C CG . TYR A 1 70 ? -9.193 -26.375 12.158 1.00 11.49 ? 101 TYR A CG 1 ATOM 561 C CD1 . TYR A 1 70 ? -10.117 -25.530 12.778 1.00 13.30 ? 101 TYR A CD1 1 ATOM 562 C CD2 . TYR A 1 70 ? -9.403 -26.704 10.819 1.00 8.87 ? 101 TYR A CD2 1 ATOM 563 C CE1 . TYR A 1 70 ? -11.209 -25.013 12.076 1.00 11.88 ? 101 TYR A CE1 1 ATOM 564 C CE2 . TYR A 1 70 ? -10.469 -26.168 10.104 1.00 13.57 ? 101 TYR A CE2 1 ATOM 565 C CZ . TYR A 1 70 ? -11.372 -25.329 10.731 1.00 14.26 ? 101 TYR A CZ 1 ATOM 566 O OH . TYR A 1 70 ? -12.459 -24.850 10.015 1.00 11.21 ? 101 TYR A OH 1 ATOM 567 N N . GLU A 1 71 ? -9.663 -27.450 15.645 1.00 9.21 ? 102 GLU A N 1 ATOM 568 C CA . GLU A 1 71 ? -10.826 -27.051 16.420 1.00 10.23 ? 102 GLU A CA 1 ATOM 569 C C . GLU A 1 71 ? -10.516 -25.817 17.247 1.00 14.14 ? 102 GLU A C 1 ATOM 570 O O . GLU A 1 71 ? -9.578 -25.843 18.048 1.00 11.44 ? 102 GLU A O 1 ATOM 571 C CB . GLU A 1 71 ? -11.340 -28.184 17.329 1.00 11.92 ? 102 GLU A CB 1 ATOM 572 C CG . GLU A 1 71 ? -12.715 -27.843 17.906 1.00 17.27 ? 102 GLU A CG 1 ATOM 573 C CD . GLU A 1 71 ? -13.379 -28.916 18.753 1.00 32.64 ? 102 GLU A CD 1 ATOM 574 O OE1 . GLU A 1 71 ? -12.785 -30.003 18.919 1.00 24.88 ? 102 GLU A OE1 1 ATOM 575 O OE2 . GLU A 1 71 ? -14.492 -28.661 19.264 1.00 28.90 ? 102 GLU A OE2 1 ATOM 576 N N . PHE A 1 72 ? -11.348 -24.788 17.112 1.00 9.71 ? 103 PHE A N 1 ATOM 577 C CA . PHE A 1 72 ? -11.268 -23.579 17.933 1.00 10.95 ? 103 PHE A CA 1 ATOM 578 C C . PHE A 1 72 ? -12.054 -23.847 19.217 1.00 15.10 ? 103 PHE A C 1 ATOM 579 O O . PHE A 1 72 ? -13.301 -23.897 19.198 1.00 16.78 ? 103 PHE A O 1 ATOM 580 C CB . PHE A 1 72 ? -11.800 -22.346 17.178 1.00 10.65 ? 103 PHE A CB 1 ATOM 581 C CG . PHE A 1 72 ? -10.839 -21.892 16.096 1.00 13.19 ? 103 PHE A CG 1 ATOM 582 C CD1 . PHE A 1 72 ? -9.806 -21.002 16.387 1.00 14.65 ? 103 PHE A CD1 1 ATOM 583 C CD2 . PHE A 1 72 ? -10.938 -22.391 14.797 1.00 11.23 ? 103 PHE A CD2 1 ATOM 584 C CE1 . PHE A 1 72 ? -8.910 -20.586 15.388 1.00 11.28 ? 103 PHE A CE1 1 ATOM 585 C CE2 . PHE A 1 72 ? -10.039 -21.982 13.798 1.00 16.29 ? 103 PHE A CE2 1 ATOM 586 C CZ . PHE A 1 72 ? -9.029 -21.082 14.101 1.00 15.93 ? 103 PHE A CZ 1 ATOM 587 N N . LEU A 1 73 ? -11.309 -24.060 20.323 1.00 13.92 ? 104 LEU A N 1 ATOM 588 C CA . LEU A 1 73 ? -11.876 -24.377 21.650 1.00 15.05 ? 104 LEU A CA 1 ATOM 589 C C . LEU A 1 73 ? -12.347 -23.164 22.411 1.00 19.90 ? 104 LEU A C 1 ATOM 590 O O . LEU A 1 73 ? -13.313 -23.253 23.172 1.00 22.02 ? 104 LEU A O 1 ATOM 591 C CB . LEU A 1 73 ? -10.869 -25.195 22.492 1.00 13.35 ? 104 LEU A CB 1 ATOM 592 C CG . LEU A 1 73 ? -10.413 -26.550 21.921 1.00 20.46 ? 104 LEU A CG 1 ATOM 593 C CD1 . LEU A 1 73 ? -9.474 -27.256 22.914 1.00 20.22 ? 104 LEU A CD1 1 ATOM 594 C CD2 . LEU A 1 73 ? -11.595 -27.458 21.619 1.00 21.23 ? 104 LEU A CD2 1 ATOM 595 N N . SER A 1 74 ? -11.679 -22.028 22.213 1.00 15.74 ? 105 SER A N 1 ATOM 596 C CA . SER A 1 74 ? -12.053 -20.773 22.867 1.00 17.40 ? 105 SER A CA 1 ATOM 597 C C . SER A 1 74 ? -11.724 -19.602 21.985 1.00 14.93 ? 105 SER A C 1 ATOM 598 O O . SER A 1 74 ? -10.631 -19.524 21.430 1.00 15.08 ? 105 SER A O 1 ATOM 599 C CB . SER A 1 74 ? -11.355 -20.630 24.218 1.00 26.16 ? 105 SER A CB 1 ATOM 600 O OG . SER A 1 74 ? -11.711 -19.414 24.860 1.00 30.69 ? 105 SER A OG 1 ATOM 601 N N . LEU A 1 75 ? -12.697 -18.727 21.812 1.00 14.03 ? 106 LEU A N 1 ATOM 602 C CA . LEU A 1 75 ? -12.604 -17.444 21.091 1.00 12.52 ? 106 LEU A CA 1 ATOM 603 C C . LEU A 1 75 ? -13.284 -16.502 22.070 1.00 18.09 ? 106 LEU A C 1 ATOM 604 O O . LEU A 1 75 ? -14.520 -16.415 22.120 1.00 18.31 ? 106 LEU A O 1 ATOM 605 C CB . LEU A 1 75 ? -13.345 -17.520 19.723 1.00 13.66 ? 106 LEU A CB 1 ATOM 606 C CG . LEU A 1 75 ? -12.602 -18.319 18.636 1.00 10.34 ? 106 LEU A CG 1 ATOM 607 C CD1 . LEU A 1 75 ? -13.505 -18.546 17.404 1.00 13.03 ? 106 LEU A CD1 1 ATOM 608 C CD2 . LEU A 1 75 ? -11.304 -17.604 18.212 1.00 12.47 ? 106 LEU A CD2 1 ATOM 609 N N . ARG A 1 76 ? -12.476 -15.877 22.941 1.00 12.83 ? 107 ARG A N 1 ATOM 610 C CA . ARG A 1 76 ? -13.028 -15.137 24.064 1.00 14.80 ? 107 ARG A CA 1 ATOM 611 C C . ARG A 1 76 ? -12.365 -13.804 24.339 1.00 12.69 ? 107 ARG A C 1 ATOM 612 O O . ARG A 1 76 ? -11.146 -13.761 24.436 1.00 15.25 ? 107 ARG A O 1 ATOM 613 C CB . ARG A 1 76 ? -12.930 -16.051 25.324 1.00 12.64 ? 107 ARG A CB 1 ATOM 614 C CG . ARG A 1 76 ? -13.505 -15.424 26.614 1.00 24.14 ? 107 ARG A CG 1 ATOM 615 C CD . ARG A 1 76 ? -13.609 -16.379 27.801 1.00 26.22 ? 107 ARG A CD 1 ATOM 616 N NE . ARG A 1 76 ? -12.308 -16.771 28.357 1.00 39.71 ? 107 ARG A NE 1 ATOM 617 C CZ . ARG A 1 76 ? -12.097 -17.022 29.649 1.00 56.13 ? 107 ARG A CZ 1 ATOM 618 N NH1 . ARG A 1 76 ? -13.080 -16.877 30.532 1.00 28.81 ? 107 ARG A NH1 1 ATOM 619 N NH2 . ARG A 1 76 ? -10.893 -17.403 30.073 1.00 26.59 ? 107 ARG A NH2 1 ATOM 620 N N . SER A 1 77 ? -13.164 -12.729 24.520 1.00 9.40 ? 108 SER A N 1 ATOM 621 C CA . SER A 1 77 ? -12.622 -11.440 24.929 1.00 10.31 ? 108 SER A CA 1 ATOM 622 C C . SER A 1 77 ? -12.733 -11.412 26.462 1.00 15.77 ? 108 SER A C 1 ATOM 623 O O . SER A 1 77 ? -13.784 -11.754 26.996 1.00 17.23 ? 108 SER A O 1 ATOM 624 C CB . SER A 1 77 ? -13.432 -10.282 24.350 1.00 15.09 ? 108 SER A CB 1 ATOM 625 O OG . SER A 1 77 ? -13.057 -9.056 24.970 1.00 18.82 ? 108 SER A OG 1 ATOM 626 N N . LEU A 1 78 ? -11.668 -10.995 27.165 1.00 13.59 ? 109 LEU A N 1 ATOM 627 C CA . LEU A 1 78 ? -11.689 -10.875 28.627 1.00 12.51 ? 109 LEU A CA 1 ATOM 628 C C . LEU A 1 78 ? -12.092 -9.440 29.059 1.00 24.70 ? 109 LEU A C 1 ATOM 629 O O . LEU A 1 78 ? -12.183 -9.153 30.254 1.00 28.64 ? 109 LEU A O 1 ATOM 630 C CB . LEU A 1 78 ? -10.318 -11.277 29.221 1.00 18.95 ? 109 LEU A CB 1 ATOM 631 C CG . LEU A 1 78 ? -9.869 -12.725 28.951 1.00 22.25 ? 109 LEU A CG 1 ATOM 632 C CD1 . LEU A 1 78 ? -8.374 -12.851 29.053 1.00 30.15 ? 109 LEU A CD1 1 ATOM 633 C CD2 . LEU A 1 78 ? -10.505 -13.684 29.933 1.00 26.60 ? 109 LEU A CD2 1 ATOM 634 N N . ASP A 1 79 ? -12.350 -8.552 28.084 1.00 18.24 ? 110 ASP A N 1 ATOM 635 C CA . ASP A 1 79 ? -12.739 -7.153 28.286 1.00 22.71 ? 110 ASP A CA 1 ATOM 636 C C . ASP A 1 79 ? -13.899 -6.873 27.335 1.00 23.03 ? 110 ASP A C 1 ATOM 637 O O . ASP A 1 79 ? -13.752 -6.163 26.337 1.00 20.44 ? 110 ASP A O 1 ATOM 638 C CB . ASP A 1 79 ? -11.540 -6.222 28.025 1.00 20.44 ? 110 ASP A CB 1 ATOM 639 C CG . ASP A 1 79 ? -10.454 -6.376 29.078 1.00 33.46 ? 110 ASP A CG 1 ATOM 640 O OD1 . ASP A 1 79 ? -10.690 -5.961 30.250 1.00 31.24 ? 110 ASP A OD1 1 ATOM 641 O OD2 . ASP A 1 79 ? -9.393 -6.955 28.752 1.00 26.30 ? 110 ASP A OD2 1 HETATM 642 N N . MLY A 1 80 ? -15.052 -7.494 27.640 1.00 20.63 ? 111 MLY A N 1 HETATM 643 C CA . MLY A 1 80 ? -16.277 -7.457 26.834 1.00 27.72 ? 111 MLY A CA 1 HETATM 644 C CB . MLY A 1 80 ? -17.306 -8.516 27.302 1.00 29.96 ? 111 MLY A CB 1 HETATM 645 C CG . MLY A 1 80 ? -16.725 -9.916 26.955 1.00 49.18 ? 111 MLY A CG 1 HETATM 646 C CD . MLY A 1 80 ? -17.780 -11.000 26.615 1.00 59.75 ? 111 MLY A CD 1 HETATM 647 C CE . MLY A 1 80 ? -17.133 -12.425 26.605 1.00 60.60 ? 111 MLY A CE 1 HETATM 648 N NZ . MLY A 1 80 ? -17.742 -13.310 27.663 1.00 72.55 ? 111 MLY A NZ 1 HETATM 649 C CH1 . MLY A 1 80 ? -17.072 -14.636 27.669 1.00 50.20 ? 111 MLY A CH1 1 HETATM 650 C CH2 . MLY A 1 80 ? -19.197 -13.524 27.393 1.00 62.88 ? 111 MLY A CH2 1 HETATM 651 C C . MLY A 1 80 ? -16.844 -6.071 26.524 1.00 33.96 ? 111 MLY A C 1 HETATM 652 O O . MLY A 1 80 ? -17.533 -5.923 25.513 1.00 29.82 ? 111 MLY A O 1 ATOM 653 N N . GLY A 1 81 ? -16.569 -5.093 27.390 1.00 23.10 ? 112 GLY A N 1 ATOM 654 C CA . GLY A 1 81 ? -17.013 -3.718 27.200 1.00 28.38 ? 112 GLY A CA 1 ATOM 655 C C . GLY A 1 81 ? -16.173 -2.953 26.200 1.00 32.46 ? 112 GLY A C 1 ATOM 656 O O . GLY A 1 81 ? -16.612 -1.923 25.677 1.00 29.70 ? 112 GLY A O 1 ATOM 657 N N . ILE A 1 82 ? -14.951 -3.459 25.917 1.00 19.66 ? 113 ILE A N 1 ATOM 658 C CA . ILE A 1 82 ? -14.012 -2.846 24.976 1.00 19.82 ? 113 ILE A CA 1 ATOM 659 C C . ILE A 1 82 ? -14.135 -3.506 23.599 1.00 20.52 ? 113 ILE A C 1 ATOM 660 O O . ILE A 1 82 ? -14.313 -2.808 22.588 1.00 20.10 ? 113 ILE A O 1 ATOM 661 C CB . ILE A 1 82 ? -12.541 -2.887 25.522 1.00 16.49 ? 113 ILE A CB 1 ATOM 662 C CG1 . ILE A 1 82 ? -12.431 -2.175 26.898 1.00 26.48 ? 113 ILE A CG1 1 ATOM 663 C CG2 . ILE A 1 82 ? -11.574 -2.245 24.511 1.00 23.24 ? 113 ILE A CG2 1 ATOM 664 C CD1 . ILE A 1 82 ? -11.108 -2.378 27.676 1.00 30.32 ? 113 ILE A CD1 1 ATOM 665 N N . MET A 1 83 ? -13.968 -4.852 23.562 1.00 17.83 ? 114 MET A N 1 ATOM 666 C CA . MET A 1 83 ? -13.991 -5.652 22.333 1.00 13.10 ? 114 MET A CA 1 ATOM 667 C C . MET A 1 83 ? -14.876 -6.850 22.552 1.00 13.35 ? 114 MET A C 1 ATOM 668 O O . MET A 1 83 ? -14.785 -7.500 23.594 1.00 17.32 ? 114 MET A O 1 ATOM 669 C CB . MET A 1 83 ? -12.551 -6.153 22.006 1.00 13.07 ? 114 MET A CB 1 ATOM 670 C CG . MET A 1 83 ? -12.384 -6.732 20.596 1.00 16.45 ? 114 MET A CG 1 ATOM 671 S SD . MET A 1 83 ? -10.791 -7.589 20.316 1.00 18.51 ? 114 MET A SD 1 ATOM 672 C CE . MET A 1 83 ? -11.071 -9.168 21.191 1.00 13.67 ? 114 MET A CE 1 ATOM 673 N N . ALA A 1 84 ? -15.677 -7.208 21.552 1.00 17.16 ? 115 ALA A N 1 ATOM 674 C CA . ALA A 1 84 ? -16.483 -8.428 21.623 1.00 13.33 ? 115 ALA A CA 1 ATOM 675 C C . ALA A 1 84 ? -15.552 -9.629 21.355 1.00 17.75 ? 115 ALA A C 1 ATOM 676 O O . ALA A 1 84 ? -14.396 -9.440 20.989 1.00 14.14 ? 115 ALA A O 1 ATOM 677 C CB . ALA A 1 84 ? -17.584 -8.387 20.569 1.00 17.28 ? 115 ALA A CB 1 ATOM 678 N N . ASP A 1 85 ? -16.063 -10.850 21.473 1.00 17.87 ? 116 ASP A N 1 ATOM 679 C CA . ASP A 1 85 ? -15.255 -12.060 21.274 1.00 15.56 ? 116 ASP A CA 1 ATOM 680 C C . ASP A 1 85 ? -14.579 -12.057 19.907 1.00 15.25 ? 116 ASP A C 1 ATOM 681 O O . ASP A 1 85 ? -15.205 -11.631 18.932 1.00 16.25 ? 116 ASP A O 1 ATOM 682 C CB . ASP A 1 85 ? -16.131 -13.318 21.402 1.00 12.99 ? 116 ASP A CB 1 ATOM 683 C CG . ASP A 1 85 ? -16.627 -13.630 22.807 1.00 25.51 ? 116 ASP A CG 1 ATOM 684 O OD1 . ASP A 1 85 ? -15.984 -13.161 23.798 1.00 19.74 ? 116 ASP A OD1 1 ATOM 685 O OD2 . ASP A 1 85 ? -17.605 -14.393 22.928 1.00 26.84 ? 116 ASP A OD2 1 ATOM 686 N N . PRO A 1 86 ? -13.297 -12.482 19.804 1.00 14.47 ? 117 PRO A N 1 ATOM 687 C CA . PRO A 1 86 ? -12.685 -12.573 18.478 1.00 12.76 ? 117 PRO A CA 1 ATOM 688 C C . PRO A 1 86 ? -13.438 -13.602 17.628 1.00 15.16 ? 117 PRO A C 1 ATOM 689 O O . PRO A 1 86 ? -14.066 -14.543 18.150 1.00 12.66 ? 117 PRO A O 1 ATOM 690 C CB . PRO A 1 86 ? -11.248 -13.030 18.765 1.00 13.19 ? 117 PRO A CB 1 ATOM 691 C CG . PRO A 1 86 ? -11.339 -13.777 20.069 1.00 13.49 ? 117 PRO A CG 1 ATOM 692 C CD . PRO A 1 86 ? -12.401 -13.012 20.857 1.00 15.44 ? 117 PRO A CD 1 ATOM 693 N N . THR A 1 87 ? -13.363 -13.429 16.325 1.00 11.86 ? 118 THR A N 1 ATOM 694 C CA . THR A 1 87 ? -14.068 -14.309 15.396 1.00 19.45 ? 118 THR A CA 1 ATOM 695 C C . THR A 1 87 ? -13.112 -14.919 14.393 1.00 16.41 ? 118 THR A C 1 ATOM 696 O O . THR A 1 87 ? -12.006 -14.419 14.242 1.00 13.25 ? 118 THR A O 1 ATOM 697 C CB . THR A 1 87 ? -15.153 -13.502 14.641 1.00 22.18 ? 118 THR A CB 1 ATOM 698 O OG1 . THR A 1 87 ? -14.517 -12.492 13.843 1.00 19.85 ? 118 THR A OG1 1 ATOM 699 C CG2 . THR A 1 87 ? -16.188 -12.894 15.575 1.00 22.68 ? 118 THR A CG2 1 ATOM 700 N N . VAL A 1 88 ? -13.549 -15.991 13.695 1.00 11.61 ? 119 VAL A N 1 ATOM 701 C CA . VAL A 1 88 ? -12.791 -16.638 12.598 1.00 10.83 ? 119 VAL A CA 1 ATOM 702 C C . VAL A 1 88 ? -13.770 -16.834 11.430 1.00 13.04 ? 119 VAL A C 1 ATOM 703 O O . VAL A 1 88 ? -14.956 -17.043 11.678 1.00 17.10 ? 119 VAL A O 1 ATOM 704 C CB . VAL A 1 88 ? -12.083 -17.964 12.972 1.00 12.83 ? 119 VAL A CB 1 ATOM 705 C CG1 . VAL A 1 88 ? -10.973 -17.717 13.981 1.00 15.53 ? 119 VAL A CG1 1 ATOM 706 C CG2 . VAL A 1 88 ? -13.080 -19.007 13.503 1.00 16.77 ? 119 VAL A CG2 1 ATOM 707 N N . ASN A 1 89 ? -13.287 -16.784 10.185 1.00 12.29 ? 120 ASN A N 1 ATOM 708 C CA . ASN A 1 89 ? -14.169 -16.877 9.011 1.00 11.31 ? 120 ASN A CA 1 ATOM 709 C C . ASN A 1 89 ? -14.274 -18.307 8.477 1.00 16.30 ? 120 ASN A C 1 ATOM 710 O O . ASN A 1 89 ? -14.540 -18.512 7.294 1.00 12.93 ? 120 ASN A O 1 ATOM 711 C CB . ASN A 1 89 ? -13.731 -15.873 7.928 1.00 14.72 ? 120 ASN A CB 1 ATOM 712 C CG . ASN A 1 89 ? -12.451 -16.237 7.234 1.00 14.54 ? 120 ASN A CG 1 ATOM 713 O OD1 . ASN A 1 89 ? -11.605 -16.952 7.779 1.00 13.51 ? 120 ASN A OD1 1 ATOM 714 N ND2 . ASN A 1 89 ? -12.306 -15.804 5.981 1.00 19.20 ? 120 ASN A ND2 1 ATOM 715 N N . VAL A 1 90 ? -14.000 -19.298 9.360 1.00 12.39 ? 121 VAL A N 1 ATOM 716 C CA . VAL A 1 90 ? -14.060 -20.720 9.028 1.00 10.17 ? 121 VAL A CA 1 ATOM 717 C C . VAL A 1 90 ? -14.955 -21.409 10.078 1.00 15.22 ? 121 VAL A C 1 ATOM 718 O O . VAL A 1 90 ? -15.128 -20.865 11.172 1.00 13.08 ? 121 VAL A O 1 ATOM 719 C CB . VAL A 1 90 ? -12.631 -21.375 8.988 1.00 15.33 ? 121 VAL A CB 1 ATOM 720 C CG1 . VAL A 1 90 ? -11.773 -20.851 7.838 1.00 12.27 ? 121 VAL A CG1 1 ATOM 721 C CG2 . VAL A 1 90 ? -11.893 -21.267 10.332 1.00 12.81 ? 121 VAL A CG2 1 ATOM 722 N N . PRO A 1 91 ? -15.520 -22.607 9.778 1.00 16.29 ? 122 PRO A N 1 ATOM 723 C CA . PRO A 1 91 ? -16.263 -23.352 10.812 1.00 12.94 ? 122 PRO A CA 1 ATOM 724 C C . PRO A 1 91 ? -15.350 -23.647 12.014 1.00 13.01 ? 122 PRO A C 1 ATOM 725 O O . PRO A 1 91 ? -14.145 -23.808 11.823 1.00 13.26 ? 122 PRO A O 1 ATOM 726 C CB . PRO A 1 91 ? -16.596 -24.689 10.114 1.00 15.10 ? 122 PRO A CB 1 ATOM 727 C CG . PRO A 1 91 ? -16.544 -24.407 8.666 1.00 23.19 ? 122 PRO A CG 1 ATOM 728 C CD . PRO A 1 91 ? -15.447 -23.367 8.509 1.00 16.53 ? 122 PRO A CD 1 ATOM 729 N N . LEU A 1 92 ? -15.910 -23.737 13.235 1.00 12.09 ? 123 LEU A N 1 ATOM 730 C CA . LEU A 1 92 ? -15.107 -23.993 14.460 1.00 11.98 ? 123 LEU A CA 1 ATOM 731 C C . LEU A 1 92 ? -14.361 -25.322 14.476 1.00 16.74 ? 123 LEU A C 1 ATOM 732 O O . LEU A 1 92 ? -13.318 -25.428 15.122 1.00 14.18 ? 123 LEU A O 1 ATOM 733 C CB . LEU A 1 92 ? -15.926 -23.826 15.739 1.00 16.30 ? 123 LEU A CB 1 ATOM 734 C CG . LEU A 1 92 ? -16.593 -22.467 15.963 1.00 25.25 ? 123 LEU A CG 1 ATOM 735 C CD1 . LEU A 1 92 ? -17.417 -22.498 17.211 1.00 19.18 ? 123 LEU A CD1 1 ATOM 736 C CD2 . LEU A 1 92 ? -15.558 -21.334 16.043 1.00 21.86 ? 123 LEU A CD2 1 ATOM 737 N N . LEU A 1 93 ? -14.910 -26.348 13.818 1.00 13.77 ? 124 LEU A N 1 ATOM 738 C CA . LEU A 1 93 ? -14.263 -27.654 13.678 1.00 6.49 ? 124 LEU A CA 1 ATOM 739 C C . LEU A 1 93 ? -14.245 -27.980 12.184 1.00 11.42 ? 124 LEU A C 1 ATOM 740 O O . LEU A 1 93 ? -15.268 -27.832 11.502 1.00 11.25 ? 124 LEU A O 1 ATOM 741 C CB . LEU A 1 93 ? -15.070 -28.727 14.460 1.00 9.19 ? 124 LEU A CB 1 ATOM 742 C CG . LEU A 1 93 ? -14.699 -30.210 14.250 1.00 14.55 ? 124 LEU A CG 1 ATOM 743 C CD1 . LEU A 1 93 ? -13.302 -30.530 14.774 1.00 12.91 ? 124 LEU A CD1 1 ATOM 744 C CD2 . LEU A 1 93 ? -15.760 -31.138 14.911 1.00 12.06 ? 124 LEU A CD2 1 ATOM 745 N N . GLY A 1 94 ? -13.086 -28.389 11.678 1.00 10.42 ? 125 GLY A N 1 ATOM 746 C CA . GLY A 1 94 ? -12.962 -28.732 10.267 1.00 13.95 ? 125 GLY A CA 1 ATOM 747 C C . GLY A 1 94 ? -11.663 -29.412 9.939 1.00 18.20 ? 125 GLY A C 1 ATOM 748 O O . GLY A 1 94 ? -10.880 -29.749 10.842 1.00 13.80 ? 125 GLY A O 1 ATOM 749 N N . THR A 1 95 ? -11.435 -29.619 8.637 1.00 13.52 ? 126 THR A N 1 ATOM 750 C CA A THR A 1 95 ? -10.231 -30.234 8.122 0.50 19.09 ? 126 THR A CA 1 ATOM 751 C CA B THR A 1 95 ? -10.177 -30.219 8.196 0.50 16.66 ? 126 THR A CA 1 ATOM 752 C C . THR A 1 95 ? -9.208 -29.117 7.818 1.00 14.53 ? 126 THR A C 1 ATOM 753 O O . THR A 1 95 ? -9.603 -28.079 7.291 1.00 10.79 ? 126 THR A O 1 ATOM 754 C CB A THR A 1 95 ? -10.601 -31.005 6.829 0.50 17.46 ? 126 THR A CB 1 ATOM 755 C CB B THR A 1 95 ? -10.315 -31.167 6.978 0.50 11.18 ? 126 THR A CB 1 ATOM 756 O OG1 A THR A 1 95 ? -11.756 -31.828 7.052 0.50 15.14 ? 126 THR A OG1 1 ATOM 757 O OG1 B THR A 1 95 ? -10.852 -30.449 5.868 0.50 9.44 ? 126 THR A OG1 1 ATOM 758 C CG2 A THR A 1 95 ? -9.467 -31.828 6.290 0.50 21.58 ? 126 THR A CG2 1 ATOM 759 C CG2 B THR A 1 95 ? -11.112 -32.417 7.277 0.50 8.55 ? 126 THR A CG2 1 ATOM 760 N N . VAL A 1 96 ? -7.925 -29.352 8.081 1.00 11.35 ? 127 VAL A N 1 ATOM 761 C CA . VAL A 1 96 ? -6.875 -28.405 7.690 1.00 8.97 ? 127 VAL A CA 1 ATOM 762 C C . VAL A 1 96 ? -6.758 -28.608 6.163 1.00 8.90 ? 127 VAL A C 1 ATOM 763 O O . VAL A 1 96 ? -6.605 -29.749 5.722 1.00 11.97 ? 127 VAL A O 1 ATOM 764 C CB . VAL A 1 96 ? -5.534 -28.613 8.428 1.00 10.67 ? 127 VAL A CB 1 ATOM 765 C CG1 . VAL A 1 96 ? -4.485 -27.600 7.930 1.00 12.62 ? 127 VAL A CG1 1 ATOM 766 C CG2 . VAL A 1 96 ? -5.737 -28.465 9.941 1.00 14.02 ? 127 VAL A CG2 1 ATOM 767 N N . PRO A 1 97 ? -6.906 -27.554 5.337 1.00 11.88 ? 128 PRO A N 1 ATOM 768 C CA . PRO A 1 97 ? -6.907 -27.776 3.874 1.00 13.23 ? 128 PRO A CA 1 ATOM 769 C C . PRO A 1 97 ? -5.581 -28.197 3.289 1.00 12.16 ? 128 PRO A C 1 ATOM 770 O O . PRO A 1 97 ? -4.529 -27.819 3.784 1.00 12.45 ? 128 PRO A O 1 ATOM 771 C CB . PRO A 1 97 ? -7.369 -26.432 3.310 1.00 10.97 ? 128 PRO A CB 1 ATOM 772 C CG . PRO A 1 97 ? -6.912 -25.434 4.335 1.00 10.90 ? 128 PRO A CG 1 ATOM 773 C CD . PRO A 1 97 ? -7.134 -26.135 5.664 1.00 9.87 ? 128 PRO A CD 1 ATOM 774 N N . HIS A 1 98 ? -5.634 -29.021 2.239 1.00 8.84 ? 129 HIS A N 1 ATOM 775 C CA . HIS A 1 98 ? -4.417 -29.434 1.558 1.00 12.53 ? 129 HIS A CA 1 ATOM 776 C C . HIS A 1 98 ? -3.843 -28.272 0.735 1.00 23.25 ? 129 HIS A C 1 ATOM 777 O O . HIS A 1 98 ? -2.632 -28.139 0.641 1.00 15.68 ? 129 HIS A O 1 ATOM 778 C CB . HIS A 1 98 ? -4.680 -30.667 0.680 1.00 12.23 ? 129 HIS A CB 1 ATOM 779 C CG . HIS A 1 98 ? -4.939 -31.879 1.519 1.00 15.71 ? 129 HIS A CG 1 ATOM 780 N ND1 . HIS A 1 98 ? -3.989 -32.355 2.408 1.00 23.59 ? 129 HIS A ND1 1 ATOM 781 C CD2 . HIS A 1 98 ? -6.045 -32.657 1.603 1.00 30.12 ? 129 HIS A CD2 1 ATOM 782 C CE1 . HIS A 1 98 ? -4.539 -33.408 3.003 1.00 28.68 ? 129 HIS A CE1 1 ATOM 783 N NE2 . HIS A 1 98 ? -5.766 -33.643 2.538 1.00 27.64 ? 129 HIS A NE2 1 HETATM 784 N N . MLY A 1 99 ? -4.708 -27.452 0.161 1.00 12.78 ? 130 MLY A N 1 HETATM 785 C CA . MLY A 1 99 ? -4.237 -26.265 -0.556 1.00 13.50 ? 130 MLY A CA 1 HETATM 786 C CB . MLY A 1 99 ? -5.235 -25.859 -1.585 1.00 13.97 ? 130 MLY A CB 1 HETATM 787 C CG . MLY A 1 99 ? -4.527 -24.790 -2.500 1.00 23.37 ? 130 MLY A CG 1 HETATM 788 C CD . MLY A 1 99 ? -5.591 -23.715 -2.570 1.00 23.87 ? 130 MLY A CD 1 HETATM 789 C CE . MLY A 1 99 ? -5.155 -22.478 -3.405 1.00 22.89 ? 130 MLY A CE 1 HETATM 790 N NZ . MLY A 1 99 ? -6.299 -21.556 -3.533 1.00 23.42 ? 130 MLY A NZ 1 HETATM 791 C CH1 . MLY A 1 99 ? -7.144 -22.078 -4.661 1.00 34.10 ? 130 MLY A CH1 1 HETATM 792 C CH2 . MLY A 1 99 ? -5.835 -20.264 -4.063 1.00 27.75 ? 130 MLY A CH2 1 HETATM 793 C C . MLY A 1 99 ? -4.104 -25.118 0.463 1.00 15.44 ? 130 MLY A C 1 HETATM 794 O O . MLY A 1 99 ? -5.045 -24.880 1.233 1.00 18.96 ? 130 MLY A O 1 ATOM 795 N N . ALA A 1 100 ? -2.956 -24.392 0.444 1.00 14.74 ? 131 ALA A N 1 ATOM 796 C CA . ALA A 1 100 ? -2.746 -23.258 1.366 1.00 14.22 ? 131 ALA A CA 1 ATOM 797 C C . ALA A 1 100 ? -3.886 -22.256 1.293 1.00 17.42 ? 131 ALA A C 1 ATOM 798 O O . ALA A 1 100 ? -4.309 -21.858 0.189 1.00 15.55 ? 131 ALA A O 1 ATOM 799 C CB . ALA A 1 100 ? -1.413 -22.594 1.102 1.00 9.37 ? 131 ALA A CB 1 ATOM 800 N N . SER A 1 101 ? -4.472 -21.932 2.464 1.00 13.11 ? 132 SER A N 1 ATOM 801 C CA . SER A 1 101 ? -5.670 -21.101 2.548 1.00 12.80 ? 132 SER A CA 1 ATOM 802 C C . SER A 1 101 ? -5.555 -20.134 3.706 1.00 13.44 ? 132 SER A C 1 ATOM 803 O O . SER A 1 101 ? -4.868 -20.421 4.680 1.00 11.73 ? 132 SER A O 1 ATOM 804 C CB . SER A 1 101 ? -6.921 -21.972 2.732 1.00 17.20 ? 132 SER A CB 1 ATOM 805 O OG . SER A 1 101 ? -6.971 -23.022 1.780 1.00 16.87 ? 132 SER A OG 1 ATOM 806 N N . VAL A 1 102 ? -6.262 -19.009 3.599 1.00 11.32 ? 133 VAL A N 1 ATOM 807 C CA . VAL A 1 102 ? -6.227 -17.931 4.584 1.00 12.31 ? 133 VAL A CA 1 ATOM 808 C C . VAL A 1 102 ? -7.371 -18.063 5.576 1.00 15.34 ? 133 VAL A C 1 ATOM 809 O O . VAL A 1 102 ? -8.516 -18.277 5.170 1.00 15.14 ? 133 VAL A O 1 ATOM 810 C CB . VAL A 1 102 ? -6.271 -16.564 3.853 1.00 17.49 ? 133 VAL A CB 1 ATOM 811 C CG1 . VAL A 1 102 ? -6.423 -15.394 4.834 1.00 22.49 ? 133 VAL A CG1 1 ATOM 812 C CG2 . VAL A 1 102 ? -5.021 -16.377 2.984 1.00 19.32 ? 133 VAL A CG2 1 ATOM 813 N N . VAL A 1 103 ? -7.047 -17.937 6.883 1.00 10.71 ? 134 VAL A N 1 ATOM 814 C CA . VAL A 1 103 ? -8.017 -17.876 7.969 1.00 10.02 ? 134 VAL A CA 1 ATOM 815 C C . VAL A 1 103 ? -7.914 -16.442 8.476 1.00 16.84 ? 134 VAL A C 1 ATOM 816 O O . VAL A 1 103 ? -6.815 -16.010 8.866 1.00 15.92 ? 134 VAL A O 1 ATOM 817 C CB . VAL A 1 103 ? -7.728 -18.851 9.128 1.00 16.77 ? 134 VAL A CB 1 ATOM 818 C CG1 . VAL A 1 103 ? -8.845 -18.785 10.193 1.00 16.86 ? 134 VAL A CG1 1 ATOM 819 C CG2 . VAL A 1 103 ? -7.563 -20.255 8.609 1.00 22.58 ? 134 VAL A CG2 1 ATOM 820 N N . GLN A 1 104 ? -9.038 -15.711 8.459 1.00 14.59 ? 135 GLN A N 1 ATOM 821 C CA . GLN A 1 104 ? -9.092 -14.328 8.928 1.00 16.02 ? 135 GLN A CA 1 ATOM 822 C C . GLN A 1 104 ? -9.584 -14.303 10.373 1.00 17.97 ? 135 GLN A C 1 ATOM 823 O O . GLN A 1 104 ? -10.705 -14.749 10.655 1.00 16.55 ? 135 GLN A O 1 ATOM 824 C CB . GLN A 1 104 ? -10.028 -13.479 8.040 1.00 22.83 ? 135 GLN A CB 1 ATOM 825 C CG . GLN A 1 104 ? -9.657 -13.450 6.551 1.00 37.07 ? 135 GLN A CG 1 ATOM 826 C CD . GLN A 1 104 ? -10.526 -12.506 5.751 1.00 60.28 ? 135 GLN A CD 1 ATOM 827 O OE1 . GLN A 1 104 ? -10.919 -11.426 6.215 1.00 45.24 ? 135 GLN A OE1 1 ATOM 828 N NE2 . GLN A 1 104 ? -10.827 -12.886 4.517 1.00 51.55 ? 135 GLN A NE2 1 ATOM 829 N N . VAL A 1 105 ? -8.753 -13.789 11.302 1.00 13.66 ? 136 VAL A N 1 ATOM 830 C CA . VAL A 1 105 ? -9.181 -13.663 12.703 1.00 12.32 ? 136 VAL A CA 1 ATOM 831 C C . VAL A 1 105 ? -9.638 -12.192 12.882 1.00 15.53 ? 136 VAL A C 1 ATOM 832 O O . VAL A 1 105 ? -8.868 -11.295 12.574 1.00 15.11 ? 136 VAL A O 1 ATOM 833 C CB . VAL A 1 105 ? -8.060 -14.065 13.722 1.00 17.19 ? 136 VAL A CB 1 ATOM 834 C CG1 . VAL A 1 105 ? -8.537 -13.873 15.155 1.00 15.72 ? 136 VAL A CG1 1 ATOM 835 C CG2 . VAL A 1 105 ? -7.600 -15.507 13.515 1.00 16.67 ? 136 VAL A CG2 1 ATOM 836 N N . GLY A 1 106 ? -10.869 -11.964 13.339 1.00 11.78 ? 137 GLY A N 1 ATOM 837 C CA . GLY A 1 106 ? -11.408 -10.612 13.520 1.00 12.82 ? 137 GLY A CA 1 ATOM 838 C C . GLY A 1 106 ? -11.323 -10.152 14.955 1.00 14.40 ? 137 GLY A C 1 ATOM 839 O O . GLY A 1 106 ? -11.474 -10.974 15.871 1.00 13.78 ? 137 GLY A O 1 ATOM 840 N N . PHE A 1 107 ? -11.053 -8.836 15.162 1.00 11.68 ? 138 PHE A N 1 ATOM 841 C CA . PHE A 1 107 ? -10.927 -8.237 16.502 1.00 15.92 ? 138 PHE A CA 1 ATOM 842 C C . PHE A 1 107 ? -11.999 -7.117 16.619 1.00 17.16 ? 138 PHE A C 1 ATOM 843 O O . PHE A 1 107 ? -11.718 -5.967 16.301 1.00 16.35 ? 138 PHE A O 1 ATOM 844 C CB . PHE A 1 107 ? -9.494 -7.691 16.712 1.00 13.78 ? 138 PHE A CB 1 ATOM 845 C CG . PHE A 1 107 ? -8.397 -8.649 16.300 1.00 14.33 ? 138 PHE A CG 1 ATOM 846 C CD1 . PHE A 1 107 ? -8.226 -9.861 16.959 1.00 13.10 ? 138 PHE A CD1 1 ATOM 847 C CD2 . PHE A 1 107 ? -7.525 -8.329 15.264 1.00 13.21 ? 138 PHE A CD2 1 ATOM 848 C CE1 . PHE A 1 107 ? -7.216 -10.755 16.570 1.00 15.10 ? 138 PHE A CE1 1 ATOM 849 C CE2 . PHE A 1 107 ? -6.513 -9.216 14.880 1.00 16.03 ? 138 PHE A CE2 1 ATOM 850 C CZ . PHE A 1 107 ? -6.365 -10.421 15.529 1.00 13.93 ? 138 PHE A CZ 1 ATOM 851 N N . PRO A 1 108 ? -13.247 -7.460 17.009 1.00 13.89 ? 139 PRO A N 1 ATOM 852 C CA . PRO A 1 108 ? -14.341 -6.466 16.945 1.00 16.24 ? 139 PRO A CA 1 ATOM 853 C C . PRO A 1 108 ? -14.440 -5.447 18.065 1.00 18.30 ? 139 PRO A C 1 ATOM 854 O O . PRO A 1 108 ? -15.215 -5.645 19.005 1.00 18.54 ? 139 PRO A O 1 ATOM 855 C CB . PRO A 1 108 ? -15.604 -7.331 16.809 1.00 17.79 ? 139 PRO A CB 1 ATOM 856 C CG . PRO A 1 108 ? -15.253 -8.608 17.463 1.00 16.46 ? 139 PRO A CG 1 ATOM 857 C CD . PRO A 1 108 ? -13.759 -8.807 17.345 1.00 11.56 ? 139 PRO A CD 1 ATOM 858 N N . CYS A 1 109 ? -13.644 -4.365 17.981 1.00 14.96 ? 140 CYS A N 1 ATOM 859 C CA . CYS A 1 109 ? -13.726 -3.258 18.958 1.00 16.26 ? 140 CYS A CA 1 ATOM 860 C C . CYS A 1 109 ? -15.138 -2.687 18.877 1.00 27.19 ? 140 CYS A C 1 ATOM 861 O O . CYS A 1 109 ? -15.642 -2.464 17.774 1.00 24.14 ? 140 CYS A O 1 ATOM 862 C CB . CYS A 1 109 ? -12.686 -2.187 18.661 1.00 20.54 ? 140 CYS A CB 1 ATOM 863 S SG . CYS A 1 109 ? -10.981 -2.756 18.841 1.00 24.25 ? 140 CYS A SG 1 ATOM 864 N N . LEU A 1 110 ? -15.797 -2.527 20.026 1.00 20.90 ? 141 LEU A N 1 ATOM 865 C CA . LEU A 1 110 ? -17.182 -2.044 20.058 1.00 28.83 ? 141 LEU A CA 1 ATOM 866 C C . LEU A 1 110 ? -17.352 -0.547 19.734 1.00 35.91 ? 141 LEU A C 1 ATOM 867 O O . LEU A 1 110 ? -18.416 -0.143 19.261 1.00 31.48 ? 141 LEU A O 1 ATOM 868 C CB . LEU A 1 110 ? -17.869 -2.430 21.368 1.00 23.71 ? 141 LEU A CB 1 ATOM 869 C CG . LEU A 1 110 ? -17.941 -3.925 21.672 1.00 25.14 ? 141 LEU A CG 1 ATOM 870 C CD1 . LEU A 1 110 ? -18.556 -4.164 23.005 1.00 34.53 ? 141 LEU A CD1 1 ATOM 871 C CD2 . LEU A 1 110 ? -18.727 -4.681 20.610 1.00 28.56 ? 141 LEU A CD2 1 ATOM 872 N N . GLY A 1 111 ? -16.287 0.226 19.922 1.00 23.20 ? 142 GLY A N 1 ATOM 873 C CA . GLY A 1 111 ? -16.270 1.662 19.668 1.00 25.68 ? 142 GLY A CA 1 ATOM 874 C C . GLY A 1 111 ? -16.900 2.482 20.778 1.00 36.90 ? 142 GLY A C 1 ATOM 875 O O . GLY A 1 111 ? -17.132 3.680 20.606 1.00 34.78 ? 142 GLY A O 1 HETATM 876 N N . MLY A 1 112 ? -17.198 1.847 21.923 1.00 28.95 ? 143 MLY A N 1 HETATM 877 C CA . MLY A 1 112 ? -17.783 2.529 23.075 1.00 34.85 ? 143 MLY A CA 1 HETATM 878 C CB . MLY A 1 112 ? -18.611 1.537 23.953 1.00 37.70 ? 143 MLY A CB 1 HETATM 879 C CG . MLY A 1 112 ? -19.675 0.702 23.199 1.00 46.29 ? 143 MLY A CG 1 HETATM 880 C CD . MLY A 1 112 ? -20.576 -0.028 24.253 1.00 71.43 ? 143 MLY A CD 1 HETATM 881 C CE . MLY A 1 112 ? -20.727 -1.565 24.040 1.00 86.23 ? 143 MLY A CE 1 HETATM 882 N NZ . MLY A 1 112 ? -21.638 -2.220 25.056 1.00 80.47 ? 143 MLY A NZ 1 HETATM 883 C CH1 . MLY A 1 112 ? -21.291 -3.660 25.225 1.00 61.26 ? 143 MLY A CH1 1 HETATM 884 C CH2 . MLY A 1 112 ? -23.020 -2.211 24.524 1.00 82.81 ? 143 MLY A CH2 1 HETATM 885 C C . MLY A 1 112 ? -16.699 3.060 24.036 1.00 45.88 ? 143 MLY A C 1 HETATM 886 O O . MLY A 1 112 ? -16.932 4.070 24.709 1.00 36.00 ? 143 MLY A O 1 ATOM 887 N N . GLN A 1 113 ? -15.524 2.365 24.097 1.00 37.40 ? 144 GLN A N 1 ATOM 888 C CA A GLN A 1 113 ? -14.416 2.715 24.987 0.50 33.44 ? 144 GLN A CA 1 ATOM 889 C CA B GLN A 1 113 ? -14.414 2.707 24.989 0.50 33.66 ? 144 GLN A CA 1 ATOM 890 C C . GLN A 1 113 ? -13.068 2.695 24.277 1.00 39.25 ? 144 GLN A C 1 ATOM 891 O O . GLN A 1 113 ? -12.885 1.947 23.311 1.00 32.97 ? 144 GLN A O 1 ATOM 892 C CB A GLN A 1 113 ? -14.354 1.725 26.163 0.50 34.17 ? 144 GLN A CB 1 ATOM 893 C CB B GLN A 1 113 ? -14.342 1.689 26.138 0.50 29.60 ? 144 GLN A CB 1 ATOM 894 C CG A GLN A 1 113 ? -15.482 1.856 27.180 0.50 52.12 ? 144 GLN A CG 1 ATOM 895 C CG B GLN A 1 113 ? -15.454 1.798 27.173 0.50 48.86 ? 144 GLN A CG 1 ATOM 896 C CD A GLN A 1 113 ? -15.338 0.865 28.309 0.50 50.20 ? 144 GLN A CD 1 ATOM 897 C CD B GLN A 1 113 ? -15.295 0.793 28.289 0.50 50.03 ? 144 GLN A CD 1 ATOM 898 O OE1 A GLN A 1 113 ? -14.274 0.728 28.926 0.50 42.69 ? 144 GLN A OE1 1 ATOM 899 O OE1 B GLN A 1 113 ? -16.261 0.149 28.710 0.50 48.52 ? 144 GLN A OE1 1 ATOM 900 N NE2 A GLN A 1 113 ? -16.417 0.164 28.620 0.50 49.15 ? 144 GLN A NE2 1 ATOM 901 N NE2 B GLN A 1 113 ? -14.078 0.637 28.801 0.50 30.99 ? 144 GLN A NE2 1 ATOM 902 N N . ASP A 1 114 ? -12.112 3.498 24.780 1.00 34.20 ? 145 ASP A N 1 ATOM 903 C CA . ASP A 1 114 ? -10.737 3.531 24.292 1.00 25.99 ? 145 ASP A CA 1 ATOM 904 C C . ASP A 1 114 ? -10.007 2.645 25.313 1.00 30.01 ? 145 ASP A C 1 ATOM 905 O O . ASP A 1 114 ? -10.220 2.788 26.528 1.00 38.40 ? 145 ASP A O 1 ATOM 906 C CB . ASP A 1 114 ? -10.136 4.948 24.357 1.00 43.45 ? 145 ASP A CB 1 ATOM 907 C CG . ASP A 1 114 ? -10.805 5.980 23.473 1.00 53.21 ? 145 ASP A CG 1 ATOM 908 O OD1 . ASP A 1 114 ? -10.554 5.965 22.243 1.00 30.30 ? 145 ASP A OD1 1 ATOM 909 O OD2 . ASP A 1 114 ? -11.527 6.844 24.017 1.00 69.00 ? 145 ASP A OD2 1 ATOM 910 N N . GLY A 1 115 ? -9.155 1.755 24.839 1.00 22.83 ? 146 GLY A N 1 ATOM 911 C CA . GLY A 1 115 ? -8.412 0.897 25.747 1.00 27.00 ? 146 GLY A CA 1 ATOM 912 C C . GLY A 1 115 ? -7.869 -0.351 25.093 1.00 26.64 ? 146 GLY A C 1 ATOM 913 O O . GLY A 1 115 ? -7.997 -0.535 23.880 1.00 22.52 ? 146 GLY A O 1 ATOM 914 N N . VAL A 1 116 ? -7.253 -1.205 25.902 1.00 20.56 ? 147 VAL A N 1 ATOM 915 C CA . VAL A 1 116 ? -6.645 -2.444 25.428 1.00 19.32 ? 147 VAL A CA 1 ATOM 916 C C . VAL A 1 116 ? -7.463 -3.624 25.942 1.00 24.90 ? 147 VAL A C 1 ATOM 917 O O . VAL A 1 116 ? -7.667 -3.741 27.141 1.00 25.46 ? 147 VAL A O 1 ATOM 918 C CB . VAL A 1 116 ? -5.155 -2.515 25.842 1.00 23.62 ? 147 VAL A CB 1 ATOM 919 C CG1 . VAL A 1 116 ? -4.526 -3.836 25.407 1.00 26.79 ? 147 VAL A CG1 1 ATOM 920 C CG2 . VAL A 1 116 ? -4.379 -1.333 25.266 1.00 28.62 ? 147 VAL A CG2 1 ATOM 921 N N . ALA A 1 117 ? -7.932 -4.496 25.033 1.00 21.98 ? 148 ALA A N 1 ATOM 922 C CA . ALA A 1 117 ? -8.708 -5.670 25.429 1.00 19.99 ? 148 ALA A CA 1 ATOM 923 C C . ALA A 1 117 ? -7.838 -6.905 25.365 1.00 18.20 ? 148 ALA A C 1 ATOM 924 O O . ALA A 1 117 ? -7.164 -7.118 24.355 1.00 14.96 ? 148 ALA A O 1 ATOM 925 C CB . ALA A 1 117 ? -9.893 -5.853 24.501 1.00 15.39 ? 