data_1H1B # _entry.id 1H1B # _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 1H1B PDBE EBI-9885 WWPDB D_1290009885 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 1B0F unspecified 'CRYSTAL STRUCTURE OF HUMAN NEUTROPHIL ELASTASE WITH MDL 101, 146' PDB 1HNE unspecified ;HUMAN NEUTROPHIL ELASTASE (HNE) (ALSO REFERRED TO AS HUMAN LEUCOCYTE ELASTASE (HLE)) COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-ALA CHLOROMETHYL KETONE (MSACK) ; PDB 1PPF unspecified 'HUMAN LEUKOCYTE ELASTASE (HLE) (NEUTROPHIL ELASTASE (HNE)) COMPLEX WITH THE THIRD DOMAIN OF TURKEY OVOMUCOID INHIBITOR (OMTKY3)' PDB 1PPG unspecified 'HUMAN LEUKOCYTE ELASTASE (HLE) COMPLEX WITH MEO-SUCCINYL-ALA-ALA-PRO-VAL CHLOROMETHYLACETONE' # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 1H1B _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2002-07-05 _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 'Macdonald, S.J.F.' 1 'Dowle, M.D.' 2 'Harrison, L.A.' 3 'Clarke, G.D.E.' 4 'Inglis, G.G.A.' 5 'Johnson, M.R.' 6 'Smith, R.A.' 7 'Amour, A.' 8 'Fleetwood, G.' 9 'Humphreys, D.C.' 10 'Molloy, C.R.' 11 'Dixon, M.' 12 'Godward, R.E.' 13 'Wonacott, A.J.' 14 'Singh, O.M.P.' 15 'Hodgson, S.T.' 16 'Hardy, G.W.' 17 # _citation.id primary _citation.title ;Discovery of Further Pyrrolidine Trans-Lactams as Inhibitors of Human Neutrophil Elastase (Hne) with Potential as Development Candidates and the Crystal Structure of Hne Complexed with an Inhibitor (Gw475151) ; _citation.journal_abbrev J.Med.Chem. _citation.journal_volume 45 _citation.page_first 3878 _citation.page_last ? _citation.year 2002 _citation.journal_id_ASTM JMCMAR _citation.country US _citation.journal_id_ISSN 0022-2623 _citation.journal_id_CSD 0151 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 12190311 _citation.pdbx_database_id_DOI 10.1021/JM020881F # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Macdonald, S.J.F.' 1 primary 'Dowle, M.D.' 2 primary 'Harrison, L.A.' 3 primary 'Clarke, G.D.E.' 4 primary 'Inglis, G.G.A.' 5 primary 'Johnson, M.R.' 6 primary 'Shah, P.' 7 primary 'Smith, R.A.' 8 primary 'Amour, A.' 9 primary 'Fleetwood, G.' 10 primary 'Humphreys, D.C.' 11 primary 'Molloy, C.R.' 12 primary 'Dixon, M.' 13 primary 'Godward, R.E.' 14 primary 'Wonacott, A.J.' 15 primary 'Singh, O.M.P.' 16 primary 'Hodgson, S.T.' 17 primary 'Hardy, G.W.' 18 # _cell.entry_id 1H1B _cell.length_a 68.880 _cell.length_b 68.880 _cell.length_c 241.150 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 16 _cell.pdbx_unique_axis ? # _symmetry.entry_id 1H1B _symmetry.space_group_name_H-M 'P 43 2 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 95 # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer nat 'LEUKOCYTE ELASTASE' 23318.982 2 3.4.21.37 ? ? ? 2 non-polymer syn ;(2S)-3-METHYL-2-((2R,3S)-3-[(METHYLSULFONYL)AMINO]-1-{[2-(PYRROLIDIN-1-YLMETHYL)-1,3-OXAZOL-4-YL]CARBONYL}PYRROLIDIN-2-YL)BUTANOIC ACID ; 442.530 2 ? ? ? ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 4 ? ? ? ? 4 non-polymer man ALPHA-L-FUCOSE 164.156 4 ? ? ? ? 5 water nat water 18.015 244 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'ELASTASE, NEUTROPHIL ELASTASE, PMN ELASTASE, BONE MARROW SERINE PROTEASE, MEDULLASIN' # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer no _entity_poly.pdbx_seq_one_letter_code ;IVGGRRARPHAWPFMVSLQLRGGHFCGATLIAPNFVMSAAHCVANVNVRAVRVVLGAHNLSRREPTRQVFAVQRIFENGY DPVNLLNDIVILQLNGSATINANVQVAQLPAQGRRLGNGVQCLAMGWGLLGRNRGIASVLQELNVTVVTSLCRRSNVCTL VRGRQAGVCFGDSGSPLVCNGLIHGIASFVRGGCASGLYPDAFAPVAQFVNWIDSIIQ ; _entity_poly.pdbx_seq_one_letter_code_can ;IVGGRRARPHAWPFMVSLQLRGGHFCGATLIAPNFVMSAAHCVANVNVRAVRVVLGAHNLSRREPTRQVFAVQRIFENGY DPVNLLNDIVILQLNGSATINANVQVAQLPAQGRRLGNGVQCLAMGWGLLGRNRGIASVLQELNVTVVTSLCRRSNVCTL VRGRQAGVCFGDSGSPLVCNGLIHGIASFVRGGCASGLYPDAFAPVAQFVNWIDSIIQ ; _entity_poly.pdbx_strand_id A,B _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 ILE n 1 2 VAL n 1 3 GLY n 1 4 GLY n 1 5 ARG n 1 6 ARG n 1 7 ALA n 1 8 ARG n 1 9 PRO n 1 10 HIS n 1 11 ALA n 1 12 TRP n 1 13 PRO n 1 14 PHE n 1 15 MET n 1 16 VAL n 1 17 SER n 1 18 LEU n 1 19 GLN n 1 20 LEU n 1 21 ARG n 1 22 GLY n 1 23 GLY n 1 24 HIS n 1 25 PHE n 1 26 CYS n 1 27 GLY n 1 28 ALA n 1 29 THR n 1 30 LEU n 1 31 ILE n 1 32 ALA n 1 33 PRO n 1 34 ASN n 1 35 PHE n 1 36 VAL n 1 37 MET n 1 38 SER n 1 39 ALA n 1 40 ALA n 1 41 HIS n 1 42 CYS n 1 43 VAL n 1 44 ALA n 1 45 ASN n 1 46 VAL n 1 47 ASN n 1 48 VAL n 1 49 ARG n 1 50 ALA n 1 51 VAL n 1 52 ARG n 1 53 VAL n 1 54 VAL n 1 55 LEU n 1 56 GLY n 1 57 ALA n 1 58 HIS n 1 59 ASN n 1 60 LEU n 1 61 SER n 1 62 ARG n 1 63 ARG n 1 64 GLU n 1 65 PRO n 1 66 THR n 1 67 ARG n 1 68 GLN n 1 69 VAL n 1 70 PHE n 1 71 ALA n 1 72 VAL n 1 73 GLN n 1 74 ARG n 1 75 ILE n 1 76 PHE n 1 77 GLU n 1 78 ASN n 1 79 GLY n 1 80 TYR n 1 81 ASP n 1 82 PRO n 1 83 VAL n 1 84 ASN n 1 85 LEU n 1 86 LEU n 1 87 ASN n 1 88 ASP n 1 89 ILE n 1 90 VAL n 1 91 ILE n 1 92 LEU n 1 93 GLN n 1 94 LEU n 1 95 ASN n 1 96 GLY n 1 97 SER n 1 98 ALA n 1 99 THR n 1 100 ILE n 1 101 ASN n 1 102 ALA n 1 103 ASN n 1 104 VAL n 1 105 GLN n 1 106 VAL n 1 107 ALA n 1 108 GLN n 1 109 LEU n 1 110 PRO n 1 111 ALA n 1 112 GLN n 1 113 GLY n 1 114 ARG n 1 115 ARG n 1 116 LEU n 1 117 GLY n 1 118 ASN n 1 119 GLY n 1 120 VAL n 1 121 GLN n 1 122 CYS n 1 123 LEU n 1 124 ALA n 1 125 MET n 1 126 GLY n 1 127 TRP n 1 128 GLY n 1 129 LEU n 1 130 LEU n 1 131 GLY n 1 132 ARG n 1 133 ASN n 1 134 ARG n 1 135 GLY n 1 136 ILE n 1 137 ALA n 1 138 SER n 1 139 VAL n 1 140 LEU n 1 141 GLN n 1 142 GLU n 1 143 LEU n 1 144 ASN n 1 145 VAL n 1 146 THR n 1 147 VAL n 1 148 VAL n 1 149 THR n 1 150 SER n 1 151 LEU n 1 152 CYS n 1 153 ARG n 1 154 ARG n 1 155 SER n 1 156 ASN n 1 157 VAL n 1 158 CYS n 1 159 THR n 1 160 LEU n 1 161 VAL n 1 162 ARG n 1 163 GLY n 1 164 ARG n 1 165 GLN n 1 166 ALA n 1 167 GLY n 1 168 VAL n 1 169 CYS n 1 170 PHE n 1 171 GLY n 1 172 ASP n 1 173 SER n 1 174 GLY n 1 175 SER n 1 176 PRO n 1 177 LEU n 1 178 VAL n 1 179 CYS n 1 180 ASN n 1 181 GLY n 1 182 LEU n 1 183 ILE n 1 184 HIS n 1 185 GLY n 1 186 ILE n 1 187 ALA n 1 188 SER n 1 189 PHE n 1 190 VAL n 1 191 ARG n 1 192 GLY n 1 193 GLY n 1 194 CYS n 1 195 ALA n 1 196 SER n 1 197 GLY n 1 198 LEU n 1 199 TYR n 1 200 PRO n 1 201 ASP n 1 202 ALA n 1 203 PHE n 1 204 ALA n 1 205 PRO n 1 206 VAL n 1 207 ALA n 1 208 GLN n 1 209 PHE n 1 210 VAL n 1 211 ASN n 1 212 TRP n 1 213 ILE n 1 214 ASP n 1 215 SER n 1 216 ILE n 1 217 ILE n 1 218 GLN n # _entity_src_nat.entity_id 1 _entity_src_nat.pdbx_src_id 1 _entity_src_nat.pdbx_alt_source_flag sample _entity_src_nat.pdbx_beg_seq_num ? _entity_src_nat.pdbx_end_seq_num ? _entity_src_nat.common_name HUMAN _entity_src_nat.pdbx_organism_scientific 'HOMO SAPIENS' _entity_src_nat.pdbx_ncbi_taxonomy_id 9606 _entity_src_nat.genus ? _entity_src_nat.species ? _entity_src_nat.strain ? _entity_src_nat.tissue ? _entity_src_nat.tissue_fraction ? _entity_src_nat.pdbx_secretion ? _entity_src_nat.pdbx_fragment ? _entity_src_nat.pdbx_variant ? _entity_src_nat.pdbx_cell_line ? _entity_src_nat.pdbx_atcc ? _entity_src_nat.pdbx_cellular_location ? _entity_src_nat.pdbx_organ ? _entity_src_nat.pdbx_organelle ? _entity_src_nat.pdbx_cell LEUKOCYTE _entity_src_nat.pdbx_plasmid_name ? _entity_src_nat.pdbx_plasmid_details ? _entity_src_nat.details ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code ELNE_HUMAN _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_align_begin ? _struct_ref.pdbx_db_accession P08246 _struct_ref.pdbx_db_isoform ? # loop_ _struct_ref_seq.align_id _struct_ref_seq.ref_id _struct_ref_seq.pdbx_PDB_id_code _struct_ref_seq.pdbx_strand_id _struct_ref_seq.seq_align_beg _struct_ref_seq.pdbx_seq_align_beg_ins_code _struct_ref_seq.seq_align_end _struct_ref_seq.pdbx_seq_align_end_ins_code _struct_ref_seq.pdbx_db_accession _struct_ref_seq.db_align_beg _struct_ref_seq.pdbx_db_align_beg_ins_code _struct_ref_seq.db_align_end _struct_ref_seq.pdbx_db_align_end_ins_code _struct_ref_seq.pdbx_auth_seq_align_beg _struct_ref_seq.pdbx_auth_seq_align_end 1 1 1H1B A 1 ? 21 ? P08246 30 ? 50 ? 16 36 2 1 1H1B A 22 ? 79 ? P08246 51 ? 108 ? 38 92 3 1 1H1B A 80 ? 81 ? P08246 109 ? 110 ? 94 95 4 1 1H1B A 82 ? 131 ? P08246 111 ? 160 ? 98 145 5 1 1H1B A 132 ? 145 ? P08246 161 ? 174 ? 147 160 6 1 1H1B A 146 ? 152 ? P08246 175 ? 183 ? 162 168 7 1 1H1B A 153 ? 179 ? P08246 184 ? 200 ? 177 201 8 1 1H1B A 180 ? 181 ? P08246 201 ? 202 ? 204 205 9 1 1H1B A 182 ? 218 ? P08246 203 ? 247 ? 208 243 10 1 1H1B B 1 ? 21 ? P08246 30 ? 50 ? 16 36 11 1 1H1B B 22 ? 79 ? P08246 51 ? 108 ? 38 92 12 1 1H1B B 80 ? 81 ? P08246 109 ? 110 ? 94 95 13 1 1H1B B 82 ? 131 ? P08246 111 ? 160 ? 98 145 14 1 1H1B B 132 ? 145 ? P08246 161 ? 174 ? 147 160 15 1 1H1B B 146 ? 152 ? P08246 175 ? 183 ? 162 168 16 1 1H1B B 153 ? 179 ? P08246 184 ? 200 ? 177 201 17 1 1H1B B 180 ? 181 ? P08246 201 ? 202 ? 204 205 18 1 1H1B B 182 ? 218 ? P08246 203 ? 247 ? 208 243 # 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 151 non-polymer . ;(2S)-3-METHYL-2-((2R,3S)-3-[(METHYLSULFONYL)AMINO]-1-{[2-(PYRROLIDIN-1-YLMETHYL)-1,3-OXAZOL-4-YL]CARBONYL}PYRROLIDIN-2-YL)BUTANOIC ACID ; ? 'C19 H30 N4 O6 S' 442.530 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 FUC saccharide . ALPHA-L-FUCOSE ? 'C6 H12 O5' 164.156 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 1H1B _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.07 _exptl_crystal.density_percent_sol 59.89 _exptl_crystal.description ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 4.00 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details ;HNE/GW475151 COMPLEX 10MG/ML IN 10MM NA CITRATE PH 5.0. HANGING DROPS OF EQUAL VOLUMES OF PROTEIN AND PRECIPITANT. PRECIPITANT 1.1-1.2M AMMONIUM SULPHATE, 100MM CITRATE PH 3.8-4.0, ROOM TEMP. ; # _diffrn.id 1 _diffrn.ambient_temp 100.0 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'ADSC CCD' _diffrn_detector.pdbx_collection_date 1999-10-15 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.87 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'SRS BEAMLINE PX9.6' _diffrn_source.pdbx_synchrotron_site SRS _diffrn_source.pdbx_synchrotron_beamline PX9.6 _diffrn_source.pdbx_wavelength 0.87 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 1H1B _reflns.observed_criterion_sigma_I ? _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 20.000 _reflns.d_resolution_high 2.000 _reflns.number_obs 38930 _reflns.number_all ? _reflns.percent_possible_obs 96.1 _reflns.pdbx_Rmerge_I_obs 0.08800 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 11.7000 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 6.400 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 2.00 _reflns_shell.d_res_low 2.10 _reflns_shell.percent_possible_all 83.0 _reflns_shell.Rmerge_I_obs 0.52000 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 2.200 _reflns_shell.pdbx_redundancy ? # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 1H1B _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 36959 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 20.0 _refine.ls_d_res_high 2.00 _refine.ls_percent_reflns_obs 96 _refine.ls_R_factor_obs 0.254 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.251 _refine.ls_R_factor_R_free 0.310 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.0 _refine.ls_number_reflns_R_free 1948 _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 41.4 _refine.aniso_B[1][1] -0.33 _refine.aniso_B[2][2] -0.33 _refine.aniso_B[3][3] 0.67 _refine.aniso_B[1][2] 0.0 _refine.aniso_B[1][3] 0.0 _refine.aniso_B[2][3] 0.0 _refine.solvent_model_details ? _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.pdbx_ls_cross_valid_method ? _refine.details ? _refine.pdbx_starting_model 'PDB ENTRY 1HNE' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ? _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.21 _refine.pdbx_overall_ESU_R_Free 0.199 _refine.overall_SU_ML 0.179 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 6.5 _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 3272 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 154 _refine_hist.number_atoms_solvent 244 _refine_hist.number_atoms_total 3670 _refine_hist.d_res_high 2.00 _refine_hist.d_res_low 20.0 # _struct_ncs_oper.id 1 _struct_ncs_oper.code given _struct_ncs_oper.details ? _struct_ncs_oper.matrix[1][1] -0.994520 _struct_ncs_oper.matrix[1][2] 0.003930 _struct_ncs_oper.matrix[1][3] -0.104440 _struct_ncs_oper.matrix[2][1] -0.004230 _struct_ncs_oper.matrix[2][2] -0.999990 _struct_ncs_oper.matrix[2][3] 0.002680 _struct_ncs_oper.matrix[3][1] -0.104430 _struct_ncs_oper.matrix[3][2] 0.003110 _struct_ncs_oper.matrix[3][3] 0.994530 _struct_ncs_oper.vector[1] 39.03800 _struct_ncs_oper.vector[2] -8.04100 _struct_ncs_oper.vector[3] 2.09500 # _struct.entry_id 1H1B _struct.title 'Crystal structure of human neutrophil elastase complexed with an inhibitor (GW475151)' _struct.pdbx_descriptor 'LEUKOCYTE ELASTASE (E.C.3.4.21.37)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 1H1B _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'HYDROLASE, SERINE PROTEASE' # 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 1 ? C N N 2 ? D N N 3 ? E N N 4 ? F N N 3 ? G N N 4 ? H N N 2 ? I N N 3 ? J N N 4 ? K N N 3 ? L N N 4 ? M N N 5 ? N 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 ALA A 39 ? ASN A 45 ? ALA A 55 ASN A 61 1 ? 7 HELX_P HELX_P2 2 ASN A 47 A ARG A 49 ? ASN A 62 ARG A 63 5 ? 3 HELX_P HELX_P3 3 PHE A 209 ? GLN A 218 ? PHE A 234 GLN A 243 1 ? 10 HELX_P HELX_P4 4 ALA B 39 ? ALA B 44 ? ALA B 55 ALA B 60 1 ? 6 HELX_P HELX_P5 5 ASN B 47 A ALA B 50 ? ASN B 62 ALA B 64 5 ? 4 HELX_P HELX_P6 6 PHE B 209 ? GLN B 218 ? PHE B 234 GLN B 243 1 ? 10 # _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 26 SG ? ? ? 1_555 A CYS 42 SG ? ? A CYS 42 A CYS 58 1_555 ? ? ? ? ? ? ? 2.049 ? disulf2 disulf ? ? A CYS 122 SG ? ? ? 1_555 A CYS 179 SG ? ? A CYS 136 A CYS 201 1_555 ? ? ? ? ? ? ? 2.042 ? disulf3 disulf ? ? A CYS 152 SG ? ? ? 1_555 A CYS 158 SG ? ? A CYS 168 A CYS 182 1_555 ? ? ? ? ? ? ? 2.070 ? disulf4 disulf ? ? A CYS 169 SG ? ? ? 1_555 A CYS 194 SG ? ? A CYS 191 A CYS 220 1_555 ? ? ? ? ? ? ? 1.972 ? disulf5 disulf ? ? B CYS 26 SG ? ? ? 1_555 B CYS 42 SG ? ? B CYS 42 B CYS 58 1_555 ? ? ? ? ? ? ? 2.035 ? disulf6 disulf ? ? B CYS 122 SG ? ? ? 1_555 B CYS 179 SG ? ? B CYS 136 B CYS 201 1_555 ? ? ? ? ? ? ? 2.035 ? disulf7 disulf ? ? B CYS 152 SG ? ? ? 1_555 B CYS 158 SG ? ? B CYS 168 B CYS 182 1_555 ? ? ? ? ? ? ? 2.034 ? disulf8 disulf ? ? B CYS 169 SG ? ? ? 1_555 B CYS 194 SG ? ? B CYS 191 B CYS 220 1_555 ? ? ? ? ? ? ? 1.954 ? covale1 covale ? ? A ASN 95 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 109 A NAG 411 1_555 ? ? ? ? ? ? ? 1.456 ? covale2 covale ? ? A ASN 144 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 159 A NAG 401 1_555 ? ? ? ? ? ? ? 1.416 ? covale3 covale ? ? A SER 173 OG ? ? ? 1_555 C 151 . C30 ? ? A SER 195 A 151 400 1_555 ? ? ? ? ? ? ? 1.540 ? covale4 covale ? ? D NAG . O6 ? ? ? 1_555 E FUC . C1 ? ? A NAG 401 A FUC 402 1_555 ? ? ? ? ? ? ? 1.438 ? covale5 covale ? ? F NAG . O6 ? ? ? 1_555 G FUC . C1 ? ? A NAG 411 A FUC 412 1_555 ? ? ? ? ? ? ? 1.441 ? covale6 covale ? ? B ASN 95 ND2 ? ? ? 1_555 K NAG . C1 ? ? B ASN 109 B NAG 411 1_555 ? ? ? ? ? ? ? 1.474 ? covale7 covale ? ? B ASN 144 ND2 ? ? ? 1_555 I NAG . C1 ? ? B ASN 159 B NAG 401 1_555 ? ? ? ? ? ? ? 1.454 ? covale8 covale ? ? B SER 173 OG ? ? ? 1_555 H 151 . C30 ? ? B SER 195 B 151 400 1_555 ? ? ? ? ? ? ? 1.386 ? covale9 covale ? ? B SER 173 OG ? ? ? 1_555 H 151 . O5 ? ? B SER 195 B 151 400 1_555 ? ? ? ? ? ? ? 2.027 ? covale10 covale ? ? I NAG . O6 ? ? ? 1_555 J FUC . C1 ? ? B NAG 401 B FUC 402 1_555 ? ? ? ? ? ? ? 1.456 ? covale11 covale ? ? K NAG . O6 ? ? ? 1_555 L FUC . C1 ? ? B NAG 411 B FUC 412 1_555 ? ? ? ? ? ? ? 1.426 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA ? 9 ? AB ? 15 ? BA ? 16 ? # 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 AA 6 7 ? anti-parallel AA 7 8 ? parallel AA 8 9 ? anti-parallel AB 1 2 ? anti-parallel AB 2 3 ? anti-parallel AB 3 4 ? anti-parallel AB 4 5 ? anti-parallel AB 5 6 ? anti-parallel AB 6 7 ? anti-parallel AB 7 8 ? anti-parallel AB 8 9 ? anti-parallel AB 9 10 ? anti-parallel AB 10 11 ? anti-parallel AB 11 12 ? parallel AB 12 13 ? anti-parallel AB 13 14 ? anti-parallel BA 1 2 ? anti-parallel BA 2 3 ? anti-parallel BA 3 4 ? anti-parallel BA 5 6 ? parallel BA 7 8 ? anti-parallel BA 9 10 ? anti-parallel BA 11 12 ? anti-parallel BA 13 14 ? anti-parallel BA 15 16 ? 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 ARG A 5 ? ARG A 6 ? ARG A 20 ARG A 21 AA 2 GLN A 141 ? VAL A 147 ? GLN A 156 VAL A 163 AA 3 VAL A 157 ? LEU A 160 ? VAL A 181 LEU A 184 AA 4 ASP A 201 ? PRO A 205 ? ASP A 226 PRO A 230 AA 5 LEU A 182 ? PHE A 189 ? LEU A 208 PHE A 215 AA 6 PRO A 176 ? CYS A 179 ? PRO A 198 CYS A 201 AA 7 GLN A 121 ? GLY A 126 ? GLN A 135 GLY A 140 AA 8 GLN A 141 ? VAL A 147 ? GLN A 156 VAL A 163 AA 9 ARG A 5 ? ARG A 6 ? ARG A 20 ARG A 21 AB 1 MET A 15 ? LEU A 20 ? MET A 30 LEU A 35 AB 2 GLY A 23 ? ALA A 32 ? GLY A 39 ALA A 48 AB 3 PHE A 35 ? SER A 38 ? PHE A 51 SER A 54 AB 4 VAL A 90 ? LEU A 94 ? VAL A 104 LEU A 108 AB 5 VAL A 72 ? TYR A 80 ? VAL A 85 TYR A 94 AB 6 GLN B 68 ? TYR B 80 ? GLN B 81 TYR B 94 AB 7 VAL B 90 ? LEU B 94 ? VAL B 104 LEU B 108 AB 8 PHE B 35 ? SER B 38 ? PHE B 51 SER B 54 AB 9 GLY B 23 ? ALA B 32 ? GLY B 39 ALA B 48 AB 10 MET B 15 ? LEU B 20 ? MET B 30 LEU B 35 AB 11 ARG B 52 A LEU B 55 ? ARG B 65 LEU B 68 AB 12 GLN B 68 ? TYR B 80 ? GLN B 81 TYR B 94 AB 13 VAL A 72 ? TYR A 80 ? VAL A 85 TYR A 94 AB 14 VAL A 90 ? LEU A 94 ? VAL A 104 LEU A 108 AB 15 MET A 15 ? LEU A 20 ? MET A 30 LEU A 35 BA 1 ARG B 5 ? ARG B 6 ? ARG B 20 ARG B 21 BA 2 GLN B 141 ? VAL B 148 ? GLN B 156 VAL B 164 BA 3 VAL B 157 ? LEU B 160 ? VAL B 181 LEU B 184 BA 4 ASP B 201 ? PRO B 205 ? ASP B 226 PRO B 230 BA 5 GLN B 121 ? GLY B 126 ? GLN B 135 GLY B 140 BA 6 GLN B 141 ? VAL B 148 ? GLN B 156 VAL B 164 BA 7 GLN B 141 ? VAL B 148 ? GLN B 156 VAL B 164 BA 8 ARG B 5 ? ARG B 6 ? ARG B 20 ARG B 21 BA 9 VAL B 157 ? LEU B 160 ? VAL B 181 LEU B 184 BA 10 GLN B 141 ? VAL B 148 ? GLN B 156 VAL B 164 BA 11 PRO B 176 ? CYS B 179 ? PRO B 198 CYS B 201 BA 12 GLN B 121 ? GLY B 126 ? GLN B 135 GLY B 140 BA 13 LEU B 182 ? PHE B 189 ? LEU B 208 PHE B 215 BA 14 PRO B 176 ? CYS B 179 ? PRO B 198 CYS B 201 BA 15 ASP B 201 ? PRO B 205 ? ASP B 226 PRO B 230 BA 16 VAL B 157 ? LEU B 160 ? VAL B 181 LEU B 184 # 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 ARG A 5 ? N ARG A 20 O GLU A 142 ? O GLU A 157 AA 2 3 N THR A 146 ? N THR A 162 O LEU A 160 ? O LEU A 184 AA 3 4 N THR A 159 ? N THR A 183 O ASP A 201 ? O ASP A 226 AA 4 5 N ALA A 204 ? N ALA A 229 O ILE A 186 ? O ILE A 212 AA 5 6 N HIS A 184 ? N HIS A 210 O LEU A 177 ? O LEU A 199 AA 6 7 N VAL A 178 ? N VAL A 200 O LEU A 123 ? O LEU A 137 AA 7 8 N GLY A 126 ? N GLY A 140 O GLN A 141 ? O GLN A 156 AA 8 9 N GLU A 142 ? N GLU A 157 O ARG A 5 ? O ARG A 20 AB 1 2 N LEU A 20 ? N LEU A 35 O GLY A 23 ? O GLY A 39 AB 2 3 N ILE A 31 ? N ILE A 47 O PHE A 35 ? O PHE A 51 AB 3 4 N SER A 38 ? N SER A 54 O VAL A 90 ? O VAL A 104 AB 4 5 O GLN A 93 ? O GLN A 107 N GLN A 73 ? N GLN A 86 AB 5 6 N TYR A 80 ? N TYR A 94 O ILE B 75 ? O ILE B 88 AB 6 7 N PHE B 76 ? N PHE B 89 O ILE B 91 ? O ILE B 105 AB 7 8 N LEU B 92 ? N LEU B 106 O VAL B 36 ? O VAL B 52 AB 8 9 N MET B 37 ? N MET B 53 O THR B 29 ? O THR B 45 AB 9 10 N ALA B 28 ? N ALA B 44 O VAL B 16 ? O VAL B 31 AB 10 11 N GLN B 19 ? N GLN B 34 O ARG B 52 A O ARG B 65 AB 11 12 N LEU B 55 ? N LEU B 68 O GLN B 68 ? O GLN B 81 AB 12 13 N GLY B 79 ? N GLY B 92 O ILE A 75 ? O ILE A 88 AB 13 14 N PHE A 76 ? N PHE A 89 O ILE A 91 ? O ILE A 105 BA 1 2 N ARG B 5 ? N ARG B 20 O GLU B 142 ? O GLU B 157 BA 2 3 N VAL B 148 ? N VAL B 164 O CYS B 158 ? O CYS B 182 BA 3 4 N THR B 159 ? N THR B 183 O ASP B 201 ? O ASP B 226 BA 5 6 N GLY B 126 ? N GLY B 140 O GLN B 141 ? O GLN B 156 BA 7 8 N GLU B 142 ? N GLU B 157 O ARG B 5 ? O ARG B 20 BA 9 10 N LEU B 160 ? N LEU B 184 O THR B 146 ? O THR B 162 BA 11 12 N VAL B 178 ? N VAL B 200 O LEU B 123 ? O LEU B 137 BA 13 14 N HIS B 184 ? N HIS B 210 O LEU B 177 ? O LEU B 199 BA 15 16 N PHE B 203 ? N PHE B 228 O VAL B 157 ? O VAL B 181 # 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 ? ? ? ? 16 'BINDING SITE FOR RESIDUE 151 A 400' AC2 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE 151 B 400' AC3 Software ? ? ? ? 5 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 109 RESIDUES 411 TO 412' AC4 Software ? ? ? ? 6 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 159 RESIDUES 401 TO 402' AC5 Software ? ? ? ? 4 'BINDING SITE FOR CHAIN B OF SUGAR BOUND TO ASN B 109 RESIDUES 411 TO 412' AC6 Software ? ? ? ? 8 'BINDING SITE FOR CHAIN B OF SUGAR BOUND TO ASN B 159 RESIDUES 401 TO 402' # 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 16 HIS A 41 ? HIS A 57 . ? 1_555 ? 2 AC1 16 LEU A 85 B LEU A 99 . ? 1_555 ? 3 AC1 16 ARG A 132 ? ARG A 147 . ? 7_555 ? 4 AC1 16 ASN A 133 ? ASN A 148 . ? 7_555 ? 5 AC1 16 ARG A 134 ? ARG A 149 . ? 7_555 ? 6 AC1 16 CYS A 169 ? CYS A 191 . ? 1_555 ? 7 AC1 16 PHE A 170 ? PHE A 192 . ? 1_555 ? 8 AC1 16 GLY A 171 ? GLY A 193 . ? 1_555 ? 9 AC1 16 SER A 173 ? SER A 195 . ? 1_555 ? 10 AC1 16 SER A 188 ? SER A 214 . ? 1_555 ? 11 AC1 16 PHE A 189 ? PHE A 215 . ? 1_555 ? 12 AC1 16 VAL A 190 ? VAL A 216 . ? 1_555 ? 13 AC1 16 HOH M . ? HOH A 2015 . ? 1_555 ? 14 AC1 16 HOH M . ? HOH A 2106 . ? 1_555 ? 15 AC1 16 HOH M . ? HOH A 2134 . ? 1_555 ? 16 AC1 16 HOH M . ? HOH A 2136 . ? 1_555 ? 17 AC2 9 LEU B 85 B LEU B 99 . ? 1_555 ? 18 AC2 9 CYS B 169 ? CYS B 191 . ? 1_555 ? 19 AC2 9 PHE B 170 ? PHE B 192 . ? 1_555 ? 20 AC2 9 GLY B 171 ? GLY B 193 . ? 1_555 ? 21 AC2 9 SER B 173 ? SER B 195 . ? 1_555 ? 22 AC2 9 SER B 188 ? SER B 214 . ? 1_555 ? 23 AC2 9 PHE B 189 ? PHE B 215 . ? 1_555 ? 24 AC2 9 VAL B 190 ? VAL B 216 . ? 1_555 ? 25 AC2 9 HOH N . ? HOH B 2105 . ? 1_555 ? 26 AC3 5 ARG A 49 ? ARG A 63 . ? 1_555 ? 27 AC3 5 VAL A 51 ? VAL A 65 . ? 1_555 ? 28 AC3 5 ARG A 52 A ARG A 65 . ? 1_555 ? 29 AC3 5 ASN A 95 ? ASN A 109 . ? 1_555 ? 30 AC3 5 HOH M . ? HOH A 2137 . ? 1_555 ? 31 AC4 6 GLN A 121 ? GLN A 135 . ? 1_555 ? 32 AC4 6 ASN A 144 ? ASN A 159 . ? 1_555 ? 33 AC4 6 VAL A 178 ? VAL A 200 . ? 1_555 ? 34 AC4 6 CYS A 179 ? CYS A 201 . ? 1_555 ? 35 AC4 6 ASN A 180 ? ASN A 204 . ? 1_555 ? 36 AC4 6 GLY A 181 ? GLY A 205 . ? 1_555 ? 37 AC5 4 ARG B 52 A ARG B 65 . ? 1_555 ? 38 AC5 4 ALA B 71 ? ALA B 84 . ? 1_555 ? 39 AC5 4 ASN B 95 ? ASN B 109 . ? 1_555 ? 40 AC5 4 HOH N . ? HOH B 2106 . ? 1_555 ? 41 AC6 8 ARG B 5 ? ARG B 20 . ? 1_555 ? 42 AC6 8 TRP B 12 ? TRP B 27 . ? 1_555 ? 43 AC6 8 GLN B 121 ? GLN B 135 . ? 1_555 ? 44 AC6 8 ASN B 144 ? ASN B 159 . ? 1_555 ? 45 AC6 8 VAL B 178 ? VAL B 200 . ? 1_555 ? 46 AC6 8 CYS B 179 ? CYS B 201 . ? 1_555 ? 47 AC6 8 ASN B 180 ? ASN B 204 . ? 1_555 ? 48 AC6 8 GLY B 181 ? GLY B 205 . ? 1_555 ? # _database_PDB_matrix.entry_id 1H1B _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 1H1B _atom_sites.fract_transf_matrix[1][1] 0.014518 _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] 0.014518 _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] 0.004147 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . ILE A 1 1 ? 6.702 16.954 23.280 1.00 27.29 ? 16 ILE A N 1 ATOM 2 C CA . ILE A 1 1 ? 6.806 18.307 22.554 1.00 29.20 ? 16 ILE A CA 1 ATOM 3 C C . ILE A 1 1 ? 6.711 19.482 23.515 1.00 30.73 ? 16 ILE A C 1 ATOM 4 O O . ILE A 1 1 ? 5.721 19.623 24.240 1.00 31.66 ? 16 ILE A O 1 ATOM 5 C CB . ILE A 1 1 ? 5.681 18.467 21.446 1.00 29.47 ? 16 ILE A CB 1 ATOM 6 C CG1 . ILE A 1 1 ? 5.692 17.306 20.405 1.00 24.94 ? 16 ILE A CG1 1 ATOM 7 C CG2 . ILE A 1 1 ? 5.745 19.841 20.764 1.00 30.62 ? 16 ILE A CG2 1 ATOM 8 C CD1 . ILE A 1 1 ? 6.916 17.219 19.572 1.00 31.20 ? 16 ILE A CD1 1 ATOM 9 N N . VAL A 1 2 ? 7.758 20.306 23.530 1.00 32.89 ? 17 VAL A N 1 ATOM 10 C CA . VAL A 1 2 ? 7.815 21.478 24.380 1.00 33.38 ? 17 VAL A CA 1 ATOM 11 C C . VAL A 1 2 ? 7.379 22.729 23.576 1.00 34.35 ? 17 VAL A C 1 ATOM 12 O O . VAL A 1 2 ? 7.924 23.022 22.499 1.00 33.66 ? 17 VAL A O 1 ATOM 13 C CB . VAL A 1 2 ? 9.223 21.666 25.002 1.00 33.62 ? 17 VAL A CB 1 ATOM 14 C CG1 . VAL A 1 2 ? 9.326 23.038 25.724 1.00 33.93 ? 17 VAL A CG1 1 ATOM 15 C CG2 . VAL A 1 2 ? 9.510 20.578 25.957 1.00 33.35 ? 17 VAL A CG2 1 ATOM 16 N N . GLY A 1 3 ? 6.361 23.409 24.105 1.00 34.54 ? 18 GLY A N 1 ATOM 17 C CA . GLY A 1 3 ? 5.800 24.605 23.516 1.00 35.17 ? 18 GLY A CA 1 ATOM 18 C C . GLY A 1 3 ? 4.967 24.465 22.235 1.00 36.13 ? 18 GLY A C 1 ATOM 19 O O . GLY A 1 3 ? 4.884 25.414 21.464 1.00 35.08 ? 18 GLY A O 1 ATOM 20 N N . GLY A 1 4 ? 4.356 23.301 22.025 1.00 35.90 ? 19 GLY A N 1 ATOM 21 C CA . GLY A 1 4 ? 3.526 23.025 20.866 1.00 36.86 ? 19 GLY A CA 1 ATOM 22 C C . GLY A 1 4 ? 2.095 23.182 21.306 1.00 37.13 ? 19 GLY A C 1 ATOM 23 O O . GLY A 1 4 ? 1.881 23.871 22.285 1.00 36.99 ? 19 GLY A O 1 ATOM 24 N N . ARG A 1 5 ? 1.146 22.592 20.582 1.00 37.99 ? 20 ARG A N 1 ATOM 25 C CA . ARG A 1 5 ? -0.290 22.572 20.948 1.00 38.81 ? 20 ARG A CA 1 ATOM 26 C C . ARG A 1 5 ? -0.922 21.187 20.768 1.00 39.09 ? 20 ARG A C 1 ATOM 27 O O . ARG A 1 5 ? -0.321 20.310 20.190 1.00 38.53 ? 20 ARG A O 1 ATOM 28 C CB . ARG A 1 5 ? -1.090 23.588 20.126 1.00 38.78 ? 20 ARG A CB 1 ATOM 29 C CG . ARG A 1 5 ? -1.032 23.341 18.630 1.00 40.09 ? 20 ARG A CG 1 ATOM 30 C CD . ARG A 1 5 ? -1.157 24.597 17.793 1.00 46.05 ? 20 ARG A CD 1 ATOM 31 N NE . ARG A 1 5 ? -1.166 24.356 16.349 1.00 47.45 ? 20 ARG A NE 1 ATOM 32 C CZ . ARG A 1 5 ? -0.119 24.495 15.555 1.00 50.68 ? 20 ARG A CZ 1 ATOM 33 N NH1 . ARG A 1 5 ? 1.077 24.842 16.034 1.00 52.30 ? 20 ARG A NH1 1 ATOM 34 N NH2 . ARG A 1 5 ? -0.256 24.262 14.264 1.00 54.16 ? 20 ARG A NH2 1 ATOM 35 N N . ARG A 1 6 ? -2.136 20.991 21.269 1.00 40.94 ? 21 ARG A N 1 ATOM 36 C CA . ARG A 1 6 ? -2.821 19.731 21.042 1.00 43.14 ? 21 ARG A CA 1 ATOM 37 C C . ARG A 1 6 ? -3.092 19.680 19.534 1.00 43.26 ? 21 ARG A C 1 ATOM 38 O O . ARG A 1 6 ? -3.334 20.721 18.891 1.00 43.41 ? 21 ARG A O 1 ATOM 39 C CB . ARG A 1 6 ? -4.140 19.617 21.830 1.00 44.05 ? 21 ARG A CB 1 ATOM 40 C CG . ARG A 1 6 ? -4.124 20.264 23.204 1.00 48.11 ? 21 ARG A CG 1 ATOM 41 C CD . ARG A 1 6 ? -4.872 19.512 24.329 1.00 54.89 ? 21 ARG A CD 1 ATOM 42 N NE . ARG A 1 6 ? -3.954 18.794 25.243 1.00 61.94 ? 21 ARG A NE 1 ATOM 43 C CZ . ARG A 1 6 ? -2.942 19.360 25.942 1.00 62.89 ? 21 ARG A CZ 1 ATOM 44 N NH1 . ARG A 1 6 ? -2.185 18.622 26.748 1.00 60.79 ? 21 ARG A NH1 1 ATOM 45 N NH2 . ARG A 1 6 ? -2.694 20.667 25.844 1.00 64.05 ? 21 ARG A NH2 1 ATOM 46 N N . ALA A 1 7 ? -2.911 18.506 18.949 1.00 42.66 ? 22 ALA A N 1 ATOM 47 C CA . ALA A 1 7 ? -3.287 18.312 17.578 1.00 42.78 ? 22 ALA A CA 1 ATOM 48 C C . ALA A 1 7 ? -4.757 17.991 17.614 1.00 43.53 ? 22 ALA A C 1 ATOM 49 O O . ALA A 1 7 ? -5.283 17.496 18.606 1.00 40.52 ? 22 ALA A O 1 ATOM 50 C CB . ALA A 1 7 ? -2.570 17.130 16.987 1.00 43.20 ? 22 ALA A CB 1 ATOM 51 N N . ARG A 1 8 ? -5.403 18.221 16.474 1.00 45.20 ? 23 ARG A N 1 ATOM 52 C CA . ARG A 1 8 ? -6.764 17.879 16.313 1.00 46.91 ? 23 ARG A CA 1 ATOM 53 C C . ARG A 1 8 ? -6.837 16.365 16.331 1.00 47.12 ? 23 ARG A C 1 ATOM 54 O O . ARG A 1 8 ? -5.975 15.707 15.795 1.00 46.72 ? 23 ARG A O 1 ATOM 55 C CB . ARG A 1 8 ? -7.216 18.409 14.977 1.00 47.47 ? 23 ARG A CB 1 ATOM 56 C CG . ARG A 1 8 ? -8.705 18.283 14.799 1.00 53.84 ? 