148 ALA A CB 1 ATOM 926 N N . ALA A 1 118 ? -7.883 -7.725 26.419 1.00 15.74 ? 149 ALA A N 1 ATOM 927 C CA . ALA A 1 118 ? -7.188 -9.019 26.489 1.00 13.43 ? 149 ALA A CA 1 ATOM 928 C C . ALA A 1 118 ? -8.137 -10.048 25.856 1.00 11.10 ? 149 ALA A C 1 ATOM 929 O O . ALA A 1 118 ? -9.360 -9.959 26.024 1.00 13.41 ? 149 ALA A O 1 ATOM 930 C CB . ALA A 1 118 ? -6.903 -9.395 27.940 1.00 17.98 ? 149 ALA A CB 1 ATOM 931 N N . PHE A 1 119 ? -7.583 -11.021 25.127 1.00 12.17 ? 150 PHE A N 1 ATOM 932 C CA . PHE A 1 119 ? -8.418 -12.032 24.489 1.00 12.29 ? 150 PHE A CA 1 ATOM 933 C C . PHE A 1 119 ? -7.660 -13.328 24.303 1.00 17.73 ? 150 PHE A C 1 ATOM 934 O O . PHE A 1 119 ? -6.422 -13.343 24.361 1.00 12.77 ? 150 PHE A O 1 ATOM 935 C CB . PHE A 1 119 ? -9.009 -11.513 23.149 1.00 12.71 ? 150 PHE A CB 1 ATOM 936 C CG . PHE A 1 119 ? -8.001 -11.299 22.036 1.00 12.95 ? 150 PHE A CG 1 ATOM 937 C CD1 . PHE A 1 119 ? -7.332 -10.086 21.905 1.00 17.43 ? 150 PHE A CD1 1 ATOM 938 C CD2 . PHE A 1 119 ? -7.749 -12.301 21.098 1.00 14.06 ? 150 PHE A CD2 1 ATOM 939 C CE1 . PHE A 1 119 ? -6.420 -9.878 20.869 1.00 14.09 ? 150 PHE A CE1 1 ATOM 940 C CE2 . PHE A 1 119 ? -6.826 -12.100 20.069 1.00 12.54 ? 150 PHE A CE2 1 ATOM 941 C CZ . PHE A 1 119 ? -6.176 -10.885 19.951 1.00 14.98 ? 150 PHE A CZ 1 ATOM 942 N N . GLU A 1 120 ? -8.419 -14.402 24.053 1.00 12.90 ? 151 GLU A N 1 ATOM 943 C CA . GLU A 1 120 ? -7.938 -15.749 23.855 1.00 10.77 ? 151 GLU A CA 1 ATOM 944 C C . GLU A 1 120 ? -8.377 -16.299 22.497 1.00 9.68 ? 151 GLU A C 1 ATOM 945 O O . GLU A 1 120 ? -9.518 -16.077 22.061 1.00 11.37 ? 151 GLU A O 1 ATOM 946 C CB . GLU A 1 120 ? -8.570 -16.677 24.900 1.00 13.27 ? 151 GLU A CB 1 ATOM 947 C CG . GLU A 1 120 ? -8.337 -16.284 26.339 1.00 26.52 ? 151 GLU A CG 1 ATOM 948 C CD . GLU A 1 120 ? -9.162 -17.063 27.344 1.00 26.70 ? 151 GLU A CD 1 ATOM 949 O OE1 . GLU A 1 120 ? -9.938 -17.967 26.948 1.00 23.93 ? 151 GLU A OE1 1 ATOM 950 O OE2 . GLU A 1 120 ? -8.983 -16.793 28.551 1.00 29.63 ? 151 GLU A OE2 1 ATOM 951 N N . VAL A 1 121 ? -7.464 -17.025 21.860 1.00 11.05 ? 152 VAL A N 1 ATOM 952 C CA . VAL A 1 121 ? -7.684 -17.815 20.631 1.00 12.41 ? 152 VAL A CA 1 ATOM 953 C C . VAL A 1 121 ? -7.014 -19.170 20.908 1.00 13.02 ? 152 VAL A C 1 ATOM 954 O O . VAL A 1 121 ? -5.826 -19.356 20.600 1.00 13.32 ? 152 VAL A O 1 ATOM 955 C CB . VAL A 1 121 ? -7.168 -17.182 19.302 1.00 11.90 ? 152 VAL A CB 1 ATOM 956 C CG1 . VAL A 1 121 ? -7.574 -18.061 18.098 1.00 12.23 ? 152 VAL A CG1 1 ATOM 957 C CG2 . VAL A 1 121 ? -7.668 -15.738 19.123 1.00 11.91 ? 152 VAL A CG2 1 ATOM 958 N N . ASP A 1 122 ? -7.780 -20.112 21.492 1.00 13.94 ? 153 ASP A N 1 ATOM 959 C CA . ASP A 1 122 ? -7.283 -21.450 21.805 1.00 11.54 ? 153 ASP A CA 1 ATOM 960 C C . ASP A 1 122 ? -7.705 -22.394 20.677 1.00 12.01 ? 153 ASP A C 1 ATOM 961 O O . ASP A 1 122 ? -8.902 -22.639 20.480 1.00 13.10 ? 153 ASP A O 1 ATOM 962 C CB . ASP A 1 122 ? -7.853 -21.956 23.145 1.00 12.45 ? 153 ASP A CB 1 ATOM 963 C CG . ASP A 1 122 ? -7.407 -21.189 24.383 1.00 23.34 ? 153 ASP A CG 1 ATOM 964 O OD1 . ASP A 1 122 ? -6.383 -20.458 24.305 1.00 18.53 ? 153 ASP A OD1 1 ATOM 965 O OD2 . ASP A 1 122 ? -8.066 -21.332 25.432 1.00 25.91 ? 153 ASP A OD2 1 ATOM 966 N N . VAL A 1 123 ? -6.732 -22.905 19.961 1.00 11.37 ? 154 VAL A N 1 ATOM 967 C CA . VAL A 1 123 ? -6.964 -23.814 18.829 1.00 9.56 ? 154 VAL A CA 1 ATOM 968 C C . VAL A 1 123 ? -6.116 -25.068 19.026 1.00 11.40 ? 154 VAL A C 1 ATOM 969 O O . VAL A 1 123 ? -5.030 -25.000 19.591 1.00 18.69 ? 154 VAL A O 1 ATOM 970 C CB . VAL A 1 123 ? -6.689 -23.093 17.457 1.00 16.14 ? 154 VAL A CB 1 ATOM 971 C CG1 . VAL A 1 123 ? -5.215 -22.707 17.286 1.00 20.01 ? 154 VAL A CG1 1 ATOM 972 C CG2 . VAL A 1 123 ? -7.187 -23.918 16.253 1.00 18.81 ? 154 VAL A CG2 1 ATOM 973 N N . ILE A 1 124 ? -6.618 -26.208 18.567 1.00 10.66 ? 155 ILE A N 1 ATOM 974 C CA . ILE A 1 124 ? -5.899 -27.480 18.585 1.00 8.87 ? 155 ILE A CA 1 ATOM 975 C C . ILE A 1 124 ? -5.913 -28.070 17.172 1.00 12.63 ? 155 ILE A C 1 ATOM 976 O O . ILE A 1 124 ? -6.823 -27.767 16.394 1.00 13.87 ? 155 ILE A O 1 ATOM 977 C CB . ILE A 1 124 ? -6.484 -28.497 19.622 1.00 14.82 ? 155 ILE A CB 1 ATOM 978 C CG1 . ILE A 1 124 ? -7.964 -28.914 19.286 1.00 16.26 ? 155 ILE A CG1 1 ATOM 979 C CG2 . ILE A 1 124 ? -6.342 -27.982 21.065 1.00 16.10 ? 155 ILE A CG2 1 ATOM 980 C CD1 . ILE A 1 124 ? -8.467 -30.246 19.987 1.00 20.26 ? 155 ILE A CD1 1 ATOM 981 N N . VAL A 1 125 ? -4.898 -28.875 16.845 1.00 9.86 ? 156 VAL A N 1 ATOM 982 C CA . VAL A 1 125 ? -4.828 -29.667 15.612 1.00 10.32 ? 156 VAL A CA 1 ATOM 983 C C . VAL A 1 125 ? -4.699 -31.105 16.060 1.00 15.13 ? 156 VAL A C 1 ATOM 984 O O . VAL A 1 125 ? -3.883 -31.409 16.948 1.00 18.06 ? 156 VAL A O 1 ATOM 985 C CB . VAL A 1 125 ? -3.736 -29.244 14.591 1.00 14.11 ? 156 VAL A CB 1 ATOM 986 C CG1 . VAL A 1 125 ? -3.675 -30.227 13.406 1.00 15.09 ? 156 VAL A CG1 1 ATOM 987 C CG2 . VAL A 1 125 ? -4.004 -27.823 14.080 1.00 16.30 ? 156 VAL A CG2 1 ATOM 988 N N . MET A 1 126 ? -5.538 -31.989 15.470 1.00 11.96 ? 157 MET A N 1 ATOM 989 C CA . MET A 1 126 ? -5.546 -33.417 15.789 1.00 9.22 ? 157 MET A CA 1 ATOM 990 C C . MET A 1 126 ? -5.203 -34.209 14.552 1.00 11.39 ? 157 MET A C 1 ATOM 991 O O . MET A 1 126 ? -5.569 -33.788 13.449 1.00 13.73 ? 157 MET A O 1 ATOM 992 C CB . MET A 1 126 ? -6.970 -33.823 16.246 1.00 16.30 ? 157 MET A CB 1 ATOM 993 C CG . MET A 1 126 ? -7.355 -33.236 17.615 1.00 23.27 ? 157 MET A CG 1 ATOM 994 S SD . MET A 1 126 ? -9.101 -33.462 18.002 1.00 24.50 ? 157 MET A SD 1 ATOM 995 C CE . MET A 1 126 ? -9.854 -32.265 16.822 1.00 22.64 ? 157 MET A CE 1 ATOM 996 N N . ASN A 1 127 ? -4.548 -35.361 14.718 1.00 10.21 ? 158 ASN A N 1 ATOM 997 C CA . ASN A 1 127 ? -4.271 -36.253 13.583 1.00 10.50 ? 158 ASN A CA 1 ATOM 998 C C . ASN A 1 127 ? -5.479 -37.203 13.417 1.00 15.60 ? 158 ASN A C 1 ATOM 999 O O . ASN A 1 127 ? -6.433 -37.122 14.195 1.00 13.61 ? 158 ASN A O 1 ATOM 1000 C CB . ASN A 1 127 ? -2.930 -37.035 13.763 1.00 15.71 ? 158 ASN A CB 1 ATOM 1001 C CG . ASN A 1 127 ? -2.849 -37.890 15.010 1.00 19.92 ? 158 ASN A CG 1 ATOM 1002 O OD1 . ASN A 1 127 ? -3.858 -38.282 15.620 1.00 16.00 ? 158 ASN A OD1 1 ATOM 1003 N ND2 . ASN A 1 127 ? -1.634 -38.185 15.425 1.00 19.39 ? 158 ASN A ND2 1 ATOM 1004 N N . SER A 1 128 ? -5.429 -38.111 12.432 1.00 11.29 ? 159 SER A N 1 ATOM 1005 C CA . SER A 1 128 ? -6.534 -39.048 12.152 1.00 14.62 ? 159 SER A CA 1 ATOM 1006 C C . SER A 1 128 ? -6.732 -40.130 13.248 1.00 17.05 ? 159 SER A C 1 ATOM 1007 O O . SER A 1 128 ? -7.714 -40.862 13.219 1.00 15.37 ? 159 SER A O 1 ATOM 1008 C CB . SER A 1 128 ? -6.353 -39.659 10.766 1.00 18.55 ? 159 SER A CB 1 ATOM 1009 O OG . SER A 1 128 ? -5.183 -40.454 10.773 1.00 24.82 ? 159 SER A OG 1 ATOM 1010 N N . GLU A 1 129 ? -5.823 -40.189 14.241 1.00 19.68 ? 160 GLU A N 1 ATOM 1011 C CA . GLU A 1 129 ? -5.925 -41.088 15.399 1.00 15.61 ? 160 GLU A CA 1 ATOM 1012 C C . GLU A 1 129 ? -6.648 -40.371 16.555 1.00 21.18 ? 160 GLU A C 1 ATOM 1013 O O . GLU A 1 129 ? -6.912 -40.995 17.581 1.00 25.00 ? 160 GLU A O 1 ATOM 1014 C CB . GLU A 1 129 ? -4.540 -41.619 15.826 1.00 23.61 ? 160 GLU A CB 1 ATOM 1015 C CG . GLU A 1 129 ? -3.905 -42.546 14.794 1.00 38.46 ? 160 GLU A CG 1 ATOM 1016 C CD . GLU A 1 129 ? -2.406 -42.764 14.927 1.00 74.23 ? 160 GLU A CD 1 ATOM 1017 O OE1 . GLU A 1 129 ? -1.950 -43.173 16.020 1.00 70.58 ? 160 GLU A OE1 1 ATOM 1018 O OE2 . GLU A 1 129 ? -1.691 -42.563 13.920 1.00 71.66 ? 160 GLU A OE2 1 ATOM 1019 N N . GLY A 1 130 ? -7.026 -39.101 16.348 1.00 17.58 ? 161 GLY A N 1 ATOM 1020 C CA . GLY A 1 130 ? -7.741 -38.289 17.335 1.00 17.30 ? 161 GLY A CA 1 ATOM 1021 C C . GLY A 1 130 ? -6.880 -37.662 18.417 1.00 33.07 ? 161 GLY A C 1 ATOM 1022 O O . GLY A 1 130 ? -7.408 -37.013 19.327 1.00 26.90 ? 161 GLY A O 1 ATOM 1023 N N . ASN A 1 131 ? -5.551 -37.782 18.301 1.00 19.59 ? 162 ASN A N 1 ATOM 1024 C CA . ASN A 1 131 ? -4.634 -37.186 19.282 1.00 15.69 ? 162 ASN A CA 1 ATOM 1025 C C . ASN A 1 131 ? -4.293 -35.741 18.937 1.00 16.78 ? 162 ASN A C 1 ATOM 1026 O O . ASN A 1 131 ? -4.018 -35.450 17.772 1.00 16.38 ? 162 ASN A O 1 ATOM 1027 C CB . ASN A 1 131 ? -3.331 -38.014 19.342 1.00 21.07 ? 162 ASN A CB 1 ATOM 1028 C CG . ASN A 1 131 ? -3.569 -39.438 19.788 1.00 34.53 ? 162 ASN A CG 1 ATOM 1029 O OD1 . ASN A 1 131 ? -4.507 -39.728 20.533 1.00 29.50 ? 162 ASN A OD1 1 ATOM 1030 N ND2 . ASN A 1 131 ? -2.770 -40.363 19.283 1.00 26.36 ? 162 ASN A ND2 1 ATOM 1031 N N . THR A 1 132 ? -4.246 -34.852 19.948 1.00 19.34 ? 163 THR A N 1 ATOM 1032 C CA . THR A 1 132 ? -3.845 -33.442 19.731 1.00 19.87 ? 163 THR A CA 1 ATOM 1033 C C . THR A 1 132 ? -2.343 -33.418 19.516 1.00 23.26 ? 163 THR A C 1 ATOM 1034 O O . THR A 1 132 ? -1.613 -33.878 20.391 1.00 23.82 ? 163 THR A O 1 ATOM 1035 C CB . THR A 1 132 ? -4.238 -32.569 20.931 1.00 22.31 ? 163 THR A CB 1 ATOM 1036 O OG1 . THR A 1 132 ? -5.651 -32.590 21.039 1.00 21.77 ? 163 THR A OG1 1 ATOM 1037 C CG2 . THR A 1 132 ? -3.742 -31.105 20.797 1.00 20.00 ? 163 THR A CG2 1 ATOM 1038 N N . ILE A 1 133 ? -1.883 -32.893 18.357 1.00 17.43 ? 164 ILE A N 1 ATOM 1039 C CA . ILE A 1 133 ? -0.459 -32.801 18.023 1.00 17.61 ? 164 ILE A CA 1 ATOM 1040 C C . ILE A 1 133 ? 0.083 -31.364 18.108 1.00 18.30 ? 164 ILE A C 1 ATOM 1041 O O . ILE A 1 133 ? 1.283 -31.185 18.241 1.00 19.82 ? 164 ILE A O 1 ATOM 1042 C CB . ILE A 1 133 ? -0.092 -33.487 16.682 1.00 21.70 ? 164 ILE A CB 1 ATOM 1043 C CG1 . ILE A 1 133 ? -0.836 -32.829 15.495 1.00 17.32 ? 164 ILE A CG1 1 ATOM 1044 C CG2 . ILE A 1 133 ? -0.305 -35.032 16.752 1.00 23.04 ? 164 ILE A CG2 1 ATOM 1045 C CD1 . ILE A 1 133 ? -0.199 -33.058 14.159 1.00 30.95 ? 164 ILE A CD1 1 ATOM 1046 N N . LEU A 1 134 ? -0.782 -30.352 17.987 1.00 12.65 ? 165 LEU A N 1 ATOM 1047 C CA . LEU A 1 134 ? -0.380 -28.941 18.077 1.00 14.49 ? 165 LEU A CA 1 ATOM 1048 C C . LEU A 1 134 ? -1.497 -28.183 18.767 1.00 19.25 ? 165 LEU A C 1 ATOM 1049 O O . LEU A 1 134 ? -2.668 -28.543 18.609 1.00 16.36 ? 165 LEU A O 1 ATOM 1050 C CB . LEU A 1 134 ? -0.132 -28.325 16.690 1.00 15.83 ? 165 LEU A CB 1 ATOM 1051 C CG . LEU A 1 134 ? 1.001 -28.898 15.821 1.00 18.64 ? 165 LEU A CG 1 ATOM 1052 C CD1 . LEU A 1 134 ? 0.790 -28.543 14.362 1.00 20.03 ? 165 LEU A CD1 1 ATOM 1053 C CD2 . LEU A 1 134 ? 2.381 -28.433 16.314 1.00 22.11 ? 165 LEU A CD2 1 HETATM 1054 N N . MLY A 1 135 ? -1.153 -27.123 19.513 1.00 13.50 ? 166 MLY A N 1 HETATM 1055 C CA . MLY A 1 135 ? -2.164 -26.296 20.157 1.00 9.68 ? 166 MLY A CA 1 HETATM 1056 C CB . MLY A 1 135 ? -2.742 -26.917 21.432 1.00 17.24 ? 166 MLY A CB 1 HETATM 1057 C CG . MLY A 1 135 ? -1.729 -27.164 22.558 1.00 23.28 ? 166 MLY A CG 1 HETATM 1058 C CD . MLY A 1 135 ? -2.479 -27.928 23.672 1.00 29.48 ? 166 MLY A CD 1 HETATM 1059 C CE . MLY A 1 135 ? -1.788 -27.753 25.056 1.00 42.08 ? 166 MLY A CE 1 HETATM 1060 N NZ . MLY A 1 135 ? -1.750 -29.003 25.878 1.00 70.17 ? 166 MLY A NZ 1 HETATM 1061 C CH1 . MLY A 1 135 ? -3.106 -29.610 26.003 1.00 65.72 ? 166 MLY A CH1 1 HETATM 1062 C CH2 . MLY A 1 135 ? -1.283 -28.657 27.249 1.00 63.93 ? 166 MLY A CH2 1 HETATM 1063 C C . MLY A 1 135 ? -1.634 -24.923 20.550 1.00 19.64 ? 166 MLY A C 1 HETATM 1064 O O . MLY A 1 135 ? -0.427 -24.757 20.711 1.00 15.10 ? 166 MLY A O 1 ATOM 1065 N N . THR A 1 136 ? -2.543 -23.950 20.737 1.00 14.12 ? 167 THR A N 1 ATOM 1066 C CA . THR A 1 136 ? -2.137 -22.642 21.251 1.00 11.58 ? 167 THR A CA 1 ATOM 1067 C C . THR A 1 136 ? -1.445 -22.924 22.621 1.00 16.01 ? 167 THR A C 1 ATOM 1068 O O . THR A 1 136 ? -1.963 -23.713 23.412 1.00 15.18 ? 167 THR A O 1 ATOM 1069 C CB . THR A 1 136 ? -3.365 -21.747 21.495 1.00 13.46 ? 167 THR A CB 1 ATOM 1070 O OG1 . THR A 1 136 ? -4.054 -21.527 20.267 1.00 15.73 ? 167 THR A OG1 1 ATOM 1071 C CG2 . THR A 1 136 ? -2.983 -20.377 22.090 1.00 16.69 ? 167 THR A CG2 1 ATOM 1072 N N . PRO A 1 137 ? -0.281 -22.327 22.914 1.00 19.65 ? 168 PRO A N 1 ATOM 1073 C CA . PRO A 1 137 ? 0.339 -22.550 24.247 1.00 17.39 ? 168 PRO A CA 1 ATOM 1074 C C . PRO A 1 137 ? -0.646 -22.296 25.395 1.00 19.23 ? 168 PRO A C 1 ATOM 1075 O O . PRO A 1 137 ? -1.423 -21.347 25.339 1.00 17.47 ? 168 PRO A O 1 ATOM 1076 C CB . PRO A 1 137 ? 1.492 -21.540 24.263 1.00 18.25 ? 168 PRO A CB 1 ATOM 1077 C CG . PRO A 1 137 ? 1.869 -21.405 22.814 1.00 20.84 ? 168 PRO A CG 1 ATOM 1078 C CD . PRO A 1 137 ? 0.530 -21.407 22.084 1.00 15.67 ? 168 PRO A CD 1 ATOM 1079 N N . GLN A 1 138 ? -0.621 -23.143 26.432 1.00 14.91 ? 169 GLN A N 1 ATOM 1080 C CA . GLN A 1 138 ? -1.530 -23.019 27.581 1.00 18.48 ? 169 GLN A CA 1 ATOM 1081 C C . GLN A 1 138 ? -1.477 -21.646 28.229 1.00 14.77 ? 169 GLN A C 1 ATOM 1082 O O . GLN A 1 138 ? -0.393 -21.090 28.400 1.00 14.25 ? 169 GLN A O 1 ATOM 1083 C CB . GLN A 1 138 ? -1.262 -24.117 28.620 1.00 22.54 ? 169 GLN A CB 1 ATOM 1084 C CG . GLN A 1 138 ? -2.482 -24.393 29.512 1.00 34.95 ? 169 GLN A CG 1 ATOM 1085 C CD . GLN A 1 138 ? -2.254 -25.467 30.553 1.00 61.32 ? 169 GLN A CD 1 ATOM 1086 O OE1 . GLN A 1 138 ? -1.514 -26.439 30.351 1.00 52.03 ? 169 GLN A OE1 1 ATOM 1087 N NE2 . GLN A 1 138 ? -2.911 -25.323 31.692 1.00 61.92 ? 169 GLN A NE2 1 ATOM 1088 N N . ASN A 1 139 ? -2.658 -21.082 28.526 1.00 16.47 ? 170 ASN A N 1 ATOM 1089 C CA . ASN A 1 139 ? -2.844 -19.770 29.156 1.00 15.78 ? 170 ASN A CA 1 ATOM 1090 C C . ASN A 1 139 ? -2.362 -18.586 28.321 1.00 13.51 ? 170 ASN A C 1 ATOM 1091 O O . ASN A 1 139 ? -2.136 -17.508 28.875 1.00 14.75 ? 170 ASN A O 1 ATOM 1092 C CB . ASN A 1 139 ? -2.284 -19.745 30.613 1.00 11.79 ? 170 ASN A CB 1 ATOM 1093 C CG . ASN A 1 139 ? -3.053 -20.661 31.522 1.00 23.88 ? 170 ASN A CG 1 ATOM 1094 O OD1 . ASN A 1 139 ? -4.273 -20.794 31.398 1.00 25.68 ? 170 ASN A OD1 1 ATOM 1095 N ND2 . ASN A 1 139 ? -2.358 -21.418 32.368 1.00 18.36 ? 170 ASN A ND2 1 ATOM 1096 N N . ALA A 1 140 ? -2.228 -18.758 26.997 1.00 10.78 ? 171 ALA A N 1 ATOM 1097 C CA . ALA A 1 140 ? -1.802 -17.630 26.145 1.00 13.59 ? 171 ALA A CA 1 ATOM 1098 C C . ALA A 1 140 ? -2.877 -16.520 26.142 1.00 16.75 ? 171 ALA A C 1 ATOM 1099 O O . ALA A 1 140 ? -4.078 -16.822 26.042 1.00 14.49 ? 171 ALA A O 1 ATOM 1100 C CB . ALA A 1 140 ? -1.551 -18.115 24.718 1.00 9.75 ? 171 ALA A CB 1 ATOM 1101 N N . ILE A 1 141 ? -2.435 -15.251 26.312 1.00 13.22 ? 172 ILE A N 1 ATOM 1102 C CA . ILE A 1 141 ? -3.264 -14.037 26.265 1.00 11.76 ? 172 ILE A CA 1 ATOM 1103 C C . ILE A 1 141 ? -2.703 -13.121 25.155 1.00 20.16 ? 172 ILE A C 1 ATOM 1104 O O . ILE A 1 141 ? -1.482 -12.940 25.051 1.00 19.48 ? 172 ILE A O 1 ATOM 1105 C CB . ILE A 1 141 ? -3.364 -13.278 27.630 1.00 18.09 ? 172 ILE A CB 1 ATOM 1106 C CG1 . ILE A 1 141 ? -3.743 -14.226 28.778 1.00 29.58 ? 172 ILE A CG1 1 ATOM 1107 C CG2 . ILE A 1 141 ? -4.413 -12.123 27.537 1.00 23.28 ? 172 ILE A CG2 1 ATOM 1108 C CD1 . ILE A 1 141 ? -3.687 -13.608 30.301 1.00 29.40 ? 172 ILE A CD1 1 ATOM 1109 N N . PHE A 1 142 ? -3.596 -12.530 24.352 1.00 12.23 ? 173 PHE A N 1 ATOM 1110 C CA . PHE A 1 142 ? -3.236 -11.615 23.265 1.00 12.01 ? 173 PHE A CA 1 ATOM 1111 C C . PHE A 1 142 ? -3.953 -10.294 23.533 1.00 20.52 ? 173 PHE A C 1 ATOM 1112 O O . PHE A 1 142 ? -4.886 -10.262 24.329 1.00 14.28 ? 173 PHE A O 1 ATOM 1113 C CB . PHE A 1 142 ? -3.599 -12.196 21.876 1.00 15.22 ? 173 PHE A CB 1 ATOM 1114 C CG . PHE A 1 142 ? -2.970 -13.548 21.612 1.00 11.61 ? 173 PHE A CG 1 ATOM 1115 C CD1 . PHE A 1 142 ? -1.624 -13.652 21.260 1.00 19.30 ? 173 PHE A CD1 1 ATOM 1116 C CD2 . PHE A 1 142 ? -3.698 -14.719 21.797 1.00 10.65 ? 173 PHE A CD2 1 ATOM 1117 C CE1 . PHE A 1 142 ? -1.020 -14.915 21.088 1.00 16.50 ? 173 PHE A CE1 1 ATOM 1118 C CE2 . PHE A 1 142 ? -3.097 -15.979 21.608 1.00 15.46 ? 173 PHE A CE2 1 ATOM 1119 C CZ . PHE A 1 142 ? -1.772 -16.064 21.234 1.00 12.16 ? 173 PHE A CZ 1 ATOM 1120 N N . PHE A 1 143 ? -3.483 -9.203 22.937 1.00 13.70 ? 174 PHE A N 1 ATOM 1121 C CA . PHE A 1 143 ? -4.035 -7.882 23.247 1.00 13.68 ? 174 PHE A CA 1 ATOM 1122 C C . PHE A 1 143 ? -4.375 -7.056 22.009 1.00 11.27 ? 174 PHE A C 1 ATOM 1123 O O . PHE A 1 143 ? -3.630 -7.061 21.031 1.00 13.14 ? 174 PHE A O 1 ATOM 1124 C CB . PHE A 1 143 ? -3.067 -7.124 24.208 1.00 18.13 ? 174 PHE A CB 1 ATOM 1125 C CG . PHE A 1 143 ? -2.773 -7.826 25.530 1.00 20.50 ? 174 PHE A CG 1 ATOM 1126 C CD1 . PHE A 1 143 ? -1.709 -8.720 25.646 1.00 22.98 ? 174 PHE A CD1 1 ATOM 1127 C CD2 . PHE A 1 143 ? -3.557 -7.587 26.654 1.00 19.61 ? 174 PHE A CD2 1 ATOM 1128 C CE1 . PHE A 1 143 ? -1.465 -9.395 26.853 1.00 21.96 ? 174 PHE A CE1 1 ATOM 1129 C CE2 . PHE A 1 143 ? -3.313 -8.260 27.861 1.00 25.93 ? 174 PHE A CE2 1 ATOM 1130 C CZ . PHE A 1 143 ? -2.259 -9.146 27.958 1.00 21.00 ? 174 PHE A CZ 1 ATOM 1131 N N . LYS A 1 144 ? -5.489 -6.310 22.068 1.00 13.45 ? 175 LYS A N 1 ATOM 1132 C CA . LYS A 1 144 ? -5.944 -5.480 20.947 1.00 13.27 ? 175 LYS A CA 1 ATOM 1133 C C . LYS A 1 144 ? -6.193 -4.039 21.393 1.00 15.89 ? 175 LYS A C 1 ATOM 1134 O O . LYS A 1 144 ? -6.917 -3.834 22.361 1.00 18.57 ? 175 LYS A O 1 ATOM 1135 C CB . LYS A 1 144 ? -7.244 -6.091 20.364 1.00 16.41 ? 175 LYS A CB 1 ATOM 1136 C CG . LYS A 1 144 ? -7.996 -5.235 19.331 1.00 15.79 ? 175 LYS A CG 1 ATOM 1137 C CD . LYS A 1 144 ? -7.300 -5.202 17.969 1.00 14.59 ? 175 LYS A CD 1 ATOM 1138 C CE . LYS A 1 144 ? -8.080 -4.389 16.952 1.00 18.31 ? 175 LYS A CE 1 ATOM 1139 N NZ . LYS A 1 144 ? -7.629 -2.951 16.860 1.00 15.93 ? 175 LYS A NZ 1 ATOM 1140 N N . THR A 1 145 ? -5.641 -3.056 20.673 1.00 15.40 ? 176 THR A N 1 ATOM 1141 C CA . THR A 1 145 ? -5.877 -1.639 21.012 1.00 15.02 ? 176 THR A CA 1 ATOM 1142 C C . THR A 1 145 ? -7.171 -1.208 20.315 1.00 18.03 ? 176 THR A C 1 ATOM 1143 O O . THR A 1 145 ? -7.285 -1.363 19.104 1.00 20.17 ? 176 THR A O 1 ATOM 1144 C CB . THR A 1 145 ? -4.676 -0.732 20.642 1.00 17.01 ? 176 THR A CB 1 ATOM 1145 O OG1 . THR A 1 145 ? -3.449 -1.355 21.051 1.00 24.11 ? 176 THR A OG1 1 ATOM 1146 C CG2 . THR A 1 145 ? -4.783 0.668 21.290 1.00 19.91 ? 176 THR A CG2 1 ATOM 1147 N N . CYS A 1 146 ? -8.143 -0.696 21.095 1.00 21.21 ? 177 CYS A N 1 ATOM 1148 C CA . CYS A 1 146 ? -9.438 -0.207 20.615 1.00 17.51 ? 177 CYS A CA 1 ATOM 1149 C C . CYS A 1 146 ? -9.592 1.305 20.847 1.00 29.47 ? 177 CYS A C 1 ATOM 1150 O O . CYS A 1 146 ? -9.120 1.834 21.857 1.00 20.42 ? 177 CYS A O 1 ATOM 1151 C CB . CYS A 1 146 ? -10.575 -0.977 21.276 1.00 17.70 ? 177 CYS A CB 1 ATOM 1152 S SG . CYS A 1 146 ? -10.617 -2.752 20.849 1.00 21.54 ? 177 CYS A SG 1 ATOM 1153 N N . GLN A 1 147 ? -10.331 1.962 19.953 1.00 21.41 ? 178 GLN A N 1 ATOM 1154 C CA . GLN A 1 147 ? -10.615 3.391 20.045 1.00 25.40 ? 178 GLN A CA 1 ATOM 1155 C C . GLN A 1 147 ? -12.131 3.629 20.173 1.00 26.33 ? 178 GLN A C 1 ATOM 1156 O O . GLN A 1 147 ? -12.922 2.794 19.736 1.00 29.55 ? 178 GLN A O 1 ATOM 1157 C CB . GLN A 1 147 ? -10.060 4.071 18.787 1.00 29.13 ? 178 GLN A CB 1 ATOM 1158 C CG . GLN A 1 147 ? -9.763 5.554 18.926 1.00 56.83 ? 178 GLN A CG 1 ATOM 1159 C CD . GLN A 1 147 ? -8.799 6.015 17.861 1.00 78.46 ? 178 GLN A CD 1 ATOM 1160 O OE1 . GLN A 1 147 ? -7.662 6.399 18.151 1.00 71.77 ? 178 GLN A OE1 1 ATOM 1161 N NE2 . GLN A 1 147 ? -9.219 5.970 16.600 1.00 71.98 ? 178 GLN A NE2 1 ATOM 1162 N N . GLN A 1 148 ? -12.538 4.757 20.787 1.00 30.87 ? 179 GLN A N 1 ATOM 1163 C CA . GLN A 1 148 ? -13.955 5.140 20.888 1.00 44.82 ? 179 GLN A CA 1 ATOM 1164 C C . GLN A 1 148 ? -14.338 5.688 19.516 1.00 37.42 ? 179 GLN A C 1 ATOM 1165 O O . GLN A 1 148 ? -13.555 6.428 18.922 1.00 44.37 ? 179 GLN A O 1 ATOM 1166 C CB . GLN A 1 148 ? -14.148 6.227 21.953 1.00 33.51 ? 179 GLN A CB 1 ATOM 1167 C CG . GLN A 1 148 ? -15.576 6.321 22.482 1.00 52.09 ? 179 GLN A CG 1 ATOM 1168 C CD . GLN A 1 148 ? -15.713 7.416 23.505 1.00 56.94 ? 179 GLN A CD 1 ATOM 1169 O OE1 . GLN A 1 148 ? -15.889 7.162 24.699 1.00 64.29 ? 179 GLN A OE1 1 ATOM 1170 N NE2 . GLN A 1 148 ? -15.610 8.664 23.064 1.00 85.48 ? 179 GLN A NE2 1 ATOM 1171 N N . ALA A 1 149 ? -15.496 5.285 18.986 1.00 29.67 ? 180 ALA A N 1 ATOM 1172 C CA . ALA A 1 149 ? -15.921 5.736 17.660 1.00 46.16 ? 180 ALA A CA 1 ATOM 1173 C C . ALA A 1 149 ? -16.431 7.173 17.656 1.00 36.65 ? 180 ALA A C 1 ATOM 1174 O O . ALA A 1 149 ? -17.097 7.599 18.598 1.00 47.09 ? 180 ALA A O 1 ATOM 1175 C CB . ALA A 1 149 ? -16.967 4.801 17.090 1.00 48.39 ? 180 ALA A CB 1 ATOM 1176 N N . GLU A 1 150 ? -16.072 7.923 16.606 1.00 48.30 ? 181 GLU A N 1 ATOM 1177 C CA . GLU A 1 150 ? -16.468 9.315 16.396 1.00 46.97 ? 181 GLU A CA 1 ATOM 1178 C C . GLU A 1 150 ? -16.762 9.473 14.901 1.00 48.76 ? 181 GLU A C 1 ATOM 1179 O O . GLU A 1 150 ? -15.840 9.473 14.079 1.00 54.91 ? 181 GLU A O 1 ATOM 1180 C CB . GLU A 1 150 ? -15.353 10.268 16.869 1.00 52.02 ? 181 GLU A CB 1 ATOM 1181 C CG . GLU A 1 150 ? -15.835 11.670 17.212 1.00 90.10 ? 181 GLU A CG 1 ATOM 1182 C CD . GLU A 1 150 ? -16.042 11.946 18.691 1.00 100.14 ? 181 GLU A CD 1 ATOM 1183 O OE1 . GLU A 1 150 ? -15.034 12.038 19.431 1.00 90.87 ? 181 GLU A OE1 1 ATOM 1184 O OE2 . GLU A 1 150 ? -17.212 12.110 19.104 1.00 89.07 ? 181 GLU A OE2 1 ATOM 1185 N N . CYS A 1 151 ? -18.058 9.527 14.547 1.00 54.09 ? 182 CYS A N 1 ATOM 1186 C CA . CYS A 1 151 ? -18.504 9.646 13.157 1.00 41.86 ? 182 CYS A CA 1 ATOM 1187 C C . CYS A 1 151 ? -18.534 11.090 12.669 1.00 46.49 ? 182 CYS A C 1 ATOM 1188 O O . CYS A 1 151 ? -18.996 11.962 13.409 1.00 66.32 ? 182 CYS A O 1 ATOM 1189 C CB . CYS A 1 151 ? -19.855 8.964 12.955 1.00 53.05 ? 182 CYS A CB 1 ATOM 1190 S SG . CYS A 1 151 ? -19.740 7.199 12.563 1.00 64.27 ? 182 CYS A SG 1 ATOM 1191 N N . PRO A 1 152 ? -18.086 11.368 11.419 1.00 60.25 ? 183 PRO A N 1 ATOM 1192 C CA . PRO A 1 152 ? -18.140 12.754 10.917 1.00 83.35 ? 183 PRO A CA 1 ATOM 1193 C C . PRO A 1 152 ? -19.590 13.231 10.778 1.00 84.35 ? 183 PRO A C 1 ATOM 1194 O O . PRO A 1 152 ? -20.378 12.635 10.038 1.00 49.62 ? 183 PRO A O 1 ATOM 1195 C CB . PRO A 1 152 ? -17.402 12.686 9.566 1.00 64.96 ? 183 PRO A CB 1 ATOM 1196 C CG . PRO A 1 152 ? -16.695 11.371 9.557 1.00 75.11 ? 183 PRO A CG 1 ATOM 1197 C CD . PRO A 1 152 ? -17.516 10.454 10.407 1.00 49.38 ? 183 PRO A CD 1 ATOM 1198 N N . GLY A 1 153 ? -19.934 14.250 11.562 1.00 86.45 ? 184 GLY A N 1 ATOM 1199 C CA . GLY A 1 153 ? -21.274 14.828 11.601 1.00 103.50 ? 184 GLY A CA 1 ATOM 1200 C C . GLY A 1 153 ? -22.229 14.154 12.573 1.00 113.77 ? 184 GLY A C 1 ATOM 1201 O O . GLY A 1 153 ? -23.394 14.552 12.666 1.00 114.85 ? 184 GLY A O 1 ATOM 1202 N N . GLY A 1 154 ? -21.746 13.121 13.272 1.00 115.60 ? 185 GLY A N 1 ATOM 1203 C CA . GLY A 1 154 ? -22.505 12.355 14.258 1.00 109.68 ? 185 GLY A CA 1 ATOM 1204 C C . GLY A 1 154 ? -23.630 11.497 13.706 1.00 110.17 ? 185 GLY A C 1 ATOM 1205 O O . GLY A 1 154 ? -23.970 11.581 12.519 1.00 100.76 ? 185 GLY A O 1 ATOM 1206 N N . CYS A 1 155 ? -24.217 10.654 14.583 1.00 97.57 ? 186 CYS A N 1 ATOM 1207 C CA . CYS A 1 155 ? -25.335 9.769 14.240 1.00 84.51 ? 186 CYS A CA 1 ATOM 1208 C C . CYS A 1 155 ? -26.614 10.259 14.936 1.00 90.13 ? 186 CYS A C 1 ATOM 1209 O O . CYS A 1 155 ? -26.650 10.357 16.165 1.00 87.07 ? 186 CYS A O 1 ATOM 1210 C CB . CYS A 1 155 ? -25.023 8.315 14.589 1.00 77.97 ? 186 CYS A CB 1 ATOM 1211 S SG . CYS A 1 155 ? -23.486 7.677 13.863 1.00 73.20 ? 186 CYS A SG 1 ATOM 1212 N N . ARG A 1 156 ? -27.642 10.601 14.141 1.00 77.81 ? 187 ARG A N 1 ATOM 1213 C CA . ARG A 1 156 ? -28.927 11.105 14.637 1.00 73.09 ? 187 ARG A CA 1 ATOM 1214 C C . ARG A 1 156 ? -29.909 9.943 14.894 1.00 77.83 ? 187 ARG A C 1 ATOM 1215 O O . ARG A 1 156 ? -29.571 8.787 14.610 1.00 63.95 ? 187 ARG A O 1 ATOM 1216 C CB . ARG A 1 156 ? -29.531 12.142 13.652 1.00 87.46 ? 187 ARG A CB 1 ATOM 1217 C CG . ARG A 1 156 ? -28.579 13.249 13.171 1.00 86.78 ? 187 ARG A CG 1 ATOM 1218 C CD . ARG A 1 156 ? -28.505 14.442 14.113 1.00 92.87 ? 187 ARG A CD 1 ATOM 1219 N NE . ARG A 1 156 ? -27.573 14.217 15.221 1.00 106.96 ? 187 ARG A NE 1 ATOM 1220 C CZ . ARG A 1 156 ? -26.286 14.548 15.203 1.00 111.03 ? 187 ARG A CZ 1 ATOM 1221 N NH1 . ARG A 1 156 ? -25.756 15.127 14.132 1.00 120.82 ? 187 ARG A NH1 1 ATOM 1222 N NH2 . ARG A 1 156 ? -25.516 14.302 16.256 1.00 103.75 ? 187 ARG A NH2 1 ATOM 1223 N N . ASN A 1 157 ? -31.111 10.258 15.451 1.00 61.36 ? 188 ASN A N 1 ATOM 1224 C CA . ASN A 1 157 ? -32.204 9.321 15.761 1.00 55.56 ? 188 ASN A CA 1 ATOM 1225 C C . ASN A 1 157 ? -31.780 8.126 16.637 1.00 57.72 ? 188 ASN A C 1 ATOM 1226 O O . ASN A 1 157 ? -32.147 6.987 16.349 1.00 51.83 ? 188 ASN A O 1 ATOM 1227 C CB . ASN A 1 157 ? -32.903 8.838 14.473 1.00 49.98 ? 188 ASN A CB 1 ATOM 1228 C CG . ASN A 1 157 ? -33.747 9.878 13.785 1.00 70.36 ? 188 ASN A CG 1 ATOM 1229 O OD1 . ASN A 1 157 ? -34.959 9.975 14.004 1.00 51.26 ? 188 ASN A OD1 1 ATOM 1230 N ND2 . ASN A 1 157 ? -33.134 10.645 12.894 1.00 74.74 ? 188 ASN A ND2 1 ATOM 1231 N N . GLY A 1 158 ? -30.999 8.397 17.683 1.00 92.05 ? 189 GLY A N 1 ATOM 1232 C CA . GLY A 1 158 ? -30.517 7.372 18.608 1.00 75.26 ? 189 GLY A CA 1 ATOM 1233 C C . GLY A 1 158 ? -29.497 6.411 18.026 1.00 94.52 ? 189 GLY A C 1 ATOM 1234 O O . GLY A 1 158 ? -29.223 5.363 18.618 1.00 92.90 ? 189 GLY A O 1 ATOM 1235 N N . GLY A 1 159 ? -28.949 6.770 16.866 1.00 83.50 ? 190 GLY A N 1 ATOM 1236 C CA . GLY A 1 159 ? -27.940 5.984 16.174 1.00 66.49 ? 190 GLY A CA 1 ATOM 1237 C C . GLY A 1 159 ? -26.596 6.066 16.867 1.00 61.38 ? 190 GLY A C 1 ATOM 1238 O O . GLY A 1 159 ? -26.327 7.023 17.602 1.00 74.05 ? 190 GLY A O 1 ATOM 1239 N N . PHE A 1 160 ? -25.748 5.062 16.643 1.00 56.59 ? 191 PHE A N 1 ATOM 1240 C CA . PHE A 1 160 ? -24.427 5.038 17.254 1.00 79.34 ? 191 PHE A CA 1 ATOM 1241 C C . PHE A 1 160 ? -23.323 4.816 16.254 1.00 71.57 ? 191 PHE A C 1 ATOM 1242 O O . PHE A 1 160 ? -23.512 4.092 15.277 1.00 45.00 ? 191 PHE A O 1 ATOM 1243 C CB . PHE A 1 160 ? -24.365 4.056 18.433 1.00 81.65 ? 191 PHE A CB 1 ATOM 1244 C CG . PHE A 1 160 ? -25.135 4.582 19.624 1.00 107.86 ? 191 PHE A CG 1 ATOM 1245 C CD1 . PHE A 1 160 ? -24.615 5.606 20.413 1.00 89.78 ? 191 PHE A CD1 1 ATOM 1246 C CD2 . PHE A 1 160 ? -26.402 4.095 19.925 1.00 117.78 ? 191 PHE A CD2 1 ATOM 1247 C CE1 . PHE A 1 160 ? -25.341 6.119 21.490 1.00 80.67 ? 191 PHE A CE1 1 ATOM 1248 C CE2 . PHE A 1 160 ? -27.124 4.600 21.013 1.00 113.50 ? 191 PHE A CE2 1 ATOM 1249 C CZ . PHE A 1 160 ? -26.590 5.611 21.784 1.00 108.88 ? 191 PHE A CZ 1 ATOM 1250 N N . CYS A 1 161 ? -22.182 5.477 16.458 1.00 54.12 ? 192 CYS A N 1 ATOM 1251 C CA . CYS A 1 161 ? -21.081 5.298 15.523 1.00 42.76 ? 192 CYS A CA 1 ATOM 1252 C C . CYS A 1 161 ? -20.316 4.027 15.823 1.00 61.31 ? 192 CYS A C 1 ATOM 1253 O O . CYS A 1 161 ? -20.011 3.739 16.982 1.00 68.30 ? 192 CYS A O 1 ATOM 1254 C CB . CYS A 1 161 ? -20.161 6.511 15.483 1.00 69.03 ? 192 CYS A CB 1 ATOM 1255 S SG . CYS A 1 161 ? -18.869 6.397 14.220 1.00 59.03 ? 192 CYS A SG 1 ATOM 1256 N N . ASN A 1 162 ? -20.035 3.250 14.777 1.00 43.21 ? 193 ASN A N 1 ATOM 1257 C CA . ASN A 1 162 ? -19.257 2.028 14.916 1.00 54.96 ? 193 ASN A CA 1 ATOM 1258 C C . ASN A 1 162 ? -17.783 2.322 14.614 1.00 51.73 ? 193 ASN A C 1 ATOM 1259 O O . ASN A 1 162 ? -17.464 3.402 14.109 1.00 50.96 ? 193 ASN A O 1 ATOM 1260 C CB . ASN A 1 162 ? -19.811 0.934 14.022 1.00 58.36 ? 193 ASN A CB 1 ATOM 1261 C CG . ASN A 1 162 ? -19.796 1.217 12.542 1.00 77.20 ? 193 ASN A CG 1 ATOM 1262 O OD1 . ASN A 1 162 ? -18.753 1.431 11.921 1.00 47.30 ? 193 ASN A OD1 1 ATOM 1263 N ND2 . ASN A 1 162 ? -20.964 1.116 11.925 1.00 104.00 ? 193 ASN A ND2 1 ATOM 1264 N N . GLU A 1 163 ? -16.892 1.361 14.878 1.00 83.75 ? 194 GLU A N 1 ATOM 1265 C CA . GLU A 1 163 ? -15.462 1.570 14.648 1.00 99.79 ? 194 GLU A CA 1 ATOM 1266 C C . GLU A 1 163 ? -14.977 1.676 13.175 1.00 39.33 ? 194 GLU A C 1 ATOM 1267 O O . GLU A 1 163 ? -13.805 1.970 12.935 1.00 61.31 ? 194 GLU A O 1 ATOM 1268 C CB . GLU A 1 163 ? -14.613 0.664 15.557 1.00 84.35 ? 194 GLU A CB 1 ATOM 1269 C CG . GLU A 1 163 ? -13.252 1.237 15.921 1.00 95.03 ? 194 GLU A CG 1 ATOM 1270 C CD . GLU A 1 163 ? -13.236 2.612 16.559 1.00 100.61 ? 194 GLU A CD 1 ATOM 1271 O OE1 . GLU A 1 163 ? -14.165 2.922 17.340 1.00 63.33 ? 194 GLU A OE1 1 ATOM 1272 O OE2 . GLU A 1 163 ? -12.292 3.385 16.276 1.00 126.97 ? 194 GLU A OE2 1 ATOM 1273 N N . ARG A 1 164 ? -15.885 1.491 12.198 1.00 64.89 ? 195 ARG A N 1 ATOM 1274 C CA . ARG A 1 164 ? -15.583 1.645 10.763 1.00 71.02 ? 195 ARG A CA 1 ATOM 1275 C C . ARG A 1 164 ? -15.969 3.081 10.320 1.00 44.21 ? 195 ARG A C 1 ATOM 1276 O O . ARG A 1 164 ? -15.883 3.416 9.136 1.00 55.83 ? 195 ARG A O 1 ATOM 1277 C CB . ARG A 1 164 ? -16.353 0.593 9.940 1.00 66.87 ? 195 ARG A CB 1 ATOM 1278 C CG . ARG A 1 164 ? -15.737 0.282 8.584 1.00 81.26 ? 195 ARG A CG 1 ATOM 1279 C CD . ARG A 1 164 ? -16.620 -0.631 7.762 1.00 102.63 ? 195 ARG A CD 1 ATOM 1280 N NE . ARG A 1 164 ? -15.823 -1.501 6.899 1.00 112.80 ? 195 ARG A NE 1 ATOM 1281 C CZ . ARG A 1 164 ? -16.222 -1.970 5.721 1.00 116.16 ? 195 ARG A CZ 1 ATOM 1282 N NH1 . ARG A 1 164 ? -17.413 -1.642 5.236 1.00 108.44 ? 195 ARG A NH1 1 ATOM 1283 N NH2 . ARG A 1 164 ? -15.424 -2.754 5.009 1.00 120.00 ? 195 ARG A NH2 1 ATOM 1284 N N . ARG A 1 165 ? -16.379 3.924 11.294 1.00 49.02 ? 196 ARG A N 1 ATOM 1285 C CA . ARG A 1 165 ? -16.848 5.309 11.127 1.00 48.50 ? 196 ARG A CA 1 ATOM 1286 C C . ARG A 1 165 ? -18.092 5.411 10.220 1.00 52.73 ? 