23 ARG A CG 1 ATOM 57 C CD . ARG A 1 8 ? -9.204 18.891 13.513 1.00 60.77 ? 23 ARG A CD 1 ATOM 58 N NE . ARG A 1 8 ? -8.314 18.556 12.400 1.00 65.36 ? 23 ARG A NE 1 ATOM 59 C CZ . ARG A 1 8 ? -8.318 17.386 11.761 1.00 67.97 ? 23 ARG A CZ 1 ATOM 60 N NH1 . ARG A 1 8 ? -9.175 16.432 12.135 1.00 70.07 ? 23 ARG A NH1 1 ATOM 61 N NH2 . ARG A 1 8 ? -7.466 17.171 10.758 1.00 66.97 ? 23 ARG A NH2 1 ATOM 62 N N . PRO A 1 9 ? -7.844 15.814 16.978 1.00 47.53 ? 24 PRO A N 1 ATOM 63 C CA . PRO A 1 9 ? -8.031 14.372 17.002 1.00 48.77 ? 24 PRO A CA 1 ATOM 64 C C . PRO A 1 9 ? -7.815 13.717 15.638 1.00 49.77 ? 24 PRO A C 1 ATOM 65 O O . PRO A 1 9 ? -8.248 14.171 14.579 1.00 50.11 ? 24 PRO A O 1 ATOM 66 C CB . PRO A 1 9 ? -9.485 14.218 17.423 1.00 49.12 ? 24 PRO A CB 1 ATOM 67 C CG . PRO A 1 9 ? -9.735 15.449 18.315 1.00 49.13 ? 24 PRO A CG 1 ATOM 68 C CD . PRO A 1 9 ? -8.859 16.533 17.766 1.00 48.41 ? 24 PRO A CD 1 ATOM 69 N N . HIS A 1 10 ? -7.082 12.625 15.666 1.00 50.84 ? 25 HIS A N 1 ATOM 70 C CA . HIS A 1 10 ? -6.909 11.852 14.458 1.00 50.69 ? 25 HIS A CA 1 ATOM 71 C C . HIS A 1 10 ? -6.674 12.748 13.245 1.00 50.37 ? 25 HIS A C 1 ATOM 72 O O . HIS A 1 10 ? -7.155 12.458 12.147 1.00 51.28 ? 25 HIS A O 1 ATOM 73 C CB . HIS A 1 10 ? -8.128 10.943 14.318 1.00 50.70 ? 25 HIS A CB 1 ATOM 74 C CG . HIS A 1 10 ? -8.383 10.129 15.551 1.00 50.13 ? 25 HIS A CG 1 ATOM 75 N ND1 . HIS A 1 10 ? -7.599 9.043 15.898 1.00 48.20 ? 25 HIS A ND1 1 ATOM 76 C CD2 . HIS A 1 10 ? -9.283 10.281 16.556 1.00 49.01 ? 25 HIS A CD2 1 ATOM 77 C CE1 . HIS A 1 10 ? -8.034 8.543 17.045 1.00 49.05 ? 25 HIS A CE1 1 ATOM 78 N NE2 . HIS A 1 10 ? -9.050 9.277 17.469 1.00 47.85 ? 25 HIS A NE2 1 ATOM 79 N N . ALA A 1 11 ? -5.903 13.824 13.467 1.00 48.94 ? 26 ALA A N 1 ATOM 80 C CA . ALA A 1 11 ? -5.458 14.745 12.423 1.00 46.14 ? 26 ALA A CA 1 ATOM 81 C C . ALA A 1 11 ? -4.360 14.146 11.606 1.00 45.25 ? 26 ALA A C 1 ATOM 82 O O . ALA A 1 11 ? -4.153 14.549 10.461 1.00 45.18 ? 26 ALA A O 1 ATOM 83 C CB . ALA A 1 11 ? -4.942 16.046 13.033 1.00 46.09 ? 26 ALA A CB 1 ATOM 84 N N . TRP A 1 12 ? -3.613 13.217 12.203 1.00 44.00 ? 27 TRP A N 1 ATOM 85 C CA . TRP A 1 12 ? -2.462 12.581 11.551 1.00 42.55 ? 27 TRP A CA 1 ATOM 86 C C . TRP A 1 12 ? -2.495 11.051 11.718 1.00 42.22 ? 27 TRP A C 1 ATOM 87 O O . TRP A 1 12 ? -1.722 10.438 12.491 1.00 41.39 ? 27 TRP A O 1 ATOM 88 C CB . TRP A 1 12 ? -1.179 13.165 12.112 1.00 41.88 ? 27 TRP A CB 1 ATOM 89 C CG . TRP A 1 12 ? -1.296 14.671 12.329 1.00 43.44 ? 27 TRP A CG 1 ATOM 90 C CD1 . TRP A 1 12 ? -1.399 15.317 13.523 1.00 42.36 ? 27 TRP A CD1 1 ATOM 91 C CD2 . TRP A 1 12 ? -1.309 15.682 11.329 1.00 44.78 ? 27 TRP A CD2 1 ATOM 92 N NE1 . TRP A 1 12 ? -1.450 16.674 13.334 1.00 44.59 ? 27 TRP A NE1 1 ATOM 93 C CE2 . TRP A 1 12 ? -1.418 16.933 11.993 1.00 45.69 ? 27 TRP A CE2 1 ATOM 94 C CE3 . TRP A 1 12 ? -1.248 15.669 9.928 1.00 47.38 ? 27 TRP A CE3 1 ATOM 95 C CZ2 . TRP A 1 12 ? -1.462 18.159 11.308 1.00 45.02 ? 27 TRP A CZ2 1 ATOM 96 C CZ3 . TRP A 1 12 ? -1.319 16.913 9.227 1.00 47.37 ? 27 TRP A CZ3 1 ATOM 97 C CH2 . TRP A 1 12 ? -1.410 18.127 9.927 1.00 45.56 ? 27 TRP A CH2 1 ATOM 98 N N . PRO A 1 13 ? -3.377 10.440 10.933 1.00 41.22 ? 28 PRO A N 1 ATOM 99 C CA . PRO A 1 13 ? -3.709 9.015 11.053 1.00 39.02 ? 28 PRO A CA 1 ATOM 100 C C . PRO A 1 13 ? -2.549 8.021 10.809 1.00 36.42 ? 28 PRO A C 1 ATOM 101 O O . PRO A 1 13 ? -2.698 6.857 11.015 1.00 35.47 ? 28 PRO A O 1 ATOM 102 C CB . PRO A 1 13 ? -4.905 8.861 10.060 1.00 40.67 ? 28 PRO A CB 1 ATOM 103 C CG . PRO A 1 13 ? -4.648 9.962 9.000 1.00 41.07 ? 28 PRO A CG 1 ATOM 104 C CD . PRO A 1 13 ? -4.162 11.119 9.880 1.00 42.01 ? 28 PRO A CD 1 ATOM 105 N N . PHE A 1 14 ? -1.413 8.479 10.338 1.00 34.63 ? 29 PHE A N 1 ATOM 106 C CA . PHE A 1 14 ? -0.266 7.612 10.264 1.00 34.09 ? 29 PHE A CA 1 ATOM 107 C C . PHE A 1 14 ? 0.563 7.618 11.578 1.00 32.61 ? 29 PHE A C 1 ATOM 108 O O . PHE A 1 14 ? 1.625 7.042 11.598 1.00 32.47 ? 29 PHE A O 1 ATOM 109 C CB . PHE A 1 14 ? 0.663 8.126 9.187 1.00 34.34 ? 29 PHE A CB 1 ATOM 110 C CG . PHE A 1 14 ? 0.857 9.642 9.205 1.00 36.96 ? 29 PHE A CG 1 ATOM 111 C CD1 . PHE A 1 14 ? 1.898 10.234 9.926 1.00 36.67 ? 29 PHE A CD1 1 ATOM 112 C CD2 . PHE A 1 14 ? -0.024 10.477 8.503 1.00 41.28 ? 29 PHE A CD2 1 ATOM 113 C CE1 . PHE A 1 14 ? 2.034 11.652 9.970 1.00 37.00 ? 29 PHE A CE1 1 ATOM 114 C CE2 . PHE A 1 14 ? 0.117 11.873 8.499 1.00 37.13 ? 29 PHE A CE2 1 ATOM 115 C CZ . PHE A 1 14 ? 1.155 12.458 9.213 1.00 40.60 ? 29 PHE A CZ 1 ATOM 116 N N . MET A 1 15 ? 0.126 8.357 12.601 1.00 30.05 ? 30 MET A N 1 ATOM 117 C CA . MET A 1 15 ? 0.966 8.617 13.793 1.00 29.31 ? 30 MET A CA 1 ATOM 118 C C . MET A 1 15 ? 0.871 7.421 14.705 1.00 27.48 ? 30 MET A C 1 ATOM 119 O O . MET A 1 15 ? -0.221 7.035 15.032 1.00 28.61 ? 30 MET A O 1 ATOM 120 C CB . MET A 1 15 ? 0.547 9.912 14.558 1.00 26.61 ? 30 MET A CB 1 ATOM 121 C CG . MET A 1 15 ? 1.306 10.162 15.899 1.00 23.74 ? 30 MET A CG 1 ATOM 122 S SD . MET A 1 15 ? 2.978 10.434 15.520 1.00 27.91 ? 30 MET A SD 1 ATOM 123 C CE . MET A 1 15 ? 3.844 9.997 17.198 1.00 28.37 ? 30 MET A CE 1 ATOM 124 N N . VAL A 1 16 ? 2.014 6.845 15.098 1.00 28.45 ? 31 VAL A N 1 ATOM 125 C CA . VAL A 1 16 ? 2.016 5.578 15.884 1.00 28.62 ? 31 VAL A CA 1 ATOM 126 C C . VAL A 1 16 ? 2.641 5.788 17.285 1.00 28.41 ? 31 VAL A C 1 ATOM 127 O O . VAL A 1 16 ? 3.548 6.594 17.380 1.00 27.66 ? 31 VAL A O 1 ATOM 128 C CB . VAL A 1 16 ? 2.803 4.491 15.124 1.00 28.55 ? 31 VAL A CB 1 ATOM 129 C CG1 . VAL A 1 16 ? 2.952 3.139 15.936 1.00 31.60 ? 31 VAL A CG1 1 ATOM 130 C CG2 . VAL A 1 16 ? 2.195 4.290 13.707 1.00 31.40 ? 31 VAL A CG2 1 ATOM 131 N N . SER A 1 17 ? 2.081 5.138 18.324 1.00 27.76 ? 32 SER A N 1 ATOM 132 C CA . SER A 1 17 ? 2.717 5.044 19.665 1.00 28.95 ? 32 SER A CA 1 ATOM 133 C C . SER A 1 17 ? 3.280 3.625 19.883 1.00 28.60 ? 32 SER A C 1 ATOM 134 O O . SER A 1 17 ? 2.527 2.675 19.825 1.00 28.42 ? 32 SER A O 1 ATOM 135 C CB . SER A 1 17 ? 1.749 5.383 20.819 1.00 28.95 ? 32 SER A CB 1 ATOM 136 O OG . SER A 1 17 ? 2.230 4.948 22.091 1.00 26.12 ? 32 SER A OG 1 ATOM 137 N N . LEU A 1 18 ? 4.604 3.534 20.069 1.00 26.79 ? 33 LEU A N 1 ATOM 138 C CA . LEU A 1 18 ? 5.296 2.363 20.531 1.00 25.86 ? 33 LEU A CA 1 ATOM 139 C C . LEU A 1 18 ? 5.227 2.335 22.056 1.00 27.32 ? 33 LEU A C 1 ATOM 140 O O . LEU A 1 18 ? 5.660 3.276 22.710 1.00 25.92 ? 33 LEU A O 1 ATOM 141 C CB . LEU A 1 18 ? 6.779 2.389 20.116 1.00 25.35 ? 33 LEU A CB 1 ATOM 142 C CG . LEU A 1 18 ? 6.987 2.479 18.607 1.00 25.04 ? 33 LEU A CG 1 ATOM 143 C CD1 . LEU A 1 18 ? 8.431 2.376 18.215 1.00 22.47 ? 33 LEU A CD1 1 ATOM 144 C CD2 . LEU A 1 18 ? 6.083 1.475 17.798 1.00 26.22 ? 33 LEU A CD2 1 ATOM 145 N N . GLN A 1 19 ? 4.735 1.220 22.597 1.00 27.95 ? 34 GLN A N 1 ATOM 146 C CA . GLN A 1 19 ? 4.506 1.030 24.028 1.00 28.84 ? 34 GLN A CA 1 ATOM 147 C C . GLN A 1 19 ? 5.128 -0.274 24.574 1.00 30.70 ? 34 GLN A C 1 ATOM 148 O O . GLN A 1 19 ? 5.171 -1.296 23.875 1.00 27.70 ? 34 GLN A O 1 ATOM 149 C CB . GLN A 1 19 ? 2.986 1.036 24.335 1.00 28.25 ? 34 GLN A CB 1 ATOM 150 C CG . GLN A 1 19 ? 2.303 2.303 23.809 1.00 30.89 ? 34 GLN A CG 1 ATOM 151 C CD . GLN A 1 19 ? 0.867 2.547 24.282 1.00 36.51 ? 34 GLN A CD 1 ATOM 152 O OE1 . GLN A 1 19 ? 0.309 3.647 23.977 1.00 38.93 ? 34 GLN A OE1 1 ATOM 153 N NE2 . GLN A 1 19 ? 0.257 1.569 25.009 1.00 25.21 ? 34 GLN A NE2 1 ATOM 154 N N . LEU A 1 20 ? 5.615 -0.209 25.819 1.00 31.94 ? 35 LEU A N 1 ATOM 155 C CA . LEU A 1 20 ? 6.094 -1.389 26.529 1.00 34.35 ? 35 LEU A CA 1 ATOM 156 C C . LEU A 1 20 ? 5.165 -1.731 27.748 1.00 34.07 ? 35 LEU A C 1 ATOM 157 O O . LEU A 1 20 ? 5.175 -1.061 28.778 1.00 35.04 ? 35 LEU A O 1 ATOM 158 C CB . LEU A 1 20 ? 7.541 -1.081 26.964 1.00 34.34 ? 35 LEU A CB 1 ATOM 159 C CG . LEU A 1 20 ? 8.360 -2.301 27.348 1.00 38.94 ? 35 LEU A CG 1 ATOM 160 C CD1 . LEU A 1 20 ? 8.751 -3.117 26.056 1.00 32.13 ? 35 LEU A CD1 1 ATOM 161 C CD2 . LEU A 1 20 ? 9.613 -1.798 28.074 1.00 39.96 ? 35 LEU A CD2 1 ATOM 162 N N . ARG A 1 21 ? 4.362 -2.796 27.636 1.00 36.41 ? 36 ARG A N 1 ATOM 163 C CA . ARG A 1 21 ? 3.329 -3.145 28.654 1.00 37.34 ? 36 ARG A CA 1 ATOM 164 C C . ARG A 1 21 ? 2.563 -1.889 29.084 1.00 37.54 ? 36 ARG A C 1 ATOM 165 O O . ARG A 1 21 ? 2.466 -1.562 30.298 1.00 38.44 ? 36 ARG A O 1 ATOM 166 C CB . ARG A 1 21 ? 3.900 -3.800 29.912 1.00 39.02 ? 36 ARG A CB 1 ATOM 167 C CG . ARG A 1 21 ? 4.413 -5.212 29.763 1.00 43.91 ? 36 ARG A CG 1 ATOM 168 C CD . ARG A 1 21 ? 3.893 -6.187 30.841 1.00 52.28 ? 36 ARG A CD 1 ATOM 169 N NE . ARG A 1 21 ? 2.870 -7.085 30.299 1.00 57.63 ? 36 ARG A NE 1 ATOM 170 C CZ . ARG A 1 21 ? 1.594 -7.106 30.680 1.00 61.47 ? 36 ARG A CZ 1 ATOM 171 N NH1 . ARG A 1 21 ? 1.147 -6.297 31.632 1.00 61.47 ? 36 ARG A NH1 1 ATOM 172 N NH2 . ARG A 1 21 ? 0.756 -7.947 30.093 1.00 63.69 ? 36 ARG A NH2 1 ATOM 173 N N . GLY A 1 22 ? 2.008 -1.214 28.079 1.00 35.50 ? 38 GLY A N 1 ATOM 174 C CA . GLY A 1 22 ? 1.126 -0.083 28.278 1.00 33.35 ? 38 GLY A CA 1 ATOM 175 C C . GLY A 1 22 ? 1.803 1.270 28.344 1.00 31.42 ? 38 GLY A C 1 ATOM 176 O O . GLY A 1 22 ? 1.124 2.292 28.403 1.00 32.54 ? 38 GLY A O 1 ATOM 177 N N . GLY A 1 23 ? 3.124 1.282 28.323 1.00 29.52 ? 39 GLY A N 1 ATOM 178 C CA . GLY A 1 23 ? 3.800 2.533 28.455 1.00 29.04 ? 39 GLY A CA 1 ATOM 179 C C . GLY A 1 23 ? 4.479 3.060 27.210 1.00 28.19 ? 39 GLY A C 1 ATOM 180 O O . GLY A 1 23 ? 5.482 2.481 26.775 1.00 27.54 ? 39 GLY A O 1 ATOM 181 N N . HIS A 1 24 ? 3.944 4.172 26.711 1.00 27.01 ? 40 HIS A N 1 ATOM 182 C CA . HIS A 1 24 ? 4.531 4.889 25.567 1.00 27.21 ? 40 HIS A CA 1 ATOM 183 C C . HIS A 1 24 ? 6.004 5.190 25.859 1.00 24.76 ? 40 HIS A C 1 ATOM 184 O O . HIS A 1 24 ? 6.304 5.724 26.897 1.00 25.77 ? 40 HIS A O 1 ATOM 185 C CB . HIS A 1 24 ? 3.778 6.191 25.289 1.00 25.19 ? 40 HIS A CB 1 ATOM 186 C CG . HIS A 1 24 ? 4.428 7.032 24.221 1.00 29.75 ? 40 HIS A CG 1 ATOM 187 N ND1 . HIS A 1 24 ? 4.212 6.830 22.867 1.00 28.80 ? 40 HIS A ND1 1 ATOM 188 C CD2 . HIS A 1 24 ? 5.334 8.039 24.310 1.00 24.30 ? 40 HIS A CD2 1 ATOM 189 C CE1 . HIS A 1 24 ? 4.953 7.687 22.179 1.00 25.03 ? 40 HIS A CE1 1 ATOM 190 N NE2 . HIS A 1 24 ? 5.656 8.416 23.027 1.00 24.38 ? 40 HIS A NE2 1 ATOM 191 N N . PHE A 1 25 ? 6.891 4.875 24.932 1.00 24.60 ? 41 PHE A N 1 ATOM 192 C CA . PHE A 1 25 ? 8.319 5.270 25.016 1.00 25.45 ? 41 PHE A CA 1 ATOM 193 C C . PHE A 1 25 ? 8.846 5.928 23.708 1.00 24.95 ? 41 PHE A C 1 ATOM 194 O O . PHE A 1 25 ? 9.931 6.403 23.686 1.00 25.78 ? 41 PHE A O 1 ATOM 195 C CB . PHE A 1 25 ? 9.238 4.074 25.374 1.00 25.18 ? 41 PHE A CB 1 ATOM 196 C CG . PHE A 1 25 ? 9.244 2.959 24.356 1.00 29.32 ? 41 PHE A CG 1 ATOM 197 C CD1 . PHE A 1 25 ? 10.121 2.968 23.280 1.00 29.70 ? 41 PHE A CD1 1 ATOM 198 C CD2 . PHE A 1 25 ? 8.383 1.868 24.487 1.00 27.47 ? 41 PHE A CD2 1 ATOM 199 C CE1 . PHE A 1 25 ? 10.105 1.889 22.343 1.00 31.29 ? 41 PHE A CE1 1 ATOM 200 C CE2 . PHE A 1 25 ? 8.400 0.836 23.598 1.00 26.23 ? 41 PHE A CE2 1 ATOM 201 C CZ . PHE A 1 25 ? 9.236 0.867 22.492 1.00 26.80 ? 41 PHE A CZ 1 ATOM 202 N N . CYS A 1 26 ? 8.120 5.856 22.594 1.00 23.22 ? 42 CYS A N 1 ATOM 203 C CA . CYS A 1 26 ? 8.609 6.469 21.342 1.00 23.23 ? 42 CYS A CA 1 ATOM 204 C C . CYS A 1 26 ? 7.464 6.504 20.348 1.00 23.22 ? 42 CYS A C 1 ATOM 205 O O . CYS A 1 26 ? 6.525 5.739 20.488 1.00 24.18 ? 42 CYS A O 1 ATOM 206 C CB . CYS A 1 26 ? 9.742 5.680 20.647 1.00 23.81 ? 42 CYS A CB 1 ATOM 207 S SG . CYS A 1 26 ? 11.427 5.910 21.147 1.00 21.37 ? 42 CYS A SG 1 ATOM 208 N N . GLY A 1 27 ? 7.572 7.345 19.306 1.00 23.96 ? 43 GLY A N 1 ATOM 209 C CA . GLY A 1 27 ? 6.543 7.351 18.253 1.00 23.54 ? 43 GLY A CA 1 ATOM 210 C C . GLY A 1 27 ? 7.025 6.528 17.054 1.00 25.50 ? 43 GLY A C 1 ATOM 211 O O . GLY A 1 27 ? 8.094 5.941 17.067 1.00 25.54 ? 43 GLY A O 1 ATOM 212 N N . ALA A 1 28 ? 6.215 6.495 16.001 1.00 27.36 ? 44 ALA A N 1 ATOM 213 C CA . ALA A 1 28 ? 6.559 5.839 14.752 1.00 27.09 ? 44 ALA A CA 1 ATOM 214 C C . ALA A 1 28 ? 5.567 6.304 13.673 1.00 27.14 ? 44 ALA A C 1 ATOM 215 O O . ALA A 1 28 ? 4.562 6.976 13.999 1.00 27.24 ? 44 ALA A O 1 ATOM 216 C CB . ALA A 1 28 ? 6.498 4.273 14.893 1.00 27.20 ? 44 ALA A CB 1 ATOM 217 N N . THR A 1 29 ? 5.834 5.859 12.434 1.00 27.04 ? 45 THR A N 1 ATOM 218 C CA . THR A 1 29 ? 4.993 6.162 11.273 1.00 28.85 ? 45 THR A CA 1 ATOM 219 C C . THR A 1 29 ? 4.510 4.940 10.461 1.00 28.43 ? 45 THR A C 1 ATOM 220 O O . THR A 1 29 ? 5.304 4.189 10.046 1.00 28.11 ? 45 THR A O 1 ATOM 221 C CB . THR A 1 29 ? 5.747 7.049 10.334 1.00 29.52 ? 45 THR A CB 1 ATOM 222 O OG1 . THR A 1 29 ? 6.035 8.296 10.977 1.00 30.27 ? 45 THR A OG1 1 ATOM 223 C CG2 . THR A 1 29 ? 4.827 7.448 9.141 1.00 30.49 ? 45 THR A CG2 1 ATOM 224 N N . LEU A 1 30 ? 3.210 4.792 10.251 1.00 28.90 ? 46 LEU A N 1 ATOM 225 C CA . LEU A 1 30 ? 2.701 3.692 9.426 1.00 32.09 ? 46 LEU A CA 1 ATOM 226 C C . LEU A 1 30 ? 3.020 3.966 7.941 1.00 32.89 ? 46 LEU A C 1 ATOM 227 O O . LEU A 1 30 ? 2.498 4.947 7.369 1.00 33.67 ? 46 LEU A O 1 ATOM 228 C CB . LEU A 1 30 ? 1.200 3.624 9.631 1.00 32.41 ? 46 LEU A CB 1 ATOM 229 C CG . LEU A 1 30 ? 0.555 2.423 8.977 1.00 34.89 ? 46 LEU A CG 1 ATOM 230 C CD1 . LEU A 1 30 ? 1.308 1.136 9.529 1.00 34.77 ? 46 LEU A CD1 1 ATOM 231 C CD2 . LEU A 1 30 ? -0.963 2.388 9.135 1.00 33.37 ? 46 LEU A CD2 1 ATOM 232 N N . ILE A 1 31 ? 3.937 3.198 7.363 1.00 33.02 ? 47 ILE A N 1 ATOM 233 C CA . ILE A 1 31 ? 4.346 3.405 5.976 1.00 33.77 ? 47 ILE A CA 1 ATOM 234 C C . ILE A 1 31 ? 3.769 2.364 4.971 1.00 35.60 ? 47 ILE A C 1 ATOM 235 O O . ILE A 1 31 ? 4.070 2.430 3.766 1.00 35.38 ? 47 ILE A O 1 ATOM 236 C CB . ILE A 1 31 ? 5.877 3.474 5.863 1.00 34.09 ? 47 ILE A CB 1 ATOM 237 C CG1 . ILE A 1 31 ? 6.509 2.223 6.419 1.00 29.77 ? 47 ILE A CG1 1 ATOM 238 C CG2 . ILE A 1 31 ? 6.450 4.782 6.565 1.00 33.71 ? 47 ILE A CG2 1 ATOM 239 C CD1 . ILE A 1 31 ? 8.050 2.071 6.155 1.00 31.51 ? 47 ILE A CD1 1 ATOM 240 N N . ALA A 1 32 ? 2.981 1.416 5.497 1.00 37.43 ? 48 ALA A N 1 ATOM 241 C CA . ALA A 1 32 ? 2.296 0.337 4.728 1.00 37.54 ? 48 ALA A CA 1 ATOM 242 C C . ALA A 1 32 ? 1.397 -0.328 5.730 1.00 37.74 ? 48 ALA A C 1 ATOM 243 O O . ALA A 1 32 ? 1.611 -0.171 6.913 1.00 36.56 ? 48 ALA A O 1 ATOM 244 C CB . ALA A 1 32 ? 3.288 -0.637 4.130 1.00 37.45 ? 48 ALA A CB 1 ATOM 245 N N . PRO A 1 33 ? 0.363 -1.060 5.298 1.00 38.54 ? 49 PRO A N 1 ATOM 246 C CA . PRO A 1 33 ? -0.633 -1.550 6.250 1.00 37.89 ? 49 PRO A CA 1 ATOM 247 C C . PRO A 1 33 ? -0.004 -2.458 7.254 1.00 37.05 ? 49 PRO A C 1 ATOM 248 O O . PRO A 1 33 ? -0.581 -2.645 8.328 1.00 35.97 ? 49 PRO A O 1 ATOM 249 C CB . PRO A 1 33 ? -1.634 -2.299 5.366 1.00 39.41 ? 49 PRO A CB 1 ATOM 250 C CG . PRO A 1 33 ? -1.450 -1.600 4.021 1.00 39.25 ? 49 PRO A CG 1 ATOM 251 C CD . PRO A 1 33 ? 0.065 -1.469 3.916 1.00 38.72 ? 49 PRO A CD 1 ATOM 252 N N . ASN A 1 34 ? 1.189 -2.966 6.919 1.00 35.96 ? 50 ASN A N 1 ATOM 253 C CA . ASN A 1 34 ? 1.876 -3.865 7.813 1.00 35.93 ? 50 ASN A CA 1 ATOM 254 C C . ASN A 1 34 ? 3.322 -3.488 8.068 1.00 34.84 ? 50 ASN A C 1 ATOM 255 O O . ASN A 1 34 ? 4.142 -4.369 8.330 1.00 35.35 ? 50 ASN A O 1 ATOM 256 C CB . ASN A 1 34 ? 1.765 -5.336 7.304 1.00 36.42 ? 50 ASN A CB 1 ATOM 257 C CG . ASN A 1 34 ? 2.390 -5.530 5.953 1.00 37.70 ? 50 ASN A CG 1 ATOM 258 O OD1 . ASN A 1 34 ? 2.331 -4.645 5.114 1.00 40.27 ? 50 ASN A OD1 1 ATOM 259 N ND2 . ASN A 1 34 ? 3.047 -6.661 5.750 1.00 40.25 ? 50 ASN A ND2 1 ATOM 260 N N . PHE A 1 35 ? 3.665 -2.190 7.980 1.00 33.55 ? 51 PHE A N 1 ATOM 261 C CA . PHE A 1 35 ? 5.019 -1.796 8.303 1.00 31.66 ? 51 PHE A CA 1 ATOM 262 C C . PHE A 1 35 ? 5.036 -0.383 8.959 1.00 31.54 ? 51 PHE A C 1 ATOM 263 O O . PHE A 1 35 ? 4.344 0.516 8.485 1.00 31.25 ? 51 PHE A O 1 ATOM 264 C CB . PHE A 1 35 ? 5.872 -1.689 7.043 1.00 32.18 ? 51 PHE A CB 1 ATOM 265 C CG . PHE A 1 35 ? 6.359 -2.992 6.472 1.00 33.10 ? 51 PHE A CG 1 ATOM 266 C CD1 . PHE A 1 35 ? 7.573 -3.518 6.855 1.00 33.67 ? 51 PHE A CD1 1 ATOM 267 C CD2 . PHE A 1 35 ? 5.642 -3.628 5.461 1.00 37.13 ? 51 PHE A CD2 1 ATOM 268 C CE1 . PHE A 1 35 ? 8.031 -4.675 6.304 1.00 34.51 ? 51 PHE A CE1 1 ATOM 269 C CE2 . PHE A 1 35 ? 6.099 -4.812 4.901 1.00 33.83 ? 51 PHE A CE2 1 ATOM 270 C CZ . PHE A 1 35 ? 7.306 -5.320 5.298 1.00 34.36 ? 51 PHE A CZ 1 ATOM 271 N N . VAL A 1 36 ? 5.796 -0.198 10.040 1.00 30.13 ? 52 VAL A N 1 ATOM 272 C CA . VAL A 1 36 ? 6.023 1.189 10.581 1.00 27.13 ? 52 VAL A CA 1 ATOM 273 C C . VAL A 1 36 ? 7.491 1.456 10.482 1.00 27.47 ? 52 VAL A C 1 ATOM 274 O O . VAL A 1 36 ? 8.244 0.544 10.239 1.00 26.04 ? 52 VAL A O 1 ATOM 275 C CB . VAL A 1 36 ? 5.516 1.381 11.987 1.00 26.53 ? 52 VAL A CB 1 ATOM 276 C CG1 . VAL A 1 36 ? 4.105 1.115 12.036 1.00 23.72 ? 52 VAL A CG1 1 ATOM 277 C CG2 . VAL A 1 36 ? 6.261 0.573 13.031 1.00 24.00 ? 52 VAL A CG2 1 ATOM 278 N N . MET A 1 37 ? 7.894 2.719 10.529 1.00 25.86 ? 53 MET A N 1 ATOM 279 C CA . MET A 1 37 ? 9.281 2.994 10.642 1.00 25.63 ? 53 MET A CA 1 ATOM 280 C C . MET A 1 37 ? 9.366 4.008 11.867 1.00 24.77 ? 53 MET A C 1 ATOM 281 O O . MET A 1 37 ? 8.404 4.749 12.142 1.00 24.62 ? 53 MET A O 1 ATOM 282 C CB . MET A 1 37 ? 9.859 3.517 9.320 1.00 27.08 ? 53 MET A CB 1 ATOM 283 C CG . MET A 1 37 ? 10.092 5.021 9.280 1.00 29.32 ? 53 MET A CG 1 ATOM 284 S SD . MET A 1 37 ? 10.434 5.806 7.574 1.00 32.00 ? 53 MET A SD 1 ATOM 285 C CE . MET A 1 37 ? 9.063 6.541 7.614 1.00 28.28 ? 53 MET A CE 1 ATOM 286 N N . SER A 1 38 ? 10.534 4.038 12.488 1.00 23.85 ? 54 SER A N 1 ATOM 287 C CA . SER A 1 38 ? 10.810 4.709 13.742 1.00 23.16 ? 54 SER A CA 1 ATOM 288 C C . SER A 1 38 ? 12.290 4.834 13.792 1.00 22.76 ? 54 SER A C 1 ATOM 289 O O . SER A 1 38 ? 12.890 4.568 12.822 1.00 23.18 ? 54 SER A O 1 ATOM 290 C CB . SER A 1 38 ? 10.373 3.799 14.870 1.00 21.94 ? 54 SER A CB 1 ATOM 291 O OG . SER A 1 38 ? 10.557 4.440 16.101 1.00 22.22 ? 54 SER A OG 1 ATOM 292 N N . ALA A 1 39 ? 12.891 5.256 14.916 1.00 22.73 ? 55 ALA A N 1 ATOM 293 C CA . ALA A 1 39 ? 14.308 5.419 15.008 1.00 21.63 ? 55 ALA A CA 1 ATOM 294 C C . ALA A 1 39 ? 14.893 4.153 15.568 1.00 24.53 ? 55 ALA A C 1 ATOM 295 O O . ALA A 1 39 ? 14.298 3.578 16.489 1.00 25.43 ? 55 ALA A O 1 ATOM 296 C CB . ALA A 1 39 ? 14.585 6.552 15.998 1.00 23.25 ? 55 ALA A CB 1 ATOM 297 N N . ALA A 1 40 ? 16.015 3.721 15.009 1.00 24.79 ? 56 ALA A N 1 ATOM 298 C CA . ALA A 1 40 ? 16.683 2.532 15.498 1.00 26.75 ? 56 ALA A CA 1 ATOM 299 C C . ALA A 1 40 ? 16.913 2.627 17.027 1.00 27.86 ? 56 ALA A C 1 ATOM 300 O O . ALA A 1 40 ? 16.796 1.631 17.780 1.00 25.69 ? 56 ALA A O 1 ATOM 301 C CB . ALA A 1 40 ? 17.974 2.372 14.816 1.00 24.58 ? 56 ALA A CB 1 ATOM 302 N N . HIS A 1 41 ? 17.192 3.831 17.524 1.00 26.98 ? 57 HIS A N 1 ATOM 303 C CA . HIS A 1 41 ? 17.691 3.894 18.931 1.00 25.97 ? 57 HIS A CA 1 ATOM 304 C C . HIS A 1 41 ? 16.544 3.582 19.842 1.00 24.56 ? 57 HIS A C 1 ATOM 305 O O . HIS A 1 41 ? 16.719 3.151 21.015 1.00 22.76 ? 57 HIS A O 1 ATOM 306 C CB . HIS A 1 41 ? 18.299 5.314 19.204 1.00 27.75 ? 57 HIS A CB 1 ATOM 307 C CG . HIS A 1 41 ? 18.656 5.544 20.632 1.00 30.43 ? 57 HIS A CG 1 ATOM 308 N ND1 . HIS A 1 41 ? 17.727 5.977 21.566 1.00 33.92 ? 57 HIS A ND1 1 ATOM 309 C CD2 . HIS A 1 41 ? 19.812 5.349 21.305 1.00 32.80 ? 57 HIS A CD2 1 ATOM 310 C CE1 . HIS A 1 41 ? 18.317 6.062 22.753 1.00 36.71 ? 57 HIS A CE1 1 ATOM 311 N NE2 . HIS A 1 41 ? 19.580 5.687 22.624 1.00 37.50 ? 57 HIS A NE2 1 ATOM 312 N N . CYS A 1 42 ? 15.334 3.779 19.317 1.00 23.90 ? 58 CYS A N 1 ATOM 313 C CA . CYS A 1 42 ? 14.148 3.495 20.105 1.00 24.78 ? 58 CYS A CA 1 ATOM 314 C C . CYS A 1 42 ? 13.993 1.995 20.533 1.00 27.76 ? 58 CYS A C 1 ATOM 315 O O . CYS A 1 42 ? 13.478 1.733 21.627 1.00 27.19 ? 58 CYS A O 1 ATOM 316 C CB . CYS A 1 42 ? 12.888 3.900 19.345 1.00 25.01 ? 58 CYS A CB 1 ATOM 317 S SG . CYS A 1 42 ? 12.410 5.729 19.358 1.00 23.68 ? 58 CYS A SG 1 ATOM 318 N N . VAL A 1 43 ? 14.447 1.051 19.698 1.00 25.92 ? 59 VAL A N 1 ATOM 319 C CA . VAL A 1 43 ? 14.263 -0.360 20.016 1.00 28.85 ? 59 VAL A CA 1 ATOM 320 C C . VAL A 1 43 ? 15.533 -0.975 20.461 1.00 30.59 ? 59 VAL A C 1 ATOM 321 O O . VAL A 1 43 ? 15.566 -2.155 20.753 1.00 32.49 ? 59 VAL A O 1 ATOM 322 C CB . VAL A 1 43 ? 13.636 -1.151 18.837 1.00 27.25 ? 59 VAL A CB 1 ATOM 323 C CG1 . VAL A 1 43 ? 12.258 -0.629 18.525 1.00 26.34 ? 59 VAL A CG1 1 ATOM 324 C CG2 . VAL A 1 43 ? 14.500 -1.116 17.635 1.00 28.35 ? 59 VAL A CG2 1 ATOM 325 N N . ALA A 1 44 ? 16.585 -0.170 20.561 1.00 30.32 ? 60 ALA A N 1 ATOM 326 C CA . ALA A 1 44 ? 17.854 -0.717 20.993 1.00 32.28 ? 60 ALA A CA 1 ATOM 327 C C . ALA A 1 44 ? 17.917 -1.344 22.416 1.00 32.57 ? 60 ALA A C 1 ATOM 328 O O . ALA A 1 44 ? 18.489 -2.401 22.604 1.00 31.03 ? 60 ALA A O 1 ATOM 329 C CB . ALA A 1 44 ? 18.920 0.285 20.838 1.00 32.31 ? 60 ALA A CB 1 ATOM 330 N N . ASN A 1 45 ? 17.368 -0.745 23.456 1.00 34.63 ? 61 ASN A N 1 ATOM 331 C CA . ASN A 1 45 ? 17.613 -1.516 24.712 1.00 37.20 ? 61 ASN A CA 1 ATOM 332 C C . ASN A 1 45 ? 16.306 -1.835 25.391 1.00 36.36 ? 61 ASN A C 1 ATOM 333 O O . ASN A 1 45 ? 16.014 -1.357 26.482 1.00 36.43 ? 61 ASN A O 1 ATOM 334 C CB . ASN A 1 45 ? 18.754 -0.865 25.579 1.00 38.45 ? 61 ASN A CB 1 ATOM 335 C CG . ASN A 1 45 ? 19.194 -1.710 26.847 1.00 41.54 ? 61 ASN A CG 1 ATOM 336 O OD1 . ASN A 1 45 ? 19.529 -2.919 26.818 1.00 40.99 ? 61 ASN A OD1 1 ATOM 337 N ND2 . ASN A 1 45 ? 19.182 -1.024 27.983 1.00 49.84 ? 61 ASN A ND2 1 ATOM 338 N N . VAL A 1 46 ? 15.486 -2.588 24.662 1.00 34.88 ? 62 VAL A N 1 ATOM 339 C CA . VAL A 1 46 ? 14.201 -3.003 25.164 1.00 35.12 ? 62 VAL A CA 1 ATOM 340 C C . VAL A 1 46 ? 14.000 -4.406 24.655 1.00 34.20 ? 62 VAL A C 1 ATOM 341 O O . VAL A 1 46 ? 14.680 -4.825 23.714 1.00 35.01 ? 62 VAL A O 1 ATOM 342 C CB . VAL A 1 46 ? 13.011 -2.102 24.733 1.00 34.74 ? 62 VAL A CB 1 ATOM 343 C CG1 . VAL A 1 46 ? 13.130 -0.653 25.319 1.00 37.54 ? 62 VAL A CG1 1 ATOM 344 C CG2 . VAL A 1 46 ? 12.841 -2.042 23.206 1.00 36.00 ? 62 VAL A CG2 1 ATOM 345 N N . ASN A 1 47 A 13.136 -5.144 25.320 1.00 31.76 ? 62 ASN A N 1 ATOM 346 C CA . ASN A 1 47 A 12.723 -6.471 24.847 1.00 30.96 ? 62 ASN A CA 1 ATOM 347 C C . ASN A 1 47 A 11.620 -6.256 23.802 1.00 29.17 ? 62 ASN A C 1 ATOM 348 O O . ASN A 1 47 A 10.477 -5.904 24.124 1.00 27.26 ? 62 ASN A O 1 ATOM 349 C CB . ASN A 1 47 A 12.204 -7.259 26.054 1.00 32.35 ? 62 ASN A CB 1 ATOM 350 C CG . ASN A 1 47 A 11.598 -8.593 25.671 1.00 36.87 ? 62 ASN A CG 1 ATOM 351 O OD1 . ASN A 1 47 A 10.839 -9.185 26.472 1.00 45.51 ? 62 ASN A OD1 1 ATOM 352 N ND2 . ASN A 1 47 A 11.879 -9.065 24.442 1.00 31.00 ? 62 ASN A ND2 1 ATOM 353 N N . VAL A 1 48 B 11.980 -6.393 22.549 1.00 30.20 ? 62 VAL A N 1 ATOM 354 C CA . VAL A 1 48 B 11.058 -6.106 21.472 1.00 32.74 ? 62 VAL A CA 1 ATOM 355 C C . VAL A 1 48 B 9.838 -7.021 21.450 1.00 33.60 ? 62 VAL A C 1 ATOM 356 O O . VAL A 1 48 B 8.775 -6.627 20.932 1.00 31.48 ? 62 VAL A O 1 ATOM 357 C CB . VAL A 1 48 B 11.757 -6.188 20.154 1.00 34.10 ? 62 VAL A CB 1 ATOM 358 C CG1 . VAL A 1 48 B 10.771 -6.127 19.013 1.00 34.61 ? 62 VAL A CG1 1 ATOM 359 C CG2 . VAL A 1 48 B 12.780 -5.054 20.067 1.00 35.91 ? 62 VAL A CG2 1 ATOM 360 N N . ARG A 1 49 ? 9.956 -8.199 22.092 1.00 33.65 ? 63 ARG A N 1 ATOM 361 C CA . ARG A 1 49 ? 8.804 -9.120 22.157 1.00 34.51 ? 63 ARG A CA 1 ATOM 362 C C . ARG A 1 49 ? 7.690 -8.528 22.887 1.00 33.62 ? 63 ARG A C 1 ATOM 363 O O . ARG A 1 49 ? 6.532 -8.866 22.672 1.00 36.74 ? 63 ARG A O 1 ATOM 364 C CB . ARG A 1 49 ? 9.156 -10.468 22.868 1.00 35.43 ? 63 ARG A CB 1 ATOM 365 C CG . ARG A 1 49 ? 9.787 -11.489 21.947 1.00 40.22 ? 63 ARG A CG 1 ATOM 366 C CD . ARG A 1 49 ? 9.863 -12.930 22.520 1.00 47.99 ? 63 ARG A CD 1 ATOM 367 N NE . ARG A 1 49 ? 8.612 -13.678 22.282 1.00 55.66 ? 63 ARG A NE 1 ATOM 368 C CZ . ARG A 1 49 ? 8.468 -15.012 22.403 1.00 57.59 ? 63 ARG A CZ 1 ATOM 369 N NH1 . ARG A 1 49 ? 7.295 -15.583 22.148 1.00 60.50 ? 63 ARG A NH1 1 ATOM 370 N NH2 . ARG A 1 49 ? 9.496 -15.778 22.766 1.00 60.18 ? 63 ARG A NH2 1 ATOM 371 N N . ALA A 1 50 ? 8.003 -7.616 23.773 1.00 32.91 ? 64 ALA A N 1 ATOM 372 C CA . ALA A 1 50 ? 6.997 -6.971 24.586 1.00 31.58 ? 64 ALA A CA 1 ATOM 373 C C . ALA A 1 50 ? 6.559 -5.624 24.010 1.00 31.37 ? 64 ALA A C 1 ATOM 374 O O . ALA A 1 50 ? 5.864 -4.869 24.649 1.00 31.49 ? 64 ALA A O 1 ATOM 375 C CB . ALA A 1 50 ? 7.561 -6.756 25.975 1.00 31.14 ? 64 ALA A CB 1 ATOM 376 N N . VAL A 1 51 ? 6.997 -5.275 22.826 1.00 32.83 ? 65 VAL A N 1 ATOM 377 C CA . VAL A 1 51 ? 6.639 -3.961 22.303 1.00 30.45 ? 65 VAL A CA 1 ATOM 378 C C . VAL A 1 51 ? 5.309 -4.017 21.576 1.00 31.12 ? 65 VAL A C 1 ATOM 379 O O . VAL A 1 51 ? 5.052 -4.935 20.794 1.00 32.17 ? 65 VAL A O 1 ATOM 380 C CB . VAL A 1 51 ? 7.741 -3.460 21.341 1.00 31.41 ? 65 VAL A CB 1 ATOM 381 C CG1 . VAL A 1 51 ? 7.288 -2.135 20.591 1.00 27.53 ? 65 VAL A CG1 1 ATOM 382 C CG2 . VAL A 1 51 ? 9.043 -3.207 22.103 1.00 31.08 ? 65 VAL A CG2 1 ATOM 383 N N . ARG A 1 52 A 4.421 -3.083 21.858 1.00 29.97 ? 65 ARG A N 1 ATOM 384 C CA . ARG A 1 52 A 3.151 -3.039 21.178 1.00 29.18 ? 65 ARG A CA 1 ATOM 385 C C . ARG A 1 52 A 3.169 -1.849 20.251 1.00 29.85 ? 65 ARG A C 1 ATOM 386 O O . ARG A 1 52 A 3.560 -0.720 20.642 1.00 28.72 ? 65 ARG A O 1 ATOM 387 C CB . ARG A 1 52 A 2.003 -2.898 22.187 1.00 30.88 ? 65 ARG A CB 1 ATOM 388 C CG . ARG A 1 52 A 1.649 -4.183 22.994 1.00 33.69 ? 65 ARG A CG 1 ATOM 389 C CD . ARG A 1 52 A 0.874 -3.868 24.340 1.00 46.38 ? 65 ARG A CD 1 ATOM 390 N NE . ARG A 1 52 A 0.570 -5.055 25.151 1.00 55.08 ? 65 ARG A NE 1 ATOM 391 C CZ . ARG A 1 52 A -0.060 -5.053 26.339 1.00 59.04 ? 65 ARG A CZ 1 ATOM 392 N NH1 . ARG A 1 52 A -0.263 -6.209 26.958 1.00 63.56 ? 65 ARG A NH1 1 ATOM 393 N NH2 . ARG A 1 52 A -0.476 -3.923 26.914 1.00 60.56 ? 65 ARG A NH2 1 ATOM 394 N N . VAL A 1 53 ? 2.761 -2.079 19.009 1.00 28.15 ? 66 VAL A N 1 ATOM 395 C CA . VAL A 1 53 ? 2.717 -0.996 18.022 1.00 28.18 ? 66 VAL A CA 1 ATOM 396 C C . VAL A 1 53 ? 1.272 -0.524 17.985 1.00 29.44 ? 66 VAL A C 1 ATOM 397 O O . VAL A 1 53 ? 0.430 -1.271 17.521 1.00 29.49 ? 66 VAL A O 1 ATOM 398 C CB . VAL A 1 53 ? 3.133 -1.567 16.700 1.00 28.66 ? 66 VAL A CB 1 ATOM 399 C CG1 . VAL A 1 53 ? 3.063 -0.540 15.564 1.00 25.80 ? 66 VAL A CG1 1 ATOM 400 C CG2 . VAL A 1 53 ? 4.527 -2.114 16.842 1.00 26.85 ? 66 VAL A CG2 1 ATOM 401 N N . VAL A 1 54 ? 0.974 0.706 18.481 1.00 28.97 ? 67 VAL A N 1 ATOM 402 C CA . VAL A 1 54 ? -0.409 1.149 18.674 1.00 30.60 ? 67 VAL A CA 1 ATOM 403 C C . VAL A 1 54 ? -0.844 2.207 17.630 1.00 32.88 ? 67 VAL A C 1 ATOM 404 O O . VAL A 1 54 ? -0.334 3.348 17.565 1.00 31.11 ? 67 VAL A O 1 ATOM 405 C CB . VAL A 1 54 ? -0.619 1.640 20.151 1.00 31.36 ? 67 VAL A CB 1 ATOM 406 C CG1 . VAL A 1 54 ? -2.050 2.023 20.420 1.00 30.85 ? 67 VAL A CG1 1 ATOM 407 C CG2 . VAL A 1 54 ? -0.145 0.558 21.138 1.00 29.82 ? 67 VAL A CG2 1 ATOM 408 N N . LEU A 1 55 ? -1.862 1.835 16.861 1.00 32.90 ? 68 LEU A N 1 ATOM 409 C CA . LEU A 1 55 ? -2.309 2.639 15.744 1.00 34.84 ? 68 LEU A CA 1 ATOM 410 C C . LEU A 1 55 ? -3.640 3.262 16.132 1.00 34.24 ? 68 LEU A C 1 ATOM 411 O O . LEU A 1 55 ? -4.333 2.759 17.006 1.00 33.23 ? 68 LEU A O 1 ATOM 412 C CB . LEU A 1 55 ? -2.503 1.715 14.537 1.00 34.30 ? 68 LEU A CB 1 ATOM 413 C CG . LEU A 1 55 ? -1.472 1.388 13.472 1.00 36.63 ? 68 LEU A CG 1 ATOM 414 C CD1 . LEU A 1 55 ? -0.023 1.166 13.904 1.00 28.73 ? 68 LEU A CD1 1 ATOM 415 C CD2 . LEU A 1 55 ? -2.001 0.210 12.556 1.00 35.79 ? 68 LEU A CD2 1 ATOM 416 N N . GLY A 1 56 ? -3.942 4.391 15.498 1.00 34.28 ? 69 GLY A N 1 ATOM 417 C CA . GLY A 1 56 ? -5.177 5.112 15.716 1.00 33.91 ? 69 GLY A CA 1 ATOM 418 C C . GLY A 1 56 ? -5.350 5.777 17.089 1.00 35.02 ? 69 GLY A C 1 ATOM 419 O O . GLY A 1 56 ? -6.474 6.053 17.529 1.00 33.02 ? 69 GLY A O 1 ATOM 420 N N . ALA A 1 57 ? -4.248 6.069 17.775 1.00 34.83 ? 70 ALA A N 1 ATOM 421 C CA . ALA A 1 57 ? -4.406 6.659 19.133 1.00 36.64 ? 70 ALA A CA 1 ATOM 422 C C . ALA A 1 57 ? -4.482 8.190 19.089 1.00 36.71 ? 70 ALA A C 1 ATOM 423 O O . ALA A 1 57 ? -3.945 8.802 18.140 1.00 36.99 ? 70 ALA A O 1 ATOM 424 C CB . ALA A 1 57 ? -3.226 6.214 20.025 1.00 35.93 ? 70 ALA A CB 1 ATOM 425 N N . HIS A 1 58 ? -5.105 8.790 20.103 1.00 37.34 ? 71 HIS A N 1 ATOM 426 C CA . HIS A 1 58 ? -5.126 10.264 20.289 1.00 38.47 ? 71 HIS A CA 1 ATOM 427 C C . HIS A 1 58 ? -4.670 10.681 21.707 1.00 38.63 ? 71 HIS A C 1 ATOM 428 O O . HIS A 1 58 ? -3.605 11.320 21.883 1.00 37.51 ? 71 HIS A O 1 ATOM 429 C CB . HIS A 1 58 ? -6.522 10.843 20.038 1.00 39.55 ? 71 HIS A CB 1 ATOM 430 C CG . HIS A 1 58 ? -6.609 12.332 20.182 1.00 40.37 ? 71 HIS A CG 1 ATOM 431 N ND1 . HIS A 1 58 ? -5.802 13.195 19.476 1.00 43.70 ? 71 HIS A ND1 1 ATOM 432 C CD2 . HIS A 1 58 ? -7.404 13.108 20.954 1.00 39.58 ? 71 HIS A CD2 1 ATOM 433 C CE1 . HIS A 1 58 ? -6.107 14.440 19.797 1.00 41.38 ? 71 HIS A CE1 1 ATOM 434 N NE2 . HIS A 1 58 ? -7.087 14.412 20.679 1.00 43.17 ? 71 HIS A NE2 1 ATOM 435 N N . ASN A 1 59 ? -5.496 10.332 22.696 1.00 38.78 ? 72 ASN A N 1 ATOM 436 C CA . ASN A 1 59 ? -5.209 10.601 24.110 1.00 38.13 ? 72 ASN A CA 1 ATOM 437 C C . ASN A 1 59 ? -4.737 9.335 24.844 1.00 38.79 ? 72 ASN A C 1 ATOM 438 O O . ASN A 1 59 ? -5.549 8.448 25.084 1.00 38.00 ? 72 ASN A O 1 ATOM 439 C CB . ASN A 1 59 ? -6.456 11.121 24.810 1.00 39.16 ? 72 ASN A CB 1 ATOM 440 C CG . ASN A 1 59 ? -6.207 11.471 26.265 1.00 39.98 ? 72 ASN A CG 1 ATOM 441 O OD1 . ASN A 1 59 ? -5.154 11.173 26.817 1.00 35.31 ? 72 ASN A OD1 1 ATOM 442 N ND2 . ASN A 1 59 ? -7.192 12.120 26.891 1.00 43.42 ? 72 ASN A ND2 1 ATOM 443 N N . LEU A 1 60 ? -3.440 9.265 25.215 1.00 37.42 ? 73 LEU A N 1 ATOM 444 C CA . LEU A 1 60 ? -2.916 8.055 25.865 1.00 38.28 ? 73 LEU A CA 1 ATOM 445 C C . LEU A 1 60 ? -3.494 7.737 27.235 1.00 39.88 ? 73 LEU A C 1 ATOM 446 O O . LEU A 1 60 ? -3.372 6.587 27.688 1.00 40.58 ? 73 LEU A O 1 ATOM 447 C CB . LEU A 1 60 ? -1.373 8.027 25.923 1.00 37.83 ? 73 LEU A CB 1 ATOM 448 C CG . LEU A 1 60 ? -0.554 8.195 24.633 1.00 36.46 ? 73 LEU A CG 1 ATOM 449 C CD1 . LEU A 1 60 ? 0.941 8.167 24.918 1.00 41.23 ? 73 LEU A CD1 1 ATOM 450 C CD2 . LEU A 1 60 ? -0.870 7.164 23.546 1.00 39.48 ? 73 LEU A CD2 1 ATOM 451 N N . SER A 1 61 ? -4.085 8.720 27.922 1.00 40.74 ? 74 SER A N 1 ATOM 452 C CA . SER A 1 61 ? -4.723 8.429 29.213 1.00 43.53 ? 74 SER A CA 1 ATOM 453 C C . SER A 1 61 ? -6.171 8.041 29.059 1.00 44.65 ? 74 SER A C 1 ATOM 454 O O . SER A 1 61 ? -6.921 8.031 30.036 1.00 45.02 ? 74 SER A O 1 ATOM 455 C CB . SER A 1 61 ? -4.652 9.567 30.232 1.00 44.27 ? 74 SER A CB 1 ATOM 456 O OG . SER A 1 61 ? -5.001 10.832 29.695 1.00 48.89 ? 74 SER A OG 1 ATOM 457 N N . ARG A 1 62 ? -6.581 7.731 27.838 1.00 45.94 ? 75 ARG A N 1 ATOM 458 C CA . ARG A 1 62 ? -7.954 7.267 27.626 1.00 47.61 ? 75 ARG A CA 1 ATOM 459 C C . ARG A 1 62 ? -8.054 5.889 26.975 1.00 47.16 ? 75 ARG A C 1 ATOM 460 O O . ARG A 1 62 ? -7.197 5.498 26.202 1.00 47.52 ? 75 ARG A O 1 ATOM 461 C CB . ARG A 1 62 ? -8.753 8.263 26.775 1.00 48.36 ? 75 ARG A CB 1 ATOM 462 C CG . ARG A 1 62 ? -9.210 9.508 27.511 1.00 52.59 ? 75 ARG A CG 1 ATOM 463 C CD . ARG A 1 62 ? -10.398 10.205 26.861 1.00 60.30 ? 75 ARG A CD 1 ATOM 464 N NE . ARG A 1 62 ? -10.623 11.524 27.440 1.00 67.30 ? 75 ARG A NE 1 ATOM 465 C CZ . ARG A 1 62 ? -10.982 12.604 26.751 1.00 71.27 ? 75 ARG A CZ 1 ATOM 466 N NH1 . ARG A 1 62 ? -11.141 13.763 27.378 1.00 73.07 ? 75 ARG A NH1 1 ATOM 467 N NH2 . ARG A 1 62 ? -11.191 12.530 25.439 1.00 73.28 ? 75 ARG A NH2 1 ATOM 468 N N . ARG A 1 63 ? -9.111 5.172 27.304 1.00 48.31 ? 76 ARG A N 1 ATOM 469 C CA . ARG A 1 63 ? -9.484 3.958 26.619 1.00 49.66 ? 76 ARG A CA 1 ATOM 470 C C . ARG A 1 63 ? -9.869 4.505 25.249 1.00 49.52 ? 76 ARG A C 1 ATOM 471 O O . ARG A 1 63 ? -10.531 5.541 25.146 1.00 50.06 ? 76 ARG A O 1 ATOM 472 C CB . ARG A 1 63 ? -10.756 3.433 27.247 1.00 50.73 ? 76 ARG A CB 1 ATOM 473 C CG . ARG A 1 63 ? -10.815 1.955 27.516 1.00 54.94 ? 76 ARG A CG 1 ATOM 474 C CD . ARG A 1 63 ? -10.691 1.649 28.983 1.00 63.96 ? 76 ARG A CD 1 ATOM 475 N NE . ARG A 1 63 ? -10.877 0.235 29.255 1.00 68.65 ? 76 ARG A NE 1 ATOM 476 C CZ . ARG A 1 63 ? -10.630 -0.325 30.429 1.00 73.24 ? 76 ARG A CZ 1 ATOM 477 N NH1 . ARG A 1 63 ? -10.824 -1.635 30.596 1.00 75.01 ? 76 ARG A NH1 1 ATOM 478 N NH2 . ARG A 1 63 ? -10.181 0.424 31.440 1.00 73.60 ? 76 ARG A NH2 1 ATOM 479 N N . GLU A 1 64 ? -9.438 3.856 24.191 1.00 48.76 ? 77 GLU A N 1 ATOM 480 C CA . GLU A 1 64 ? -9.768 4.351 22.864 1.00 48.00 ? 77 GLU A CA 1 ATOM 481 C C . GLU A 1 64 ? -10.050 3.217 21.880 1.00 47.18 ? 77 GLU A C 1 ATOM 482 O O . GLU A 1 64 ? -9.140 2.537 21.420 1.00 47.03 ? 77 GLU A O 1 ATOM 483 C CB . GLU A 1 64 ? -8.673 5.267 22.314 1.00 48.06 ? 77 GLU A CB 1 ATOM 484 C CG . GLU A 1 64 ? -8.405 6.505 23.167 1.00 47.54 ? 77 GLU A CG 1 ATOM 485 C CD . GLU A 1 64 ? -7.499 7.502 22.470 1.00 45.71 ? 77 GLU A CD 1 ATOM 486 O OE1 . GLU A 1 64 ? -7.849 8.694 22.464 1.00 45.66 ? 77 GLU A OE1 1 ATOM 487 O OE2 . GLU A 1 64 ? -6.455 7.098 21.923 1.00 39.00 ? 77 GLU A OE2 1 ATOM 488 N N . PRO A 1 65 ? -11.334 3.027 21.581 1.00 46.91 ? 78 PRO A N 1 ATOM 489 C CA . PRO A 1 65 ? -11.798 2.050 20.584 1.00 45.56 ? 78 PRO A CA 1 ATOM 490 C C . PRO A 1 65 ? -11.277 2.287 19.159 1.00 45.68 ? 78 PRO A C 1 ATOM 491 O O . PRO A 1 65 ? -11.207 1.352 18.347 1.00 45.65 ? 78 PRO A O 1 ATOM 492 C CB . PRO A 1 65 ? -13.314 2.191 20.656 1.00 46.91 ? 78 PRO A CB 1 ATOM 493 C CG . PRO A 1 65 ? -13.564 2.711 22.098 1.00 47.57 ? 78 PRO A CG 1 ATOM 494 C CD . PRO A 1 65 ? -12.439 3.700 22.289 1.00 46.54 ? 78 PRO A CD 1 ATOM 495 N N . THR A 1 66 ? -10.907 3.511 18.813 1.00 44.42 ? 79 THR A N 1 ATOM 496 C CA . THR A 1 66 ? -10.304 3.691 17.500 1.00 44.32 ? 79 THR A CA 1 ATOM 497 C C . THR A 1 66 ? -8.953 2.941 17.381 1.00 43.31 ? 79 THR A C 1 ATOM 498 O O . THR A 1 66 ? -8.452 2.812 16.274 1.00 43.47 ? 79 THR A O 1 ATOM 499 C CB . THR A 1 66 ? -10.032 5.176 17.192 1.00 44.70 ? 79 THR A CB 1 ATOM 500 O OG1 . THR A 1 66 ? -9.360 5.787 18.315 1.00 46.96 ? 79 THR A OG1 1 ATOM 501 C CG2 . THR A 1 66 ? -11.334 5.976 17.075 1.00 45.16 ? 79 THR A CG2 1 ATOM 502 N N . ARG A 1 67 ? -8.345 2.451 18.474 1.00 40.98 ? 80 ARG A N 1 ATOM 503 C CA . ARG A 1 67 ? -6.973 1.876 18.342 1.00 40.24 ? 80 ARG A CA 1 ATOM 504 C C . ARG A 1 67 ? -6.785 0.476 17.693 1.00 39.49 ? 80 ARG A C 1 ATOM 505 O O . ARG A 1 67 ? -7.585 -0.443 17.896 1.00 40.99 ? 80 ARG A O 1 ATOM 506 C CB . ARG A 1 67 ? -6.245 1.826 19.709 1.00 39.73 ? 80 ARG A CB 1 ATOM 507 C CG . ARG A 1 67 ? -5.956 3.183 20.334 1.00 38.57 ? 80 ARG A CG 1 ATOM 508 C CD . ARG A 1 67 ? -5.353 3.077 21.726 1.00 40.61 ? 80 ARG A CD 1 ATOM 509 N NE . ARG A 1 67 ? -5.443 4.344 22.444 1.00 44.07 ? 80 ARG A NE 1 ATOM 510 C CZ . ARG A 1 67 ? -4.825 4.598 23.594 1.00 44.93 ? 80 ARG A CZ 1 ATOM 511 N NH1 . ARG A 1 67 ? -4.034 3.670 24.119 1.00 42.59 ? 80 ARG A NH1 1 ATOM 512 N NH2 . ARG A 1 67 ? -4.962 5.798 24.184 1.00 39.25 ? 80 ARG A NH2 1 ATOM 513 N N . GLN A 1 68 ? -5.700 0.305 16.949 1.00 38.55 ? 81 GLN A N 1 ATOM 514 C CA . GLN A 1 68 ? -5.336 -1.034 16.445 1.00 37.73 ? 81 GLN A CA 1 ATOM 515 C C . GLN A 1 68 ? -3.942 -1.352 17.003 1.00 36.05 ? 81 GLN A C 1 ATOM 516 O O . GLN A 1 68 ? -3.070 -0.523 16.894 1.00 34.62 ? 81 GLN A O 1 ATOM 517 C CB . GLN A 1 68 ? -5.342 -1.108 14.917 1.00 37.28 ? 81 GLN A CB 1 ATOM 518 C CG . GLN A 1 68 ? -6.757 -1.345 14.296 1.00 38.38 ? 81 GLN A CG 1 ATOM 519 C CD . GLN A 1 68 ? -6.739 -1.138 12.783 1.00 38.26 ? 81 GLN A CD 1 ATOM 520 O OE1 . GLN A 1 68 ? -6.278 -1.988 12.049 1.00 41.92 ? 81 GLN A OE1 1 ATOM 521 N NE2 . GLN A 1 68 ? -7.186 0.021 12.329 1.00 39.84 ? 81 GLN A NE2 1 ATOM 522 N N . VAL A 1 69 ? -3.769 -2.555 17.569 1.00 34.71 ? 82 VAL A N 1 ATOM 523 C CA . VAL A 1 69 ? -2.512 -2.969 18.225 1.00 33.85 ? 82 VAL A CA 1 ATOM 524 C C . VAL A 1 69 ? -1.907 -4.205 17.615 1.00 33.97 ? 82 VAL A C 1 ATOM 525 O O . VAL A 1 69 ? -2.568 -5.248 17.592 1.00 35.01 ? 82 VAL A O 1 ATOM 526 C CB . VAL A 1 69 ? -2.710 -3.310 19.722 1.00 33.37 ? 82 VAL A CB 1 ATOM 527 C CG1 . VAL A 1 69 ? -1.343 -3.609 20.377 1.00 33.90 ? 82 VAL A CG1 1 ATOM 528 C CG2 . VAL A 1 69 ? -3.431 -2.184 20.473 1.00 34.42 ? 82 VAL A CG2 1 ATOM 529 N N . PHE A 1 70 ? -0.641 -4.095 17.191 1.00 32.84 ? 83 PHE A N 1 ATOM 530 C CA . PHE A 1 70 ? 0.102 -5.162 16.553 1.00 33.68 ? 83 PHE A CA 1 ATOM 531 C C . PHE A 1 70 ? 1.435 -5.373 17.308 1.00 33.03 ? 83 PHE A C 1 ATOM 532 O O . PHE A 1 70 ? 1.800 -4.579 18.213 1.00 32.65 ? 83 PHE A O 1 ATOM 533 C CB . PHE A 1 70 ? 0.377 -4.803 15.067 1.00 32.92 ? 83 PHE A CB 1 ATOM 534 C CG . PHE A 1 70 ? -0.911 -4.688 14.224 1.00 38.50 ? 83 PHE A CG 1 ATOM 535 C CD1 . PHE A 1 70 ? -1.653 -3.514 14.216 1.00 38.96 ? 83 PHE A CD1 1 ATOM 536 C CD2 . PHE A 1 70 ? -1.401 -5.800 13.524 1.00 34.98 ? 83 PHE A CD2 1 ATOM 537 C CE1 . PHE A 1 70 ? -2.816 -3.416 13.469 1.00 44.05 ? 83 PHE A CE1 1 ATOM 538 C CE2 . PHE A 1 70 ? -2.546 -5.714 12.811 1.00 41.51 ? 83 PHE A CE2 1 ATOM 539 C CZ . PHE A 1 70 ? -3.281 -4.512 12.779 1.00 43.98 ? 83 PHE A CZ 1 ATOM 540 N N . ALA A 1 71 ? 2.128 -6.445 16.944 1.00 31.44 ? 84 ALA A N 1 ATOM 541 C CA . ALA A 1 71 ? 3.448 -6.705 17.465 1.00 31.05 ? 84 ALA A CA 1 ATOM 542 C C . ALA A 1 71 ? 4.402 -6.658 16.323 1.00 30.38 ? 84 ALA A C 1 ATOM 543 O O . ALA A 1 71 ? 4.023 -6.661 15.138 1.00 30.21 ? 84 ALA A O 1 ATOM 544 C CB . ALA A 1 71 ? 3.514 -8.094 18.149 1.00 32.94 ? 84 ALA A CB 1 ATOM 545 N N . VAL A 1 72 ? 5.658 -6.683 16.679 1.00 29.17 ? 85 VAL A N 1 ATOM 546 C CA . VAL A 1 72 ? 6.679 -6.649 15.717 1.00 29.78 ? 85 VAL A CA 1 ATOM 547 C C . VAL A 1 72 ? 6.923 -8.142 15.290 1.00 30.77 ? 85 VAL A C 1 ATOM 548 O O . VAL A 1 72 ? 7.128 -9.015 16.135 1.00 28.71 ? 85 VAL A O 1 ATOM 549 C CB . VAL A 1 72 ? 7.940 -6.101 16.364 1.00 29.58 ? 85 VAL A CB 1 ATOM 550 C CG1 . VAL A 1 72 ? 9.117 -6.137 15.383 1.00 29.38 ? 85 VAL A CG1 1 ATOM 551 C CG2 . VAL A 1 72 ? 7.686 -4.673 16.914 1.00 32.40 ? 85 VAL A CG2 1 ATOM 552 N N . GLN A 1 73 ? 6.871 -8.381 13.981 1.00 31.58 ? 86 GLN A N 1 ATOM 553 C CA . GLN A 1 73 ? 7.245 -9.655 13.422 1.00 34.19 ? 86 GLN A CA 1 ATOM 554 C C . GLN A 1 73 ? 8.655 -9.638 12.812 1.00 33.78 ? 86 GLN A C 1 ATOM 555 O O . GLN A 1 73 ? 9.370 -10.655 12.889 1.00 34.61 ? 86 GLN A O 1 ATOM 556 C CB . GLN A 1 73 ? 6.191 -10.067 12.404 1.00 35.69 ? 86 GLN A CB 1 ATOM 557 C CG . GLN A 1 73 ? 6.530 -11.290 11.561 1.00 38.81 ? 86 GLN A CG 1 ATOM 558 C CD . GLN A 1 73 ? 5.338 -11.725 10.785 1.00 43.01 ? 86 GLN A CD 1 ATOM 559 O OE1 . GLN A 1 73 ? 5.351 -11.703 9.555 1.00 47.23 ? 86 GLN A OE1 1 ATOM 560 N NE2 . GLN A 1 73 ? 4.266 -12.047 11.496 1.00 40.69 ? 86 GLN A NE2 1 ATOM 561 N N . ARG A 1 74 ? 9.111 -8.511 12.216 1.00 33.33 ? 87 ARG A N 1 ATOM 562 C CA . ARG A 1 74 ? 10.500 -8.462 11.666 1.00 31.51 ? 87 ARG A CA 1 ATOM 563 C C . ARG A 1 74 ? 11.328 -7.161 11.797 1.00 31.79 ? 87 ARG A C 1 ATOM 564 O O . ARG A 1 74 ? 10.801 -6.124 11.674 1.00 29.99 ? 87 ARG A O 1 ATOM 565 C CB . ARG A 1 74 ? 10.481 -8.768 10.185 1.00 31.98 ? 87 ARG A CB 1 ATOM 566 C CG . ARG A 1 74 ? 10.308 -10.283 9.910 1.00 36.44 ? 87 ARG A CG 1 ATOM 567 C CD . ARG A 1 74 ? 10.049 -10.656 8.477 1.00 47.47 ? 87 ARG A CD 1 ATOM 568 N NE . ARG A 1 74 ? 9.488 -12.004 8.483 1.00 55.66 ? 87 ARG A NE 1 ATOM 569 C CZ . ARG A 1 74 ? 9.213 -12.738 7.423 1.00 60.36 ? 87 ARG A CZ 1 ATOM 570 N NH1 . ARG A 1 74 ? 9.457 -12.284 6.195 1.00 63.18 ? 87 ARG A NH1 1 ATOM 571 N NH2 . ARG A 1 74 ? 8.684 -13.948 7.604 1.00 61.52 ? 87 ARG A NH2 1 ATOM 572 N N . ILE A 1 75 ? 12.651 -7.229 11.815 1.00 31.43 ? 88 ILE A N 1 ATOM 573 C CA . ILE A 1 75 ? 13.352 -5.991 12.027 1.00 30.85 ? 88 ILE A CA 1 ATOM 574 C C . ILE A 1 75 ? 14.372 -5.774 10.965 1.00 30.09 ? 88 ILE A C 1 ATOM 575 O O . ILE A 1 75 ? 15.164 -6.668 10.673 1.00 31.14 ? 88 ILE A O 1 ATOM 576 C CB . ILE A 1 75 ? 13.992 -6.003 13.448 1.00 30.44 ? 88 ILE A CB 1 ATOM 577 C CG1 . ILE A 1 75 ? 12.926 -6.134 14.537 1.00 29.47 ? 88 ILE A CG1 1 ATOM 578 C CG2 . ILE A 1 75 ? 14.839 -4.755 13.690 1.00 31.23 ? 88 ILE A CG2 1 ATOM 579 C CD1 . ILE A 1 75 ? 13.506 -6.413 15.948 1.00 27.63 ? 88 ILE A CD1 1 ATOM 580 N N . PHE A 1 76 ? 14.440 -4.538 10.461 1.00 29.43 ? 89 PHE A N 1 ATOM 581 C CA . PHE A 1 76 ? 15.416 -4.145 9.449 1.00 28.04 ? 89 PHE A CA 1 ATOM 582 C C . PHE A 1 76 ? 16.163 -2.840 9.804 1.00 29.09 ? 89 PHE A C 1 ATOM 583 O O . PHE A 1 76 ? 15.500 -1.862 10.051 1.00 25.71 ? 89 PHE A O 1 ATOM 584 C CB . PHE A 1 76 ? 14.651 -3.826 8.148 1.00 28.74 ? 89 PHE A CB 1 ATOM 585 C CG . PHE A 1 76 ? 13.801 -4.971 7.587 1.00 24.97 ? 89 PHE A CG 1 ATOM 586 C CD1 . PHE A 1 76 ? 14.319 -5.810 6.614 1.00 31.55 ? 89 PHE A CD1 1 ATOM 587 C CD2 . PHE A 1 76 ? 12.476 -5.134 7.969 1.00 24.16 ? 89 PHE A CD2 1 ATOM 588 C CE1 . PHE A 1 76 ? 13.541 -6.863 6.089 1.00 29.21 ? 89 PHE A CE1 1 ATOM 589 C CE2 . PHE A 1 76 ? 11.678 -6.159 7.459 1.00 33.31 ? 89 PHE A CE2 1 ATOM 590 C CZ . PHE A 1 76 ? 12.183 -7.007 6.502 1.00 27.42 ? 89 PHE A CZ 1 ATOM 591 N N . GLU A 1 77 ? 17.512 -2.815 9.760 1.00 28.63 ? 90 GLU A N 1 ATOM 592 C CA . GLU A 1 77 ? 18.280 -1.640 10.097 1.00 32.09 ? 90 GLU A CA 1 ATOM 593 C C . GLU A 1 77 ? 19.368 -1.590 9.040 1.00 32.48 ? 90 GLU A C 1 ATOM 594 O O . GLU A 1 77 ? 19.807 -2.644 8.547 1.00 31.12 ? 90 GLU A O 1 ATOM 595 C CB . GLU A 1 77 ? 18.937 -1.731 11.512 1.00 29.35 ? 90 GLU A CB 1 ATOM 596 C CG . GLU A 1 77 ? 17.910 -1.528 12.620 1.00 32.69 ? 90 GLU A CG 1 ATOM 597 C CD . GLU A 1 77 ? 18.488 -1.611 14.019 1.00 23.89 ? 90 GLU A CD 1 ATOM 598 O OE1 . GLU A 1 77 ? 17.726 -1.487 14.980 1.00 33.74 ? 90 GLU A OE1 1 ATOM 599 O OE2 . GLU A 1 77 ? 19.689 -1.859 14.165 1.00 32.91 ? 90 GLU A OE2 1 ATOM 600 N N . ASN A 1 78 ? 19.819 -0.381 8.718 1.00 32.14 ? 91 ASN A N 1 ATOM 601 C CA . ASN A 1 78 ? 20.806 -0.253 7.642 1.00 32.64 ? 91 ASN A CA 1 ATOM 602 C C . ASN A 1 78 ? 21.916 0.705 7.982 1.00 33.27 ? 91 ASN A C 1 ATOM 603 O O . ASN A 1 78 ? 21.911 1.886 7.588 1.00 32.51 ? 91 ASN A O 1 ATOM 604 C CB . ASN A 1 78 ? 20.069 0.086 6.363 1.00 33.72 ? 91 ASN A CB 1 ATOM 605 C CG . ASN A 1 78 ? 20.991 0.352 5.177 1.00 32.31 ? 91 ASN A CG 1 ATOM 606 O OD1 . ASN A 1 78 ? 20.444 0.763 4.158 1.00 33.66 ? 91 ASN A OD1 1 ATOM 607 N ND2 . ASN A 1 78 ? 22.223 0.249 5.180 1.00 31.70 ? 91 ASN A ND2 1 ATOM 608 N N . GLY A 1 79 ? 22.838 0.208 8.788 1.00 32.64 ? 92 GLY A N 1 ATOM 609 C CA . GLY A 1 79 ? 23.995 0.986 9.164 1.00 34.40 ? 92 GLY A CA 1 ATOM 610 C C . GLY A 1 79 ? 23.784 1.946 10.339 1.00 34.94 ? 92 GLY A C 1 ATOM 611 O O . GLY A 1 79 ? 24.460 2.975 10.441 1.00 36.11 ? 92 GLY A O 1 ATOM 612 N N . TYR A 1 80 ? 22.866 1.597 11.233 1.00 34.80 ? 94 TYR A N 1 ATOM 613 C CA . TYR A 1 80 ? 22.616 2.415 12.436 1.00 33.48 ? 94 TYR A CA 1 ATOM 614 C C . TYR A 1 80 ? 23.892 2.446 13.279 1.00 32.11 ? 94 TYR A C 1 ATOM 615 O O . TYR A 1 80 ? 24.473 1.402 13.587 1.00 31.37 ? 94 TYR A O 1 ATOM 616 C CB . TYR A 1 80 ? 21.408 1.849 13.212 1.00 32.20 ? 94 TYR A CB 1 ATOM 617 C CG . TYR A 1 80 ? 21.306 2.314 14.667 1.00 33.90 ? 94 TYR A CG 1 ATOM 618 C CD1 . TYR A 1 80 ? 21.244 1.397 15.723 1.00 26.28 ? 94 TYR A CD1 1 ATOM 619 C CD2 . TYR A 1 80 ? 21.151 3.679 14.969 1.00 28.79 ? 94 TYR A CD2 1 ATOM 620 C CE1 . TYR A 1 80 ? 21.118 1.841 17.072 1.00 27.36 ? 94 TYR A CE1 1 ATOM 621 C CE2 . TYR A 1 80 ? 21.041 4.122 16.287 1.00 27.49 ? 94 TYR A CE2 1 ATOM 622 C CZ . TYR A 1 80 ? 21.021 3.225 17.313 1.00 30.27 ? 94 TYR A CZ 1 ATOM 623 O OH . TYR A 1 80 ? 20.918 3.724 18.561 1.00 32.19 ? 94 TYR A OH 1 ATOM 624 N N . ASP A 1 81 ? 24.329 3.650 13.655 1.00 31.18 ? 95 ASP A N 1 ATOM 625 C CA . ASP A 1 81 ? 25.544 3.873 14.436 1.00 31.19 ? 95 ASP A CA 1 ATOM 626 C C . ASP A 1 81 ? 25.105 4.286 15.850 1.00 33.16 ? 95 ASP A C 1 ATOM 627 O O . ASP A 1 81 ? 24.593 5.409 16.071 1.00 31.39 ? 95 ASP A O 1 ATOM 628 C CB . ASP A 1 81 ? 26.364 5.032 13.796 1.00 31.38 ? 95 ASP A CB 1 ATOM 629 C CG . ASP A 1 81 ? 27.640 5.277 14.475 1.00 29.27 ? 95 ASP A CG 1 ATOM 630 O OD1 . ASP A 1 81 ? 27.711 5.110 15.712 1.00 33.02 ? 95 ASP A OD1 1 ATOM 631 O OD2 . ASP A 1 81 ? 28.687 5.542 13.865 1.00 29.62 ? 95 ASP A OD2 1 ATOM 632 N N . PRO A 1 82 ? 25.287 3.387 16.797 1.00 33.44 ? 98 PRO A N 1 ATOM 633 C CA . PRO A 1 82 ? 24.776 3.594 18.137 1.00 33.62 ? 98 PRO A CA 1 ATOM 634 C C . PRO A 1 82 ? 25.565 4.609 18.886 1.00 33.93 ? 98 PRO A C 1 ATOM 635 O O . PRO A 1 82 ? 25.088 5.023 19.938 1.00 32.65 ? 98 PRO A O 1 ATOM 636 C CB . PRO A 1 82 ? 25.012 2.219 18.775 1.00 32.37 ? 98 PRO A CB 1 ATOM 637 C CG . PRO A 1 82 ? 26.168 1.737 18.068 1.00 33.77 ? 98 PRO A CG 1 ATOM 638 C CD . PRO A 1 82 ? 25.910 2.062 16.666 1.00 33.06 ? 98 PRO A CD 1 ATOM 639 N N . VAL A 1 83 ? 26.788 4.907 18.428 1.00 35.08 ? 99 VAL A N 1 ATOM 640 C CA . VAL A 1 83 ? 27.629 5.862 19.124 1.00 34.41 ? 99 VAL A CA 1 ATOM 641 C C . VAL A 1 83 ? 27.206 7.298 18.767 1.00 35.06 ? 99 VAL A C 1 ATOM 642 O O . VAL A 1 83 ? 27.150 8.146 19.639 1.00 36.12 ? 99 VAL A O 1 ATOM 643 C CB . VAL A 1 83 ? 29.148 5.687 18.810 1.00 35.62 ? 99 VAL A CB 1 ATOM 644 C CG1 . VAL A 1 83 ? 29.952 6.780 19.475 1.00 34.45 ? 99 VAL A CG1 1 ATOM 645 C CG2 . VAL A 1 83 ? 29.724 4.291 19.287 1.00 34.53 ? 99 VAL A CG2 1 ATOM 646 N N . ASN A 1 84 A 26.816 7.581 17.529 1.00 34.94 ? 99 ASN A N 1 ATOM 647 C CA . ASN A 1 84 A 26.467 8.996 17.220 1.00 35.93 ? 99 ASN A CA 1 ATOM 648 C C . ASN A 1 84 A 25.120 9.183 16.614 1.00 33.51 ? 99 ASN A C 1 ATOM 649 O O . ASN A 1 84 A 24.760 10.271 16.202 1.00 33.45 ? 99 ASN A O 1 ATOM 650 C CB . ASN A 1 84 A 27.506 9.636 16.292 1.00 36.58 ? 99 ASN A CB 1 ATOM 651 C CG . ASN A 1 84 A 27.626 8.885 14.969 1.00 40.39 ? 99 ASN A CG 1 ATOM 652 O OD1 . ASN A 1 84 A 26.961 7.905 14.780 1.00 41.18 ? 99 ASN A OD1 1 ATOM 653 N ND2 . ASN A 1 84 A 28.503 9.349 14.063 1.00 44.78 ? 99 ASN A ND2 1 ATOM 654 N N . LEU A 1 85 B 24.370 8.100 16.507 1.00 31.36 ? 99 LEU A N 1 ATOM 655 C CA . LEU A 1 85 B 23.012 8.156 15.932 1.00 29.40 ? 99 LEU A CA 1 ATOM 656 C C . LEU A 1 85 B 22.862 8.376 14.417 1.00 27.23 ? 99 LEU A C 1 ATOM 657 O O . LEU A 1 85 B 21.791 8.566 13.887 1.00 24.91 ? 99 LEU A O 1 ATOM 658 C CB . LEU A 1 85 B 22.065 9.015 16.793 1.00 28.39 ? 99 LEU A CB 1 ATOM 659 C CG . LEU A 1 85 B 22.175 8.826 18.338 1.00 32.97 ? 99 LEU A CG 1 ATOM 660 C CD1 . LEU A 1 85 B 21.056 9.607 19.014 1.00 32.01 ? 99 LEU A CD1 1 ATOM 661 C CD2 . LEU A 1 85 B 22.198 7.349 18.904 1.00 28.41 ? 99 LEU A CD2 1 ATOM 662 N N . LEU A 1 86 ? 23.969 8.366 13.715 1.00 29.46 ? 100 LEU A N 1 ATOM 663 C CA . LEU A 1 86 ? 23.940 8.280 12.270 1.00 29.65 ? 100 LEU A CA 1 ATOM 664 C C . LEU A 1 86 ? 23.053 7.082 11.850 1.00 30.43 ? 100 LEU A C 1 ATOM 665 O O . LEU A 1 86 ? 23.091 6.008 12.491 1.00 30.42 ? 100 LEU A O 1 ATOM 666 C CB . LEU A 1 86 ? 25.387 7.950 11.851 1.00 31.48 ? 100 LEU A CB 1 ATOM 667 C CG . LEU A 1 86 ? 25.740 8.212 10.403 1.00 36.05 ? 100 LEU A CG 1 ATOM 668 C CD1 . LEU A 1 86 ? 25.986 9.724 10.377 1.00 35.93 ? 100 LEU A CD1 1 ATOM 669 C CD2 . LEU A 1 86 ? 27.003 7.492 9.928 1.00 39.80 ? 100 LEU A CD2 1 ATOM 670 N N . ASN A 1 87 ? 22.279 7.272 10.789 1.00 30.80 ? 101 ASN A N 1 ATOM 671 C CA . ASN A 1 87 ? 21.341 6.289 10.245 1.00 34.00 ? 101 ASN A CA 1 ATOM 672 C C . ASN A 1 87 ? 20.393 5.730 11.314 1.00 33.79 ? 101 ASN A C 1 ATOM 673 O O . ASN A 1 87 ? 20.250 4.475 11.445 1.00 32.72 ? 101 ASN A O 1 ATOM 674 C CB . ASN A 1 87 ? 22.123 5.168 9.527 1.00 32.01 ? 101 ASN A CB 1 ATOM 675 C CG . ASN A 1 87 ? 23.034 5.740 8.422 1.00 38.39 ? 101 ASN A CG 1 ATOM 676 O OD1 . ASN A 1 87 ? 24.194 5.364 8.276 1.00 44.60 ? 101 ASN A OD1 1 ATOM 677 N ND2 . ASN A 1 87 ? 22.513 6.716 7.705 1.00 40.86 ? 101 ASN A ND2 1 ATOM 678 N N . ASP A 1 88 ? 19.726 6.657 12.022 1.00 31.11 ? 102 ASP A N 1 ATOM 679 C CA . ASP A 1 88 ? 18.828 6.321 13.162 1.00 29.44 ? 102 ASP A CA 1 ATOM 680 C C . ASP A 1 88 ? 17.459 5.961 12.657 1.00 28.21 ? 102 ASP A C 1 ATOM 681 O O . ASP A 1 88 ? 16.448 6.651 12.877 1.00 27.61 ? 102 ASP A O 1 ATOM 682 C CB . ASP A 1 88 ? 18.843 7.496 14.180 1.00 29.36 ? 102 ASP A CB 1 ATOM 683 C CG . ASP A 1 88 ? 18.158 7.157 15.526 1.00 33.15 ? 102 ASP A CG 1 ATOM 684 O OD1 . ASP A 1 88 ? 17.764 5.954 15.723 1.00 30.09 ? 102 ASP A OD1 1 ATOM 685 O OD2 . ASP A 1 88 ? 18.011 8.062 16.428 1.00 25.29 ? 102 ASP A OD2 1 ATOM 686 N N . ILE A 1 89 ? 17.399 4.812 11.962 1.00 27.14 ? 103 ILE A N 1 ATOM 687 C CA . ILE A 1 89 ? 16.157 4.417 11.355 1.00 26.07 ? 103 ILE A CA 1 ATOM 688 C C . ILE A 1 89 ? 16.020 2.841 11.428 1.00 25.49 ? 103 ILE A C 1 ATOM 689 O O . ILE A 1 89 ? 16.994 2.144 11.235 1.00 25.65 ? 103 ILE A O 1 ATOM 690 C CB . ILE A 1 89 ? 16.092 4.923 9.862 1.00 24.89 ? 103 ILE A CB 1 ATOM 691 C CG1 . ILE A 1 89 ? 14.699 4.625 9.299 1.00 25.98 ? 103 ILE A CG1 1 ATOM 692 C CG2 . ILE A 1 89 ? 17.253 4.349 9.030 1.00 27.04 ? 103 ILE A CG2 1 ATOM 693 C CD1 . ILE A 1 89 ? 14.440 5.173 7.874 1.00 32.34 ? 103 ILE A CD1 1 ATOM 694 N N . VAL A 1 90 ? 14.804 2.378 11.673 1.00 26.27 ? 104 VAL A N 1 ATOM 695 C CA . VAL A 1 90 ? 14.485 0.979 11.790 1.00 27.73 ? 104 VAL A CA 1 ATOM 696 C C . VAL A 1 90 ? 13.162 0.762 11.090 1.00 28.23 ? 104 VAL A C 1 ATOM 697 O O . VAL A 1 90 ? 12.332 1.631 11.209 1.00 28.64 ? 104 VAL A O 1 ATOM 698 C CB . VAL A 1 90 ? 14.401 0.560 13.316 1.00 27.92 ? 104 VAL A CB 1 ATOM 699 C CG1 . VAL A 1 90 ? 13.242 1.318 14.064 1.00 23.71 ? 104 VAL A CG1 1 ATOM 700 C CG2 . VAL A 1 90 ? 14.201 -0.912 13.401 1.00 27.72 ? 104 VAL A CG2 1 ATOM 701 N N . ILE A 1 91 ? 12.995 -0.324 10.297 1.00 26.49 ? 105 ILE A N 1 ATOM 702 C CA . ILE A 1 91 ? 11.688 -0.603 9.727 1.00 27.98 ? 105 ILE A CA 1 ATOM 703 C C . ILE A 1 91 ? 11.132 -1.818 10.478 1.00 27.43 ? 105 ILE A C 1 ATOM 704 O O . ILE A 1 91 ? 11.875 -2.799 10.677 1.00 27.38 ? 105 ILE A O 1 ATOM 705 C CB . ILE A 1 91 ? 11.774 -0.932 8.202 1.00 26.37 ? 105 ILE A CB 1 ATOM 706 C CG1 . ILE A 1 91 ? 12.617 0.108 7.461 1.00 29.86 ? 105 ILE A CG1 1 ATOM 707 C CG2 . ILE A 1 91 ? 10.396 -1.061 7.703 1.00 28.61 ? 105 ILE A CG2 1 ATOM 708 C CD1 . ILE A 1 91 ? 12.101 1.608 7.628 1.00 32.74 ? 105 ILE A CD1 1 ATOM 709 N N . LEU A 1 92 ? 9.867 -1.759 10.872 1.00 27.44 ? 106 LEU A N 1 ATOM 710 C CA . LEU A 1 92 ? 9.295 -2.846 11.640 1.00 30.16 ? 106 LEU A CA 1 ATOM 711 C C . LEU A 1 92 ? 8.128 -3.532 10.957 1.00 30.02 ? 106 LEU A C 1 ATOM 712 O O . LEU A 1 92 ? 7.067 -2.980 10.801 1.00 30.56 ? 106 LEU A O 1 ATOM 713 C CB . LEU A 1 92 ? 8.888 -2.356 13.069 1.00 30.45 ? 106 LEU A CB 1 ATOM 714 C CG . LEU A 1 92 ? 9.980 -1.632 13.885 1.00 30.27 ? 106 LEU A CG 1 ATOM 715 C CD1 . LEU A 1 92 ? 9.349 -0.959 15.141 1.00 26.86 ? 106 LEU A CD1 1 ATOM 716 C CD2 . LEU A 1 92 ? 11.123 -2.633 14.298 1.00 26.70 ? 106 LEU A CD2 1 ATOM 717 N N . GLN A 1 93 ? 8.321 -4.772 10.520 1.00 32.15 ? 107 GLN A N 1 ATOM 718 C CA . GLN A 1 93 ? 7.156 -5.515 10.027 1.00 31.20 ? 107 GLN A CA 1 ATOM 719 C C . GLN A 1 93 ? 6.144 -5.850 11.165 1.00 29.22 ? 107 GLN A C 1 ATOM 720 O O . GLN A 1 93 ? 6.493 -6.213 12.264 1.00 29.27 ? 107 GLN A O 1 ATOM 721 C CB . GLN A 1 93 ? 7.581 -6.758 9.169 1.00 31.00 ? 107 GLN A CB 1 ATOM 722 C CG . GLN A 1 93 ? 6.392 -7.217 8.198 1.00 34.69 ? 107 GLN A CG 1 ATOM 723 C CD . GLN A 1 93 ? 6.718 -8.469 7.287 1.00 39.53 ? 107 GLN A CD 1 ATOM 724 O OE1 . GLN A 1 93 ? 7.862 -8.725 6.945 1.00 37.08 ? 107 GLN A OE1 1 ATOM 725 N NE2 . GLN A 1 93 ? 5.680 -9.193 6.900 1.00 40.04 ? 107 GLN A NE2 1 ATOM 726 N N . LEU A 1 94 ? 4.861 -5.671 10.935 1.00 29.48 ? 108 LEU A N 1 ATOM 727 C CA . LEU A 1 94 ? 3.925 -6.000 11.986 1.00 30.81 ? 108 LEU A CA 1 ATOM 728 C C . LEU A 1 94 ? 3.399 -7.485 11.853 1.00 33.90 ? 108 LEU A C 1 ATOM 729 O O . LEU A 1 94 ? 3.588 -8.114 10.816 1.00 33.24 ? 108 LEU A O 1 ATOM 730 C CB . LEU A 1 94 ? 2.776 -5.047 11.913 1.00 31.37 ? 108 LEU A CB 1 ATOM 731 C CG . LEU A 1 94 ? 3.128 -3.548 11.879 1.00 31.16 ? 108 LEU A CG 1 ATOM 732 C CD1 . LEU A 1 94 ? 1.796 -2.808 11.828 1.00 27.87 ? 108 LEU A CD1 1 ATOM 733 C CD2 . LEU A 1 94 ? 3.885 -3.245 13.166 1.00 26.37 ? 108 LEU A CD2 1 ATOM 734 N N . ASN A 1 95 ? 2.769 -8.013 12.892 1.00 36.24 ? 109 ASN A N 1 ATOM 735 C CA . ASN A 1 95 ? 2.284 -9.412 12.870 1.00 39.07 ? 109 ASN A CA 1 ATOM 736 C C . ASN A 1 95 ? 0.957 -9.523 12.153 1.00 39.84 ? 109 ASN A C 1 ATOM 737 O O . ASN A 1 95 ? 0.351 -10.587 12.169 1.00 41.33 ? 109 ASN A O 1 ATOM 738 C CB . ASN A 1 95 ? 2.095 -9.984 14.271 1.00 37.47 ? 109 ASN A CB 1 ATOM 739 C CG . ASN A 1 95 ? 1.074 -9.206 15.081 1.00 41.01 ? 109 ASN A CG 1 ATOM 740 O OD1 . ASN A 1 95 ? 0.985 -7.972 14.944 1.00 36.99 ? 109 ASN A OD1 1 ATOM 741 N ND2 . ASN A 1 95 ? 0.318 -9.917 15.948 1.00 42.49 ? 109 ASN A ND2 1 ATOM 742 N N . GLY A 1 96 ? 0.515 -8.434 11.533 1.00 39.99 ? 110 GLY A N 1 ATOM 743 C CA . GLY A 1 96 ? -0.745 -8.403 10.788 1.00 39.83 ? 110 GLY A CA 1 ATOM 744 C C . GLY A 1 96 ? -0.894 -7.145 9.932 1.00 40.51 ? 110 GLY A C 1 ATOM 745 O O . GLY A 1 96 ? 0.079 -6.390 9.728 1.00 39.39 ? 110 GLY A O 1 ATOM 746 N N . SER A 1 97 ? -2.103 -6.924 9.411 1.00 40.88 ? 111 SER A N 1 ATOM 747 C CA . SER A 1 97 ? -2.380 -5.741 8.610 1.00 41.38 ? 111 SER A CA 1 ATOM 748 C C . SER A 1 97 ? -3.418 -4.847 9.248 1.00 41.19 ? 111 SER A C 1 ATOM 749 O O . SER A 1 97 ? -4.442 -5.299 9.681 1.00 42.08 ? 111 SER A O 1 ATOM 750 C CB . SER A 1 97 ? -2.838 -6.119 7.188 1.00 41.44 ? 111 SER A CB 1 ATOM 751 O OG . SER A 1 97 ? -1.716 -6.372 6.401 1.00 41.14 ? 111 SER A OG 1 ATOM 752 N N . ALA A 1 98 ? -3.108 -3.565 9.332 1.00 42.12 ? 112 ALA A N 1 ATOM 753 C CA . ALA A 1 98 ? -4.026 -2.567 9.842 1.00 42.48 ? 112 ALA A CA 1 ATOM 754 C C . ALA A 1 98 ? -5.215 -2.423 8.889 1.00 43.43 ? 112 ALA A C 1 ATOM 755 O O . ALA A 1 98 ? -5.083 -2.581 7.673 1.00 41.97 ? 112 ALA A O 1 ATOM 756 C CB . ALA A 1 98 ? -3.334 -1.263 9.930 1.00 42.48 ? 112 ALA A CB 1 ATOM 757 N N . THR A 1 99 ? -6.356 -2.119 9.475 1.00 44.00 ? 113 THR A N 1 ATOM 758 C CA . THR A 1 99 ? -7.566 -1.884 8.740 1.00 45.19 ? 113 THR A CA 1 ATOM 759 C C . THR A 1 99 ? -7.566 -0.401 8.378 1.00 46.13 ? 113 THR A C 1 ATOM 760 O O . THR A 1 99 ? -7.625 0.441 9.273 1.00 46.19 ? 113 THR A O 1 ATOM 761 C CB . THR A 1 99 ? -8.738 -2.199 9.685 1.00 45.73 ? 113 THR A CB 1 ATOM 762 O OG1 . THR A 1 99 ? -8.779 -3.617 9.959 1.00 45.07 ? 113 THR A OG1 1 ATOM 763 C CG2 . THR A 1 99 ? -10.077 -1.899 9.033 1.00 45.15 ? 113 THR A CG2 1 ATOM 764 N N . ILE A 1 100 ? -7.467 -0.062 7.090 1.00 46.50 ? 114 ILE A N 1 ATOM 765 C CA . ILE A 1 100 ? -7.420 1.355 6.706 1.00 47.37 ? 114 ILE A CA 1 ATOM 766 C C . ILE A 1 100 ? -8.754 2.033 6.948 1.00 47.40 ? 114 ILE A C 1 ATOM 767 O O . ILE A 1 100 ? -9.786 1.516 6.584 1.00 48.97 ? 114 ILE A O 1 ATOM 768 C CB . ILE A 1 100 ? -6.947 1.549 5.254 1.00 47.65 ? 114 ILE A CB 1 ATOM 769 C CG1 . ILE A 1 100 ? -5.475 1.145 5.106 1.00 49.70 ? 114 ILE A CG1 1 ATOM 770 C CG2 . ILE A 1 100 ? -7.059 2.992 4.838 1.00 47.29 ? 114 ILE A CG2 1 ATOM 771 C CD1 . ILE A 1 100 ? -4.574 1.714 6.190 1.00 48.60 ? 114 ILE A CD1 1 ATOM 772 N N . ASN A 1 101 ? -8.737 3.172 7.625 1.00 47.63 ? 115 ASN A N 1 ATOM 773 C CA . ASN A 1 101 ? -9.958 3.887 7.935 1.00 47.29 ? 