196 ARG A C 1 ATOM 1287 O O . ARG A 1 165 ? -18.236 6.350 9.431 1.00 51.64 ? 196 ARG A O 1 ATOM 1288 C CB . ARG A 1 165 ? -15.713 6.285 10.751 1.00 46.80 ? 196 ARG A CB 1 ATOM 1289 C CG . ARG A 1 165 ? -14.727 6.510 11.886 1.00 57.77 ? 196 ARG A CG 1 ATOM 1290 C CD . ARG A 1 165 ? -13.685 7.554 11.546 1.00 73.45 ? 196 ARG A CD 1 ATOM 1291 N NE . ARG A 1 165 ? -12.673 7.653 12.600 1.00 80.20 ? 196 ARG A NE 1 ATOM 1292 C CZ . ARG A 1 165 ? -11.649 8.500 12.588 1.00 77.58 ? 196 ARG A CZ 1 ATOM 1293 N NH1 . ARG A 1 165 ? -11.482 9.340 11.572 1.00 47.62 ? 196 ARG A NH1 1 ATOM 1294 N NH2 . ARG A 1 165 ? -10.781 8.514 13.592 1.00 84.40 ? 196 ARG A NH2 1 ATOM 1295 N N . ILE A 1 166 ? -19.003 4.428 10.377 1.00 56.21 ? 197 ILE A N 1 ATOM 1296 C CA . ILE A 1 166 ? -20.286 4.308 9.676 1.00 56.99 ? 197 ILE A CA 1 ATOM 1297 C C . ILE A 1 166 ? -21.391 4.351 10.749 1.00 75.87 ? 197 ILE A C 1 ATOM 1298 O O . ILE A 1 166 ? -21.219 3.777 11.828 1.00 51.98 ? 197 ILE A O 1 ATOM 1299 C CB . ILE A 1 166 ? -20.319 3.008 8.797 1.00 68.13 ? 197 ILE A CB 1 ATOM 1300 C CG1 . ILE A 1 166 ? -19.368 3.098 7.559 1.00 85.07 ? 197 ILE A CG1 1 ATOM 1301 C CG2 . ILE A 1 166 ? -21.743 2.553 8.398 1.00 41.33 ? 197 ILE A CG2 1 ATOM 1302 C CD1 . ILE A 1 166 ? -19.745 4.127 6.394 1.00 45.96 ? 197 ILE A CD1 1 ATOM 1303 N N . CYS A 1 167 ? -22.496 5.067 10.480 1.00 71.25 ? 198 CYS A N 1 ATOM 1304 C CA . CYS A 1 167 ? -23.578 5.148 11.458 1.00 68.19 ? 198 CYS A CA 1 ATOM 1305 C C . CYS A 1 167 ? -24.419 3.873 11.525 1.00 80.54 ? 198 CYS A C 1 ATOM 1306 O O . CYS A 1 167 ? -24.776 3.299 10.491 1.00 51.43 ? 198 CYS A O 1 ATOM 1307 C CB . CYS A 1 167 ? -24.437 6.391 11.252 1.00 54.42 ? 198 CYS A CB 1 ATOM 1308 S SG . CYS A 1 167 ? -23.674 7.922 11.850 1.00 54.17 ? 198 CYS A SG 1 ATOM 1309 N N . GLU A 1 168 ? -24.680 3.420 12.766 1.00 103.85 ? 199 GLU A N 1 ATOM 1310 C CA . GLU A 1 168 ? -25.491 2.254 13.126 1.00 104.02 ? 199 GLU A CA 1 ATOM 1311 C C . GLU A 1 168 ? -26.905 2.801 13.395 1.00 97.02 ? 199 GLU A C 1 ATOM 1312 O O . GLU A 1 168 ? -27.200 3.234 14.513 1.00 80.94 ? 199 GLU A O 1 ATOM 1313 C CB . GLU A 1 168 ? -24.908 1.597 14.392 1.00 124.09 ? 199 GLU A CB 1 ATOM 1314 C CG . GLU A 1 168 ? -23.553 0.927 14.205 1.00 133.41 ? 199 GLU A CG 1 ATOM 1315 C CD . GLU A 1 168 ? -22.934 0.345 15.464 1.00 130.30 ? 199 GLU A CD 1 ATOM 1316 O OE1 . GLU A 1 168 ? -22.832 1.075 16.477 1.00 138.92 ? 199 GLU A OE1 1 ATOM 1317 O OE2 . GLU A 1 168 ? -22.494 -0.826 15.417 1.00 117.23 ? 199 GLU A OE2 1 ATOM 1318 N N . CYS A 1 169 ? -27.750 2.841 12.345 1.00 116.58 ? 200 CYS A N 1 ATOM 1319 C CA . CYS A 1 169 ? -29.095 3.441 12.361 1.00 129.91 ? 200 CYS A CA 1 ATOM 1320 C C . CYS A 1 169 ? -30.231 2.516 12.780 1.00 127.08 ? 200 CYS A C 1 ATOM 1321 O O . CYS A 1 169 ? -30.331 1.443 12.198 1.00 137.41 ? 200 CYS A O 1 ATOM 1322 C CB . CYS A 1 169 ? -29.397 4.084 11.010 1.00 121.47 ? 200 CYS A CB 1 ATOM 1323 S SG . CYS A 1 169 ? -28.108 5.199 10.411 1.00 102.78 ? 200 CYS A SG 1 ATOM 1324 N N . PRO A 1 170 ? -31.124 2.947 13.664 1.00 95.82 ? 201 PRO A N 1 ATOM 1325 C CA . PRO A 1 170 ? -32.216 2.076 14.102 1.00 84.34 ? 201 PRO A CA 1 ATOM 1326 C C . PRO A 1 170 ? -33.380 2.030 13.112 1.00 95.18 ? 201 PRO A C 1 ATOM 1327 O O . PRO A 1 170 ? -33.242 2.339 11.930 1.00 59.36 ? 201 PRO A O 1 ATOM 1328 C CB . PRO A 1 170 ? -32.658 2.699 15.424 1.00 69.41 ? 201 PRO A CB 1 ATOM 1329 C CG . PRO A 1 170 ? -32.337 4.117 15.283 1.00 84.45 ? 201 PRO A CG 1 ATOM 1330 C CD . PRO A 1 170 ? -31.054 4.164 14.489 1.00 98.30 ? 201 PRO A CD 1 ATOM 1331 N N . ASP A 1 171 ? -34.531 1.621 13.626 1.00 144.65 ? 202 ASP A N 1 ATOM 1332 C CA . ASP A 1 171 ? -35.703 1.297 12.838 1.00 137.72 ? 202 ASP A CA 1 ATOM 1333 C C . ASP A 1 171 ? -36.076 2.393 11.873 1.00 139.05 ? 202 ASP A C 1 ATOM 1334 O O . ASP A 1 171 ? -36.073 3.554 12.212 1.00 161.46 ? 202 ASP A O 1 ATOM 1335 C CB . ASP A 1 171 ? -36.858 1.198 13.815 1.00 140.52 ? 202 ASP A CB 1 ATOM 1336 C CG . ASP A 1 171 ? -37.168 2.539 14.486 1.00 128.38 ? 202 ASP A CG 1 ATOM 1337 O OD1 . ASP A 1 171 ? -37.696 3.449 13.830 1.00 121.30 ? 202 ASP A OD1 1 ATOM 1338 O OD2 . ASP A 1 171 ? -36.894 2.690 15.680 1.00 121.09 ? 202 ASP A OD2 1 ATOM 1339 N N . GLY A 1 172 ? -36.332 2.021 10.630 1.00 94.62 ? 203 GLY A N 1 ATOM 1340 C CA . GLY A 1 172 ? -36.863 2.957 9.662 1.00 78.75 ? 203 GLY A CA 1 ATOM 1341 C C . GLY A 1 172 ? -36.025 4.206 9.496 1.00 79.38 ? 203 GLY A C 1 ATOM 1342 O O . GLY A 1 172 ? -36.551 5.256 9.136 1.00 73.06 ? 203 GLY A O 1 ATOM 1343 N N . PHE A 1 173 ? -34.723 4.101 9.733 1.00 63.53 ? 204 PHE A N 1 ATOM 1344 C CA . PHE A 1 173 ? -33.831 5.232 9.517 1.00 72.27 ? 204 PHE A CA 1 ATOM 1345 C C . PHE A 1 173 ? -32.614 4.799 8.699 1.00 60.39 ? 204 PHE A C 1 ATOM 1346 O O . PHE A 1 173 ? -31.968 3.818 9.036 1.00 59.26 ? 204 PHE A O 1 ATOM 1347 C CB . PHE A 1 173 ? -33.461 5.884 10.855 1.00 69.47 ? 204 PHE A CB 1 ATOM 1348 C CG . PHE A 1 173 ? -34.656 6.428 11.605 1.00 85.44 ? 204 PHE A CG 1 ATOM 1349 C CD1 . PHE A 1 173 ? -35.170 7.675 11.309 1.00 89.35 ? 204 PHE A CD1 1 ATOM 1350 C CD2 . PHE A 1 173 ? -35.283 5.678 12.577 1.00 84.85 ? 204 PHE A CD2 1 ATOM 1351 C CE1 . PHE A 1 173 ? -36.275 8.163 11.985 1.00 71.57 ? 204 PHE A CE1 1 ATOM 1352 C CE2 . PHE A 1 173 ? -36.386 6.161 13.241 1.00 73.03 ? 204 PHE A CE2 1 ATOM 1353 C CZ . PHE A 1 173 ? -36.878 7.407 12.940 1.00 60.26 ? 204 PHE A CZ 1 ATOM 1354 N N . HIS A 1 174 ? -32.306 5.524 7.628 1.00 109.94 ? 205 HIS A N 1 ATOM 1355 C CA . HIS A 1 174 ? -31.179 5.159 6.776 1.00 132.01 ? 205 HIS A CA 1 ATOM 1356 C C . HIS A 1 174 ? -30.288 6.366 6.464 1.00 126.98 ? 205 HIS A C 1 ATOM 1357 O O . HIS A 1 174 ? -30.589 7.488 6.880 1.00 125.45 ? 205 HIS A O 1 ATOM 1358 C CB . HIS A 1 174 ? -31.681 4.484 5.476 1.00 147.25 ? 205 HIS A CB 1 ATOM 1359 C CG . HIS A 1 174 ? -32.455 5.384 4.554 1.00 154.44 ? 205 HIS A CG 1 ATOM 1360 N ND1 . HIS A 1 174 ? -33.814 5.216 4.356 1.00 155.76 ? 205 HIS A ND1 1 ATOM 1361 C CD2 . HIS A 1 174 ? -32.028 6.412 3.781 1.00 160.70 ? 205 HIS A CD2 1 ATOM 1362 C CE1 . HIS A 1 174 ? -34.169 6.147 3.485 1.00 160.00 ? 205 HIS A CE1 1 ATOM 1363 N NE2 . HIS A 1 174 ? -33.131 6.899 3.121 1.00 167.06 ? 205 HIS A NE2 1 ATOM 1364 N N . GLY A 1 175 ? -29.223 6.121 5.707 1.00 111.59 ? 206 GLY A N 1 ATOM 1365 C CA . GLY A 1 175 ? -28.299 7.159 5.274 1.00 124.01 ? 206 GLY A CA 1 ATOM 1366 C C . GLY A 1 175 ? -27.070 7.347 6.144 1.00 118.56 ? 206 GLY A C 1 ATOM 1367 O O . GLY A 1 175 ? -26.908 6.655 7.157 1.00 102.22 ? 206 GLY A O 1 ATOM 1368 N N . PRO A 1 176 ? -26.193 8.311 5.761 1.00 112.10 ? 207 PRO A N 1 ATOM 1369 C CA . PRO A 1 176 ? -24.957 8.546 6.530 1.00 104.31 ? 207 PRO A CA 1 ATOM 1370 C C . PRO A 1 176 ? -25.125 9.003 7.979 1.00 85.85 ? 207 PRO A C 1 ATOM 1371 O O . PRO A 1 176 ? -24.241 8.729 8.785 1.00 78.98 ? 207 PRO A O 1 ATOM 1372 C CB . PRO A 1 176 ? -24.217 9.601 5.698 1.00 110.89 ? 207 PRO A CB 1 ATOM 1373 C CG . PRO A 1 176 ? -25.279 10.275 4.899 1.00 100.59 ? 207 PRO A CG 1 ATOM 1374 C CD . PRO A 1 176 ? -26.255 9.189 4.573 1.00 108.62 ? 207 PRO A CD 1 ATOM 1375 N N . HIS A 1 177 ? -26.224 9.711 8.306 1.00 75.33 ? 208 HIS A N 1 ATOM 1376 C CA . HIS A 1 177 ? -26.453 10.213 9.666 1.00 99.87 ? 208 HIS A CA 1 ATOM 1377 C C . HIS A 1 177 ? -27.783 9.756 10.295 1.00 110.20 ? 208 HIS A C 1 ATOM 1378 O O . HIS A 1 177 ? -28.168 10.291 11.338 1.00 122.45 ? 208 HIS A O 1 ATOM 1379 C CB . HIS A 1 177 ? -26.321 11.748 9.722 1.00 101.21 ? 208 HIS A CB 1 ATOM 1380 C CG . HIS A 1 177 ? -25.167 12.294 8.944 1.00 104.28 ? 208 HIS A CG 1 ATOM 1381 N ND1 . HIS A 1 177 ? -23.886 12.294 9.460 1.00 102.88 ? 208 HIS A ND1 1 ATOM 1382 C CD2 . HIS A 1 177 ? -25.143 12.831 7.703 1.00 114.23 ? 208 HIS A CD2 1 ATOM 1383 C CE1 . HIS A 1 177 ? -23.123 12.830 8.521 1.00 111.73 ? 208 HIS A CE1 1 ATOM 1384 N NE2 . HIS A 1 177 ? -23.835 13.168 7.446 1.00 116.62 ? 208 HIS A NE2 1 ATOM 1385 N N . CYS A 1 178 ? -28.454 8.742 9.693 1.00 99.90 ? 209 CYS A N 1 ATOM 1386 C CA . CYS A 1 178 ? -29.744 8.173 10.137 1.00 104.86 ? 209 CYS A CA 1 ATOM 1387 C C . CYS A 1 178 ? -30.881 9.211 10.065 1.00 89.36 ? 209 CYS A C 1 ATOM 1388 O O . CYS A 1 178 ? -31.667 9.346 11.005 1.00 87.98 ? 209 CYS A O 1 ATOM 1389 C CB . CYS A 1 178 ? -29.645 7.534 11.526 1.00 105.71 ? 209 CYS A CB 1 ATOM 1390 S SG . CYS A 1 178 ? -28.099 6.642 11.838 1.00 87.02 ? 209 CYS A SG 1 ATOM 1391 N N . GLU A 1 179 ? -30.959 9.941 8.942 1.00 67.71 ? 210 GLU A N 1 ATOM 1392 C CA . GLU A 1 179 ? -31.964 10.986 8.733 1.00 79.21 ? 210 GLU A CA 1 ATOM 1393 C C . GLU A 1 179 ? -33.133 10.515 7.863 1.00 90.49 ? 210 GLU A C 1 ATOM 1394 O O . GLU A 1 179 ? -34.287 10.783 8.206 1.00 95.60 ? 210 GLU A O 1 ATOM 1395 C CB . GLU A 1 179 ? -31.319 12.260 8.156 1.00 83.62 ? 210 GLU A CB 1 ATOM 1396 C CG . GLU A 1 179 ? -30.378 12.969 9.118 1.00 84.26 ? 210 GLU A CG 1 ATOM 1397 C CD . GLU A 1 179 ? -29.345 13.870 8.467 1.00 97.68 ? 210 GLU A CD 1 ATOM 1398 O OE1 . GLU A 1 179 ? -28.493 13.351 7.710 1.00 98.92 ? 210 GLU A OE1 1 ATOM 1399 O OE2 . GLU A 1 179 ? -29.368 15.092 8.740 1.00 95.24 ? 210 GLU A OE2 1 ATOM 1400 N N . GLY A 1 180 ? -32.820 9.812 6.768 1.00 103.32 ? 211 GLY A N 1 ATOM 1401 C CA . GLY A 1 180 ? -33.785 9.293 5.799 1.00 110.99 ? 211 GLY A CA 1 ATOM 1402 C C . GLY A 1 180 ? -34.776 8.278 6.336 1.00 110.87 ? 211 GLY A C 1 ATOM 1403 O O . GLY A 1 180 ? -34.559 7.705 7.406 1.00 80.35 ? 211 GLY A O 1 ATOM 1404 N N . THR A 1 181 ? -35.882 8.057 5.590 1.00 109.11 ? 212 THR A N 1 ATOM 1405 C CA . THR A 1 181 ? -36.947 7.110 5.952 1.00 104.38 ? 212 THR A CA 1 ATOM 1406 C C . THR A 1 181 ? -37.264 6.110 4.839 1.00 96.11 ? 212 THR A C 1 ATOM 1407 O O . THR A 1 181 ? -37.441 6.495 3.684 1.00 95.91 ? 212 THR A O 1 ATOM 1408 C CB . THR A 1 181 ? -38.208 7.829 6.464 1.00 103.23 ? 212 THR A CB 1 ATOM 1409 O OG1 . THR A 1 181 ? -38.501 8.947 5.625 1.00 120.17 ? 212 THR A OG1 1 ATOM 1410 C CG2 . THR A 1 181 ? -38.085 8.280 7.909 1.00 82.87 ? 212 THR A CG2 1 HETATM 1411 N N . PCF B 2 . ? 11.317 -14.530 13.768 1.00 76.01 ? 1213 PCF A N 1 HETATM 1412 P P . PCF B 2 . ? 8.655 -11.607 14.742 1.00 95.16 ? 1213 PCF A P 1 HETATM 1413 O O11 . PCF B 2 . ? 7.178 -11.931 15.295 1.00 108.51 ? 1213 PCF A O11 1 HETATM 1414 O O12 . PCF B 2 . ? 8.700 -11.839 13.254 1.00 111.09 ? 1213 PCF A O12 1 HETATM 1415 O O13 . PCF B 2 . ? 9.595 -12.724 15.421 1.00 78.45 ? 1213 PCF A O13 1 HETATM 1416 O O14 . PCF B 2 . ? 9.061 -10.265 15.296 1.00 83.33 ? 1213 PCF A O14 1 HETATM 1417 C C11 . PCF B 2 . ? 9.348 -14.121 15.268 1.00 57.63 ? 1213 PCF A C11 1 HETATM 1418 C C12 . PCF B 2 . ? 9.836 -14.604 13.912 1.00 72.63 ? 1213 PCF A C12 1 HETATM 1419 C C13 . PCF B 2 . ? 11.822 -15.767 13.158 1.00 83.35 ? 1213 PCF A C13 1 HETATM 1420 C C14 . PCF B 2 . ? 11.916 -14.355 15.095 1.00 68.77 ? 1213 PCF A C14 1 HETATM 1421 C C15 . PCF B 2 . ? 11.665 -13.387 12.917 1.00 77.20 ? 1213 PCF A C15 1 HETATM 1422 C C1 . PCF B 2 . ? 6.498 -10.923 16.040 1.00 73.56 ? 1213 PCF A C1 1 HETATM 1423 C C2 . PCF B 2 . ? 5.008 -11.219 16.180 1.00 37.10 ? 1213 PCF A C2 1 HETATM 1424 C C3 . PCF B 2 . ? 4.210 -10.075 15.578 1.00 62.62 ? 1213 PCF A C3 1 HETATM 1425 O O31 . PCF B 2 . ? 2.829 -10.288 15.854 1.00 75.24 ? 1213 PCF A O31 1 HETATM 1426 O O32 . PCF B 2 . ? 2.580 -8.238 16.898 1.00 83.46 ? 1213 PCF A O32 1 HETATM 1427 C C31 . PCF B 2 . ? 2.038 -9.254 16.497 1.00 73.12 ? 1213 PCF A C31 1 HETATM 1428 C C32 . PCF B 2 . ? 0.554 -9.447 16.665 1.00 54.16 ? 1213 PCF A C32 1 HETATM 1429 C C33 . PCF B 2 . ? 0.297 -10.060 18.030 1.00 32.01 ? 1213 PCF A C33 1 HETATM 1430 C C34 . PCF B 2 . ? -1.048 -10.786 18.062 1.00 43.78 ? 1213 PCF A C34 1 HETATM 1431 C C35 . PCF B 2 . ? -1.162 -11.908 17.035 1.00 41.05 ? 1213 PCF A C35 1 HETATM 1432 C C36 . PCF B 2 . ? -2.060 -13.019 17.573 1.00 42.45 ? 1213 PCF A C36 1 HETATM 1433 C C37 . PCF B 2 . ? -3.548 -12.786 17.314 1.00 32.44 ? 1213 PCF A C37 1 HETATM 1434 C C38 . PCF B 2 . ? -4.443 -13.944 17.770 1.00 24.81 ? 1213 PCF A C38 1 HETATM 1435 C C39 . PCF B 2 . ? -4.233 -15.279 17.052 1.00 33.65 ? 1213 PCF A C39 1 HETATM 1436 C C40 . PCF B 2 . ? -3.253 -16.114 17.873 1.00 32.38 ? 1213 PCF A C40 1 HETATM 1437 C C41 . PCF B 2 . ? -3.387 -17.611 17.588 1.00 31.67 ? 1213 PCF A C41 1 HETATM 1438 C C42 . PCF B 2 . ? -2.850 -17.965 16.201 1.00 56.66 ? 1213 PCF A C42 1 HETATM 1439 C C43 . PCF B 2 . ? -3.467 -19.243 15.626 1.00 41.56 ? 1213 PCF A C43 1 HETATM 1440 O O21 . PCF B 2 . ? 4.652 -12.436 15.528 1.00 60.22 ? 1213 PCF A O21 1 HETATM 1441 O O22 . PCF B 2 . ? 4.193 -13.291 17.607 1.00 70.28 ? 1213 PCF A O22 1 HETATM 1442 C C21 . PCF B 2 . ? 3.900 -13.300 16.424 1.00 63.05 ? 1213 PCF A C21 1 HETATM 1443 C C22 . PCF B 2 . ? 2.784 -14.187 15.914 1.00 44.45 ? 1213 PCF A C22 1 HETATM 1444 C C23 . PCF B 2 . ? 1.747 -14.392 17.015 1.00 45.11 ? 1213 PCF A C23 1 HETATM 1445 C C24 . PCF B 2 . ? 0.993 -15.713 16.889 1.00 30.43 ? 1213 PCF A C24 1 HETATM 1446 C C25 . PCF B 2 . ? 1.662 -16.811 17.722 1.00 44.78 ? 1213 PCF A C25 1 HETATM 1447 C C26 . PCF B 2 . ? 0.625 -17.708 18.401 1.00 39.07 ? 1213 PCF A C26 1 HETATM 1448 C C27 . PCF B 2 . ? 0.933 -19.208 18.377 1.00 38.85 ? 1213 PCF A C27 1 HETATM 1449 C C28 . PCF B 2 . ? -0.204 -20.082 17.832 1.00 42.30 ? 1213 PCF A C28 1 HETATM 1450 C C29 . PCF B 2 . ? 0.163 -21.544 17.563 1.00 39.14 ? 1213 PCF A C29 1 HETATM 1451 C C30 . PCF B 2 . ? -1.100 -22.363 17.294 1.00 29.81 ? 1213 PCF A C30 1 HETATM 1452 C C47 . PCF B 2 . ? -0.794 -23.832 16.991 1.00 28.97 ? 1213 PCF A C47 1 HETATM 1453 C C48 . PCF B 2 . ? -2.066 -24.603 16.637 1.00 26.61 ? 1213 PCF A C48 1 HETATM 1454 C C49 . PCF B 2 . ? -2.505 -24.468 15.170 1.00 20.05 ? 1213 PCF A C49 1 HETATM 1455 C C50 . PCF B 2 . ? -1.585 -25.179 14.158 1.00 15.80 ? 1213 PCF A C50 1 HETATM 1456 C C51 . PCF B 2 . ? -2.077 -24.985 12.719 1.00 17.28 ? 1213 PCF A C51 1 HETATM 1457 C C52 . PCF B 2 . ? -1.364 -25.830 11.673 1.00 33.85 ? 1213 PCF A C52 1 HETATM 1458 C C44 . PCF B 2 . ? -4.545 -18.967 14.579 1.00 34.96 ? 1213 PCF A C44 1 HETATM 1459 C C45 . PCF B 2 . ? -4.695 -20.105 13.567 1.00 41.67 ? 1213 PCF A C45 1 HETATM 1460 C C46 . PCF B 2 . ? -5.577 -19.740 12.383 1.00 28.80 ? 1213 PCF A C46 1 HETATM 1461 C C1 . NAG C 3 . ? -6.341 -10.768 4.108 1.00 28.96 ? 1214 NAG A C1 1 HETATM 1462 C C2 . NAG C 3 . ? -5.840 -9.590 3.291 1.00 28.13 ? 1214 NAG A C2 1 HETATM 1463 C C3 . NAG C 3 . ? -7.038 -9.095 2.477 1.00 43.72 ? 1214 NAG A C3 1 HETATM 1464 C C4 . NAG C 3 . ? -7.487 -10.257 1.578 1.00 48.52 ? 1214 NAG A C4 1 HETATM 1465 C C5 . NAG C 3 . ? -7.898 -11.435 2.479 1.00 38.98 ? 1214 NAG A C5 1 HETATM 1466 C C6 . NAG C 3 . ? -8.315 -12.655 1.638 1.00 38.83 ? 1214 NAG A C6 1 HETATM 1467 C C7 . NAG C 3 . ? -4.064 -8.252 4.379 1.00 27.84 ? 1214 NAG A C7 1 HETATM 1468 C C8 . NAG C 3 . ? -3.647 -7.169 5.332 1.00 27.45 ? 1214 NAG A C8 1 HETATM 1469 N N2 . NAG C 3 . ? -5.383 -8.530 4.204 1.00 25.84 ? 1214 NAG A N2 1 HETATM 1470 O O3 . NAG C 3 . ? -6.636 -7.984 1.675 1.00 35.66 ? 1214 NAG A O3 1 HETATM 1471 O O4 . NAG C 3 . ? -8.622 -9.847 0.807 1.00 43.05 ? 1214 NAG A O4 1 HETATM 1472 O O5 . NAG C 3 . ? -6.775 -11.841 3.264 1.00 31.48 ? 1214 NAG A O5 1 HETATM 1473 O O6 . NAG C 3 . ? -8.122 -12.419 0.243 1.00 68.55 ? 1214 NAG A O6 1 HETATM 1474 O O7 . NAG C 3 . ? -3.212 -8.854 3.764 1.00 35.48 ? 1214 NAG A O7 1 HETATM 1475 NA NA . NA D 4 . ? -25.134 9.470 17.793 1.00 127.33 1 1215 NA A NA 1 HETATM 1476 O O . HOH E 5 . ? 2.416 -35.759 7.539 1.00 31.73 ? 2001 HOH A O 1 HETATM 1477 O O . HOH E 5 . ? 2.492 -32.660 10.191 1.00 39.25 ? 2002 HOH A O 1 HETATM 1478 O O . HOH E 5 . ? -0.877 -33.339 5.293 1.00 26.15 ? 2003 HOH A O 1 HETATM 1479 O O . HOH E 5 . ? 5.180 -30.708 2.778 1.00 37.16 ? 2004 HOH A O 1 HETATM 1480 O O . HOH E 5 . ? 5.825 -21.996 8.242 1.00 31.41 ? 2005 HOH A O 1 HETATM 1481 O O . HOH E 5 . ? 1.908 -16.727 1.745 1.00 24.48 ? 2006 HOH A O 1 HETATM 1482 O O . HOH E 5 . ? -1.205 -14.939 6.147 1.00 15.74 ? 2007 HOH A O 1 HETATM 1483 O O . HOH E 5 . ? -2.861 -11.340 3.643 1.00 39.29 ? 2008 HOH A O 1 HETATM 1484 O O . HOH E 5 . ? 3.792 -14.798 1.390 1.00 29.66 ? 2009 HOH A O 1 HETATM 1485 O O . HOH E 5 . ? -6.344 -8.868 7.537 1.00 35.20 ? 2010 HOH A O 1 HETATM 1486 O O . HOH E 5 . ? -4.412 -6.547 8.976 1.00 24.35 ? 2011 HOH A O 1 HETATM 1487 O O . HOH E 5 . ? 3.568 -33.657 12.435 1.00 35.17 ? 2012 HOH A O 1 HETATM 1488 O O . HOH E 5 . ? 3.820 -1.148 7.973 1.00 33.96 ? 2013 HOH A O 1 HETATM 1489 O O . HOH E 5 . ? 1.829 -3.210 15.319 1.00 47.87 ? 2014 HOH A O 1 HETATM 1490 O O . HOH E 5 . ? 8.031 -10.134 9.100 1.00 28.81 ? 2015 HOH A O 1 HETATM 1491 O O . HOH E 5 . ? 10.509 -5.160 4.581 1.00 32.81 ? 2016 HOH A O 1 HETATM 1492 O O . HOH E 5 . ? 5.837 -28.124 22.121 1.00 62.19 ? 2017 HOH A O 1 HETATM 1493 O O . HOH E 5 . ? 8.730 -13.898 2.556 1.00 32.76 ? 2018 HOH A O 1 HETATM 1494 O O . HOH E 5 . ? 9.686 -16.442 10.439 1.00 34.30 ? 2019 HOH A O 1 HETATM 1495 O O . HOH E 5 . ? 10.085 -13.429 9.849 1.00 38.92 ? 2020 HOH A O 1 HETATM 1496 O O . HOH E 5 . ? 10.560 -15.982 6.489 1.00 42.61 ? 2021 HOH A O 1 HETATM 1497 O O . HOH E 5 . ? 5.793 -17.549 0.768 1.00 32.38 ? 2022 HOH A O 1 HETATM 1498 O O . HOH E 5 . ? 9.002 -18.130 3.425 1.00 36.07 ? 2023 HOH A O 1 HETATM 1499 O O . HOH E 5 . ? 4.018 -28.999 20.177 1.00 40.63 ? 2024 HOH A O 1 HETATM 1500 O O . HOH E 5 . ? 9.635 -18.194 12.912 1.00 34.10 ? 2025 HOH A O 1 HETATM 1501 O O . HOH E 5 . ? 4.212 -24.992 22.689 1.00 51.27 ? 2026 HOH A O 1 HETATM 1502 O O . HOH E 5 . ? 9.037 -22.588 11.552 1.00 37.41 ? 2027 HOH A O 1 HETATM 1503 O O . HOH E 5 . ? 9.667 -25.059 12.870 1.00 38.11 ? 2028 HOH A O 1 HETATM 1504 O O . HOH E 5 . ? 6.336 -28.763 17.783 1.00 26.91 ? 2029 HOH A O 1 HETATM 1505 O O . HOH E 5 . ? 11.762 -18.893 15.178 1.00 33.68 ? 2030 HOH A O 1 HETATM 1506 O O . HOH E 5 . ? 12.140 -19.690 22.231 1.00 35.03 ? 2031 HOH A O 1 HETATM 1507 O O . HOH E 5 . ? 11.312 -16.889 22.659 1.00 35.13 ? 2032 HOH A O 1 HETATM 1508 O O . HOH E 5 . ? 5.293 -22.968 23.817 1.00 34.97 ? 2033 HOH A O 1 HETATM 1509 O O . HOH E 5 . ? 6.669 -24.087 21.081 1.00 48.31 ? 2034 HOH A O 1 HETATM 1510 O O . HOH E 5 . ? -7.116 -39.954 7.439 1.00 23.50 ? 2035 HOH A O 1 HETATM 1511 O O . HOH E 5 . ? 7.437 -19.555 28.868 1.00 23.07 ? 2036 HOH A O 1 HETATM 1512 O O . HOH E 5 . ? 14.481 -18.536 26.173 1.00 45.24 ? 2037 HOH A O 1 HETATM 1513 O O . HOH E 5 . ? -13.464 -23.250 5.401 1.00 39.57 ? 2038 HOH A O 1 HETATM 1514 O O . HOH E 5 . ? 9.514 -21.350 29.962 1.00 47.12 ? 2039 HOH A O 1 HETATM 1515 O O . HOH E 5 . ? -16.718 -19.741 19.463 1.00 31.89 ? 2040 HOH A O 1 HETATM 1516 O O . HOH E 5 . ? -20.911 -7.119 22.184 1.00 50.15 ? 2041 HOH A O 1 HETATM 1517 O O . HOH E 5 . ? 7.365 -12.965 19.648 1.00 38.34 ? 2042 HOH A O 1 HETATM 1518 O O . HOH E 5 . ? 1.980 -9.455 25.099 1.00 36.52 ? 2043 HOH A O 1 HETATM 1519 O O . HOH E 5 . ? -0.294 -14.911 28.558 1.00 50.96 ? 2044 HOH A O 1 HETATM 1520 O O . HOH E 5 . ? -19.794 -11.622 20.657 1.00 42.06 ? 2045 HOH A O 1 HETATM 1521 O O . HOH E 5 . ? -18.554 -14.177 18.283 1.00 45.28 ? 2046 HOH A O 1 HETATM 1522 O O . HOH E 5 . ? -12.583 -10.912 9.980 1.00 50.59 ? 2047 HOH A O 1 HETATM 1523 O O . HOH E 5 . ? 4.867 -6.180 23.838 1.00 48.09 ? 2048 HOH A O 1 HETATM 1524 O O . HOH E 5 . ? 7.368 -6.746 29.958 1.00 47.96 ? 2049 HOH A O 1 HETATM 1525 O O . HOH E 5 . ? -0.893 -9.259 21.649 1.00 26.07 ? 2050 HOH A O 1 HETATM 1526 O O . HOH E 5 . ? 0.920 -1.418 19.734 1.00 41.20 ? 2051 HOH A O 1 HETATM 1527 O O . HOH E 5 . ? -2.886 1.670 17.854 1.00 26.25 ? 2052 HOH A O 1 HETATM 1528 O O . HOH E 5 . ? -9.493 -1.309 15.749 1.00 27.79 ? 2053 HOH A O 1 HETATM 1529 O O . HOH E 5 . ? -7.956 -0.365 8.604 1.00 55.11 ? 2054 HOH A O 1 HETATM 1530 O O . HOH E 5 . ? -9.175 1.323 30.098 0.50 74.00 ? 2055 HOH A O 1 HETATM 1531 O O . HOH E 5 . ? -7.810 -4.257 9.023 1.00 36.36 ? 2056 HOH A O 1 HETATM 1532 O O . HOH E 5 . ? -11.005 -3.487 15.392 1.00 33.25 ? 2057 HOH A O 1 HETATM 1533 O O . HOH E 5 . ? -12.456 0.629 8.496 1.00 50.37 ? 2058 HOH A O 1 HETATM 1534 O O . HOH E 5 . ? -8.694 -10.081 6.955 1.00 46.01 ? 2059 HOH A O 1 HETATM 1535 O O . HOH E 5 . ? -6.420 -26.794 24.731 1.00 45.77 ? 2060 HOH A O 1 HETATM 1536 O O . HOH E 5 . ? -1.142 -16.497 2.152 1.00 22.98 ? 2061 HOH A O 1 HETATM 1537 O O . HOH E 5 . ? -9.133 -22.968 5.879 1.00 22.11 ? 2062 HOH A O 1 HETATM 1538 O O . HOH E 5 . ? -3.375 -34.836 0.195 1.00 48.83 ? 2063 HOH A O 1 HETATM 1539 O O . HOH E 5 . ? 2.494 -37.078 1.863 1.00 52.84 ? 2064 HOH A O 1 HETATM 1540 O O . HOH E 5 . ? 1.406 -36.918 4.780 1.00 48.04 ? 2065 HOH A O 1 HETATM 1541 O O . HOH E 5 . ? -4.530 -39.440 7.674 1.00 38.23 ? 2066 HOH A O 1 HETATM 1542 O O . HOH E 5 . ? -3.447 -37.786 10.400 1.00 14.39 ? 2067 HOH A O 1 HETATM 1543 O O . HOH E 5 . ? -9.329 -33.068 2.686 1.00 34.84 ? 2068 HOH A O 1 HETATM 1544 O O . HOH E 5 . ? -6.012 -32.365 6.229 1.00 17.96 ? 2069 HOH A O 1 HETATM 1545 O O . HOH E 5 . ? -0.702 -38.138 10.702 1.00 40.88 ? 2070 HOH A O 1 HETATM 1546 O O . HOH E 5 . ? 3.106 -37.329 9.743 1.00 50.94 ? 2071 HOH A O 1 HETATM 1547 O O . HOH E 5 . ? -11.973 -24.710 7.018 1.00 28.37 ? 2072 HOH A O 1 HETATM 1548 O O . HOH E 5 . ? -15.639 -30.914 20.128 1.00 39.86 ? 2073 HOH A O 1 HETATM 1549 O O . HOH E 5 . ? -15.526 -25.656 19.768 1.00 43.72 ? 2074 HOH A O 1 HETATM 1550 O O . HOH E 5 . ? -16.418 -21.872 22.573 1.00 51.32 ? 2075 HOH A O 1 HETATM 1551 O O . HOH E 5 . ? -15.405 -19.381 22.738 1.00 39.35 ? 2076 HOH A O 1 HETATM 1552 O O . HOH E 5 . ? -16.768 -17.175 20.723 1.00 38.93 ? 2077 HOH A O 1 HETATM 1553 O O . HOH E 5 . ? -16.929 -17.143 24.413 1.00 52.71 ? 2078 HOH A O 1 HETATM 1554 O O . HOH E 5 . ? -14.995 -12.278 29.386 1.00 44.59 ? 2079 HOH A O 1 HETATM 1555 O O . HOH E 5 . ? -12.900 -10.807 32.166 1.00 49.80 ? 2080 HOH A O 1 HETATM 1556 O O . HOH E 5 . ? -15.003 -8.747 30.422 1.00 38.39 ? 2081 HOH A O 1 HETATM 1557 O O . HOH E 5 . ? -12.592 -3.964 30.934 1.00 32.40 ? 2082 HOH A O 1 HETATM 1558 O O . HOH E 5 . ? -14.874 -4.752 29.712 1.00 31.40 ? 2083 HOH A O 1 HETATM 1559 O O . HOH E 5 . ? -19.119 -7.821 24.144 1.00 48.54 ? 2084 HOH A O 1 HETATM 1560 O O . HOH E 5 . ? -15.561 -0.260 23.293 1.00 25.06 ? 2085 HOH A O 1 HETATM 1561 O O . HOH E 5 . ? -13.748 0.346 21.121 1.00 29.78 ? 2086 HOH A O 1 HETATM 1562 O O . HOH E 5 . ? -18.671 -10.825 22.980 1.00 37.82 ? 2087 HOH A O 1 HETATM 1563 O O . HOH E 5 . ? -17.937 -11.563 18.415 1.00 23.23 ? 2088 HOH A O 1 HETATM 1564 O O . HOH E 5 . ? -16.481 -15.693 18.322 1.00 21.60 ? 2089 HOH A O 1 HETATM 1565 O O . HOH E 5 . ? -13.228 -13.199 11.074 1.00 22.91 ? 2090 HOH A O 1 HETATM 1566 O O . HOH E 5 . ? -16.032 -17.090 14.740 1.00 17.45 ? 2091 HOH A O 1 HETATM 1567 O O . HOH E 5 . ? -16.761 -19.354 12.771 1.00 28.49 ? 2092 HOH A O 1 HETATM 1568 O O . HOH E 5 . ? -15.853 -13.801 10.687 1.00 34.16 ? 2093 HOH A O 1 HETATM 1569 O O . HOH E 5 . ? -13.073 -19.396 4.811 1.00 29.09 ? 2094 HOH A O 1 HETATM 1570 O O . HOH E 5 . ? -14.596 -14.373 4.957 1.00 45.32 ? 2095 HOH A O 1 HETATM 1571 O O . HOH E 5 . ? -10.037 -16.236 4.094 1.00 30.24 ? 2096 HOH A O 1 HETATM 1572 O O . HOH E 5 . ? -18.820 -23.016 13.154 1.00 16.43 ? 2097 HOH A O 1 HETATM 1573 O O . HOH E 5 . ? -16.128 -27.993 8.735 1.00 17.82 ? 2098 HOH A O 1 HETATM 1574 O O . HOH E 5 . ? -13.820 -28.721 7.085 1.00 21.75 ? 2099 HOH A O 1 HETATM 1575 O O . HOH E 5 . ? -11.332 -27.041 5.656 1.00 39.59 ? 2100 HOH A O 1 HETATM 1576 O O . HOH E 5 . ? -10.438 -28.976 2.767 1.00 53.10 ? 2101 HOH A O 1 HETATM 1577 O O . HOH E 5 . ? -8.382 -30.221 1.574 1.00 27.39 ? 2102 HOH A O 1 HETATM 1578 O O . HOH E 5 . ? -7.802 -28.104 -0.042 1.00 28.69 ? 2103 HOH A O 1 HETATM 1579 O O . HOH E 5 . ? -3.816 -19.161 -0.020 1.00 29.75 ? 2104 HOH A O 1 HETATM 1580 O O . HOH E 5 . ? -7.626 -18.695 0.920 1.00 19.37 ? 2105 HOH A O 1 HETATM 1581 O O . HOH E 5 . ? -10.049 -20.439 4.757 1.00 28.63 ? 2106 HOH A O 1 HETATM 1582 O O . HOH E 5 . ? -10.871 0.566 17.579 1.00 25.31 ? 2107 HOH A O 1 HETATM 1583 O O . HOH E 5 . ? -20.908 -2.038 18.743 1.00 54.56 ? 2108 HOH A O 1 HETATM 1584 O O . HOH E 5 . ? -11.455 1.625 28.632 1.00 30.63 ? 2109 HOH A O 1 HETATM 1585 O O . HOH E 5 . ? -13.104 5.193 26.971 1.00 39.13 ? 2110 HOH A O 1 HETATM 1586 O O . HOH E 5 . ? -8.389 4.406 28.340 1.00 48.22 ? 2111 HOH A O 1 HETATM 1587 O O . HOH E 5 . ? -7.663 5.713 21.518 1.00 66.01 ? 2112 HOH A O 1 HETATM 1588 O O . HOH E 5 . ? -6.297 0.062 28.377 1.00 34.21 ? 2113 HOH A O 1 HETATM 1589 O O . HOH E 5 . ? -5.171 -17.835 23.668 1.00 13.63 ? 2114 HOH A O 1 HETATM 1590 O O . HOH E 5 . ? -9.342 -23.590 26.043 1.00 42.56 ? 2115 HOH A O 1 HETATM 1591 O O . HOH E 5 . ? -5.915 -24.975 22.845 1.00 36.88 ? 2116 HOH A O 1 HETATM 1592 O O . HOH E 5 . ? -0.912 -40.097 17.313 1.00 48.87 ? 2117 HOH A O 1 HETATM 1593 O O . HOH E 5 . ? 0.676 -37.085 13.683 1.00 30.18 ? 2118 HOH A O 1 HETATM 1594 O O . HOH E 5 . ? -5.335 -42.939 11.288 1.00 31.04 ? 2119 HOH A O 1 HETATM 1595 O O . HOH E 5 . ? -7.454 -34.832 21.076 1.00 32.38 ? 2120 HOH A O 1 HETATM 1596 O O . HOH E 5 . ? -3.064 -43.309 19.646 1.00 46.17 ? 2121 HOH A O 1 HETATM 1597 O O . HOH E 5 . ? -4.250 -35.931 22.661 1.00 26.08 ? 2122 HOH A O 1 HETATM 1598 O O . HOH E 5 . ? -5.948 -31.494 23.640 1.00 39.40 ? 2123 HOH A O 1 HETATM 1599 O O . HOH E 5 . ? 3.699 -32.275 17.571 1.00 51.35 ? 2124 HOH A O 1 HETATM 1600 O O . HOH E 5 . ? 1.698 -27.226 20.184 1.00 34.91 ? 2125 HOH A O 1 HETATM 1601 O O . HOH E 5 . ? 1.588 -25.488 22.423 1.00 26.36 ? 2126 HOH A O 1 HETATM 1602 O O . HOH E 5 . ? -4.333 -24.316 24.555 1.00 35.57 ? 2127 HOH A O 1 HETATM 1603 O O . HOH E 5 . ? -1.197 -25.436 34.017 1.00 30.26 ? 2128 HOH A O 1 HETATM 1604 O O . HOH E 5 . ? -3.867 -23.489 33.982 1.00 33.53 ? 2129 HOH A O 1 HETATM 1605 O O . HOH E 5 . ? -5.020 -22.498 27.231 1.00 35.25 ? 2130 HOH A O 1 HETATM 1606 O O . HOH E 5 . ? -6.345 -21.632 33.282 1.00 48.59 ? 2131 HOH A O 1 HETATM 1607 O O . HOH E 5 . ? 0.393 -11.287 23.711 1.00 36.62 ? 2132 HOH A O 1 HETATM 1608 O O . HOH E 5 . ? -1.591 0.257 22.230 1.00 32.63 ? 2133 HOH A O 1 HETATM 1609 O O . HOH E 5 . ? -6.871 3.354 22.328 1.00 42.29 ? 2134 HOH A O 1 HETATM 1610 O O . HOH E 5 . ? -20.171 10.355 16.437 1.00 71.20 ? 2135 HOH A O 1 HETATM 1611 O O . HOH E 5 . ? -18.754 13.119 15.814 1.00 52.67 ? 2136 HOH A O 1 HETATM 1612 O O . HOH E 5 . ? -24.205 11.659 17.188 1.00 76.10 ? 2137 HOH A O 1 HETATM 1613 O O . HOH E 5 . ? -27.686 9.158 18.631 1.00 77.26 ? 2138 HOH A O 1 HETATM 1614 O O . HOH E 5 . ? -31.312 12.918 16.319 1.00 79.12 ? 2139 HOH A O 1 HETATM 1615 O O . HOH E 5 . ? -20.154 -0.227 9.667 1.00 69.74 ? 2140 HOH A O 1 HETATM 1616 O O . HOH E 5 . ? -20.442 8.223 8.721 1.00 66.06 ? 2141 HOH A O 1 HETATM 1617 O O . HOH E 5 . ? -13.434 10.509 9.897 1.00 57.98 ? 2142 HOH A O 1 HETATM 1618 O O . HOH E 5 . ? -27.390 3.580 7.956 1.00 64.77 ? 2143 HOH A O 1 HETATM 1619 O O . HOH E 5 . ? -28.343 1.307 9.512 1.00 65.73 ? 2144 HOH A O 1 HETATM 1620 O O . HOH E 5 . ? -28.637 2.646 4.392 1.00 80.80 ? 2145 HOH A O 1 HETATM 1621 O O . HOH E 5 . ? -28.588 10.716 6.903 1.00 60.02 ? 2146 HOH A O 1 HETATM 1622 O O . HOH E 5 . ? -36.127 11.100 4.148 1.00 91.89 ? 2147 HOH A O 1 HETATM 1623 O O . HOH E 5 . ? -40.918 8.481 4.546 1.00 63.72 ? 2148 HOH A O 1 HETATM 1624 O O . HOH E 5 . ? -9.665 -11.278 -1.493 1.00 37.42 ? 2149 HOH A O 1 HETATM 1625 O O . HOH E 5 . ? -7.976 -15.414 -0.287 1.00 73.95 ? 2150 HOH A O 1 HETATM 1626 O O . HOH E 5 . ? -23.980 9.117 19.863 1.00 49.42 ? 2151 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 2 ? 0.9964 0.9585 1.0019 0.0276 0.0244 -0.0478 33 THR A N 2 C CA . THR A 2 ? 1.0933 1.0401 1.0938 0.0274 0.0201 -0.0448 33 THR A CA 3 C C . THR A 2 ? 0.8731 0.8192 0.8676 0.0196 0.0168 -0.0410 33 THR A C 4 O O . THR A 2 ? 0.8981 0.8371 0.8845 0.0147 0.0153 -0.0416 33 THR A O 5 C CB . THR A 2 ? 1.1293 1.0704 1.1372 0.0351 0.0180 -0.0415 33 THR A CB 6 O OG1 . THR A 2 ? 1.0641 0.9903 1.0655 0.0332 0.0139 -0.0375 33 THR A OG1 7 C CG2 . THR A 2 ? 1.0465 1.0012 1.0660 0.0381 0.0165 -0.0375 33 THR A CG2 8 N N . GLY A 3 ? 0.6134 0.5680 0.6131 0.0186 0.0155 -0.0374 34 GLY A N 9 C CA . GLY A 3 ? 0.5067 0.4617 0.5013 0.0118 0.0129 -0.0338 34 GLY A CA 10 C C . GLY A 3 ? 0.4492 0.4116 0.4378 0.0052 0.0151 -0.0352 34 GLY A C 11 O O . GLY A 3 ? 0.5194 0.4902 0.5102 0.0059 0.0187 -0.0384 34 GLY A O 12 N N . SER A 4 ? 0.4162 0.3768 0.3980 -0.0010 0.0124 -0.0319 35 SER A N 13 C CA . SER A 4 ? 0.3566 0.3240 0.3337 -0.0067 0.0135 -0.0316 35 SER A CA 14 C C . SER A 4 ? 0.3388 0.3122 0.3149 -0.0112 0.0110 -0.0264 35 SER A C 15 O O . SER A 4 ? 0.3142 0.2934 0.2880 -0.0151 0.0116 -0.0252 35 SER A O 16 C CB . SER A 4 ? 0.4824 0.4442 0.4536 -0.0094 0.0136 -0.0331 35 SER A CB 17 O OG . SER A 4 ? 0.4110 0.3665 0.3803 -0.0110 0.0100 -0.0297 35 SER A OG 18 N N . LEU A 5 ? 0.2664 0.2379 0.2444 -0.0105 0.0079 -0.0230 36 LEU A N 19 C CA . LEU A 5 ? 0.2458 0.2232 0.2238 -0.0136 0.0054 -0.0181 36 LEU A CA 20 C C . LEU A 5 ? 0.2284 0.2140 0.2096 -0.0141 0.0064 -0.0180 36 LEU A C 21 O O . LEU A 5 ? 0.2022 0.1905 0.1885 -0.0107 0.0074 -0.0197 36 LEU A O 22 C CB . LEU A 5 ? 0.3250 0.2994 0.3042 -0.0130 0.0020 -0.0144 36 LEU A CB 23 C CG . LEU A 5 ? 