115 ASN A CA 1 ATOM 774 C C . ASN A 1 101 ? -9.685 5.339 8.243 1.00 47.31 ? 115 ASN A C 1 ATOM 775 O O . ASN A 1 101 ? -8.646 5.871 7.870 1.00 48.07 ? 115 ASN A O 1 ATOM 776 C CB . ASN A 1 101 ? -10.764 3.221 9.042 1.00 47.76 ? 115 ASN A CB 1 ATOM 777 C CG . ASN A 1 101 ? -10.058 3.265 10.412 1.00 47.59 ? 115 ASN A CG 1 ATOM 778 O OD1 . ASN A 1 101 ? -9.175 4.089 10.634 1.00 44.09 ? 115 ASN A OD1 1 ATOM 779 N ND2 . ASN A 1 101 ? -10.494 2.393 11.341 1.00 47.47 ? 115 ASN A ND2 1 ATOM 780 N N . ALA A 1 102 ? -10.618 5.983 8.922 1.00 47.11 ? 116 ALA A N 1 ATOM 781 C CA . ALA A 1 102 ? -10.517 7.410 9.212 1.00 46.96 ? 116 ALA A CA 1 ATOM 782 C C . ALA A 1 102 ? -9.350 7.698 10.141 1.00 47.06 ? 116 ALA A C 1 ATOM 783 O O . ALA A 1 102 ? -8.646 8.715 10.012 1.00 46.48 ? 116 ALA A O 1 ATOM 784 C CB . ALA A 1 102 ? -11.787 7.860 9.881 1.00 46.67 ? 116 ALA A CB 1 ATOM 785 N N . ASN A 1 103 ? -9.197 6.794 11.098 1.00 47.28 ? 117 ASN A N 1 ATOM 786 C CA . ASN A 1 103 ? -8.200 6.913 12.145 1.00 47.48 ? 117 ASN A CA 1 ATOM 787 C C . ASN A 1 103 ? -6.848 6.275 11.871 1.00 46.61 ? 117 ASN A C 1 ATOM 788 O O . ASN A 1 103 ? -5.938 6.392 12.685 1.00 46.88 ? 117 ASN A O 1 ATOM 789 C CB . ASN A 1 103 ? -8.801 6.348 13.419 1.00 47.55 ? 117 ASN A CB 1 ATOM 790 C CG . ASN A 1 103 ? -10.034 7.071 13.808 1.00 48.79 ? 117 ASN A CG 1 ATOM 791 O OD1 . ASN A 1 103 ? -11.097 6.478 13.937 1.00 52.91 ? 117 ASN A OD1 1 ATOM 792 N ND2 . ASN A 1 103 ? -9.925 8.390 13.937 1.00 50.03 ? 117 ASN A ND2 1 ATOM 793 N N . VAL A 1 104 ? -6.704 5.600 10.742 1.00 45.60 ? 118 VAL A N 1 ATOM 794 C CA . VAL A 1 104 ? -5.453 4.943 10.420 1.00 44.86 ? 118 VAL A CA 1 ATOM 795 C C . VAL A 1 104 ? -5.200 4.991 8.918 1.00 45.72 ? 118 VAL A C 1 ATOM 796 O O . VAL A 1 104 ? -6.034 4.558 8.146 1.00 47.60 ? 118 VAL A O 1 ATOM 797 C CB . VAL A 1 104 ? -5.448 3.476 10.901 1.00 44.46 ? 118 VAL A CB 1 ATOM 798 C CG1 . VAL A 1 104 ? -4.058 2.860 10.679 1.00 44.32 ? 118 VAL A CG1 1 ATOM 799 C CG2 . VAL A 1 104 ? -5.858 3.365 12.364 1.00 42.57 ? 118 VAL A CG2 1 ATOM 800 N N . GLN A 1 105 ? -4.067 5.532 8.500 1.00 46.80 ? 119 GLN A N 1 ATOM 801 C CA . GLN A 1 105 ? -3.751 5.679 7.082 1.00 46.97 ? 119 GLN A CA 1 ATOM 802 C C . GLN A 1 105 ? -2.272 5.634 6.899 1.00 46.62 ? 119 GLN A C 1 ATOM 803 O O . GLN A 1 105 ? -1.526 6.124 7.762 1.00 46.11 ? 119 GLN A O 1 ATOM 804 C CB . GLN A 1 105 ? -4.207 7.032 6.553 1.00 47.61 ? 119 GLN A CB 1 ATOM 805 C CG . GLN A 1 105 ? -5.678 7.366 6.833 1.00 52.89 ? 119 GLN A CG 1 ATOM 806 C CD . GLN A 1 105 ? -6.549 6.985 5.666 1.00 60.19 ? 119 GLN A CD 1 ATOM 807 O OE1 . GLN A 1 105 ? -7.720 6.650 5.848 1.00 63.72 ? 119 GLN A OE1 1 ATOM 808 N NE2 . GLN A 1 105 ? -5.975 7.024 4.447 1.00 62.53 ? 119 GLN A NE2 1 ATOM 809 N N . VAL A 1 106 ? -1.855 5.097 5.756 1.00 44.98 ? 120 VAL A N 1 ATOM 810 C CA . VAL A 1 106 ? -0.456 5.015 5.391 1.00 45.00 ? 120 VAL A CA 1 ATOM 811 C C . VAL A 1 106 ? -0.009 6.431 5.045 1.00 45.90 ? 120 VAL A C 1 ATOM 812 O O . VAL A 1 106 ? -0.765 7.195 4.432 1.00 47.11 ? 120 VAL A O 1 ATOM 813 C CB . VAL A 1 106 ? -0.288 4.038 4.181 1.00 45.40 ? 120 VAL A CB 1 ATOM 814 C CG1 . VAL A 1 106 ? 1.057 4.176 3.474 1.00 44.02 ? 120 VAL A CG1 1 ATOM 815 C CG2 . VAL A 1 106 ? -0.543 2.586 4.634 1.00 43.02 ? 120 VAL A CG2 1 ATOM 816 N N . ALA A 1 107 ? 1.183 6.834 5.454 1.00 45.07 ? 121 ALA A N 1 ATOM 817 C CA . ALA A 1 107 ? 1.614 8.183 5.084 1.00 45.51 ? 121 ALA A CA 1 ATOM 818 C C . ALA A 1 107 ? 2.313 8.101 3.766 1.00 45.02 ? 121 ALA A C 1 ATOM 819 O O . ALA A 1 107 ? 2.639 7.010 3.316 1.00 44.11 ? 121 ALA A O 1 ATOM 820 C CB . ALA A 1 107 ? 2.560 8.777 6.109 1.00 44.59 ? 121 ALA A CB 1 ATOM 821 N N . GLN A 1 108 ? 2.631 9.258 3.195 1.00 45.35 ? 122 GLN A N 1 ATOM 822 C CA . GLN A 1 108 ? 3.282 9.286 1.887 1.00 46.58 ? 122 GLN A CA 1 ATOM 823 C C . GLN A 1 108 ? 4.747 9.617 2.068 1.00 46.02 ? 122 GLN A C 1 ATOM 824 O O . GLN A 1 108 ? 5.095 10.366 2.986 1.00 46.40 ? 122 GLN A O 1 ATOM 825 C CB . GLN A 1 108 ? 2.632 10.333 0.974 1.00 47.25 ? 122 GLN A CB 1 ATOM 826 C CG . GLN A 1 108 ? 2.826 10.023 -0.504 1.00 50.88 ? 122 GLN A CG 1 ATOM 827 C CD . GLN A 1 108 ? 2.616 11.238 -1.415 1.00 57.15 ? 122 GLN A CD 1 ATOM 828 O OE1 . GLN A 1 108 ? 3.232 11.346 -2.493 1.00 57.46 ? 122 GLN A OE1 1 ATOM 829 N NE2 . GLN A 1 108 ? 1.760 12.150 -0.981 1.00 58.36 ? 122 GLN A NE2 1 ATOM 830 N N . LEU A 1 109 ? 5.606 9.221 1.143 1.00 46.46 ? 123 LEU A N 1 ATOM 831 C CA . LEU A 1 109 ? 7.013 9.500 1.363 1.00 45.91 ? 123 LEU A CA 1 ATOM 832 C C . LEU A 1 109 ? 7.585 10.352 0.244 1.00 47.35 ? 123 LEU A C 1 ATOM 833 O O . LEU A 1 109 ? 6.948 10.531 -0.743 1.00 46.83 ? 123 LEU A O 1 ATOM 834 C CB . LEU A 1 109 ? 7.799 8.205 1.567 1.00 46.67 ? 123 LEU A CB 1 ATOM 835 C CG . LEU A 1 109 ? 7.359 7.223 2.682 1.00 45.76 ? 123 LEU A CG 1 ATOM 836 C CD1 . LEU A 1 109 ? 8.312 6.050 2.778 1.00 46.27 ? 123 LEU A CD1 1 ATOM 837 C CD2 . LEU A 1 109 ? 7.339 7.948 4.035 1.00 39.77 ? 123 LEU A CD2 1 ATOM 838 N N . PRO A 1 110 ? 8.764 10.898 0.456 1.00 47.62 ? 124 PRO A N 1 ATOM 839 C CA . PRO A 1 110 ? 9.475 11.652 -0.569 1.00 48.79 ? 124 PRO A CA 1 ATOM 840 C C . PRO A 1 110 ? 10.284 10.688 -1.400 1.00 49.98 ? 124 PRO A C 1 ATOM 841 O O . PRO A 1 110 ? 10.478 9.548 -0.945 1.00 49.42 ? 124 PRO A O 1 ATOM 842 C CB . PRO A 1 110 ? 10.477 12.477 0.229 1.00 49.03 ? 124 PRO A CB 1 ATOM 843 C CG . PRO A 1 110 ? 10.533 11.870 1.607 1.00 48.06 ? 124 PRO A CG 1 ATOM 844 C CD . PRO A 1 110 ? 9.480 10.871 1.740 1.00 47.63 ? 124 PRO A CD 1 ATOM 845 N N . ALA A 1 111 ? 10.793 11.134 -2.546 1.00 49.29 ? 125 ALA A N 1 ATOM 846 C CA . ALA A 1 111 ? 11.567 10.247 -3.385 1.00 49.25 ? 125 ALA A CA 1 ATOM 847 C C . ALA A 1 111 ? 13.020 10.290 -2.950 1.00 49.07 ? 125 ALA A C 1 ATOM 848 O O . ALA A 1 111 ? 13.482 11.287 -2.350 1.00 48.59 ? 125 ALA A O 1 ATOM 849 C CB . ALA A 1 111 ? 11.417 10.634 -4.834 1.00 50.29 ? 125 ALA A CB 1 ATOM 850 N N . GLN A 1 112 ? 13.702 9.172 -3.178 1.00 48.21 ? 126 GLN A N 1 ATOM 851 C CA . GLN A 1 112 ? 15.117 9.016 -2.829 1.00 48.55 ? 126 GLN A CA 1 ATOM 852 C C . GLN A 1 112 ? 15.896 10.268 -3.128 1.00 50.75 ? 126 GLN A C 1 ATOM 853 O O . GLN A 1 112 ? 15.770 10.818 -4.219 1.00 52.19 ? 126 GLN A O 1 ATOM 854 C CB . GLN A 1 112 ? 15.765 7.850 -3.618 1.00 47.01 ? 126 GLN A CB 1 ATOM 855 C CG . GLN A 1 112 ? 17.287 7.737 -3.409 1.00 41.74 ? 126 GLN A CG 1 ATOM 856 C CD . GLN A 1 112 ? 17.628 7.158 -2.042 1.00 37.29 ? 126 GLN A CD 1 ATOM 857 O OE1 . GLN A 1 112 ? 16.817 6.440 -1.480 1.00 34.05 ? 126 GLN A OE1 1 ATOM 858 N NE2 . GLN A 1 112 ? 18.819 7.451 -1.523 1.00 33.58 ? 126 GLN A NE2 1 ATOM 859 N N . GLY A 1 113 ? 16.723 10.683 -2.172 1.00 52.20 ? 127 GLY A N 1 ATOM 860 C CA . GLY A 1 113 ? 17.603 11.830 -2.295 1.00 53.69 ? 127 GLY A CA 1 ATOM 861 C C . GLY A 1 113 ? 16.981 13.229 -2.259 1.00 55.04 ? 127 GLY A C 1 ATOM 862 O O . GLY A 1 113 ? 17.729 14.198 -2.374 1.00 55.15 ? 127 GLY A O 1 ATOM 863 N N . ARG A 1 114 ? 15.650 13.334 -2.145 1.00 55.76 ? 128 ARG A N 1 ATOM 864 C CA . ARG A 1 114 ? 14.953 14.617 -2.076 1.00 57.44 ? 128 ARG A CA 1 ATOM 865 C C . ARG A 1 114 ? 15.303 15.366 -0.789 1.00 58.45 ? 128 ARG A C 1 ATOM 866 O O . ARG A 1 114 ? 14.665 15.146 0.252 1.00 59.29 ? 128 ARG A O 1 ATOM 867 C CB . ARG A 1 114 ? 13.425 14.409 -2.128 1.00 57.56 ? 128 ARG A CB 1 ATOM 868 C CG . ARG A 1 114 ? 12.586 15.598 -2.704 1.00 59.92 ? 128 ARG A CG 1 ATOM 869 C CD . ARG A 1 114 ? 11.143 15.829 -2.068 1.00 61.17 ? 128 ARG A CD 1 ATOM 870 N NE . ARG A 1 114 ? 10.981 17.212 -1.562 1.00 58.47 ? 128 ARG A NE 1 ATOM 871 C CZ . ARG A 1 114 ? 9.837 17.865 -1.334 1.00 58.75 ? 128 ARG A CZ 1 ATOM 872 N NH1 . ARG A 1 114 ? 9.897 19.114 -0.883 1.00 61.67 ? 128 ARG A NH1 1 ATOM 873 N NH2 . ARG A 1 114 ? 8.639 17.322 -1.554 1.00 58.40 ? 128 ARG A NH2 1 ATOM 874 N N . ARG A 1 115 ? 16.327 16.223 -0.860 1.00 58.74 ? 129 ARG A N 1 ATOM 875 C CA . ARG A 1 115 ? 16.776 17.090 0.253 1.00 59.19 ? 129 ARG A CA 1 ATOM 876 C C . ARG A 1 115 ? 15.917 18.364 0.441 1.00 58.82 ? 129 ARG A C 1 ATOM 877 O O . ARG A 1 115 ? 15.249 18.820 -0.498 1.00 59.56 ? 129 ARG A O 1 ATOM 878 C CB . ARG A 1 115 ? 18.247 17.498 0.032 1.00 59.21 ? 129 ARG A CB 1 ATOM 879 C CG . ARG A 1 115 ? 19.042 17.906 1.287 1.00 61.04 ? 129 ARG A CG 1 ATOM 880 C CD . ARG A 1 115 ? 20.567 17.885 1.082 1.00 64.85 ? 129 ARG A CD 1 ATOM 881 N NE . ARG A 1 115 ? 21.353 17.976 2.318 1.00 68.14 ? 129 ARG A NE 1 ATOM 882 C CZ . ARG A 1 115 ? 21.950 16.940 2.913 1.00 70.02 ? 129 ARG A CZ 1 ATOM 883 N NH1 . ARG A 1 115 ? 21.840 15.717 2.404 1.00 71.97 ? 129 ARG A NH1 1 ATOM 884 N NH2 . ARG A 1 115 ? 22.650 17.120 4.024 1.00 70.49 ? 129 ARG A NH2 1 ATOM 885 N N . LEU A 1 116 ? 15.940 18.934 1.649 1.00 57.89 ? 130 LEU A N 1 ATOM 886 C CA . LEU A 1 116 ? 15.240 20.207 1.940 1.00 56.21 ? 130 LEU A CA 1 ATOM 887 C C . LEU A 1 116 ? 16.226 21.345 2.208 1.00 55.18 ? 130 LEU A C 1 ATOM 888 O O . LEU A 1 116 ? 17.324 21.133 2.717 1.00 54.78 ? 130 LEU A O 1 ATOM 889 C CB . LEU A 1 116 ? 14.258 20.057 3.118 1.00 56.47 ? 130 LEU A CB 1 ATOM 890 C CG . LEU A 1 116 ? 13.154 19.001 2.904 1.00 55.54 ? 130 LEU A CG 1 ATOM 891 C CD1 . LEU A 1 116 ? 12.279 18.731 4.137 1.00 53.16 ? 130 LEU A CD1 1 ATOM 892 C CD2 . LEU A 1 116 ? 12.294 19.340 1.689 1.00 57.03 ? 130 LEU A CD2 1 ATOM 893 N N . GLY A 1 117 ? 15.832 22.570 1.872 1.00 54.59 ? 131 GLY A N 1 ATOM 894 C CA . GLY A 1 117 ? 16.718 23.701 2.058 1.00 53.39 ? 131 GLY A CA 1 ATOM 895 C C . GLY A 1 117 ? 16.352 24.576 3.242 1.00 52.71 ? 131 GLY A C 1 ATOM 896 O O . GLY A 1 117 ? 15.227 24.564 3.703 1.00 52.76 ? 131 GLY A O 1 ATOM 897 N N . ASN A 1 118 ? 17.305 25.367 3.721 1.00 52.87 ? 132 ASN A N 1 ATOM 898 C CA . ASN A 1 118 ? 17.043 26.216 4.883 1.00 52.31 ? 132 ASN A CA 1 ATOM 899 C C . ASN A 1 118 ? 15.746 27.004 4.716 1.00 50.55 ? 132 ASN A C 1 ATOM 900 O O . ASN A 1 118 ? 15.525 27.632 3.690 1.00 50.82 ? 132 ASN A O 1 ATOM 901 C CB . ASN A 1 118 ? 18.238 27.134 5.173 1.00 53.40 ? 132 ASN A CB 1 ATOM 902 C CG . ASN A 1 118 ? 18.504 27.290 6.673 1.00 55.45 ? 132 ASN A CG 1 ATOM 903 O OD1 . ASN A 1 118 ? 19.650 27.357 7.126 1.00 61.39 ? 132 ASN A OD1 1 ATOM 904 N ND2 . ASN A 1 118 ? 17.443 27.345 7.444 1.00 59.01 ? 132 ASN A ND2 1 ATOM 905 N N . GLY A 1 119 ? 14.851 26.925 5.699 1.00 48.44 ? 133 GLY A N 1 ATOM 906 C CA . GLY A 1 119 ? 13.625 27.704 5.656 1.00 44.34 ? 133 GLY A CA 1 ATOM 907 C C . GLY A 1 119 ? 12.356 27.007 5.333 1.00 42.57 ? 133 GLY A C 1 ATOM 908 O O . GLY A 1 119 ? 11.269 27.550 5.491 1.00 41.55 ? 133 GLY A O 1 ATOM 909 N N . VAL A 1 120 ? 12.449 25.774 4.864 1.00 41.61 ? 134 VAL A N 1 ATOM 910 C CA . VAL A 1 120 ? 11.216 25.094 4.583 1.00 39.83 ? 134 VAL A CA 1 ATOM 911 C C . VAL A 1 120 ? 10.401 24.961 5.882 1.00 39.45 ? 134 VAL A C 1 ATOM 912 O O . VAL A 1 120 ? 10.938 24.807 6.963 1.00 38.78 ? 134 VAL A O 1 ATOM 913 C CB . VAL A 1 120 ? 11.519 23.722 3.967 1.00 40.52 ? 134 VAL A CB 1 ATOM 914 C CG1 . VAL A 1 120 ? 10.243 22.934 3.851 1.00 37.60 ? 134 VAL A CG1 1 ATOM 915 C CG2 . VAL A 1 120 ? 12.259 23.910 2.579 1.00 40.39 ? 134 VAL A CG2 1 ATOM 916 N N . GLN A 1 121 ? 9.099 25.022 5.780 1.00 39.18 ? 135 GLN A N 1 ATOM 917 C CA . GLN A 1 121 ? 8.309 24.967 6.949 1.00 40.69 ? 135 GLN A CA 1 ATOM 918 C C . GLN A 1 121 ? 7.773 23.568 7.164 1.00 39.99 ? 135 GLN A C 1 ATOM 919 O O . GLN A 1 121 ? 7.179 22.986 6.277 1.00 39.83 ? 135 GLN A O 1 ATOM 920 C CB . GLN A 1 121 ? 7.176 25.931 6.808 1.00 41.79 ? 135 GLN A CB 1 ATOM 921 C CG . GLN A 1 121 ? 7.694 27.312 6.432 1.00 47.04 ? 135 GLN A CG 1 ATOM 922 C CD . GLN A 1 121 ? 8.193 28.064 7.638 1.00 52.09 ? 135 GLN A CD 1 ATOM 923 O OE1 . GLN A 1 121 ? 9.053 28.963 7.509 1.00 58.75 ? 135 GLN A OE1 1 ATOM 924 N NE2 . GLN A 1 121 ? 7.663 27.723 8.814 1.00 52.32 ? 135 GLN A NE2 1 ATOM 925 N N . CYS A 1 122 ? 7.982 23.037 8.358 1.00 39.09 ? 136 CYS A N 1 ATOM 926 C CA . CYS A 1 122 ? 7.482 21.701 8.678 1.00 38.23 ? 136 CYS A CA 1 ATOM 927 C C . CYS A 1 122 ? 6.634 21.668 9.955 1.00 37.86 ? 136 CYS A C 1 ATOM 928 O O . CYS A 1 122 ? 6.424 22.695 10.656 1.00 37.26 ? 136 CYS A O 1 ATOM 929 C CB . CYS A 1 122 ? 8.632 20.724 8.819 1.00 38.63 ? 136 CYS A CB 1 ATOM 930 S SG . CYS A 1 122 ? 9.904 20.620 7.514 1.00 39.28 ? 136 CYS A SG 1 ATOM 931 N N . LEU A 1 123 ? 6.175 20.467 10.275 1.00 34.85 ? 137 LEU A N 1 ATOM 932 C CA . LEU A 1 123 ? 5.364 20.231 11.448 1.00 33.66 ? 137 LEU A CA 1 ATOM 933 C C . LEU A 1 123 ? 5.863 18.958 12.168 1.00 33.45 ? 137 LEU A C 1 ATOM 934 O O . LEU A 1 123 ? 5.838 17.889 11.569 1.00 32.36 ? 137 LEU A O 1 ATOM 935 C CB . LEU A 1 123 ? 3.938 19.954 11.053 1.00 31.08 ? 137 LEU A CB 1 ATOM 936 C CG . LEU A 1 123 ? 2.993 20.096 12.240 1.00 35.24 ? 137 LEU A CG 1 ATOM 937 C CD1 . LEU A 1 123 ? 2.954 21.568 12.741 1.00 34.65 ? 137 LEU A CD1 1 ATOM 938 C CD2 . LEU A 1 123 ? 1.583 19.613 11.923 1.00 37.93 ? 137 LEU A CD2 1 ATOM 939 N N . ALA A 1 124 ? 6.328 19.098 13.410 1.00 34.00 ? 138 ALA A N 1 ATOM 940 C CA . ALA A 1 124 ? 6.765 17.946 14.218 1.00 33.35 ? 138 ALA A CA 1 ATOM 941 C C . ALA A 1 124 ? 5.635 17.608 15.156 1.00 31.85 ? 138 ALA A C 1 ATOM 942 O O . ALA A 1 124 ? 4.738 18.421 15.369 1.00 32.94 ? 138 ALA A O 1 ATOM 943 C CB . ALA A 1 124 ? 8.036 18.247 14.981 1.00 33.61 ? 138 ALA A CB 1 ATOM 944 N N . MET A 1 125 ? 5.614 16.381 15.678 1.00 30.95 ? 139 MET A N 1 ATOM 945 C CA . MET A 1 125 ? 4.545 15.955 16.554 1.00 29.14 ? 139 MET A CA 1 ATOM 946 C C . MET A 1 125 ? 5.058 14.776 17.463 1.00 27.89 ? 139 MET A C 1 ATOM 947 O O . MET A 1 125 ? 6.133 14.205 17.239 1.00 26.29 ? 139 MET A O 1 ATOM 948 C CB . MET A 1 125 ? 3.358 15.461 15.705 1.00 28.99 ? 139 MET A CB 1 ATOM 949 C CG . MET A 1 125 ? 3.758 14.366 14.664 1.00 30.72 ? 139 MET A CG 1 ATOM 950 S SD . MET A 1 125 ? 2.378 13.835 13.616 1.00 31.73 ? 139 MET A SD 1 ATOM 951 C CE . MET A 1 125 ? 2.310 15.193 12.481 1.00 37.51 ? 139 MET A CE 1 ATOM 952 N N . GLY A 1 126 ? 4.258 14.430 18.438 1.00 27.78 ? 140 GLY A N 1 ATOM 953 C CA . GLY A 1 126 ? 4.529 13.281 19.283 1.00 28.32 ? 140 GLY A CA 1 ATOM 954 C C . GLY A 1 126 ? 3.924 13.359 20.655 1.00 28.51 ? 140 GLY A C 1 ATOM 955 O O . GLY A 1 126 ? 3.315 14.366 21.024 1.00 29.61 ? 140 GLY A O 1 ATOM 956 N N . TRP A 1 127 ? 4.065 12.283 21.420 1.00 28.53 ? 141 TRP A N 1 ATOM 957 C CA . TRP A 1 127 ? 3.578 12.286 22.796 1.00 29.27 ? 141 TRP A CA 1 ATOM 958 C C . TRP A 1 127 ? 4.646 12.520 23.876 1.00 29.84 ? 141 TRP A C 1 ATOM 959 O O . TRP A 1 127 ? 4.439 12.132 25.023 1.00 33.46 ? 141 TRP A O 1 ATOM 960 C CB . TRP A 1 127 ? 2.831 10.978 23.089 1.00 28.86 ? 141 TRP A CB 1 ATOM 961 C CG . TRP A 1 127 ? 1.461 10.834 22.465 1.00 25.72 ? 141 TRP A CG 1 ATOM 962 C CD1 . TRP A 1 127 ? 0.284 11.335 22.919 1.00 27.61 ? 141 TRP A CD1 1 ATOM 963 C CD2 . TRP A 1 127 ? 1.135 10.064 21.289 1.00 28.81 ? 141 TRP A CD2 1 ATOM 964 N NE1 . TRP A 1 127 ? -0.756 10.945 22.095 1.00 27.53 ? 141 TRP A NE1 1 ATOM 965 C CE2 . TRP A 1 127 ? -0.259 10.160 21.088 1.00 26.74 ? 141 TRP A CE2 1 ATOM 966 C CE3 . TRP A 1 127 ? 1.890 9.325 20.362 1.00 25.91 ? 141 TRP A CE3 1 ATOM 967 C CZ2 . TRP A 1 127 ? -0.913 9.545 19.988 1.00 24.83 ? 141 TRP A CZ2 1 ATOM 968 C CZ3 . TRP A 1 127 ? 1.239 8.729 19.266 1.00 27.60 ? 141 TRP A CZ3 1 ATOM 969 C CH2 . TRP A 1 127 ? -0.153 8.818 19.117 1.00 25.13 ? 141 TRP A CH2 1 ATOM 970 N N . GLY A 1 128 ? 5.769 13.153 23.567 1.00 30.60 ? 142 GLY A N 1 ATOM 971 C CA . GLY A 1 128 ? 6.801 13.392 24.597 1.00 30.20 ? 142 GLY A CA 1 ATOM 972 C C . GLY A 1 128 ? 6.546 14.451 25.682 1.00 29.14 ? 142 GLY A C 1 ATOM 973 O O . GLY A 1 128 ? 5.474 14.977 25.816 1.00 30.36 ? 142 GLY A O 1 ATOM 974 N N . LEU A 1 129 ? 7.567 14.763 26.455 1.00 30.56 ? 143 LEU A N 1 ATOM 975 C CA . LEU A 1 129 ? 7.440 15.636 27.596 1.00 31.28 ? 143 LEU A CA 1 ATOM 976 C C . LEU A 1 129 ? 7.063 17.040 27.150 1.00 32.66 ? 143 LEU A C 1 ATOM 977 O O . LEU A 1 129 ? 7.568 17.528 26.117 1.00 29.36 ? 143 LEU A O 1 ATOM 978 C CB . LEU A 1 129 ? 8.808 15.775 28.303 1.00 32.01 ? 143 LEU A CB 1 ATOM 979 C CG . LEU A 1 129 ? 9.370 14.525 28.990 1.00 33.93 ? 143 LEU A CG 1 ATOM 980 C CD1 . LEU A 1 129 ? 10.650 14.874 29.763 1.00 34.46 ? 143 LEU A CD1 1 ATOM 981 C CD2 . LEU A 1 129 ? 8.322 13.885 29.891 1.00 32.81 ? 143 LEU A CD2 1 ATOM 982 N N . LEU A 1 130 ? 6.188 17.642 27.958 1.00 33.23 ? 144 LEU A N 1 ATOM 983 C CA . LEU A 1 130 ? 5.676 18.999 27.781 1.00 36.02 ? 144 LEU A CA 1 ATOM 984 C C . LEU A 1 130 ? 6.663 20.068 28.103 1.00 37.54 ? 144 LEU A C 1 ATOM 985 O O . LEU A 1 130 ? 6.462 21.234 27.749 1.00 38.48 ? 144 LEU A O 1 ATOM 986 C CB . LEU A 1 130 ? 4.435 19.187 28.643 1.00 35.72 ? 144 LEU A CB 1 ATOM 987 C CG . LEU A 1 130 ? 3.451 18.181 28.168 1.00 36.02 ? 144 LEU A CG 1 ATOM 988 C CD1 . LEU A 1 130 ? 2.217 18.201 29.054 1.00 36.60 ? 144 LEU A CD1 1 ATOM 989 C CD2 . LEU A 1 130 ? 3.077 18.350 26.694 1.00 35.58 ? 144 LEU A CD2 1 ATOM 990 N N . GLY A 1 131 ? 7.734 19.729 28.803 1.00 41.51 ? 145 GLY A N 1 ATOM 991 C CA . GLY A 1 131 ? 8.770 20.792 28.929 1.00 46.41 ? 145 GLY A CA 1 ATOM 992 C C . GLY A 1 131 ? 9.862 20.713 29.969 1.00 49.54 ? 145 GLY A C 1 ATOM 993 O O . GLY A 1 131 ? 11.038 21.141 29.753 1.00 50.51 ? 145 GLY A O 1 ATOM 994 N N . ARG A 1 132 ? 9.422 20.231 31.127 1.00 52.61 ? 147 ARG A N 1 ATOM 995 C CA . ARG A 1 132 ? 10.198 19.946 32.355 1.00 53.40 ? 147 ARG A CA 1 ATOM 996 C C . ARG A 1 132 ? 9.405 20.344 33.603 1.00 54.45 ? 147 ARG A C 1 ATOM 997 O O . ARG A 1 132 ? 9.890 20.239 34.752 1.00 52.85 ? 147 ARG A O 1 ATOM 998 C CB . ARG A 1 132 ? 11.641 20.395 32.344 1.00 54.05 ? 147 ARG A CB 1 ATOM 999 C CG . ARG A 1 132 ? 12.558 19.202 32.443 1.00 55.80 ? 147 ARG A CG 1 ATOM 1000 C CD . ARG A 1 132 ? 13.478 18.966 31.254 1.00 58.94 ? 147 ARG A CD 1 ATOM 1001 N NE . ARG A 1 132 ? 13.645 17.532 31.027 1.00 59.61 ? 147 ARG A NE 1 ATOM 1002 C CZ . ARG A 1 132 ? 14.437 17.016 30.104 1.00 60.87 ? 147 ARG A CZ 1 ATOM 1003 N NH1 . ARG A 1 132 ? 15.179 17.823 29.342 1.00 60.04 ? 147 ARG A NH1 1 ATOM 1004 N NH2 . ARG A 1 132 ? 14.513 15.694 29.965 1.00 60.72 ? 147 ARG A NH2 1 ATOM 1005 N N . ASN A 1 133 ? 8.184 20.810 33.295 1.00 55.33 ? 148 ASN A N 1 ATOM 1006 C CA . ASN A 1 133 ? 7.055 21.032 34.208 1.00 56.56 ? 148 ASN A CA 1 ATOM 1007 C C . ASN A 1 133 ? 5.930 20.219 33.517 1.00 56.79 ? 148 ASN A C 1 ATOM 1008 O O . ASN A 1 133 ? 5.796 20.291 32.275 1.00 57.12 ? 148 ASN A O 1 ATOM 1009 C CB . ASN A 1 133 ? 6.621 22.497 34.257 1.00 56.80 ? 148 ASN A CB 1 ATOM 1010 C CG . ASN A 1 133 ? 5.419 22.698 35.173 1.00 58.75 ? 148 ASN A CG 1 ATOM 1011 O OD1 . ASN A 1 133 ? 5.179 21.887 36.051 1.00 58.34 ? 148 ASN A OD1 1 ATOM 1012 N ND2 . ASN A 1 133 ? 4.655 23.772 34.960 1.00 63.33 ? 148 ASN A ND2 1 ATOM 1013 N N . ARG A 1 134 ? 5.122 19.459 34.261 1.00 56.16 ? 149 ARG A N 1 ATOM 1014 C CA . ARG A 1 134 ? 4.142 18.576 33.596 1.00 54.89 ? 149 ARG A CA 1 ATOM 1015 C C . ARG A 1 134 ? 4.919 17.443 32.906 1.00 52.73 ? 149 ARG A C 1 ATOM 1016 O O . ARG A 1 134 ? 5.977 17.657 32.332 1.00 52.84 ? 149 ARG A O 1 ATOM 1017 C CB . ARG A 1 134 ? 3.340 19.335 32.531 1.00 55.09 ? 149 ARG A CB 1 ATOM 1018 C CG . ARG A 1 134 ? 3.082 20.801 32.832 1.00 56.90 ? 149 ARG A CG 1 ATOM 1019 C CD . ARG A 1 134 ? 3.168 21.721 31.607 1.00 58.99 ? 149 ARG A CD 1 ATOM 1020 N NE . ARG A 1 134 ? 1.877 21.858 30.942 1.00 62.59 ? 149 ARG A NE 1 ATOM 1021 C CZ . ARG A 1 134 ? 1.561 22.846 30.101 1.00 66.46 ? 149 ARG A CZ 1 ATOM 1022 N NH1 . ARG A 1 134 ? 2.462 23.804 29.824 1.00 65.73 ? 149 ARG A NH1 1 ATOM 1023 N NH2 . ARG A 1 134 ? 0.340 22.886 29.555 1.00 65.52 ? 149 ARG A NH2 1 ATOM 1024 N N . GLY A 1 135 ? 4.407 16.232 32.928 1.00 50.65 ? 150 GLY A N 1 ATOM 1025 C CA . GLY A 1 135 ? 5.187 15.170 32.332 1.00 46.94 ? 150 GLY A CA 1 ATOM 1026 C C . GLY A 1 135 ? 5.052 15.037 30.840 1.00 44.82 ? 150 GLY A C 1 ATOM 1027 O O . GLY A 1 135 ? 5.161 16.024 30.085 1.00 43.40 ? 150 GLY A O 1 ATOM 1028 N N . ILE A 1 136 ? 4.884 13.776 30.453 1.00 42.35 ? 151 ILE A N 1 ATOM 1029 C CA . ILE A 1 136 ? 4.646 13.294 29.113 1.00 41.80 ? 151 ILE A CA 1 ATOM 1030 C C . ILE A 1 136 ? 3.247 13.737 28.732 1.00 40.12 ? 151 ILE A C 1 ATOM 1031 O O . ILE A 1 136 ? 2.364 13.831 29.585 1.00 39.34 ? 151 ILE A O 1 ATOM 1032 C CB . ILE A 1 136 ? 4.511 11.712 29.096 1.00 42.31 ? 151 ILE A CB 1 ATOM 1033 C CG1 . ILE A 1 136 ? 5.842 10.972 29.156 1.00 44.15 ? 151 ILE A CG1 1 ATOM 1034 C CG2 . ILE A 1 136 ? 3.887 11.277 27.813 1.00 41.60 ? 151 ILE A CG2 1 ATOM 1035 C CD1 . ILE A 1 136 ? 6.460 10.661 27.784 1.00 41.72 ? 151 ILE A CD1 1 ATOM 1036 N N . ALA A 1 137 ? 3.076 14.078 27.463 1.00 38.87 ? 152 ALA A N 1 ATOM 1037 C CA . ALA A 1 137 ? 1.765 14.468 26.968 1.00 39.42 ? 152 ALA A CA 1 ATOM 1038 C C . ALA A 1 137 ? 0.724 13.354 27.089 1.00 39.43 ? 152 ALA A C 1 ATOM 1039 O O . ALA A 1 137 ? 1.034 12.172 27.004 1.00 41.62 ? 152 ALA A O 1 ATOM 1040 C CB . ALA A 1 137 ? 1.866 14.921 25.513 1.00 37.45 ? 152 ALA A CB 1 ATOM 1041 N N . SER A 1 138 ? -0.518 13.736 27.286 1.00 39.18 ? 153 SER A N 1 ATOM 1042 C CA . SER A 1 138 ? -1.590 12.794 27.261 1.00 40.00 ? 153 SER A CA 1 ATOM 1043 C C . SER A 1 138 ? -2.116 12.815 25.810 1.00 38.04 ? 153 SER A C 1 ATOM 1044 O O . SER A 1 138 ? -2.116 11.796 25.134 1.00 36.55 ? 153 SER A O 1 ATOM 1045 C CB . SER A 1 138 ? -2.677 13.247 28.225 1.00 40.45 ? 153 SER A CB 1 ATOM 1046 O OG . SER A 1 138 ? -2.465 12.709 29.517 1.00 48.17 ? 153 SER A OG 1 ATOM 1047 N N . VAL A 1 139 ? -2.540 13.992 25.361 1.00 36.70 ? 154 VAL A N 1 ATOM 1048 C CA . VAL A 1 139 ? -3.028 14.195 23.989 1.00 36.47 ? 154 VAL A CA 1 ATOM 1049 C C . VAL A 1 139 ? -1.860 14.489 23.031 1.00 35.13 ? 154 VAL A C 1 ATOM 1050 O O . VAL A 1 139 ? -0.952 15.226 23.365 1.00 35.06 ? 154 VAL A O 1 ATOM 1051 C CB . VAL A 1 139 ? -4.024 15.371 23.927 1.00 36.85 ? 154 VAL A CB 1 ATOM 1052 C CG1 . VAL A 1 139 ? -4.534 15.589 22.521 1.00 39.29 ? 154 VAL A CG1 1 ATOM 1053 C CG2 . VAL A 1 139 ? -5.222 15.074 24.821 1.00 38.77 ? 154 VAL A CG2 1 ATOM 1054 N N . LEU A 1 140 ? -1.876 13.887 21.858 1.00 33.33 ? 155 LEU A N 1 ATOM 1055 C CA . LEU A 1 140 ? -0.889 14.134 20.829 1.00 32.83 ? 155 LEU A CA 1 ATOM 1056 C C . LEU A 1 140 ? -0.666 15.651 20.633 1.00 32.02 ? 155 LEU A C 1 ATOM 1057 O O . LEU A 1 140 ? -1.609 16.407 20.629 1.00 33.35 ? 155 LEU A O 1 ATOM 1058 C CB . LEU A 1 140 ? -1.384 13.537 19.491 1.00 32.55 ? 155 LEU A CB 1 ATOM 1059 C CG . LEU A 1 140 ? -0.430 13.702 18.314 1.00 29.78 ? 155 LEU A CG 1 ATOM 1060 C CD1 . LEU A 1 140 ? 0.907 12.980 18.558 1.00 32.46 ? 155 LEU A CD1 1 ATOM 1061 C CD2 . LEU A 1 140 ? -1.153 13.225 16.928 1.00 25.73 ? 155 LEU A CD2 1 ATOM 1062 N N . GLN A 1 141 ? 0.580 16.063 20.511 1.00 31.68 ? 156 GLN A N 1 ATOM 1063 C CA . GLN A 1 141 ? 0.935 17.441 20.340 1.00 32.12 ? 156 GLN A CA 1 ATOM 1064 C C . GLN A 1 141 ? 1.560 17.648 19.010 1.00 32.40 ? 156 GLN A C 1 ATOM 1065 O O . GLN A 1 141 ? 2.179 16.740 18.456 1.00 30.64 ? 156 GLN A O 1 ATOM 1066 C CB . GLN A 1 141 ? 1.987 17.926 21.379 1.00 31.82 ? 156 GLN A CB 1 ATOM 1067 C CG . GLN A 1 141 ? 1.661 17.826 22.871 1.00 31.11 ? 156 GLN A CG 1 ATOM 1068 C CD . GLN A 1 141 ? 0.638 18.827 23.369 1.00 34.18 ? 156 GLN A CD 1 ATOM 1069 O OE1 . GLN A 1 141 ? -0.399 18.422 23.854 1.00 36.75 ? 156 GLN A OE1 1 ATOM 1070 N NE2 . GLN A 1 141 ? 0.926 20.139 23.242 1.00 33.94 ? 156 GLN A NE2 1 ATOM 1071 N N . GLU A 1 142 ? 1.497 18.904 18.547 1.00 32.95 ? 157 GLU A N 1 ATOM 1072 C CA . GLU A 1 142 ? 2.114 19.294 17.298 1.00 33.41 ? 157 GLU A CA 1 ATOM 1073 C C . GLU A 1 142 ? 2.805 20.630 17.441 1.00 34.18 ? 157 GLU A C 1 ATOM 1074 O O . GLU A 1 142 ? 2.453 21.455 18.314 1.00 33.26 ? 157 GLU A O 1 ATOM 1075 C CB . GLU A 1 142 ? 1.086 19.326 16.149 1.00 34.65 ? 157 GLU A CB 1 ATOM 1076 C CG . GLU A 1 142 ? 0.089 20.495 16.200 1.00 37.20 ? 157 GLU A CG 1 ATOM 1077 C CD . GLU A 1 142 ? -0.842 20.546 14.994 1.00 40.45 ? 157 GLU A CD 1 ATOM 1078 O OE1 . GLU A 1 142 ? -1.478 19.524 14.694 1.00 42.30 ? 157 GLU A OE1 1 ATOM 1079 O OE2 . GLU A 1 142 ? -0.892 21.609 14.320 1.00 43.14 ? 157 GLU A OE2 1 ATOM 1080 N N . LEU A 1 143 ? 3.802 20.849 16.592 1.00 34.37 ? 158 LEU A N 1 ATOM 1081 C CA . LEU A 1 143 ? 4.614 22.048 16.703 1.00 35.53 ? 158 LEU A CA 1 ATOM 1082 C C . LEU A 1 143 ? 5.146 22.498 15.344 1.00 35.81 ? 158 LEU A C 1 ATOM 1083 O O . LEU A 1 143 ? 5.806 21.709 14.637 1.00 35.75 ? 158 LEU A O 1 ATOM 1084 C CB . LEU A 1 143 ? 5.794 21.775 17.619 1.00 34.33 ? 158 LEU A CB 1 ATOM 1085 C CG . LEU A 1 143 ? 6.812 22.887 17.726 1.00 36.87 ? 158 LEU A CG 1 ATOM 1086 C CD1 . LEU A 1 143 ? 6.182 24.053 18.607 1.00 31.36 ? 158 LEU A CD1 1 ATOM 1087 C CD2 . LEU A 1 143 ? 8.136 22.395 18.323 1.00 33.59 ? 158 LEU A CD2 1 ATOM 1088 N N . ASN A 1 144 ? 4.879 23.770 14.989 1.00 35.99 ? 159 ASN A N 1 ATOM 1089 C CA . ASN A 1 144 ? 5.388 24.348 13.739 1.00 35.27 ? 159 ASN A CA 1 ATOM 1090 C C . ASN A 1 144 ? 6.883 24.545 13.873 1.00 33.46 ? 159 ASN A C 1 ATOM 1091 O O . ASN A 1 144 ? 7.338 25.086 14.861 1.00 33.58 ? 159 ASN A O 1 ATOM 1092 C CB . ASN A 1 144 ? 4.682 25.669 13.449 1.00 36.50 ? 159 ASN A CB 1 ATOM 1093 C CG . ASN A 1 144 ? 3.366 25.486 12.794 1.00 39.46 ? 159 ASN A CG 1 ATOM 1094 O OD1 . ASN A 1 144 ? 2.385 25.012 13.392 1.00 41.17 ? 159 ASN A OD1 1 ATOM 1095 N ND2 . ASN A 1 144 ? 3.311 25.900 11.526 1.00 44.56 ? 159 ASN A ND2 1 ATOM 1096 N N . VAL A 1 145 ? 7.678 24.028 12.941 1.00 31.08 ? 160 VAL A N 1 ATOM 1097 C CA . VAL A 1 145 ? 9.136 24.148 13.039 1.00 29.96 ? 160 VAL A CA 1 ATOM 1098 C C . VAL A 1 145 ? 9.743 24.597 11.670 1.00 30.75 ? 160 VAL A C 1 ATOM 1099 O O . VAL A 1 145 ? 9.028 24.569 10.679 1.00 30.44 ? 160 VAL A O 1 ATOM 1100 C CB . VAL A 1 145 ? 9.783 22.818 13.515 1.00 31.96 ? 160 VAL A CB 1 ATOM 1101 C CG1 . VAL A 1 145 ? 9.398 22.460 15.029 1.00 26.12 ? 160 VAL A CG1 1 ATOM 1102 C CG2 . VAL A 1 145 ? 9.305 21.595 12.616 1.00 30.93 ? 160 VAL A CG2 1 ATOM 1103 N N . THR A 1 146 ? 11.056 24.931 11.620 1.00 30.98 ? 162 THR A N 1 ATOM 1104 C CA . THR A 1 146 ? 11.687 25.333 10.404 1.00 31.43 ? 162 THR A CA 1 ATOM 1105 C C . THR A 1 146 ? 12.983 24.625 10.136 1.00 31.91 ? 162 THR A C 1 ATOM 1106 O O . THR A 1 146 ? 13.874 24.615 10.997 1.00 31.06 ? 162 THR A O 1 ATOM 1107 C CB . THR A 1 146 ? 12.025 26.886 10.503 1.00 31.51 ? 162 THR A CB 1 ATOM 1108 O OG1 . THR A 1 146 ? 10.804 27.575 10.733 1.00 33.41 ? 162 THR A OG1 1 ATOM 1109 C CG2 . THR A 1 146 ? 12.574 27.410 9.187 1.00 30.55 ? 162 THR A CG2 1 ATOM 1110 N N . VAL A 1 147 ? 13.120 24.083 8.913 1.00 31.19 ? 163 VAL A N 1 ATOM 1111 C CA . VAL A 1 147 ? 14.348 23.417 8.558 1.00 32.66 ? 163 VAL A CA 1 ATOM 1112 C C . VAL A 1 147 ? 15.543 24.339 8.536 1.00 33.67 ? 163 VAL A C 1 ATOM 1113 O O . VAL A 1 147 ? 15.476 25.447 7.963 1.00 34.70 ? 163 VAL A O 1 ATOM 1114 C CB . VAL A 1 147 ? 14.211 22.686 7.168 1.00 32.60 ? 163 VAL A CB 1 ATOM 1115 C CG1 . VAL A 1 147 ? 15.539 22.218 6.682 1.00 33.29 ? 163 VAL A CG1 1 ATOM 1116 C CG2 . VAL A 1 147 ? 13.321 21.517 7.311 1.00 33.79 ? 163 VAL A CG2 1 ATOM 1117 N N . VAL A 1 148 ? 16.661 23.898 9.093 1.00 35.34 ? 164 VAL A N 1 ATOM 1118 C CA . VAL A 1 148 ? 17.861 24.720 9.102 1.00 36.12 ? 164 VAL A CA 1 ATOM 1119 C C . VAL A 1 148 ? 19.098 23.869 8.797 1.00 38.71 ? 164 VAL A C 1 ATOM 1120 O O . VAL A 1 148 ? 19.108 22.640 9.062 1.00 39.14 ? 164 VAL A O 1 ATOM 1121 C CB . VAL A 1 148 ? 18.092 25.352 10.522 1.00 38.28 ? 164 VAL A CB 1 ATOM 1122 C CG1 . VAL A 1 148 ? 16.839 26.184 11.011 1.00 36.82 ? 164 VAL A CG1 1 ATOM 1123 C CG2 . VAL A 1 148 ? 18.363 24.236 11.505 1.00 36.13 ? 164 VAL A CG2 1 ATOM 1124 N N . THR A 1 149 ? 20.178 24.489 8.317 1.00 38.35 ? 165 THR A N 1 ATOM 1125 C CA . THR A 1 149 ? 21.375 23.726 7.999 1.00 39.33 ? 165 THR A CA 1 ATOM 1126 C C . THR A 1 149 ? 22.591 24.042 8.825 1.00 40.13 ? 165 THR A C 1 ATOM 1127 O O . THR A 1 149 ? 23.606 23.364 8.731 1.00 40.78 ? 165 THR A O 1 ATOM 1128 C CB . THR A 1 149 ? 21.728 23.857 6.489 1.00 40.94 ? 165 THR A CB 1 ATOM 1129 O OG1 . THR A 1 149 ? 21.515 25.225 6.050 1.00 41.93 ? 165 THR A OG1 1 ATOM 1130 C CG2 . THR A 1 149 ? 20.743 23.048 5.665 1.00 40.46 ? 165 THR A CG2 1 ATOM 1131 N N . SER A 1 150 ? 22.536 25.106 9.613 1.00 40.81 ? 166 SER A N 1 ATOM 1132 C CA . SER A 1 150 ? 23.654 25.400 10.507 1.00 40.77 ? 166 SER A CA 1 ATOM 1133 C C . SER A 1 150 ? 23.461 24.558 11.741 1.00 38.98 ? 166 SER A C 1 ATOM 1134 O O . SER A 1 150 ? 22.338 24.383 12.180 1.00 39.23 ? 166 SER A O 1 ATOM 1135 C CB . SER A 1 150 ? 23.667 26.889 10.950 1.00 40.59 ? 166 SER A CB 1 ATOM 1136 O OG . SER A 1 150 ? 22.334 27.418 10.909 1.00 44.57 ? 166 SER A OG 1 ATOM 1137 N N . LEU A 1 151 ? 24.569 24.170 12.329 1.00 38.06 ? 167 LEU A N 1 ATOM 1138 C CA . LEU A 1 151 ? 24.614 23.339 13.512 1.00 40.08 ? 167 LEU A CA 1 ATOM 1139 C C . LEU A 1 151 ? 23.902 22.006 13.229 1.00 39.85 ? 167 LEU A C 1 ATOM 1140 O O . LEU A 1 151 ? 23.272 21.429 14.122 1.00 38.25 ? 167 LEU A O 1 ATOM 1141 C CB . LEU A 1 151 ? 23.955 24.049 14.721 1.00 39.17 ? 167 LEU A CB 1 ATOM 1142 C CG . LEU A 1 151 ? 24.523 25.427 15.081 1.00 40.48 ? 167 LEU A CG 1 ATOM 1143 C CD1 . LEU A 1 151 ? 24.084 25.875 16.519 1.00 36.82 ? 167 LEU A CD1 1 ATOM 1144 C CD2 . LEU A 1 151 ? 26.056 25.443 14.970 1.00 41.26 ? 167 LEU A CD2 1 ATOM 1145 N N . CYS A 1 152 ? 23.990 21.556 11.974 1.00 39.82 ? 168 CYS A N 1 ATOM 1146 C CA . CYS A 1 152 ? 23.345 20.327 11.514 1.00 40.13 ? 168 CYS A CA 1 ATOM 1147 C C . CYS A 1 152 ? 24.266 19.505 10.641 1.00 41.30 ? 168 CYS A C 1 ATOM 1148 O O . CYS A 1 152 ? 24.988 20.061 9.785 1.00 38.60 ? 168 CYS A O 1 ATOM 1149 C CB . CYS A 1 152 ? 22.080 20.639 10.695 1.00 40.26 ? 168 CYS A CB 1 ATOM 1150 S SG . CYS A 1 152 ? 21.084 19.136 10.422 1.00 37.05 ? 168 CYS A SG 1 ATOM 1151 N N . ARG A 1 153 ? 24.250 18.176 10.828 1.00 41.10 ? 177 ARG A N 1 ATOM 1152 C CA . ARG A 1 153 ? 25.060 17.320 9.950 1.00 41.52 ? 177 ARG A CA 1 ATOM 1153 C C . ARG A 1 153 ? 24.385 17.237 8.628 1.00 39.69 ? 177 ARG A C 1 ATOM 1154 O O . ARG A 1 153 ? 23.164 17.333 8.521 1.00 38.89 ? 177 ARG A O 1 ATOM 1155 C CB . ARG A 1 153 ? 25.195 15.871 10.517 1.00 42.34 ? 177 ARG A CB 1 ATOM 1156 C CG . ARG A 1 153 ? 26.310 15.711 11.544 1.00 45.56 ? 177 ARG A CG 1 ATOM 1157 C CD . ARG A 1 153 ? 25.928 14.997 12.874 1.00 52.34 ? 177 ARG A CD 1 ATOM 1158 N NE . ARG A 1 153 ? 25.244 13.713 12.753 1.00 54.18 ? 177 ARG A NE 1 ATOM 1159 C CZ . ARG A 1 153 ? 25.147 12.817 13.748 1.00 56.71 ? 177 ARG A CZ 1 ATOM 1160 N NH1 . ARG A 1 153 ? 25.699 13.065 14.935 1.00 56.48 ? 177 ARG A NH1 1 ATOM 1161 N NH2 . ARG A 1 153 ? 24.501 11.668 13.561 1.00 56.36 ? 177 ARG A NH2 1 ATOM 1162 N N . ARG A 1 154 ? 25.194 17.033 7.590 1.00 41.00 ? 178 ARG A N 1 ATOM 1163 C CA . ARG A 1 154 ? 24.677 16.758 6.252 1.00 40.72 ? 178 ARG A CA 1 ATOM 1164 C C . ARG A 1 154 ? 23.788 15.496 6.260 1.00 39.60 ? 178 ARG A C 1 ATOM 1165 O O . ARG A 1 154 ? 22.839 15.367 5.483 1.00 39.26 ? 178 ARG A O 1 ATOM 1166 C CB . ARG A 1 154 ? 25.862 16.523 5.304 1.00 41.40 ? 178 ARG A CB 1 ATOM 1167 C CG . ARG A 1 154 ? 25.566 16.869 3.847 1.00 48.34 ? 178 ARG A CG 1 ATOM 1168 C CD . ARG A 1 154 ? 26.764 16.643 2.926 1.00 57.34 ? 178 ARG A CD 1 ATOM 1169 N NE . ARG A 1 154 ? 26.404 16.030 1.645 1.00 64.11 ? 178 ARG A NE 1 ATOM 1170 C CZ . ARG A 1 154 ? 27.264 15.406 0.832 1.00 68.15 ? 178 ARG A CZ 1 ATOM 1171 N NH1 . ARG A 1 154 ? 26.845 14.884 -0.317 1.00 68.34 ? 178 ARG A NH1 1 ATOM 1172 N NH2 . ARG A 1 154 ? 28.550 15.324 1.153 1.00 68.75 ? 178 ARG A NH2 1 ATOM 1173 N N . SER A 1 155 ? 24.075 14.584 7.177 1.00 39.30 ? 179 SER A N 1 ATOM 1174 C CA . SER A 1 155 ? 23.327 13.311 7.263 1.00 38.09 ? 179 SER A CA 1 ATOM 1175 C C . SER A 1 155 ? 22.054 13.354 8.116 1.00 38.05 ? 179 SER A C 1 ATOM 1176 O O . SER A 1 155 ? 21.441 12.329 8.446 1.00 36.27 ? 179 SER A O 1 ATOM 1177 C CB . SER A 1 155 ? 24.287 12.247 7.732 1.00 37.74 ? 179 SER A CB 1 ATOM 1178 O OG . SER A 1 155 ? 24.892 12.606 8.967 1.00 39.53 ? 179 SER A OG 1 ATOM 1179 N N . ASN A 1 156 ? 21.665 14.572 8.499 1.00 35.56 ? 180 ASN A N 1 ATOM 1180 C CA . ASN A 1 156 ? 20.462 14.813 9.243 1.00 33.96 ? 180 ASN A CA 1 ATOM 1181 C C . ASN A 1 156 ? 19.668 15.873 8.579 1.00 34.38 ? 180 ASN A C 1 ATOM 1182 O O . ASN A 1 156 ? 20.248 16.730 7.891 1.00 34.56 ? 180 ASN A O 1 ATOM 1183 C CB . ASN A 1 156 ? 20.830 15.392 10.644 1.00 34.06 ? 180 ASN A CB 1 ATOM 1184 C CG . ASN A 1 156 ? 21.176 14.333 11.632 1.00 25.88 ? 180 ASN A CG 1 ATOM 1185 O OD1 . ASN A 1 156 ? 22.307 14.238 12.182 1.00 26.68 ? 180 ASN A OD1 1 ATOM 1186 N ND2 . ASN A 1 156 ? 20.213 13.510 11.871 1.00 31.47 ? 180 ASN A ND2 1 ATOM 1187 N N . VAL A 1 157 ? 18.357 15.823 8.795 1.00 33.90 ? 181 VAL A N 1 ATOM 1188 C CA . VAL A 1 157 ? 17.458 16.900 8.487 1.00 34.13 ? 181 VAL A CA 1 ATOM 1189 C C . VAL A 1 157 ? 17.252 17.544 9.888 1.00 35.02 ? 181 VAL A C 1 ATOM 1190 O O . VAL A 1 157 ? 17.061 16.839 10.887 1.00 33.16 ? 181 VAL A O 1 ATOM 1191 C CB . VAL A 1 157 ? 16.118 16.463 7.916 1.00 33.02 ? 181 VAL A CB 1 ATOM 1192 C CG1 . VAL A 1 157 ? 15.247 17.658 7.693 1.00 37.89 ? 181 VAL A CG1 1 ATOM 1193 C CG2 . VAL A 1 157 ? 16.298 15.776 6.527 1.00 33.37 ? 181 VAL A CG2 1 ATOM 1194 N N . CYS A 1 158 ? 17.272 18.866 9.969 1.00 33.83 ? 182 CYS A N 1 ATOM 1195 C CA . CYS A 1 158 ? 17.210 19.472 11.311 1.00 35.06 ? 182 CYS A CA 1 ATOM 1196 C C . CYS A 1 158 ? 16.300 20.656 11.280 1.00 35.51 ? 182 CYS A C 1 ATOM 1197 O O . CYS A 1 158 ? 16.213 21.348 10.234 1.00 34.67 ? 182 CYS A O 1 ATOM 1198 C CB . CYS A 1 158 ? 18.565 19.967 11.816 1.00 32.92 ? 182 CYS A CB 1 ATOM 1199 S SG . CYS A 1 158 ? 20.004 18.984 12.181 1.00 32.55 ? 182 CYS A SG 1 ATOM 1200 N N . THR A 1 159 ? 15.675 20.915 12.452 1.00 35.82 ? 183 THR A N 1 ATOM 1201 C CA . THR A 1 159 ? 14.711 21.956 12.624 1.00 36.09 ? 183 THR A CA 1 ATOM 1202 C C . THR A 1 159 ? 15.048 22.867 13.829 1.00 38.38 ? 183 THR A C 1 ATOM 1203 O O . THR A 1 159 ? 15.874 22.521 14.719 1.00 37.72 ? 183 THR A O 1 ATOM 1204 C CB . THR A 1 159 ? 13.240 21.405 12.734 1.00 36.79 ? 183 THR A CB 1 ATOM 1205 O OG1 . THR A 1 159 ? 13.036 20.675 13.970 1.00 35.90 ? 183 THR A OG1 1 ATOM 1206 C CG2 . THR A 1 159 ? 12.904 20.409 11.591 1.00 32.31 ? 183 THR A CG2 1 ATOM 1207 N N . LEU A 1 160 ? 14.425 24.035 13.830 1.00 37.94 ? 184 LEU A N 1 ATOM 1208 C CA . LEU A 1 160 ? 14.624 24.960 14.953 1.00 39.92 ? 184 LEU A CA 1 ATOM 1209 C C . LEU A 1 160 ? 13.499 25.940 15.087 1.00 39.83 ? 184 LEU A C 1 ATOM 1210 O O . LEU A 1 160 ? 12.955 26.387 14.083 1.00 42.12 ? 184 LEU A O 1 ATOM 1211 C CB . LEU A 1 160 ? 15.970 25.660 14.893 1.00 38.79 ? 184 LEU A CB 1 ATOM 1212 C CG . LEU A 1 160 ? 16.201 26.651 16.050 1.00 39.15 ? 184 LEU A CG 1 ATOM 1213 C CD1 . LEU A 1 160 ? 16.735 26.009 17.340 1.00 30.94 ? 184 LEU A CD1 1 ATOM 1214 C CD2 . LEU A 1 160 ? 17.110 27.797 15.546 1.00 36.23 ? 184 LEU A CD2 1 ATOM 1215 N N . VAL A 1 161 ? 13.071 26.197 16.315 1.00 39.37 ? 185 VAL A N 1 ATOM 1216 C CA . VAL A 1 161 ? 12.019 27.171 16.556 1.00 38.93 ? 185 VAL A CA 1 ATOM 1217 C C . VAL A 1 161 ? 12.737 28.456 16.929 1.00 40.19 ? 185 VAL A C 1 ATOM 1218 O O . VAL A 1 161 ? 13.630 28.498 17.796 1.00 39.62 ? 185 VAL A O 1 ATOM 1219 C CB . VAL A 1 161 ? 11.045 26.755 17.684 1.00 39.12 ? 185 VAL A CB 1 ATOM 1220 C CG1 . VAL A 1 161 ? 10.195 27.927 18.123 1.00 37.79 ? 185 VAL A CG1 1 ATOM 1221 C CG2 . VAL A 1 161 ? 10.146 25.646 17.218 1.00 36.57 ? 185 VAL A CG2 1 ATOM 1222 N N . ARG A 1 162 ? 12.381 29.496 16.214 1.00 41.68 ? 186 ARG A N 1 ATOM 1223 C CA . ARG A 1 162 ? 13.017 30.793 16.387 1.00 43.51 ? 186 ARG A CA 1 ATOM 1224 C C . ARG A 1 162 ? 12.227 31.659 17.341 1.00 42.47 ? 186 ARG A C 1 ATOM 1225 O O . ARG A 1 162 ? 10.996 31.702 17.275 1.00 43.08 ? 186 ARG A O 1 ATOM 1226 C CB . ARG A 1 162 ? 13.032 31.505 15.021 1.00 44.27 ? 186 ARG A CB 1 ATOM 1227 C CG . ARG A 1 162 ? 13.166 30.570 13.805 1.00 48.37 ? 186 ARG A CG 1 ATOM 1228 C CD . ARG A 1 162 ? 14.272 31.070 12.836 1.00 52.75 ? 186 ARG A CD 1 ATOM 1229 N NE . ARG A 1 162 ? 14.252 30.537 11.465 1.00 52.04 ? 186 ARG A NE 1 ATOM 1230 C CZ . ARG A 1 162 ? 15.360 30.179 10.845 1.00 47.41 ? 186 ARG A CZ 1 ATOM 1231 N NH1 . ARG A 1 162 ? 16.511 30.258 11.497 1.00 47.23 ? 186 ARG A NH1 1 ATOM 1232 N NH2 . ARG A 1 162 ? 15.329 29.725 9.614 1.00 48.74 ? 186 ARG A NH2 1 ATOM 1233 N N . GLY A 1 163 A 12.926 32.349 18.227 1.00 42.62 ? 186 GLY A N 1 ATOM 1234 C CA . GLY A 1 163 A 12.281 33.330 19.090 1.00 43.22 ? 186 GLY A CA 1 ATOM 1235 C C . GLY A 1 163 A 11.679 32.854 20.402 1.00 42.46 ? 186 GLY A C 1 ATOM 1236 O O . GLY A 1 163 A 11.103 33.647 21.133 1.00 42.72 ? 186 GLY A O 1 ATOM 1237 N N . ARG A 1 164 ? 11.771 31.548 20.652 1.00 42.02 ? 187 ARG A N 1 ATOM 1238 C CA . ARG A 1 164 ? 11.255 30.953 21.863 1.00 40.10 ? 187 ARG A CA 1 ATOM 1239 C C . ARG A 1 164 ? 11.921 29.585 22.087 1.00 40.02 ? 187 ARG A C 1 ATOM 1240 O O . ARG A 1 164 ? 12.634 29.077 21.226 1.00 40.41 ? 187 ARG A O 1 ATOM 1241 C CB . ARG A 1 164 ? 9.726 30.869 21.864 1.00 41.02 ? 187 ARG A CB 1 ATOM 1242 C CG . ARG A 1 164 ? 9.044 30.277 20.680 1.00 38.87 ? 187 ARG A CG 1 ATOM 1243 C CD . ARG A 1 164 ? 7.556 30.386 20.765 1.00 41.75 ? 187 ARG A CD 1 ATOM 1244 N NE . ARG A 1 164 ? 6.929 29.392 19.911 1.00 44.39 ? 187 ARG A NE 1 ATOM 1245 C CZ . ARG A 1 164 ? 6.273 28.316 20.355 1.00 45.83 ? 187 ARG A CZ 1 ATOM 1246 N NH1 . ARG A 1 164 ? 6.124 28.091 21.653 1.00 41.73 ? 187 ARG A NH1 1 ATOM 1247 N NH2 . ARG A 1 164 ? 5.761 27.460 19.488 1.00 46.63 ? 187 ARG A NH2 1 ATOM 1248 N N . GLN A 1 165 ? 11.734 29.037 23.270 1.00 37.11 ? 188 GLN A N 1 ATOM 1249 C CA . GLN A 1 165 ? 12.295 27.735 23.630 1.00 36.56 ? 188 GLN A CA 1 ATOM 1250 C C . GLN A 1 165 ? 11.243 26.714 23.304 1.00 35.14 ? 188 GLN A C 1 ATOM 1251 O O . GLN A 1 165 ? 10.236 26.627 23.988 1.00 35.96 ? 188 GLN A O 1 ATOM 1252 C CB . GLN A 1 165 ? 12.618 27.734 25.128 1.00 34.29 ? 188 GLN A CB 1 ATOM 1253 C CG . GLN A 1 165 ? 13.998 28.200 25.380 1.00 36.69 ? 188 GLN A CG 1 ATOM 1254 C CD . GLN A 1 165 ? 14.232 28.407 26.875 1.00 45.13 ? 188 GLN A CD 1 ATOM 1255 O OE1 . GLN A 1 165 ? 15.220 28.947 27.274 1.00 45.01 ? 188 GLN A OE1 1 ATOM 1256 N NE2 . GLN A 1 165 ? 13.306 27.959 27.685 1.00 48.14 ? 188 GLN A NE2 1 ATOM 1257 N N . ALA A 1 166 A 11.429 25.959 22.221 1.00 34.17 ? 188 ALA A N 1 ATOM 1258 C CA . ALA A 1 166 A 10.429 24.959 21.830 1.00 31.04 ? 188 ALA A CA 1 ATOM 1259 C C . ALA A 1 166 A 11.103 23.890 20.999 1.00 31.49 ? 188 ALA A C 1 ATOM 1260 O O . ALA A 1 166 A 12.134 24.184 20.350 1.00 31.28 ? 188 ALA A O 1 ATOM 1261 C CB . ALA A 1 166 A 9.259 25.577 21.041 1.00 31.40 ? 188 ALA A CB 1 ATOM 1262 N N . GLY A 1 167 ? 10.583 22.655 21.071 1.00 28.66 ? 189 GLY A N 1 ATOM 1263 C CA . GLY A 1 167 ? 11.140 21.549 20.311 1.00 28.24 ? 189 GLY A CA 1 ATOM 1264 C C . GLY A 1 167 ? 10.667 20.180 20.854 1.00 27.51 ? 189 GLY A C 1 ATOM 1265 O O . GLY A 1 167 ? 9.767 20.115 21.731 1.00 26.80 ? 189 GLY A O 1 ATOM 1266 N N . VAL A 1 168 ? 11.265 19.119 20.317 1.00 26.39 ? 190 VAL A N 1 ATOM 1267 C CA . VAL A 1 168 ? 10.968 17.711 20.707 1.00 25.66 ? 190 VAL A CA 1 ATOM 1268 C C . VAL A 1 168 ? 11.682 17.307 22.018 1.00 25.26 ? 190 VAL A C 1 ATOM 1269 O O . VAL A 1 168 ? 12.690 17.885 22.413 1.00 25.43 ? 190 VAL A O 1 ATOM 1270 C CB . VAL A 1 168 ? 11.336 16.715 19.543 1.00 25.68 ? 190 VAL A CB 1 ATOM 1271 C CG1 . VAL A 1 168 ? 10.454 16.994 18.297 1.00 24.33 ? 190 VAL A CG1 1 ATOM 1272 C CG2 . VAL A 1 168 ? 12.828 16.837 19.188 1.00 26.24 ? 190 VAL A CG2 1 ATOM 1273 N N . CYS A 1 169 ? 11.170 16.289 22.704 1.00 25.51 ? 191 CYS A N 1 ATOM 1274 C CA . CYS A 1 169 ? 11.791 15.933 23.957 1.00 23.27 ? 191 CYS A CA 1 ATOM 1275 C C . CYS A 1 169 ? 11.545 14.419 24.174 1.00 23.90 ? 191 CYS A C 1 ATOM 1276 O O . CYS A 1 169 ? 10.890 13.753 23.362 1.00 21.24 ? 191 CYS A O 1 ATOM 1277 C CB . CYS A 1 169 ? 11.210 16.747 25.151 1.00 25.21 ? 191 CYS A CB 1 ATOM 1278 S SG . CYS A 1 169 ? 12.366 16.899 26.558 1.00 23.56 ? 191 CYS A SG 1 ATOM 1279 N N . PHE A 1 170 ? 12.067 13.927 25.273 1.00 23.45 ? 192 PHE A N 1 ATOM 1280 C CA . PHE A 1 170 ? 11.886 12.500 25.593 1.00 23.82 ? 192 PHE A CA 1 ATOM 1281 C C . PHE A 1 170 ? 10.479 12.025 25.289 1.00 23.54 ? 192 PHE A C 1 ATOM 1282 O O . PHE A 1 170 ? 9.511 12.553 25.769 1.00 24.84 ? 192 PHE A O 1 ATOM 1283 C CB . PHE A 1 170 ? 12.185 12.158 27.054 1.00 23.11 ? 192 PHE A CB 1 ATOM 1284 C CG . PHE A 1 170 ? 11.845 10.703 27.368 1.00 25.38 ? 192 PHE A CG 1 ATOM 1285 C CD1 . PHE A 1 170 ? 12.531 9.685 26.755 1.00 26.98 ? 192 PHE A CD1 1 ATOM 1286 C CD2 . PHE A 1 170 ? 10.766 10.384 28.178 1.00 27.62 ? 192 PHE A CD2 1 ATOM 1287 C CE1 . PHE A 1 170 ? 12.212 8.327 27.008 1.00 30.39 ? 192 PHE A CE1 1 ATOM 1288 C CE2 . PHE A 1 170 ? 10.412 9.045 28.422 1.00 31.76 ? 192 PHE A CE2 1 ATOM 1289 C CZ . PHE A 1 170 ? 11.133 8.023 27.825 1.00 29.11 ? 192 PHE A CZ 1 ATOM 1290 N N . GLY A 1 171 ? 10.354 10.969 24.529 1.00 23.39 ? 193 GLY A N 1 ATOM 1291 C CA . GLY A 1 171 ? 9.041 10.483 24.246 1.00 24.79 ? 193 GLY A CA 1 ATOM 1292 C C . GLY A 1 171 ? 8.676 10.795 22.789 1.00 26.10 ? 193 GLY A C 1 ATOM 1293 O O . GLY A 1 171 ? 7.840 10.158 22.218 1.00 26.77 ? 193 GLY A O 1 ATOM 1294 N N . ASP A 1 172 ? 9.364 11.754 22.167 1.00 28.79 ? 194 ASP A N 1 ATOM 1295 C CA . ASP A 1 172 ? 9.033 12.101 20.800 1.00 28.18 ? 194 ASP A CA 1 ATOM 1296 C C . ASP A 1 172 ? 9.908 11.356 19.833 1.00 29.16 ? 194 ASP A C 1 ATOM 1297 O O . ASP A 1 172 ? 9.622 11.359 18.663 1.00 29.57 ? 194 ASP A O 1 ATOM 1298 C CB . ASP A 1 172 ? 9.216 13.600 20.561 1.00 28.14 ? 194 ASP A CB 1 ATOM 1299 C CG . ASP A 1 172 ? 8.180 14.431 21.266 1.00 26.81 ? 194 ASP A CG 1 ATOM 1300 O OD1 . ASP A 1 172 ? 6.979 14.081 21.324 1.00 30.87 ? 194 ASP A OD1 1 ATOM 1301 O OD2 . ASP A 1 172 ? 8.504 15.482 21.838 1.00 25.69 ? 194 ASP A OD2 1 ATOM 1302 N N . SER A 1 173 ? 10.999 10.759 20.322 1.00 27.95 ? 195 SER A N 1 ATOM 1303 C CA . SER A 1 173 ? 11.921 10.090 19.452 1.00 28.93 ? 195 SER A CA 1 ATOM 1304 C C . SER A 1 173 ? 11.156 8.991 18.639 1.00 27.28 ? 195 SER A C 1 ATOM 1305 O O . SER A 1 173 ? 10.141 8.456 19.110 1.00 26.67 ? 195 SER A O 1 ATOM 1306 C CB . SER A 1 173 ? 13.081 9.447 20.208 1.00 27.88 ? 195 SER A CB 1 ATOM 1307 O OG . SER A 1 173 ? 14.176 10.314 20.213 1.00 30.11 ? 195 SER A OG 1 ATOM 1308 N N . GLY A 1 174 ? 11.549 8.865 17.366 1.00 27.88 ? 196 GLY A N 1 ATOM 1309 C CA . GLY A 1 174 ? 10.883 7.979 16.422 1.00 29.03 ? 196 GLY A CA 1 ATOM 1310 C C . GLY A 1 174 ? 9.673 8.585 15.721 1.00 28.93 ? 196 GLY A C 1 ATOM 1311 O O . GLY A 1 174 ? 9.152 7.984 14.775 1.00 28.29 ? 196 GLY A O 1 ATOM 1312 N N . SER A 1 175 ? 9.232 9.764 16.140 1.00 28.12 ? 197 SER A N 1 ATOM 1313 C CA . SER A 1 175 ? 8.016 10.384 15.535 1.00 29.14 ? 197 SER A CA 1 ATOM 1314 C C . SER A 1 175 ? 8.346 11.052 14.191 1.00 27.39 ? 197 SER A C 1 ATOM 1315 O O . SER A 1 175 ? 9.471 11.370 13.923 1.00 26.54 ? 197 SER A O 1 ATOM 1316 C CB . SER A 1 175 ? 7.331 11.407 16.496 1.00 28.98 ? 197 SER A CB 1 ATOM 1317 O OG . SER A 1 175 ? 7.285 10.905 17.819 1.00 33.44 ? 197 SER A OG 1 ATOM 1318 N N . PRO A 1 176 ? 7.363 11.177 13.324 1.00 27.63 ? 198 PRO A N 1 ATOM 1319 C CA . PRO A 1 176 ? 7.573 11.773 12.012 1.00 29.07 ? 198 PRO A CA 1 ATOM 1320 C C . PRO A 1 176 ? 7.668 13.343 12.060 1.00 30.12 ? 198 PRO A C 1 ATOM 1321 O O . PRO A 1 176 ? 7.029 13.944 12.943 1.00 26.42 ? 198 PRO A O 1 ATOM 1322 C CB . PRO A 1 176 ? 6.296 11.365 11.240 1.00 29.61 ? 198 PRO A CB 1 ATOM 1323 C CG . PRO A 1 176 ? 5.250 11.145 12.329 1.00 29.59 ? 198 PRO A CG 1 ATOM 1324 C CD . PRO A 1 176 ? 5.978 10.730 13.515 1.00 27.23 ? 198 PRO A CD 1 ATOM 1325 N N . LEU A 1 177 ? 8.541 13.880 11.179 1.00 29.52 ? 199 LEU A N 1 ATOM 1326 C CA . LEU A 1 177 ? 8.629 15.277 10.791 1.00 30.32 ? 199 LEU A CA 1 ATOM 1327 C C . LEU A 1 177 ? 7.984 15.379 9.383 1.00 32.62 ? 199 LEU A C 1 ATOM 1328 O O . LEU A 1 177 ? 8.546 14.853 8.393 1.00 32.91 ? 199 LEU A O 1 ATOM 1329 C CB . LEU A 1 177 ? 10.072 15.728 10.731 1.00 30.98 ? 199 LEU A CB 1 ATOM 1330 C CG . LEU A 1 177 ? 10.226 17.204 10.230 1.00 31.96 ? 199 LEU A CG 1 ATOM 1331 C CD1 . LEU A 1 177 ? 9.958 18.122 11.396 1.00 30.94 ? 199 LEU A CD1 1 ATOM 1332 C CD2 . LEU A 1 177 ? 11.613 17.439 9.749 1.00 29.64 ? 199 LEU A CD2 1 ATOM 1333 N N . VAL A 1 178 ? 6.784 15.970 9.311 1.00 33.57 ? 200 VAL A N 1 ATOM 1334 C CA . VAL A 1 178 ? 6.087 16.172 8.065 1.00 36.12 ? 200 VAL A CA 1 ATOM 1335 C C . VAL A 1 178 ? 6.449 17.555 7.436 1.00 37.80 ? 200 VAL A C 1 ATOM 1336 O O . VAL A 1 178 ? 6.387 18.581 8.111 1.00 37.95 ? 200 VAL A O 1 ATOM 1337 C CB . VAL A 1 178 ? 4.621 16.131 8.297 1.00 35.14 ? 200 VAL A CB 1 ATOM 1338 C CG1 . VAL A 1 178 ? 3.889 16.000 6.962 1.00 39.76 ? 200 VAL A CG1 1 ATOM 1339 C CG2 . VAL A 1 178 ? 4.271 14.937 9.176 1.00 38.12 ? 200 VAL A CG2 1 ATOM 1340 N N . CYS A 1 179 ? 6.834 17.547 6.162 1.00 38.82 ? 201 CYS A N 1 ATOM 1341 C CA . CYS A 1 179 ? 7.133 18.760 5.423 1.00 40.72 ? 201 CYS A CA 1 ATOM 1342 C C . CYS A 1 179 ? 6.440 18.667 4.053 1.00 42.08 ? 201 CYS A C 1 ATOM 1343 O O . CYS A 1 179 ? 6.640 17.709 3.292 1.00 42.09 ? 201 CYS A O 1 ATOM 1344 C CB . CYS A 1 179 ? 8.646 18.937 5.252 1.00 39.41 ? 201 CYS A CB 1 ATOM 1345 S SG . CYS A 1 179 ? 9.671 18.752 6.723 1.00 41.39 ? 201 CYS A SG 1 ATOM 1346 N N . ASN A 1 180 ? 5.571 19.629 3.766 1.00 43.88 ? 204 ASN A N 1 ATOM 1347 C CA . ASN A 1 180 ? 4.826 19.628 2.496 1.00 43.88 ? 204 ASN A CA 1 ATOM 1348 C C . ASN A 1 180 ? 4.097 18.311 2.304 1.00 43.19 ? 204 ASN A C 1 ATOM 1349 O O . ASN A 1 180 ? 4.030 17.745 1.212 1.00 43.46 ? 204 ASN A O 1 ATOM 1350 C CB . ASN A 1 180 ? 5.809 19.867 1.367 1.00 43.80 ? 204 ASN A CB 1 ATOM 1351 C CG . ASN A 1 180 ? 6.444 21.239 1.459 1.00 46.53 ? 204 ASN A CG 1 ATOM 1352 O OD1 . ASN A 1 180 ? 5.747 22.219 1.676 1.00 49.41 ? 204 ASN A OD1 1 ATOM 1353 N ND2 . ASN A 1 180 ? 7.763 21.312 1.327 1.00 45.75 ? 204 ASN A ND2 1 ATOM 1354 N N . GLY A 1 181 ? 3.574 17.808 3.404 1.00 41.09 ? 205 GLY A N 1 ATOM 1355 C CA . GLY A 1 181 ? 2.808 16.581 3.378 1.00 38.36 ? 205 GLY A CA 1 ATOM 1356 C C . GLY A 1 181 ? 3.551 15.259 3.233 1.00 36.60 ? 205 GLY A C 1 ATOM 1357 O O . GLY A 1 181 ? 2.894 14.265 3.288 1.00 35.09 ? 205 GLY A O 1 ATOM 1358 N N . LEU A 1 182 ? 4.872 15.251 3.001 1.00 36.25 ? 208 LEU A N 1 ATOM 1359 C CA . LEU A 1 182 ? 5.654 14.018 3.006 1.00 36.71 ? 208 LEU A CA 1 ATOM 1360 C C . LEU A 1 182 ? 6.514 13.877 4.278 1.00 36.41 ? 208 LEU A C 1 ATOM 1361 O O . LEU A 1 182 ? 6.999 14.883 4.853 1.00 37.36 ? 208 LEU A O 1 ATOM 1362 C CB . LEU A 1 182 ? 6.638 13.942 1.830 1.00 37.03 ? 208 LEU A CB 1 ATOM 1363 C CG . LEU A 1 182 ? 6.368 14.530 0.452 1.00 37.13 ? 208 LEU A CG 1 ATOM 1364 C CD1 . LEU A 1 182 ? 7.638 14.484 -0.402 1.00 37.14 ? 208 LEU A CD1 1 ATOM 1365 C CD2 . LEU A 1 182 ? 5.312 13.661 -0.148 1.00 41.00 ? 208 LEU A CD2 1 ATOM 1366 N N . ILE A 1 183 ? 6.766 12.631 4.687 1.00 34.04 ? 209 ILE A N 1 ATOM 1367 C CA . ILE A 1 183 ? 7.624 12.372 5.832 1.00 29.54 ? 209 ILE A CA 1 ATOM 1368 C C . ILE A 1 183 ? 9.060 12.505 5.487 1.00 31.58 ? 209 ILE A C 1 ATOM 1369 O O . ILE A 1 183 ? 9.662 11.624 4.905 1.00 32.20 ? 209 ILE A O 1 ATOM 1370 C CB . ILE A 1 183 ? 7.307 10.982 6.452 1.00 31.46 ? 209 ILE A CB 1 ATOM 1371 C CG1 . ILE A 1 183 ? 5.788 10.852 6.650 1.00 27.64 ? 209 ILE A CG1 1 ATOM 1372 C CG2 . ILE A 1 183 ? 7.937 10.831 7.903 1.00 24.57 ? 209 ILE A CG2 1 ATOM 1373 C CD1 . ILE A 1 183 ? 5.194 12.059 7.355 1.00 33.82 ? 209 ILE A CD1 1 ATOM 1374 N N . HIS A 1 184 ? 9.667 13.611 5.883 1.00 30.64 ? 210 HIS A N 1 ATOM 1375 C CA . HIS A 1 184 ? 11.043 13.820 5.586 1.00 30.83 ? 210 HIS A CA 1 ATOM 1376 C C . HIS A 1 184 ? 11.920 13.482 6.729 1.00 27.95 ? 210 HIS A C 1 ATOM 1377 O O . HIS A 1 184 ? 13.120 13.499 6.583 1.00 28.39 ? 210 HIS A O 1 ATOM 1378 C CB . HIS A 1 184 ? 11.325 15.314 5.146 1.00 30.95 ? 210 HIS A CB 1 ATOM 1379 C CG . HIS A 1 184 ? 10.864 15.632 3.742 1.00 34.36 ? 210 HIS A CG 1 ATOM 1380 N ND1 . HIS A 1 184 ? 11.717 15.653 2.656 1.00 34.63 ? 210 HIS A ND1 1 ATOM 1381 C CD2 . HIS A 1 184 ? 9.633 15.905 3.255 1.00 35.54 ? 210 HIS A CD2 1 ATOM 1382 C CE1 . HIS A 1 184 ? 11.035 15.955 1.567 1.00 37.03 ? 210 HIS A CE1 1 ATOM 1383 N NE2 . HIS A 1 184 ? 9.769 16.124 1.904 1.00 36.83 ? 210 HIS A NE2 1 ATOM 1384 N N . GLY A 1 185 ? 11.370 13.209 7.893 1.00 30.35 ? 211 GLY A N 1 ATOM 1385 C CA . GLY A 1 185 ? 12.260 13.046 9.062 1.00 28.51 ? 211 GLY A CA 1 ATOM 1386 C C . GLY A 1 185 ? 11.732 12.124 10.160 1.00 26.73 ? 211 GLY A C 1 ATOM 1387 O O . GLY A 1 185 ? 10.563 11.987 10.296 1.00 27.29 ? 211 GLY A O 1 ATOM 1388 N N . ILE A 1 186 ? 12.620 11.531 10.946 1.00 25.85 ? 212 ILE A N 1 ATOM 1389 C CA . ILE A 1 186 ? 12.194 10.739 12.097 1.00 24.78 ? 212 ILE A CA 1 ATOM 1390 C C . ILE A 1 186 ? 12.870 11.349 13.255 1.00 22.80 ? 212 ILE A C 1 ATOM 1391 O O . ILE A 1 186 ? 14.091 11.393 13.297 1.00 21.46 ? 212 ILE A O 1 ATOM 1392 C CB . ILE A 1 186 ? 12.653 9.246 11.906 1.00 23.87 ? 212 ILE A CB 1 ATOM 1393 C CG1 . ILE A 1 186 ? 11.850 8.679 10.702 1.00 26.42 ? 212 ILE A CG1 1 ATOM 1394 C CG2 . ILE A 1 186 ? 12.520 8.422 13.234 1.00 24.41 ? 212 ILE A CG2 1 ATOM 1395 C CD1 . ILE A 1 186 ? 12.527 7.386 10.000 1.00 28.15 ? 212 ILE A CD1 1 ATOM 1396 N N . ALA A 1 187 ? 12.099 11.735 14.257 1.00 22.37 ? 213 ALA A N 1 ATOM 1397 C CA . ALA A 1 187 ? 12.789 12.412 15.415 1.00 24.32 ? 213 ALA A CA 1 ATOM 1398 C C . ALA A 1 187 ? 13.931 11.566 16.047 1.00 23.46 ? 213 ALA A C 1 ATOM 1399 O O . ALA A 1 187 ? 13.751 10.317 16.434 1.00 23.08 ? 213 ALA A O 1 ATOM 1400 C CB . ALA A 1 187 ? 11.754 12.895 16.422 1.00 22.62 ? 213 ALA A CB 1 ATOM 1401 N N . SER A 1 188 ? 15.099 12.153 16.177 1.00 21.93 ? 214 SER A N 1 ATOM 1402 C CA . SER A 1 188 ? 16.285 11.352 16.550 1.00 22.95 ? 214 SER A CA 1 ATOM 1403 C C . SER A 1 188 ? 16.988 11.791 17.800 1.00 25.65 ? 214 SER A C 1 ATOM 1404 O O . SER A 1 188 ? 17.073 11.015 18.807 1.00 23.56 ? 214 SER A O 1 ATOM 1405 C CB . SER A 1 188 ? 17.314 11.295 15.376 1.00 24.03 ? 214 SER A CB 1 ATOM 1406 O OG . SER A 1 188 ? 18.521 10.528 15.718 1.00 21.29 ? 214 SER A OG 1 ATOM 1407 N N . PHE A 1 189 ? 17.438 13.077 17.794 1.00 25.06 ? 215 PHE A N 1 ATOM 1408 C CA . PHE A 1 189 ? 18.187 13.588 18.915 1.00 25.78 ? 215 PHE A CA 1 ATOM 1409 C C . PHE A 1 189 ? 18.128 15.128 19.055 1.00 25.96 ? 215 PHE A C 1 ATOM 1410 O O . PHE A 1 189 ? 17.751 15.844 18.098 1.00 26.30 ? 215 PHE A O 1 ATOM 1411 C CB . PHE A 1 189 ? 19.630 13.097 18.934 1.00 25.84 ? 215 PHE A CB 1 ATOM 1412 C CG . PHE A 1 189 ? 20.539 13.695 17.849 1.00 30.56 ? 215 PHE A CG 1 ATOM 1413 C CD1 . PHE A 1 189 ? 20.747 13.010 16.629 1.00 32.46 ? 215 PHE A CD1 1 ATOM 1414 C CD2 . PHE A 1 189 ? 21.222 14.896 18.073 1.00 31.69 ? 215 PHE A CD2 1 ATOM 1415 C CE1 . PHE A 1 189 ? 21.615 13.503 15.627 1.00 31.33 ? 215 PHE A CE1 1 ATOM 1416 C CE2 . PHE A 1 189 ? 22.087 15.449 17.047 1.00 36.72 ? 215 PHE A CE2 1 ATOM 1417 C CZ . PHE A 1 189 ? 22.300 14.721 15.821 1.00 32.88 ? 215 PHE A CZ 1 ATOM 1418 N N . VAL A 1 190 ? 18.488 15.567 20.238 1.00 27.03 ? 216 VAL A N 1 ATOM 1419 C CA . VAL A 1 190 ? 18.476 16.971 20.659 1.00 27.67 ? 216 VAL A CA 1 ATOM 1420 C C . VAL A 1 190 ? 19.794 17.253 21.255 1.00 28.09 ? 216 VAL A C 1 ATOM 1421 O O . VAL A 1 190 ? 20.512 16.331 21.577 1.00 29.04 ? 216 VAL A O 1 ATOM 1422 C CB . VAL A 1 190 ? 17.331 17.355 21.682 1.00 27.98 ? 216 VAL A CB 1 ATOM 1423 C CG1 . VAL A 1 190 ? 16.026 17.056 21.151 1.00 26.68 ? 216 VAL A CG1 1 ATOM 1424 C CG2 . VAL A 1 190 ? 17.543 16.778 23.069 1.00 26.74 ? 216 VAL A CG2 1 ATOM 1425 N N . ARG A 1 191 A 20.151 18.535 21.400 1.00 29.89 ? 217 ARG A N 1 ATOM 1426 C CA . ARG A 1 191 A 21.462 18.923 21.963 1.00 32.25 ? 217 ARG A CA 1 ATOM 1427 C C . ARG A 1 191 A 21.267 20.132 22.915 1.00 32.29 ? 217 ARG A C 1 ATOM 1428 O O . ARG A 1 191 A 20.373 20.987 22.688 1.00 31.15 ? 217 ARG A O 1 ATOM 1429 C CB . ARG A 1 191 A 22.468 19.334 20.856 1.00 32.36 ? 217 ARG A CB 1 ATOM 1430 C CG . ARG A 1 191 A 23.226 18.208 20.132 1.00 37.47 ? 217 ARG A CG 1 ATOM 1431 C CD . ARG A 1 191 A 23.870 18.581 18.754 1.00 43.00 ? 217 ARG A CD 1 ATOM 1432 N NE . ARG A 1 191 A 22.871 18.670 17.678 1.00 47.00 ? 217 ARG A NE 1 ATOM 1433 C CZ . ARG A 1 191 A 22.828 19.662 16.790 1.00 51.92 ? 217 ARG A CZ 1 ATOM 1434 N NH1 . ARG A 1 191 A 23.734 20.632 16.831 1.00 50.80 ? 217 ARG A NH1 1 ATOM 1435 N NH2 . ARG A 1 191 A 21.884 19.682 15.855 1.00 57.76 ? 217 ARG A NH2 1 ATOM 1436 N N . GLY A 1 192 ? 22.084 20.154 23.970 1.00 32.26 ? 218 GLY A N 1 ATOM 1437 C CA . GLY A 1 192 ? 21.979 21.219 24.974 1.00 33.28 ? 218 GLY A CA 1 ATOM 1438 C C . GLY A 1 192 ? 20.675 21.029 25.739 1.00 33.31 ? 218 GLY A C 1 ATOM 1439 O O . GLY A 1 192 ? 20.132 21.965 26.310 1.00 32.67 ? 218 GLY A O 1 ATOM 1440 N N . GLY A 1 193 ? 20.163 19.789 25.800 1.00 32.40 ? 219 GLY A N 1 ATOM 1441 C CA . GLY A 1 193 ? 18.872 19.631 26.489 1.00 29.93 ? 219 GLY A CA 1 ATOM 1442 C C . GLY A 1 193 ? 17.718 19.931 25.545 1.00 28.97 ? 219 GLY A C 1 ATOM 1443 O O . GLY A 1 193 ? 17.926 20.406 24.434 1.00 29.18 ? 219 GLY A O 1 ATOM 1444 N N . CYS A 1 194 ? 16.500 19.622 25.977 1.00 27.49 ? 220 CYS A N 1 ATOM 1445 C CA . CYS A 1 194 ? 15.329 19.831 25.196 1.00 25.54 ? 220 CYS A CA 1 ATOM 1446 C C . CYS A 1 194 ? 15.044 21.341 25.149 1.00 27.41 ? 220 CYS A C 1 ATOM 1447 O O . CYS A 1 194 ? 15.120 22.047 26.183 1.00 25.58 ? 220 CYS A O 1 ATOM 1448 C CB . CYS A 1 194 ? 14.108 19.139 25.831 1.00 24.26 ? 220 CYS A CB 1 ATOM 1449 S SG . CYS A 1 194 ? 14.186 17.281 25.903 1.00 23.85 ? 220 CYS A SG 1 ATOM 1450 N N . ALA A 1 195 ? 14.728 21.788 23.937 1.00 24.96 ? 221 ALA A N 1 ATOM 1451 C CA . ALA A 1 195 ? 14.246 23.105 23.733 1.00 26.77 ? 221 ALA A CA 1 ATOM 1452 C C . ALA A 1 195 ? 15.174 24.154 24.321 1.00 26.44 ? 221 ALA A C 1 ATOM 1453 O O . ALA A 1 195 ? 14.731 25.038 25.065 1.00 27.17 ? 221 ALA A O 1 ATOM 1454 C CB . ALA A 1 195 ? 12.703 23.188 24.264 1.00 25.85 ? 221 ALA A CB 1 ATOM 1455 N N . SER A 1 196 ? 16.459 24.058 23.942 1.00 28.05 ? 222 SER A N 1 ATOM 1456 C CA . SER A 1 196 ? 17.524 24.908 24.390 1.00 27.59 ? 222 SER A CA 1 ATOM 1457 C C . SER A 1 196 ? 17.420 26.331 23.791 1.00 28.69 ? 222 SER A C 1 ATOM 1458 O O . SER A 1 196 ? 17.909 27.239 24.407 1.00 29.11 ? 222 SER A O 1 ATOM 1459 C CB . SER A 1 196 ? 18.871 24.320 24.000 1.00 29.67 ? 222 SER A CB 1 ATOM 1460 O OG . SER A 1 196 ? 19.178 24.384 22.580 1.00 29.57 ? 222 SER A OG 1 ATOM 1461 N N . GLY A 1 197 A 16.755 26.472 22.638 1.00 28.56 ? 222 GLY A N 1 ATOM 1462 C CA . GLY A 1 197 A 16.690 27.678 21.845 1.00 30.92 ? 222 GLY A CA 1 ATOM 1463 C C . GLY A 1 197 A 18.053 27.896 21.219 1.00 32.14 ? 222 GLY A C 1 ATOM 1464 O O . GLY A 1 197 A 18.253 28.854 20.449 1.00 34.23 ? 222 GLY A O 1 ATOM 1465 N N . LEU A 1 198 ? 19.014 27.041 21.537 1.00 30.09 ? 