0.3436 0.3131 0.3199 -0.0141 0.0007 -0.0128 36 LEU A CG 24 C CD1 . LEU A 5 ? 0.3883 0.3536 0.3658 -0.0129 -0.0017 -0.0105 36 LEU A CD1 25 C CD2 . LEU A 5 ? 0.3571 0.3324 0.3318 -0.0169 0.0002 -0.0094 36 LEU A CD2 26 N N . TYR A 6 ? 0.1834 0.1742 0.1637 -0.0171 0.0056 -0.0145 37 TYR A N 27 C CA . TYR A 6 ? 0.1513 0.1493 0.1343 -0.0183 0.0059 -0.0133 37 TYR A CA 28 C C . TYR A 6 ? 0.1432 0.1422 0.1267 -0.0185 0.0033 -0.0080 37 TYR A C 29 O O . TYR A 6 ? 0.1462 0.1434 0.1273 -0.0192 0.0027 -0.0058 37 TYR A O 30 C CB . TYR A 6 ? 0.1913 0.1941 0.1726 -0.0213 0.0087 -0.0150 37 TYR A CB 31 C CG . TYR A 6 ? 0.2225 0.2272 0.2048 -0.0195 0.0125 -0.0207 37 TYR A CG 32 C CD1 . TYR A 6 ? 0.2693 0.2690 0.2488 -0.0186 0.0142 -0.0238 37 TYR A CD1 33 C CD2 . TYR A 6 ? 0.2134 0.2260 0.2005 -0.0181 0.0146 -0.0227 37 TYR A CD2 34 C CE1 . TYR A 6 ? 0.3346 0.3360 0.3163 -0.0156 0.0179 -0.0289 37 TYR A CE1 35 C CE2 . TYR A 6 ? 0.3277 0.3439 0.3183 -0.0149 0.0184 -0.0273 37 TYR A CE2 36 C CZ . TYR A 6 ? 0.3478 0.3579 0.3356 -0.0134 0.0201 -0.0305 37 TYR A CZ 37 O OH . TYR A 6 ? 0.5456 0.5588 0.5372 -0.0097 0.0237 -0.0351 37 TYR A OH 38 N N . LEU A 7 ? 0.1290 0.1311 0.1159 -0.0174 0.0022 -0.0064 38 LEU A N 39 C CA . LEU A 7 ? 0.1040 0.1061 0.0912 -0.0161 0.0005 -0.0027 38 LEU A CA 40 C C . LEU A 7 ? 0.1917 0.1971 0.1802 -0.0166 0.0006 -0.0024 38 LEU A C 41 O O . LEU A 7 ? 0.1546 0.1628 0.1466 -0.0163 0.0009 -0.0039 38 LEU A O 42 C CB . LEU A 7 ? 0.1292 0.1295 0.1190 -0.0133 -0.0012 -0.0017 38 LEU A CB 43 C CG . LEU A 7 ? 0.1577 0.1582 0.1472 -0.0127 -0.0020 0.0006 38 LEU A CG 44 C CD1 . LEU A 7 ? 0.1817 0.1813 0.1681 -0.0138 -0.0024 0.0024 38 LEU A CD1 45 C CD2 . LEU A 7 ? 0.2107 0.2110 0.2023 -0.0111 -0.0028 0.0008 38 LEU A CD2 46 N N . TRP A 8 ? 0.1457 0.1509 0.1314 -0.0177 0.0001 -0.0005 39 TRP A N 47 C CA . TRP A 8 ? 0.1739 0.1810 0.1601 -0.0186 -0.0004 0.0000 39 TRP A CA 48 C C . TRP A 8 ? 0.1833 0.1881 0.1677 -0.0189 -0.0025 0.0027 39 TRP A C 49 O O . TRP A 8 ? 0.1730 0.1760 0.1566 -0.0183 -0.0035 0.0038 39 TRP A O 50 C CB . TRP A 8 ? 0.1493 0.1607 0.1331 -0.0221 0.0014 -0.0019 39 TRP A CB 51 C CG . TRP A 8 ? 0.1444 0.1555 0.1245 -0.0245 0.0013 -0.0016 39 TRP A CG 52 C CD1 . TRP A 8 ? 0.1748 0.1865 0.1527 -0.0268 -0.0002 0.0000 39 TRP A CD1 53 C CD2 . TRP A 8 ? 0.1979 0.2083 0.1766 -0.0253 0.0026 -0.0031 39 TRP A CD2 54 N NE1 . TRP A 8 ? 0.1875 0.1993 0.1629 -0.0289 -0.0003 -0.0002 39 TRP A NE1 55 C CE2 . TRP A 8 ? 0.1329 0.1441 0.1087 -0.0282 0.0015 -0.0025 39 TRP A CE2 56 C CE3 . TRP A 8 ? 0.2451 0.2542 0.2247 -0.0249 0.0045 -0.0049 39 TRP A CE3 57 C CZ2 . TRP A 8 ? 0.2285 0.2397 0.2038 -0.0310 0.0022 -0.0039 39 TRP A CZ2 58 C CZ3 . TRP A 8 ? 0.2410 0.2494 0.2189 -0.0276 0.0058 -0.0061 39 TRP A CZ3 59 C CH2 . TRP A 8 ? 0.2697 0.2794 0.2457 -0.0306 0.0049 -0.0053 39 TRP A CH2 60 N N . ILE A 9 ? 0.1307 0.1359 0.1162 -0.0196 -0.0032 0.0034 40 ILE A N 61 C CA . ILE A 9 ? 0.1306 0.1335 0.1150 -0.0207 -0.0055 0.0058 40 ILE A CA 62 C C . ILE A 9 ? 0.1945 0.1993 0.1756 -0.0242 -0.0058 0.0065 40 ILE A C 63 O O . ILE A 9 ? 0.1907 0.1980 0.1725 -0.0255 -0.0044 0.0055 40 ILE A O 64 C CB . ILE A 9 ? 0.1489 0.1499 0.1368 -0.0196 -0.0063 0.0060 40 ILE A CB 65 C CG1 . ILE A 9 ? 0.1967 0.1967 0.1875 -0.0167 -0.0061 0.0049 40 ILE A CG1 66 C CG2 . ILE A 9 ? 0.1406 0.1386 0.1282 -0.0210 -0.0088 0.0084 40 ILE A CG2 67 C CD1 . ILE A 9 ? 0.2781 0.2776 0.2721 -0.0161 -0.0060 0.0037 40 ILE A CD1 68 N N . ASP A 10 ? 0.1459 0.1500 0.1241 -0.0259 -0.0076 0.0082 41 ASP A N 69 C CA . ASP A 10 ? 0.1785 0.1849 0.1535 -0.0302 -0.0081 0.0089 41 ASP A CA 70 C C . ASP A 10 ? 0.2609 0.2666 0.2356 -0.0324 -0.0094 0.0107 41 ASP A C 71 O O . ASP A 10 ? 0.1924 0.1943 0.1704 -0.0305 -0.0105 0.0119 41 ASP A O 72 C CB . ASP A 10 ? 0.2212 0.2271 0.1951 -0.0316 -0.0100 0.0105 41 ASP A CB 73 C CG . ASP A 10 ? 0.3951 0.3979 0.3705 -0.0315 -0.0138 0.0140 41 ASP A CG 74 O OD1 . ASP A 10 ? 0.3070 0.3089 0.2808 -0.0347 -0.0163 0.0166 41 ASP A OD1 75 O OD2 . ASP A 10 ? 0.2920 0.2935 0.2703 -0.0287 -0.0144 0.0142 41 ASP A OD2 76 N N . ALA A 11 ? 0.2033 0.2125 0.1750 -0.0364 -0.0085 0.0104 42 ALA A N 77 C CA . ALA A 11 ? 0.2152 0.2241 0.1870 -0.0391 -0.0091 0.0121 42 ALA A CA 78 C C . ALA A 11 ? 0.2654 0.2686 0.2375 -0.0398 -0.0126 0.0159 42 ALA A C 79 O O . ALA A 11 ? 0.2862 0.2862 0.2606 -0.0397 -0.0128 0.0166 42 ALA A O 80 C CB . ALA A 11 ? 0.2392 0.2537 0.2069 -0.0442 -0.0080 0.0116 42 ALA A CB 81 N N . HIS A 12 ? 0.2089 0.2106 0.1794 -0.0407 -0.0156 0.0182 43 HIS A N 82 C CA . HIS A 12 ? 0.2654 0.2618 0.2375 -0.0412 -0.0193 0.0220 43 HIS A CA 83 C C . HIS A 12 ? 0.2820 0.2735 0.2594 -0.0365 -0.0195 0.0214 43 HIS A C 84 O O . HIS A 12 ? 0.2338 0.2199 0.2132 -0.0366 -0.0206 0.0229 43 HIS A O 85 C CB . HIS A 12 ? 0.2884 0.2857 0.2589 -0.0435 -0.0227 0.0247 43 HIS A CB 86 C CG . HIS A 12 ? 0.3864 0.3779 0.3592 -0.0441 -0.0266 0.0292 43 HIS A CG 87 N ND1 . HIS A 12 ? 0.5534 0.5427 0.5308 -0.0413 -0.0290 0.0307 43 HIS A ND1 88 C CD2 . HIS A 12 ? 0.4305 0.4178 0.4020 -0.0470 -0.0284 0.0324 43 HIS A CD2 89 C CE1 . HIS A 12 ? 0.3536 0.3370 0.3326 -0.0420 -0.0320 0.0347 43 HIS A CE1 90 N NE2 . HIS A 12 ? 0.5308 0.5123 0.5060 -0.0455 -0.0319 0.0360 43 HIS A NE2 91 N N . GLN A 13 ? 0.2237 0.2169 0.2032 -0.0328 -0.0182 0.0192 44 GLN A N 92 C CA . GLN A 13 ? 0.2190 0.2088 0.2034 -0.0288 -0.0180 0.0180 44 GLN A CA 93 C C . GLN A 13 ? 0.2804 0.2690 0.2667 -0.0280 -0.0154 0.0156 44 GLN A C 94 O O . GLN A 13 ? 0.2083 0.1922 0.1978 -0.0268 -0.0160 0.0153 44 GLN A O 95 C CB . GLN A 13 ? 0.1985 0.1911 0.1837 -0.0258 -0.0170 0.0162 44 GLN A CB 96 C CG . GLN A 13 ? 0.2106 0.2008 0.2005 -0.0222 -0.0164 0.0146 44 GLN A CG 97 C CD . GLN A 13 ? 0.2633 0.2494 0.2570 -0.0218 -0.0199 0.0170 44 GLN A CD 98 O OE1 . GLN A 13 ? 0.2462 0.2336 0.2414 -0.0214 -0.0222 0.0187 44 GLN A OE1 99 N NE2 . GLN A 13 ? 0.2742 0.2550 0.2698 -0.0220 -0.0205 0.0174 44 GLN A NE2 100 N N . ALA A 14 ? 0.1789 0.1718 0.1634 -0.0290 -0.0128 0.0137 45 ALA A N 101 C CA . ALA A 14 ? 0.1702 0.1637 0.1565 -0.0292 -0.0110 0.0118 45 ALA A CA 102 C C . ALA A 14 ? 0.1835 0.1729 0.1695 -0.0323 -0.0123 0.0135 45 ALA A C 103 O O . ALA A 14 ? 0.2684 0.2551 0.2570 -0.0319 -0.0120 0.0122 45 ALA A O 104 C CB . ALA A 14 ? 0.2101 0.2098 0.1948 -0.0303 -0.0086 0.0102 45 ALA A CB 105 N N . ARG A 15 ? 0.2490 0.2376 0.2315 -0.0357 -0.0140 0.0165 46 ARG A N 106 C CA . ARG A 15 ? 0.3608 0.3446 0.3424 -0.0392 -0.0156 0.0188 46 ARG A CA 107 C C . ARG A 15 ? 0.3482 0.3235 0.3329 -0.0372 -0.0176 0.0195 46 ARG A C 108 O O . ARG A 15 ? 0.2763 0.2474 0.2625 -0.0381 -0.0172 0.0186 46 ARG A O 109 C CB . ARG A 15 ? 0.2422 0.2271 0.2187 -0.0437 -0.0176 0.0222 46 ARG A CB 110 C CG . ARG A 15 ? 0.4346 0.4148 0.4091 -0.0482 -0.0192 0.0250 46 ARG A CG 111 C CD . ARG A 15 ? 0.5413 0.5222 0.5109 -0.0527 -0.0217 0.0289 46 ARG A CD 112 N NE . ARG A 15 ? 1.0566 1.0285 1.0259 -0.0546 -0.0252 0.0331 46 ARG A NE 113 C CZ . ARG A 15 ? 1.1811 1.1475 1.1523 -0.0524 -0.0283 0.0357 46 ARG A CZ 114 N NH1 . ARG A 15 ? 1.2218 1.1916 1.1952 -0.0487 -0.0284 0.0346 46 ARG A NH1 115 N NH2 . ARG A 15 ? 1.0403 0.9978 1.0115 -0.0539 -0.0315 0.0396 46 ARG A NH2 116 N N . VAL A 16 ? 0.3542 0.3274 0.3405 -0.0346 -0.0196 0.0208 47 VAL A N 117 C CA . VAL A 16 ? 0.3733 0.3384 0.3633 -0.0322 -0.0213 0.0212 47 VAL A CA 118 C C . VAL A 16 ? 0.3564 0.3205 0.3501 -0.0294 -0.0188 0.0167 47 VAL A C 119 O O . VAL A 16 ? 0.3216 0.2783 0.3174 -0.0288 -0.0192 0.0158 47 VAL A O 120 C CB . VAL A 16 ? 0.4809 0.4442 0.4726 -0.0301 -0.0246 0.0242 47 VAL A CB 121 C CG1 . VAL A 16 ? 0.4914 0.4607 0.4795 -0.0327 -0.0260 0.0269 47 VAL A CG1 122 C CG2 . VAL A 16 ? 0.3642 0.3285 0.3605 -0.0256 -0.0240 0.0216 47 VAL A CG2 123 N N . LEU A 17 ? 0.2887 0.2599 0.2828 -0.0279 -0.0162 0.0137 48 LEU A N 124 C CA . LEU A 17 ? 0.3006 0.2726 0.2979 -0.0257 -0.0140 0.0096 48 LEU A CA 125 C C . LEU A 17 ? 0.3852 0.3578 0.3827 -0.0279 -0.0123 0.0073 48 LEU A C 126 O O . LEU A 17 ? 0.4429 0.4114 0.4427 -0.0276 -0.0118 0.0047 48 LEU A O 127 C CB . LEU A 17 ? 0.3000 0.2788 0.2978 -0.0230 -0.0125 0.0079 48 LEU A CB 128 C CG . LEU A 17 ? 0.4970 0.4777 0.4977 -0.0207 -0.0106 0.0041 48 LEU A CG 129 C CD1 . LEU A 17 ? 0.5411 0.5167 0.5442 -0.0188 -0.0117 0.0031 48 LEU A CD1 130 C CD2 . LEU A 17 ? 0.4712 0.4581 0.4711 -0.0190 -0.0096 0.0036 48 LEU A CD2 131 N N . ILE A 18 ? 0.2972 0.2750 0.2921 -0.0304 -0.0118 0.0083 49 ILE A N 132 C CA . ILE A 18 ? 0.3752 0.3552 0.3700 -0.0330 -0.0109 0.0067 49 ILE A CA 133 C C . ILE A 18 ? 0.2597 0.2386 0.2515 -0.0379 -0.0117 0.0091 49 ILE A C 134 O O . ILE A 18 ? 0.4730 0.4533 0.4648 -0.0406 -0.0112 0.0080 49 ILE A O 135 C CB . ILE A 18 ? 0.4316 0.4198 0.4271 -0.0316 -0.0092 0.0048 49 ILE A CB 136 C CG1 . ILE A 18 ? 0.4249 0.4185 0.4179 -0.0319 -0.0085 0.0064 49 ILE A CG1 137 C CG2 . ILE A 18 ? 0.7301 0.7188 0.7285 -0.0277 -0.0087 0.0023 49 ILE A CG2 138 C CD1 . ILE A 18 ? 0.7446 0.7450 0.7371 -0.0341 -0.0072 0.0058 49 ILE A CD1 139 N N . GLY A 19 ? 0.3073 0.2843 0.2961 -0.0395 -0.0131 0.0125 50 GLY A N 140 C CA . GLY A 19 ? 0.3660 0.3420 0.3513 -0.0447 -0.0140 0.0151 50 GLY A CA 141 C C . GLY A 19 ? 0.5667 0.5514 0.5487 -0.0474 -0.0129 0.0159 50 GLY A C 142 O O . GLY A 19 ? 0.6048 0.5894 0.5831 -0.0522 -0.0137 0.0183 50 GLY A O 143 N N . PHE A 20 ? 0.4285 0.4203 0.4116 -0.0446 -0.0109 0.0137 51 PHE A N 144 C CA . PHE A 20 ? 0.5436 0.5439 0.5245 -0.0466 -0.0092 0.0135 51 PHE A CA 145 C C . PHE A 20 ? 0.3323 0.3347 0.3114 -0.0449 -0.0090 0.0139 51 PHE A C 146 O O . PHE A 20 ? 0.2913 0.2932 0.2726 -0.0406 -0.0086 0.0125 51 PHE A O 147 C CB . PHE A 20 ? 0.4138 0.4212 0.3978 -0.0459 -0.0069 0.0106 51 PHE A CB 148 C CG . PHE A 20 ? 0.7968 0.8031 0.7814 -0.0491 -0.0074 0.0104 51 PHE A CG 149 C CD1 . PHE A 20 ? 0.5773 0.5859 0.5590 -0.0547 -0.0075 0.0120 51 PHE A CD1 150 C CD2 . PHE A 20 ? 0.7533 0.7559 0.7409 -0.0471 -0.0078 0.0087 51 PHE A CD2 151 C CE1 . PHE A 20 ? 0.6774 0.6844 0.6592 -0.0583 -0.0082 0.0120 51 PHE A CE1 152 C CE2 . PHE A 20 ? 0.5658 0.5669 0.5536 -0.0507 -0.0084 0.0084 51 PHE A CE2 153 C CZ . PHE A 20 ? 0.7956 0.7985 0.7804 -0.0563 -0.0086 0.0101 51 PHE A CZ 154 N N . GLU A 21 ? 0.3295 0.3343 0.3043 -0.0487 -0.0095 0.0157 52 GLU A N 155 C CA . GLU A 21 ? 0.3884 0.3955 0.3608 -0.0483 -0.0096 0.0160 52 GLU A CA 156 C C . GLU A 21 ? 0.5532 0.5687 0.5259 -0.0478 -0.0063 0.0126 52 GLU A C 157 O O . GLU A 21 ? 0.3583 0.3796 0.3278 -0.0517 -0.0052 0.0121 52 GLU A O 158 C CB . GLU A 21 ? 0.3850 0.3903 0.3522 -0.0532 -0.0122 0.0196 52 GLU A CB 159 C CG . GLU A 21 ? 0.5553 0.5615 0.5199 -0.0530 -0.0136 0.0204 52 GLU A CG 160 C CD . GLU A 21 ? 0.8553 0.8572 0.8169 -0.0563 -0.0176 0.0249 52 GLU A CD 161 O OE1 . GLU A 21 ? 0.6996 0.6999 0.6586 -0.0609 -0.0190 0.0276 52 GLU A OE1 162 O OE2 . GLU A 21 ? 0.9349 0.9354 0.8969 -0.0546 -0.0196 0.0259 52 GLU A OE2 163 N N . GLU A 22 ? 0.3311 0.3470 0.3079 -0.0430 -0.0049 0.0100 53 GLU A N 164 C CA . GLU A 22 ? 0.2821 0.3045 0.2606 -0.0415 -0.0020 0.0067 53 GLU A CA 165 C C . GLU A 22 ? 0.2422 0.2614 0.2228 -0.0366 -0.0021 0.0056 53 GLU A C 166 O O . GLU A 22 ? 0.2297 0.2437 0.2127 -0.0338 -0.0034 0.0064 53 GLU A O 167 C CB . GLU A 22 ? 0.3779 0.4054 0.3608 -0.0413 -0.0004 0.0050 53 GLU A CB 168 C CG . GLU A 22 ? 0.9124 0.9479 0.8942 -0.0459 0.0013 0.0043 53 GLU A CG 169 C CD . GLU A 22 ? 1.3101 1.3445 1.2900 -0.0502 -0.0001 0.0067 53 GLU A CD 170 O OE1 . GLU A 22 ? 1.2145 1.2477 1.1976 -0.0495 -0.0005 0.0068 53 GLU A OE1 171 O OE2 . GLU A 22 ? 1.3885 1.4236 1.3636 -0.0549 -0.0007 0.0085 53 GLU A OE2 172 N N . ASP A 23 ? 0.2150 0.2373 0.1947 -0.0360 -0.0005 0.0033 54 ASP A N 173 C CA . ASP A 23 ? 0.2023 0.2217 0.1836 -0.0320 -0.0004 0.0023 54 ASP A CA 174 C C . ASP A 23 ? 0.2174 0.2372 0.2044 -0.0287 0.0002 0.0012 54 ASP A C 175 O O . ASP A 23 ? 0.2624 0.2877 0.2524 -0.0295 0.0016 -0.0002 54 ASP A O 176 C CB . ASP A 23 ? 0.2254 0.2487 0.2053 -0.0327 0.0017 -0.0008 54 ASP A CB 177 C CG . ASP A 23 ? 0.3148 0.3381 0.2891 -0.0362 0.0009 -0.0006 54 ASP A CG 178 O OD1 . ASP A 23 ? 0.3057 0.3250 0.2771 -0.0372 -0.0021 0.0027 54 ASP A OD1 179 O OD2 . ASP A 23 ? 0.3986 0.4261 0.3723 -0.0382 0.0030 -0.0040 54 ASP A OD2 180 N N . ILE A 24 ? 0.1716 0.1865 0.1603 -0.0253 -0.0009 0.0019 55 ILE A N 181 C CA . ILE A 24 ? 0.1936 0.2090 0.1871 -0.0225 -0.0008 0.0008 55 ILE A CA 182 C C . ILE A 24 ? 0.2039 0.2198 0.1982 -0.0205 0.0000 -0.0008 55 ILE A C 183 O O . ILE A 24 ? 0.2109 0.2228 0.2034 -0.0192 -0.0007 -0.0001 55 ILE A O 184 C CB . ILE A 24 ? 0.1827 0.1934 0.1765 -0.0215 -0.0026 0.0020 55 ILE A CB 185 C CG1 . ILE A 24 ? 0.2270 0.2364 0.2199 -0.0243 -0.0036 0.0033 55 ILE A CG1 186 C CG2 . ILE A 24 ? 0.2219 0.2334 0.2193 -0.0190 -0.0026 0.0006 55 ILE A CG2 187 C CD1 . ILE A 24 ? 0.2821 0.2858 0.2756 -0.0235 -0.0053 0.0041 55 ILE A CD1 188 N N . LEU A 25 ? 0.2262 0.2477 0.2238 -0.0203 0.0014 -0.0029 56 LEU A N 189 C CA . LEU A 25 ? 0.2101 0.2328 0.2094 -0.0189 0.0023 -0.0049 56 LEU A CA 190 C C . LEU A 25 ? 0.2302 0.2501 0.2324 -0.0161 0.0005 -0.0041 56 LEU A C 191 O O . LEU A 25 ? 0.2520 0.2740 0.2573 -0.0153 -0.0005 -0.0037 56 LEU A O 192 C CB . LEU A 25 ? 0.2049 0.2365 0.2086 -0.0194 0.0051 -0.0082 56 LEU A CB 193 C CG . LEU A 25 ? 0.3930 0.4290 0.3943 -0.0225 0.0071 -0.0093 56 LEU A CG 194 C CD1 . LEU A 25 ? 0.5189 0.5640 0.5261 -0.0210 0.0106 -0.0132 56 LEU A CD1 195 C CD2 . LEU A 25 ? 0.3640 0.3952 0.3580 -0.0252 0.0071 -0.0090 56 LEU A CD2 196 N N . ILE A 26 ? 0.1700 0.1853 0.1703 -0.0149 -0.0002 -0.0039 57 ILE A N 197 C CA . ILE A 26 ? 0.1946 0.2071 0.1964 -0.0126 -0.0020 -0.0032 57 ILE A CA 198 C C . ILE A 26 ? 0.1769 0.1910 0.1806 -0.0124 -0.0023 -0.0051 57 ILE A C 199 O O . ILE A 26 ? 0.1844 0.2013 0.1918 -0.0111 -0.0040 -0.0051 57 ILE A O 200 C CB . ILE A 26 ? 0.1618 0.1692 0.1609 -0.0114 -0.0026 -0.0016 57 ILE A CB 201 C CG1 . ILE A 26 ? 0.1942 0.2013 0.1918 -0.0126 -0.0026 -0.0005 57 ILE A CG1 202 C CG2 . ILE A 26 ? 0.1629 0.1693 0.1628 -0.0099 -0.0037 -0.0013 57 ILE A CG2 203 C CD1 . ILE A 26 ? 0.2251 0.2291 0.2202 -0.0124 -0.0033 0.0009 57 ILE A CD1 204 N N . VAL A 27 ? 0.1338 0.1457 0.1346 -0.0137 -0.0009 -0.0071 58 VAL A N 205 C CA . VAL A 27 ? 0.1494 0.1579 0.1506 -0.0105 -0.0002 -0.0088 58 VAL A CA 206 C C . VAL A 27 ? 0.1885 0.1990 0.1893 -0.0104 0.0035 -0.0122 58 VAL A C 207 O O . VAL A 27 ? 0.1923 0.2029 0.1886 -0.0143 0.0047 -0.0127 58 VAL A O 208 C CB . VAL A 27 ? 0.1839 0.1842 0.1801 -0.0111 -0.0017 -0.0079 58 VAL A CB 209 C CG1 . VAL A 27 ? 0.2039 0.1981 0.1993 -0.0083 -0.0007 -0.0098 58 VAL A CG1 210 C CG2 . VAL A 27 ? 0.2048 0.2046 0.2015 -0.0113 -0.0047 -0.0051 58 VAL A CG2 211 N N . SER A 28 ? 0.1583 0.1709 0.1638 -0.0061 0.0052 -0.0145 59 SER A N 212 C CA . SER A 28 ? 0.3116 0.3267 0.3171 -0.0056 0.0094 -0.0188 59 SER A CA 213 C C . SER A 28 ? 0.3414 0.3503 0.3487 -0.0002 0.0102 -0.0215 59 SER A C 214 O O . SER A 28 ? 0.2745 0.2838 0.2879 0.0046 0.0084 -0.0201 59 SER A O 215 C CB . SER A 28 ? 0.4171 0.4442 0.4285 -0.0057 0.0115 -0.0198 59 SER A CB 216 O OG . SER A 28 ? 0.3916 0.4225 0.4003 -0.0113 0.0108 -0.0173 59 SER A OG 217 N N . GLU A 29 ? 0.2424 0.2445 0.2438 -0.0014 0.0126 -0.0250 60 GLU A N 218 C CA . GLU A 29 ? 0.2698 0.2630 0.2714 0.0031 0.0138 -0.0283 60 GLU A CA 219 C C . GLU A 29 ? 0.3007 0.2854 0.3030 0.0056 0.0093 -0.0243 60 GLU A C 220 O O . GLU A 29 ? 0.3133 0.2947 0.3210 0.0116 0.0087 -0.0246 60 GLU A O 221 C CB . GLU A 29 ? 0.2854 0.2849 0.2950 0.0089 0.0175 -0.0328 60 GLU A CB 222 C CG . GLU A 29 ? 0.3919 0.4011 0.4005 0.0059 0.0223 -0.0370 60 GLU A CG 223 C CD . GLU A 29 ? 0.7877 0.8073 0.8055 0.0108 0.0249 -0.0389 60 GLU A CD 224 O OE1 . GLU A 29 ? 0.7561 0.7712 0.7779 0.0172 0.0257 -0.0411 60 GLU A OE1 225 O OE2 . GLU A 29 ? 0.7533 0.7848 0.7737 0.0079 0.0257 -0.0377 60 GLU A OE2 226 N N . GLY A 30 ? 0.2596 0.2419 0.2570 0.0011 0.0062 -0.0203 61 GLY A N 227 C CA . GLY A 30 ? 0.2693 0.2449 0.2658 0.0017 0.0022 -0.0162 61 GLY A CA 228 C C . GLY A 30 ? 0.3026 0.2840 0.3057 0.0047 -0.0007 -0.0124 61 GLY A C 229 O O . GLY A 30 ? 0.3062 0.2825 0.3085 0.0053 -0.0040 -0.0089 61 GLY A O 230 N N . MLY A 31 ? 0.2363 0.2287 0.2454 0.0059 0.0003 -0.0127 62 MLY A N 231 C CA . MLY A 31 ? 0.2433 0.2423 0.2584 0.0081 -0.0027 -0.0093 62 MLY A CA 232 C CB . MLY A 31 ? 0.3391 0.3460 0.3633 0.0135 -0.0010 -0.0113 62 MLY A CB 233 C CG . MLY A 31 ? 0.5566 0.5553 0.5826 0.0191 0.0004 -0.0140 62 MLY A CG 234 C CD . MLY A 31 ? 0.8704 0.8639 0.8997 0.0236 -0.0040 -0.0097 62 MLY A CD 235 C CE . MLY A 31 ? 0.9436 0.9208 0.9672 0.0246 -0.0043 -0.0104 62 MLY A CE 236 N NZ . MLY A 31 ? 1.0612 1.0316 1.0870 0.0284 -0.0091 -0.0054 62 MLY A NZ 237 C CH1 . MLY A 31 ? 1.1342 1.0877 1.1541 0.0288 -0.0089 -0.0067 62 MLY A CH1 238 C CH2 . MLY A 31 ? 0.8937 0.8660 0.9150 0.0233 -0.0131 0.0002 62 MLY A CH2 239 C C . MLY A 31 ? 0.2779 0.2849 0.2926 0.0037 -0.0034 -0.0076 62 MLY A C 240 O O . MLY A 31 ? 0.2308 0.2431 0.2454 0.0013 -0.0009 -0.0097 62 MLY A O 241 N N . MET A 32 ? 0.2494 0.2572 0.2638 0.0025 -0.0068 -0.0041 63 MET A N 242 C CA . MET A 32 ? 0.1989 0.2129 0.2129 -0.0013 -0.0077 -0.0030 63 MET A CA 243 C C . MET A 32 ? 0.2291 0.2534 0.2493 -0.0008 -0.0066 -0.0041 63 MET A C 244 O O . MET A 32 ? 0.2406 0.2697 0.2670 0.0032 -0.0069 -0.0039 63 MET A O 245 C CB . MET A 32 ? 0.2823 0.2964 0.2954 -0.0021 -0.0114 0.0003 63 MET A CB 246 C CG . MET A 32 ? 0.3914 0.3972 0.3984 -0.0037 -0.0125 0.0017 63 MET A CG 247 S SD . MET A 32 ? 0.4047 0.4084 0.4062 -0.0083 -0.0111 0.0004 63 MET A SD 248 C CE . MET A 32 ? 0.4478 0.4559 0.4501 -0.0081 -0.0096 0.0005 63 MET A CE 249 N N . ALA A 33 ? 0.1510 0.1789 0.1699 -0.0050 -0.0053 -0.0048 64 ALA A N 250 C CA . ALA A 33 ? 0.2435 0.2814 0.2675 -0.0061 -0.0042 -0.0056 64 ALA A CA 251 C C . ALA A 33 ? 0.2884 0.3302 0.3157 -0.0051 -0.0068 -0.0033 64 ALA A C 252 O O . ALA A 33 ? 0.2506 0.2871 0.2746 -0.0055 -0.0091 -0.0016 64 ALA A O 253 C CB . ALA A 33 ? 0.2686 0.3023 0.2868 -0.0102 -0.0028 -0.0052 64 ALA A CB 254 N N . PRO A 34 ? 0.3626 0.4122 0.3955 -0.0038 -0.0059 -0.0036 65 PRO A N 255 C CA . PRO A 34 ? 0.3048 0.3573 0.3405 -0.0033 -0.0085 -0.0016 65 PRO A CA 256 C C . PRO A 34 ? 0.3925 0.4391 0.4219 -0.0069 -0.0097 -0.0009 65 PRO A C 257 O O . PRO A 34 ? 0.4750 0.5210 0.5040 -0.0063 -0.0121 0.0003 65 PRO A O 258 C CB . PRO A 34 ? 0.4180 0.4797 0.4596 -0.0026 -0.0066 -0.0025 65 PRO A CB 259 C CG . PRO A 34 ? 0.3989 0.4633 0.4434 0.0002 -0.0033 -0.0052 65 PRO A CG 260 C CD . PRO A 34 ? 0.4645 0.5210 0.5015 -0.0029 -0.0024 -0.0061 65 PRO A CD 261 N N . PHE A 35 ? 0.3245 0.3664 0.3489 -0.0100 -0.0078 -0.0017 66 PHE A N 262 C CA . PHE A 35 ? 0.4202 0.4567 0.4397 -0.0120 -0.0083 -0.0016 66 PHE A CA 263 C C . PHE A 35 ? 0.3583 0.3888 0.3742 -0.0110 -0.0093 -0.0013 66 PHE A C 264 O O . PHE A 35 ? 0.3920 0.4217 0.4051 -0.0125 -0.0097 -0.0012 66 PHE A O 265 C CB . PHE A 35 ? 0.4608 0.4936 0.4767 -0.0144 -0.0065 -0.0021 66 PHE A CB 266 C CG . PHE A 35 ? 0.5034 0.5294 0.5152 -0.0141 -0.0056 -0.0021 66 PHE A CG 267 C CD1 . PHE A 35 ? 0.3783 0.4037 0.3902 -0.0134 -0.0045 -0.0024 66 PHE A CD1 268 C CD2 . PHE A 35 ? 0.3754 0.3964 0.3834 -0.0147 -0.0058 -0.0021 66 PHE A CD2 269 C CE1 . PHE A 35 ? 0.3237 0.3432 0.3318 -0.0132 -0.0040 -0.0021 66 PHE A CE1 270 C CE2 . PHE A 35 ? 0.4269 0.4429 0.4322 -0.0141 -0.0051 -0.0019 66 PHE A CE2 271 C CZ . PHE A 35 ? 0.3727 0.3880 0.3777 -0.0134 -0.0044 -0.0017 66 PHE A CZ 272 N N . THR A 36 ? 0.2910 0.3192 0.3066 -0.0094 -0.0095 -0.0011 67 THR A N 273 C CA . THR A 36 ? 0.2991 0.3223 0.3109 -0.0088 -0.0101 -0.0008 67 THR A CA 274 C C . THR A 36 ? 0.3724 0.3983 0.3849 -0.0078 -0.0124 0.0006 67 THR A C 275 O O . THR A 36 ? 0.4127 0.4354 0.4214 -0.0083 -0.0125 0.0010 67 THR A O 276 C CB . THR A 36 ? 0.3102 0.3295 0.3203 -0.0081 -0.0092 -0.0010 67 THR A CB 277 O OG1 . THR A 36 ? 0.3365 0.3596 0.3501 -0.0068 -0.0107 -0.0005 67 THR A OG1 278 C CG2 . THR A 36 ? 0.3743 0.3906 0.3829 -0.0090 -0.0072 -0.0018 67 THR A CG2 279 N N . HIS A 37 ? 0.3726 0.4050 0.3902 -0.0063 -0.0143 0.0016 68 HIS A N 280 C CA . HIS A 37 ? 0.2867 0.3216 0.3051 -0.0048 -0.0172 0.0039 68 HIS A CA 281 C C . HIS A 37 ? 0.4508 0.4854 0.4654 -0.0073 -0.0176 0.0043 68 HIS A C 282 O O . HIS A 37 ? 0.4904 0.5227 0.5014 -0.0077 -0.0185 0.0058 68 HIS A O 283 C CB . HIS A 37 ? 0.4331 0.4755 0.4594 -0.0015 -0.0191 0.0050 68 HIS A CB 284 C CG . HIS A 37 ? 0.6491 0.6928 0.6805 0.0021 -0.0184 0.0048 68 HIS A CG 285 N ND1 . HIS A 37 ? 0.7178 0.7684 0.7581 0.0064 -0.0189 0.0050 68 HIS A ND1 286 C CD2 . HIS A 37 ? 0.6328 0.6720 0.6623 0.0022 -0.0171 0.0043 68 HIS A CD2 287 C CE1 . HIS A 37 ? 0.7663 0.8163 0.8098 0.0096 -0.0170 0.0042 68 HIS A CE1 288 N NE2 . HIS A 37 ? 0.6735 0.7159 0.7101 0.0069 -0.0160 0.0037 68 HIS A NE2 289 N N . ASP A 38 ? 0.2345 0.2714 0.2495 -0.0093 -0.0167 0.0030 69 ASP A N 290 C CA . ASP A 38 ? 0.1786 0.2163 0.1898 -0.0123 -0.0168 0.0033 69 ASP A CA 291 C C . ASP A 38 ? 0.1744 0.2067 0.1814 -0.0141 -0.0141 0.0015 69 ASP A C 292 O O . ASP A 38 ? 0.2013 0.2334 0.2081 -0.0156 -0.0128 0.0002 69 ASP A O 293 C CB . ASP A 38 ? 0.1891 0.2332 0.2028 -0.0140 -0.0176 0.0033 69 ASP A CB 294 C CG . ASP A 38 ? 0.3898 0.4358 0.3995 -0.0177 -0.0181 0.0035 69 ASP A CG 295 O OD1 . ASP A 38 ? 0.2803 0.3222 0.2852 -0.0192 -0.0169 0.0028 69 ASP A OD1 296 O OD2 . ASP A 38 ? 0.3286 0.3809 0.3402 -0.0192 -0.0196 0.0042 69 ASP A OD2 297 N N . PHE A 39 ? 0.1595 0.1875 0.1636 -0.0136 -0.0134 0.0017 70 PHE A N 298 C CA . PHE A 39 ? 0.2170 0.2405 0.2183 -0.0143 -0.0111 0.0002 70 PHE A CA 299 C C . PHE A 39 ? 0.2683 0.2922 0.2672 -0.0168 -0.0102 -0.0014 70 PHE A C 300 O O . PHE A 39 ? 0.1870 0.2081 0.1857 -0.0170 -0.0089 -0.0030 70 PHE A O 301 C CB . PHE A 39 ? 0.3044 0.3245 0.3037 -0.0135 -0.0105 0.0008 70 PHE A CB 302 C CG . PHE A 39 ? 0.3179 0.3343 0.3162 -0.0131 -0.0085 -0.0006 70 PHE A CG 303 C CD1 . PHE A 39 ? 0.3533 0.3678 0.3533 -0.0119 -0.0079 -0.0009 70 PHE A CD1 304 C CD2 . PHE A 39 ? 0.3369 0.3524 0.3331 -0.0141 -0.0073 -0.0017 70 PHE A CD2 305 C CE1 . PHE A 39 ? 0.4708 0.4823 0.4701 -0.0116 -0.0066 -0.0017 70 PHE A CE1 306 C CE2 . PHE A 39 ? 0.3588 0.3715 0.3552 -0.0133 -0.0061 -0.0029 70 PHE A CE2 307 C CZ . PHE A 39 ? 0.3820 0.3927 0.3799 -0.0120 -0.0060 -0.0026 70 PHE A CZ 308 N N . ARG A 40 ? 0.1806 0.2079 0.1778 -0.0188 -0.0112 -0.0010 71 ARG A N 309 C CA . ARG A 40 ? 0.1835 0.2113 0.1783 -0.0215 -0.0104 -0.0033 71 ARG A CA 310 C C . ARG A 40 ? 0.2096 0.2378 0.2059 -0.0227 -0.0105 -0.0045 71 ARG A C 311 O O . ARG A 40 ? 0.2004 0.2259 0.1956 -0.0240 -0.0095 -0.0069 71 ARG A O 312 C CB . ARG A 40 ? 0.1893 0.2213 0.1814 -0.0241 -0.0114 -0.0027 71 ARG A CB 313 C CG . ARG A 40 ? 0.2274 0.2585 0.2171 -0.0241 -0.0106 -0.0021 71 ARG A CG 314 C CD . ARG A 40 ? 0.2472 0.2830 0.2341 -0.0271 -0.0119 -0.0006 71 ARG A CD 315 N NE . ARG A 40 ? 0.2311 0.2693 0.2199 -0.0261 -0.0147 0.0032 71 ARG A NE 316 C CZ . ARG A 40 ? 0.3123 0.3541 0.2991 -0.0281 -0.0166 0.0058 71 ARG A CZ 317 N NH1 . ARG A 40 ? 0.1880 0.2321 0.1707 -0.0317 -0.0156 0.0050 71 ARG A NH1 318 N NH2 . ARG A 40 ? 0.2039 0.2475 0.1933 -0.0264 -0.0197 0.0092 71 ARG A NH2 319 N N . MLY A 41 ? 0.1725 0.2043 0.1717 -0.0223 -0.0117 -0.0029 72 MLY A N 320 C CA . MLY A 41 ? 0.2812 0.3143 0.2820 -0.0239 -0.0117 -0.0037 72 MLY A CA 321 C CB . MLY A 41 ? 0.2578 0.2977 0.2623 -0.0236 -0.0134 -0.0018 72 MLY A CB 322 C CG . MLY A 41 ? 0.3772 0.4190 0.3837 -0.0252 -0.0129 -0.0024 72 MLY A CG 323 C CD . MLY A 41 ? 0.5226 0.5730 0.5326 -0.0263 -0.0148 -0.0011 72 MLY A CD 324 C CE . MLY A 41 ? 0.9172 0.9700 0.9269 -0.0302 -0.0143 -0.0020 72 MLY A CE 325 N NZ . MLY A 41 ? 1.0400 1.0858 1.0475 -0.0311 -0.0124 -0.0036 72 MLY A NZ 326 C CH1 . MLY A 41 ? 0.9861 1.0330 0.9970 -0.0292 -0.0115 -0.0028 72 MLY A CH1 327 C CH2 . MLY A 41 ? 0.8566 0.9025 0.8619 -0.0358 -0.0125 -0.0048 72 MLY A CH2 328 C C . MLY A 41 ? 0.3651 0.3931 0.3667 -0.0226 -0.0102 -0.0045 72 MLY A C 329 O O . MLY A 41 ? 0.2890 0.3148 0.2899 -0.0245 -0.0097 -0.0058 72 MLY A O 330 N N . ALA A 42 ? 0.2547 0.2806 0.2574 -0.0197 -0.0097 -0.0035 73 ALA A N 331 C CA . ALA A 42 ? 0.2601 0.2817 0.2632 -0.0186 -0.0085 -0.0038 73 ALA A CA 332 C C . ALA A 42 ? 0.3159 0.3325 0.3169 -0.0190 -0.0078 -0.0054 73 ALA A C 333 O O . ALA A 42 ? 0.2798 0.2934 0.2812 -0.0198 -0.0076 -0.0061 73 ALA A O 334 C CB . ALA A 42 ? 0.1887 0.2094 0.1928 -0.0159 -0.0082 -0.0027 73 ALA A CB 335 N N . GLN A 43 ? 0.2260 0.2419 0.2253 -0.0187 -0.0077 -0.0062 74 GLN A N 336 C CA . GLN A 43 ? 0.2509 0.2632 0.2493 -0.0188 -0.0073 -0.0083 74 GLN A CA 337 C C . GLN A 43 ? 0.4042 0.4148 0.4022 -0.0212 -0.0076 -0.0105 74 GLN A C 338 O O . GLN A 43 ? 0.3754 0.3812 0.3742 -0.0210 -0.0078 -0.0122 74 GLN A O 339 C CB . GLN A 43 ? 0.2608 0.2746 0.2573 -0.0186 -0.0068 -0.0088 74 GLN A CB 340 C CG . GLN A 43 ? 0.4200 0.4327 0.4166 -0.0164 -0.0062 -0.0076 74 GLN A CG 341 C CD . GLN A 43 ? 0.6937 0.7084 0.6884 -0.0169 -0.0055 -0.0083 74 GLN A CD 342 O OE1 . GLN A 43 ? 0.8411 0.8545 0.8361 -0.0160 -0.0048 -0.0093 74 GLN A OE1 343 N NE2 . GLN A 43 ? 1.0002 1.0185 0.9930 -0.0186 -0.0059 -0.0074 74 GLN A NE2 344 N N . GLN A 44 ? 0.4513 0.4655 0.4483 -0.0237 -0.0082 -0.0107 75 GLN A N 345 C CA . GLN A 44 ? 0.4464 0.4587 0.4425 -0.0267 -0.0086 -0.0130 75 GLN A CA 346 C C . GLN A 44 ? 0.3710 0.3804 0.3688 -0.0278 -0.0089 -0.0125 75 GLN A C 347 O O . GLN A 44 ? 0.6004 0.6058 0.5978 -0.0300 -0.0094 -0.0146 75 GLN A O 348 C CB . GLN A 44 ? 0.4949 0.5123 0.4888 -0.0298 -0.0090 -0.0136 75 GLN A CB 349 C CG . GLN A 44 ? 0.3500 0.3694 0.3415 -0.0296 -0.0084 -0.0145 75 GLN A CG 350 C CD . GLN A 44 ? 0.5642 0.5789 0.5543 -0.0296 -0.0074 -0.0183 75 GLN A CD 351 O OE1 . GLN A 44 ? 0.4809 0.4931 0.4695 -0.0320 -0.0075 -0.0214 75 GLN A OE1 352 N NE2 . GLN A 44 ? 0.5019 0.5156 0.4924 -0.0269 -0.0065 -0.0183 75 GLN A NE2 353 N N . ARG A 45 ? 0.3749 0.3857 0.3745 -0.0262 -0.0087 -0.0100 76 ARG A N 354 C CA . ARG A 45 ? 0.3265 0.3352 0.3273 -0.0272 -0.0086 -0.0091 76 ARG A CA 355 C C . ARG A 45 ? 0.5532 0.5563 0.5551 -0.0250 -0.0084 -0.0089 76 ARG A C 356 O O . ARG A 45 ? 0.5108 0.5118 0.5132 -0.0259 -0.0083 -0.0078 76 ARG A O 357 C CB . ARG A 45 ? 0.4133 0.4277 0.4151 -0.0271 -0.0083 -0.0068 76 ARG A CB 358 C CG . ARG A 45 ? 0.8335 0.8541 0.8356 -0.0299 -0.0088 -0.0066 76 ARG A CG 359 C CD . ARG A 45 ? 0.9878 1.0138 0.9921 -0.0300 -0.0085 -0.0048 76 ARG A CD 360 N NE . ARG A 45 ? 1.1867 1.2109 1.1904 -0.0327 -0.0080 -0.0045 76 ARG A NE 361 C CZ . ARG A 45 ? 1.1609 1.1823 1.1644 -0.0317 -0.0072 -0.0035 76 ARG A CZ 362 N NH1 . ARG A 45 ? 1.0079 1.0280 1.0119 -0.0281 -0.0067 -0.0031 76 ARG A NH1 363 N NH2 . ARG A 45 ? 0.9083 0.9281 0.9107 -0.0349 -0.0071 -0.0028 76 ARG A NH2 364 N N . MET A 46 ? 0.3855 0.3869 0.3876 -0.0224 -0.0083 -0.0098 77 MET A N 365 C CA . MET A 46 ? 0.2568 0.2541 0.2607 -0.0202 -0.0084 -0.0098 77 MET A CA 366 C C . MET A 46 ? 0.2827 0.2741 0.2881 -0.0206 -0.0095 -0.0126 77 MET A C 367 O O . MET A 46 ? 0.4480 0.4386 0.4519 -0.0200 -0.0100 -0.0145 77 MET A O 368 C CB . MET A 46 ? 0.2538 0.2532 0.2573 -0.0174 -0.0079 -0.0091 77 MET A CB 369 C CG . MET A 46 ? 0.3841 0.3868 0.3870 -0.0164 -0.0070 -0.0066 77 MET A CG 370 S SD . MET A 46 ? 0.3950 0.3988 0.3970 -0.0139 -0.0065 -0.0061 77 MET A SD 371 C CE . MET A 46 ? 0.3423 0.3498 0.3435 -0.0136 -0.0061 -0.0041 77 MET A CE 372 N N . PRO A 47 ? 0.5152 0.5019 0.5229 -0.0218 -0.0096 -0.0131 78 PRO A N 373 C CA . PRO A 47 ? 0.4143 0.3944 0.4238 -0.0214 -0.0105 -0.0160 78 PRO A CA 374 C C . PRO A 47 ? 0.2838 0.2629 0.2958 -0.0175 -0.0097 -0.0165 78 PRO A C 375 O O . PRO A 47 ? 0.3264 0.3095 0.3375 -0.0174 -0.0063 -0.0152 78 PRO A O 376 C CB . PRO A 47 ? 0.3799 0.3554 0.3905 -0.0246 -0.0095 -0.0157 78 PRO A CB 377 C CG . PRO A 47 ? 0.5813 0.5599 0.5899 -0.0251 -0.0088 -0.0115 78 PRO A CG 378 C CD . PRO A 47 ? 0.7190 0.7053 0.7260 -0.0236 -0.0088 -0.0103 78 PRO A CD 379 N N . ALA A 48 ? 0.3317 0.2967 0.3281 -0.0197 -0.0124 -0.0155 79 ALA A N 380 C CA . ALA A 48 ? 0.3122 0.2743 0.3088 -0.0188 -0.0078 -0.0187 79 ALA A CA 381 C C . ALA A 48 ? 0.4906 0.4498 0.4924 -0.0181 -0.0068 -0.0168 79 ALA A C 382 O O . ALA A 48 ? 0.3571 0.3112 0.3598 -0.0200 -0.0064 -0.0163 79 ALA A O 383 C CB . ALA A 48 ? 0.3353 0.2902 0.3325 -0.0171 -0.0078 -0.0241 79 ALA A CB 384 N N . ILE A 49 ? 0.2559 0.2192 0.2620 -0.0147 -0.0082 -0.0146 80 ILE A N 385 C CA . ILE A 49 ? 0.2271 0.1878 0.2367 -0.0130 -0.0106 -0.0102 80 ILE A CA 386 C C . ILE A 49 ? 0.2463 0.1962 0.2582 -0.0111 -0.0119 -0.0106 80 ILE A C 387 O O . ILE A 49 ? 0.2607 0.2076 0.2755 -0.0076 -0.0116 -0.0145 80 ILE A O 388 C CB . ILE A 49 ? 0.1846 0.1506 0.1979 -0.0101 -0.0123 -0.0085 80 ILE A CB 389 C CG1 . ILE A 49 ? 0.2551 0.2304 0.2651 -0.0120 -0.0105 -0.0078 80 ILE A CG1 390 C CG2 . ILE A 49 ? 0.2049 0.1677 0.2205 -0.0090 -0.0155 -0.0033 80 ILE A CG2 391 C CD1 . ILE A 49 ? 0.3550 0.3358 0.3676 -0.0099 -0.0109 -0.0087 80 ILE A CD1 392 N N . PRO A 50 ? 0.2641 0.2086 0.2748 -0.0131 -0.0130 -0.0070 81 PRO A N 393 C CA . PRO A 50 ? 0.2344 0.1675 0.2466 -0.0113 -0.0141 -0.0071 81 PRO A CA 394 C C . PRO A 50 ? 0.2721 0.2021 0.2903 -0.0055 -0.0169 -0.0054 81 PRO A C 395 O O . PRO A 50 ? 