223 LEU A N 1 ATOM 1466 C CA . LEU A 1 198 ? 20.319 27.235 20.973 1.00 31.34 ? 223 LEU A CA 1 ATOM 1467 C C . LEU A 1 198 ? 20.675 26.261 19.805 1.00 31.99 ? 223 LEU A C 1 ATOM 1468 O O . LEU A 1 198 ? 21.225 26.653 18.770 1.00 33.32 ? 223 LEU A O 1 ATOM 1469 C CB . LEU A 1 198 ? 21.337 27.119 22.073 1.00 29.74 ? 223 LEU A CB 1 ATOM 1470 C CG . LEU A 1 198 ? 21.283 28.081 23.251 1.00 32.70 ? 223 LEU A CG 1 ATOM 1471 C CD1 . LEU A 1 198 ? 22.500 27.836 24.169 1.00 28.67 ? 223 LEU A CD1 1 ATOM 1472 C CD2 . LEU A 1 198 ? 21.215 29.574 22.734 1.00 26.58 ? 223 LEU A CD2 1 ATOM 1473 N N . TYR A 1 199 ? 20.370 24.989 19.996 1.00 31.59 ? 224 TYR A N 1 ATOM 1474 C CA . TYR A 1 199 ? 20.680 23.936 19.014 1.00 29.94 ? 224 TYR A CA 1 ATOM 1475 C C . TYR A 1 199 ? 19.411 23.416 18.355 1.00 28.80 ? 224 TYR A C 1 ATOM 1476 O O . TYR A 1 199 ? 18.362 23.286 19.012 1.00 27.78 ? 224 TYR A O 1 ATOM 1477 C CB . TYR A 1 199 ? 21.353 22.848 19.770 1.00 31.29 ? 224 TYR A CB 1 ATOM 1478 C CG . TYR A 1 199 ? 22.628 23.246 20.461 1.00 32.85 ? 224 TYR A CG 1 ATOM 1479 C CD1 . TYR A 1 199 ? 23.806 23.316 19.774 1.00 33.48 ? 224 TYR A CD1 1 ATOM 1480 C CD2 . TYR A 1 199 ? 22.658 23.471 21.846 1.00 36.76 ? 224 TYR A CD2 1 ATOM 1481 C CE1 . TYR A 1 199 ? 24.966 23.634 20.414 1.00 38.17 ? 224 TYR A CE1 1 ATOM 1482 C CE2 . TYR A 1 199 ? 23.837 23.793 22.503 1.00 37.79 ? 224 TYR A CE2 1 ATOM 1483 C CZ . TYR A 1 199 ? 24.982 23.870 21.786 1.00 40.25 ? 224 TYR A CZ 1 ATOM 1484 O OH . TYR A 1 199 ? 26.178 24.164 22.430 1.00 45.18 ? 224 TYR A OH 1 ATOM 1485 N N . PRO A 1 200 ? 19.469 23.155 17.047 1.00 27.56 ? 225 PRO A N 1 ATOM 1486 C CA . PRO A 1 200 ? 18.319 22.655 16.287 1.00 27.47 ? 225 PRO A CA 1 ATOM 1487 C C . PRO A 1 200 ? 18.053 21.170 16.667 1.00 26.80 ? 225 PRO A C 1 ATOM 1488 O O . PRO A 1 200 ? 18.974 20.549 17.088 1.00 25.44 ? 225 PRO A O 1 ATOM 1489 C CB . PRO A 1 200 ? 18.814 22.608 14.818 1.00 28.15 ? 225 PRO A CB 1 ATOM 1490 C CG . PRO A 1 200 ? 20.322 22.808 14.881 1.00 28.50 ? 225 PRO A CG 1 ATOM 1491 C CD . PRO A 1 200 ? 20.711 23.251 16.248 1.00 28.93 ? 225 PRO A CD 1 ATOM 1492 N N . ASP A 1 201 ? 16.834 20.704 16.515 1.00 27.24 ? 226 ASP A N 1 ATOM 1493 C CA . ASP A 1 201 ? 16.484 19.303 16.715 1.00 28.28 ? 226 ASP A CA 1 ATOM 1494 C C . ASP A 1 201 ? 16.897 18.515 15.456 1.00 30.31 ? 226 ASP A C 1 ATOM 1495 O O . ASP A 1 201 ? 16.745 19.009 14.355 1.00 29.89 ? 226 ASP A O 1 ATOM 1496 C CB . ASP A 1 201 ? 14.986 19.199 16.917 1.00 25.59 ? 226 ASP A CB 1 ATOM 1497 C CG . ASP A 1 201 ? 14.548 19.787 18.236 1.00 24.70 ? 226 ASP A CG 1 ATOM 1498 O OD1 . ASP A 1 201 ? 13.319 19.927 18.406 1.00 24.32 ? 226 ASP A OD1 1 ATOM 1499 O OD2 . ASP A 1 201 ? 15.393 20.104 19.130 1.00 20.40 ? 226 ASP A OD2 1 ATOM 1500 N N . ALA A 1 202 ? 17.417 17.299 15.644 1.00 30.57 ? 227 ALA A N 1 ATOM 1501 C CA . ALA A 1 202 ? 17.865 16.459 14.512 1.00 30.97 ? 227 ALA A CA 1 ATOM 1502 C C . ALA A 1 202 ? 16.964 15.216 14.237 1.00 31.27 ? 227 ALA A C 1 ATOM 1503 O O . ALA A 1 202 ? 16.533 14.496 15.175 1.00 27.65 ? 227 ALA A O 1 ATOM 1504 C CB . ALA A 1 202 ? 19.296 16.046 14.721 1.00 28.34 ? 227 ALA A CB 1 ATOM 1505 N N . PHE A 1 203 ? 16.671 15.010 12.941 1.00 30.58 ? 228 PHE A N 1 ATOM 1506 C CA . PHE A 1 203 ? 15.811 13.981 12.495 1.00 30.54 ? 228 PHE A CA 1 ATOM 1507 C C . PHE A 1 203 ? 16.577 13.227 11.411 1.00 32.13 ? 228 PHE A C 1 ATOM 1508 O O . PHE A 1 203 ? 17.435 13.787 10.700 1.00 32.56 ? 228 PHE A O 1 ATOM 1509 C CB . PHE A 1 203 ? 14.464 14.414 11.897 1.00 30.40 ? 228 PHE A CB 1 ATOM 1510 C CG . PHE A 1 203 ? 13.664 15.320 12.716 1.00 32.53 ? 228 PHE A CG 1 ATOM 1511 C CD1 . PHE A 1 203 ? 12.404 14.962 13.127 1.00 30.46 ? 228 PHE A CD1 1 ATOM 1512 C CD2 . PHE A 1 203 ? 14.152 16.582 13.067 1.00 31.25 ? 228 PHE A CD2 1 ATOM 1513 C CE1 . PHE A 1 203 ? 11.644 15.816 13.880 1.00 34.20 ? 228 PHE A CE1 1 ATOM 1514 C CE2 . PHE A 1 203 ? 13.379 17.416 13.852 1.00 32.94 ? 228 PHE A CE2 1 ATOM 1515 C CZ . PHE A 1 203 ? 12.133 17.038 14.236 1.00 31.18 ? 228 PHE A CZ 1 ATOM 1516 N N . ALA A 1 204 ? 16.329 11.922 11.391 1.00 28.41 ? 229 ALA A N 1 ATOM 1517 C CA . ALA A 1 204 ? 16.891 11.036 10.399 1.00 27.44 ? 229 ALA A CA 1 ATOM 1518 C C . ALA A 1 204 ? 16.272 11.393 9.089 1.00 25.09 ? 229 ALA A C 1 ATOM 1519 O O . ALA A 1 204 ? 15.063 11.566 8.967 1.00 27.48 ? 229 ALA A O 1 ATOM 1520 C CB . ALA A 1 204 ? 16.478 9.566 10.753 1.00 25.69 ? 229 ALA A CB 1 ATOM 1521 N N . PRO A 1 205 ? 17.086 11.485 8.082 1.00 26.77 ? 230 PRO A N 1 ATOM 1522 C CA . PRO A 1 205 ? 16.604 11.932 6.775 1.00 28.38 ? 230 PRO A CA 1 ATOM 1523 C C . PRO A 1 205 ? 15.936 10.851 5.975 1.00 29.79 ? 230 PRO A C 1 ATOM 1524 O O . PRO A 1 205 ? 16.648 10.180 5.226 1.00 31.01 ? 230 PRO A O 1 ATOM 1525 C CB . PRO A 1 205 ? 17.880 12.377 6.058 1.00 27.73 ? 230 PRO A CB 1 ATOM 1526 C CG . PRO A 1 205 ? 18.963 11.903 6.801 1.00 29.53 ? 230 PRO A CG 1 ATOM 1527 C CD . PRO A 1 205 ? 18.524 11.221 8.104 1.00 25.39 ? 230 PRO A CD 1 ATOM 1528 N N . VAL A 1 206 ? 14.618 10.781 5.999 1.00 30.64 ? 231 VAL A N 1 ATOM 1529 C CA . VAL A 1 206 ? 13.947 9.658 5.442 1.00 33.86 ? 231 VAL A CA 1 ATOM 1530 C C . VAL A 1 206 ? 14.317 9.473 3.954 1.00 36.56 ? 231 VAL A C 1 ATOM 1531 O O . VAL A 1 206 ? 14.379 8.348 3.427 1.00 35.04 ? 231 VAL A O 1 ATOM 1532 C CB . VAL A 1 206 ? 12.428 9.852 5.504 1.00 33.82 ? 231 VAL A CB 1 ATOM 1533 C CG1 . VAL A 1 206 ? 11.741 8.810 4.638 1.00 34.81 ? 231 VAL A CG1 1 ATOM 1534 C CG2 . VAL A 1 206 ? 11.917 9.773 6.931 1.00 36.18 ? 231 VAL A CG2 1 ATOM 1535 N N . ALA A 1 207 ? 14.497 10.610 3.287 1.00 36.22 ? 232 ALA A N 1 ATOM 1536 C CA . ALA A 1 207 ? 14.635 10.639 1.847 1.00 37.66 ? 232 ALA A CA 1 ATOM 1537 C C . ALA A 1 207 ? 15.878 9.940 1.410 1.00 38.42 ? 232 ALA A C 1 ATOM 1538 O O . ALA A 1 207 ? 15.940 9.386 0.324 1.00 39.46 ? 232 ALA A O 1 ATOM 1539 C CB . ALA A 1 207 ? 14.642 12.182 1.359 1.00 38.48 ? 232 ALA A CB 1 ATOM 1540 N N . GLN A 1 208 ? 16.854 9.878 2.293 1.00 37.71 ? 233 GLN A N 1 ATOM 1541 C CA . GLN A 1 208 ? 18.077 9.205 1.957 1.00 39.07 ? 233 GLN A CA 1 ATOM 1542 C C . GLN A 1 208 ? 17.897 7.623 2.023 1.00 39.65 ? 233 GLN A C 1 ATOM 1543 O O . GLN A 1 208 ? 18.834 6.894 1.736 1.00 39.35 ? 233 GLN A O 1 ATOM 1544 C CB . GLN A 1 208 ? 19.162 9.576 2.948 1.00 38.73 ? 233 GLN A CB 1 ATOM 1545 C CG . GLN A 1 208 ? 19.583 11.077 3.015 1.00 42.17 ? 233 GLN A CG 1 ATOM 1546 C CD . GLN A 1 208 ? 20.911 11.255 3.839 1.00 48.05 ? 233 GLN A CD 1 ATOM 1547 O OE1 . GLN A 1 208 ? 21.610 10.277 4.107 1.00 50.69 ? 233 GLN A OE1 1 ATOM 1548 N NE2 . GLN A 1 208 ? 21.214 12.482 4.257 1.00 50.17 ? 233 GLN A NE2 1 ATOM 1549 N N . PHE A 1 209 ? 16.692 7.171 2.379 1.00 37.91 ? 234 PHE A N 1 ATOM 1550 C CA . PHE A 1 209 ? 16.440 5.757 2.704 1.00 37.92 ? 234 PHE A CA 1 ATOM 1551 C C . PHE A 1 209 ? 15.287 5.215 1.883 1.00 38.01 ? 234 PHE A C 1 ATOM 1552 O O . PHE A 1 209 ? 14.989 4.009 1.915 1.00 36.59 ? 234 PHE A O 1 ATOM 1553 C CB . PHE A 1 209 ? 16.163 5.609 4.252 1.00 36.81 ? 234 PHE A CB 1 ATOM 1554 C CG . PHE A 1 209 ? 17.387 5.855 5.089 1.00 33.94 ? 234 PHE A CG 1 ATOM 1555 C CD1 . PHE A 1 209 ? 17.606 7.078 5.700 1.00 36.57 ? 234 PHE A CD1 1 ATOM 1556 C CD2 . PHE A 1 209 ? 18.332 4.902 5.214 1.00 36.78 ? 234 PHE A CD2 1 ATOM 1557 C CE1 . PHE A 1 209 ? 18.750 7.309 6.415 1.00 31.97 ? 234 PHE A CE1 1 ATOM 1558 C CE2 . PHE A 1 209 ? 19.456 5.119 5.920 1.00 34.91 ? 234 PHE A CE2 1 ATOM 1559 C CZ . PHE A 1 209 ? 19.650 6.354 6.546 1.00 37.70 ? 234 PHE A CZ 1 ATOM 1560 N N . VAL A 1 210 ? 14.651 6.117 1.128 1.00 37.62 ? 235 VAL A N 1 ATOM 1561 C CA . VAL A 1 210 ? 13.508 5.679 0.328 1.00 38.06 ? 235 VAL A CA 1 ATOM 1562 C C . VAL A 1 210 ? 13.689 4.330 -0.517 1.00 38.37 ? 235 VAL A C 1 ATOM 1563 O O . VAL A 1 210 ? 12.769 3.531 -0.523 1.00 37.34 ? 235 VAL A O 1 ATOM 1564 C CB . VAL A 1 210 ? 12.787 6.774 -0.444 1.00 38.31 ? 235 VAL A CB 1 ATOM 1565 C CG1 . VAL A 1 210 ? 12.029 6.214 -1.680 1.00 32.29 ? 235 VAL A CG1 1 ATOM 1566 C CG2 . VAL A 1 210 ? 11.813 7.445 0.514 1.00 39.85 ? 235 VAL A CG2 1 ATOM 1567 N N . ASN A 1 211 ? 14.823 4.181 -1.227 1.00 38.30 ? 236 ASN A N 1 ATOM 1568 C CA . ASN A 1 211 ? 15.091 3.020 -2.105 1.00 39.18 ? 236 ASN A CA 1 ATOM 1569 C C . ASN A 1 211 ? 15.168 1.737 -1.227 1.00 39.04 ? 236 ASN A C 1 ATOM 1570 O O . ASN A 1 211 ? 14.699 0.694 -1.625 1.00 38.52 ? 236 ASN A O 1 ATOM 1571 C CB . ASN A 1 211 ? 16.444 3.146 -2.867 1.00 39.60 ? 236 ASN A CB 1 ATOM 1572 C CG . ASN A 1 211 ? 16.399 4.086 -4.128 1.00 39.39 ? 236 ASN A CG 1 ATOM 1573 O OD1 . ASN A 1 211 ? 17.451 4.416 -4.695 1.00 37.92 ? 236 ASN A OD1 1 ATOM 1574 N ND2 . ASN A 1 211 ? 15.213 4.483 -4.551 1.00 33.93 ? 236 ASN A ND2 1 ATOM 1575 N N . TRP A 1 212 ? 15.796 1.827 -0.055 1.00 39.51 ? 237 TRP A N 1 ATOM 1576 C CA . TRP A 1 212 ? 15.976 0.678 0.838 1.00 39.18 ? 237 TRP A CA 1 ATOM 1577 C C . TRP A 1 212 ? 14.637 0.320 1.426 1.00 39.08 ? 237 TRP A C 1 ATOM 1578 O O . TRP A 1 212 ? 14.286 -0.906 1.541 1.00 37.53 ? 237 TRP A O 1 ATOM 1579 C CB . TRP A 1 212 ? 16.966 1.032 1.955 1.00 39.97 ? 237 TRP A CB 1 ATOM 1580 C CG . TRP A 1 212 ? 17.054 0.056 3.123 1.00 39.52 ? 237 TRP A CG 1 ATOM 1581 C CD1 . TRP A 1 212 ? 17.535 -1.250 3.096 1.00 41.64 ? 237 TRP A CD1 1 ATOM 1582 C CD2 . TRP A 1 212 ? 16.686 0.314 4.475 1.00 35.50 ? 237 TRP A CD2 1 ATOM 1583 N NE1 . TRP A 1 212 ? 17.485 -1.788 4.353 1.00 38.26 ? 237 TRP A NE1 1 ATOM 1584 C CE2 . TRP A 1 212 ? 16.957 -0.864 5.222 1.00 37.40 ? 237 TRP A CE2 1 ATOM 1585 C CE3 . TRP A 1 212 ? 16.148 1.425 5.145 1.00 35.38 ? 237 TRP A CE3 1 ATOM 1586 C CZ2 . TRP A 1 212 ? 16.712 -0.965 6.613 1.00 34.72 ? 237 TRP A CZ2 1 ATOM 1587 C CZ3 . TRP A 1 212 ? 15.916 1.334 6.541 1.00 37.53 ? 237 TRP A CZ3 1 ATOM 1588 C CH2 . TRP A 1 212 ? 16.183 0.123 7.253 1.00 35.08 ? 237 TRP A CH2 1 ATOM 1589 N N . ILE A 1 213 ? 13.892 1.361 1.786 1.00 37.25 ? 238 ILE A N 1 ATOM 1590 C CA . ILE A 1 213 ? 12.575 1.187 2.358 1.00 35.69 ? 238 ILE A CA 1 ATOM 1591 C C . ILE A 1 213 ? 11.648 0.505 1.351 1.00 37.81 ? 238 ILE A C 1 ATOM 1592 O O . ILE A 1 213 ? 11.015 -0.509 1.676 1.00 37.08 ? 238 ILE A O 1 ATOM 1593 C CB . ILE A 1 213 ? 12.035 2.503 2.819 1.00 35.83 ? 238 ILE A CB 1 ATOM 1594 C CG1 . ILE A 1 213 ? 12.838 2.967 4.034 1.00 33.81 ? 238 ILE A CG1 1 ATOM 1595 C CG2 . ILE A 1 213 ? 10.531 2.422 3.125 1.00 32.17 ? 238 ILE A CG2 1 ATOM 1596 C CD1 . ILE A 1 213 ? 12.625 4.447 4.386 1.00 37.36 ? 238 ILE A CD1 1 ATOM 1597 N N . ASP A 1 214 ? 11.591 1.028 0.126 1.00 37.05 ? 239 ASP A N 1 ATOM 1598 C CA . ASP A 1 214 ? 10.740 0.403 -0.863 1.00 38.14 ? 239 ASP A CA 1 ATOM 1599 C C . ASP A 1 214 ? 11.134 -1.077 -1.008 1.00 37.33 ? 239 ASP A C 1 ATOM 1600 O O . ASP A 1 214 ? 10.280 -1.889 -1.073 1.00 38.44 ? 239 ASP A O 1 ATOM 1601 C CB . ASP A 1 214 ? 10.799 1.087 -2.238 1.00 38.13 ? 239 ASP A CB 1 ATOM 1602 C CG . ASP A 1 214 ? 10.112 2.479 -2.263 1.00 42.29 ? 239 ASP A CG 1 ATOM 1603 O OD1 . ASP A 1 214 ? 10.681 3.418 -2.921 1.00 39.08 ? 239 ASP A OD1 1 ATOM 1604 O OD2 . ASP A 1 214 ? 9.026 2.709 -1.684 1.00 46.02 ? 239 ASP A OD2 1 ATOM 1605 N N . SER A 1 215 ? 12.417 -1.404 -1.064 1.00 38.03 ? 240 SER A N 1 ATOM 1606 C CA . SER A 1 215 ? 12.844 -2.770 -1.245 1.00 40.82 ? 240 SER A CA 1 ATOM 1607 C C . SER A 1 215 ? 12.400 -3.723 -0.124 1.00 41.96 ? 240 SER A C 1 ATOM 1608 O O . SER A 1 215 ? 12.474 -4.952 -0.278 1.00 42.88 ? 240 SER A O 1 ATOM 1609 C CB . SER A 1 215 ? 14.359 -2.823 -1.374 1.00 41.54 ? 240 SER A CB 1 ATOM 1610 O OG . SER A 1 215 ? 15.000 -2.963 -0.116 1.00 46.27 ? 240 SER A OG 1 ATOM 1611 N N . ILE A 1 216 ? 11.982 -3.186 1.015 1.00 41.25 ? 241 ILE A N 1 ATOM 1612 C CA . ILE A 1 216 ? 11.564 -4.027 2.132 1.00 39.94 ? 241 ILE A CA 1 ATOM 1613 C C . ILE A 1 216 ? 10.078 -4.090 2.103 1.00 40.82 ? 241 ILE A C 1 ATOM 1614 O O . ILE A 1 216 ? 9.494 -5.102 2.390 1.00 39.14 ? 241 ILE A O 1 ATOM 1615 C CB . ILE A 1 216 ? 11.975 -3.381 3.469 1.00 39.25 ? 241 ILE A CB 1 ATOM 1616 C CG1 . ILE A 1 216 ? 13.466 -3.531 3.649 1.00 37.53 ? 241 ILE A CG1 1 ATOM 1617 C CG2 . ILE A 1 216 ? 11.069 -3.895 4.645 1.00 36.96 ? 241 ILE A CG2 1 ATOM 1618 C CD1 . ILE A 1 216 ? 13.991 -2.653 4.688 1.00 38.94 ? 241 ILE A CD1 1 ATOM 1619 N N . ILE A 1 217 ? 9.469 -2.973 1.754 1.00 41.89 ? 242 ILE A N 1 ATOM 1620 C CA . ILE A 1 217 ? 8.032 -2.881 1.781 1.00 45.61 ? 242 ILE A CA 1 ATOM 1621 C C . ILE A 1 217 ? 7.377 -3.433 0.535 1.00 46.78 ? 242 ILE A C 1 ATOM 1622 O O . ILE A 1 217 ? 6.200 -3.800 0.588 1.00 46.41 ? 242 ILE A O 1 ATOM 1623 C CB . ILE A 1 217 ? 7.659 -1.405 1.994 1.00 47.34 ? 242 ILE A CB 1 ATOM 1624 C CG1 . ILE A 1 217 ? 6.185 -1.211 2.333 1.00 49.89 ? 242 ILE A CG1 1 ATOM 1625 C CG2 . ILE A 1 217 ? 8.069 -0.494 0.787 1.00 47.89 ? 242 ILE A CG2 1 ATOM 1626 C CD1 . ILE A 1 217 ? 5.839 0.295 2.493 1.00 51.26 ? 242 ILE A CD1 1 ATOM 1627 N N . GLN A 1 218 ? 8.144 -3.508 -0.560 1.00 49.09 ? 243 GLN A N 1 ATOM 1628 C CA . GLN A 1 218 ? 7.635 -3.953 -1.878 1.00 52.54 ? 243 GLN A CA 1 ATOM 1629 C C . GLN A 1 218 ? 6.349 -4.765 -1.777 1.00 53.40 ? 243 GLN A C 1 ATOM 1630 O O . GLN A 1 218 ? 6.432 -5.988 -1.686 1.00 55.86 ? 243 GLN A O 1 ATOM 1631 C CB . GLN A 1 218 ? 8.683 -4.809 -2.589 1.00 53.65 ? 243 GLN A CB 1 ATOM 1632 C CG . GLN A 1 218 ? 9.070 -6.111 -1.795 1.00 56.99 ? 243 GLN A CG 1 ATOM 1633 C CD . GLN A 1 218 ? 8.553 -7.416 -2.415 1.00 63.89 ? 243 GLN A CD 1 ATOM 1634 O OE1 . GLN A 1 218 ? 9.221 -8.448 -2.309 1.00 67.84 ? 243 GLN A OE1 1 ATOM 1635 N NE2 . GLN A 1 218 ? 7.365 -7.380 -3.044 1.00 66.35 ? 243 GLN A NE2 1 ATOM 1636 O OXT . GLN A 1 218 ? 5.205 -4.290 -1.757 1.00 53.83 ? 243 GLN A OXT 1 ATOM 1637 N N . ILE B 1 1 ? 29.996 -25.023 24.528 1.00 37.59 ? 16 ILE B N 1 ATOM 1638 C CA . ILE B 1 1 ? 29.962 -26.322 23.799 1.00 37.55 ? 16 ILE B CA 1 ATOM 1639 C C . ILE B 1 1 ? 29.977 -27.470 24.814 1.00 39.22 ? 16 ILE B C 1 ATOM 1640 O O . ILE B 1 1 ? 30.901 -27.586 25.658 1.00 38.70 ? 16 ILE B O 1 ATOM 1641 C CB . ILE B 1 1 ? 31.148 -26.459 22.829 1.00 38.22 ? 16 ILE B CB 1 ATOM 1642 C CG1 . ILE B 1 1 ? 31.239 -25.276 21.833 1.00 34.17 ? 16 ILE B CG1 1 ATOM 1643 C CG2 . ILE B 1 1 ? 31.123 -27.853 22.155 1.00 38.74 ? 16 ILE B CG2 1 ATOM 1644 C CD1 . ILE B 1 1 ? 30.148 -25.231 20.786 1.00 36.45 ? 16 ILE B CD1 1 ATOM 1645 N N . VAL B 1 2 ? 28.914 -28.270 24.762 1.00 40.41 ? 17 VAL B N 1 ATOM 1646 C CA . VAL B 1 2 ? 28.760 -29.449 25.612 1.00 42.20 ? 17 VAL B CA 1 ATOM 1647 C C . VAL B 1 2 ? 29.352 -30.676 24.894 1.00 42.82 ? 17 VAL B C 1 ATOM 1648 O O . VAL B 1 2 ? 28.936 -30.999 23.796 1.00 42.28 ? 17 VAL B O 1 ATOM 1649 C CB . VAL B 1 2 ? 27.281 -29.704 25.887 1.00 42.56 ? 17 VAL B CB 1 ATOM 1650 C CG1 . VAL B 1 2 ? 27.065 -31.113 26.507 1.00 45.10 ? 17 VAL B CG1 1 ATOM 1651 C CG2 . VAL B 1 2 ? 26.712 -28.616 26.811 1.00 42.21 ? 17 VAL B CG2 1 ATOM 1652 N N . GLY B 1 3 ? 30.370 -31.298 25.484 1.00 43.82 ? 18 GLY B N 1 ATOM 1653 C CA . GLY B 1 3 ? 30.968 -32.525 24.939 1.00 44.83 ? 18 GLY B CA 1 ATOM 1654 C C . GLY B 1 3 ? 31.915 -32.417 23.748 1.00 45.06 ? 18 GLY B C 1 ATOM 1655 O O . GLY B 1 3 ? 31.962 -33.298 22.873 1.00 44.04 ? 18 GLY B O 1 ATOM 1656 N N . GLY B 1 4 ? 32.687 -31.343 23.697 1.00 46.43 ? 19 GLY B N 1 ATOM 1657 C CA . GLY B 1 4 ? 33.601 -31.133 22.581 1.00 47.82 ? 19 GLY B CA 1 ATOM 1658 C C . GLY B 1 4 ? 35.005 -31.239 23.084 1.00 49.09 ? 19 GLY B C 1 ATOM 1659 O O . GLY B 1 4 ? 35.232 -31.754 24.171 1.00 50.00 ? 19 GLY B O 1 ATOM 1660 N N . ARG B 1 5 ? 35.960 -30.750 22.308 1.00 50.91 ? 20 ARG B N 1 ATOM 1661 C CA . ARG B 1 5 ? 37.344 -30.742 22.751 1.00 52.61 ? 20 ARG B CA 1 ATOM 1662 C C . ARG B 1 5 ? 37.938 -29.340 22.648 1.00 53.42 ? 20 ARG B C 1 ATOM 1663 O O . ARG B 1 5 ? 37.517 -28.543 21.822 1.00 53.16 ? 20 ARG B O 1 ATOM 1664 C CB . ARG B 1 5 ? 38.179 -31.724 21.898 1.00 52.24 ? 20 ARG B CB 1 ATOM 1665 C CG . ARG B 1 5 ? 38.404 -31.292 20.440 1.00 53.61 ? 20 ARG B CG 1 ATOM 1666 C CD . ARG B 1 5 ? 38.733 -32.444 19.475 1.00 55.79 ? 20 ARG B CD 1 ATOM 1667 N NE . ARG B 1 5 ? 38.431 -32.117 18.079 1.00 58.10 ? 20 ARG B NE 1 ATOM 1668 C CZ . ARG B 1 5 ? 37.380 -32.559 17.404 1.00 58.29 ? 20 ARG B CZ 1 ATOM 1669 N NH1 . ARG B 1 5 ? 36.491 -33.350 17.972 1.00 59.42 ? 20 ARG B NH1 1 ATOM 1670 N NH2 . ARG B 1 5 ? 37.210 -32.204 16.145 1.00 59.88 ? 20 ARG B NH2 1 ATOM 1671 N N . ARG B 1 6 ? 38.920 -29.059 23.494 1.00 55.42 ? 21 ARG B N 1 ATOM 1672 C CA . ARG B 1 6 ? 39.694 -27.825 23.413 1.00 57.08 ? 21 ARG B CA 1 ATOM 1673 C C . ARG B 1 6 ? 40.258 -27.662 22.009 1.00 57.35 ? 21 ARG B C 1 ATOM 1674 O O . ARG B 1 6 ? 40.605 -28.644 21.359 1.00 57.73 ? 21 ARG B O 1 ATOM 1675 C CB . ARG B 1 6 ? 40.871 -27.871 24.392 1.00 57.45 ? 21 ARG B CB 1 ATOM 1676 C CG . ARG B 1 6 ? 40.610 -27.196 25.731 1.00 60.01 ? 21 ARG B CG 1 ATOM 1677 C CD . ARG B 1 6 ? 41.708 -27.419 26.761 1.00 65.03 ? 21 ARG B CD 1 ATOM 1678 N NE . ARG B 1 6 ? 41.656 -28.788 27.254 1.00 71.56 ? 21 ARG B NE 1 ATOM 1679 C CZ . ARG B 1 6 ? 42.278 -29.228 28.344 1.00 75.58 ? 21 ARG B CZ 1 ATOM 1680 N NH1 . ARG B 1 6 ? 42.147 -30.506 28.708 1.00 77.15 ? 21 ARG B NH1 1 ATOM 1681 N NH2 . ARG B 1 6 ? 43.024 -28.399 29.071 1.00 77.65 ? 21 ARG B NH2 1 ATOM 1682 N N . ALA B 1 7 ? 40.340 -26.435 21.520 1.00 57.88 ? 22 ALA B N 1 ATOM 1683 C CA . ALA B 1 7 ? 40.888 -26.217 20.185 1.00 58.56 ? 22 ALA B CA 1 ATOM 1684 C C . ALA B 1 7 ? 42.364 -25.875 20.262 1.00 58.97 ? 22 ALA B C 1 ATOM 1685 O O . ALA B 1 7 ? 42.843 -25.378 21.270 1.00 58.13 ? 22 ALA B O 1 ATOM 1686 C CB . ALA B 1 7 ? 40.141 -25.142 19.462 1.00 58.84 ? 22 ALA B CB 1 ATOM 1687 N N . ARG B 1 8 ? 43.083 -26.174 19.193 1.00 60.22 ? 23 ARG B N 1 ATOM 1688 C CA . ARG B 1 8 ? 44.495 -25.845 19.143 1.00 61.95 ? 23 ARG B CA 1 ATOM 1689 C C . ARG B 1 8 ? 44.622 -24.323 19.035 1.00 62.25 ? 23 ARG B C 1 ATOM 1690 O O . ARG B 1 8 ? 44.033 -23.692 18.161 1.00 62.05 ? 23 ARG B O 1 ATOM 1691 C CB . ARG B 1 8 ? 45.177 -26.572 17.978 1.00 62.60 ? 23 ARG B CB 1 ATOM 1692 C CG . ARG B 1 8 ? 46.516 -25.960 17.541 1.00 66.65 ? 23 ARG B CG 1 ATOM 1693 C CD . ARG B 1 8 ? 47.204 -26.638 16.327 1.00 71.76 ? 23 ARG B CD 1 ATOM 1694 N NE . ARG B 1 8 ? 46.561 -26.350 15.034 1.00 73.87 ? 23 ARG B NE 1 ATOM 1695 C CZ . ARG B 1 8 ? 46.773 -25.255 14.309 1.00 73.42 ? 23 ARG B CZ 1 ATOM 1696 N NH1 . ARG B 1 8 ? 47.607 -24.327 14.745 1.00 71.95 ? 23 ARG B NH1 1 ATOM 1697 N NH2 . ARG B 1 8 ? 46.140 -25.086 13.152 1.00 73.41 ? 23 ARG B NH2 1 ATOM 1698 N N . PRO B 1 9 ? 45.365 -23.734 19.962 1.00 62.85 ? 24 PRO B N 1 ATOM 1699 C CA . PRO B 1 9 ? 45.590 -22.293 19.983 1.00 62.95 ? 24 PRO B CA 1 ATOM 1700 C C . PRO B 1 9 ? 45.575 -21.646 18.620 1.00 62.68 ? 24 PRO B C 1 ATOM 1701 O O . PRO B 1 9 ? 46.432 -21.924 17.786 1.00 62.85 ? 24 PRO B O 1 ATOM 1702 C CB . PRO B 1 9 ? 46.986 -22.197 20.569 1.00 63.08 ? 24 PRO B CB 1 ATOM 1703 C CG . PRO B 1 9 ? 46.983 -23.299 21.581 1.00 63.71 ? 24 PRO B CG 1 ATOM 1704 C CD . PRO B 1 9 ? 46.069 -24.405 21.064 1.00 62.94 ? 24 PRO B CD 1 ATOM 1705 N N . HIS B 1 10 ? 44.572 -20.806 18.395 1.00 62.35 ? 25 HIS B N 1 ATOM 1706 C CA . HIS B 1 10 ? 44.509 -20.008 17.185 1.00 61.60 ? 25 HIS B CA 1 ATOM 1707 C C . HIS B 1 10 ? 44.404 -20.857 15.921 1.00 61.03 ? 25 HIS B C 1 ATOM 1708 O O . HIS B 1 10 ? 45.085 -20.599 14.933 1.00 61.24 ? 25 HIS B O 1 ATOM 1709 C CB . HIS B 1 10 ? 45.719 -19.069 17.157 1.00 61.77 ? 25 HIS B CB 1 ATOM 1710 C CG . HIS B 1 10 ? 45.911 -18.296 18.438 1.00 61.73 ? 25 HIS B CG 1 ATOM 1711 N ND1 . HIS B 1 10 ? 44.937 -17.472 18.967 1.00 61.20 ? 25 HIS B ND1 1 ATOM 1712 C CD2 . HIS B 1 10 ? 46.962 -18.229 19.295 1.00 61.22 ? 25 HIS B CD2 1 ATOM 1713 C CE1 . HIS B 1 10 ? 45.382 -16.929 20.089 1.00 60.00 ? 25 HIS B CE1 1 ATOM 1714 N NE2 . HIS B 1 10 ? 46.609 -17.368 20.309 1.00 59.43 ? 25 HIS B NE2 1 ATOM 1715 N N . ALA B 1 11 ? 43.533 -21.868 15.976 1.00 60.03 ? 26 ALA B N 1 ATOM 1716 C CA . ALA B 1 11 ? 43.234 -22.765 14.853 1.00 58.74 ? 26 ALA B CA 1 ATOM 1717 C C . ALA B 1 11 ? 42.150 -22.181 13.984 1.00 57.79 ? 26 ALA B C 1 ATOM 1718 O O . ALA B 1 11 ? 41.961 -22.582 12.839 1.00 58.20 ? 26 ALA B O 1 ATOM 1719 C CB . ALA B 1 11 ? 42.756 -24.109 15.376 1.00 58.99 ? 26 ALA B CB 1 ATOM 1720 N N . TRP B 1 12 ? 41.385 -21.262 14.561 1.00 56.45 ? 27 TRP B N 1 ATOM 1721 C CA . TRP B 1 12 ? 40.314 -20.579 13.841 1.00 54.45 ? 27 TRP B CA 1 ATOM 1722 C C . TRP B 1 12 ? 40.413 -19.067 14.124 1.00 53.62 ? 27 TRP B C 1 ATOM 1723 O O . TRP B 1 12 ? 39.662 -18.530 14.935 1.00 53.22 ? 27 TRP B O 1 ATOM 1724 C CB . TRP B 1 12 ? 38.997 -21.128 14.318 1.00 53.65 ? 27 TRP B CB 1 ATOM 1725 C CG . TRP B 1 12 ? 39.086 -22.583 14.523 1.00 53.33 ? 27 TRP B CG 1 ATOM 1726 C CD1 . TRP B 1 12 ? 39.083 -23.248 15.707 1.00 51.69 ? 27 TRP B CD1 1 ATOM 1727 C CD2 . TRP B 1 12 ? 39.212 -23.567 13.506 1.00 51.11 ? 27 TRP B CD2 1 ATOM 1728 N NE1 . TRP B 1 12 ? 39.176 -24.600 15.489 1.00 51.46 ? 27 TRP B NE1 1 ATOM 1729 C CE2 . TRP B 1 12 ? 39.259 -24.821 14.139 1.00 52.54 ? 27 TRP B CE2 1 ATOM 1730 C CE3 . TRP B 1 12 ? 39.271 -23.518 12.112 1.00 50.60 ? 27 TRP B CE3 1 ATOM 1731 C CZ2 . TRP B 1 12 ? 39.380 -26.006 13.433 1.00 50.01 ? 27 TRP B CZ2 1 ATOM 1732 C CZ3 . TRP B 1 12 ? 39.400 -24.698 11.409 1.00 51.00 ? 27 TRP B CZ3 1 ATOM 1733 C CH2 . TRP B 1 12 ? 39.454 -25.926 12.074 1.00 50.81 ? 27 TRP B CH2 1 ATOM 1734 N N . PRO B 1 13 ? 41.365 -18.406 13.459 1.00 52.76 ? 28 PRO B N 1 ATOM 1735 C CA . PRO B 1 13 ? 41.669 -16.989 13.697 1.00 51.65 ? 28 PRO B CA 1 ATOM 1736 C C . PRO B 1 13 ? 40.586 -16.040 13.206 1.00 50.32 ? 28 PRO B C 1 ATOM 1737 O O . PRO B 1 13 ? 40.798 -14.830 13.234 1.00 50.47 ? 28 PRO B O 1 ATOM 1738 C CB . PRO B 1 13 ? 42.951 -16.786 12.883 1.00 52.31 ? 28 PRO B CB 1 ATOM 1739 C CG . PRO B 1 13 ? 42.779 -17.737 11.766 1.00 53.17 ? 28 PRO B CG 1 ATOM 1740 C CD . PRO B 1 13 ? 42.253 -18.989 12.439 1.00 52.16 ? 28 PRO B CD 1 ATOM 1741 N N . PHE B 1 14 ? 39.468 -16.575 12.734 1.00 48.15 ? 29 PHE B N 1 ATOM 1742 C CA . PHE B 1 14 ? 38.361 -15.756 12.335 1.00 45.86 ? 29 PHE B CA 1 ATOM 1743 C C . PHE B 1 14 ? 37.335 -15.718 13.496 1.00 44.38 ? 29 PHE B C 1 ATOM 1744 O O . PHE B 1 14 ? 36.332 -15.003 13.441 1.00 44.09 ? 29 PHE B O 1 ATOM 1745 C CB . PHE B 1 14 ? 37.729 -16.266 11.029 1.00 45.84 ? 29 PHE B CB 1 ATOM 1746 C CG . PHE B 1 14 ? 37.340 -17.706 11.067 1.00 46.71 ? 29 PHE B CG 1 ATOM 1747 C CD1 . PHE B 1 14 ? 36.250 -18.131 11.827 1.00 47.69 ? 29 PHE B CD1 1 ATOM 1748 C CD2 . PHE B 1 14 ? 38.067 -18.653 10.344 1.00 49.70 ? 29 PHE B CD2 1 ATOM 1749 C CE1 . PHE B 1 14 ? 35.901 -19.478 11.898 1.00 45.87 ? 29 PHE B CE1 1 ATOM 1750 C CE2 . PHE B 1 14 ? 37.738 -20.000 10.401 1.00 48.13 ? 29 PHE B CE2 1 ATOM 1751 C CZ . PHE B 1 14 ? 36.660 -20.425 11.173 1.00 46.37 ? 29 PHE B CZ 1 ATOM 1752 N N . MET B 1 15 ? 37.634 -16.423 14.572 1.00 42.51 ? 30 MET B N 1 ATOM 1753 C CA . MET B 1 15 ? 36.656 -16.610 15.635 1.00 41.15 ? 30 MET B CA 1 ATOM 1754 C C . MET B 1 15 ? 36.691 -15.423 16.577 1.00 40.62 ? 30 MET B C 1 ATOM 1755 O O . MET B 1 15 ? 37.775 -14.921 16.932 1.00 41.40 ? 30 MET B O 1 ATOM 1756 C CB . MET B 1 15 ? 36.910 -17.947 16.366 1.00 41.18 ? 30 MET B CB 1 ATOM 1757 C CG . MET B 1 15 ? 36.023 -18.235 17.560 1.00 38.88 ? 30 MET B CG 1 ATOM 1758 S SD . MET B 1 15 ? 34.300 -18.398 17.088 1.00 35.55 ? 30 MET B SD 1 ATOM 1759 C CE . MET B 1 15 ? 33.541 -18.178 18.701 1.00 37.07 ? 30 MET B CE 1 ATOM 1760 N N . VAL B 1 16 ? 35.520 -14.951 16.976 1.00 38.93 ? 31 VAL B N 1 ATOM 1761 C CA . VAL B 1 16 ? 35.468 -13.703 17.761 1.00 38.08 ? 31 VAL B CA 1 ATOM 1762 C C . VAL B 1 16 ? 34.636 -13.827 19.013 1.00 38.74 ? 31 VAL B C 1 ATOM 1763 O O . VAL B 1 16 ? 33.585 -14.508 18.992 1.00 40.88 ? 31 VAL B O 1 ATOM 1764 C CB . VAL B 1 16 ? 34.952 -12.547 16.880 1.00 38.02 ? 31 VAL B CB 1 ATOM 1765 C CG1 . VAL B 1 16 ? 34.798 -11.172 17.700 1.00 36.48 ? 31 VAL B CG1 1 ATOM 1766 C CG2 . VAL B 1 16 ? 35.857 -12.363 15.664 1.00 35.49 ? 31 VAL B CG2 1 ATOM 1767 N N . SER B 1 17 ? 35.103 -13.211 20.098 1.00 39.20 ? 32 SER B N 1 ATOM 1768 C CA . SER B 1 17 ? 34.362 -13.153 21.356 1.00 38.76 ? 32 SER B CA 1 ATOM 1769 C C . SER B 1 17 ? 33.742 -11.784 21.632 1.00 39.86 ? 32 SER B C 1 ATOM 1770 O O . SER B 1 17 ? 34.462 -10.790 21.717 1.00 40.28 ? 32 SER B O 1 ATOM 1771 C CB . SER B 1 17 ? 35.281 -13.487 22.495 1.00 38.59 ? 32 SER B CB 1 ATOM 1772 O OG . SER B 1 17 ? 34.677 -13.192 23.731 1.00 37.45 ? 32 SER B OG 1 ATOM 1773 N N . LEU B 1 18 ? 32.416 -11.738 21.792 1.00 40.46 ? 33 LEU B N 1 ATOM 1774 C CA . LEU B 1 18 ? 31.692 -10.504 22.109 1.00 40.12 ? 33 LEU B CA 1 ATOM 1775 C C . LEU B 1 18 ? 31.537 -10.395 23.643 1.00 41.74 ? 33 LEU B C 1 ATOM 1776 O O . LEU B 1 18 ? 31.083 -11.344 24.269 1.00 41.35 ? 33 LEU B O 1 ATOM 1777 C CB . LEU B 1 18 ? 30.335 -10.507 21.419 1.00 39.16 ? 33 LEU B CB 1 ATOM 1778 C CG . LEU B 1 18 ? 30.356 -10.579 19.893 1.00 36.32 ? 33 LEU B CG 1 ATOM 1779 C CD1 . LEU B 1 18 ? 28.939 -10.454 19.289 1.00 32.17 ? 33 LEU B CD1 1 ATOM 1780 C CD2 . LEU B 1 18 ? 31.254 -9.491 19.318 1.00 34.48 ? 33 LEU B CD2 1 ATOM 1781 N N . GLN B 1 19 ? 31.968 -9.274 24.255 1.00 43.41 ? 34 GLN B N 1 ATOM 1782 C CA . GLN B 1 19 ? 31.955 -9.108 25.736 1.00 44.41 ? 34 GLN B CA 1 ATOM 1783 C C . GLN B 1 19 ? 31.291 -7.816 26.250 1.00 45.36 ? 34 GLN B C 1 ATOM 1784 O O . GLN B 1 19 ? 31.249 -6.802 25.578 1.00 44.41 ? 34 GLN B O 1 ATOM 1785 C CB . GLN B 1 19 ? 33.367 -9.249 26.349 1.00 44.25 ? 34 GLN B CB 1 ATOM 1786 C CG . GLN B 1 19 ? 34.316 -10.114 25.532 1.00 43.96 ? 34 GLN B CG 1 ATOM 1787 C CD . GLN B 1 19 ? 35.557 -10.603 26.279 1.00 46.70 ? 34 GLN B CD 1 ATOM 1788 O OE1 . GLN B 1 19 ? 36.155 -11.604 25.854 1.00 47.52 ? 34 GLN B OE1 1 ATOM 1789 N NE2 . GLN B 1 19 ? 35.965 -9.911 27.368 1.00 41.58 ? 34 GLN B NE2 1 ATOM 1790 N N . LEU B 1 20 ? 30.821 -7.856 27.480 1.00 47.61 ? 35 LEU B N 1 ATOM 1791 C CA . LEU B 1 20 ? 30.088 -6.755 28.063 1.00 50.10 ? 35 LEU B CA 1 ATOM 1792 C C . LEU B 1 20 ? 30.550 -6.813 29.483 1.00 51.55 ? 35 LEU B C 1 ATOM 1793 O O . LEU B 1 20 ? 30.379 -7.841 30.147 1.00 52.14 ? 35 LEU B O 1 ATOM 1794 C CB . LEU B 1 20 ? 28.586 -6.997 27.969 1.00 49.60 ? 35 LEU B CB 1 ATOM 1795 C CG . LEU B 1 20 ? 27.766 -5.722 27.792 1.00 52.85 ? 35 LEU B CG 1 ATOM 1796 C CD1 . LEU B 1 20 ? 28.241 -4.968 26.558 1.00 51.60 ? 35 LEU B CD1 1 ATOM 1797 C CD2 . LEU B 1 20 ? 26.288 -6.045 27.695 1.00 54.49 ? 35 LEU B CD2 1 ATOM 1798 N N . ARG B 1 21 ? 31.131 -5.715 29.944 1.00 53.67 ? 36 ARG B N 1 ATOM 1799 C CA . ARG B 1 21 ? 31.850 -5.718 31.204 1.00 55.58 ? 36 ARG B CA 1 ATOM 1800 C C . ARG B 1 21 ? 33.117 -6.486 30.872 1.00 55.67 ? 36 ARG B C 1 ATOM 1801 O O . ARG B 1 21 ? 33.759 -6.223 29.836 1.00 56.42 ? 36 ARG B O 1 ATOM 1802 C CB . ARG B 1 21 ? 31.055 -6.424 32.277 1.00 56.31 ? 36 ARG B CB 1 ATOM 1803 C CG . ARG B 1 21 ? 29.896 -5.583 32.742 1.00 60.31 ? 36 ARG B CG 1 ATOM 1804 C CD . ARG B 1 21 ? 28.569 -6.318 32.796 1.00 67.52 ? 36 ARG B CD 1 ATOM 1805 N NE . ARG B 1 21 ? 27.458 -5.373 32.720 1.00 72.91 ? 36 ARG B NE 1 ATOM 1806 C CZ . ARG B 1 21 ? 26.173 -5.717 32.593 1.00 76.24 ? 36 ARG B CZ 1 ATOM 1807 N NH1 . ARG B 1 21 ? 25.819 -7.002 32.532 1.00 77.32 ? 36 ARG B NH1 1 ATOM 1808 N NH2 . ARG B 1 21 ? 25.235 -4.766 32.527 1.00 76.14 ? 36 ARG B NH2 1 ATOM 1809 N N . GLY B 1 22 ? 33.497 -7.439 31.712 1.00 55.21 ? 38 GLY B N 1 ATOM 1810 C CA . GLY B 1 22 ? 34.693 -8.210 31.382 1.00 53.96 ? 38 GLY B CA 1 ATOM 1811 C C . GLY B 1 22 ? 34.357 -9.647 31.032 1.00 52.78 ? 38 GLY B C 1 ATOM 1812 O O . GLY B 1 22 ? 35.216 -10.540 31.088 1.00 54.18 ? 38 GLY B O 1 ATOM 1813 N N . GLY B 1 23 ? 33.110 -9.876 30.630 1.00 50.44 ? 39 GLY B N 1 ATOM 1814 C CA . GLY B 1 23 ? 32.661 -11.225 30.376 1.00 46.76 ? 39 GLY B CA 1 ATOM 1815 C C . GLY B 1 23 ? 32.066 -11.553 29.010 1.00 44.18 ? 39 GLY B C 1 ATOM 1816 O O . GLY B 1 23 ? 31.259 -10.798 28.465 1.00 41.28 ? 39 GLY B O 1 ATOM 1817 N N . HIS B 1 24 ? 32.413 -12.741 28.504 1.00 42.03 ? 40 HIS B N 1 ATOM 1818 C CA . HIS B 1 24 ? 31.958 -13.229 27.205 1.00 39.26 ? 40 HIS B CA 1 ATOM 1819 C C . HIS B 1 24 ? 30.483 -13.486 27.265 1.00 38.01 ? 40 HIS B C 1 ATOM 1820 O O . HIS B 1 24 ? 29.984 -13.984 28.269 1.00 38.35 ? 40 HIS B O 1 ATOM 1821 C CB . HIS B 1 24 ? 32.685 -14.534 26.862 1.00 40.28 ? 40 HIS B CB 1 ATOM 1822 C CG . HIS B 1 24 ? 32.071 -15.291 25.722 1.00 39.84 ? 40 HIS B CG 1 ATOM 1823 N ND1 . HIS B 1 24 ? 32.572 -15.232 24.435 1.00 37.03 ? 40 HIS B ND1 1 ATOM 1824 C CD2 . HIS B 1 24 ? 30.974 -16.089 25.668 1.00 39.53 ? 40 HIS B CD2 1 ATOM 1825 C CE1 . HIS B 1 24 ? 31.836 -15.998 23.649 1.00 38.85 ? 40 HIS B CE1 1 ATOM 1826 N NE2 . HIS B 1 24 ? 30.852 -16.520 24.368 1.00 39.80 ? 40 HIS B NE2 1 ATOM 1827 N N . PHE B 1 25 ? 29.761 -13.128 26.212 1.00 36.20 ? 41 PHE B N 1 ATOM 1828 C CA . PHE B 1 25 ? 28.337 -13.441 26.190 1.00 35.15 ? 41 PHE B CA 1 ATOM 1829 C C . PHE B 1 25 ? 27.902 -14.041 24.864 1.00 34.19 ? 41 PHE B C 1 ATOM 1830 O O . PHE B 1 25 ? 26.857 -14.625 24.804 1.00 34.46 ? 41 PHE B O 1 ATOM 1831 C CB . PHE B 1 25 ? 27.462 -12.224 26.559 1.00 34.35 ? 41 PHE B CB 1 ATOM 1832 C CG . PHE B 1 25 ? 27.481 -11.110 25.521 1.00 35.93 ? 41 PHE B CG 1 ATOM 1833 C CD1 . PHE B 1 25 ? 26.587 -11.114 24.433 1.00 35.58 ? 41 PHE B CD1 1 ATOM 1834 C CD2 . PHE B 1 25 ? 28.393 -10.041 25.640 1.00 37.75 ? 41 PHE B CD2 1 ATOM 1835 C CE1 . PHE B 1 25 ? 26.613 -10.100 23.483 1.00 36.94 ? 41 PHE B CE1 1 ATOM 1836 C CE2 . PHE B 1 25 ? 28.435 -9.021 24.688 1.00 34.26 ? 41 PHE B CE2 1 ATOM 1837 C CZ . PHE B 1 25 ? 27.553 -9.045 23.606 1.00 35.59 ? 41 PHE B CZ 1 ATOM 1838 N N . CYS B 1 26 ? 28.654 -13.823 23.779 1.00 32.82 ? 42 CYS B N 1 ATOM 1839 C CA . CYS B 1 26 ? 28.301 -14.426 22.478 1.00 31.81 ? 42 CYS B CA 1 ATOM 1840 C C . CYS B 1 26 ? 29.530 -14.479 21.591 1.00 32.62 ? 42 CYS B C 1 ATOM 1841 O O . CYS B 1 26 ? 30.486 -13.707 21.790 1.00 32.27 ? 42 CYS B O 1 ATOM 1842 C CB . CYS B 1 26 ? 27.257 -13.632 21.700 1.00 31.09 ? 42 CYS B CB 1 ATOM 1843 S SG . CYS B 1 26 ? 25.520 -13.970 21.985 1.00 26.85 ? 42 CYS B SG 1 ATOM 1844 N N . GLY B 1 27 ? 29.476 -15.333 20.562 1.00 32.17 ? 43 GLY B N 1 ATOM 1845 C CA . GLY B 1 27 ? 30.561 -15.370 19.613 1.00 31.22 ? 43 GLY B CA 1 ATOM 1846 C C . GLY B 1 27 ? 30.214 -14.535 18.391 1.00 31.40 ? 43 GLY B C 1 ATOM 1847 O O . GLY B 1 27 ? 29.094 -14.012 18.244 1.00 29.99 ? 43 GLY B O 1 ATOM 1848 N N . ALA B 1 28 ? 31.175 -14.463 17.469 1.00 30.96 ? 44 ALA B N 1 ATOM 1849 C CA . ALA B 1 28 ? 30.935 -13.806 16.191 1.00 31.88 ? 44 ALA B CA 1 ATOM 1850 C C . ALA B 1 28 ? 32.045 -14.281 15.299 1.00 31.78 ? 44 ALA B C 1 ATOM 1851 O O . ALA B 1 28 ? 32.976 -14.953 15.804 1.00 33.54 ? 44 ALA B O 1 ATOM 1852 C CB . ALA B 1 28 ? 31.008 -12.250 16.325 1.00 30.63 ? 44 ALA B CB 1 ATOM 1853 N N . THR B 1 29 ? 31.968 -13.861 14.043 1.00 30.93 ? 45 THR B N 1 ATOM 1854 C CA . THR B 1 29 ? 32.924 -14.171 12.991 1.00 32.69 ? 45 THR B CA 1 ATOM 1855 C C . THR B 1 29 ? 33.479 -12.940 12.190 1.00 32.75 ? 45 THR B C 1 ATOM 1856 O O . THR B 1 29 ? 32.735 -12.216 11.574 1.00 32.47 ? 45 THR B O 1 ATOM 1857 C CB . THR B 1 29 ? 32.238 -15.165 11.952 1.00 32.94 ? 45 THR B CB 1 ATOM 1858 O OG1 . THR B 1 29 ? 31.859 -16.423 12.580 1.00 31.43 ? 45 THR B OG1 1 ATOM 1859 C CG2 . THR B 1 29 ? 33.297 -15.587 10.865 1.00 30.86 ? 45 THR B CG2 1 ATOM 1860 N N . LEU B 1 30 ? 34.791 -12.794 12.124 1.00 34.76 ? 46 LEU B N 1 ATOM 1861 C CA . LEU B 1 30 ? 35.414 -11.738 11.321 1.00 35.40 ? 46 LEU B CA 1 ATOM 1862 C C . LEU B 1 30 ? 35.324 -12.068 9.855 1.00 36.03 ? 46 LEU B C 1 ATOM 1863 O O . LEU B 1 30 ? 35.928 -13.055 9.401 1.00 37.65 ? 46 LEU B O 1 ATOM 1864 C CB . LEU B 1 30 ? 36.890 -11.636 11.692 1.00 34.08 ? 46 LEU B CB 1 ATOM 1865 C CG . LEU B 1 30 ? 37.642 -10.440 11.101 1.00 34.59 ? 46 LEU B CG 1 ATOM 1866 C CD1 . LEU B 1 30 ? 37.107 -9.181 11.823 1.00 32.11 ? 46 LEU B CD1 1 ATOM 1867 C CD2 . LEU B 1 30 ? 39.184 -10.579 11.274 1.00 33.11 ? 46 LEU B CD2 1 ATOM 1868 N N . ILE B 1 31 ? 34.579 -11.266 9.111 1.00 35.39 ? 47 ILE B N 1 ATOM 1869 C CA . ILE B 1 31 ? 34.346 -11.512 7.703 1.00 34.97 ? 47 ILE B CA 1 ATOM 1870 C C . ILE B 1 31 ? 35.022 -10.436 6.823 1.00 36.29 ? 47 ILE B C 1 ATOM 1871 O O . ILE B 1 31 ? 35.055 -10.579 5.638 1.00 38.00 ? 47 ILE B O 1 ATOM 1872 C CB . ILE B 1 31 ? 32.823 -11.544 7.389 1.00 34.77 ? 47 ILE B CB 1 ATOM 1873 C CG1 . ILE B 1 31 ? 32.172 -10.264 7.927 1.00 32.71 ? 47 ILE B CG1 1 ATOM 1874 C CG2 . ILE B 1 31 ? 32.100 -12.795 8.038 1.00 31.34 ? 47 ILE B CG2 1 ATOM 1875 C CD1 . ILE B 1 31 ? 30.749 -10.077 7.449 1.00 34.06 ? 47 ILE B CD1 1 ATOM 1876 N N . ALA B 1 32 ? 35.476 -9.335 7.401 1.00 37.40 ? 48 ALA B N 1 ATOM 1877 C CA . ALA B 1 32 ? 36.250 -8.320 6.668 1.00 38.78 ? 48 ALA B CA 1 ATOM 1878 C C . ALA B 1 32 ? 37.020 -7.682 7.808 1.00 40.09 ? 48 ALA B C 1 ATOM 1879 O O . ALA B 1 32 ? 36.531 -7.782 8.938 1.00 41.38 ? 48 ALA B O 1 ATOM 1880 C CB . ALA B 1 32 ? 35.380 -7.376 6.001 1.00 37.80 ? 48 ALA B CB 1 ATOM 1881 N N . PRO B 1 33 ? 38.203 -7.081 7.578 1.00 39.37 ? 49 PRO B N 1 ATOM 1882 C CA . PRO B 1 33 ? 38.997 -6.560 8.703 1.00 39.27 ? 49 PRO B CA 1 ATOM 1883 C C . PRO B 1 33 ? 38.238 -5.538 9.606 1.00 38.41 ? 49 PRO B C 1 ATOM 1884 O O . PRO B 1 33 ? 38.570 -5.427 10.791 1.00 38.89 ? 49 PRO B O 1 ATOM 1885 C CB . PRO B 1 33 ? 40.219 -5.930 8.024 1.00 40.21 ? 49 PRO B CB 1 ATOM 1886 C CG . PRO B 1 33 ? 40.283 -6.610 6.641 1.00 38.74 ? 49 PRO B CG 1 ATOM 1887 C CD . PRO B 1 33 ? 38.858 -6.838 6.283 1.00 39.77 ? 49 PRO B CD 1 ATOM 1888 N N . ASN B 1 34 ? 37.222 -4.868 9.079 1.00 37.78 ? 50 ASN B N 1 ATOM 1889 C CA . ASN B 1 34 ? 36.421 -3.944 9.897 1.00 37.51 ? 50 ASN B CA 1 ATOM 1890 C C . ASN B 1 34 ? 34.977 -4.411 10.023 1.00 37.32 ? 50 ASN B C 1 ATOM 1891 O O . ASN B 1 34 ? 34.100 -3.583 10.207 1.00 36.96 ? 50 ASN B O 1 ATOM 1892 C CB . ASN B 1 34 ? 36.475 -2.487 9.350 1.00 35.76 ? 50 ASN B CB 1 ATOM 1893 C CG . ASN B 1 34 ? 35.994 -2.382 7.917 1.00 38.01 ? 50 ASN B CG 1 ATOM 1894 O OD1 . ASN B 1 34 ? 36.110 -3.343 7.139 1.00 40.24 ? 50 ASN B OD1 1 ATOM 1895 N ND2 . ASN B 1 34 ? 35.454 -1.216 7.539 1.00 35.33 ? 50 ASN B ND2 1 ATOM 1896 N N . PHE B 1 35 ? 34.720 -5.730 9.913 1.00 36.17 ? 51 PHE B N 1 ATOM 1897 C CA . PHE B 1 35 ? 33.347 -6.212 9.931 1.00 35.01 ? 51 PHE B CA 1 ATOM 1898 C C . PHE B 1 35 ? 33.211 -7.627 10.554 1.00 34.88 ? 51 PHE B C 1 ATOM 1899 O O . PHE B 1 35 ? 34.026 -8.555 10.221 1.00 34.13 ? 51 PHE B O 1 ATOM 1900 C CB . PHE B 1 35 ? 32.843 -6.300 8.515 1.00 35.41 ? 51 PHE B CB 1 ATOM 1901 C CG . PHE B 1 35 ? 32.353 -4.985 7.928 1.00 37.91 ? 51 PHE B CG 1 ATOM 1902 C CD1 . PHE B 1 35 ? 31.077 -4.511 8.219 1.00 35.27 ? 51 PHE B CD1 1 ATOM 1903 C CD2 . PHE B 1 35 ? 33.144 -4.271 7.042 1.00 37.71 ? 51 PHE B CD2 1 ATOM 1904 C CE1 . PHE B 1 35 ? 30.597 -3.337 7.665 1.00 38.15 ? 51 PHE B CE1 1 ATOM 1905 C CE2 . PHE B 1 35 ? 32.667 -3.070 6.500 1.00 40.03 ? 51 PHE B CE2 1 ATOM 1906 C CZ . PHE B 1 35 ? 31.378 -2.617 6.812 1.00 36.88 ? 51 PHE B CZ 1 ATOM 1907 N N . VAL B 1 36 ? 32.218 -7.793 11.445 1.00 33.01 ? 52 VAL B N 1 ATOM 1908 C CA . VAL B 1 36 ? 31.910 -9.128 11.997 1.00 30.74 ? 52 VAL B CA 1 ATOM 1909 C C . VAL B 1 36 ? 30.486 -9.510 11.779 1.00 31.16 ? 52 VAL B C 1 ATOM 1910 O O . VAL B 1 36 ? 29.673 -8.672 11.445 1.00 27.62 ? 52 VAL B O 1 ATOM 1911 C CB . VAL B 1 36 ? 32.228 -9.281 13.466 1.00 32.61 ? 52 VAL B CB 1 ATOM 1912 C CG1 . VAL B 1 36 ? 33.688 -9.165 13.679 1.00 28.54 ? 52 VAL B CG1 1 ATOM 1913 C CG2 . VAL B 1 36 ? 31.412 -8.302 14.344 1.00 31.05 ? 52 VAL B CG2 1 ATOM 1914 N N . MET B 1 37 ? 30.177 -10.817 11.950 1.00 30.24 ? 53 MET B N 1 ATOM 1915 C CA . MET B 1 37 ? 28.830 -11.291 11.709 1.00 30.07 ? 53 MET B CA 1 ATOM 1916 C C . MET B 1 37 ? 28.467 -12.075 12.948 1.00 29.29 ? 53 MET B C 1 ATOM 1917 O O . MET B 1 37 ? 29.335 -12.710 13.522 1.00 29.97 ? 53 MET B O 1 ATOM 1918 C CB . MET B 1 37 ? 28.860 -12.170 10.450 1.00 32.98 ? 53 MET B CB 1 ATOM 1919 C CG . MET B 1 37 ? 27.579 -12.915 10.056 1.00 34.69 ? 53 MET B CG 1 ATOM 1920 S SD . MET B 1 37 ? 27.937 -13.921 8.500 1.00 35.27 ? 53 MET B SD 1 ATOM 1921 C CE . MET B 1 37 ? 29.259 -14.774 8.956 1.00 33.79 ? 53 MET B CE 1 ATOM 1922 N N . SER B 1 38 ? 27.205 -12.021 13.380 1.00 28.73 ? 54 SER B N 1 ATOM 1923 C CA . SER B 1 38 ? 26.811 -12.712 14.583 1.00 26.20 ? 54 SER B CA 1 ATOM 1924 C C . SER B 1 38 ? 25.329 -12.911 14.535 1.00 27.17 ? 54 SER B C 1 ATOM 1925 O O . SER B 1 38 ? 24.691 -12.634 13.528 1.00 25.00 ? 54 SER B O 1 ATOM 1926 C CB . SER B 1 38 ? 27.182 -11.868 15.783 1.00 27.47 ? 54 SER B CB 1 ATOM 1927 O OG . SER B 1 38 ? 27.020 -12.598 16.958 1.00 26.71 ? 54 SER B OG 1 ATOM 1928 N N . ALA B 1 39 ? 24.771 -13.353 15.658 1.00 26.44 ? 55 ALA B N 1 ATOM 1929 C CA . ALA B 1 39 ? 23.340 -13.564 15.710 1.00 26.05 ? 55 ALA B CA 1 ATOM 1930 C C . ALA B 1 39 ? 22.678 -12.231 16.162 1.00 26.56 ? 55 ALA B C 1 ATOM 1931 O O . ALA B 1 39 ? 23.081 -11.653 17.183 1.00 25.61 ? 55 ALA B O 1 ATOM 1932 C CB . ALA B 1 39 ? 23.033 -14.694 16.764 1.00 23.73 ? 55 ALA B CB 1 ATOM 1933 N N . ALA B 1 40 ? 21.667 -11.821 15.435 1.00 26.45 ? 56 ALA B N 1 ATOM 1934 C CA . ALA B 1 40 ? 20.824 -10.681 15.815 1.00 28.00 ? 56 ALA B CA 1 ATOM 1935 C C . ALA B 1 40 ? 20.394 -10.708 17.302 1.00 28.99 ? 56 ALA B C 1 ATOM 1936 O O . ALA B 1 40 ? 20.370 -9.650 17.997 1.00 28.60 ? 56 ALA B O 1 ATOM 1937 C CB . ALA B 1 40 ? 19.620 -10.648 14.944 1.00 25.14 ? 56 ALA B CB 1 ATOM 1938 N N . HIS B 1 41 ? 20.127 -11.918 17.812 1.00 28.91 ? 57 HIS B N 1 ATOM 1939 C CA . HIS B 1 41 ? 19.556 -12.045 19.147 1.00 28.07 ? 57 HIS B CA 1 ATOM 1940 C C . HIS B 1 41 ? 20.558 -11.615 20.175 1.00 26.48 ? 57 HIS B C 1 ATOM 1941 O O . HIS B 1 41 ? 20.196 -11.207 21.272 1.00 25.61 ? 57 HIS B O 1 ATOM 1942 C CB . HIS B 1 41 ? 19.095 -13.513 19.436 1.00 30.09 ? 57 HIS B CB 1 ATOM 1943 C CG . HIS B 1 41 ? 18.350 -13.645 20.727 1.00 30.68 ? 57 HIS B CG 1 ATOM 1944 N ND1 . HIS B 1 41 ? 18.984 -13.949 21.918 1.00 34.30 ? 57 HIS B ND1 1 ATOM 1945 C CD2 . HIS B 1 41 ? 17.046 -13.417 21.037 1.00 33.27 ? 57 HIS B CD2 1 ATOM 1946 C CE1 . HIS B 1 41 ? 18.085 -13.969 22.899 1.00 35.67 ? 57 HIS B CE1 1 ATOM 1947 N NE2 . HIS B 1 41 ? 16.909 -13.635 22.396 1.00 36.53 ? 57 HIS B NE2 1 ATOM 1948 N N . CYS B 1 42 ? 21.832 -11.799 19.848 1.00 25.79 ? 58 CYS B N 1 ATOM 1949 C CA . CYS B 1 42 ? 22.917 -11.473 20.726 1.00 26.75 ? 58 CYS B CA 1 ATOM 1950 C C . CYS B 1 42 ? 22.997 -9.976 21.113 1.00 27.59 ? 58 CYS B C 1 ATOM 1951 O O . CYS B 1 42 ? 23.410 -9.658 22.239 1.00 28.61 ? 58 CYS B O 1 ATOM 1952 C CB . CYS B 1 42 ? 24.266 -11.907 20.108 1.00 27.47 ? 58 CYS B CB 1 ATOM 1953 S SG . CYS B 1 42 ? 24.599 -13.769 20.182 1.00 29.78 ? 58 CYS B SG 1 ATOM 1954 N N . VAL B 1 43 ? 22.659 -9.082 20.183 1.00 26.91 ? 59 VAL B N 1 ATOM 1955 C CA . VAL B 1 43 ? 22.764 -7.650 20.469 1.00 28.42 ? 59 VAL B CA 1 ATOM 1956 C C . VAL B 1 43 ? 21.432 -7.011 20.773 1.00 30.44 ? 59 VAL B C 1 ATOM 1957 O O . VAL B 1 43 ? 21.409 -5.811 21.042 1.00 33.65 ? 59 VAL B O 1 ATOM 1958 C CB . VAL B 1 43 ? 23.488 -6.849 19.331 1.00 27.17 ? 59 VAL B CB 1 ATOM 1959 C CG1 . VAL B 1 43 ? 24.929 -7.347 19.094 1.00 24.24 ? 59 VAL B CG1 1 ATOM 1960 C CG2 . VAL B 1 43 ? 22.727 -6.872 18.054 1.00 22.68 ? 59 VAL B CG2 1 ATOM 1961 N N . ALA B 1 44 ? 20.339 -7.787 20.776 1.00 30.59 ? 60 ALA B N 1 ATOM 1962 C CA . ALA B 1 44 ? 18.976 -7.223 20.939 1.00 32.88 ? 60 ALA B CA 1 ATOM 1963 C C . ALA B 1 44 ? 18.614 -6.492 22.256 1.00 34.73 ? 60 ALA B C 1 ATOM 1964 O O . ALA B 1 44 ? 17.846 -5.525 22.285 1.00 35.60 ? 60 ALA B O 1 ATOM 1965 C CB . ALA B 1 44 ? 17.910 -8.218 20.660 1.00 29.93 ? 60 ALA B CB 1 ATOM 1966 N N . ASN B 1 45 ? 19.053 -6.933 23.381 1.00 36.55 ? 61 ASN B N 1 ATOM 1967 C CA . ASN B 1 45 ? 18.524 -6.058 24.447 1.00 38.24 ? 61 ASN B CA 1 ATOM 1968 C C . ASN B 1 45 ? 19.644 -5.896 25.402 1.00 37.42 ? 61 ASN B C 1 ATOM 1969 O O . ASN B 1 45 ? 19.572 -6.320 26.514 1.00 36.64 ? 61 ASN B O 1 ATOM 1970 C CB . ASN B 1 45 ? 17.184 -6.625 25.020 1.00 38.21 ? 61 ASN B CB 1 ATOM 1971 C CG . ASN B 1 45 ? 16.628 -5.834 26.251 1.00 40.43 ? 61 ASN B CG 1 ATOM 1972 O OD1 . ASN B 1 45 ? 16.758 -4.610 26.369 1.00 43.45 ? 61 ASN B OD1 1 ATOM 1973 N ND2 . ASN B 1 45 ? 16.024 -6.557 27.154 1.00 38.21 ? 61 ASN B ND2 1 ATOM 1974 N N . VAL B 1 46 ? 20.736 -5.359 24.846 1.00 37.36 ? 62 VAL B N 1 ATOM 1975 C CA . VAL B 1 46 ? 21.961 -5.039 25.545 1.00 38.00 ? 62 VAL B CA 1 ATOM 1976 C C . VAL B 1 46 ? 22.382 -3.626 25.142 1.00 37.50 ? 62 VAL B C 1 ATOM 1977 O O . VAL B 1 46 ? 21.854 -3.069 24.177 1.00 37.20 ? 62 VAL B O 1 ATOM 1978 C CB . VAL B 1 46 ? 23.102 -6.033 25.216 1.00 37.63 ? 62 VAL B CB 1 ATOM 1979 C CG1 . VAL B 1 46 ? 22.756 -7.433 25.742 1.00 40.90 ? 62 VAL B CG1 1 ATOM 1980 C CG2 . VAL B 1 46 ? 23.419 -6.039 23.741 1.00 36.89 ? 62 VAL B CG2 1 ATOM 1981 N N . ASN B 1 47 A 23.337 -3.061 25.870 1.00 37.02 ? 62 ASN B N 1 ATOM 1982 C CA . ASN B 1 47 A 23.826 -1.750 25.551 1.00 36.19 ? 62 ASN B CA 1 ATOM 1983 C C . ASN B 1 47 A 24.962 -1.914 24.599 1.00 34.52 ? 62 ASN B C 1 ATOM 1984 O O . ASN B 1 47 A 26.119 -2.136 25.007 1.00 32.71 ? 62 ASN B O 1 ATOM 1985 C CB . ASN B 1 47 A 24.353 -1.001 26.768 1.00 38.11 ? 62 ASN B CB 1 ATOM 1986 C CG . ASN B 1 47 A 25.144 0.269 26.342 1.00 40.88 ? 62 ASN B CG 1 ATOM 1987 O OD1 . ASN B 1 47 A 26.204 0.561 26.891 1.00 46.20 ? 62 ASN B OD1 1 ATOM 1988 N ND2 . ASN B 1 47 A 24.644 0.969 25.317 1.00 39.51 ? 62 ASN B ND2 1 ATOM 1989 N N . VAL B 1 48 B 24.640 -1.792 23.325 1.00 34.27 ? 62 VAL B N 1 ATOM 1990 C CA . VAL B 1 48 B 25.638 -2.067 22.294 1.00 35.33 ? 62 VAL B CA 1 ATOM 1991 C C . VAL B 1 48 B 26.877 -1.229 22.352 1.00 35.56 ? 62 VAL B C 1 ATOM 1992 O O . VAL B 1 48 B 27.948 -1.671 21.930 1.00 36.34 ? 62 VAL B O 1 ATOM 1993 C CB . VAL B 1 48 B 25.000 -1.993 20.908 1.00 35.52 ? 62 VAL B CB 1 ATOM 1994 C CG1 . VAL B 1 48 B 25.956 -2.519 19.853 1.00 35.84 ? 62 VAL B CG1 1 ATOM 1995 C CG2 . VAL B 1 48 B 23.691 -2.827 20.921 1.00 36.44 ? 62 VAL B CG2 1 ATOM 1996 N N . ARG B 1 49 ? 26.749 0.000 22.843 1.00 35.12 ? 63 ARG B N 1 ATOM 1997 C CA . ARG B 1 49 ? 27.894 0.887 22.986 1.00 36.29 ? 63 ARG B CA 1 ATOM 1998 C C . ARG B 1 49 ? 28.919 0.323 23.900 1.00 35.99 ? 63 ARG B C 1 ATOM 1999 O O . ARG B 1 49 ? 30.109 0.598 23.823 1.00 35.19 ? 63 ARG B O 1 ATOM 2000 C CB . ARG B 1 49 ? 27.444 2.240 23.584 1.00 37.82 ? 63 ARG B CB 1 ATOM 2001 C CG . ARG B 1 49 ? 26.772 3.160 22.625 1.00 39.60 ? 63 ARG B CG 1 ATOM 2002 C CD . ARG B 1 49 ? 26.911 4.643 23.079 1.00 47.74 ? 63 ARG B CD 1 ATOM 2003 N NE . ARG B 1 49 ? 25.954 5.527 22.409 1.00 55.05 ? 63 ARG B NE 1 ATOM 2004 C CZ . ARG B 1 49 ? 25.467 6.658 22.951 1.00 61.79 ? 63 ARG B CZ 1 ATOM 2005 N NH1 . ARG B 1 49 ? 24.570 7.403 22.292 1.00 64.47 ? 63 ARG B NH1 1 ATOM 2006 N NH2 . ARG B 1 49 ? 25.881 7.047 24.158 1.00 63.45 ? 63 ARG B NH2 1 ATOM 2007 N N . ALA B 1 50 ? 28.465 -0.482 24.822 1.00 37.15 ? 64 ALA B N 1 ATOM 2008 C CA . ALA B 1 50 ? 29.406 -1.055 25.773 1.00 37.70 ? 64 ALA B CA 1 ATOM 2009 C C . ALA B 1 50 ? 30.074 -2.323 25.250 1.00 38.85 ? 64 ALA B C 1 ATOM 2010 O O . ALA B 1 50 ? 31.008 -2.793 25.868 1.00 40.12 ? 64 ALA B O 1 ATOM 2011 C CB . ALA B 1 50 ? 28.670 -1.334 27.101 1.00 37.96 ? 64 ALA B CB 1 ATOM 2012 N N . VAL B 1 51 ? 29.612 -2.867 24.115 1.00 38.40 ? 65 VAL B N 1 ATOM 2013 C CA . VAL B 1 51 ? 30.114 -4.151 23.610 1.00 38.13 ? 65 VAL B CA 1 ATOM 2014 C C . VAL B 1 51 ? 31.553 -4.108 23.078 1.00 39.15 ? 65 VAL B C 1 ATOM 2015 O O . VAL B 1 51 ? 31.882 -3.265 22.234 1.00 39.65 ? 65 VAL B O 1 ATOM 2016 C CB . VAL B 1 51 ? 29.193 -4.668 22.469 1.00 39.04 ? 65 VAL B CB 1 ATOM 2017 C CG1 . VAL B 1 51 ? 29.750 -5.970 21.837 1.00 36.68 ? 65 VAL B CG1 1 ATOM 2018 C CG2 . VAL B 1 51 ? 27.763 -4.870 22.986 1.00 36.72 ? 65 VAL B CG2 1 ATOM 2019 N N . ARG B 1 52 A 32.410 -4.958 23.624 1.00 38.67 ? 65 ARG B N 1 ATOM 2020 C CA . ARG B 1 52 A 33.750 -5.114 23.134 1.00 40.37 ? 65 ARG B CA 1 ATOM 2021 C C . ARG B 1 52 A 33.869 -6.339 22.188 1.00 40.60 ? 65 ARG B C 1 ATOM 2022 O O . ARG B 1 52 A 33.462 -7.476 22.526 1.00 39.38 ? 65 ARG B O 1 ATOM 2023 C CB . ARG B 1 52 A 34.731 -5.254 24.288 1.00 41.48 ? 65 ARG B CB 1 ATOM 2024 C CG . ARG B 1 52 A 34.976 -3.934 25.059 1.00 44.74 ? 65 ARG B CG 1 ATOM 2025 C CD . ARG B 1 52 A 36.055 -4.068 26.132 1.00 51.13 ? 65 ARG B CD 1 ATOM 2026 N NE . ARG B 1 52 A 36.392 -2.809 26.798 1.00 57.65 ? 65 ARG B NE 1 ATOM 2027 C CZ . ARG B 1 52 A 36.863 -2.737 28.036 1.00 59.25 ? 65 ARG B CZ 1 ATOM 2028 N NH1 . ARG B 1 52 A 37.138 -1.562 28.578 1.00 61.91 ? 65 ARG B NH1 1 ATOM 2029 N NH2 . ARG B 1 52 A 37.050 -3.846 28.742 1.00 60.84 ? 65 ARG B NH2 1 ATOM 2030 N N . VAL B 1 53 ? 34.409 -6.088 21.005 1.00 39.36 ? 66 VAL B N 1 ATOM 2031 C CA . VAL B 1 53 ? 34.588 -7.123 20.028 1.00 39.67 ? 66 VAL B CA 1 ATOM 2032 C C . VAL B 1 53 ? 36.040 -7.562 20.124 1.00 40.80 ? 66 VAL B C 1 ATOM 2033 O O . VAL B 1 53 ? 36.925 -6.828 19.727 1.00 41.01 ? 66 VAL B O 1 ATOM 2034 C CB . VAL B 1 53 ? 34.286 -6.595 18.656 1.00 39.42 ? 66 VAL B CB 1 ATOM 2035 C CG1 . VAL B 1 53 ? 34.403 -7.723 17.664 1.00 37.82 ? 66 VAL B CG1 1 ATOM 2036 C CG2 . VAL B 1 53 ? 32.860 -5.971 18.624 1.00 37.50 ? 66 VAL B CG2 1 ATOM 2037 N N . VAL B 1 54 ? 36.282 -8.756 20.657 1.00 41.50 ? 67 VAL B N 1 ATOM 2038 C CA . VAL B 1 54 ? 37.652 -9.234 20.888 1.00 42.01 ? 67 VAL B CA 1 ATOM 2039 C C . VAL B 1 54 ? 38.092 -10.243 19.827 1.00 43.80 ? 67 VAL B C 1 ATOM 2040 O O . VAL B 1 54 ? 37.505 -11.313 19.694 1.00 43.85 ? 67 VAL B O 1 ATOM 2041 C CB . VAL B 1 54 ? 37.754 -9.919 22.242 1.00 41.97 ? 67 VAL B CB 1 ATOM 2042 C CG1 . VAL B 1 54 ? 39.138 -10.404 22.493 1.00 41.45 ? 67 VAL B CG1 1 ATOM 2043 C CG2 . VAL B 1 54 ? 37.268 -8.999 23.378 1.00 41.88 ? 67 VAL B CG2 1 ATOM 2044 N N . LEU B 1 55 ? 39.101 -9.878 19.048 1.00 45.02 ? 68 LEU B N 1 ATOM 2045 C CA . LEU B 1 55 ? 39.671 -10.743 18.022 1.00 46.44 ? 68 LEU B CA 1 ATOM 2046 C C . LEU B 1 55 ? 40.886 -11.395 18.587 1.00 47.25 ? 68 LEU B C 1 ATOM 2047 O O . LEU B 1 55 ? 41.451 -10.932 19.578 1.00 47.87 ? 68 LEU B O 1 ATOM 2048 C CB . LEU B 1 55 ? 40.235 -9.914 16.893 1.00 45.91 ? 68 LEU B CB 1 ATOM 2049 C CG . LEU B 1 55 ? 39.379 -9.372 15.780 1.00 47.51 ? 68 LEU B CG 1 ATOM 2050 C CD1 . LEU B 1 55 ? 37.922 -9.337 16.106 1.00 44.35 ? 68 LEU B CD1 1 ATOM 2051 C CD2 . LEU B 1 55 ? 39.931 -7.988 15.432 1.00 49.30 ? 68 LEU B CD2 1 ATOM 2052 N N . GLY B 1 56 ? 41.328 -12.451 17.924 1.00 48.90 ? 69 GLY B N 1 ATOM 2053 C CA . GLY B 1 56 ? 42.575 -13.099 18.279 1.00 48.95 ? 69 GLY B CA 1 ATOM 2054 C C . GLY B 1 56 ? 42.658 -13.705 19.659 1.00 49.96 ? 69 GLY B C 1 ATOM 2055 O O . GLY B 1 56 ? 43.760 -13.869 20.194 1.00 49.55 ? 69 GLY B O 1 ATOM 2056 N N . ALA B 1 57 ? 41.510 -14.046 20.247 1.00 50.47 ? 70 ALA B N 1 ATOM 2057 C CA . ALA B 1 57 ? 41.523 -14.634 21.579 1.00 51.20 ? 70 ALA B CA 1 ATOM 2058 C C . ALA B 1 57 ? 41.605 -16.160 21.478 1.00 51.31 ? 70 ALA B C 1 ATOM 2059 O O . ALA B 1 57 ? 41.370 -16.718 20.418 1.00 50.96 ? 70 ALA B O 1 ATOM 2060 C CB . ALA B 1 57 ? 40.301 -14.199 22.375 1.00 51.04 ? 70 ALA B CB 1 ATOM 2061 N N . HIS B 1 58 ? 42.038 -16.811 22.546 1.00 52.58 ? 71 HIS B N 1 ATOM 2062 C CA . HIS B 1 58 ? 42.033 -18.269 22.594 1.00 54.32 ? 71 HIS B CA 1 ATOM 2063 C C . HIS B 1 58 ? 41.590 -18.795 23.954 1.00 54.85 ? 71 HIS B C 1 ATOM 2064 O O . HIS B 1 58 ? 40.786 -19.729 24.015 1.00 55.59 ? 71 HIS B O 1 ATOM 2065 C CB . HIS B 1 58 ? 43.364 -18.897 22.190 1.00 54.92 ? 71 HIS B CB 1 ATOM 2066 C CG . HIS B 1 58 ? 43.369 -20.389 22.324 1.00 56.33 ? 71 HIS B CG 1 ATOM 2067 N ND1 . HIS B 1 58 ? 42.728 -21.221 21.428 1.00 57.08 ? 71 HIS B ND1 1 ATOM 2068 C CD2 . HIS B 1 58 ? 43.880 -21.195 23.283 1.00 57.08 ? 71 HIS B CD2 1 ATOM 2069 C CE1 . HIS B 1 58 ? 42.881 -22.477 21.805 1.00 56.20 ? 71 HIS B CE1 1 ATOM 2070 N NE2 . HIS B 1 58 ? 43.569 -22.489 22.933 1.00 58.74 ? 71 HIS B NE2 1 ATOM 2071 N N . ASN B 1 59 ? 42.108 -18.204 25.027 1.00 55.68 ? 72 ASN B N 1 ATOM 2072 C CA . ASN B 1 59 ? 41.728 -18.574 26.385 1.00 56.96 ? 72 ASN B CA 1 ATOM 2073 C C . ASN B 1 59 ? 41.351 -17.350 27.211 1.00 57.26 ? 72 ASN B C 1 ATOM 2074 O O . ASN B 1 59 ? 42.197 -16.708 27.824 1.00 57.90 ? 72 ASN B O 1 ATOM 2075 C CB . ASN B 1 59 ? 42.845 -19.409 27.041 1.00 57.36 ? 72 ASN B CB 1 ATOM 2076 C CG . ASN B 1 59 ? 42.882 -19.297 28.563 1.00 58.29 ? 72 ASN B CG 1 ATOM 2077 O OD1 . ASN B 1 59 ? 41.861 -19.277 29.240 1.00 57.24 ? 72 ASN B OD1 1 ATOM 2078 N ND2 . ASN B 1 59 ? 44.091 -19.225 29.102 1.00 62.38 ? 72 ASN B ND2 1 ATOM 2079 N N . LEU B 1 60 ? 40.056 -17.058 27.233 1.00 57.91 ? 73 LEU B N 1 ATOM 2080 C CA . LEU B 1 60 ? 39.481 -15.891 27.905 1.00 58.28 ? 73 LEU B CA 1 ATOM 2081 C C . LEU B 1 60 ? 39.903 -15.665 29.358 1.00 59.30 ? 73 LEU B C 1 ATOM 2082 O O . LEU B 1 60 ? 39.730 -14.576 29.865 1.00 58.99 ? 73 LEU B O 1 ATOM 2083 C CB . LEU B 1 60 ? 37.941 -15.926 27.834 1.00 57.72 ? 73 LEU B CB 1 ATOM 2084 C CG . LEU B 1 60 ? 37.188 -16.062 26.502 1.00 56.88 ? 73 LEU B CG 1 ATOM 2085 C CD1 . LEU B 1 60 ? 35.677 -16.055 26.734 1.00 55.75 ? 73 LEU B CD1 1 ATOM 2086 C CD2 . LEU B 1 60 ? 37.582 -15.044 25.434 1.00 55.19 ? 73 LEU B CD2 1 ATOM 2087 N N . SER B 1 61 ? 40.407 -16.682 30.044 1.00 60.51 ? 74 SER B N 1 ATOM 2088 C CA . SER B 1 61 ? 40.840 -16.480 31.426 1.00 62.40 ? 74 SER B CA 1 ATOM 2089 C C . SER B 1 61 ? 42.210 -15.818 31.553 1.00 63.51 ? 74 SER B C 1 ATOM 2090 O O . SER B 1 61 ? 42.578 -15.335 32.623 1.00 63.89 ? 74 SER B O 1 ATOM 2091 C CB . SER B 1 61 ? 40.904 -17.816 32.145 1.00 62.72 ? 74 SER B CB 1 ATOM 2092 O OG . SER B 1 61 ? 41.509 -18.772 31.283 1.00 63.54 ? 74 SER B OG 1 ATOM 2093 N N . ARG B 1 62 ? 42.982 -15.813 30.478 1.00 64.72 ? 75 ARG B N 1 ATOM 2094 C CA . ARG B 1 62 ? 44.305 -15.214 30.542 1.00 66.42 ? 75 ARG B CA 1 ATOM 2095 C C . ARG B 1 62 ? 44.458 -13.932 29.727 1.00 66.45 ? 75 ARG B C 1 ATOM 2096 O O . ARG B 1 62 ? 43.672 -13.627 28.827 1.00 66.41 ? 75 ARG B O 1 ATOM 2097 C CB . ARG B 1 62 ? 45.383 -16.222 30.102 1.00 66.58 ? 75 ARG B CB 1 ATOM 2098 C CG . ARG B 1 62 ? 45.735 -17.257 31.166 1.00 69.68 ? 75 ARG B CG 1 ATOM 2099 C CD . ARG B 1 62 ? 46.199 -16.659 32.512 1.00 74.60 ? 75 ARG B CD 1 ATOM 2100 N NE . ARG B 1 62 ? 47.629 -16.330 32.526 1.00 76.08 ? 75 ARG B NE 1 ATOM 2101 C CZ . ARG B 1 62 ? 48.118 -15.094 32.561 1.00 77.72 ? 75 ARG B CZ 1 ATOM 2102 N NH1 . ARG B 1 62 ? 47.299 -14.047 32.598 1.00 77.46 ? 75 ARG B NH1 1 ATOM 2103 N NH2 . ARG B 1 62 ? 49.434 -14.902 32.565 1.00 79.11 ? 75 ARG B NH2 1 ATOM 2104 N N . ARG B 1 63 ? 45.497 -13.182 30.071 1.00 67.09 ? 76 ARG B N 1 ATOM 2105 C CA . ARG B 1 63 ? 45.901 -12.003 29.324 1.00 67.51 ? 76 ARG B CA 1 ATOM 2106 C C . ARG B 1 63 ? 46.407 -12.548 28.004 1.00 66.87 ? 76 ARG B C 1 ATOM 2107 O O . ARG B 1 63 ? 47.042 -13.603 27.967 1.00 67.06 ? 76 ARG B O 1 ATOM 2108 C CB . ARG B 1 63 ? 47.051 -11.329 30.046 1.00 68.34 ? 76 ARG B CB 1 ATOM 2109 C CG . ARG B 1 63 ? 48.343 -12.152 29.990 1.00 71.38 ? 76 ARG B CG 1 ATOM 2110 C CD . ARG B 1 63 ? 49.622 -11.379 30.361 1.00 77.51 ? 76 ARG B CD 1 ATOM 2111 N NE . ARG B 1 63 ? 49.672 -10.042 29.753 1.00 81.83 ? 76 ARG B NE 1 ATOM 2112 C CZ . ARG B 1 63 ? 49.564 -9.816 28.451 1.00 84.05 ? 76 ARG B CZ 1 ATOM 2113 N NH1 . ARG B 1 63 ? 49.410 -10.835 27.619 1.00 85.66 ? 76 ARG B NH1 1 ATOM 2114 N NH2 . ARG B 1 63 ? 49.589 -8.583 27.979 1.00 85.77 ? 76 ARG B NH2 1 ATOM 2115 N N . GLU B 1 64 ? 46.144 -11.837 26.918 1.00 66.15 ? 77 GLU B N 1 ATOM 2116 C CA . GLU B 1 64 ? 46.553 -12.332 25.614 1.00 65.22 ? 77 GLU B CA 1 ATOM 2117 C C . GLU B 1 64 ? 46.962 -11.199 24.663 1.00 64.87 ? 77 GLU B C 1 ATOM 2118 O O . GLU B 1 64 ? 46.113 -10.527 24.084 1.00 64.84 ? 77 GLU B O 1 ATOM 2119 C CB . GLU B 1 64 ? 45.438 -13.200 24.990 1.00 64.94 ? 77 GLU B CB 1 ATOM 2120 C CG . GLU B 1 64 ? 45.000 -14.411 25.813 1.00 63.76 ? 77 GLU B CG 1 ATOM 2121 C CD . GLU B 1 64 ? 44.154 -15.390 25.016 1.00 63.95 ? 77 GLU B CD 1 ATOM 2122 O OE1 . GLU B 1 64 ? 44.453 -16.594 25.028 1.00 62.92 ? 77 GLU B OE1 1 ATOM 2123 O OE2 . GLU B 1 64 ? 43.186 -14.963 24.358 1.00 65.62 ? 77 GLU B OE2 1 ATOM 2124 N N . PRO B 1 65 ? 48.269 -10.992 24.518 1.00 64.38 ? 78 PRO B N 1 ATOM 2125 C CA . PRO B 1 65 ? 48.812 -9.948 23.642 1.00 63.68 ? 78 PRO B CA 1 ATOM 2126 C C . PRO B 1 65 ? 48.264 -10.075 22.237 1.00 62.97 ? 78 PRO B C 1 ATOM 2127 O O . PRO B 1 65 ? 48.167 -9.079 21.524 1.00 62.98 ? 78 PRO B O 1 ATOM 2128 C CB . PRO B 1 65 ? 50.315 -10.254 23.621 1.00 63.86 ? 78 PRO B CB 1 ATOM 2129 C CG . PRO B 1 65 ? 50.585 -10.988 24.895 1.00 64.24 ? 78 PRO B CG 1 ATOM 2130 C CD . PRO B 1 65 ? 49.327 -11.736 25.226 1.00 64.56 ? 78 PRO B CD 1 ATOM 2131 N N . THR B 1 66 ? 47.919 -11.301 21.858 1.00 62.02 ? 79 THR B N 1 ATOM 2132 C CA . THR B 1 66 ? 47.384 -11.593 20.536 1.00 61.02 ? 79 THR B CA 1 ATOM 2133 C C . THR B 1 66 ? 46.031 -10.946 20.300 1.00 59.53 ? 79 THR B C 1 ATOM 2134 O O . THR B 1 66 ? 45.535 -10.965 19.187 1.00 59.59 ? 79 THR B O 1 ATOM 2135 C CB . THR B 1 66 ? 47.254 -13.130 20.328 1.00 61.34 ? 79 THR B CB 1 ATOM 2136 O OG1 . THR B 1 66 ? 46.552 -13.707 21.434 1.00 62.89 ? 79 THR B OG1 1 ATOM 2137 C CG2 . THR B 1 66 ? 48.630 -13.814 20.417 1.00 61.59 ? 79 THR B CG2 1 ATOM 2138 N N . ARG B 1 67 ? 45.414 -10.387 21.333 1.00 57.88 ? 80 ARG B N 1 ATOM 2139 C CA . ARG B 1 67 ? 44.094 -9.786 21.131 1.00 56.74 ? 80 ARG B CA 1 ATOM 2140 C C . ARG B 1 67 ? 44.115 -8.414 20.458 1.00 55.30 ? 80 ARG B C 1 ATOM 2141 O O . ARG B 1 67 ? 45.038 -7.621 20.616 1.00 54.84 ? 80 ARG B O 1 ATOM 2142 C CB . ARG B 1 67 ? 43.315 -9.682 22.434 1.00 57.27 ? 80 ARG B CB 1 ATOM 2143 C CG . ARG B 1 67 ? 42.738 -10.987 22.934 1.00 57.96 ? 80 ARG B CG 1 ATOM 2144 C CD . ARG B 1 67 ? 42.269 -10.891 24.366 1.00 60.04 ? 80 ARG B CD 1 ATOM 2145 N NE . ARG B 1 67 ? 42.219 -12.179 25.043 1.00 62.17 ? 80 ARG B NE 1 ATOM 2146 C CZ . ARG B 1 67 ? 41.714 -12.340 26.263 1.00 62.83 ? 80 ARG B CZ 1 ATOM 2147 N NH1 . ARG B 1 67 ? 41.219 -11.282 26.907 1.00 62.86 ? 80 ARG B NH1 1 ATOM 2148 N NH2 . ARG B 1 67 ? 41.698 -13.544 26.836 1.00 61.09 ? 80 ARG B NH2 1 ATOM 2149 N N . GLN B 1 68 ? 43.087 -8.179 19.667 1.00 53.00 ? 81 GLN B N 1 ATOM 2150 C CA . GLN B 1 68 ? 42.857 -6.900 19.039 1.00 50.19 ? 81 GLN B CA 1 ATOM 2151 C C . GLN B 1 68 ? 41.424 -6.639 19.457 1.00 48.69 ? 81 GLN B C 1 ATOM 2152 O O . GLN B 1 68 ? 40.528 -7.470 19.190 1.00 47.34 ? 81 GLN B O 1 ATOM 2153 C CB . GLN B 1 68 ? 42.991 -6.988 17.513 1.00 50.27 ? 81 GLN B CB 1 ATOM 2154 C CG . GLN B 1 68 ? 44.442 -6.899 17.012 1.00 49.04 ? 81 GLN B CG 1 ATOM 2155 C CD . GLN B 1 68 ? 44.565 -6.970 15.520 1.00 50.21 ? 81 GLN B CD 1 ATOM 2156 O OE1 . GLN B 1 68 ? 43.945 -6.187 14.769 1.00 53.25 ? 81 GLN B OE1 1 ATOM 2157 N NE2 . GLN B 1 68 ? 45.372 -7.906 15.058 1.00 52.77 ? 81 GLN B NE2 1 ATOM 2158 N N . VAL B 1 69 ? 41.210 -5.515 20.146 1.00 45.99 ? 82 VAL B N 1 ATOM 2159 C CA . VAL B 1 69 ? 39.887 -5.202 20.668 1.00 43.22 ? 82 VAL B CA 1 ATOM 2160 C C . VAL B 1 69 ? 