0.2610 0.1974 0.2822 -0.0036 -0.0187 -0.0026 81 PRO A O 396 C CB . PRO A 50 ? 0.2902 0.2200 0.2993 -0.0157 -0.0148 -0.0033 81 PRO A CB 397 C CG . PRO A 50 ? 0.4276 0.3674 0.4352 -0.0179 -0.0150 -0.0001 81 PRO A CG 398 C CD . PRO A 50 ? 0.3792 0.3280 0.3872 -0.0168 -0.0132 -0.0031 81 PRO A CD 399 N N . VAL A 51 ? 0.2490 0.1690 0.2692 -0.0025 -0.0170 -0.0070 82 VAL A N 400 C CA . VAL A 51 ? 0.2266 0.1435 0.2537 0.0040 -0.0192 -0.0057 82 VAL A CA 401 C C . VAL A 51 ? 0.3319 0.2504 0.3606 0.0042 -0.0232 0.0020 82 VAL A C 402 O O . VAL A 51 ? 0.3982 0.3202 0.4330 0.0091 -0.0250 0.0036 82 VAL A O 403 C CB . VAL A 51 ? 0.2501 0.1547 0.2781 0.0069 -0.0183 -0.0088 82 VAL A CB 404 C CG1 . VAL A 51 ? 0.2903 0.1947 0.3170 0.0076 -0.0144 -0.0170 82 VAL A CG1 405 C CG2 . VAL A 51 ? 0.4156 0.3098 0.4382 0.0022 -0.0190 -0.0054 82 VAL A CG2 406 N N . ASN A 52 ? 0.3086 0.2254 0.3318 -0.0012 -0.0244 0.0066 83 ASN A N 407 C CA . ASN A 52 ? 0.3533 0.2717 0.3762 -0.0022 -0.0280 0.0137 83 ASN A CA 408 C C . ASN A 52 ? 0.3120 0.2424 0.3347 -0.0035 -0.0288 0.0158 83 ASN A C 409 O O . ASN A 52 ? 0.4203 0.3535 0.4428 -0.0044 -0.0317 0.0212 83 ASN A O 410 C CB . ASN A 52 ? 0.3761 0.2892 0.3930 -0.0079 -0.0287 0.0172 83 ASN A CB 411 C CG . ASN A 52 ? 0.4151 0.3339 0.4266 -0.0136 -0.0259 0.0152 83 ASN A CG 412 O OD1 . ASN A 52 ? 0.4800 0.3982 0.4906 -0.0143 -0.0227 0.0100 83 ASN A OD1 413 N ND2 . ASN A 52 ? 0.5341 0.4593 0.5418 -0.0175 -0.0269 0.0191 83 ASN A ND2 414 N N . ILE A 53 ? 0.3109 0.2480 0.3329 -0.0043 -0.0261 0.0117 84 ILE A N 415 C CA . ILE A 53 ? 0.2099 0.1571 0.2310 -0.0057 -0.0263 0.0131 84 ILE A CA 416 C C . ILE A 53 ? 0.3157 0.2671 0.3438 -0.0006 -0.0266 0.0108 84 ILE A C 417 O O . ILE A 53 ? 0.3867 0.3383 0.4169 0.0013 -0.0241 0.0053 84 ILE A O 418 C CB . ILE A 53 ? 0.2702 0.2225 0.2856 -0.0101 -0.0232 0.0107 84 ILE A CB 419 C CG1 . ILE A 53 ? 0.4061 0.3564 0.4160 -0.0147 -0.0231 0.0134 84 ILE A CG1 420 C CG2 . ILE A 53 ? 0.3058 0.2675 0.3203 -0.0109 -0.0228 0.0111 84 ILE A CG2 421 C CD1 . ILE A 53 ? 0.5226 0.4780 0.5283 -0.0181 -0.0198 0.0109 84 ILE A CD1 422 N N . HIS A 54 ? 0.2151 0.1712 0.2465 0.0011 -0.0292 0.0149 85 HIS A N 423 C CA . HIS A 54 ? 0.2519 0.2144 0.2903 0.0061 -0.0292 0.0133 85 HIS A CA 424 C C . HIS A 54 ? 0.2352 0.2069 0.2717 0.0035 -0.0288 0.0138 85 HIS A C 425 O O . HIS A 54 ? 0.1884 0.1675 0.2299 0.0069 -0.0281 0.0115 85 HIS A O 426 C CB . HIS A 54 ? 0.2612 0.2249 0.3047 0.0100 -0.0320 0.0174 85 HIS A CB 427 C CG . HIS A 54 ? 0.5130 0.4666 0.5582 0.0128 -0.0329 0.0179 85 HIS A CG 428 N ND1 . HIS A 54 ? 0.5678 0.5157 0.6165 0.0169 -0.0306 0.0123 85 HIS A ND1 429 C CD2 . HIS A 54 ? 0.6619 0.6102 0.7051 0.0116 -0.0358 0.0233 85 HIS A CD2 430 C CE1 . HIS A 54 ? 0.4057 0.3440 0.4544 0.0183 -0.0322 0.0146 85 HIS A CE1 431 N NE2 . HIS A 54 ? 0.5726 0.5108 0.6183 0.0153 -0.0356 0.0215 85 HIS A NE2 432 N N . SER A 55 ? 0.2186 0.1912 0.2475 -0.0024 -0.0287 0.0163 86 SER A N 433 C CA . SER A 55 ? 0.2130 0.1929 0.2382 -0.0055 -0.0280 0.0169 86 SER A CA 434 C C . SER A 55 ? 0.3106 0.2906 0.3277 -0.0109 -0.0262 0.0167 86 SER A C 435 O O . SER A 55 ? 0.2812 0.2572 0.2955 -0.0122 -0.0263 0.0177 86 SER A O 436 C CB . SER A 55 ? 0.2448 0.2321 0.2704 -0.0058 -0.0294 0.0204 86 SER A CB 437 O OG . SER A 55 ? 0.3480 0.3330 0.3705 -0.0086 -0.0310 0.0243 86 SER A OG 438 N N . MET A 56 ? 0.2080 0.1935 0.2209 -0.0128 -0.0239 0.0152 87 MET A N 439 C CA . MET A 56 ? 0.2063 0.1938 0.2117 -0.0145 -0.0207 0.0140 87 MET A CA 440 C C . MET A 56 ? 0.1775 0.1696 0.1777 -0.0156 -0.0195 0.0151 87 MET A C 441 O O . MET A 56 ? 0.1856 0.1798 0.1864 -0.0146 -0.0180 0.0144 87 MET A O 442 C CB . MET A 56 ? 0.2442 0.2322 0.2492 -0.0132 -0.0167 0.0093 87 MET A CB 443 C CG . MET A 56 ? 0.4004 0.3897 0.4011 -0.0143 -0.0138 0.0082 87 MET A CG 444 S SD . MET A 56 ? 0.4308 0.4213 0.4334 -0.0130 -0.0107 0.0036 87 MET A SD 445 C CE . MET A 56 ? 0.5149 0.5081 0.5143 -0.0140 -0.0090 0.0036 87 MET A CE 446 N N . ASN A 57 ? 0.1931 0.1864 0.1884 -0.0176 -0.0189 0.0156 88 ASN A N 447 C CA . ASN A 57 ? 0.1668 0.1633 0.1586 -0.0182 -0.0160 0.0145 88 ASN A CA 448 C C . ASN A 57 ? 0.1669 0.1644 0.1560 -0.0173 -0.0124 0.0116 88 ASN A C 449 O O . ASN A 57 ? 0.1902 0.1873 0.1777 -0.0183 -0.0121 0.0112 88 ASN A O 450 C CB . ASN A 57 ? 0.2028 0.2004 0.1926 -0.0213 -0.0177 0.0162 88 ASN A CB 451 C CG . ASN A 57 ? 0.2767 0.2746 0.2702 -0.0233 -0.0215 0.0195 88 ASN A CG 452 O OD1 . ASN A 57 ? 0.2702 0.2681 0.2685 -0.0224 -0.0225 0.0207 88 ASN A OD1 453 N ND2 . ASN A 57 ? 0.3739 0.3719 0.3656 -0.0268 -0.0236 0.0220 88 ASN A ND2 454 N N . PHE A 58 ? 0.1223 0.1210 0.1112 -0.0159 -0.0100 0.0098 89 PHE A N 455 C CA . PHE A 58 ? 0.1085 0.1079 0.0956 -0.0157 -0.0076 0.0077 89 PHE A CA 456 C C . PHE A 58 ? 0.1908 0.1913 0.1759 -0.0168 -0.0066 0.0071 89 PHE A C 457 O O . PHE A 58 ? 0.1672 0.1680 0.1524 -0.0173 -0.0072 0.0081 89 PHE A O 458 C CB . PHE A 58 ? 0.1519 0.1512 0.1402 -0.0140 -0.0065 0.0065 89 PHE A CB 459 C CG . PHE A 58 ? 0.1492 0.1479 0.1399 -0.0130 -0.0069 0.0061 89 PHE A CG 460 C CD1 . PHE A 58 ? 0.2529 0.2510 0.2470 -0.0121 -0.0082 0.0061 89 PHE A CD1 461 C CD2 . PHE A 58 ? 0.1975 0.1967 0.1888 -0.0125 -0.0057 0.0045 89 PHE A CD2 462 C CE1 . PHE A 58 ? 0.2538 0.2517 0.2512 -0.0111 -0.0081 0.0042 89 PHE A CE1 463 C CE2 . PHE A 58 ? 0.2273 0.2264 0.2216 -0.0116 -0.0058 0.0033 89 PHE A CE2 464 C CZ . PHE A 58 ? 0.2429 0.2412 0.2398 -0.0110 -0.0068 0.0030 89 PHE A CZ 465 N N . THR A 59 ? 0.1309 0.1321 0.1142 -0.0177 -0.0050 0.0055 90 THR A N 466 C CA . THR A 59 ? 0.1200 0.1220 0.1012 -0.0194 -0.0038 0.0046 90 THR A CA 467 C C . THR A 59 ? 0.2006 0.2020 0.1818 -0.0189 -0.0019 0.0026 90 THR A C 468 O O . THR A 59 ? 0.1472 0.1490 0.1294 -0.0183 -0.0010 0.0014 90 THR A O 469 C CB . THR A 59 ? 0.1503 0.1540 0.1286 -0.0224 -0.0038 0.0044 90 THR A CB 470 O OG1 . THR A 59 ? 0.1979 0.2016 0.1761 -0.0234 -0.0065 0.0068 90 THR A OG1 471 C CG2 . THR A 59 ? 0.1648 0.1694 0.1401 -0.0253 -0.0023 0.0037 90 THR A CG2 472 N N . TRP A 60 ? 0.1351 0.1357 0.1151 -0.0199 -0.0014 0.0022 91 TRP A N 473 C CA . TRP A 60 ? 0.1077 0.1067 0.0867 -0.0203 0.0002 0.0003 91 TRP A CA 474 C C . TRP A 60 ? 0.1535 0.1516 0.1289 -0.0237 0.0016 -0.0010 91 TRP A C 475 O O . TRP A 60 ? 0.1291 0.1282 0.1034 -0.0253 0.0008 0.0001 91 TRP A O 476 C CB . TRP A 60 ? 0.1856 0.1830 0.1657 -0.0184 -0.0007 0.0011 91 TRP A CB 477 C CG . TRP A 60 ? 0.1636 0.1611 0.1437 -0.0185 -0.0019 0.0025 91 TRP A CG 478 C CD1 . TRP A 60 ? 0.1813 0.1799 0.1603 -0.0203 -0.0025 0.0033 91 TRP A CD1 479 C CD2 . TRP A 60 ? 0.1923 0.1896 0.1739 -0.0171 -0.0027 0.0032 91 TRP A CD2 480 N NE1 . TRP A 60 ? 0.2254 0.2246 0.2051 -0.0202 -0.0035 0.0045 91 TRP A NE1 481 C CE2 . TRP A 60 ? 0.1850 0.1836 0.1663 -0.0183 -0.0035 0.0043 91 TRP A CE2 482 C CE3 . TRP A 60 ? 0.3170 0.3137 0.2999 -0.0155 -0.0028 0.0030 91 TRP A CE3 483 C CZ2 . TRP A 60 ? 0.2872 0.2868 0.2697 -0.0179 -0.0041 0.0050 91 TRP A CZ2 484 C CZ3 . TRP A 60 ? 0.3106 0.3081 0.2945 -0.0151 -0.0034 0.0037 91 TRP A CZ3 485 C CH2 . TRP A 60 ? 0.2357 0.2348 0.2194 -0.0164 -0.0039 0.0046 91 TRP A CH2 486 N N . GLN A 61 ? 0.1427 0.1386 0.1160 -0.0251 0.0038 -0.0037 92 GLN A N 487 C CA . GLN A 61 ? 0.1022 0.0956 0.0720 -0.0274 0.0052 -0.0065 92 GLN A CA 488 C C . GLN A 61 ? 0.1265 0.1148 0.0962 -0.0248 0.0055 -0.0101 92 GLN A C 489 O O . GLN A 61 ? 0.1834 0.1711 0.1561 -0.0220 0.0055 -0.0117 92 GLN A O 490 C CB . GLN A 61 ? 0.2033 0.1998 0.1713 -0.0311 0.0072 -0.0084 92 GLN A CB 491 C CG . GLN A 61 ? 0.4139 0.4122 0.3835 -0.0300 0.0093 -0.0124 92 GLN A CG 492 C CD . GLN A 61 ? 0.4062 0.4073 0.3728 -0.0341 0.0114 -0.0147 92 GLN A CD 493 O OE1 . GLN A 61 ? 0.2230 0.2293 0.1907 -0.0363 0.0120 -0.0148 92 GLN A OE1 494 N NE2 . GLN A 61 ? 0.5845 0.5826 0.5469 -0.0361 0.0120 -0.0159 92 GLN A NE2 495 N N . ALA A 62 ? 0.1900 0.1742 0.1561 -0.0262 0.0059 -0.0115 93 ALA A N 496 C CA . ALA A 62 ? 0.2240 0.2013 0.1890 -0.0242 0.0063 -0.0151 93 ALA A CA 497 C C . ALA A 62 ? 0.3121 0.2884 0.2734 -0.0263 0.0090 -0.0193 93 ALA A C 498 O O . ALA A 62 ? 0.3431 0.3181 0.3002 -0.0296 0.0093 -0.0193 93 ALA A O 499 C CB . ALA A 62 ? 0.2911 0.2648 0.2542 -0.0251 0.0044 -0.0129 93 ALA A CB 500 N N . ALA A 63 ? 0.3427 0.3212 0.3058 -0.0247 0.0113 -0.0226 94 ALA A N 501 C CA . ALA A 63 ? 0.3048 0.2857 0.2658 -0.0263 0.0146 -0.0267 94 ALA A CA 502 C C . ALA A 63 ? 0.4145 0.3889 0.3725 -0.0250 0.0169 -0.0323 94 ALA A C 503 O O . ALA A 63 ? 0.4700 0.4472 0.4259 -0.0266 0.0199 -0.0359 94 ALA A O 504 C CB . ALA A 63 ? 0.3880 0.3753 0.3532 -0.0245 0.0165 -0.0280 94 ALA A CB 505 N N . GLY A 64 ? 0.3136 0.2794 0.2714 -0.0223 0.0153 -0.0331 95 GLY A N 506 C CA . GLY A 64 ? 0.5289 0.4864 0.4841 -0.0205 0.0169 -0.0384 95 GLY A CA 507 C C . GLY A 64 ? 0.5733 0.5254 0.5233 -0.0246 0.0153 -0.0373 95 GLY A C 508 O O . GLY A 64 ? 0.5952 0.5524 0.5428 -0.0295 0.0143 -0.0334 95 GLY A O 509 N N . GLN A 65 ? 0.4468 0.3886 0.3956 -0.0226 0.0150 -0.0407 96 GLN A N 510 C CA . GLN A 65 ? 0.3553 0.2911 0.2989 -0.0267 0.0137 -0.0402 96 GLN A CA 511 C C . GLN A 65 ? 0.4095 0.3415 0.3551 -0.0264 0.0101 -0.0355 96 GLN A C 512 O O . GLN A 65 ? 0.4184 0.3488 0.3600 -0.0308 0.0088 -0.0332 96 GLN A O 513 C CB . GLN A 65 ? 0.5015 0.4277 0.4419 -0.0256 0.0156 -0.0470 96 GLN A CB 514 C CG . GLN A 65 ? 0.5683 0.4902 0.5018 -0.0317 0.0152 -0.0471 96 GLN A CG 515 C CD . GLN A 65 ? 1.0489 0.9604 0.9788 -0.0308 0.0171 -0.0543 96 GLN A CD 516 O OE1 . GLN A 65 ? 1.1262 1.0393 1.0539 -0.0305 0.0205 -0.0596 96 GLN A OE1 517 N NE2 . GLN A 65 ? 0.9811 0.8818 0.9101 -0.0309 0.0150 -0.0547 96 GLN A NE2 518 N N . ALA A 66 ? 0.4874 0.4186 0.4388 -0.0217 0.0087 -0.0340 97 ALA A N 519 C CA . ALA A 66 ? 0.4411 0.3697 0.3945 -0.0217 0.0056 -0.0294 97 ALA A CA 520 C C . ALA A 66 ? 0.3582 0.2963 0.3106 -0.0254 0.0043 -0.0236 97 ALA A C 521 O O . ALA A 66 ? 0.3677 0.3142 0.3212 -0.0258 0.0052 -0.0227 97 ALA A O 522 C CB . ALA A 66 ? 0.4713 0.3977 0.4312 -0.0160 0.0048 -0.0292 97 ALA A CB 523 N N . GLU A 67 ? 0.3389 0.2758 0.2894 -0.0279 0.0023 -0.0200 98 GLU A N 524 C CA . GLU A 67 ? 0.3397 0.2854 0.2897 -0.0304 0.0011 -0.0149 98 GLU A CA 525 C C . GLU A 67 ? 0.2426 0.1908 0.1969 -0.0276 -0.0007 -0.0116 98 GLU A C 526 O O . GLU A 67 ? 0.2835 0.2252 0.2388 -0.0261 -0.0019 -0.0116 98 GLU A O 527 C CB . GLU A 67 ? 0.3217 0.2660 0.2661 -0.0351 0.0003 -0.0131 98 GLU A CB 528 C CG . GLU A 67 ? 0.4808 0.4239 0.4199 -0.0392 0.0018 -0.0156 98 GLU A CG 529 C CD . GLU A 67 ? 0.7860 0.7375 0.7252 -0.0405 0.0032 -0.0151 98 GLU A CD 530 O OE1 . GLU A 67 ? 0.5259 0.4850 0.4666 -0.0410 0.0025 -0.0108 98 GLU A OE1 531 O OE2 . GLU A 67 ? 0.5505 0.5002 0.4875 -0.0416 0.0052 -0.0190 98 GLU A OE2 532 N N . TYR A 68 ? 0.1900 0.1473 0.1469 -0.0271 -0.0010 -0.0088 99 TYR A N 533 C CA . TYR A 68 ? 0.1529 0.1137 0.1135 -0.0249 -0.0025 -0.0060 99 TYR A CA 534 C C . TYR A 68 ? 0.1861 0.1537 0.1452 -0.0268 -0.0031 -0.0023 99 TYR A C 535 O O . TYR A 68 ? 0.2053 0.1764 0.1623 -0.0291 -0.0022 -0.0017 99 TYR A O 536 C CB . TYR A 68 ? 0.1581 0.1216 0.1236 -0.0215 -0.0019 -0.0070 99 TYR A CB 537 C CG . TYR A 68 ? 0.2661 0.2222 0.2329 -0.0191 -0.0012 -0.0108 99 TYR A CG 538 C CD1 . TYR A 68 ? 0.2449 0.1947 0.2133 -0.0170 -0.0025 -0.0103 99 TYR A CD1 539 C CD2 . TYR A 68 ? 0.3559 0.3112 0.3222 -0.0187 0.0010 -0.0148 99 TYR A CD2 540 C CE1 . TYR A 68 ? 0.2986 0.2407 0.2692 -0.0135 -0.0017 -0.0136 99 TYR A CE1 541 C CE2 . TYR A 68 ? 0.3923 0.3411 0.3602 -0.0152 0.0022 -0.0190 99 TYR A CE2 542 C CZ . TYR A 68 ? 0.4255 0.3674 0.3962 -0.0122 0.0008 -0.0184 99 TYR A CZ 543 O OH . TYR A 68 ? 0.4414 0.3766 0.4151 -0.0074 0.0020 -0.0222 99 TYR A OH 544 N N . PHE A 69 ? 0.1462 0.1153 0.1058 -0.0263 -0.0046 0.0000 100 PHE A N 545 C CA . PHE A 69 ? 0.1522 0.1272 0.1102 -0.0280 -0.0052 0.0030 100 PHE A CA 546 C C . PHE A 69 ? 0.1928 0.1730 0.1570 -0.0247 -0.0055 0.0038 100 PHE A C 547 O O . PHE A 69 ? 0.1969 0.1745 0.1611 -0.0234 -0.0065 0.0040 100 PHE A O 548 C CB . PHE A 69 ? 0.1631 0.1354 0.1163 -0.0311 -0.0065 0.0041 100 PHE A CB 549 C CG . PHE A 69 ? 0.1561 0.1225 0.1046 -0.0343 -0.0061 0.0026 100 PHE A CG 550 C CD1 . PHE A 69 ? 0.1812 0.1390 0.1297 -0.0334 -0.0061 0.0000 100 PHE A CD1 551 C CD2 . PHE A 69 ? 0.1978 0.1671 0.1426 -0.0380 -0.0056 0.0034 100 PHE A CD2 552 C CE1 . PHE A 69 ? 0.1910 0.1425 0.1353 -0.0363 -0.0054 -0.0021 100 PHE A CE1 553 C CE2 . PHE A 69 ? 0.2372 0.2009 0.1773 -0.0414 -0.0050 0.0016 100 PHE A CE2 554 C CZ . PHE A 69 ? 0.2307 0.1853 0.1704 -0.0404 -0.0048 -0.0014 100 PHE A CZ 555 N N . TYR A 70 ? 0.1564 0.1433 0.1260 -0.0232 -0.0050 0.0042 101 TYR A N 556 C CA . TYR A 70 ? 0.1275 0.1185 0.1025 -0.0203 -0.0049 0.0045 101 TYR A CA 557 C C . TYR A 70 ? 0.1628 0.1578 0.1395 -0.0209 -0.0050 0.0053 101 TYR A C 558 O O . TYR A 70 ? 0.1483 0.1448 0.1235 -0.0231 -0.0052 0.0058 101 TYR A O 559 C CB . TYR A 70 ? 0.1409 0.1346 0.1192 -0.0185 -0.0042 0.0042 101 TYR A CB 560 C CG . TYR A 70 ? 0.1535 0.1505 0.1328 -0.0194 -0.0042 0.0048 101 TYR A CG 561 C CD1 . TYR A 70 ? 0.1741 0.1751 0.1562 -0.0190 -0.0044 0.0055 101 TYR A CD1 562 C CD2 . TYR A 70 ? 0.1213 0.1176 0.0981 -0.0215 -0.0041 0.0047 101 TYR A CD2 563 C CE1 . TYR A 70 ? 0.1548 0.1592 0.1374 -0.0204 -0.0049 0.0065 101 TYR A CE1 564 C CE2 . TYR A 70 ? 0.1795 0.1792 0.1570 -0.0228 -0.0046 0.0057 101 TYR A CE2 565 C CZ . TYR A 70 ? 0.1858 0.1896 0.1663 -0.0222 -0.0051 0.0068 101 TYR A CZ 566 O OH . TYR A 70 ? 0.1458 0.1534 0.1267 -0.0241 -0.0060 0.0082 101 TYR A OH 567 N N . GLU A 71 ? 0.1243 0.1216 0.1039 -0.0194 -0.0049 0.0055 102 GLU A N 568 C CA . GLU A 71 ? 0.1354 0.1372 0.1163 -0.0203 -0.0046 0.0059 102 GLU A CA 569 C C . GLU A 71 ? 0.1828 0.1876 0.1669 -0.0186 -0.0040 0.0055 102 GLU A C 570 O O . GLU A 71 ? 0.1490 0.1521 0.1334 -0.0176 -0.0040 0.0053 102 GLU A O 571 C CB . GLU A 71 ? 0.1580 0.1591 0.1360 -0.0225 -0.0052 0.0065 102 GLU A CB 572 C CG . GLU A 71 ? 0.2235 0.2304 0.2023 -0.0243 -0.0048 0.0069 102 GLU A CG 573 C CD . GLU A 71 ? 0.4191 0.4263 0.3947 -0.0272 -0.0055 0.0076 102 GLU A CD 574 O OE1 . GLU A 71 ? 0.3237 0.3256 0.2960 -0.0281 -0.0068 0.0080 102 GLU A OE1 575 O OE2 . GLU A 71 ? 0.3697 0.3827 0.3457 -0.0290 -0.0051 0.0077 102 GLU A OE2 576 N N . PHE A 72 ? 0.1246 0.1339 0.1105 -0.0188 -0.0037 0.0055 103 PHE A N 577 C CA . PHE A 72 ? 0.1384 0.1514 0.1264 -0.0180 -0.0031 0.0049 103 PHE A CA 578 C C . PHE A 72 ? 0.1897 0.2069 0.1773 -0.0195 -0.0025 0.0044 103 PHE A C 579 O O . PHE A 72 ? 0.2092 0.2316 0.1967 -0.0211 -0.0024 0.0045 103 PHE A O 580 C CB . PHE A 72 ? 0.1325 0.1492 0.1229 -0.0175 -0.0035 0.0048 103 PHE A CB 581 C CG . PHE A 72 ? 0.1660 0.1784 0.1567 -0.0161 -0.0041 0.0052 103 PHE A CG 582 C CD1 . PHE A 72 ? 0.1843 0.1949 0.1772 -0.0139 -0.0043 0.0039 103 PHE A CD1 583 C CD2 . PHE A 72 ? 0.1425 0.1528 0.1315 -0.0170 -0.0046 0.0063 103 PHE A CD2 584 C CE1 . PHE A 72 ? 0.1428 0.1501 0.1355 -0.0132 -0.0047 0.0045 103 PHE A CE1 585 C CE2 . PHE A 72 ? 0.2076 0.2148 0.1966 -0.0160 -0.0049 0.0064 103 PHE A CE2 586 C CZ . PHE A 72 ? 0.2031 0.2090 0.1933 -0.0145 -0.0049 0.0060 103 PHE A CZ 587 N N . LEU A 73 ? 0.1753 0.1911 0.1625 -0.0192 -0.0023 0.0041 104 LEU A N 588 C CA . LEU A 73 ? 0.1886 0.2081 0.1750 -0.0209 -0.0018 0.0038 104 LEU A CA 589 C C . LEU A 73 ? 0.2471 0.2735 0.2354 -0.0208 -0.0005 0.0016 104 LEU A C 590 O O . LEU A 73 ? 0.2723 0.3043 0.2603 -0.0223 0.0000 0.0007 104 LEU A O 591 C CB . LEU A 73 ? 0.1690 0.1843 0.1540 -0.0213 -0.0024 0.0047 104 LEU A CB 592 C CG . LEU A 73 ? 0.2619 0.2710 0.2447 -0.0216 -0.0037 0.0062 104 LEU A CG 593 C CD1 . LEU A 73 ? 0.2601 0.2664 0.2418 -0.0224 -0.0047 0.0072 104 LEU A CD1 594 C CD2 . LEU A 73 ? 0.2723 0.2819 0.2526 -0.0238 -0.0042 0.0068 104 LEU A CD2 595 N N . SER A 74 ? 0.1937 0.2205 0.1839 -0.0190 -0.0001 0.0002 105 SER A N 596 C CA . SER A 74 ? 0.2117 0.2437 0.2058 -0.0174 0.0004 -0.0034 105 SER A CA 597 C C . SER A 74 ? 0.1795 0.2091 0.1785 -0.0143 -0.0012 -0.0047 105 SER A C 598 O O . SER A 74 ? 0.1836 0.2073 0.1821 -0.0133 -0.0020 -0.0036 105 SER A O 599 C CB . SER A 74 ? 0.3226 0.3562 0.3151 -0.0186 0.0017 -0.0045 105 SER A CB 600 O OG . SER A 74 ? 0.3767 0.4170 0.3723 -0.0179 0.0028 -0.0091 105 SER A OG 601 N N . LEU A 75 ? 0.1643 0.2002 0.1684 -0.0134 -0.0015 -0.0069 106 LEU A N 602 C CA . LEU A 75 ? 0.1431 0.1789 0.1536 -0.0108 -0.0032 -0.0082 106 LEU A CA 603 C C . LEU A 75 ? 0.2087 0.2539 0.2246 -0.0096 -0.0016 -0.0134 106 LEU A C 604 O O . LEU A 75 ? 0.2075 0.2606 0.2277 -0.0088 -0.0010 -0.0144 106 LEU A O 605 C CB . LEU A 75 ? 0.1566 0.1924 0.1702 -0.0101 -0.0052 -0.0054 106 LEU A CB 606 C CG . LEU A 75 ? 0.1190 0.1462 0.1277 -0.0107 -0.0060 -0.0024 106 LEU A CG 607 C CD1 . LEU A 75 ? 0.1522 0.1810 0.1621 -0.0110 -0.0073 -0.0004 106 LEU A CD1 608 C CD2 . LEU A 75 ? 0.1479 0.1689 0.1570 -0.0093 -0.0070 -0.0025 106 LEU A CD2 609 N N . ARG A 76 ? 0.1425 0.1870 0.1581 -0.0095 -0.0004 -0.0172 107 ARG A N 610 C CA . ARG A 76 ? 0.1631 0.2163 0.1828 -0.0088 0.0021 -0.0239 107 ARG A CA 611 C C . ARG A 76 ? 0.1350 0.1867 0.1606 -0.0065 0.0025 -0.0296 107 ARG A C 612 O O . ARG A 76 ? 0.1718 0.2154 0.1920 -0.0082 0.0015 -0.0287 107 ARG A O 613 C CB . ARG A 76 ? 0.1377 0.1936 0.1489 -0.0128 0.0043 -0.0241 107 ARG A CB 614 C CG . ARG A 76 ? 0.2796 0.3447 0.2928 -0.0136 0.0065 -0.0315 107 ARG A CG 615 C CD . ARG A 76 ? 0.3075 0.3746 0.3140 -0.0180 0.0071 -0.0292 107 ARG A CD 616 N NE . ARG A 76 ? 0.4812 0.5427 0.4851 -0.0199 0.0079 -0.0249 107 ARG A NE 617 C CZ . ARG A 76 ? 0.6886 0.7532 0.6908 -0.0234 0.0084 -0.0250 107 ARG A CZ 618 N NH1 . ARG A 76 ? 0.3392 0.4128 0.3427 -0.0257 0.0090 -0.0291 107 ARG A NH1 619 N NH2 . ARG A 76 ? 0.3175 0.3768 0.3158 -0.0249 0.0081 -0.0215 107 ARG A NH2 620 N N . SER A 77 ? 0.0898 0.1442 0.1230 -0.0015 0.0043 -0.0341 108 SER A N 621 C CA . SER A 77 ? 0.1034 0.1500 0.1381 0.0014 0.0054 -0.0391 108 SER A CA 622 C C . SER A 77 ? 0.1722 0.2241 0.2030 -0.0012 0.0087 -0.0443 108 SER A C 623 O O . SER A 77 ? 0.1873 0.2481 0.2193 -0.0017 0.0101 -0.0451 108 SER A O 624 C CB . SER A 77 ? 0.1613 0.2059 0.2061 0.0085 0.0052 -0.0407 108 SER A CB 625 O OG . SER A 77 ? 0.2112 0.2475 0.2562 0.0106 0.0066 -0.0458 108 SER A OG 626 N N . LEU A 78 ? 0.1484 0.1937 0.1741 -0.0038 0.0087 -0.0454 109 LEU A N 627 C CA . LEU A 78 ? 0.1345 0.1840 0.1570 -0.0067 0.0110 -0.0482 109 LEU A CA 628 C C . LEU A 78 ? 0.2886 0.3343 0.3154 -0.0026 0.0131 -0.0541 109 LEU A C 629 O O . LEU A 78 ? 0.3382 0.3871 0.3627 -0.0045 0.0154 -0.0577 109 LEU A O 630 C CB . LEU A 78 ? 0.2198 0.2655 0.2349 -0.0114 0.0101 -0.0446 109 LEU A CB 631 C CG . LEU A 78 ? 0.2624 0.3100 0.2731 -0.0146 0.0086 -0.0376 109 LEU A CG 632 C CD1 . LEU A 78 ? 0.3668 0.4066 0.3721 -0.0160 0.0070 -0.0332 109 LEU A CD1 633 C CD2 . LEU A 78 ? 0.3148 0.3722 0.3238 -0.0185 0.0099 -0.0368 109 LEU A CD2 634 N N . ASP A 79 ? 0.2072 0.2458 0.2402 0.0031 0.0122 -0.0547 110 ASP A N 635 C CA . ASP A 79 ? 0.2642 0.2968 0.3018 0.0079 0.0137 -0.0591 110 ASP A CA 636 C C . ASP A 79 ? 0.2645 0.2989 0.3115 0.0144 0.0130 -0.0581 110 ASP A C 637 O O . ASP A 79 ? 0.2335 0.2585 0.2846 0.0184 0.0106 -0.0558 110 ASP A O 638 C CB . ASP A 79 ? 0.2412 0.2597 0.2756 0.0075 0.0120 -0.0586 110 ASP A CB 639 C CG . ASP A 79 ? 0.4093 0.4273 0.4349 0.0015 0.0127 -0.0591 110 ASP A CG 640 O OD1 . ASP A 79 ? 0.3808 0.4016 0.4047 0.0006 0.0155 -0.0640 110 ASP A OD1 641 O OD2 . ASP A 79 ? 0.3211 0.3366 0.3417 -0.0022 0.0104 -0.0545 110 ASP A OD2 642 N N . MLY A 80 ? 0.2290 0.2759 0.2790 0.0149 0.0147 -0.0587 111 MLY A N 643 C CA . MLY A 80 ? 0.3140 0.3664 0.3727 0.0202 0.0141 -0.0565 111 MLY A CA 644 C CB . MLY A 80 ? 0.3375 0.4049 0.3959 0.0176 0.0158 -0.0560 111 MLY A CB 645 C CG . MLY A 80 ? 0.5824 0.6524 0.6337 0.0113 0.0136 -0.0509 111 MLY A CG 646 C CD . MLY A 80 ? 0.7125 0.7934 0.7645 0.0095 0.0131 -0.0467 111 MLY A CD 647 C CE . MLY A 80 ? 0.7263 0.8078 0.7686 0.0023 0.0115 -0.0424 111 MLY A CE 648 N NZ . MLY A 80 ? 0.8765 0.9668 0.9133 -0.0028 0.0131 -0.0433 111 MLY A NZ 649 C CH1 . MLY A 80 ? 0.5975 0.6855 0.6243 -0.0092 0.0110 -0.0387 111 MLY A CH1 650 C CH2 . MLY A 80 ? 0.7493 0.8487 0.7912 -0.0011 0.0137 -0.0420 111 MLY A CH2 651 C C . MLY A 80 ? 0.3926 0.4384 0.4594 0.0278 0.0143 -0.0583 111 MLY A C 652 O O . MLY A 80 ? 0.3374 0.3841 0.4114 0.0324 0.0121 -0.0541 111 MLY A O 653 N N . GLY A 81 ? 0.2577 0.2971 0.3228 0.0287 0.0167 -0.0638 112 GLY A N 654 C CA . GLY A 81 ? 0.3252 0.3563 0.3967 0.0357 0.0171 -0.0659 112 GLY A CA 655 C C . GLY A 81 ? 0.3823 0.3977 0.4535 0.0374 0.0133 -0.0621 112 GLY A C 656 O O . GLY A 81 ? 0.3478 0.3557 0.4249 0.0436 0.0123 -0.0613 112 GLY A O 657 N N . ILE A 82 ? 0.2242 0.2344 0.2883 0.0317 0.0111 -0.0592 113 ILE A N 658 C CA . ILE A 82 ? 0.2318 0.2275 0.2939 0.0316 0.0074 -0.0550 113 ILE A CA 659 C C . ILE A 82 ? 0.2388 0.2364 0.3043 0.0322 0.0032 -0.0476 113 ILE A C 660 O O . ILE A 82 ? 0.2347 0.2247 0.3044 0.0359 0.0001 -0.0431 113 ILE A O 661 C CB . ILE A 82 ? 0.1952 0.1842 0.2471 0.0248 0.0075 -0.0562 113 ILE A CB 662 C CG1 . ILE A 82 ? 0.3237 0.3108 0.3716 0.0238 0.0113 -0.0632 113 ILE A CG1 663 C CG2 . ILE A 82 ? 0.2863 0.2610 0.3357 0.0238 0.0038 -0.0513 113 ILE A CG2 664 C CD1 . ILE A 82 ? 0.3766 0.3612 0.4142 0.0165 0.0117 -0.0642 113 ILE A CD1 665 N N . MET A 83 ? 0.2024 0.2097 0.2653 0.0280 0.0031 -0.0461 114 MET A N 666 C CA . MET A 83 ? 0.1410 0.1510 0.2058 0.0275 -0.0006 -0.0394 114 MET A CA 667 C C . MET A 83 ? 0.1382 0.1643 0.2047 0.0265 0.0009 -0.0392 114 MET A C 668 O O . MET A 83 ? 0.1877 0.2208 0.2494 0.0226 0.0041 -0.0431 114 MET A O 669 C CB . MET A 83 ? 0.1453 0.1484 0.2027 0.0220 -0.0024 -0.0373 114 MET A CB 670 C CG . MET A 83 ? 0.1885 0.1907 0.2459 0.0208 -0.0068 -0.0292 114 MET A CG 671 S SD . MET A 83 ? 0.2199 0.2178 0.2654 0.0124 -0.0079 -0.0253 114 MET A SD 672 C CE . MET A 83 ? 0.1553 0.1675 0.1964 0.0084 -0.0051 -0.0268 114 MET A CE 673 N N . ALA A 84 ? 0.1829 0.2147 0.2545 0.0285 -0.0017 -0.0335 115 ALA A N 674 C CA . ALA A 84 ? 0.1296 0.1760 0.2009 0.0258 -0.0008 -0.0317 115 ALA A CA 675 C C . ALA A 84 ? 0.1878 0.2348 0.2518 0.0194 -0.0021 -0.0289 115 ALA A C 676 O O . ALA A 84 ? 0.1472 0.1835 0.2065 0.0175 -0.0039 -0.0273 115 ALA A O 677 C CB . ALA A 84 ? 0.1758 0.2273 0.2535 0.0290 -0.0036 -0.0257 115 ALA A CB 678 N N . ASP A 85 ? 0.1873 0.2442 0.2474 0.0150 -0.0014 -0.0267 116 ASP A N 679 C CA . ASP A 85 ? 0.1612 0.2173 0.2127 0.0084 -0.0025 -0.0234 116 ASP A CA 680 C C . ASP A 85 ? 0.1605 0.2083 0.2105 0.0078 -0.0067 -0.0176 116 ASP A C 681 O O . ASP A 85 ? 0.1711 0.2194 0.2268 0.0109 -0.0094 -0.0141 116 ASP A O 682 C CB . ASP A 85 ? 0.1278 0.1914 0.1743 0.0042 -0.0017 -0.0203 116 ASP A CB 683 C CG . ASP A 85 ? 0.2849 0.3555 0.3287 0.0024 0.0021 -0.0249 116 ASP A CG 684 O OD1 . ASP A 85 ? 0.2129 0.2819 0.2551 0.0024 0.0043 -0.0302 116 ASP A OD1 685 O OD2 . ASP A 85 ? 0.3001 0.3772 0.3424 0.0003 0.0027 -0.0231 116 ASP A OD2 686 N N . PRO A 86 ? 0.1563 0.1958 0.1977 0.0036 -0.0073 -0.0160 117 PRO A N 687 C CA . PRO A 86 ? 0.1380 0.1703 0.1765 0.0021 -0.0107 -0.0105 117 PRO A CA 688 C C . PRO A 86 ? 0.1669 0.2053 0.2039 -0.0003 -0.0122 -0.0059 117 PRO A C 689 O O . PRO A 86 ? 0.1348 0.1777 0.1686 -0.0026 -0.0101 -0.0058 117 PRO A O 690 C CB . PRO A 86 ? 0.1485 0.1740 0.1787 -0.0019 -0.0101 -0.0108 117 PRO A CB 691 C CG . PRO A 86 ? 0.1512 0.1829 0.1784 -0.0042 -0.0073 -0.0143 117 PRO A CG 692 C CD . PRO A 86 ? 0.1715 0.2095 0.2056 -0.0003 -0.0051 -0.0188 117 PRO A CD 693 N N . THR A 87 ? 0.1265 0.1613 0.1628 -0.0005 -0.0151 -0.0013 118 THR A N 694 C CA . THR A 87 ? 0.2232 0.2605 0.2553 -0.0024 -0.0154 0.0009 118 THR A CA 695 C C . THR A 87 ? 0.1908 0.2191 0.2137 -0.0056 -0.0151 0.0034 118 THR A C 696 O O . THR A 87 ? 0.1534 0.1756 0.1745 -0.0060 -0.0155 0.0041 118 THR A O 697 C CB . THR A 87 ? 0.2540 0.2959 0.2930 0.0012 -0.0180 0.0037 118 THR A CB 698 O OG1 . THR A 87 ? 0.2270 0.2605 0.2669 0.0026 -0.0206 0.0071 118 THR A OG1 699 C CG2 . THR A 87 ? 0.2537 0.3055 0.3026 0.0056 -0.0169 0.0017 118 THR A CG2 700 N N . VAL A 88 ? 0.1318 0.1596 0.1498 -0.0078 -0.0143 0.0049 119 VAL A N 701 C CA . VAL A 88 ? 0.1265 0.1479 0.1372 -0.0104 -0.0135 0.0072 119 VAL A CA 702 C C . VAL A 88 ? 0.1535 0.1779 0.1639 -0.0118 -0.0149 0.0102 119 VAL A C 703 O O . VAL A 88 ? 0.2018 0.2323 0.2154 -0.0115 -0.0155 0.0099 119 VAL A O 704 C CB . VAL A 88 ? 0.1553 0.1727 0.1596 -0.0121 -0.0105 0.0064 119 VAL A CB 705 C CG1 . VAL A 88 ? 0.1905 0.2049 0.1947 -0.0109 -0.0094 0.0041 119 VAL A CG1 706 C CG2 . VAL A 88 ? 0.2043 0.2255 0.2074 -0.0136 -0.0095 0.0063 119 VAL A CG2 707 N N . ASN A 89 ? 0.1465 0.1673 0.1533 -0.0139 -0.0155 0.0130 120 ASN A N 708 C CA . ASN A 89 ? 0.1331 0.1570 0.1396 -0.0160 -0.0172 0.0161 120 ASN A CA 709 C C . ASN A 89 ? 0.1986 0.2219 0.1989 -0.0198 -0.0151 0.0165 120 ASN A C 710 O O . ASN A 89 ? 0.1564 0.1805 0.1543 -0.0229 -0.0159 0.0190 120 ASN A O 711 C CB . ASN A 89 ? 0.1769 0.1984 0.1839 -0.0169 -0.0196 0.0196 120 ASN A CB 712 C CG . ASN A 89 ? 0.1786 0.1943 0.1795 -0.0201 -0.0178 0.0200 120 ASN A CG 713 O OD1 . ASN A 89 ? 0.1678 0.1802 0.1653 -0.0199 -0.0150 0.0174 120 ASN A OD1 714 N ND2 . ASN A 89 ? 0.2381 0.2534 0.2379 -0.0231 -0.0195 0.0232 120 ASN A ND2 715 N N . VAL A 90 ? 0.1506 0.1723 0.1480 -0.0202 -0.0126 0.0144 121 VAL A N 716 C CA . VAL A 90 ? 0.1249 0.1453 0.1161 -0.0238 -0.0108 0.0149 121 VAL A CA 717 C C . VAL A 90 ? 0.1874 0.2116 0.1792 -0.0239 -0.0101 0.0138 121 VAL A C 718 O O . VAL A 90 ? 0.1581 0.1846 0.1542 -0.0210 -0.0102 0.0120 121 VAL A O 719 C CB . VAL A 90 ? 0.1936 0.2073 0.1813 -0.0229 -0.0089 0.0124 121 VAL A CB 720 C CG1 . VAL A 90 ? 0.1560 0.1672 0.1430 -0.0229 -0.0093 0.0126 121 VAL A CG1 721 C CG2 . VAL A 90 ? 0.1621 0.1737 0.1508 -0.0203 -0.0078 0.0107 121 VAL A CG2 722 N N . PRO A 91 ? 0.2023 0.2272 0.1895 -0.0274 -0.0093 0.0145 122 PRO A N 723 C CA . PRO A 91 ? 0.1591 0.1870 0.1456 -0.0283 -0.0085 0.0137 122 PRO A CA 724 C C . PRO A 91 ? 0.1616 0.1849 0.1479 -0.0259 -0.0071 0.0113 122 PRO A C 725 O O . PRO A 91 ? 0.1672 0.1841 0.1525 -0.0241 -0.0066 0.0099 122 PRO A O 726 C CB . PRO A 91 ? 0.1886 0.2141 0.1710 -0.0312 -0.0084 0.0132 122 PRO A CB 727 C CG . PRO A 91 ? 0.2913 0.3167 0.2730 -0.0326 -0.0094 0.0145 122 PRO A CG 728 C CD . PRO A 91 ? 0.2073 0.2295 0.1911 -0.0297 -0.0095 0.0143 122 PRO A CD 729 N N . LEU A 92 ? 0.1483 0.1757 0.1352 -0.0260 -0.0065 0.0108 123 LEU A N 730 C CA . LEU A 92 ? 0.1483 0.1720 0.1349 -0.0243 -0.0054 0.0089 123 LEU A CA 731 C C . LEU A 92 ? 0.2120 0.2284 0.1955 -0.0244 -0.0051 0.0080 123 LEU A C 732 O O . LEU A 92 ? 0.1809 0.1934 0.1645 -0.0225 -0.0046 0.0070 123 LEU A O 733 C CB . LEU A 92 ? 0.2004 0.2310 0.1881 -0.0249 -0.0047 0.0083 123 LEU A CB 734 C CG . LEU A 92 ? 0.3088 0.3461 0.3045 -0.0219 -0.0057 0.0066 123 LEU A CG 735 C CD1 . LEU A 92 ? 0.2291 0.2734 0.2264 -0.0224 -0.0048 0.0050 123 LEU A CD1 736 C CD2 . LEU A 92 ? 0.2658 0.2994 0.2654 -0.0182 -0.0062 0.0050 123 LEU A CD2 737 N N . LEU A 93 ? 0.1758 0.1911 0.1563 -0.0269 -0.0055 0.0085 124 LEU A N 738 C CA . LEU A 93 ? 0.0869 0.0958 0.0637 -0.0276 -0.0056 0.0079 124 LEU A CA 739 C C . LEU A 93 ? 0.1508 0.1577 0.1252 -0.0292 -0.0059 0.0080 124 LEU A C 740 O O . LEU A 93 ? 0.1474 0.1585 0.1216 -0.0316 -0.0064 0.0090 124 LEU A O 741 C CB . LEU A 93 ? 0.1219 0.1314 0.0957 -0.0306 -0.0059 0.0083 124 LEU A CB 742 C CG . LEU A 93 ? 0.1939 0.1968 0.1622 -0.0328 -0.0066 0.0081 124 LEU A CG 743 C CD1 . LEU A 93 ? 0.1752 0.1724 0.1430 -0.0306 -0.0067 0.0074 124 LEU A CD1 744 C CD2 . LEU A 93 ? 0.1629 0.1674 0.1278 -0.0368 -0.0073 0.0089 124 LEU A CD2 745 N N . GLY A 94 ? 0.1406 0.1422 0.1132 -0.0283 -0.0056 0.0070 125 GLY A N 746 C CA . GLY A 94 ? 0.1870 0.1865 0.1565 -0.0304 -0.0055 0.0067 125 GLY A CA 747 C C . GLY A 94 ? 0.2439 0.2373 0.2102 -0.0301 -0.0048 0.0053 125 GLY A C 748 O O . GLY A 94 ? 0.1894 0.1796 0.1554 -0.0285 -0.0048 0.0048 125 GLY A O 749 N N . THR A 95 ? 0.1863 0.1780 0.1495 -0.0323 -0.0043 0.0047 126 THR A N 750 C CA A THR A 95 ? 0.2601 0.2459 0.2191 -0.0330 -0.0030 0.0030 126 THR A CA 751 C CA B THR A 95 ? 0.2294 0.2151 0.1885 -0.0328 -0.0030 0.0030 126 THR A CA 752 C C . THR A 95 ? 0.2003 0.1883 0.1635 -0.0301 -0.0024 0.0026 126 THR A C 753 O O . THR A 95 ? 0.1502 0.1428 0.1168 -0.0294 -0.0030 0.0035 126 THR A O 754 C CB A THR A 95 ? 0.2424 0.2257 0.1951 -0.0378 -0.0022 0.0022 126 THR A CB 755 C CB B THR A 95 ? 0.1637 0.1454 0.1157 -0.0376 -0.0019 0.0019 126 THR A CB 756 O OG1 A THR A 95 ? 0.2143 0.1972 0.1636 -0.0410 -0.0031 0.0030 126 THR A OG1 757 O OG1 B THR A 95 ? 0.1394 0.1263 0.0931 -0.0389 -0.0022 0.0025 126 THR A OG1 758 C CG2 A THR A 95 ? 0.2987 0.2748 0.2463 -0.0392 -0.0002 -0.0005 126 THR A CG2 759 C CG2 B THR A 95 ? 0.1338 0.1113 0.0797 -0.0412 -0.0024 0.0020 126 THR A CG2 760 N N . VAL A 96 ? 0.1618 0.1457 0.1237 -0.0289 -0.0014 0.0012 127 VAL A N 761 C CA . VAL A 96 ? 0.1300 0.1160 0.0949 -0.0271 -0.0006 0.0006 127 VAL A CA 762 C C . VAL A 96 ? 0.1305 0.1160 0.0918 -0.0306 0.0009 -0.0006 127 VAL A C 763 O O . VAL A 96 ? 0.1720 0.1530 0.1297 -0.0323 0.0018 -0.0032 127 VAL A O 764 C CB . VAL A 96 ? 0.1517 0.1350 0.1189 -0.0241 -0.0003 -0.0014 127 VAL A CB 765 C CG1 . VAL A 96 ? 0.1743 0.1607 0.1446 -0.0229 0.0005 -0.0021 127 VAL A CG1 766 C CG2 . VAL A 96 ? 0.1932 0.1770 0.1626 -0.0220 -0.0018 0.0003 127 VAL A CG2 767 N N . PRO A 97 ? 0.1656 0.1560 0.1298 -0.0306 0.0003 0.0002 128 PRO A N 768 C CA . PRO A 97 ? 0.1838 0.1745 0.1442 -0.0347 0.0014 -0.0008 128 PRO A CA 769 C C . PRO A 97 ? 0.1719 0.1602 0.1299 -0.0361 0.0042 -0.0041 128 PRO A C 770 O O . PRO A 97 ? 0.1744 0.1630 0.1357 -0.0329 0.0045 -0.0052 128 PRO A O 771 C CB . PRO A 97 ? 0.1522 0.1482 0.1163 -0.0340 -0.0005 0.0014 128 PRO A CB 772 C CG . PRO A 97 ? 0.1492 0.1463 0.1185 -0.0294 -0.0013 0.0023 128 PRO A CG 773 C CD . PRO A 97 ? 0.1368 0.1316 0.1066 -0.0275 -0.0014 0.0021 128 PRO A CD 774 N N . HIS A 98 ? 0.1320 0.1184 0.0856 -0.0394 0.0055 -0.0067 129 HIS A N 775 C CA . HIS A 98 ? 0.1797 0.1645 0.1319 -0.0396 0.0078 -0.0114 129 HIS A CA 776 C C . HIS A 98 ? 0.3131 0.3039 0.2665 -0.0418 0.0085 -0.0105 129 HIS A C 777 O O . HIS A 98 ? 0.2164 0.2081 0.1713 -0.0405 0.0102 -0.0135 129 HIS A O 778 C CB . HIS A 98 ? 0.1792 0.1599 0.1257 -0.0428 0.0093 -0.0150 129 HIS A CB 779 C CG . HIS A 98 ? 0.2260 0.1994 0.1714 -0.0405 0.0087 -0.0167 129 HIS A CG 780 N ND1 . HIS A 98 ? 0.3264 0.2952 0.2747 -0.0357 0.0088 -0.0194 129 HIS A ND1 781 C CD2 . HIS A 98 ? 0.4108 0.3810 0.3527 -0.0429 0.0076 -0.0157 129 HIS A CD2 782 C CE1 . HIS A 98 ? 0.3936 0.3560 0.3403 -0.0354 0.0077 -0.0198 129 HIS A CE1 783 N NE2 . HIS A 98 ? 0.3816 0.3446 0.3241 -0.0398 0.0071 -0.0178 129 HIS A NE2 784 N N . MLY A 99 ? 0.1792 0.1740 0.1324 -0.0452 0.0070 -0.0066 130 MLY A N 785 C CA . MLY A 99 ? 0.1859 0.1858 0.1412 -0.0457 0.0059 -0.0056 130 MLY A CA 786 C CB . MLY A 99 ? 0.1914 0.1942 0.1449 -0.0489 0.0038 -0.0032 130 MLY A CB 787 C CG . MLY A 99 ? 0.3090 0.3162 0.2628 -0.0511 0.0032 -0.0027 130 MLY A CG 788 C CD . MLY A 99 ? 0.3137 0.3230 0.2701 -0.0500 -0.0008 0.0018 130 MLY A CD 789 C CE . MLY A 99 ? 0.3001 0.3131 0.2565 -0.0523 -0.0026 0.0037 130 MLY A CE 790 N NZ . MLY A 99 ? 0.3055 0.3203 0.2639 -0.0522 -0.0063 0.0080 130 MLY A NZ 791 C CH1 . MLY A 99 ? 0.4414 0.4588 0.3954 -0.0578 -0.0068 0.0088 130 MLY A CH1 792 C CH2 . MLY A 99 ? 0.3594 0.3766 0.3182 -0.0539 -0.0085 0.0103 130 MLY A CH2 793 C C . MLY A 99 ? 0.2082 0.2092 0.1694 -0.0402 0.0035 -0.0028 130 MLY A C 794 O O . MLY A 99 ? 0.2520 0.2524 0.2159 -0.0371 0.0013 -0.0004 130 MLY A O 795 N N . ALA A 100 ? 0.1980 0.2011 0.1610 -0.0397 0.0041 -0.0036 131 ALA A N 796 C CA . ALA A 100 ? 0.1896 0.1934 0.1574 -0.0353 0.0021 -0.0013 131 ALA A CA 797 C C . ALA A 100 ? 0.2291 0.2338 0.1989 -0.0342 -0.0010 0.0024 131 ALA A C 798 O O . ALA A 100 ? 0.2054 0.2122 0.1733 -0.0377 -0.0022 0.0036 131 ALA A O 799 C CB . ALA A 100 ? 0.1271 0.1336 0.0956 -0.0363 0.0030 -0.0026 131 ALA A CB 800 N N . SER A 101 ? 0.1739 0.1772 0.1469 -0.0300 -0.0022 0.0039 132 SER A N 801 C CA . SER A 101 ? 0.1690 0.1732 0.1441 -0.0292 -0.0045 0.0067 132 SER A CA 802 C C . SER A 101 ? 0.1763 0.1797 0.1547 -0.0253 -0.0054 0.0077 132 SER A C 803 O O . SER A 101 ? 0.1547 0.1569 0.1340 -0.0227 -0.0043 0.0061 132 SER A O 804 C CB . SER A 101 ? 0.2251 0.2291 0.1994 -0.0297 -0.0048 0.0070 132 SER A CB 805 O OG . SER A 101 ? 0.2223 0.2263 0.1925 -0.0335 -0.0037 0.0056 132 SER A OG 806 N N . VAL A 102 ? 0.1484 0.1528 0.1287 -0.0258 -0.0076 0.0102 133 VAL A N 807 C CA . VAL A 102 ? 0.1604 0.1638 0.1434 -0.0232 -0.0087 0.0113 133 VAL A CA 808 C C . VAL A 102 ? 0.1979 0.2016 0.1835 -0.0214 -0.0094 0.0118 133 VAL A C 809 O O . VAL A 102 ? 0.1945 0.2002 0.1805 -0.0232 -0.0104 0.0132 133 VAL A O 810 C CB . VAL A 102 ? 0.2252 0.2294 0.2098 -0.0259 -0.0115 0.0140 133 VAL A CB 811 C CG1 . VAL A 102 ? 0.2880 0.2905 0.2759 -0.0240 -0.0134 0.0156 133 VAL A CG1 812 C CG2 . VAL A 102 ? 0.2486 0.2542 0.2311 -0.0282 -0.0122 0.0122 133 VAL A CG2 813 N N . VAL A 103 ? 0.1391 0.1416 0.1263 -0.0187 -0.0088 0.0106 134 VAL A N 814 C CA . VAL A 103 ? 0.1292 0.1325 0.1189 -0.0177 -0.0095 0.0112 134 VAL A CA 815 C C . VAL A 103 ? 0.2149 0.2172 0.2076 -0.0170 -0.0116 0.0129 134 VAL A C 816 O O . VAL A 103 ? 0.2041 0.2045 0.1963 -0.0159 -0.0112 0.0118 134 VAL A O 817 C CB . VAL A 103 ? 0.2151 0.2178 0.2042 -0.0162 -0.0077 0.0091 134 VAL A CB 818 C CG1 . VAL A 103 ? 0.2150 0.2196 0.2061 -0.0161 -0.0084 0.0099 134 VAL A CG1 819 C CG2 . VAL A 103 ? 0.2897 0.2920 0.2761 -0.0170 -0.0063 0.0076 134 VAL A CG2 820 N N . GLN A 104 ? 0.1848 0.1885 0.1811 -0.0182 -0.0144 0.0160 135 GLN A N 821 C CA . GLN A 104 ? 0.2015 0.2039 0.2031 -0.0169 -0.0175 0.0174 135 GLN A CA 822 C C . GLN A 104 ? 0.2240 0.2289 0.2299 -0.0134 -0.0171 0.0140 135 GLN A C 823 O O . GLN A 104 ? 0.2036 0.2135 0.2117 -0.0122 -0.0169 0.0131 135 GLN A O 824 C CB . GLN A 104 ? 0.2858 0.2902 0.2915 -0.0177 -0.0211 0.0210 135 GLN A CB 825 C CG . GLN A 104 ? 0.4675 0.4713 0.4698 -0.0225 -0.0218 0.0237 135 GLN A CG 826 C CD . GLN A 104 ? 0.7596 0.7653 0.7657 -0.0223 -0.0258 0.0275 135 GLN A CD 827 O OE1 . GLN A 104 ? 0.5678 0.5719 0.5792 -0.0185 -0.0286 0.0288 135 GLN A OE1 828 N NE2 . GLN A 104 ? 0.6489 0.6574 0.6522 -0.0260 -0.0262 0.0296 135 GLN A NE2 829 N N . VAL A 105 ? 0.1699 0.1721 0.1772 -0.0121 -0.0169 0.0119 136 VAL A N 830 C CA . VAL A 105 ? 0.1503 0.1556 0.1623 -0.0097 -0.0164 0.0084 136 VAL A CA 831 C C . VAL A 105 ? 0.1884 0.1926 0.2092 -0.0072 -0.0208 0.0095 136 VAL A C 832 O O . VAL A 105 ? 0.1851 0.1827 0.2063 -0.0079 -0.0228 0.0110 136 VAL A O 833 C CB . VAL A 105 ? 0.2135 0.2171 0.2224 -0.0096 -0.0132 0.0048 136 VAL A CB 834 C CG1 . VAL A 105 ? 0.1922 0.1995 0.2054 -0.0083 -0.0128 0.0011 136 VAL A CG1 835 C CG2 . VAL A 105 ? 0.2088 0.2126 0.2121 -0.0100 -0.0100 0.0042 136 VAL A CG2 836 N N . GLY A 106 ? 0.1366 0.1465 0.1643 -0.0037 -0.0215 0.0086 137 GLY A N 837 C CA . GLY A 106 ? 0.1479 0.1552 0.1841 0.0014 -0.0236 0.0087 137 GLY A CA 838 C C . GLY A 106 ? 0.1673 0.1735 0.2064 0.0044 -0.0204 0.0024 137 GLY A C 839 O O . GLY A 106 ? 0.1577 0.1703 0.1955 0.0033 -0.0176 -0.0012 137 GLY A O 840 N N . PHE A 107 ? 0.1346 0.1320 0.1771 0.0075 -0.0210 0.0012 138 PHE A N 841 C CA . PHE A 107 ? 0.1884 0.1833 0.2331 0.0100 -0.0179 -0.0056 138 PHE A CA 842 C C . PHE A 107 ? 0.2012 0.1949 0.2558 0.0171 -0.0187 -0.0069 138 PHE A C 843 O O . PHE A 107 ? 0.1940 0.1767 0.2507 0.0193 -0.0207 -0.0059 138 PHE A O 844 C CB . PHE A 107 ? 0.1668 0.1511 0.2058 0.0067 -0.0175 -0.0068 138 PHE A CB 845 C CG . PHE A 107 ? 0.1760 0.1614 0.2071 0.0007 -0.0174 -0.0043 138 PHE A CG 846 C CD1 . PHE A 107 ? 0.1591 0.1520 0.1866 -0.0017 -0.0151 -0.0065 138 PHE A CD1 847 C CD2 . PHE A 107 ? 0.1653 0.1440 0.1926 -0.0025 -0.0196 0.0001 138 PHE A CD2 848 C CE1 . PHE A 107 ? 0.1864 0.1798 0.2077 -0.0062 -0.0150 -0.0044 138 PHE A CE1 849 C CE2 . PHE A 107 ? 0.2024 0.1832 0.2234 -0.0074 -0.0190 0.0017 138 PHE A CE2 850 C CZ . PHE A 107 ? 0.1743 0.1626 0.1923 -0.0083 -0.0163 -0.0006 138 PHE A CZ 851 N N . PRO A 108 ? 0.1538 0.1590 0.2151 0.0207 -0.0175 -0.0089 139 PRO A N 852 C CA . PRO A 108 ? 0.1807 0.1861 0.2503 0.0272 -0.0180 -0.0092 139 PRO A CA 853 C C . PRO A 108 ? 0.2075 0.2081 0.2798 0.0311 -0.0146 -0.0162 139 PRO A C 854 O O . PRO A 108 ? 0.2063 0.2163 0.2819 0.0332 -0.0110 -0.0213 139 PRO A O 855 C CB . PRO A 108 ? 0.1940 0.2149 0.2671 0.0278 -0.0176 -0.0076 139 PRO A CB 856 C CG . PRO A 108 ? 0.1760 0.2047 0.2448 0.0230 -0.0152 -0.0104 139 PRO A CG 857 C CD . PRO A 108 ? 0.1205 0.1389 0.1798 0.0178 -0.0156 -0.0096 139 PRO A CD 858 N N . CYS A 109 ? 0.1709 0.1573 0.2402 0.0309 -0.0154 -0.0162 140 CYS A N 859 C CA . CYS A 109 ? 0.1890 0.1694 0.2596 0.0341 -0.0123 -0.0224 140 CYS A CA 860 C C . CYS A 109 ? 0.3229 0.3082 0.4019 0.0410 -0.0121 -0.0222 140 CYS A C 861 O O . CYS A 109 ? 0.2833 0.2683 0.3654 0.0432 -0.0158 -0.0157 140 CYS A O 862 C CB . CYS A 109 ? 0.2502 0.2148 0.3154 0.0320 -0.0138 -0.0209 140 CYS A CB 863 S SG . CYS A 109 ? 0.3022 0.2622 0.3571 0.0236 -0.0136 -0.0212 140 CYS A SG 864 N N . LEU A 110 ? 0.2402 0.2315 0.3224 0.0440 -0.0078 -0.0291 141 LEU A N 865 C CA . LEU A 110 ? 0.3356 0.3334 0.4265 0.0509 -0.0069 -0.0295 141 LEU A CA 866 C C . LEU A 110 ? 0.4283 0.4134 0.5225 0.0565 -0.0082 -0.0285 141 LEU A C 867 O O . LEU A 110 ? 0.3685 0.3574 0.4702 0.0626 -0.0095 -0.0257 141 LEU A O 868 C CB . LEU A 110 ? 0.2660 0.2757 0.3590 0.0518 -0.0015 -0.0369 141 LEU A CB 869 C CG . LEU A 110 ? 0.2804 0.3042 0.3706 0.0465 -0.0002 -0.0371 141 LEU A CG 870 C CD1 . LEU A 110 ? 0.3958 0.4299 0.4864 0.0463 0.0051 -0.0441 141 LEU A CD1 871 C CD2 . LEU A 110 ? 0.3191 0.3529 0.4133 0.0468 -0.0033 -0.0299 141 LEU A CD2 872 N N . GLY A 111 ? 0.2745 0.2446 0.3625 0.0541 -0.0083 -0.0302 142 GLY A N 873 C CA . GLY A 111 ? 0.3103 0.2660 0.3995 0.0583 -0.0095 -0.0294 142 GLY A CA 874 C C . GLY A 111 ? 0.4515 0.4059 0.5446 0.0640 -0.0051 -0.0372 142 GLY A C 875 O O . GLY A 111 ? 0.4275 0.3707 0.5232 0.0690 -0.0057 -0.0370 142 GLY A O 876 N N . MLY A 112 ? 0.3470 0.3128 0.4403 0.0630 -0.0004 -0.0441 143 MLY A N 877 C CA . MLY A 112 ? 0.4206 0.3867 0.5167 0.0674 0.0045 -0.0523 143 MLY A CA 878 C CB . MLY A 112 ? 0.4493 0.4347 0.5486 0.0671 0.0086 -0.0569 143 MLY A CB 879 C CG . MLY A 112 ? 0.5503 0.5510 0.6574 0.0695 0.0068 -0.0512 143 MLY A CG 880 C CD . MLY A 112 ? 0.8619 0.8804 0.9719 0.0693 0.0118 -0.0568 143 MLY A CD 881 C CE . MLY A 112 ? 1.0449 1.0783 1.1531 0.0635 0.0111 -0.0533 143 MLY A CE 882 N NZ . MLY A 112 ? 0.9657 1.0158 1.0760 0.0626 0.0158 -0.0581 143 MLY A NZ 883 C CH1 . MLY A 112 ? 0.7217 0.7810 0.8250 0.0543 0.0157 -0.0565 143 MLY A CH1 884 C CH2 . MLY A 112 ? 0.9879 1.0495 1.1091 0.0684 0.0154 -0.0546 143 MLY A CH2 885 C C . MLY A 112 ? 0.5672 0.5220 0.6540 0.0629 0.0071 -0.0585 143 MLY A C 886 O O . MLY A 112 ? 0.4443 0.3917 0.5319 0.0669 0.0099 -0.0642 143 MLY A O 887 N N . GLN A 113 ? 0.4630 0.4169 0.5410 0.0547 0.0061 -0.0574 144 GLN A N 888 C CA A GLN A 113 ? 0.4190 0.3644 0.4872 0.0491 0.0082 -0.0623 144 GLN A CA 889 C CA B GLN A 113 ? 0.4218 0.3673 0.4900 0.0491 0.0082 -0.0623 144 GLN A CA 890 C C . GLN A 113 ? 0.4985 0.4337 0.5590 0.0429 0.0045 -0.0570 144 GLN A C 891 O O . GLN A 113 ? 0.4173 0.3566 0.4787 0.0409 0.0012 -0.0504 144 GLN A O 892 C CB A GLN A 113 ? 0.4249 0.3840 0.4895 0.0445 0.0119 -0.0676 144 GLN A CB 893 C CB B GLN A 113 ? 0.3670 0.3262 0.4315 0.0443 0.0118 -0.0674 144 GLN A CB 894 C CG A GLN A 113 ? 0.6474 0.6160 0.7169 0.0488 0.0166 -0.0746 144 GLN A CG 895 C CG B GLN A 113 ? 0.6061 0.5751 0.6754 0.0485 0.0165 -0.0744 144 GLN A CG 896 C CD A GLN A 113 ? 0.6204 0.6021 0.6849 0.0428 0.0198 -0.0787 144 GLN A CD 897 C CD B GLN A 113 ? 0.6182 0.6003 0.6823 0.0424 0.0196 -0.0785 144 GLN A CD 898 O OE1 A GLN A 113 ? 0.5295 0.5079 0.5847 0.0363 0.0201 -0.0804 144 GLN A OE1 899 O OE1 B GLN A 113 ? 0.5928 0.5894 0.6613 0.0437 0.0221 -0.0804 144 GLN A OE1 900 N NE2 A GLN A 113 ? 0.6001 0.5973 0.6700 0.0446 0.0220 -0.0801 144 GLN A NE2 901 N NE2 B GLN A 113 ? 0.3819 0.3595 0.4362 0.0354 0.0194 -0.0793 144 GLN A NE2 902 N N . ASP A 114 ? 0.4415 0.3642 0.4939 0.0393 0.0053 -0.0599 145 ASP A N 903 C CA . ASP A 114 ? 0.3432 0.2571 0.3871 0.0323 0.0026 -0.0556 145 ASP A CA 904 C C . ASP A 114 ? 0.3936 0.3164 0.4305 0.0258 0.0048 -0.0592 145 ASP A C 905 O O . ASP A 114 ? 0.4993 0.4253 0.5344 0.0258 0.0083 -0.0662 145 ASP A O 906 C CB . ASP A 114 ? 0.5725 0.4677 0.6107 0.0317 0.0024 -0.0570 145 ASP A CB 907 C CG . ASP A 114 ? 0.6977 0.5820 0.7419 0.0382 0.0005 -0.0536 145 ASP A CG 908 O OD1 . ASP A 114 ? 0.4085 0.2894 0.4535 0.0371 -0.0034 -0.0457 145 ASP A OD1 909 O OD2 . ASP A 114 ? 0.8986 0.7771 0.9460 0.0441 0.0027 -0.0587 145 ASP A OD2 910 N N . GLY A 115 ? 0.3025 0.2295 0.3354 0.0202 0.0027 -0.0544 146 GLY A N 911 C CA . GLY A 115 ? 0.3548 0.2902 0.3811 0.0141 0.0041 -0.0566 146 GLY A CA 912 C C . GLY A 115 ? 0.3478 0.2913 0.3731 0.0103 0.0020 -0.0509 146 GLY A C 913 O O . GLY A 115 ? 0.2950 0.2370 0.3239 0.0117 -0.0007 -0.0454 146 GLY A O 914 N N . VAL A 116 ? 0.2698 0.2216 0.2897 0.0054 0.0030 -0.0521 147 VAL A N 915 C CA . VAL A 116 ? 0.2523 0.2115 0.2702 0.0016 0.0013 -0.0470 147 VAL A CA 916 C C . VAL A 116 ? 0.3172 0.2904 0.3383 0.0025 0.0032 -0.0487 147 VAL A C 917 O O . VAL A 116 ? 0.3231 0.3021 0.3422 0.0015 0.0058 -0.0531 147 VAL A O 918 C CB . VAL A 116 ? 0.3104 0.2677 0.3193 -0.0047 0.0002 -0.0454 147 VAL A CB 919 C CG1 . VAL A 116 ? 0.3486 0.3139 0.3555 -0.0078 -0.0014 -0.0400 147 VAL A CG1 920 C CG2 . VAL A 116 ? 0.3796 0.3232 0.3846 -0.0064 -0.0018 -0.0437 147 VAL A CG2 921 N N . ALA A 117 ? 0.2770 0.2554 0.3026 0.0040 0.0017 -0.0451 148 ALA A N 922 C CA . ALA A 117 ? 0.2468 0.2381 0.2745 0.0042 0.0033 -0.0463 148 ALA A CA 923 C C . ALA A 117 ? 0.2245 0.2207 0.2464 -0.0008 0.0021 -0.0420 148 ALA A C 924 O O . ALA A 117 ? 0.1854 0.1772 0.2060 -0.0021 -0.0005 -0.0371 148 ALA A O 925 C CB . ALA A 117 ? 0.1846 0.1790 0.2210 0.0094 0.0023 -0.0452 148 ALA A CB 926 N N . ALA A 118 ? 0.1914 0.1968 0.2099 -0.0036 0.0040 -0.0432 149 ALA A N 927 C CA . ALA A 118 ? 0.1622 0.1726 0.1754 -0.0075 0.0030 -0.0382 149 ALA A CA 928 C C . ALA A 118 ? 0.1293 0.1467 0.1459 -0.0064 0.0027 -0.0368 149 ALA A C 929 O O . ALA A 118 ? 0.1549 0.1782 0.1765 -0.0039 0.0044 -0.0409 149 ALA A O 930 C CB . ALA A 118 ? 0.2195 0.2357 0.2281 -0.0107 0.0048 -0.0393 149 ALA A CB 931 N N . PHE A 119 ? 0.1441 0.1609 0.1576 -0.0081 0.0007 -0.0308 150 PHE A N 932 C CA . PHE A 119 ? 0.1432 0.1656 0.1583 -0.0078 0.0000 -0.0287 150 PHE A CA 933 C C . PHE A 119 ? 0.2146 0.2356 0.2234 -0.0099 -0.0009 -0.0215 150 PHE A C 934 O O . PHE A 119 ? 0.1548 0.1705 0.1600 -0.0107 -0.0018 -0.0186 150 PHE A O 935 C CB . PHE A 119 ? 0.1473 0.1667 0.1691 -0.0047 -0.0023 -0.0285 150 PHE A CB 936 C CG . PHE A 119 ? 0.1537 0.1644 0.1740 -0.0056 -0.0051 -0.0241 150 PHE A CG 937 C CD1 . PHE A 119 ? 0.2132 0.2150 0.2341 -0.0047 -0.0056 -0.0252 150 PHE A CD1 938 C CD2 . PHE A 119 ? 0.1687 0.1797 0.1857 -0.0070 -0.0064 -0.0177 150 PHE A CD2 939 C CE1 . PHE A 119 ? 0.1739 0.1691 0.1923 -0.0060 -0.0076 -0.0201 150 PHE A CE1 940 C CE2 . PHE A 119 ? 0.1525 0.1569 0.1671 -0.0078 -0.0080 -0.0136 150 PHE A CE2 941 C CZ . PHE A 119 ? 0.1854 0.1829 0.2010 -0.0076 -0.0086 -0.0148 150 PHE A CZ 942 N N . GLU A 120 ? 0.1523 0.1775 0.1604 -0.0103 -0.0007 -0.0189 151 GLU A N 943 C CA . GLU A 120 ? 0.1280 0.1501 0.1312 -0.0112 -0.0014 -0.0132 151 GLU A CA 944 C C . GLU A 120 ? 0.1147 0.1343 0.1187 -0.0103 -0.0029 -0.0099 151 GLU A C 945 O O . GLU A 120 ? 0.1335 0.1575 0.1410 -0.0099 -0.0031 -0.0111 151 GLU A O 946 C CB . GLU A 120 ? 0.1585 0.1866 0.1592 -0.0132 0.0006 -0.0132 151 GLU A CB 947 C CG . GLU A 120 ? 0.3251 0.3575 0.3249 -0.0150 0.0025 -0.0163 151 GLU A CG 948 C CD . GLU A 120 ? 0.3254 0.3658 0.3235 -0.0180 0.0046 -0.0165 151 GLU A CD 949 O OE1 . GLU A 120 ? 0.2901 0.3322 0.2870 -0.0187 0.0047 -0.0141 151 GLU A OE1 950 O OE2 . GLU A 120 ? 0.3612 0.4059 0.3589 -0.0202 0.0059 -0.0186 151 GLU A OE2 951 N N . VAL A 121 ? 0.1345 0.1491 0.1361 -0.0100 -0.0036 -0.0067 152 VAL A N 952 C CA . VAL A 121 ? 0.1525 0.1655 0.1534 -0.0099 -0.0041 -0.0042 152 VAL A CA 953 C C . VAL A 121 ? 0.1621 0.1740 0.1586 -0.0112 -0.0029 -0.0020 152 VAL A C 954 O O . VAL A 121 ? 0.1672 0.1762 0.1627 -0.0109 -0.0032 -0.0011 152 VAL A O 955 C CB . VAL A 121 ? 0.1467 0.1561 0.1494 -0.0088 -0.0055 -0.0036 152 VAL A CB 956 C CG1 . VAL A 121 ? 0.1518 0.1607 0.1524 -0.0094 -0.0052 -0.0012 152 VAL A CG1 957 C CG2 . VAL A 121 ? 0.1451 0.1544 0.1529 -0.0081 -0.0077 -0.0049 152 VAL A CG2 958 N N . ASP A 122 ? 0.1737 0.1881 0.1680 -0.0130 -0.0021 -0.0012 153 ASP A N 959 C CA . ASP A 122 ? 0.1450 0.1575 0.1359 -0.0148 -0.0018 0.0013 153 ASP A CA 960 C C . ASP A 122 ? 0.1525 0.1622 0.1417 -0.0153 -0.0022 0.0031 153 ASP A C 961 O O . ASP A 122 ? 0.1655 0.1775 0.1546 -0.0161 -0.0021 0.0032 153 ASP A O 962 C CB . ASP A 122 ? 0.1559 0.1722 0.1450 -0.0173 -0.0010 0.0015 153 ASP A CB 963 C CG . ASP A 122 ? 0.2925 0.3119 0.2824 -0.0175 -0.0005 -0.0004 153 ASP A CG 964 O OD1 . ASP A 122 ? 0.2319 0.2492 0.2231 -0.0158 -0.0011 -0.0014 153 ASP A OD1 965 O OD2 . ASP A 122 ? 0.3238 0.3478 0.3128 -0.0197 0.0006 -0.0010 153 ASP A OD2 966 N N . VAL A 123 ? 0.1458 0.1513 0.1348 -0.0142 -0.0030 0.0038 154 VAL A N 967 C CA . VAL A 123 ? 0.1241 0.1268 0.1122 -0.0140 -0.0035 0.0043 154 VAL A CA 968 C C . VAL A 123 ? 0.1491 0.1483 0.1357 -0.0142 -0.0044 0.0048 154 VAL A C 969 O O . VAL A 123 ? 0.2415 0.2400 0.2285 -0.0138 -0.0049 0.0050 154 VAL A O 970 C CB . VAL A 123 ? 0.2075 0.2095 0.1964 -0.0130 -0.0035 0.0040 154 VAL A CB 971 C CG1 . VAL A 123 ? 0.2568 0.2572 0.2461 -0.0120 -0.0036 0.0038 154 VAL A CG1 972 C CG2 . VAL A 123 ? 0.2422 0.2426 0.2297 -0.0135 -0.0037 0.0043 154 VAL A CG2 973 N N . ILE A 124 ? 0.1412 0.1382 0.1257 -0.0151 -0.0050 0.0052 155 ILE A N 974 C CA . ILE A 124 ? 0.1209 0.1134 0.1027 -0.0157 -0.0065 0.0057 155 ILE A CA 975 C C . ILE A 124 ? 0.1704 0.1598 0.1495 -0.0162 -0.0067 0.0051 155 ILE A C 976 O O . ILE A 124 ? 0.1855 0.1768 0.1648 -0.0167 -0.0057 0.0049 155 ILE A O 977 C CB . ILE A 124 ? 0.1973 0.1890 0.1769 -0.0176 -0.0076 0.0067 155 ILE A CB 978 C CG1 . ILE A 124 ? 0.2157 0.2086 0.1934 -0.0195 -0.0072 0.0068 155 ILE A CG1 979 C CG2 . ILE A 124 ? 0.2118 0.2065 0.1933 -0.0180 -0.0073 0.0073 155 ILE A CG2 980 C CD1 . ILE A 124 ? 0.2687 0.2591 0.2419 -0.0226 -0.0092 0.0078 155 ILE A CD1 981 N N . VAL A 125 ? 0.1384 0.1221 0.1141 -0.0166 -0.0081 0.0051 156 VAL A N 982 C CA . VAL A 125 ? 0.1462 0.1257 0.1201 -0.0173 -0.0076 0.0034 156 VAL A CA 983 C C . VAL A 125 ? 0.2109 0.1828 0.1813 -0.0187 -0.0093 0.0036 156 VAL A C 984 O O . VAL A 125 ? 0.2487 0.2174 0.2200 -0.0179 -0.0111 0.0044 156 VAL A O 985 C CB . VAL A 125 ? 0.1933 0.1726 0.1703 -0.0157 -0.0063 0.0011 156 VAL A CB 986 C CG1 . VAL A 125 ? 0.2083 0.1822 0.1827 -0.0168 -0.0053 -0.0011 156 VAL A CG1 987 C CG2 . VAL A 125 ? 0.2182 0.2036 0.1973 -0.0151 -0.0050 0.0016 156 VAL A CG2 988 N N . MET A 126 ? 0.1730 0.1417 0.1396 -0.0209 -0.0090 0.0033 157 MET A N 989 C CA . MET A 126 ? 0.1423 0.1025 0.1056 -0.0223 -0.0104 0.0035 157 MET A CA 990 C C . MET A 126 ? 0.1722 0.1257 0.1348 -0.0222 -0.0088 0.0008 157 MET A C 991 O O . MET A 126 ? 0.2008 0.1579 0.1631 -0.0229 -0.0071 -0.0007 157 MET A O 992 C CB . MET A 126 ? 0.2328 0.1949 0.1915 -0.0260 -0.0114 0.0053 157 MET A CB 993 C CG . MET A 126 ? 0.3192 0.2872 0.2778 -0.0267 -0.0131 0.0074 157 MET A CG 994 S SD . MET A 126 ? 0.3338 0.3069 0.2904 -0.0302 -0.0130 0.0084 157 MET A SD 995 C CE . MET A 126 ? 0.3059 0.2867 0.2678 -0.0283 -0.0097 0.0072 157 MET A CE 996 N N . ASN A 127 ? 0.1607 0.1042 0.1229 -0.0213 -0.0093 0.0002 158 ASN A N 997 C CA . ASN A 127 ? 0.1673 0.1032 0.1285 -0.0212 -0.0077 -0.0033 158 ASN A CA 998 C C . ASN A 127 ? 0.2350 0.1673 0.1905 -0.0254 -0.0082 -0.0026 158 ASN A C 999 O O . ASN A 127 ? 0.2094 0.1455 0.1621 -0.0281 -0.0099 0.0004 158 ASN A O 1000 C CB . ASN A 127 ? 0.2354 0.1616 0.2001 -0.0169 -0.0076 -0.0047 158 ASN A CB 1001 C CG . ASN A 127 ? 0.2911 0.2105 0.2552 -0.0164 -0.0102 -0.0010 158 ASN A CG 1002 O OD1 . ASN A 127 ? 0.2429 0.1623 0.2027 -0.0202 -0.0119 0.0018 158 ASN A OD1 1003 N ND2 . ASN A 127 ? 0.2848 0.1987 0.2533 -0.0115 -0.0107 -0.0006 158 ASN A ND2 1004 N N . SER A 128 ? 0.1835 0.1084 0.1370 -0.0263 -0.0070 -0.0058 159 SER A N 1005 C CA . SER A 128 ? 0.2292 0.1497 0.1767 -0.0309 -0.0075 -0.0056 159 SER A CA 1006 C C . SER A 128 ? 0.2636 0.1755 0.2088 -0.0321 -0.0098 -0.0029 159 SER A C 1007 O O . SER A 128 ? 0.2452 0.1539 0.1848 -0.0366 -0.0106 -0.0020 159 SER A O 1008 C CB . SER A 128 ? 0.2814 0.1962 0.2270 -0.0316 -0.0054 -0.0103 159 SER A CB 1009 O OG . SER A 128 ? 0.3631 0.2677 0.3122 -0.0276 -0.0049 -0.0132 159 SER A OG 1010 N N . GLU A 129 ? 0.2966 0.2054 0.2457 -0.0285 -0.0110 -0.0010 160 GLU A N 1011 C CA . GLU A 129 ? 0.2482 0.1498 0.1953 -0.0295 -0.0136 0.0027 160 GLU A CA 1012 C C . GLU A 129 ? 0.3160 0.2274 0.2613 -0.0321 -0.0157 0.0067 160 GLU A C 1013 O O . GLU A 129 ? 0.3664 0.2742 0.3092 -0.0341 -0.0182 0.0101 160 GLU A O 1014 C CB . GLU A 129 ? 0.3506 0.2433 0.3030 -0.0240 -0.0140 0.0031 160 GLU A CB 1015 C CG . GLU A 129 ? 0.5417 0.4233 0.4961 -0.0214 -0.0119 -0.0014 160 GLU A CG 1016 C CD . GLU A 129 ? 0.9944 0.8701 0.9559 -0.0142 -0.0112 -0.0023 160 GLU A CD 1017 O OE1 . GLU A 129 ? 0.9491 0.8205 0.9122 -0.0118 -0.0135 0.0023 160 GLU A OE1 1018 O OE2 . GLU A 129 ? 0.9604 0.8364 0.9260 -0.0108 -0.0085 -0.0075 160 GLU A OE2 1019 N N . GLY A 130 ? 0.2661 0.1895 0.2126 -0.0322 -0.0148 0.0061 161 GLY A N 1020 C CA . GLY A 130 ? 0.2594 0.1930 0.2050 -0.0341 -0.0163 0.0086 161 GLY A CA 1021 C C . GLY A 130 ? 0.4567 0.3935 0.4064 -0.0313 -0.0176 0.0104 161 GLY A C 1022 O O . GLY A 130 ? 0.3759 0.3209 0.3252 -0.0330 -0.0189 0.0119 161 GLY A O 1023 N N . ASN A 131 ? 0.2864 0.2176 0.2404 -0.0269 -0.0173 0.0100 162 ASN A N 1024 C CA . ASN A 131 ? 0.2347 0.1690 0.1926 -0.0242 -0.0188 0.0120 162 ASN A CA 1025 C C . ASN A 131 ? 0.2442 0.1877 0.2058 -0.0222 -0.0173 0.0101 162 ASN A C 1026 O O . ASN A 131 ? 0.2386 0.1819 0.2019 -0.0205 -0.0149 0.0072 162 ASN A O 1027 C CB . ASN A 131 ? 0.3051 0.2292 0.2661 -0.0197 -0.0194 0.0129 162 ASN A CB 1028 C CG . ASN A 131 ? 0.4802 0.3940 0.4379 -0.0211 -0.0212 0.0154 162 ASN A CG 1029 O OD1 . ASN A 131 ? 0.4173 0.3328 0.3706 -0.0258 -0.0230 0.0178 162 ASN A OD1 1030 N ND2 . ASN A 131 ? 0.3796 0.2825 0.3396 -0.0173 -0.0205 0.0145 162 ASN A ND2 1031 N N . THR A 132 ? 0.2734 0.2247 0.2365 -0.0226 -0.0187 0.0117 163 THR A N 1032 C CA . THR A 132 ? 0.2763 0.2355 0.2431 -0.0209 -0.0175 0.0102 163 THR A CA 1033 C C . THR A 132 ? 0.3192 0.2741 0.2904 -0.0166 -0.0176 0.0102 163 THR A C 1034 O O . THR A 132 ? 0.3268 0.2788 0.2995 -0.0150 -0.0199 0.0130 163 THR A O 1035 C CB . THR A 132 ? 0.3041 0.2721 0.2715 -0.0230 -0.0190 0.0113 163 THR A CB 1036 O OG1 . THR A 132 ? 0.2969 0.2690 0.2611 -0.0260 -0.0184 0.0109 163 THR A OG1 1037 C CG2 . THR A 132 ? 0.2711 0.2462 0.2426 -0.0210 -0.0176 0.0100 163 THR A CG2 1038 N N . ILE A 133 ? 0.2445 0.1997 0.2179 -0.0146 -0.0152 0.0073 164 ILE A N 1039 C CA . ILE A 133 ? 0.2465 0.1981 0.2243 -0.0102 -0.0152 0.0064 164 ILE A CA 1040 C C . ILE A 133 ? 0.2516 0.2108 0.2329 -0.0098 -0.0153 0.0061 164 ILE A C 1041 O O . ILE A 133 ? 0.2683 0.2299 0.2550 -0.0055 -0.0158 0.0061 164 ILE A O 1042 C CB . ILE A 133 ? 0.3005 0.2452 0.2787 -0.0081 -0.0125 0.0024 164 ILE A CB 1043 C CG1 . ILE A 133 ? 0.2439 0.1941 0.2202 -0.0110 -0.0095 -0.0009 164 ILE A CG1 1044 C CG2 . ILE A 133 ? 0.3215 0.2564 0.2975 -0.0077 -0.0129 0.0030 164 ILE A CG2 1045 C CD1 . ILE A 133 ? 0.4172 0.3641 0.3945 -0.0092 -0.0067 -0.0056 164 ILE A CD1 1046 N N . LEU A 134 ? 0.1777 0.1452 0.1579 -0.0128 -0.0140 0.0052 165 LEU A N 1047 C CA . LEU A 134 ? 0.1971 0.1727 0.1808 -0.0128 -0.0136 0.0046 165 LEU A CA 1048 C C . LEU A 134 ? 0.2554 0.2381 0.2378 -0.0141 -0.0124 0.0061 165 LEU A C 1049 O O . LEU A 134 ? 0.2200 0.2025 0.1991 -0.0152 -0.0115 0.0064 165 LEU A O 1050 C CB . LEU A 134 ? 0.2126 0.1908 0.1980 -0.0119 -0.0106 0.0011 165 LEU A CB 1051 C CG . LEU A 134 ? 0.2487 0.2232 0.2364 -0.0087 -0.0093 -0.0015 165 LEU A CG 1052 C CD1 . LEU A 134 ? 0.2667 0.2419 0.2525 -0.0104 -0.0064 -0.0049 165 LEU A CD1 1053 C CD2 . LEU A 134 ? 0.2880 0.2693 0.2825 -0.0048 -0.0096 -0.0011 165 LEU A CD2 1054 N N . MLY A 135 ? 0.1795 0.1679 0.1654 -0.0134 -0.0115 0.0064 166 MLY A N 1055 C CA . MLY A 135 ? 0.1295 0.1224 0.1161 -0.0137 -0.0089 0.0065 166 MLY A CA 1056 C CB . MLY A 135 ? 0.2256 0.2185 0.2108 -0.0158 -0.0097 0.0080 166 MLY A CB 1057 C CG . MLY A 135 ? 0.3020 0.2949 0.2877 -0.0172 -0.0123 0.0099 166 MLY A CG 1058 C CD . MLY A 135 ? 0.3811 0.3741 0.3648 -0.0201 -0.0132 0.0112 166 MLY A CD 1059 C CE . MLY A 135 ? 0.5394 0.5359 0.5237 -0.0213 -0.0146 0.0129 166 MLY A CE 1060 N NZ . MLY A 135 ? 0.8968 0.8907 0.8787 -0.0237 -0.0181 0.0157 166 MLY A NZ 1061 C CH1 . MLY A 135 ? 0.8417 0.8344 0.8209 -0.0273 -0.0178 0.0156 166 MLY A CH1 1062 C CH2 . MLY A 135 ? 0.8161 0.8151 0.7980 -0.0245 -0.0184 0.0171 166 MLY A CH2 1063 C C . MLY A 135 ? 0.2528 0.2505 0.2429 -0.0121 -0.0076 0.0050 166 MLY A C 1064 O O . MLY A 135 ? 0.1941 0.1933 0.1864 -0.0110 -0.0086 0.0044 166 MLY A O 1065 N N . THR A 136 ? 0.1822 0.1822 0.1720 -0.0127 -0.0059 0.0048 167 THR A N 1066 C CA . THR A 136 ? 0.1485 0.1516 0.1401 -0.0120 -0.0053 0.0034 167 THR A CA 1067 C C . THR A 136 ? 0.2040 0.2088 0.1955 -0.0129 -0.0064 0.0040 167 THR A C 1068 O O . THR A 136 ? 0.1941 0.1988 0.1838 -0.0147 -0.0069 0.0055 167 THR A O 1069 C CB . THR A 136 ? 0.1715 0.1768 0.1629 -0.0124 -0.0040 0.0025 167 THR A CB 1070 O OG1 . THR A 136 ? 0.2006 0.2049 0.1923 -0.0118 -0.0036 0.0024 167 THR A OG1 1071 C CG2 . THR A 136 ? 0.2111 0.2187 0.2042 -0.0118 -0.0038 0.0005 167 THR A CG2 1072 N N . PRO A 137 ? 0.2489 0.2555 0.2421 -0.0121 -0.0070 0.0032 168 PRO A N 1073 C CA . PRO A 137 ? 0.2197 0.2287 0.2124 -0.0132 -0.0083 0.0041 168 PRO A CA 1074 C C . PRO A 137 ? 0.2430 0.2542 0.2334 -0.0155 -0.0073 0.0042 168 PRO A C 1075 O O . PRO A 137 ? 0.2204 0.2327 0.2107 -0.0155 -0.0056 0.0023 168 PRO A O 1076 C CB . PRO A 137 ? 0.2292 0.2405 0.2239 -0.0125 -0.0085 0.0027 168 PRO A CB 1077 C CG . PRO A 137 ? 0.2618 0.2715 0.2586 -0.0107 -0.0081 0.0019 168 PRO A CG 1078 C CD . PRO A 137 ? 0.1976 0.2047 0.1930 -0.0107 -0.0067 0.0018 168 PRO A CD 1079 N N . GLN A 138 ? 0.1885 0.2006 0.1772 -0.0175 -0.0086 0.0061 169 GLN A N 1080 C CA . GLN A 138 ? 0.2335 0.2488 0.2198 -0.0205 -0.0075 0.0062 169 GLN A CA 1081 C C . GLN A 138 ? 0.1853 0.2045 0.1716 -0.0209 -0.0060 0.0035 169 GLN A C 1082 O O . GLN A 138 ? 0.1781 0.1981 0.1652 -0.0203 -0.0069 0.0029 169 GLN A O 1083 C CB . GLN A 138 ? 0.2853 0.3012 0.2698 -0.0231 -0.0097 0.0091 169 GLN A CB 1084 C CG . GLN A 138 ? 0.4423 0.4611 0.4244 -0.0270 -0.0086 0.0097 169 GLN A CG 1085 C CD . GLN A 138 ? 0.7770 0.7962 0.7569 -0.0303 -0.0112 0.0130 169 GLN A CD 1086 O OE1 . GLN A 138 ? 0.6605 0.6759 0.6406 -0.0293 -0.0143 0.0155 169 GLN A OE1 1087 N NE2 . GLN A 138 ? 0.7835 0.8079 0.7613 -0.0344 -0.0102 0.0130 169 GLN A NE2 1088 N N . ASN A 139 ? 0.2060 0.2279 0.1918 -0.0219 -0.0039 0.0015 170 ASN A N 1089 C CA . ASN A 139 ? 0.1960 0.2214 0.1821 -0.0223 -0.0024 -0.0021 170 ASN A CA 1090 C C . ASN A 139 ? 0.1673 0.1901 0.1558 -0.0196 -0.0024 -0.0045 170 ASN A C 1091 O O . ASN A 139 ? 0.1825 0.2067 0.1712 -0.0202 -0.0019 -0.0073 170 ASN A O 1092 C CB . ASN A 139 ? 0.1449 0.1744 0.1286 -0.0255 -0.0028 -0.0019 170 ASN A CB 1093 C CG . ASN A 139 ? 0.2976 0.3306 0.2791 -0.0291 -0.0025 -0.0001 170 ASN A CG 1094 O OD1 . ASN A 139 ? 0.3196 0.3544 0.3016 -0.0297 -0.0009 -0.0009 170 ASN A OD1 1095 N ND2 . ASN A 139 ? 0.2280 0.2621 0.2073 -0.0317 -0.0045 0.0029 170 ASN A ND2 1096 N N . ALA A 140 ? 0.1335 0.1523 0.1238 -0.0172 -0.0030 -0.0035 171 ALA A N 1097 C CA . ALA A 140 ? 0.1691 0.1854 0.1617 -0.0153 -0.0033 -0.0053 171 ALA A CA 1098 C C . ALA A 140 ? 0.2085 0.2252 0.2027 -0.0148 -0.0023 -0.0085 171 ALA A C 1099 O O . ALA A 140 ? 0.1793 0.1974 0.1738 -0.0146 -0.0015 -0.0088 171 ALA A O 1100 C CB . ALA A 140 ? 0.1212 0.1341 0.1151 -0.0134 -0.0039 -0.0035 171 ALA A CB 1101 N N . ILE A 141 ? 0.1640 0.1794 0.1591 -0.0148 -0.0026 -0.0110 172 ILE A N 1102 C CA . ILE A 141 ? 0.1452 0.1594 0.1422 -0.0141 -0.0023 -0.0145 172 ILE A CA 1103 C C . ILE A 141 ? 0.2529 0.2615 0.2517 -0.0130 -0.0039 -0.0143 172 ILE A C 1104 O O . ILE A 141 ? 0.2448 0.2522 0.2431 -0.0138 -0.0046 -0.0133 172 ILE A O 1105 C CB . ILE A 141 ? 0.2250 0.2416 0.2208 -0.0159 -0.0011 -0.0184 172 ILE A CB 1106 C CG1 . ILE A 141 ? 0.3691 0.3920 0.3627 -0.0180 0.0004 -0.0179 172 ILE A CG1 1107 C CG2 . ILE A 141 ? 0.2899 0.3062 0.2885 -0.0150 0.0003 -0.0235 172 ILE A CG2 1108 C CD1 . ILE A 141 ? 0.3663 0.3933 0.3577 -0.0209 0.0019 -0.0217 172 ILE A CD1 1109 N N . PHE A 142 ? 0.1527 0.1585 0.1535 -0.0118 -0.0044 -0.0151 173 PHE A N 1110 C CA . PHE A 142 ? 0.1514 0.1515 0.1533 -0.0116 -0.0059 -0.0145 173 PHE A CA 1111 C C . PHE A 142 ? 0.2592 0.2569 0.2635 -0.0113 -0.0048 -0.0197 173 PHE A C 1112 O O . PHE A 142 ? 0.1781 0.1800 0.1844 -0.0105 -0.0029 -0.0238 173 PHE A O 1113 C CB . PHE A 142 ? 0.1920 0.1913 0.1950 -0.0108 -0.0071 -0.0111 173 PHE A CB 1114 C CG . PHE A 142 ? 0.1455 0.1475 0.1482 -0.0101 -0.0068 -0.0085 173 PHE A CG 1115 C CD1 . PHE A 142 ? 0.2428 0.2448 0.2456 -0.0104 -0.0067 -0.0075 173 PHE A CD1 1116 C CD2 . PHE A 142 ? 0.1325 0.1378 0.1344 -0.0097 -0.0057 -0.0077 173 PHE A CD2 1117 C CE1 . PHE A 142 ? 0.2072 0.2115 0.2083 -0.0103 -0.0056 -0.0057 173 PHE A CE1 1118 C CE2 . PHE A 142 ? 0.1936 0.2001 0.1937 -0.0097 -0.0048 -0.0056 173 PHE A CE2 1119 C CZ . PHE A 142 ? 0.1522 0.1579 0.1518 -0.0099 -0.0050 -0.0046 173 PHE A CZ 1120 N N . PHE A 143 ? 0.1752 0.1659 0.1795 -0.0118 -0.0059 -0.0198 174 PHE A N 1121 C CA . PHE A 143 ? 0.1757 0.1613 0.1828 -0.0104 -0.0049 -0.0247 174 PHE A CA 1122 C C . PHE A 143 ? 0.1464 0.1247 0.1573 -0.0087 -0.0062 -0.0235 174 PHE A C 1123 O O . PHE A 143 ? 0.1717 0.1473 0.1803 -0.0108 -0.0075 -0.0192 174 PHE A O 1124 C CB . PHE A 143 ? 0.2346 0.2169 0.2373 -0.0127 -0.0049 -0.0265 174 PHE A CB 1125 C CG . PHE A 143 ? 0.2630 0.2526 0.2633 -0.0141 -0.0038 -0.0275 174 PHE A CG 1126 C CD1 . PHE A 143 ? 0.2938 0.2873 0.2920 -0.0155 -0.0052 -0.0234 174 PHE A CD1 1127 C CD2 . PHE A 143 ? 0.2504 0.2433 0.2514 -0.0136 -0.0012 -0.0327 174 PHE A CD2 1128 C CE1 . PHE A 143 ? 0.2794 0.2792 0.2758 -0.0167 -0.0040 -0.0239 174 PHE A CE1 1129 C CE2 . PHE A 143 ? 0.3290 0.3291 0.3273 -0.0156 -0.0001 -0.0331 174 PHE A CE2 1130 C CZ . PHE A 143 ? 0.2664 0.2693 0.2622 -0.0173 -0.0017 -0.0284 174 PHE A CZ 1131 N N . LYS A 144 ? 0.1728 0.1482 0.1899 -0.0047 -0.0058 -0.0272 175 LYS A N 1132 C CA . LYS A 144 ? 0.1715 0.1393 0.1935 -0.0018 -0.0080 -0.0249 175 LYS A CA 1133 C C . LYS A 144 ? 0.2071 0.1663 0.2304 0.0007 -0.0071 -0.0283 175 LYS A C 1134 O O . LYS A 144 ? 0.2393 0.2011 0.2651 0.0034 -0.0048 -0.0337 175 LYS A O 1135 C CB . LYS A 144 ? 0.2071 0.1797 0.2369 0.0024 -0.0093 -0.0244 175 LYS A CB 1136 C CG . LYS A 144 ? 0.1993 0.1655 0.2353 0.0069 -0.0120 -0.0210 175 LYS A CG 1137 C CD . LYS A 144 ? 0.1868 0.1484 0.2193 0.0037 -0.0152 -0.0137 175 LYS A CD 1138 C CE . LYS A 144 ? 0.2338 0.1906 0.2712 0.0075 -0.0182 -0.0092 175 LYS A CE 1139 N NZ . LYS A 144 ? 0.2079 0.1542 0.2431 0.0073 -0.0183 -0.0088 175 LYS A NZ 1140 N N . THR A 145 ? 0.2049 0.1542 0.2261 -0.0004 -0.0086 -0.0253 176 THR A N 1141 C CA . THR A 145 ? 0.2032 0.1423 0.2251 0.0019 -0.0080 -0.0281 176 THR A CA 1142 C C . THR A 145 ? 0.2393 0.1762 0.2697 0.0084 -0.0096 -0.0266 176 THR A C 1143 O O . THR A 145 ? 0.2658 0.2023 0.2983 0.0087 -0.0126 -0.0205 176 THR A O 1144 C CB . THR A 145 ? 0.2340 0.1631 0.2492 -0.0029 -0.0085 -0.0258 176 THR A CB 1145 O OG1 . THR A 145 ? 0.3248 0.2586 0.3327 -0.0091 -0.0076 -0.0256 176 THR A OG1 1146 C CG2 . THR A 145 ? 0.2752 0.1925 0.2887 -0.0016 -0.0073 -0.0301 176 THR A CG2 1147 N N . CYS A 146 ? 0.2779 0.2148 0.3130 0.0136 -0.0076 -0.0318 177 CYS A N 1148 C CA . CYS A 146 ? 0.2284 0.1647 0.2722 0.0207 -0.0087 -0.0308 177 CYS A CA 1149 C C . CYS A 146 ? 0.3841 0.3077 0.4281 0.0238 -0.0080 -0.0331 177 CYS A C 1150 O O . CYS A 146 ? 0.2728 0.1914 0.3118 0.0220 -0.0053 -0.0386 177 CYS A O 1151 C CB . CYS A 146 ? 0.2244 0.1737 0.2745 0.0246 -0.0064 -0.0349 177 CYS A CB 1152 S SG . CYS A 146 ? 0.2683 0.2312 0.3191 0.0218 -0.0075 -0.0319 177 CYS A SG 1153 N N . GLN A 147 ? 0.2817 0.2004 0.3313 0.0288 -0.0106 -0.0289 178 GLN A N 1154 C CA . GLN A 147 ? 0.3361 0.2420 0.3870 0.0329 -0.0103 -0.0304 178 GLN A CA 1155 C C . GLN A 147 ? 0.3429 0.2538 0.4038 0.0417 -0.0096 -0.0322 178 GLN A C 1156 O O . GLN A 147 ? 0.3777 0.3007 0.4446 0.0441 -0.0108 -0.0294 178 GLN A O 1157 C CB . GLN A 147 ? 0.3879 0.2828 0.4360 0.0306 -0.0142 -0.0227 178 GLN A CB 1158 C CG . GLN A 147 ? 0.7455 0.6234 0.7905 0.0314 -0.0137 -0.0241 178 GLN A CG 1159 C CD . GLN A 147 ? 1.0242 0.8931 1.0637 0.0257 -0.0167 -0.0171 178 GLN A CD 1160 O OE1 . GLN A 147 ? 0.9446 0.8061 0.9763 0.0194 -0.0153 -0.0186 178 GLN A OE1 1161 N NE2 . GLN A 147 ? 0.9405 0.8109 0.9836 0.0273 -0.0209 -0.0094 178 GLN A NE2 1162 N N . GLN A 148 ? 0.4027 0.3047 0.4653 0.0465 -0.0074 -0.0370 179 GLN A N 1163 C CA . GLN A 148 ? 0.5747 0.4808 0.6473 0.0555 -0.0065 -0.0387 179 GLN A CA 1164 C C . GLN A 148 ? 0.4817 0.3816 0.5585 0.0590 -0.0114 -0.0301 179 GLN A C 1165 O O . GLN A 148 ? 0.5761 0.4621 0.6475 0.0560 -0.0138 -0.0261 179 GLN A O 1166 C CB . GLN A 148 ? 0.4349 0.3315 0.5069 0.0594 -0.0026 -0.0467 179 GLN A CB 1167 C CG . GLN A 148 ? 0.6638 0.5698 0.7458 0.0680 0.0003 -0.0512 179 GLN A CG 1168 C CD . GLN A 148 ? 0.7289 0.6248 0.8099 0.0717 0.0044 -0.0595 179 GLN A CD 1169 O OE1 . GLN A 148 ? 0.8199 0.7231 0.8997 0.0711 0.0090 -0.0675 179 GLN A OE1 1170 N NE2 . GLN A 148 ? 1.0963 0.9745 1.1769 0.0751 0.0027 -0.0577 179 GLN A NE2 1171 N N . ALA A 149 ? 0.3769 0.2880 0.4626 0.0645 -0.0130 -0.0267 180 ALA A N 1172 C CA . ALA A 149 ? 0.5859 0.4930 0.6752 0.0676 -0.0181 -0.0179 180 ALA A CA 1173 C C . ALA A 149 ? 0.4684 0.3623 0.5618 0.0749 -0.0184 -0.0184 180 ALA A C 1174 O O . ALA A 149 ? 0.5987 0.4934 0.6971 0.0810 -0.0144 -0.0254 180 ALA A O 1175 C CB . ALA A 149 ? 0.6060 0.5302 0.7026 0.0704 -0.0199 -0.0137 180 ALA A CB 1176 N N . GLU A 150 ? 0.6209 0.5024 0.7119 0.0740 -0.0228 -0.0110 181 GLU A N 1177 C CA . GLU A 150 ? 0.6079 0.4746 0.7021 0.0806 -0.0241 -0.0098 181 GLU A CA 1178 C C . GLU A 150 ? 0.6302 0.4961 0.7264 0.0812 -0.0304 0.0013 181 GLU A C 1179 O O . GLU A 150 ? 0.7126 0.5724 0.8013 0.0738 -0.0336 0.0072 181 GLU A O 1180 C CB . GLU A 150 ? 0.6812 0.5287 0.7666 0.0763 -0.0223 -0.0133 181 GLU A CB 1181 C CG . GLU A 150 ? 1.1676 0.9994 1.2565 0.0840 -0.0211 -0.0163 181 GLU A CG 1182 C CD . GLU A 150 ? 1.2950 1.1253 1.3844 0.0875 -0.0149 -0.0278 181 GLU A CD 1183 O OE1 . GLU A 150 ? 1.1832 1.0062 1.2632 0.0808 -0.0119 -0.0332 181 GLU A OE1 1184 O OE2 . GLU A 150 ? 1.1496 0.9862 1.2485 0.0967 -0.0129 -0.0315 181 GLU A OE2 1185 N N . CYS A 151 ? 0.6916 0.5659 0.7978 0.0897 -0.0322 0.0040 182 CYS A N 1186 C CA . CYS A 151 ? 0.5355 0.4111 0.6440 0.0909 -0.0385 0.0144 182 CYS A CA 1187 C C . CYS A 151 ? 0.6000 0.4571 0.7093 0.0952 -0.0415 0.0186 182 CYS A C 1188 O O . CYS A 151 ? 0.8523 0.7011 0.9666 0.1029 -0.0387 0.0132 182 CYS A O 1189 C CB . CYS A 151 ? 0.6675 0.5622 0.7860 0.0972 -0.0394 0.0160 182 CYS A CB 1190 S SG . CYS A 151 ? 0.8040 0.7190 0.9190 0.0891 -0.0400 0.0183 182 CYS A SG 1191 N N . PRO A 152 ? 0.7782 0.6286 0.8825 0.0905 -0.0471 0.0280 183 PRO A N 1192 C CA . PRO A 152 ? 1.0766 0.9088 1.1815 0.0945 -0.0504 0.0328 183 PRO A CA 1193 C C . PRO A 152 ? 1.0841 0.9200 1.2010 0.1068 -0.0523 0.0347 183 PRO A C 1194 O O . PRO A 152 ? 0.6376 0.4883 0.7595 0.1088 -0.0559 0.0403 183 PRO A O 1195 C CB . PRO A 152 ? 0.8474 0.6764 0.9443 0.0856 -0.0559 0.0428 183 PRO A CB 1196 C CG . PRO A 152 ? 0.9736 0.8159 1.0642 0.0763 -0.0543 0.0414 183 PRO A CG 1197 C CD . PRO A 152 ? 0.6399 0.4987 0.7375 0.0812 -0.0505 0.0347 183 PRO A CD 1198 N N . GLY A 153 ? 1.1131 0.9368 1.2348 0.1150 -0.0494 0.0292 184 GLY A N 1199 C CA . GLY A 153 ? 1.3243 1.1502 1.4582 0.1279 -0.0503 0.0296 184 GLY A CA 1200 C C . GLY A 153 ? 1.4452 1.2894 1.5883 0.1346 -0.0452 0.0215 184 GLY A C 1201 O O . GLY A 153 ? 1.4533 1.3026 1.6077 0.1458 -0.0453 0.0213 184 GLY A O 1202 N N . GLY A 154 ? 1.4662 1.3213 1.6048 0.1277 -0.0408 0.0153 185 GLY A N 1203 C CA . GLY A 154 ? 1.3828 1.2562 1.5284 0.1318 -0.0354 0.0074 185 GLY A CA 1204 C C . GLY A 154 ? 1.3786 1.2745 1.5327 0.1354 -0.0379 0.0120 185 GLY A C 1205 O O . GLY A 154 ? 1.2584 1.1560 1.4141 0.1363 -0.0442 0.0216 185 GLY A O 1206 N N . CYS A 155 ? 1.2113 1.1253 1.3706 0.1370 -0.0328 0.0052 186 CYS A N 1207 C CA . CYS A 155 ? 1.0353 0.9728 1.2028 0.1401 -0.0340 0.0084 186 CYS A CA 1208 C C . CYS A 155 ? 1.0992 1.0452 1.2802 0.1524 -0.0303 0.0036 186 CYS A C 1209 O O . CYS A 155 ? 1.0597 1.0061 1.2426 0.1544 -0.0235 -0.0062 186 CYS A O 1210 C CB . CYS A 155 ? 0.9488 0.9021 1.1115 0.1313 -0.0313 0.0057 186 CYS A CB 1211 S SG . CYS A 155 ? 0.8964 0.8408 1.0439 0.1173 -0.0347 0.0104 186 CYS A SG 1212 N N . ARG A 156 ? 0.9377 0.8906 1.1281 0.1606 -0.0348 0.0104 187 ARG A N 1213 C CA . ARG A 156 ? 0.8701 0.8324 1.0747 0.1734 -0.0320 0.0072 187 ARG A CA 1214 C C . ARG A 156 ? 0.9178 0.9093 1.1300 0.1738 -0.0294 0.0061 187 ARG A C 1215 O O . ARG A 156 ? 0.7407 0.7429 0.9463 0.1643 -0.0305 0.0083 187 ARG A O 1216 C CB . ARG A 156 ? 1.0525 1.0069 1.2638 0.1827 -0.0385 0.0155 187 ARG A CB 1217 C CG . ARG A 156 ? 1.0561 0.9819 1.2593 0.1810 -0.0423 0.0190 187 ARG A CG 1218 C CD . ARG A 156 ? 1.1383 1.0460 1.3444 0.1885 -0.0373 0.0110 187 ARG A CD 1219 N NE . ARG A 156 ? 1.3220 1.2227 1.5194 0.1812 -0.0307 0.0010 187 ARG A NE 1220 C CZ . ARG A 156 ? 1.3844 1.2652 1.5692 0.1727 -0.0313 0.0006 187 ARG A CZ 1221 N NH1 . ARG A 156 ? 1.5154 1.3807 1.6947 0.1700 -0.0378 0.0097 187 ARG A NH1 1222 N NH2 . ARG A 156 ? 1.2959 1.1728 1.4734 0.1665 -0.0253 -0.0087 187 ARG A NH2 1223 N N . ASN A 157 ? 0.7004 0.7044 0.9265 0.1847 -0.0257 0.0026 188 ASN A N 1224 C CA . ASN A 157 ? 0.6141 0.6469 0.8498 0.1864 -0.0226 0.0017 188 ASN A CA 1225 C C . ASN A 157 ? 0.6400 0.6834 0.8696 0.1761 -0.0167 -0.0046 188 ASN A C 1226 O O . ASN A 157 ? 0.5588 0.6219 0.7887 0.1707 -0.0175 -0.0011 188 ASN A O 1227 C CB . ASN A 157 ? 0.5372 0.5856 0.7763 0.1871 -0.0302 0.0125 188 ASN A CB 1228 C CG . ASN A 157 ? 0.7925 0.8389 1.0419 0.1995 -0.0353 0.0181 188 ASN A CG 1229 O OD1 . ASN A 157 ? 0.5400 0.6042 0.8034 0.2090 -0.0334 0.0179 188 ASN A OD1 1230 N ND2 . ASN A 157 ? 0.8572 0.8826 1.1001 0.1993 -0.0420 0.0242 188 ASN A ND2 1231 N N . GLY A 158 ? 1.0814 1.1113 1.3048 0.1730 -0.0111 -0.0139 189 GLY A N 1232 C CA . GLY A 158 ? 0.8685 0.9060 1.0852 0.1634 -0.0056 -0.0206 189 GLY A CA 1233 C C . GLY A 158 ? 1.1175 1.1527 1.3213 0.1513 -0.0094 -0.0161 189 GLY A C 1234 O O . GLY A 158 ? 1.0953 1.1401 1.2943 0.1433 -0.0059 -0.0197 189 GLY A O 1235 N N . GLY A 159 ? 0.9841 1.0063 1.1822 0.1499 -0.0165 -0.0082 190 GLY A N 1236 C CA . GLY A 159 ? 0.7741 0.7922 0.9600 0.1389 -0.0205 -0.0034 190 GLY A CA 1237 C C . GLY A 159 ? 0.7186 0.7201 0.8934 0.1317 -0.0176 -0.0096 190 GLY A C 1238 O O . GLY A 159 ? 0.8837 0.8713 1.0585 0.1355 -0.0143 -0.0158 190 GLY A O 1239 N N . PHE A 160 ? 0.6607 0.6639 0.8257 0.1214 -0.0187 -0.0079 191 PHE A N 1240 C CA . PHE A 160 ? 0.9569 0.9463 1.1113 0.1140 -0.0164 -0.0131 191 PHE A CA 1241 C C . PHE A 160 ? 0.8654 0.8444 1.0096 0.1060 -0.0216 -0.0065 191 PHE A C 1242 O O . PHE A 160 ? 0.5263 0.5141 0.6694 0.1029 -0.0258 0.0007 191 PHE A O 1243 C CB . PHE A 160 ? 0.9827 0.9843 1.1352 0.1093 -0.0103 -0.0209 191 PHE A CB 1244 C CG . PHE A 160 ? 1.3107 1.3167 1.4707 0.1161 -0.0041 -0.0295 191 PHE A CG 1245 C CD1 . PHE A 160 ? 1.0880 1.0779 1.2451 0.1183 -0.0010 -0.0366 191 PHE A CD1 1246 C CD2 . PHE A 160 ? 1.4262 1.4526 1.5963 0.1203 -0.0014 -0.0304 191 PHE A CD2 1247 C CE1 . PHE A 160 ? 0.9693 0.9630 1.1329 0.1247 0.0049 -0.0450 191 PHE A CE1 1248 C CE2 . PHE A 160 ? 1.3681 1.3992 1.5454 0.1265 0.0047 -0.0386 191 PHE A CE2 1249 C CZ . PHE A 160 ? 1.3162 1.3307 1.4900 0.1289 0.0078 -0.0461 191 PHE A CZ 1250 N N . CYS A 161 ? 0.6533 0.6135 0.7896 0.1025 -0.0214 -0.0086 192 CYS A N 1251 C CA . CYS A 161 ? 0.5158 0.4665 0.6424 0.0944 -0.0259 -0.0023 192 CYS A CA 1252 C C . CYS A 161 ? 0.7507 0.7088 0.8701 0.0854 -0.0241 -0.0044 192 CYS A C 1253 O O . CYS A 161 ? 0.8391 0.7991 0.9568 0.0836 -0.0191 -0.0123 192 CYS A O 1254 C CB . CYS A 161 ? 0.8578 0.7863 0.9788 0.0936 -0.0268 -0.0025 192 CYS A CB 1255 S SG . CYS A 161 ? 0.7383 0.6565 0.8482 0.0836 -0.0322 0.0062 192 CYS A SG 1256 N N . ASN A 162 ? 0.5213 0.4841 0.6365 0.0797 -0.0282 0.0027 193 ASN A N 1257 C CA . ASN A 162 ? 0.6705 0.6391 0.7787 0.0712 -0.0271 0.0017 193 ASN A CA 1258 C C . ASN A 162 ? 0.6380 0.5915 0.7362 0.0642 -0.0286 0.0033 193 ASN A C 1259 O O . ASN A 162 ? 0.6333 0.5731 0.7299 0.0653 -0.0310 0.0065 193 ASN A O 1260 C CB . ASN A 162 ? 0.7085 0.6917 0.8172 0.0688 -0.0301 0.0077 193 ASN A CB 1261 C CG . ASN A 162 ? 0.9493 0.9283 1.0556 0.0672 -0.0361 0.0169 193 ASN A CG 1262 O OD1 . ASN A 162 ? 0.5769 0.5448 0.6754 0.0615 -0.0383 0.0204 193 ASN A OD1 1263 N ND2 . ASN A 162 ? 1.2831 1.2731 1.3954 0.0715 -0.0387 0.0211 193 ASN A ND2 1264 N N . GLU A 163 ? 1.0447 1.0010 1.1363 0.0570 -0.0271 0.0014 194 GLU A N 1265 C CA . GLU A 163 ? 1.2551 1.1992 1.3374 0.0502 -0.0280 0.0026 194 GLU A CA 1266 C C . GLU A 163 ? 0.4926 0.4319 0.5699 0.0456 -0.0331 0.0117 194 GLU A C 1267 O O . GLU A 163 ? 0.7767 0.7064 0.8465 0.0399 -0.0336 0.0129 194 GLU A O 1268 C CB . GLU A 163 ? 1.0600 1.0077 1.1373 0.0448 -0.0245 -0.0030 194 GLU A CB 1269 C CG . GLU A 163 ? 1.2022 1.1370 1.2716 0.0399 -0.0234 -0.0053 194 GLU A CG 1270 C CD . GLU A 163 ? 1.2769 1.1992 1.3468 0.0436 -0.0216 -0.0095 194 GLU A CD 1271 O OE1 . GLU A 163 ? 0.8015 0.7269 0.8778 0.0499 -0.0189 -0.0147 194 GLU A OE1 1272 O OE2 . GLU A 163 ? 1.6170 1.5266 1.6808 0.0399 -0.0226 -0.0077 194 GLU A OE2 1273 N N . ARG A 164 ? 0.8126 0.7591 0.8936 0.0478 -0.0365 0.0178 195 ARG A N 1274 C CA . ARG A 164 ? 0.8930 0.8362 0.9692 0.0435 -0.0413 0.0262 195 ARG A CA 1275 C C . ARG A 164 ? 0.5561 0.4881 0.6356 0.0486 -0.0441 0.0298 195 ARG A C 1276 O O . ARG A 164 ? 0.7053 0.6341 0.7819 0.0461 -0.0483 0.0371 195 ARG A O 1277 C CB . ARG A 164 ? 0.8352 0.7928 0.9125 0.0422 -0.0435 0.0307 195 ARG A CB 1278 C CG . ARG A 164 ? 1.0204 0.9773 1.0899 0.0346 -0.0469 0.0376 195 ARG A CG 1279 C CD . ARG A 164 ? 1.2863 1.2566 1.3566 0.0335 -0.0490 0.0415 195 ARG A CD 1280 N NE . ARG A 164 ? 1.4173 1.3901 1.4786 0.0246 -0.0495 0.0444 195 ARG A NE 1281 C CZ . ARG A 164 ? 1.4585 1.4380 1.5170 0.0210 -0.0523 0.0496 195 ARG A CZ 1282 N NH1 . ARG A 164 ? 1.3572 1.3418 1.4214 0.0255 -0.0554 0.0531 195 ARG A NH1 1283 N NH2 . ARG A 164 ? 1.5094 1.4907 1.5596 0.0128 -0.0519 0.0509 195 ARG A NH2 1284 N N . ARG A 165 ? 0.6171 0.5432 0.7023 0.0556 -0.0415 0.0244 196 ARG A N 1285 C CA . ARG A 165 ? 0.6128 0.5276 0.7023 0.0621 -0.0434 0.0263 196 ARG A CA 1286 C C . ARG A 165 ? 0.6615 0.5839 0.7580 0.0677 -0.0476 0.0328 196 ARG A C 1287 O O . ARG A 165 ? 0.6506 0.5639 0.7475 0.0698 -0.0517 0.0387 196 ARG A O 1288 C CB . ARG A 165 ? 0.5997 0.4969 0.6816 0.0574 -0.0448 0.0289 196 ARG A CB 1289 C CG . ARG A 165 ? 0.7431 0.6318 0.8202 0.0546 -0.0402 0.0213 196 ARG A CG 1290 C CD . ARG A 165 ? 0.9497 0.8214 1.0197 0.0501 -0.0414 0.0238 196 ARG A CD 1291 N NE . ARG A 165 ? 1.0392 0.9045 1.1036 0.0461 -0.0369 0.0166 196 ARG A NE 1292 C CZ . ARG A 165 ? 1.0130 0.8641 1.0705 0.0414 -0.0366 0.0168 196 ARG A CZ 1293 N NH1 . ARG A 165 ? 0.6375 0.4787 0.6930 0.0401 -0.0406 0.0240 196 ARG A NH1 1294 N NH2 . ARG A 165 ? 1.1025 0.9496 1.1549 0.0375 -0.0324 0.0101 196 ARG A NH2 1295 N N . ILE A 166 ? 0.6982 0.6377 0.7999 0.0700 -0.0467 0.0315 197 ILE A N 1296 C CA . ILE A 166 ? 0.7019 0.6530 0.8106 0.0752 -0.0501 0.0365 197 ILE A CA 1297 C C . ILE A 166 ? 0.9343 0.8948 1.0536 0.0844 -0.0463 0.0300 197 ILE A C 1298 O O . ILE A 166 ? 0.6300 0.5956 0.7494 0.0834 -0.0411 0.0227 197 ILE A O 1299 C CB . ILE A 166 ? 0.8401 0.8046 0.9441 0.0681 -0.0524 0.0409 197 ILE A CB 1300 C CG1 . ILE A 166 ? 1.0606 1.0167 1.1549 0.0596 -0.0564 0.0480 197 ILE A CG1 1301 C CG2 . ILE A 166 ? 0.4925 0.4738 0.6040 0.0729 -0.0546 0.0435 197 ILE A CG2 1302 C CD1 . ILE A 166 ? 0.5672 0.5164 0.6627 0.0618 -0.0623 0.0564 197 ILE A CD1 1303 N N . CYS A 167 ? 0.8720 0.8349 1.0002 0.0933 -0.0486 0.0327 198 CYS A N 1304 C CA . CYS A 167 ? 0.8263 0.7995 0.9651 0.1022 -0.0446 0.0267 198 CYS A CA 1305 C C . CYS A 167 ? 0.9738 0.9700 1.1163 0.1014 -0.0435 0.0261 198 CYS A C 1306 O O . CYS A 167 ? 0.6026 0.6079 0.7436 0.0985 -0.0481 0.0325 198 CYS A O 1307 C CB . CYS A 167 ? 0.6507 0.6185 0.7986 0.1128 -0.0469 0.0291 198 CYS A CB 1308 S SG . CYS A 167 ? 0.6567 0.5987 0.8028 0.1162 -0.0449 0.0252 198 CYS A SG 1309 N N . GLU A 168 ? 1.2649 1.2700 1.4111 0.1030 -0.0373 0.0181 199 GLU A N 1310 C CA . GLU A 168 ? 1.2583 1.2854 1.4085 0.1022 -0.0348 0.0161 199 GLU A CA 1311 C C . GLU A 168 ? 1.1615 1.2000 1.3249 0.1130 -0.0338 0.0154 199 GLU A C 1312 O O . GLU A 168 ? 0.9556 0.9944 1.1252 0.1182 -0.0281 0.0085 199 GLU A O 1313 C CB . GLU A 168 ? 1.5132 1.5418 1.6599 0.0975 -0.0282 0.0079 199 GLU A CB 1314 C CG . GLU A 168 ? 1.6380 1.6581 1.7727 0.0873 -0.0289 0.0083 199 GLU A CG 1315 C CD . GLU A 168 ? 1.5997 1.6205 1.7307 0.0830 -0.0231 0.0003 199 GLU A CD 1316 O OE1 . GLU A 168 ? 1.7104 1.7243 1.8437 0.0867 -0.0190 -0.0066 199 GLU A OE1 1317 O OE2 . GLU A 168 ? 1.4339 1.4612 1.5590 0.0757 -0.0228 0.0007 199 GLU A OE2 1318 N N . CYS A 169 ? 1.4047 1.4522 1.5724 0.1164 -0.0394 0.0224 200 CYS A N 1319 C CA . CYS A 169 ? 1.5656 1.6241 1.7463 0.1274 -0.0399 0.0233 200 CYS A CA 1320 C C . CYS A 169 ? 1.5183 1.6033 1.7068 0.1287 -0.0369 0.0216 200 CYS A C 1321 O O . CYS A 169 ? 1.6467 1.7439 1.8302 0.1219 -0.0397 0.0243 200 CYS A O 1322 C CB . CYS A 169 ? 1.4600 1.5136 1.6416 0.1306 -0.0482 0.0319 200 CYS A CB 1323 S SG . CYS A 169 ? 1.2364 1.2598 1.4090 0.1279 -0.0518 0.0358 200 CYS A SG 1324 N N . PRO A 170 ? 1.1153 1.2094 1.3160 0.1371 -0.0318 0.0177 201 PRO A N 1325 C CA . PRO A 170 ? 0.9583 1.0786 1.1676 0.1373 -0.0281 0.0172 201 PRO A CA 1326 C C . PRO A 170 ? 1.0879 1.2249 1.3034 0.1415 -0.0343 0.0230 201 PRO A C 1327 O O . PRO A 170 ? 0.6381 0.7684 0.8491 0.1425 -0.0426 0.0279 201 PRO A O 1328 C CB . PRO A 170 ? 0.7654 0.8860 0.9857 0.1440 -0.0201 0.0100 201 PRO A CB 1329 C CG . PRO A 170 ? 0.9626 1.0624 1.1837 0.1522 -0.0221 0.0090 201 PRO A CG 1330 C CD . PRO A 170 ? 1.1495 1.2294 1.3560 0.1450 -0.0276 0.0122 201 PRO A CD 1331 N N . ASP A 171 ? 1.7040 1.8621 1.9302 0.1427 -0.0301 0.0225 202 ASP A N 1332 C CA . ASP A 171 ? 1.6081 1.7861 1.8387 0.1442 -0.0353 0.0263 202 ASP A CA 1333 C C . ASP A 171 ? 1.6254 1.7975 1.8604 0.1548 -0.0435 0.0294 202 ASP A C 1334 O O . ASP A 171 ? 1.9103 2.0712 2.1531 0.1648 -0.0416 0.0295 202 ASP A O 1335 C CB . ASP A 171 ? 1.6314 1.8278 1.8800 0.1467 -0.0271 0.0268 202 ASP A CB 1336 C CG . ASP A 171 ? 1.4755 1.6646 1.7377 0.1602 -0.0233 0.0234 202 ASP A CG 1337 O OD1 . ASP A 171 ? 1.3843 1.5731 1.6516 0.1708 -0.0286 0.0261 202 ASP A OD1 1338 O OD2 . ASP A 171 ? 1.3835 1.5669 1.6505 0.1606 -0.0155 0.0166 202 ASP A OD2 1339 N N . GLY A 172 ? 1.0627 1.2394 1.2931 0.1519 -0.0535 0.0314 203 GLY A N 1340 C CA . GLY A 172 ? 0.8603 1.0339 1.0977 0.1610 -0.0619 0.0365 203 GLY A CA 1341 C C . GLY A 172 ? 0.8773 1.0255 1.1132 0.1674 -0.0627 0.0410 203 GLY A C 1342 O O . GLY A 172 ? 0.7955 0.9401 1.0402 0.1782 -0.0664 0.0449 203 GLY A O 1343 N N . PHE A 173 ? 0.6865 0.8164 0.9110 0.1604 -0.0598 0.0402 204 PHE A N 1344 C CA . PHE A 173 ? 0.8078 0.9100 1.0281 0.1621 -0.0611 0.0431 204 PHE A CA 1345 C C . PHE A 173 ? 0.6676 0.7546 0.8724 0.1495 -0.0650 0.0470 204 PHE A C 1346 O O . PHE A 173 ? 0.6554 0.7446 0.8517 0.1401 -0.0616 0.0435 204 PHE A O 1347 C CB . PHE A 173 ? 0.7749 0.8659 0.9988 0.1668 -0.0522 0.0363 204 PHE A CB 1348 C CG . PHE A 173 ? 0.9673 1.0716 1.2074 0.1794 -0.0478 0.0332 204 PHE A CG 1349 C CD1 . PHE A 173 ? 1.0166 1.1127 1.2657 0.1912 -0.0509 0.0360 204 PHE A CD1 1350 C CD2 . PHE A 173 ? 0.9505 1.0758 1.1976 0.1791 -0.0403 0.0282 204 PHE A CD2 1351 C CE1 . PHE A 173 ? 0.7818 0.8907 1.0468 0.2032 -0.0464 0.0332 204 PHE A CE1 1352 C CE2 . PHE A 173 ? 0.7914 0.9292 1.0543 0.1892 -0.0356 0.0259 204 PHE A CE2 1353 C CZ . PHE A 173 ? 0.6290 0.7593 0.9012 0.2023 -0.0386 0.0282 204 PHE A CZ 1354 N N . HIS A 174 ? 1.3012 1.3735 1.5026 0.1494 -0.0718 0.0546 205 HIS A N 1355 C CA . HIS A 174 ? 1.5897 1.6490 1.7771 0.1372 -0.0750 0.0593 205 HIS A CA 1356 C C . HIS A 174 ? 1.5362 1.5695 1.7190 0.1379 -0.0768 0.0634 205 HIS A C 1357 O O . HIS A 174 ? 1.5172 1.5417 1.7078 0.1480 -0.0759 0.0625 205 HIS A O 1358 C CB . HIS A 174 ? 1.7795 1.8507 1.9646 0.1316 -0.0824 0.0660 205 HIS A CB 1359 C CG . HIS A 174 ? 1.8684 1.9391 2.0607 0.1389 -0.0899 0.0738 205 HIS A CG 1360 N ND1 . HIS A 174 ? 1.8745 1.9655 2.0780 0.1456 -0.0934 0.0742 205 HIS A ND1 1361 C CD2 . HIS A 174 ? 1.9546 2.0072 2.1441 0.1399 -0.0946 0.0814 205 HIS A CD2 1362 C CE1 . HIS A 174 ? 1.9291 2.0137 2.1365 0.1510 -0.1002 0.0823 205 HIS A CE1 1363 N NE2 . HIS A 174 ? 2.0291 2.0904 2.2282 0.1478 -0.1011 0.0870 205 HIS A NE2 1364 N N . GLY A 175 ? 1.3492 1.3711 1.5196 0.1269 -0.0792 0.0678 206 GLY A N 1365 C CA . GLY A 175 ? 1.5163 1.5149 1.6808 0.1253 -0.0814 0.0723 206 GLY A CA 1366 C C . GLY A 175 ? 1.4549 1.4376 1.6124 0.1210 -0.0756 0.0662 206 GLY A C 1367 O O . GLY A 175 ? 1.2457 1.2352 1.4031 0.1195 -0.0694 0.0583 206 GLY A O 1368 N N . PRO A 176 ? 1.3820 1.3435 1.5337 0.1188 -0.0776 0.0700 207 PRO A N 1369 C CA . PRO A 176 ? 1.2909 1.2368 1.4354 0.1140 -0.0727 0.0643 207 PRO A CA 1370 C C . PRO A 176 ? 1.0562 0.9983 1.2072 0.1218 -0.0661 0.0546 207 PRO A C 1371 O O . PRO A 176 ? 0.9731 0.9096 1.1183 0.1166 -0.0611 0.0481 207 PRO A O 1372 C CB . PRO A 176 ? 1.3831 1.3089 1.5214 0.1112 -0.0772 0.0714 207 PRO A CB 1373 C CG . PRO A 176 ? 1.2493 1.1772 1.3955 0.1192 -0.0834 0.0788 207 PRO A CG 1374 C CD . PRO A 176 ? 1.3416 1.2932 1.4923 0.1196 -0.0849 0.0799 207 PRO A CD 1375 N N . HIS A 177 ? 0.9182 0.8630 1.0810 0.1340 -0.0660 0.0536 208 HIS A N 1376 C CA . HIS A 177 ? 1.2280 1.1692 1.3975 0.1417 -0.0594 0.0441 208 HIS A CA 1377 C C . HIS A 177 ? 1.3474 1.3104 1.5293 0.1504 -0.0562 0.0397 208 HIS A C 1378 O O . HIS A 177 ? 1.5007 1.4620 1.6900 0.1582 -0.0508 0.0324 208 HIS A O 1379 C CB . HIS A 177 ? 1.2516 1.1707 1.4233 0.1488 -0.0604 0.0448 208 HIS A CB 1380 C CG . HIS A 177 ? 1.3009 1.2000 1.4614 0.1407 -0.0644 0.0508 208 HIS A CG 1381 N ND1 . HIS A 177 ? 1.2907 1.1770 1.4411 0.1323 -0.0608 0.0461 208 HIS A ND1 1382 C CD2 . HIS A 177 ? 1.4301 1.3216 1.5884 0.1397 -0.0716 0.0612 208 HIS A CD2 1383 C CE1 . HIS A 177 ? 1.4103 1.2822 1.5528 0.1265 -0.0656 0.0537 208 HIS A CE1 1384 N NE2 . HIS A 177 ? 1.4701 1.3442 1.6167 0.1304 -0.0722 0.0629 208 HIS A NE2 1385 N N . CYS A 178 ? 1.2093 1.1933 1.3931 0.1482 -0.0590 0.0437 209 CYS A N 1386 C CA . CYS A 178 ? 1.2604 1.2685 1.4554 0.1549 -0.0567 0.0407 209 CYS A CA 1387 C C . CYS A 178 ? 1.0589 1.0688 1.2674 0.1689 -0.0586 0.0427 209 CYS A C 1388 O O . CYS A 178 ? 1.0346 1.0546 1.2537 0.1773 -0.0531 0.0365 209 CYS A O 1389 C CB . CYS A 178 ? 1.2680 1.2843 1.4640 0.1533 -0.0479 0.0306 209 CYS A CB 1390 S SG . CYS A 178 ? 1.0394 1.0470 1.2199 0.1386 -0.0450 0.0271 209 CYS A SG 1391 N N . GLU A 179 ? 0.7881 0.7883 0.9963 0.1713 -0.0663 0.0515 210 GLU A N 1392 C CA . GLU A 179 ? 0.9298 0.9295 1.1503 0.1848 -0.0693 0.0547 210 GLU A CA 1393 C C . GLU A 179 ? 1.0629 1.0849 1.2907 0.1883 -0.0755 0.0610 210 GLU A C 1394 O O . GLU A 179 ? 1.1183 1.1542 1.3597 0.1999 -0.0746 0.0593 210 GLU A O 1395 C CB . GLU A 179 ? 0.9962 0.9686 1.2124 0.1862 -0.0737 0.0602 210 GLU A CB 1396 C CG . GLU A 179 ? 1.0133 0.9636 1.2248 0.1855 -0.0676 0.0529 210 GLU A CG 1397 C CD . GLU A 179 ? 1.1953 1.1190 1.3971 0.1808 -0.0718 0.0585 210 GLU A CD 1398 O OE1 . GLU A 179 ? 1.2158 1.1366 1.4061 0.1689 -0.0751 0.0636 210 GLU A OE1 1399 O OE2 . GLU A 179 ? 1.1691 1.0748 1.3747 0.1887 -0.0714 0.0576 210 GLU A OE2 1400 N N . GLY A 180 ? 1.2271 1.2528 1.4459 0.1782 -0.0816 0.0677 211 GLY A N 1401 C CA . GLY A 180 ? 1.3162 1.3615 1.5394 0.1788 -0.0886 0.0737 211 GLY A CA 1402 C C . GLY A 180 ? 1.3027 1.3764 1.5336 0.1807 -0.0856 0.0680 211 GLY A C 1403 O O . GLY A 180 ? 0.9145 0.9939 1.1445 0.1785 -0.0777 0.0599 211 GLY A O 1404 N N . THR A 181 ? 1.2717 1.3638 1.5102 0.1845 -0.0922 0.0723 212 THR A N 1405 C CA . THR A 181 ? 1.1993 1.3206 1.4460 0.1861 -0.0909 0.0671 212 THR A CA 1406 C C . THR A 181 ? 1.0916 1.2261 1.3340 0.1764 -0.0984 0.0712 212 THR A C 1407 O O . THR A 181 ? 1.0906 1.2208 1.3327 0.1760 -0.1066 0.0800 212 THR A O 1408 C CB . THR A 181 ? 1.1743 1.3093 1.4386 0.2023 -0.0899 0.0651 212 THR A CB 1409 O OG1 . THR A 181 ? 1.3909 1.5148 1.6602 0.2104 -0.0973 0.0733 212 THR A OG1 1410 C CG2 . THR A 181 ? 0.9160 1.0470 1.1856 0.2093 -0.0790 0.0577 212 THR A CG2 1411 N N . PCF B . ? 0.9482 0.9822 0.9577 -0.0232 -0.0015 -0.0019 1213 PCF A N 1412 P P . PCF B . ? 1.2001 1.2145 1.2011 -0.0251 -0.0045 0.0000 1213 PCF A P 1413 O O11 . PCF B . ? 1.3708 1.3805 1.3716 -0.0219 -0.0050 -0.0004 1213 PCF A O11 1414 O O12 . PCF B . ? 1.4020 1.4174 1.4013 -0.0260 -0.0036 0.0010 1213 PCF A O12 1415 O O13 . PCF B . ? 0.9852 1.0063 0.9894 -0.0237 -0.0041 -0.0010 1213 PCF A O13 1416 O O14 . PCF B . ? 1.0511 1.0634 1.0517 -0.0279 -0.0054 -0.0002 1213 PCF A O14 1417 C C11 . PCF B . ? 0.7203 0.7432 0.7262 -0.0208 -0.0036 -0.0014 1213 PCF A C11 1418 C C12 . PCF B . ? 0.9089 0.9353 0.9153 -0.0215 -0.0021 -0.0014 1213 PCF A C12 1419 C C13 . PCF B . ? 1.0378 1.0787 1.0505 -0.0220 0.0000 -0.0031 1213 PCF A C13 1420 C C14 . PCF B . ? 0.8548 0.8914 0.8667 -0.0231 -0.0028 -0.0020 1213 PCF A C14 1421 C C15 . PCF B . ? 0.9644 0.9982 0.9707 -0.0271 -0.0010 -0.0010 1213 PCF A C15 1422 C C1 . PCF B . ? 0.9297 0.9348 0.9306 -0.0221 -0.0059 -0.0011 1213 PCF A C1 1423 C C2 . PCF B . ? 0.4689 0.4707 0.4700 -0.0194 -0.0061 -0.0014 1213 PCF A C2 1424 C C3 . PCF B . ? 0.7939 0.7906 0.7949 -0.0202 -0.0069 -0.0009 1213 PCF A C3 1425 O O31 . PCF B . ? 0.9539 0.9487 0.9560 -0.0179 -0.0071 -0.0016 1213 PCF A O31 1426 O O32 . PCF B . ? 1.0592 1.0474 1.0644 -0.0196 -0.0076 -0.0048 1213 PCF A O32 1427 C C31 . PCF B . ? 0.9277 0.9184 0.9321 -0.0178 -0.0074 -0.0036 1213 PCF A C31 1428 C C32 . PCF B . ? 0.6875 0.6771 0.6930 -0.0158 -0.0072 -0.0045 1213 PCF A C32 1429 C C33 . PCF B . ? 0.4053 0.3983 0.4124 -0.0144 -0.0065 -0.0074 1213 PCF A C33 1430 C C34 . PCF B . ? 0.5540 0.5485 0.5609 -0.0128 -0.0060 -0.0076 1213 PCF A C34 1431 C C35 . PCF B . ? 0.5195 0.5157 0.5246 -0.0118 -0.0065 -0.0043 1213 PCF A C35 1432 C C36 . PCF B . ? 0.5362 0.5352 0.5414 -0.0103 -0.0062 -0.0048 1213 PCF A C36 1433 C C37 . PCF B . ? 0.4092 0.4082 0.4154 -0.0101 -0.0065 -0.0051 1213 PCF A C37 1434 C C38 . PCF B . ? 0.3112 0.3139 0.3178 -0.0089 -0.0062 -0.0055 1213 PCF A C38 1435 C C39 . PCF B . ? 0.4243 0.4266 0.4275 -0.0087 -0.0062 -0.0024 1213 PCF A C39 1436 C C40 . PCF B . ? 0.4090 0.4116 0.4099 -0.0087 -0.0054 -0.0021 1213 PCF A C40 1437 C C41 . PCF B . ? 0.4010 0.4037 0.3987 -0.0090 -0.0046 -0.0003 1213 PCF A C41 1438 C C42 . PCF B . ? 0.7186 0.7199 0.7145 -0.0094 -0.0045 0.0012 1213 PCF A C42 1439 C C43 . PCF B . ? 0.5282 0.5291 0.5216 -0.0099 -0.0042 0.0024 1213 PCF A C43 1440 O O21 . PCF B . ? 0.7614 0.7649 0.7616 -0.0177 -0.0055 -0.0005 1213 PCF A O21 1441 O O22 . PCF B . ? 0.8879 0.8929 0.8895 -0.0152 -0.0056 -0.0024 1213 PCF A O22 1442 C C21 . PCF B . ? 0.7970 0.8007 0.7977 -0.0153 -0.0054 -0.0013 1213 PCF A C21 1443 C C22 . PCF B . ? 0.5621 0.5649 0.5618 -0.0136 -0.0051 -0.0006 1213 PCF A C22 1444 C C23 . PCF B . ? 0.5705 0.5726 0.5709 -0.0121 -0.0053 -0.0016 1213 PCF A C23 1445 C C24 . PCF B . ? 0.3848 0.3874 0.3841 -0.0108 -0.0049 -0.0009 1213 PCF A C24 1446 C C25 . PCF B . ? 0.5658 0.5705 0.5651 -0.0104 -0.0047 -0.0010 1213 PCF A C25 1447 C C26 . PCF B . ? 0.4939 0.4982 0.4922 -0.0096 -0.0046 -0.0008 1213 PCF A C26 1448 C C27 . PCF B . ? 0.4911 0.4959 0.4890 -0.0093 -0.0047 -0.0001 1213 PCF A C27 1449 C C28 . PCF B . ? 0.5361 0.5390 0.5322 -0.0092 -0.0043 0.0007 1213 PCF A C28 1450 C C29 . PCF B . ? 0.4964 0.4985 0.4923 -0.0090 -0.0048 0.0009 1213 PCF A C29 1451 C C30 . PCF B . ? 0.3798 0.3798 0.3731 -0.0096 -0.0046 0.0018 1213 PCF A C30 1452 C C47 . PCF B . ? 0.3701 0.3679 0.3629 -0.0097 -0.0055 0.0015 1213 PCF A C47 1453 C C48 . PCF B . ? 0.3421 0.3374 0.3315 -0.0109 -0.0053 0.0025 1213 PCF A C48 1454 C C49 . PCF B . ? 0.2597 0.2546 0.2476 -0.0115 -0.0043 0.0021 1213 PCF A C49 1455 C C50 . PCF B . ? 0.2062 0.1995 0.1947 -0.0114 -0.0041 0.0000 1213 PCF A C50 1456 C C51 . PCF B . ? 0.2258 0.2191 0.2118 -0.0128 -0.0029 -0.0001 1213 PCF A C51 1457 C C52 . PCF B . ? 0.4368 0.4276 0.4217 -0.0136 -0.0021 -0.0027 1213 PCF A C52 1458 C C44 . PCF B . ? 0.4450 0.4456 0.4378 -0.0105 -0.0047 0.0035 1213 PCF A C44 1459 C C45 . PCF B . ? 0.5311 0.5310 0.5210 -0.0116 -0.0043 0.0043 1213 PCF A C45 1460 C C46 . PCF B . ? 0.3681 0.3684 0.3578 -0.0124 -0.0050 0.0052 1213 PCF A C46 1461 C C1 . NAG C . ? 0.3691 0.3672 0.3641 -0.0293 -0.0276 0.0264 1214 NAG A C1 1462 C C2 . NAG C . ? 0.3597 0.3557 0.3536 -0.0326 -0.0314 0.0300 1214 NAG A C2 1463 C C3 . NAG C . ? 0.5561 0.5522 0.5528 -0.0335 -0.0343 0.0348 1214 NAG A C3 1464 C C4 . NAG C . ? 0.6156 0.6180 0.6100 -0.0372 -0.0332 0.0344 1214 NAG A C4 1465 C C5 . NAG C . ? 0.4940 0.4978 0.4891 -0.0335 -0.0289 0.0304 1214 NAG A C5 1466 C C6 . NAG C . ? 0.4921 0.4998 0.4833 -0.0354 -0.0263 0.0291 1214 NAG A C6 1467 C C7 . NAG C . ? 0.3594 0.3472 0.3510 -0.0303 -0.0299 0.0284 1214 NAG A C7 1468 C C8 . NAG C . ? 0.3561 0.3369 0.3500 -0.0280 -0.0295 0.0282 1214 NAG A C8 1469 N N2 . NAG C . ? 0.3321 0.3218 0.3278 -0.0295 -0.0316 0.0301 1214 NAG A N2 1470 O O3 . NAG C . ? 0.4558 0.4487 0.4505 -0.0356 -0.0370 0.0386 1214 NAG A O3 1471 O O4 . NAG C . ? 0.5453 0.5489 0.5416 -0.0377 -0.0359 0.0393 1214 NAG A O4 1472 O O5 . NAG C . ? 0.4005 0.4026 0.3929 -0.0308 -0.0253 0.0256 1214 NAG A O5 1473 O O6 . NAG C . ? 0.8690 0.8787 0.8568 -0.0401 -0.0282 0.0315 1214 NAG A O6 1474 O O7 . NAG C . ? 0.4567 0.4482 0.4431 -0.0330 -0.0283 0.0270 1214 NAG A O7 1475 NA NA . NA D . ? 1.5756 1.5187 1.7437 0.1405 -0.0151 -0.0195 1215 NA A NA 1476 O O . HOH E . ? 0.4324 0.3672 0.4060 -0.0015 0.0087 -0.0342 2001 HOH A O 1477 O O . HOH E . ? 0.5199 0.4707 0.5007 -0.0030 0.0046 -0.0227 2002 HOH A O 1478 O O . HOH E . ? 0.3588 0.3156 0.3192 -0.0204 0.0084 -0.0257 2003 HOH A O 1479 O O . HOH E . ? 0.4827 0.4722 0.4569 -0.0130 0.0241 -0.0400 2004 HOH A O 1480 O O . HOH E . ? 0.3917 0.4150 0.3869 -0.0218 0.0081 -0.0126 2005 HOH A O 1481 O O . HOH E . ? 0.3157 0.3288 0.2856 -0.0358 -0.0040 0.0036 2006 HOH A O 1482 O O . HOH E . ? 0.2052 0.2064 0.1867 -0.0222 -0.0094 0.0096 2007 HOH A O 1483 O O . HOH E . ? 0.5039 0.5029 0.4860 -0.0312 -0.0216 0.0206 2008 HOH A O 1484 O O . HOH E . ? 0.3809 0.3983 0.3477 -0.0413 -0.0051 0.0057 2009 HOH A O 1485 O O . HOH E . ? 0.4485 0.4342 0.4546 -0.0197 -0.0289 0.0243 2010 HOH A O 1486 O O . HOH E . ? 0.3161 0.2872 0.3217 -0.0180 -0.0265 0.0211 2011 HOH A O 1487 O O . HOH E . ? 0.4680 0.4106 0.4578 0.0063 -0.0001 -0.0174 2012 HOH A O 1488 O O . HOH E . ? 0.4546 0.3739 0.4616 -0.0187 -0.0356 0.0327 2013 HOH A O 1489 O O . HOH E . ? 0.6189 0.5770 0.6230 -0.0256 -0.0107 -0.0019 2014 HOH A O 1490 O O . HOH E . ? 0.3655 0.3756 0.3536 -0.0340 -0.0047 0.0067 2015 HOH A O 1491 O O . HOH E . ? 0.4234 0.4309 0.3925 -0.0603 -0.0102 0.0191 2016 HOH A O 1492 O O . HOH E . ? 0.7827 0.7878 0.7925 0.0016 -0.0239 0.0138 2017 HOH A O 1493 O O . HOH E . ? 0.4130 0.4466 0.3850 -0.0454 0.0018 0.0011 2018 HOH A O 1494 O O . HOH E . ? 0.4224 0.4551 0.4255 -0.0232 0.0024 -0.0034 2019 HOH A O 1495 O O . HOH E . ? 0.4846 0.5125 0.4817 -0.0294 0.0005 0.0004 2020 HOH A O 1496 O O . HOH E . ? 0.5281 0.5698 0.5212 -0.0328 0.0065 -0.0051 2021 HOH A O 1497 O O . HOH E . ? 0.4109 0.4401 0.3793 -0.0443 0.0036 -0.0054 2022 HOH A O 1498 O O . HOH E . ? 0.4485 0.4900 0.4320 -0.0370 0.0099 -0.0108 2023 HOH A O 1499 O O . HOH E . ? 0.5179 0.5062 0.5197 -0.0001 -0.0190 0.0094 2024 HOH A O 1500 O O . HOH E . ? 0.4165 0.4509 0.4284 -0.0168 0.0004 -0.0044 2025 HOH A O 1501 O O . HOH E . ? 0.6451 0.6564 0.6466 -0.0075 -0.0160 0.0071 2026 HOH A O 1502 O O . HOH E . ? 0.4542 0.4940 0.4733 -0.0095 0.0057 -0.0125 2027 HOH A O 1503 O O . HOH E . ? 0.4615 0.4974 0.4893 0.0026 0.0039 -0.0133 2028 HOH A O 1504 O O . HOH E . ? 0.3369 0.3338 0.3519 0.0082 -0.0126 0.0015 2029 HOH A O 1505 O O . HOH E . ? 0.4029 0.4501 0.4268 -0.0133 -0.0022 -0.0041 2030 HOH A O 1506 O O . HOH E . ? 0.4197 0.4667 0.4444 -0.0100 -0.0146 0.0012 2031 HOH A O 1507 O O . HOH E . ? 0.4270 0.4664 0.4414 -0.0166 -0.0118 -0.0007 2032 HOH A O 1508 O O . HOH E . ? 0.4358 0.4541 0.4389 -0.0085 -0.0143 0.0044 2033 HOH A O 1509 O O . HOH E . ? 0.6002 0.6227 0.6129 -0.0042 -0.0157 0.0041 2034 HOH A O 1510 O O . HOH E . ? 0.3469 0.2625 0.2836 -0.0380 -0.0010 -0.0183 2035 HOH A O 1511 O O . HOH E . ? 0.2816 0.3160 0.2790 -0.0190 -0.0159 0.0044 2036 HOH A O 1512 O O . HOH E . ? 0.5444 0.6069 0.5676 -0.0165 -0.0207 0.0045 2037 HOH A O 1513 O O . HOH E . ? 0.5034 0.5177 0.4822 -0.0316 -0.0095 0.0133 2038 HOH A O 1514 O O . HOH E . ? 0.5866 0.6310 0.5728 -0.0298 0.0033 -0.0053 2039 HOH A O 1515 O O . HOH E . ? 0.3835 0.4341 0.3941 -0.0151 -0.0039 -0.0023 2040 HOH A O 1516 O O . HOH E . ? 0.5514 0.5915 0.7625 0.1577 0.0140 -0.0492 2041 HOH A O 1517 O O . HOH E . ? 0.4797 0.4940 0.4831 -0.0192 -0.0066 -0.0036 2042 HOH A O 1518 O O . HOH E . ? 0.4635 0.4623 0.4617 -0.0193 -0.0077 -0.0167 2043 HOH A O 1519 O O . HOH E . ? 0.6418 0.6619 0.6326 -0.0196 -0.0031 -0.0118 2044 HOH A O 1520 O O . HOH E . ? 0.4811 0.5636 0.5535 0.0175 -0.0017 -0.0190 2045 HOH A O 1521 O O . HOH E . ? 0.5318 0.6027 0.5861 0.0039 -0.0089 -0.0056 2046 HOH A O 1522 O O . HOH E . ? 0.6279 0.6379 0.6564 -0.0038 -0.0277 0.0209 2047 HOH A O 1523 O O . HOH E . ? 0.6124 0.6016 0.6132 -0.0267 -0.0105 -0.0180 2048 HOH A O 1524 O O . HOH E . ? 0.6008 0.6130 0.6084 -0.0104 0.0104 -0.0542 2049 HOH A O 1525 O O . HOH E . ? 0.3340 0.3213 0.3352 -0.0141 -0.0098 -0.0118 2050 HOH A O 1526 O O . HOH E . ? 0.5383 0.4841 0.5431 -0.0251 -0.0049 -0.0192 2051 HOH A O 1527 O O . HOH E . ? 0.3603 0.2666 0.3707 -0.0107 -0.0123 -0.0133 2052 HOH A O 1528 O O . HOH E . ? 0.3572 0.2960 0.4029 0.0169 -0.0224 -0.0036 2053 HOH A O 1529 O O . HOH E . ? 0.7193 0.6759 0.6989 -0.0568 -0.0184 0.0212 2054 HOH A O 1530 O O . HOH E . ? 0.9476 0.8975 0.9666 0.0122 0.0153 -0.0788 2055 HOH A O 1531 O O . HOH E . ? 0.4665 0.4257 0.4892 -0.0068 -0.0341 0.0267 2056 HOH A O 1532 O O . HOH E . ? 0.2444 0.4679 0.5509 0.1786 -0.0156 0.0245 2057 HOH A O 1533 O O . HOH E . ? 0.4855 0.7009 0.7272 0.1328 -0.0759 0.0233 2058 HOH A O 1534 O O . HOH E . ? 0.5813 0.5751 0.5919 -0.0191 -0.0294 0.0269 2059 HOH A O 1535 O O . HOH E . ? 0.5837 0.5882 0.5669 -0.0221 -0.0066 0.0083 2060 HOH A O 1536 O O . HOH E . ? 0.2974 0.3050 0.2707 -0.0314 -0.0085 0.0079 2061 HOH A O 1537 O O . HOH E . ? 0.2860 0.2893 0.2646 -0.0246 -0.0056 0.0076 2062 HOH A O 1538 O O . HOH E . ? 0.6538 0.6104 0.5910 -0.0396 0.0141 -0.0320 2063 HOH A O 1539 O O . HOH E . ? 0.7050 0.6429 0.6597 -0.0104 0.0214 -0.0528 2064 HOH A O 1540 O O . HOH E . ? 0.6442 0.5756 0.6055 -0.0088 0.0127 -0.0417 2065 HOH A O 1541 O O . HOH E . ? 0.5303 0.4439 0.4782 -0.0276 0.0006 -0.0229 2066 HOH A O 1542 O O . HOH E . ? 0.2216 0.1445 0.1808 -0.0206 -0.0025 -0.0148 2067 HOH A O 1543 O O . HOH E . ? 0.4718 0.4436 0.4085 -0.0489 0.0035 -0.0070 2068 HOH A O 1544 O O . HOH E . ? 0.2535 0.2211 0.2079 -0.0311 0.0019 -0.0091 2069 HOH A O 1545 O O . HOH E . ? 0.5563 0.4705 0.5263 -0.0096 -0.0010 -0.0198 2070 HOH A O 1546 O O . HOH E . ? 0.6772 0.5967 0.6616 0.0069 0.0044 -0.0308 2071 HOH A O 1547 O O . HOH E . ? 0.3648 0.3713 0.3419 -0.0277 -0.0065 0.0088 2072 HOH A O 1548 O O . HOH E . ? 0.5117 0.5233 0.4795 -0.0361 -0.0074 0.0094 2073 HOH A O 1549 O O . HOH E . ? 0.5497 0.5780 0.5333 -0.0265 -0.0028 0.0057 2074 HOH A O 1550 O O . HOH E . ? 0.6343 0.6876 0.6281 -0.0228 0.0007 -0.0034 2075 HOH A O 1551 O O . HOH E . ? 0.4789 0.5326 0.4837 -0.0165 0.0006 -0.0089 2076 HOH A O 1552 O O . HOH E . ? 0.4643 0.5254 0.4893 -0.0089 -0.0028 -0.0092 2077 HOH A O 1553 O O . HOH E . ? 0.6364 0.7110 0.6552 -0.0123 0.0040 -0.0203 2078 HOH A O 1554 O O . HOH E . ? 0.5302 0.6066 0.5576 -0.0075 0.0142 -0.0499 2079 HOH A O 1555 O O . HOH E . ? 0.6019 0.6701 0.6201 -0.0135 0.0176 -0.0573 2080 HOH A O 1556 O O . HOH E . ? 0.4527 0.5163 0.4896 0.0029 0.0196 -0.0639 2081 HOH A O 1557 O O . HOH E . ? 0.3929 0.4114 0.4269 0.0105 0.0208 -0.0753 2082 HOH A O 1558 O O . HOH E . ? 0.3702 0.4038 0.4192 0.0188 0.0208 -0.0724 2083 HOH A O 1559 O O . HOH E . ? 0.5657 0.6335 0.6452 0.0310 0.0090 -0.0437 2084 HOH A O 1560 O O . HOH E . ? 0.2987 0.2766 0.3770 0.0477 0.0033 -0.0498 2085 HOH A O 1561 O O . HOH E . ? 0.3688 0.3233 0.4394 0.0424 -0.0055 -0.0369 2086 HOH A O 1562 O O . HOH E . ? 0.4309 0.5081 0.4980 0.0179 0.0046 -0.0320 2087 HOH A O 1563 O O . HOH E . ? 0.2505 0.3154 0.3170 0.0155 -0.0095 -0.0099 2088 HOH A O 1564 O O . HOH E . ? 0.2431 0.2985 0.2790 -0.0039 -0.0086 -0.0046 2089 HOH A O 1565 O O . HOH E . ? 0.2753 0.2961 0.2990 -0.0057 -0.0221 0.0147 2090 HOH A O 1566 O O . HOH E . ? 0.1996 0.2407 0.2226 -0.0085 -0.0132 0.0034 2091 HOH A O 1567 O O . HOH E . ? 0.3446 0.3833 0.3545 -0.0157 -0.0123 0.0088 2092 HOH A O 1568 O O . HOH E . ? 0.4109 0.4467 0.4403 -0.0040 -0.0234 0.0154 2093 HOH A O 1569 O O . HOH E . ? 0.3665 0.3844 0.3543 -0.0295 -0.0142 0.0198 2094 HOH A O 1570 O O . HOH E . ? 0.5629 0.5875 0.5716 -0.0211 -0.0267 0.0297 2095 HOH A O 1571 O O . HOH E . ? 0.3828 0.3926 0.3735 -0.0276 -0.0169 0.0209 2096 HOH A O 1572 O O . HOH E . ? 0.1944 0.2402 0.1897 -0.0271 -0.0088 0.0117 2097 HOH A O 1573 O O . HOH E . ? 0.2312 0.2445 0.2013 -0.0371 -0.0075 0.0105 2098 HOH A O 1574 O O . HOH E . ? 0.2866 0.2887 0.2511 -0.0369 -0.0059 0.0076 2099 HOH A O 1575 O O . HOH E . ? 0.5122 0.5123 0.4798 -0.0329 -0.0046 0.0061 2100 HOH A O 1576 O O . HOH E . ? 0.6902 0.6838 0.6438 -0.0431 -0.0014 0.0023 2101 HOH A O 1577 O O . HOH E . ? 0.3704 0.3556 0.3149 -0.0478 0.0041 -0.0035 2102 HOH A O 1578 O O . HOH E . ? 0.3817 0.3769 0.3316 -0.0481 0.0027 -0.0019 2103 HOH A O 1579 O O . HOH E . ? 0.3798 0.4032 0.3474 -0.0436 0.0040 -0.0061 2104 HOH A O 1580 O O . HOH E . ? 0.2497 0.2594 0.2268 -0.0347 -0.0112 0.0141 2105 HOH A O 1581 O O . HOH E . ? 0.3657 0.3739 0.3482 -0.0263 -0.0094 0.0125 2106 HOH A O 1582 O O . HOH E . ? 0.3254 0.2560 0.3802 0.0282 -0.0178 -0.0147 2107 HOH A O 1583 O O . HOH E . ? 0.5936 0.6866 0.7927 0.1265 -0.0032 -0.0156 2108 HOH A O 1584 O O . HOH E . ? 0.3913 0.3432 0.4291 0.0262 0.0154 -0.0767 2109 HOH A O 1585 O O . HOH E . ? 0.5061 0.4217 0.5591 0.0466 0.0134 -0.0764 2110 HOH A O 1586 O O . HOH E . ? 0.6368 0.5426 0.6527 0.0170 0.0102 -0.0757 2111 HOH A O 1587 O O . HOH E . ? 0.8701 0.7416 0.8964 0.0192 -0.0062 -0.0385 2112 HOH A O 1588 O O . HOH E . ? 0.4489 0.3945 0.4566 0.0000 0.0065 -0.0627 2113 HOH A O 1589 O O . HOH E . ? 0.1691 0.1833 0.1653 -0.0121 -0.0023 -0.0056 2114 HOH A O 1590 O O . HOH E . ? 0.5360 0.5593 0.5220 -0.0230 -0.0007 0.0023 2115 HOH A O 1591 O O . HOH E . ? 0.4701 0.4747 0.4564 -0.0175 -0.0047 0.0059 2116 HOH A O 1592 O O . HOH E . ? 0.6630 0.5613 0.6326 -0.0077 -0.0153 0.0067 2117 HOH A O 1593 O O . HOH E . ? 0.4170 0.3346 0.3952 -0.0025 -0.0054 -0.0096 2118 HOH A O 1594 O O . HOH E . ? 0.4507 0.3324 0.3962 -0.0292 -0.0067 -0.0135 2119 HOH A O 1595 O O . HOH E . ? 0.4376 0.4012 0.3916 -0.0328 -0.0203 0.0128 2120 HOH A O 1596 O O . HOH E . ? 0.6408 0.5179 0.5955 -0.0190 -0.0230 0.0182 2121 HOH A O 1597 O O . HOH E . ? 0.3603 0.3097 0.3208 -0.0265 -0.0244 0.0187 2122 HOH A O 1598 O O . HOH E . ? 0.5136 0.4985 0.4850 -0.0278 -0.0172 0.0122 2123 HOH A O 1599 O O . HOH E . ? 0.6649 0.6235 0.6627 0.0062 -0.0146 0.0034 2124 HOH A O 1600 O O . HOH E . ? 0.4471 0.4392 0.4402 -0.0096 -0.0168 0.0072 2125 HOH A O 1601 O O . HOH E . ? 0.3350 0.3374 0.3293 -0.0109 -0.0135 0.0071 2126 HOH A O 1602 O O . HOH E . ? 0.4526 0.4600 0.4388 -0.0190 -0.0053 0.0066 2127 HOH A O 1603 O O . HOH E . ? 0.3837 0.3925 0.3736 -0.0159 -0.0145 0.0107 2128 HOH A O 1604 O O . HOH E . ? 0.4203 0.4375 0.4162 -0.0126 -0.0150 0.0075 2129 HOH A O 1605 O O . HOH E . ? 0.4447 0.4644 0.4302 -0.0226 -0.0025 0.0034 2130 HOH A O 1606 O O . HOH E . ? 0.6065 0.6332 0.6064 -0.0135 -0.0161 0.0059 2131 HOH A O 1607 O O . HOH E . ? 0.4634 0.4641 0.4637 -0.0148 -0.0071 -0.0127 2132 HOH A O 1608 O O . HOH E . ? 0.4421 0.3618 0.4358 -0.0180 -0.0064 -0.0297 2133 HOH A O 1609 O O . HOH E . ? 0.5629 0.4594 0.5847 0.0117 -0.0047 -0.0401 2134 HOH A O 1610 O O . HOH E . ? 0.8997 0.7811 1.0245 0.1094 -0.0240 -0.0102 2135 HOH A O 1611 O O . HOH E . ? 0.6854 0.5167 0.7991 0.1088 -0.0279 -0.0057 2136 HOH A O 1612 O O . HOH E . ? 0.9423 0.8448 1.1044 0.1443 -0.0196 -0.0160 2137 HOH A O 1613 O O . HOH E . ? 0.9219 0.8999 1.1140 0.1561 -0.0087 -0.0247 2138 HOH A O 1614 O O . HOH E . ? 0.9337 0.9032 1.1692 0.2036 -0.0217 -0.0057 2139 HOH A O 1615 O O . HOH E . ? 0.7881 0.8989 0.9627 0.1124 -0.0547 0.0343 2140 HOH A O 1616 O O . HOH E . ? 0.8292 0.7377 0.9433 0.0887 -0.0580 0.0462 2141 HOH A O 1617 O O . HOH E . ? 0.7667 0.6028 0.8336 0.0520 -0.0494 0.0369 2142 HOH A O 1618 O O . HOH E . ? 0.7590 0.7886 0.9134 0.1085 -0.0627 0.0492 2143 HOH A O 1619 O O . HOH E . ? 0.7574 0.8240 0.9161 0.1054 -0.0537 0.0373 2144 HOH A O 1620 O O . HOH E . ? 0.9570 1.0066 1.1064 0.0984 -0.0806 0.0693 2145 HOH A O 1621 O O . HOH E . ? 0.7132 0.6716 0.8956 0.1525 -0.0771 0.0664 2146 HOH A O 1622 O O . HOH E . ? 1.0630 1.1175 1.3108 0.2033 -0.1053 0.0897 2147 HOH A O 1623 O O . HOH E . ? 0.6540 0.8223 0.9446 0.2201 -0.1102 0.0770 2148 HOH A O 1624 O O . HOH E . ? 0.4741 0.5078 0.4398 -0.0547 -0.0015 0.0073 2149 HOH A O 1625 O O . HOH E . ? 0.9353 0.9733 0.9012 -0.0506 0.0033 -0.0030 2150 HOH A O 1626 O O . HOH E . ? 0.5942 0.5326 0.7509 0.1317 -0.0051 -0.0359 2151 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 GLU 1 32 ? ? ? A . n A 1 2 THR 2 33 33 THR THR A . n A 1 3 GLY 3 34 34 GLY GLY A . n A 1 4 SER 4 35 35 SER SER A . n A 1 5 LEU 5 36 36 LEU LEU A . n A 1 6 TYR 6 37 37 TYR TYR A . n A 1 7 LEU 7 38 38 LEU LEU A . n A 1 8 TRP 8 39 39 TRP TRP A . n A 1 9 ILE 9 40 40 ILE ILE A . n A 1 10 ASP 10 41 41 ASP ASP A . n A 1 11 ALA 11 42 42 ALA ALA A . n A 1 12 HIS 12 43 43 HIS HIS A . n A 1 13 GLN 13 44 44 GLN GLN A . n A 1 14 ALA 14 45 45 ALA ALA A . n A 1 15 ARG 15 46 46 ARG ARG A . n A 1 16 VAL 16 47 47 VAL VAL A . n A 1 17 LEU 17 48 48 LEU LEU A . n A 1 18 ILE 18 49 49 ILE ILE A . n A 1 19 GLY 19 50 50 GLY GLY A . n A 1 20 PHE 20 51 51 PHE PHE A . n A 1 21 GLU 21 52 52 GLU GLU A . n A 1 22 GLU 22 53 53 GLU GLU A . n A 1 23 ASP 23 54 54 ASP ASP A . n A 1 24 ILE 24 55 55 ILE ILE A . n A 1 25 LEU 25 56 56 LEU LEU A . n A 1 26 ILE 26 57 57 ILE ILE A . n A 1 27 VAL 27 58 58 VAL VAL A . n A 1 28 SER 28 59 59 SER SER A . n A 1 29 GLU 29 60 60 GLU GLU A . n A 1 30 GLY 30 61 61 GLY GLY A . n A 1 31 MLY 31 62 62 MLY MLY A . n A 1 32 MET 32 63 63 MET MET A . n A 1 33 ALA 33 64 64 ALA ALA A . n A 1 34 PRO 34 65 65 PRO PRO A . n A 1 35 PHE 35 66 66 PHE PHE A . n A 1 36 THR 36 67 67 THR THR A . n A 1 37 HIS 37 68 68 HIS HIS A . n A 1 38 ASP 38 69 69 ASP ASP A . n A 1 39 PHE 39 70 70 PHE PHE A . n A 1 40 ARG 40 71 71 ARG ARG A . n A 1 41 MLY 41 72 72 MLY MLY A . n A 1 42 ALA 42 73 73 ALA ALA A . n A 1 43 GLN 43 74 74 GLN GLN A . n A 1 44 GLN 44 75 75 GLN GLN A . n A 1 45 ARG 45 76 76 ARG ARG A . n A 1 46 MET 46 77 77 MET MET A . n A 1 47 PRO 47 78 78 PRO PRO A . n A 1 48 ALA 48 79 79 ALA ALA A . n A 1 49 ILE 49 80 80 ILE ILE A . n A 1 50 PRO 50 81 81 PRO PRO A . n A 1 51 VAL 51 82 82 VAL VAL A . n A 1 52 ASN 52 83 83 ASN ASN A . n A 1 53 ILE 53 84 84 ILE ILE A . n A 1 54 HIS 54 85 85 HIS HIS A . n A 1 55 SER 55 86 86 SER SER A . n A 1 56 MET 56 87 87 MET MET A . n A 1 57 ASN 57 88 88 ASN ASN A . n A 1 58 PHE 58 89 89 PHE PHE A . n A 1 59 THR 59 90 90 THR THR A . n A 1 60 TRP 60 91 91 TRP TRP A . n A 1 61 GLN 61 92 92 GLN GLN A . n A 1 62 ALA 62 93 93 ALA ALA A . n A 1 63 ALA 63 94 94 ALA ALA A . n A 1 64 GLY 64 95 95 GLY GLY A . n A 1 65 GLN 65 96 96 GLN GLN A . n A 1 66 ALA 66 97 97 ALA ALA A . n A 1 67 GLU 67 98 98 GLU GLU A . n A 1 68 TYR 68 99 99 TYR TYR A . n A 1 69 PHE 69 100 100 PHE PHE A . n A 1 70 TYR 70 101 101 TYR TYR A . n A 1 71 GLU 71 102 102 GLU GLU A . n A 1 72 PHE 72 103 103 PHE PHE A . n A 1 73 LEU 73 104 104 LEU LEU A . n A 1 74 SER 74 105 105 SER SER A . n A 1 75 LEU 75 106 106 LEU LEU A . n A 1 76 ARG 76 107 107 ARG ARG A . n A 1 77 SER 77 108 108 SER SER A . n A 1 78 LEU 78 109 109 LEU LEU A . n A 1 79 ASP 79 110 110 ASP ASP A . n A 1 80 MLY 80 111 111 MLY MLY A . n A 1 81 GLY 81 112 112 GLY GLY A . n A 1 82 ILE 82 113 113 ILE ILE A . n A 1 83 MET 83 114 114 MET MET A . n A 1 84 ALA 84 115 115 ALA ALA A . n A 1 85 ASP 85 116 116 ASP ASP A . n A 1 86 PRO 86 117 117 PRO PRO A . n A 1 87 THR 87 118 118 THR THR A . n A 1 88 VAL 88 119 119 VAL VAL A . n A 1 89 ASN 89 120 120 ASN ASN A . n A 1 90 VAL 90 121 121 VAL VAL A . n A 1 91 PRO 91 122 122 PRO PRO A . n A 1 92 LEU 92 123 123 LEU LEU A . n A 1 93 LEU 93 124 124 LEU LEU A . n A 1 94 GLY 94 125 125 GLY GLY A . n A 1 95 THR 95 126 126 THR THR A . n A 1 96 VAL 96 127 127 VAL VAL A . n A 1 97 PRO 97 128 128 PRO PRO A . n A 1 98 HIS 98 129 129 HIS HIS A . n A 1 99 MLY 99 130 130 MLY MLY A . n A 1 100 ALA 100 131 131 ALA ALA A . n A 1 101 SER 101 132 132 SER SER A . n A 1 102 VAL 102 133 133 VAL VAL A . n A 1 103 VAL 103 134 134 VAL VAL A . n A 1 104 GLN 104 135 135 GLN GLN A . n A 1 105 VAL 105 136 136 VAL VAL A . n A 1 106 GLY 106 137 137 GLY GLY A . n A 1 107 PHE 107 138 138 PHE PHE A . n A 1 108 PRO 108 139 139 PRO PRO A . n A 1 109 CYS 109 140 140 CYS CYS A . n A 1 110 LEU 110 141 141 LEU LEU A . n A 1 111 GLY 111 142 142 GLY GLY A . n A 1 112 MLY 112 143 143 MLY MLY A . n A 1 113 GLN 113 144 144 GLN GLN A . n A 1 114 ASP 114 145 145 ASP ASP A . n A 1 115 GLY 115 146 146 GLY GLY A . n A 1 116 VAL 116 147 147 VAL VAL A . n A 1 117 ALA 117 148 148 ALA ALA A . n A 1 118 ALA 118 149 149 ALA ALA A . n A 1 119 PHE 119 150 150 PHE PHE A . n A 1 120 GLU 120 151 151 GLU GLU A . n A 1 121 VAL 121 152 152 VAL VAL A . n A 1 122 ASP 122 153 153 ASP ASP A . n A 1 123 VAL 123 154 154 VAL VAL A . n A 1 124 ILE 124 155 155 ILE ILE A . n A 1 125 VAL 125 156 156 VAL VAL A . n A 1 126 MET 126 157 157 MET MET A . n A 1 127 ASN 127 158 158 ASN ASN A . n A 1 128 SER 128 159 159 SER SER A . n A 1 129 GLU 129 160 160 GLU GLU A . n A 1 130 GLY 130 161 161 GLY GLY A . n A 1 131 ASN 131 162 162 ASN ASN A . n A 1 132 THR 132 163 163 THR THR A . n A 1 133 ILE 133 164 164 ILE ILE A . n A 1 134 LEU 134 165 165 LEU LEU A . n A 1 135 MLY 135 166 166 MLY MLY A . n A 1 136 THR 136 167 167 THR THR A . n A 1 137 PRO 137 168 168 PRO PRO A . n A 1 138 GLN 138 169 169 GLN GLN A . n A 1 139 ASN 139 170 170 ASN ASN A . n A 1 140 ALA 140 171 171 ALA ALA A . n A 1 141 ILE 141 172 172 ILE ILE A . n A 1 142 PHE 142 173 173 PHE PHE A . n A 1 143 PHE 143 174 174 PHE PHE A . n A 1 144 LYS 144 175 175 LYS LYS A . n A 1 145 THR 145 176 176 THR THR A . n A 1 146 CYS 146 177 177 CYS CYS A . n A 1 147 GLN 147 178 178 GLN GLN A . n A 1 148 GLN 148 179 179 GLN GLN A . n A 1 149 ALA 149 180 180 ALA ALA A . n A 1 150 GLU 150 181 181 GLU GLU A . n A 1 151 CYS 151 182 182 CYS CYS A . n A 1 152 PRO 152 183 183 PRO PRO A . n A 1 153 GLY 153 184 184 GLY GLY A . n A 1 154 GLY 154 185 185 GLY GLY A . n A 1 155 CYS 155 186 186 CYS CYS A . n A 1 156 ARG 156 187 187 ARG ARG A . n A 1 157 ASN 157 188 188 ASN ASN A . n A 1 158 GLY 158 189 189 GLY GLY A . n A 1 159 GLY 159 190 190 GLY GLY A . n A 1 160 PHE 160 191 191 PHE PHE A . n A 1 161 CYS 161 192 192 CYS CYS A . n A 1 162 ASN 162 193 193 ASN ASN A . n A 1 163 GLU 163 194 194 GLU GLU A . n A 1 164 ARG 164 195 195 ARG ARG A . n A 1 165 ARG 165 196 196 ARG ARG A . n A 1 166 ILE 166 197 197 ILE ILE A . n A 1 167 CYS 167 198 198 CYS CYS A . n A 1 168 GLU 168 199 199 GLU GLU A . n A 1 169 CYS 169 200 200 CYS CYS A . n A 1 170 PRO 170 201 201 PRO PRO A . n A 1 171 ASP 171 202 202 ASP ASP A . n A 1 172 GLY 172 203 203 GLY GLY A . n A 1 173 PHE 173 204 204 PHE PHE A . n A 1 174 HIS 174 205 205 HIS HIS A . n A 1 175 GLY 175 206 206 GLY GLY A . n A 1 176 PRO 176 207 207 PRO PRO A . n A 1 177 HIS 177 208 208 HIS HIS A . n A 1 178 CYS 178 209 209 CYS CYS A . n A 1 179 GLU 179 210 210 GLU GLU A . n A 1 180 GLY 180 211 211 GLY GLY A . n A 1 181 THR 181 212 212 THR THR A . n A 1 182 LYS 182 213 ? ? ? A . n A 1 183 HIS 183 214 ? ? ? A . n A 1 184 HIS 184 215 ? ? ? A . n A 1 185 HIS 185 216 ? ? ? A . n A 1 186 HIS 186 217 ? ? ? A . n A 1 187 HIS 187 218 ? ? ? A . n A 1 188 HIS 188 219 ? ? ? 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 PCF 1 1213 1213 PCF PCF A . C 3 NAG 1 1214 1214 NAG NAG A . D 4 NA 1 1215 1215 NA NA A . E 5 HOH 1 2001 2001 HOH HOH A . E 5 HOH 2 2002 2002 HOH HOH A . E 5 HOH 3 2003 2003 HOH HOH A . E 5 HOH 4 2004 2004 HOH HOH A . E 5 HOH 5 2005 2005 HOH HOH A . E 5 HOH 6 2006 2006 HOH HOH A . E 5 HOH 7 2007 2007 HOH HOH A . E 5 HOH 8 2008 2008 HOH HOH A . E 5 HOH 9 2009 2009 HOH HOH A . E 5 HOH 10 2010 2010 HOH HOH A . E 5 HOH 11 2011 2011 HOH HOH A . E 5 HOH 12 2012 2012 HOH HOH A . E 5 HOH 13 2013 2013 HOH HOH A . E 5 HOH 14 2014 2014 HOH HOH A . E 5 HOH 15 2015 2015 HOH HOH A . E 5 HOH 16 2016 2016 HOH HOH A . E 5 HOH 17 2017 2017 HOH HOH A . E 5 HOH 18 2018 2018 HOH HOH A . E 5 HOH 19 2019 2019 HOH HOH A . E 5 HOH 20 2020 2020 HOH HOH A . E 5 HOH 21 2021 2021 HOH HOH A . E 5 HOH 22 2022 2022 HOH HOH A . E 5 HOH 23 2023 2023 HOH HOH A . E 5 HOH 24 2024 2024 HOH HOH A . E 5 HOH 25 2025 2025 HOH HOH A . E 5 HOH 26 2026 2026 HOH HOH A . E 5 HOH 27 2027 2027 HOH HOH A . E 5 HOH 28 2028 2028 HOH HOH A . E 5 HOH 29 2029 2029 HOH HOH A . E 5 HOH 30 2030 2030 HOH HOH A . E 5 HOH 31 2031 2031 HOH HOH A . E 5 HOH 32 2032 2032 HOH HOH A . E 5 HOH 33 2033 2033 HOH HOH A . E 5 HOH 34 2034 2034 HOH HOH A . E 5 HOH 35 2035 2035 HOH HOH A . E 5 HOH 36 2036 2036 HOH HOH A . E 5 HOH 37 2037 2037 HOH HOH A . E 5 HOH 38 2038 2038 HOH HOH A . E 5 HOH 39 2039 2039 HOH HOH A . E 5 HOH 40 2040 2040 HOH HOH A . E 5 HOH 41 2041 2041 HOH HOH A . E 5 HOH 42 2042 2042 HOH HOH A . E 5 HOH 43 2043 2043 HOH HOH A . E 5 HOH 44 2044 2044 HOH HOH A . E 5 HOH 45 2045 2045 HOH HOH A . E 5 HOH 46 2046 2046 HOH HOH A . E 5 HOH 47 2047 2047 HOH HOH A . E 5 HOH 48 2048 2048 HOH HOH A . E 5 HOH 49 2049 2049 HOH HOH A . E 5 HOH 50 2050 2050 HOH HOH A . E 5 HOH 51 2051 2051 HOH HOH A . E 5 HOH 52 2052 2052 HOH HOH A . E 5 HOH 53 2053 2053 HOH HOH A . E 5 HOH 54 2054 2054 HOH HOH A . E 5 HOH 55 2055 2055 HOH HOH A . E 5 HOH 56 2056 2056 HOH HOH A . E 5 HOH 57 2057 2057 HOH HOH A . E 5 HOH 58 2058 2058 HOH HOH A . E 5 HOH 59 2059 2059 HOH HOH A . E 5 HOH 60 2060 2060 HOH HOH A . E 5 HOH 61 2061 2061 HOH HOH A . E 5 HOH 62 2062 2062 HOH HOH A . E 5 HOH 63 2063 2063 HOH HOH A . E 5 HOH 64 2064 2064 HOH HOH A . E 5 HOH 65 2065 2065 HOH HOH A . E 5 HOH 66 2066 2066 HOH HOH A . E 5 HOH 67 2067 2067 HOH HOH A . E 5 HOH 68 2068 2068 HOH HOH A . E 5 HOH 69 2069 2069 HOH HOH A . E 5 HOH 70 2070 2070 HOH HOH A . E 5 HOH 71 2071 2071 HOH HOH A . E 5 HOH 72 2072 2072 HOH HOH A . E 5 HOH 73 2073 2073 HOH HOH A . E 5 HOH 74 2074 2074 HOH HOH A . E 5 HOH 75 2075 2075 HOH HOH A . E 5 HOH 76 2076 2076 HOH HOH A . E 5 HOH 77 2077 2077 HOH HOH A . E 5 HOH 78 2078 2078 HOH HOH A . E 5 HOH 79 2079 2079 HOH HOH A . E 5 HOH 80 2080 2080 HOH HOH A . E 5 HOH 81 2081 2081 HOH HOH A . E 5 HOH 82 2082 2082 HOH HOH A . E 5 HOH 83 2083 2083 HOH HOH A . E 5 HOH 84 2084 2084 HOH HOH A . E 5 HOH 85 2085 2085 HOH HOH A . E 5 HOH 86 2086 2086 HOH HOH A . E 5 HOH 87 2087 2087 HOH HOH A . E 5 HOH 88 2088 2088 HOH HOH A . E 5 HOH 89 2089 2089 HOH HOH A . E 5 HOH 90 2090 2090 HOH HOH A . E 5 HOH 91 2091 2091 HOH HOH A . E 5 HOH 92 2092 2092 HOH HOH A . E 5 HOH 93 2093 2093 HOH HOH A . E 5 HOH 94 2094 2094 HOH HOH A . E 5 HOH 95 2095 2095 HOH HOH A . E 5 HOH 96 2096 2096 HOH HOH A . E 5 HOH 97 2097 2097 HOH HOH A . E 5 HOH 98 2098 2098 HOH HOH A . E 5 HOH 99 2099 2099 HOH HOH A . E 5 HOH 100 2100 2100 HOH HOH A . E 5 HOH 101 2101 2101 HOH HOH A . E 5 HOH 102 2102 2102 HOH HOH A . E 5 HOH 103 2103 2103 HOH HOH A . E 5 HOH 104 2104 2104 HOH HOH A . E 5 HOH 105 2105 2105 HOH HOH A . E 5 HOH 106 2106 2106 HOH HOH A . E 5 HOH 107 2107 2107 HOH HOH A . E 5 HOH 108 2108 2108 HOH HOH A . E 5 HOH 109 2109 2109 HOH HOH A . E 5 HOH 110 2110 2110 HOH HOH A . E 5 HOH 111 2111 2111 HOH HOH A . E 5 HOH 112 2112 2112 HOH HOH A . E 5 HOH 113 2113 2113 HOH HOH A . E 5 HOH 114 2114 2114 HOH HOH A . E 5 HOH 115 2115 2115 HOH HOH A . E 5 HOH 116 2116 2116 HOH HOH A . E 5 HOH 117 2117 2117 HOH HOH A . E 5 HOH 118 2118 2118 HOH HOH A . E 5 HOH 119 2119 2119 HOH HOH A . E 5 HOH 120 2120 2120 HOH HOH A . E 5 HOH 121 2121 2121 HOH HOH A . E 5 HOH 122 2122 2122 HOH HOH A . E 5 HOH 123 2123 2123 HOH HOH A . E 5 HOH 124 2124 2124 HOH HOH A . E 5 HOH 125 2125 2125 HOH HOH A . E 5 HOH 126 2126 2126 HOH HOH A . E 5 HOH 127 2127 2127 HOH HOH A . E 5 HOH 128 2128 2128 HOH HOH A . E 5 HOH 129 2129 2129 HOH HOH A . E 5 HOH 130 2130 2130 HOH HOH A . E 5 HOH 131 2131 2131 HOH HOH A . E 5 HOH 132 2132 2132 HOH HOH A . E 5 HOH 133 2133 2133 HOH HOH A . E 5 HOH 134 2134 2134 HOH HOH A . E 5 HOH 135 2135 2135 HOH HOH A . E 5 HOH 136 2136 2136 HOH HOH A . E 5 HOH 137 2137 2137 HOH HOH A . E 5 HOH 138 2138 2138 HOH HOH A . E 5 HOH 139 2139 2139 HOH HOH A . E 5 HOH 140 2140 2140 HOH HOH A . E 5 HOH 141 2141 2141 HOH HOH A . E 5 HOH 142 2142 2142 HOH HOH A . E 5 HOH 143 2143 2143 HOH HOH A . E 5 HOH 144 2144 2144 HOH HOH A . E 5 HOH 145 2145 2145 HOH HOH A . E 5 HOH 146 2146 2146 HOH HOH A . E 5 HOH 147 2147 2147 HOH HOH A . E 5 HOH 148 2148 2148 HOH HOH A . E 5 HOH 149 2149 2149 HOH HOH A . E 5 HOH 150 2150 2150 HOH HOH A . E 5 HOH 151 2151 2151 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 57 A ASN 88 ? ASN 'GLYCOSYLATION SITE' 2 A MLY 31 A MLY 62 ? LYS N-DIMETHYL-LYSINE 3 A MLY 41 A MLY 72 ? LYS N-DIMETHYL-LYSINE 4 A MLY 80 A MLY 111 ? LYS N-DIMETHYL-LYSINE 5 A MLY 99 A MLY 130 ? LYS N-DIMETHYL-LYSINE 6 A MLY 112 A MLY 143 ? LYS N-DIMETHYL-LYSINE 7 A MLY 135 A MLY 166 ? LYS N-DIMETHYL-LYSINE # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details dimeric _pdbx_struct_assembly.oligomeric_count 2 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1,2 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 6200 ? 1 MORE -59.0 ? 1 'SSA (A^2)' 19190 ? # 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' 2_455 -x-1,-y,z -1.0000000000 0.0000000000 0.0000000000 -50.9960000000 0.0000000000 -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 # loop_ _pdbx_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 O ? E HOH . ? A HOH 2151 ? 1_555 NA ? D NA . ? A NA 1215 ? 1_555 O ? E HOH . ? A HOH 2137 ? 1_555 99.3 ? 2 O ? E HOH . ? A HOH 2151 ? 1_555 NA ? D NA . ? A NA 1215 ? 1_555 O ? E HOH . ? A HOH 2138 ? 1_555 99.8 ? 3 O ? E HOH . ? A HOH 2137 ? 1_555 NA ? D NA . ? A NA 1215 ? 1_555 O ? E HOH . ? A HOH 2138 ? 1_555 122.5 ? 4 O ? E HOH . ? A HOH 2151 ? 1_555 NA ? D NA . ? A NA 1215 ? 1_555 O ? A CYS 155 ? A CYS 186 ? 1_555 161.2 ? 5 O ? E HOH . ? A HOH 2137 ? 1_555 NA ? D NA . ? A NA 1215 ? 1_555 O ? A CYS 155 ? A CYS 186 ? 1_555 75.0 ? 6 O ? E HOH . ? A HOH 2138 ? 1_555 NA ? D NA . ? A NA 1215 ? 1_555 O ? A CYS 155 ? A CYS 186 ? 1_555 69.9 ? 7 O ? E HOH . ? A HOH 2151 ? 1_555 NA ? D NA . ? A NA 1215 ? 1_555 O ? A GLY 159 ? A GLY 190 ? 1_555 98.0 ? 8 O ? E HOH . ? A HOH 2137 ? 1_555 NA ? D NA . ? A NA 1215 ? 1_555 O ? A GLY 159 ? A GLY 190 ? 1_555 161.5 ? 9 O ? E HOH . ? A HOH 2138 ? 1_555 NA ? D NA . ? A NA 1215 ? 1_555 O ? A GLY 159 ? A GLY 190 ? 1_555 60.4 ? 10 O ? A CYS 155 ? A CYS 186 ? 1_555 NA ? D NA . ? A NA 1215 ? 1_555 O ? A GLY 159 ? A GLY 190 ? 1_555 90.4 ? # 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 2011-07-13 2 'Structure model' 1 1 2011-08-17 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # _pdbx_audit_revision_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Database references' # _pdbx_refine_tls.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls.id 1 _pdbx_refine_tls.details ? _pdbx_refine_tls.method refined _pdbx_refine_tls.origin_x -7.1040 _pdbx_refine_tls.origin_y -13.2309 _pdbx_refine_tls.origin_z 14.8380 _pdbx_refine_tls.T[1][1] 0.0225 _pdbx_refine_tls.T[2][2] 0.0237 _pdbx_refine_tls.T[3][3] 0.0358 _pdbx_refine_tls.T[1][2] -0.0117 _pdbx_refine_tls.T[1][3] -0.0160 _pdbx_refine_tls.T[2][3] 0.0020 _pdbx_refine_tls.L[1][1] 0.9297 _pdbx_refine_tls.L[2][2] 0.5518 _pdbx_refine_tls.L[3][3] 1.0348 _pdbx_refine_tls.L[1][2] 0.4263 _pdbx_refine_tls.L[1][3] 0.0996 _pdbx_refine_tls.L[2][3] -0.0090 _pdbx_refine_tls.S[1][1] -0.0336 _pdbx_refine_tls.S[1][2] -0.0007 _pdbx_refine_tls.S[1][3] 0.1715 _pdbx_refine_tls.S[2][1] -0.0312 _pdbx_refine_tls.S[2][2] 0.0257 _pdbx_refine_tls.S[2][3] 0.0797 _pdbx_refine_tls.S[3][1] -0.0979 _pdbx_refine_tls.S[3][2] -0.0863 _pdbx_refine_tls.S[3][3] 0.0012 # _pdbx_refine_tls_group.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls_group.id 1 _pdbx_refine_tls_group.refine_tls_id 1 _pdbx_refine_tls_group.beg_auth_asym_id ? _pdbx_refine_tls_group.beg_auth_seq_id ? _pdbx_refine_tls_group.beg_label_asym_id ? _pdbx_refine_tls_group.beg_label_seq_id ? _pdbx_refine_tls_group.end_auth_asym_id ? _pdbx_refine_tls_group.end_auth_seq_id ? _pdbx_refine_tls_group.end_label_asym_id ? _pdbx_refine_tls_group.end_label_seq_id ? _pdbx_refine_tls_group.selection ? _pdbx_refine_tls_group.selection_details ALL # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal PHENIX refinement '(PHENIX.REFINE)' ? 1 DENZO 'data reduction' . ? 2 SCALEPACK 'data scaling' . ? 3 PHASER phasing . ? 4 # _pdbx_entry_details.entry_id 2YGO _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ? _pdbx_entry_details.sequence_details ;ISOFORM Q166K. THE N-TERMINAL THREE AMINO ACID RESIDUES (ETG) AND C-TERMINAL NINE AMINO ACID RESIDUES (GTKHHHHHH) OF THE CRYSTALLISATION CONSTRUCT ARE DERIVED FROM THE PHLSEC VECTOR. ; # _pdbx_validate_close_contact.id 1 _pdbx_validate_close_contact.PDB_model_num 1 _pdbx_validate_close_contact.auth_atom_id_1 ND2 _pdbx_validate_close_contact.auth_asym_id_1 A _pdbx_validate_close_contact.auth_comp_id_1 ASN _pdbx_validate_close_contact.auth_seq_id_1 88 _pdbx_validate_close_contact.PDB_ins_code_1 ? _pdbx_validate_close_contact.label_alt_id_1 ? _pdbx_validate_close_contact.auth_atom_id_2 O5 _pdbx_validate_close_contact.auth_asym_id_2 A _pdbx_validate_close_contact.auth_comp_id_2 NAG _pdbx_validate_close_contact.auth_seq_id_2 1214 _pdbx_validate_close_contact.PDB_ins_code_2 ? _pdbx_validate_close_contact.label_alt_id_2 ? _pdbx_validate_close_contact.dist 2.15 # _pdbx_validate_torsion.id 1 _pdbx_validate_torsion.PDB_model_num 1 _pdbx_validate_torsion.auth_comp_id PRO _pdbx_validate_torsion.auth_asym_id A _pdbx_validate_torsion.auth_seq_id 201 _pdbx_validate_torsion.PDB_ins_code ? _pdbx_validate_torsion.label_alt_id ? _pdbx_validate_torsion.phi -80.72 _pdbx_validate_torsion.psi -159.67 # _pdbx_distant_solvent_atoms.id 1 _pdbx_distant_solvent_atoms.PDB_model_num 1 _pdbx_distant_solvent_atoms.auth_atom_id O _pdbx_distant_solvent_atoms.label_alt_id ? _pdbx_distant_solvent_atoms.auth_asym_id A _pdbx_distant_solvent_atoms.auth_comp_id HOH _pdbx_distant_solvent_atoms.auth_seq_id 2017 _pdbx_distant_solvent_atoms.PDB_ins_code ? _pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 5.88 _pdbx_distant_solvent_atoms.neighbor_ligand_distance . # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A GLU 32 ? A GLU 1 2 1 Y 1 A LYS 213 ? A LYS 182 3 1 Y 1 A HIS 214 ? A HIS 183 4 1 Y 1 A HIS 215 ? A HIS 184 5 1 Y 1 A HIS 216 ? A HIS 185 6 1 Y 1 A HIS 217 ? A HIS 186 7 1 Y 1 A HIS 218 ? A HIS 187 8 1 Y 1 A HIS 219 ? A HIS 188 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE PCF 3 N-ACETYL-D-GLUCOSAMINE NAG 4 'SODIUM ION' NA 5 water HOH #