39.237 -4.013 20.005 1.00 42.32 ? 82 VAL B C 1 ATOM 2161 O O . VAL B 1 69 ? 39.817 -2.949 19.912 1.00 42.71 ? 82 VAL B O 1 ATOM 2162 C CB . VAL B 1 69 ? 39.902 -5.007 22.176 1.00 42.77 ? 82 VAL B CB 1 ATOM 2163 C CG1 . VAL B 1 69 ? 38.485 -4.960 22.679 1.00 43.28 ? 82 VAL B CG1 1 ATOM 2164 C CG2 . VAL B 1 69 ? 40.561 -6.146 22.824 1.00 43.44 ? 82 VAL B CG2 1 ATOM 2165 N N . PHE B 1 70 ? 38.019 -4.206 19.526 1.00 41.30 ? 83 PHE B N 1 ATOM 2166 C CA . PHE B 1 70 ? 37.270 -3.157 18.861 1.00 39.76 ? 83 PHE B CA 1 ATOM 2167 C C . PHE B 1 70 ? 35.901 -2.848 19.508 1.00 37.95 ? 83 PHE B C 1 ATOM 2168 O O . PHE B 1 70 ? 35.466 -3.510 20.478 1.00 37.95 ? 83 PHE B O 1 ATOM 2169 C CB . PHE B 1 70 ? 37.109 -3.512 17.379 1.00 40.62 ? 83 PHE B CB 1 ATOM 2170 C CG . PHE B 1 70 ? 38.426 -3.515 16.603 1.00 42.93 ? 83 PHE B CG 1 ATOM 2171 C CD1 . PHE B 1 70 ? 39.206 -4.649 16.526 1.00 44.74 ? 83 PHE B CD1 1 ATOM 2172 C CD2 . PHE B 1 70 ? 38.882 -2.349 15.973 1.00 46.72 ? 83 PHE B CD2 1 ATOM 2173 C CE1 . PHE B 1 70 ? 40.439 -4.644 15.828 1.00 48.72 ? 83 PHE B CE1 1 ATOM 2174 C CE2 . PHE B 1 70 ? 40.102 -2.329 15.263 1.00 46.32 ? 83 PHE B CE2 1 ATOM 2175 C CZ . PHE B 1 70 ? 40.872 -3.467 15.181 1.00 46.44 ? 83 PHE B CZ 1 ATOM 2176 N N . ALA B 1 71 ? 35.247 -1.844 18.950 1.00 36.18 ? 84 ALA B N 1 ATOM 2177 C CA . ALA B 1 71 ? 33.936 -1.375 19.355 1.00 35.10 ? 84 ALA B CA 1 ATOM 2178 C C . ALA B 1 71 ? 33.038 -1.376 18.166 1.00 33.14 ? 84 ALA B C 1 ATOM 2179 O O . ALA B 1 71 ? 33.510 -1.372 17.045 1.00 31.96 ? 84 ALA B O 1 ATOM 2180 C CB . ALA B 1 71 ? 34.027 0.064 19.934 1.00 36.35 ? 84 ALA B CB 1 ATOM 2181 N N . VAL B 1 72 ? 31.725 -1.353 18.404 1.00 32.80 ? 85 VAL B N 1 ATOM 2182 C CA . VAL B 1 72 ? 30.754 -1.433 17.336 1.00 32.70 ? 85 VAL B CA 1 ATOM 2183 C C . VAL B 1 72 ? 30.492 -0.063 16.742 1.00 34.02 ? 85 VAL B C 1 ATOM 2184 O O . VAL B 1 72 ? 30.262 0.899 17.494 1.00 33.84 ? 85 VAL B O 1 ATOM 2185 C CB . VAL B 1 72 ? 29.375 -1.999 17.837 1.00 32.53 ? 85 VAL B CB 1 ATOM 2186 C CG1 . VAL B 1 72 ? 28.343 -1.717 16.835 1.00 32.40 ? 85 VAL B CG1 1 ATOM 2187 C CG2 . VAL B 1 72 ? 29.442 -3.531 18.081 1.00 34.24 ? 85 VAL B CG2 1 ATOM 2188 N N . GLN B 1 73 ? 30.471 0.043 15.410 1.00 34.10 ? 86 GLN B N 1 ATOM 2189 C CA . GLN B 1 73 ? 30.231 1.332 14.772 1.00 34.58 ? 86 GLN B CA 1 ATOM 2190 C C . GLN B 1 73 ? 28.960 1.442 13.920 1.00 34.70 ? 86 GLN B C 1 ATOM 2191 O O . GLN B 1 73 ? 28.383 2.537 13.778 1.00 33.70 ? 86 GLN B O 1 ATOM 2192 C CB . GLN B 1 73 ? 31.480 1.753 13.928 1.00 35.73 ? 86 GLN B CB 1 ATOM 2193 C CG . GLN B 1 73 ? 31.342 3.120 13.133 1.00 35.55 ? 86 GLN B CG 1 ATOM 2194 C CD . GLN B 1 73 ? 32.665 3.513 12.379 1.00 40.64 ? 86 GLN B CD 1 ATOM 2195 O OE1 . GLN B 1 73 ? 32.678 3.779 11.173 1.00 44.26 ? 86 GLN B OE1 1 ATOM 2196 N NE2 . GLN B 1 73 ? 33.737 3.497 13.088 1.00 40.95 ? 86 GLN B NE2 1 ATOM 2197 N N . ARG B 1 74 ? 28.566 0.358 13.250 1.00 33.31 ? 87 ARG B N 1 ATOM 2198 C CA . ARG B 1 74 ? 27.326 0.347 12.482 1.00 33.57 ? 87 ARG B CA 1 ATOM 2199 C C . ARG B 1 74 ? 26.690 -1.024 12.609 1.00 33.11 ? 87 ARG B C 1 ATOM 2200 O O . ARG B 1 74 ? 27.401 -1.999 12.677 1.00 31.94 ? 87 ARG B O 1 ATOM 2201 C CB . ARG B 1 74 ? 27.590 0.488 10.999 1.00 35.50 ? 87 ARG B CB 1 ATOM 2202 C CG . ARG B 1 74 ? 27.298 1.827 10.422 1.00 40.05 ? 87 ARG B CG 1 ATOM 2203 C CD . ARG B 1 74 ? 28.478 2.615 10.024 1.00 41.05 ? 87 ARG B CD 1 ATOM 2204 N NE . ARG B 1 74 ? 28.034 3.575 9.022 1.00 50.26 ? 87 ARG B NE 1 ATOM 2205 C CZ . ARG B 1 74 ? 28.757 4.563 8.541 1.00 53.09 ? 87 ARG B CZ 1 ATOM 2206 N NH1 . ARG B 1 74 ? 28.231 5.365 7.623 1.00 53.70 ? 87 ARG B NH1 1 ATOM 2207 N NH2 . ARG B 1 74 ? 30.010 4.750 8.956 1.00 56.09 ? 87 ARG B NH2 1 ATOM 2208 N N . ILE B 1 75 ? 25.361 -1.059 12.523 1.00 31.74 ? 88 ILE B N 1 ATOM 2209 C CA . ILE B 1 75 ? 24.587 -2.254 12.635 1.00 31.81 ? 88 ILE B CA 1 ATOM 2210 C C . ILE B 1 75 ? 23.616 -2.385 11.458 1.00 31.12 ? 88 ILE B C 1 ATOM 2211 O O . ILE B 1 75 ? 22.926 -1.443 11.081 1.00 29.61 ? 88 ILE B O 1 ATOM 2212 C CB . ILE B 1 75 ? 23.757 -2.185 13.987 1.00 32.98 ? 88 ILE B CB 1 ATOM 2213 C CG1 . ILE B 1 75 ? 24.697 -1.905 15.189 1.00 28.45 ? 88 ILE B CG1 1 ATOM 2214 C CG2 . ILE B 1 75 ? 22.869 -3.478 14.147 1.00 26.63 ? 88 ILE B CG2 1 ATOM 2215 C CD1 . ILE B 1 75 ? 23.985 -1.464 16.548 1.00 27.79 ? 88 ILE B CD1 1 ATOM 2216 N N . PHE B 1 76 ? 23.565 -3.592 10.908 1.00 29.85 ? 89 PHE B N 1 ATOM 2217 C CA . PHE B 1 76 ? 22.730 -3.940 9.788 1.00 29.77 ? 89 PHE B CA 1 ATOM 2218 C C . PHE B 1 76 ? 21.952 -5.258 10.121 1.00 28.78 ? 89 PHE B C 1 ATOM 2219 O O . PHE B 1 76 ? 22.565 -6.195 10.531 1.00 25.75 ? 89 PHE B O 1 ATOM 2220 C CB . PHE B 1 76 ? 23.669 -4.264 8.627 1.00 30.23 ? 89 PHE B CB 1 ATOM 2221 C CG . PHE B 1 76 ? 24.554 -3.115 8.194 1.00 29.96 ? 89 PHE B CG 1 ATOM 2222 C CD1 . PHE B 1 76 ? 24.138 -2.267 7.179 1.00 28.83 ? 89 PHE B CD1 1 ATOM 2223 C CD2 . PHE B 1 76 ? 25.810 -2.935 8.759 1.00 28.20 ? 89 PHE B CD2 1 ATOM 2224 C CE1 . PHE B 1 76 ? 24.973 -1.217 6.713 1.00 30.96 ? 89 PHE B CE1 1 ATOM 2225 C CE2 . PHE B 1 76 ? 26.645 -1.902 8.310 1.00 31.84 ? 89 PHE B CE2 1 ATOM 2226 C CZ . PHE B 1 76 ? 26.234 -1.062 7.272 1.00 29.49 ? 89 PHE B CZ 1 ATOM 2227 N N . GLU B 1 77 ? 20.639 -5.295 9.905 1.00 29.32 ? 90 GLU B N 1 ATOM 2228 C CA . GLU B 1 77 ? 19.828 -6.452 10.168 1.00 32.59 ? 90 GLU B CA 1 ATOM 2229 C C . GLU B 1 77 ? 18.838 -6.481 9.028 1.00 33.37 ? 90 GLU B C 1 ATOM 2230 O O . GLU B 1 77 ? 18.433 -5.426 8.531 1.00 31.10 ? 90 GLU B O 1 ATOM 2231 C CB . GLU B 1 77 ? 19.097 -6.345 11.558 1.00 31.74 ? 90 GLU B CB 1 ATOM 2232 C CG . GLU B 1 77 ? 20.078 -6.482 12.715 1.00 29.06 ? 90 GLU B CG 1 ATOM 2233 C CD . GLU B 1 77 ? 19.393 -6.389 14.094 1.00 28.07 ? 90 GLU B CD 1 ATOM 2234 O OE1 . GLU B 1 77 ? 20.070 -6.522 15.094 1.00 29.17 ? 90 GLU B OE1 1 ATOM 2235 O OE2 . GLU B 1 77 ? 18.176 -6.204 14.199 1.00 27.32 ? 90 GLU B OE2 1 ATOM 2236 N N . ASN B 1 78 ? 18.423 -7.687 8.633 1.00 32.75 ? 91 ASN B N 1 ATOM 2237 C CA . ASN B 1 78 ? 17.537 -7.810 7.475 1.00 32.62 ? 91 ASN B CA 1 ATOM 2238 C C . ASN B 1 78 ? 16.404 -8.735 7.759 1.00 33.99 ? 91 ASN B C 1 ATOM 2239 O O . ASN B 1 78 ? 16.421 -9.886 7.269 1.00 34.36 ? 91 ASN B O 1 ATOM 2240 C CB . ASN B 1 78 ? 18.369 -8.364 6.290 1.00 32.54 ? 91 ASN B CB 1 ATOM 2241 C CG . ASN B 1 78 ? 17.616 -8.387 4.972 1.00 36.79 ? 91 ASN B CG 1 ATOM 2242 O OD1 . ASN B 1 78 ? 16.377 -8.118 4.884 1.00 38.96 ? 91 ASN B OD1 1 ATOM 2243 N ND2 . ASN B 1 78 ? 18.195 -8.755 3.950 1.00 36.44 ? 91 ASN B ND2 1 ATOM 2244 N N . GLY B 1 79 ? 15.411 -8.291 8.529 1.00 32.60 ? 92 GLY B N 1 ATOM 2245 C CA . GLY B 1 79 ? 14.224 -9.105 8.694 1.00 33.78 ? 92 GLY B CA 1 ATOM 2246 C C . GLY B 1 79 ? 14.215 -10.054 9.907 1.00 34.72 ? 92 GLY B C 1 ATOM 2247 O O . GLY B 1 79 ? 13.405 -10.976 9.955 1.00 35.33 ? 92 GLY B O 1 ATOM 2248 N N . TYR B 1 80 ? 15.053 -9.776 10.904 1.00 33.47 ? 94 TYR B N 1 ATOM 2249 C CA . TYR B 1 80 ? 15.082 -10.555 12.152 1.00 33.27 ? 94 TYR B CA 1 ATOM 2250 C C . TYR B 1 80 ? 13.742 -10.511 12.828 1.00 33.45 ? 94 TYR B C 1 ATOM 2251 O O . TYR B 1 80 ? 13.140 -9.452 12.968 1.00 31.19 ? 94 TYR B O 1 ATOM 2252 C CB . TYR B 1 80 ? 16.156 -9.983 13.095 1.00 33.77 ? 94 TYR B CB 1 ATOM 2253 C CG . TYR B 1 80 ? 16.092 -10.407 14.551 1.00 33.77 ? 94 TYR B CG 1 ATOM 2254 C CD1 . TYR B 1 80 ? 16.006 -9.470 15.588 1.00 33.61 ? 94 TYR B CD1 1 ATOM 2255 C CD2 . TYR B 1 80 ? 16.180 -11.740 14.897 1.00 31.85 ? 94 TYR B CD2 1 ATOM 2256 C CE1 . TYR B 1 80 ? 16.013 -9.886 16.933 1.00 32.55 ? 94 TYR B CE1 1 ATOM 2257 C CE2 . TYR B 1 80 ? 16.205 -12.129 16.209 1.00 31.03 ? 94 TYR B CE2 1 ATOM 2258 C CZ . TYR B 1 80 ? 16.114 -11.244 17.192 1.00 30.51 ? 94 TYR B CZ 1 ATOM 2259 O OH . TYR B 1 80 ? 16.078 -11.723 18.454 1.00 32.01 ? 94 TYR B OH 1 ATOM 2260 N N . ASP B 1 81 ? 13.255 -11.698 13.193 1.00 33.06 ? 95 ASP B N 1 ATOM 2261 C CA . ASP B 1 81 ? 12.006 -11.885 13.855 1.00 34.21 ? 95 ASP B CA 1 ATOM 2262 C C . ASP B 1 81 ? 12.328 -12.202 15.345 1.00 35.31 ? 95 ASP B C 1 ATOM 2263 O O . ASP B 1 81 ? 12.931 -13.247 15.651 1.00 35.89 ? 95 ASP B O 1 ATOM 2264 C CB . ASP B 1 81 ? 11.290 -13.090 13.171 1.00 33.55 ? 95 ASP B CB 1 ATOM 2265 C CG . ASP B 1 81 ? 9.903 -13.302 13.666 1.00 33.91 ? 95 ASP B CG 1 ATOM 2266 O OD1 . ASP B 1 81 ? 9.690 -13.134 14.892 1.00 34.97 ? 95 ASP B OD1 1 ATOM 2267 O OD2 . ASP B 1 81 ? 8.957 -13.655 12.908 1.00 33.68 ? 95 ASP B OD2 1 ATOM 2268 N N . PRO B 1 82 ? 12.013 -11.302 16.268 1.00 35.62 ? 98 PRO B N 1 ATOM 2269 C CA . PRO B 1 82 ? 12.340 -11.553 17.679 1.00 36.45 ? 98 PRO B CA 1 ATOM 2270 C C . PRO B 1 82 ? 11.517 -12.665 18.323 1.00 36.42 ? 98 PRO B C 1 ATOM 2271 O O . PRO B 1 82 ? 11.940 -13.206 19.334 1.00 35.47 ? 98 PRO B O 1 ATOM 2272 C CB . PRO B 1 82 ? 11.974 -10.244 18.385 1.00 35.95 ? 98 PRO B CB 1 ATOM 2273 C CG . PRO B 1 82 ? 11.362 -9.400 17.429 1.00 35.32 ? 98 PRO B CG 1 ATOM 2274 C CD . PRO B 1 82 ? 11.356 -10.013 16.067 1.00 34.80 ? 98 PRO B CD 1 ATOM 2275 N N . VAL B 1 83 ? 10.341 -12.950 17.760 1.00 38.00 ? 99 VAL B N 1 ATOM 2276 C CA . VAL B 1 83 ? 9.431 -13.980 18.265 1.00 38.25 ? 99 VAL B CA 1 ATOM 2277 C C . VAL B 1 83 ? 9.919 -15.405 17.975 1.00 39.40 ? 99 VAL B C 1 ATOM 2278 O O . VAL B 1 83 ? 9.976 -16.224 18.889 1.00 40.61 ? 99 VAL B O 1 ATOM 2279 C CB . VAL B 1 83 ? 8.032 -13.765 17.697 1.00 39.27 ? 99 VAL B CB 1 ATOM 2280 C CG1 . VAL B 1 83 ? 6.988 -14.768 18.265 1.00 38.19 ? 99 VAL B CG1 1 ATOM 2281 C CG2 . VAL B 1 83 ? 7.590 -12.339 17.969 1.00 38.34 ? 99 VAL B CG2 1 ATOM 2282 N N . ASN B 1 84 A 10.340 -15.705 16.751 1.00 37.72 ? 99 ASN B N 1 ATOM 2283 C CA . ASN B 1 84 A 10.752 -17.091 16.461 1.00 36.73 ? 99 ASN B CA 1 ATOM 2284 C C . ASN B 1 84 A 12.200 -17.216 16.045 1.00 35.56 ? 99 ASN B C 1 ATOM 2285 O O . ASN B 1 84 A 12.637 -18.294 15.677 1.00 34.11 ? 99 ASN B O 1 ATOM 2286 C CB . ASN B 1 84 A 9.832 -17.694 15.394 1.00 36.44 ? 99 ASN B CB 1 ATOM 2287 C CG . ASN B 1 84 A 9.780 -16.831 14.131 1.00 39.53 ? 99 ASN B CG 1 ATOM 2288 O OD1 . ASN B 1 84 A 10.616 -15.968 13.949 1.00 35.94 ? 99 ASN B OD1 1 ATOM 2289 N ND2 . ASN B 1 84 A 8.823 -17.101 13.244 1.00 42.90 ? 99 ASN B ND2 1 ATOM 2290 N N . LEU B 1 85 B 12.974 -16.115 16.080 1.00 33.08 ? 99 LEU B N 1 ATOM 2291 C CA . LEU B 1 85 B 14.395 -16.184 15.626 1.00 30.79 ? 99 LEU B CA 1 ATOM 2292 C C . LEU B 1 85 B 14.676 -16.456 14.133 1.00 29.17 ? 99 LEU B C 1 ATOM 2293 O O . LEU B 1 85 B 15.789 -16.764 13.768 1.00 29.83 ? 99 LEU B O 1 ATOM 2294 C CB . LEU B 1 85 B 15.306 -17.016 16.531 1.00 30.78 ? 99 LEU B CB 1 ATOM 2295 C CG . LEU B 1 85 B 15.272 -16.873 18.072 1.00 33.34 ? 99 LEU B CG 1 ATOM 2296 C CD1 . LEU B 1 85 B 16.357 -17.727 18.812 1.00 29.52 ? 99 LEU B CD1 1 ATOM 2297 C CD2 . LEU B 1 85 B 15.361 -15.390 18.481 1.00 35.91 ? 99 LEU B CD2 1 ATOM 2298 N N . LEU B 1 86 ? 13.689 -16.342 13.277 1.00 31.83 ? 100 LEU B N 1 ATOM 2299 C CA . LEU B 1 86 ? 13.929 -16.325 11.818 1.00 34.07 ? 100 LEU B CA 1 ATOM 2300 C C . LEU B 1 86 ? 14.946 -15.206 11.488 1.00 33.63 ? 100 LEU B C 1 ATOM 2301 O O . LEU B 1 86 ? 14.901 -14.126 12.120 1.00 35.03 ? 100 LEU B O 1 ATOM 2302 C CB . LEU B 1 86 ? 12.663 -15.871 11.054 1.00 34.66 ? 100 LEU B CB 1 ATOM 2303 C CG . LEU B 1 86 ? 11.340 -16.568 10.702 1.00 40.96 ? 100 LEU B CG 1 ATOM 2304 C CD1 . LEU B 1 86 ? 10.697 -15.823 9.565 1.00 44.00 ? 100 LEU B CD1 1 ATOM 2305 C CD2 . LEU B 1 86 ? 11.481 -18.077 10.268 1.00 40.16 ? 100 LEU B CD2 1 ATOM 2306 N N . ASN B 1 87 ? 15.805 -15.408 10.484 1.00 31.98 ? 101 ASN B N 1 ATOM 2307 C CA . ASN B 1 87 ? 16.763 -14.371 10.071 1.00 32.71 ? 101 ASN B CA 1 ATOM 2308 C C . ASN B 1 87 ? 17.575 -13.816 11.253 1.00 32.55 ? 101 ASN B C 1 ATOM 2309 O O . ASN B 1 87 ? 17.698 -12.589 11.445 1.00 29.25 ? 101 ASN B O 1 ATOM 2310 C CB . ASN B 1 87 ? 16.039 -13.205 9.367 1.00 31.74 ? 101 ASN B CB 1 ATOM 2311 C CG . ASN B 1 87 ? 15.223 -13.659 8.107 1.00 35.46 ? 101 ASN B CG 1 ATOM 2312 O OD1 . ASN B 1 87 ? 14.314 -12.976 7.682 1.00 40.90 ? 101 ASN B OD1 1 ATOM 2313 N ND2 . ASN B 1 87 ? 15.554 -14.828 7.545 1.00 29.80 ? 101 ASN B ND2 1 ATOM 2314 N N . ASP B 1 88 ? 18.123 -14.733 12.034 1.00 29.84 ? 102 ASP B N 1 ATOM 2315 C CA . ASP B 1 88 ? 18.953 -14.381 13.203 1.00 30.07 ? 102 ASP B CA 1 ATOM 2316 C C . ASP B 1 88 ? 20.378 -14.024 12.874 1.00 28.47 ? 102 ASP B C 1 ATOM 2317 O O . ASP B 1 88 ? 21.294 -14.736 13.291 1.00 28.76 ? 102 ASP B O 1 ATOM 2318 C CB . ASP B 1 88 ? 19.006 -15.596 14.131 1.00 28.79 ? 102 ASP B CB 1 ATOM 2319 C CG . ASP B 1 88 ? 19.316 -15.230 15.523 1.00 30.98 ? 102 ASP B CG 1 ATOM 2320 O OD1 . ASP B 1 88 ? 19.424 -14.012 15.775 1.00 30.14 ? 102 ASP B OD1 1 ATOM 2321 O OD2 . ASP B 1 88 ? 19.469 -16.088 16.435 1.00 31.32 ? 102 ASP B OD2 1 ATOM 2322 N N . ILE B 1 89 ? 20.590 -12.897 12.170 1.00 29.24 ? 103 ILE B N 1 ATOM 2323 C CA . ILE B 1 89 ? 21.950 -12.508 11.815 1.00 26.45 ? 103 ILE B CA 1 ATOM 2324 C C . ILE B 1 89 ? 22.059 -10.957 11.861 1.00 25.94 ? 103 ILE B C 1 ATOM 2325 O O . ILE B 1 89 ? 21.099 -10.254 11.541 1.00 24.40 ? 103 ILE B O 1 ATOM 2326 C CB . ILE B 1 89 ? 22.222 -13.011 10.380 1.00 26.33 ? 103 ILE B CB 1 ATOM 2327 C CG1 . ILE B 1 89 ? 23.593 -12.643 9.851 1.00 28.35 ? 103 ILE B CG1 1 ATOM 2328 C CG2 . ILE B 1 89 ? 21.166 -12.570 9.485 1.00 23.22 ? 103 ILE B CG2 1 ATOM 2329 C CD1 . ILE B 1 89 ? 23.870 -13.299 8.434 1.00 30.58 ? 103 ILE B CD1 1 ATOM 2330 N N . VAL B 1 90 ? 23.252 -10.481 12.176 1.00 26.50 ? 104 VAL B N 1 ATOM 2331 C CA . VAL B 1 90 ? 23.515 -9.079 12.190 1.00 27.97 ? 104 VAL B CA 1 ATOM 2332 C C . VAL B 1 90 ? 24.974 -8.924 11.753 1.00 28.98 ? 104 VAL B C 1 ATOM 2333 O O . VAL B 1 90 ? 25.811 -9.737 12.087 1.00 29.79 ? 104 VAL B O 1 ATOM 2334 C CB . VAL B 1 90 ? 23.276 -8.506 13.591 1.00 27.44 ? 104 VAL B CB 1 ATOM 2335 C CG1 . VAL B 1 90 ? 24.116 -9.236 14.668 1.00 26.85 ? 104 VAL B CG1 1 ATOM 2336 C CG2 . VAL B 1 90 ? 23.574 -6.992 13.645 1.00 25.49 ? 104 VAL B CG2 1 ATOM 2337 N N . ILE B 1 91 ? 25.244 -7.888 10.960 1.00 30.06 ? 105 ILE B N 1 ATOM 2338 C CA . ILE B 1 91 ? 26.602 -7.555 10.558 1.00 28.87 ? 105 ILE B CA 1 ATOM 2339 C C . ILE B 1 91 ? 26.994 -6.316 11.363 1.00 29.71 ? 105 ILE B C 1 ATOM 2340 O O . ILE B 1 91 ? 26.236 -5.358 11.393 1.00 28.95 ? 105 ILE B O 1 ATOM 2341 C CB . ILE B 1 91 ? 26.588 -7.156 9.092 1.00 29.81 ? 105 ILE B CB 1 ATOM 2342 C CG1 . ILE B 1 91 ? 26.119 -8.324 8.241 1.00 31.39 ? 105 ILE B CG1 1 ATOM 2343 C CG2 . ILE B 1 91 ? 27.990 -6.783 8.649 1.00 27.00 ? 105 ILE B CG2 1 ATOM 2344 C CD1 . ILE B 1 91 ? 26.890 -9.606 8.563 1.00 35.05 ? 105 ILE B CD1 1 ATOM 2345 N N . LEU B 1 92 ? 28.148 -6.346 12.005 1.00 29.66 ? 106 LEU B N 1 ATOM 2346 C CA . LEU B 1 92 ? 28.612 -5.226 12.794 1.00 31.57 ? 106 LEU B CA 1 ATOM 2347 C C . LEU B 1 92 ? 29.852 -4.671 12.171 1.00 32.46 ? 106 LEU B C 1 ATOM 2348 O O . LEU B 1 92 ? 30.840 -5.342 12.095 1.00 32.91 ? 106 LEU B O 1 ATOM 2349 C CB . LEU B 1 92 ? 28.926 -5.631 14.233 1.00 28.86 ? 106 LEU B CB 1 ATOM 2350 C CG . LEU B 1 92 ? 27.723 -6.381 14.887 1.00 30.99 ? 106 LEU B CG 1 ATOM 2351 C CD1 . LEU B 1 92 ? 28.062 -7.133 16.191 1.00 32.53 ? 106 LEU B CD1 1 ATOM 2352 C CD2 . LEU B 1 92 ? 26.517 -5.480 15.060 1.00 28.46 ? 106 LEU B CD2 1 ATOM 2353 N N . GLN B 1 93 ? 29.813 -3.409 11.757 1.00 34.03 ? 107 GLN B N 1 ATOM 2354 C CA . GLN B 1 93 ? 31.066 -2.733 11.367 1.00 33.17 ? 107 GLN B CA 1 ATOM 2355 C C . GLN B 1 93 ? 31.795 -2.296 12.643 1.00 32.57 ? 107 GLN B C 1 ATOM 2356 O O . GLN B 1 93 ? 31.166 -1.954 13.644 1.00 32.96 ? 107 GLN B O 1 ATOM 2357 C CB . GLN B 1 93 ? 30.698 -1.578 10.436 1.00 33.78 ? 107 GLN B CB 1 ATOM 2358 C CG . GLN B 1 93 ? 31.851 -0.882 9.832 1.00 34.14 ? 107 GLN B CG 1 ATOM 2359 C CD . GLN B 1 93 ? 31.421 0.171 8.839 1.00 37.04 ? 107 GLN B CD 1 ATOM 2360 O OE1 . GLN B 1 93 ? 30.330 0.101 8.234 1.00 41.09 ? 107 GLN B OE1 1 ATOM 2361 N NE2 . GLN B 1 93 ? 32.269 1.134 8.647 1.00 36.04 ? 107 GLN B NE2 1 ATOM 2362 N N . LEU B 1 94 ? 33.129 -2.363 12.646 1.00 32.86 ? 108 LEU B N 1 ATOM 2363 C CA . LEU B 1 94 ? 33.925 -2.058 13.793 1.00 33.63 ? 108 LEU B CA 1 ATOM 2364 C C . LEU B 1 94 ? 34.392 -0.571 13.755 1.00 35.85 ? 108 LEU B C 1 ATOM 2365 O O . LEU B 1 94 ? 34.244 0.095 12.713 1.00 36.46 ? 108 LEU B O 1 ATOM 2366 C CB . LEU B 1 94 ? 35.131 -2.989 13.838 1.00 33.34 ? 108 LEU B CB 1 ATOM 2367 C CG . LEU B 1 94 ? 34.711 -4.483 13.718 1.00 33.87 ? 108 LEU B CG 1 ATOM 2368 C CD1 . LEU B 1 94 ? 35.974 -5.285 13.877 1.00 25.89 ? 108 LEU B CD1 1 ATOM 2369 C CD2 . LEU B 1 94 ? 33.693 -4.770 14.794 1.00 25.68 ? 108 LEU B CD2 1 ATOM 2370 N N . ASN B 1 95 ? 34.975 -0.082 14.838 1.00 36.80 ? 109 ASN B N 1 ATOM 2371 C CA . ASN B 1 95 ? 35.361 1.331 14.817 1.00 40.76 ? 109 ASN B CA 1 ATOM 2372 C C . ASN B 1 95 ? 36.675 1.507 14.060 1.00 42.45 ? 109 ASN B C 1 ATOM 2373 O O . ASN B 1 95 ? 36.984 2.625 13.689 1.00 43.69 ? 109 ASN B O 1 ATOM 2374 C CB . ASN B 1 95 ? 35.457 1.940 16.198 1.00 40.24 ? 109 ASN B CB 1 ATOM 2375 C CG . ASN B 1 95 ? 36.345 1.167 17.086 1.00 41.39 ? 109 ASN B CG 1 ATOM 2376 O OD1 . ASN B 1 95 ? 36.419 -0.066 16.952 1.00 42.65 ? 109 ASN B OD1 1 ATOM 2377 N ND2 . ASN B 1 95 ? 37.002 1.861 18.043 1.00 43.81 ? 109 ASN B ND2 1 ATOM 2378 N N . GLY B 1 96 ? 37.379 0.394 13.800 1.00 42.33 ? 110 GLY B N 1 ATOM 2379 C CA . GLY B 1 96 ? 38.634 0.342 13.027 1.00 42.93 ? 110 GLY B CA 1 ATOM 2380 C C . GLY B 1 96 ? 38.860 -1.000 12.274 1.00 42.49 ? 110 GLY B C 1 ATOM 2381 O O . GLY B 1 96 ? 37.953 -1.807 12.153 1.00 41.90 ? 110 GLY B O 1 ATOM 2382 N N . SER B 1 97 ? 40.054 -1.228 11.733 1.00 42.62 ? 111 SER B N 1 ATOM 2383 C CA . SER B 1 97 ? 40.341 -2.449 10.945 1.00 41.97 ? 111 SER B CA 1 ATOM 2384 C C . SER B 1 97 ? 41.300 -3.375 11.613 1.00 41.99 ? 111 SER B C 1 ATOM 2385 O O . SER B 1 97 ? 42.315 -2.942 12.168 1.00 42.02 ? 111 SER B O 1 ATOM 2386 C CB . SER B 1 97 ? 40.903 -2.079 9.566 1.00 41.71 ? 111 SER B CB 1 ATOM 2387 O OG . SER B 1 97 ? 39.902 -1.418 8.838 1.00 40.99 ? 111 SER B OG 1 ATOM 2388 N N . ALA B 1 98 ? 41.015 -4.664 11.544 1.00 41.34 ? 112 ALA B N 1 ATOM 2389 C CA . ALA B 1 98 ? 41.928 -5.621 12.168 1.00 42.74 ? 112 ALA B CA 1 ATOM 2390 C C . ALA B 1 98 ? 43.262 -5.630 11.417 1.00 43.27 ? 112 ALA B C 1 ATOM 2391 O O . ALA B 1 98 ? 43.309 -5.271 10.258 1.00 42.08 ? 112 ALA B O 1 ATOM 2392 C CB . ALA B 1 98 ? 41.321 -7.029 12.189 1.00 41.41 ? 112 ALA B CB 1 ATOM 2393 N N . THR B 1 99 ? 44.338 -5.978 12.117 1.00 45.27 ? 113 THR B N 1 ATOM 2394 C CA . THR B 1 99 ? 45.618 -6.231 11.469 1.00 47.91 ? 113 THR B CA 1 ATOM 2395 C C . THR B 1 99 ? 45.698 -7.728 11.150 1.00 48.66 ? 113 THR B C 1 ATOM 2396 O O . THR B 1 99 ? 45.887 -8.548 12.040 1.00 48.48 ? 113 THR B O 1 ATOM 2397 C CB . THR B 1 99 ? 46.789 -5.823 12.397 1.00 49.34 ? 113 THR B CB 1 ATOM 2398 O OG1 . THR B 1 99 ? 46.978 -4.389 12.353 1.00 50.81 ? 113 THR B OG1 1 ATOM 2399 C CG2 . THR B 1 99 ? 48.115 -6.382 11.839 1.00 50.39 ? 113 THR B CG2 1 ATOM 2400 N N . ILE B 1 100 ? 45.514 -8.081 9.884 1.00 50.41 ? 114 ILE B N 1 ATOM 2401 C CA . ILE B 1 100 ? 45.546 -9.474 9.458 1.00 52.03 ? 114 ILE B CA 1 ATOM 2402 C C . ILE B 1 100 ? 46.896 -10.075 9.720 1.00 53.85 ? 114 ILE B C 1 ATOM 2403 O O . ILE B 1 100 ? 47.885 -9.653 9.107 1.00 54.40 ? 114 ILE B O 1 ATOM 2404 C CB . ILE B 1 100 ? 45.302 -9.583 7.961 1.00 52.16 ? 114 ILE B CB 1 ATOM 2405 C CG1 . ILE B 1 100 ? 43.991 -8.960 7.570 1.00 50.87 ? 114 ILE B CG1 1 ATOM 2406 C CG2 . ILE B 1 100 ? 45.261 -11.043 7.501 1.00 51.50 ? 114 ILE B CG2 1 ATOM 2407 C CD1 . ILE B 1 100 ? 43.907 -8.879 6.073 1.00 49.15 ? 114 ILE B CD1 1 ATOM 2408 N N . ASN B 1 101 ? 46.944 -11.036 10.639 1.00 54.57 ? 115 ASN B N 1 ATOM 2409 C CA . ASN B 1 101 ? 48.170 -11.770 10.936 1.00 55.85 ? 115 ASN B CA 1 ATOM 2410 C C . ASN B 1 101 ? 47.883 -13.274 11.190 1.00 56.20 ? 115 ASN B C 1 ATOM 2411 O O . ASN B 1 101 ? 46.838 -13.798 10.764 1.00 56.02 ? 115 ASN B O 1 ATOM 2412 C CB . ASN B 1 101 ? 48.912 -11.138 12.113 1.00 55.08 ? 115 ASN B CB 1 ATOM 2413 C CG . ASN B 1 101 ? 48.090 -11.141 13.374 1.00 56.18 ? 115 ASN B CG 1 ATOM 2414 O OD1 . ASN B 1 101 ? 47.155 -11.929 13.496 1.00 55.77 ? 115 ASN B OD1 1 ATOM 2415 N ND2 . ASN B 1 101 ? 48.420 -10.248 14.322 1.00 53.94 ? 115 ASN B ND2 1 ATOM 2416 N N . ALA B 1 102 ? 48.798 -13.944 11.888 1.00 56.66 ? 116 ALA B N 1 ATOM 2417 C CA . ALA B 1 102 ? 48.662 -15.375 12.181 1.00 57.05 ? 116 ALA B CA 1 ATOM 2418 C C . ALA B 1 102 ? 47.413 -15.641 13.002 1.00 56.96 ? 116 ALA B C 1 ATOM 2419 O O . ALA B 1 102 ? 46.675 -16.596 12.744 1.00 57.15 ? 116 ALA B O 1 ATOM 2420 C CB . ALA B 1 102 ? 49.895 -15.896 12.931 1.00 56.88 ? 116 ALA B CB 1 ATOM 2421 N N . ASN B 1 103 ? 47.188 -14.772 13.980 1.00 56.21 ? 117 ASN B N 1 ATOM 2422 C CA . ASN B 1 103 ? 46.073 -14.890 14.917 1.00 55.27 ? 117 ASN B CA 1 ATOM 2423 C C . ASN B 1 103 ? 44.737 -14.270 14.480 1.00 53.98 ? 117 ASN B C 1 ATOM 2424 O O . ASN B 1 103 ? 43.706 -14.514 15.087 1.00 54.37 ? 117 ASN B O 1 ATOM 2425 C CB . ASN B 1 103 ? 46.495 -14.325 16.277 1.00 55.00 ? 117 ASN B CB 1 ATOM 2426 C CG . ASN B 1 103 ? 47.611 -15.131 16.919 1.00 56.95 ? 117 ASN B CG 1 ATOM 2427 O OD1 . ASN B 1 103 ? 48.373 -14.619 17.739 1.00 59.58 ? 117 ASN B OD1 1 ATOM 2428 N ND2 . ASN B 1 103 ? 47.717 -16.398 16.544 1.00 56.85 ? 117 ASN B ND2 1 ATOM 2429 N N . VAL B 1 104 ? 44.727 -13.483 13.423 1.00 52.70 ? 118 VAL B N 1 ATOM 2430 C CA . VAL B 1 104 ? 43.487 -12.838 13.034 1.00 50.93 ? 118 VAL B CA 1 ATOM 2431 C C . VAL B 1 104 ? 43.310 -12.849 11.547 1.00 50.55 ? 118 VAL B C 1 ATOM 2432 O O . VAL B 1 104 ? 44.106 -12.231 10.865 1.00 50.38 ? 118 VAL B O 1 ATOM 2433 C CB . VAL B 1 104 ? 43.477 -11.331 13.509 1.00 50.71 ? 118 VAL B CB 1 ATOM 2434 C CG1 . VAL B 1 104 ? 42.224 -10.635 13.026 1.00 49.60 ? 118 VAL B CG1 1 ATOM 2435 C CG2 . VAL B 1 104 ? 43.623 -11.227 15.034 1.00 47.88 ? 118 VAL B CG2 1 ATOM 2436 N N . GLN B 1 105 ? 42.271 -13.509 11.036 1.00 51.38 ? 119 GLN B N 1 ATOM 2437 C CA . GLN B 1 105 ? 42.040 -13.578 9.587 1.00 52.02 ? 119 GLN B CA 1 ATOM 2438 C C . GLN B 1 105 ? 40.571 -13.594 9.273 1.00 52.39 ? 119 GLN B C 1 ATOM 2439 O O . GLN B 1 105 ? 39.762 -13.988 10.095 1.00 53.70 ? 119 GLN B O 1 ATOM 2440 C CB . GLN B 1 105 ? 42.658 -14.848 8.959 1.00 52.48 ? 119 GLN B CB 1 ATOM 2441 C CG . GLN B 1 105 ? 44.146 -15.071 9.146 1.00 52.31 ? 119 GLN B CG 1 ATOM 2442 C CD . GLN B 1 105 ? 45.021 -14.482 8.001 1.00 55.53 ? 119 GLN B CD 1 ATOM 2443 O OE1 . GLN B 1 105 ? 44.664 -14.531 6.802 1.00 51.14 ? 119 GLN B OE1 1 ATOM 2444 N NE2 . GLN B 1 105 ? 46.181 -13.946 8.384 1.00 55.01 ? 119 GLN B NE2 1 ATOM 2445 N N . VAL B 1 106 ? 40.232 -13.204 8.058 1.00 52.42 ? 120 VAL B N 1 ATOM 2446 C CA . VAL B 1 106 ? 38.861 -13.165 7.603 1.00 53.67 ? 120 VAL B CA 1 ATOM 2447 C C . VAL B 1 106 ? 38.482 -14.568 7.137 1.00 54.97 ? 120 VAL B C 1 ATOM 2448 O O . VAL B 1 106 ? 39.256 -15.191 6.428 1.00 55.21 ? 120 VAL B O 1 ATOM 2449 C CB . VAL B 1 106 ? 38.692 -12.126 6.460 1.00 53.22 ? 120 VAL B CB 1 ATOM 2450 C CG1 . VAL B 1 106 ? 37.379 -12.278 5.746 1.00 53.12 ? 120 VAL B CG1 1 ATOM 2451 C CG2 . VAL B 1 106 ? 38.815 -10.736 7.013 1.00 52.62 ? 120 VAL B CG2 1 ATOM 2452 N N . ALA B 1 107 ? 37.321 -15.063 7.567 1.00 55.69 ? 121 ALA B N 1 ATOM 2453 C CA . ALA B 1 107 ? 36.822 -16.394 7.203 1.00 56.71 ? 121 ALA B CA 1 ATOM 2454 C C . ALA B 1 107 ? 36.167 -16.229 5.874 1.00 57.18 ? 121 ALA B C 1 ATOM 2455 O O . ALA B 1 107 ? 35.876 -15.104 5.488 1.00 58.09 ? 121 ALA B O 1 ATOM 2456 C CB . ALA B 1 107 ? 35.788 -16.874 8.214 1.00 55.91 ? 121 ALA B CB 1 ATOM 2457 N N . GLN B 1 108 ? 35.909 -17.320 5.161 1.00 57.54 ? 122 GLN B N 1 ATOM 2458 C CA . GLN B 1 108 ? 35.291 -17.156 3.850 1.00 58.36 ? 122 GLN B CA 1 ATOM 2459 C C . GLN B 1 108 ? 33.850 -17.627 3.911 1.00 57.60 ? 122 GLN B C 1 ATOM 2460 O O . GLN B 1 108 ? 33.516 -18.510 4.691 1.00 57.78 ? 122 GLN B O 1 ATOM 2461 C CB . GLN B 1 108 ? 36.070 -17.910 2.745 1.00 58.96 ? 122 GLN B CB 1 ATOM 2462 C CG . GLN B 1 108 ? 37.584 -17.551 2.554 1.00 63.30 ? 122 GLN B CG 1 ATOM 2463 C CD . GLN B 1 108 ? 37.863 -16.110 1.981 1.00 68.03 ? 122 GLN B CD 1 ATOM 2464 O OE1 . GLN B 1 108 ? 37.282 -15.704 0.967 1.00 70.48 ? 122 GLN B OE1 1 ATOM 2465 N NE2 . GLN B 1 108 ? 38.759 -15.355 2.640 1.00 68.50 ? 122 GLN B NE2 1 ATOM 2466 N N . LEU B 1 109 ? 33.000 -17.038 3.090 1.00 56.84 ? 123 LEU B N 1 ATOM 2467 C CA . LEU B 1 109 ? 31.599 -17.393 3.068 1.00 56.84 ? 123 LEU B CA 1 ATOM 2468 C C . LEU B 1 109 ? 31.199 -18.254 1.849 1.00 57.57 ? 123 LEU B C 1 ATOM 2469 O O . LEU B 1 109 ? 31.891 -18.242 0.835 1.00 57.91 ? 123 LEU B O 1 ATOM 2470 C CB . LEU B 1 109 ? 30.759 -16.095 3.077 1.00 56.21 ? 123 LEU B CB 1 ATOM 2471 C CG . LEU B 1 109 ? 30.688 -15.184 4.336 1.00 54.64 ? 123 LEU B CG 1 ATOM 2472 C CD1 . LEU B 1 109 ? 29.289 -15.059 4.926 1.00 48.80 ? 123 LEU B CD1 1 ATOM 2473 C CD2 . LEU B 1 109 ? 31.647 -15.615 5.443 1.00 51.83 ? 123 LEU B CD2 1 ATOM 2474 N N . PRO B 1 110 ? 30.057 -18.934 1.959 1.00 58.01 ? 124 PRO B N 1 ATOM 2475 C CA . PRO B 1 110 ? 29.448 -19.723 0.876 1.00 57.94 ? 124 PRO B CA 1 ATOM 2476 C C . PRO B 1 110 ? 28.776 -18.814 -0.184 1.00 58.08 ? 124 PRO B C 1 ATOM 2477 O O . PRO B 1 110 ? 28.347 -17.692 0.111 1.00 57.83 ? 124 PRO B O 1 ATOM 2478 C CB . PRO B 1 110 ? 28.331 -20.443 1.617 1.00 57.98 ? 124 PRO B CB 1 ATOM 2479 C CG . PRO B 1 110 ? 27.939 -19.409 2.650 1.00 58.25 ? 124 PRO B CG 1 ATOM 2480 C CD . PRO B 1 110 ? 29.266 -19.009 3.200 1.00 57.26 ? 124 PRO B CD 1 ATOM 2481 N N . ALA B 1 111 ? 28.643 -19.330 -1.400 1.00 56.75 ? 125 ALA B N 1 ATOM 2482 C CA . ALA B 1 111 ? 27.972 -18.599 -2.448 1.00 56.26 ? 125 ALA B CA 1 ATOM 2483 C C . ALA B 1 111 ? 26.502 -18.436 -2.111 1.00 55.88 ? 125 ALA B C 1 ATOM 2484 O O . ALA B 1 111 ? 25.900 -19.329 -1.524 1.00 55.89 ? 125 ALA B O 1 ATOM 2485 C CB . ALA B 1 111 ? 28.104 -19.339 -3.791 1.00 56.12 ? 125 ALA B CB 1 ATOM 2486 N N . GLN B 1 112 ? 25.917 -17.315 -2.507 1.00 54.76 ? 126 GLN B N 1 ATOM 2487 C CA . GLN B 1 112 ? 24.498 -17.147 -2.321 1.00 54.71 ? 126 GLN B CA 1 ATOM 2488 C C . GLN B 1 112 ? 23.890 -18.428 -2.791 1.00 56.56 ? 126 GLN B C 1 ATOM 2489 O O . GLN B 1 112 ? 24.417 -19.043 -3.733 1.00 57.05 ? 126 GLN B O 1 ATOM 2490 C CB . GLN B 1 112 ? 23.938 -15.986 -3.153 1.00 53.63 ? 126 GLN B CB 1 ATOM 2491 C CG . GLN B 1 112 ? 22.427 -15.788 -3.048 1.00 47.98 ? 126 GLN B CG 1 ATOM 2492 C CD . GLN B 1 112 ? 21.999 -15.352 -1.641 1.00 46.56 ? 126 GLN B CD 1 ATOM 2493 O OE1 . GLN B 1 112 ? 22.829 -14.961 -0.860 1.00 44.29 ? 126 GLN B OE1 1 ATOM 2494 N NE2 . GLN B 1 112 ? 20.703 -15.432 -1.334 1.00 45.48 ? 126 GLN B NE2 1 ATOM 2495 N N . GLY B 1 113 ? 22.805 -18.813 -2.113 1.00 57.82 ? 127 GLY B N 1 ATOM 2496 C CA . GLY B 1 113 ? 21.974 -19.965 -2.433 1.00 59.86 ? 127 GLY B CA 1 ATOM 2497 C C . GLY B 1 113 ? 22.431 -21.375 -2.092 1.00 60.40 ? 127 GLY B C 1 ATOM 2498 O O . GLY B 1 113 ? 21.610 -22.289 -2.034 1.00 60.25 ? 127 GLY B O 1 ATOM 2499 N N . ARG B 1 114 ? 23.728 -21.555 -1.892 1.00 61.45 ? 128 ARG B N 1 ATOM 2500 C CA . ARG B 1 114 ? 24.280 -22.866 -1.624 1.00 63.57 ? 128 ARG B CA 1 ATOM 2501 C C . ARG B 1 114 ? 23.608 -23.576 -0.420 1.00 64.34 ? 128 ARG B C 1 ATOM 2502 O O . ARG B 1 114 ? 23.759 -23.170 0.749 1.00 63.58 ? 128 ARG B O 1 ATOM 2503 C CB . ARG B 1 114 ? 25.796 -22.762 -1.462 1.00 63.82 ? 128 ARG B CB 1 ATOM 2504 C CG . ARG B 1 114 ? 26.419 -24.003 -0.891 1.00 66.36 ? 128 ARG B CG 1 ATOM 2505 C CD . ARG B 1 114 ? 27.919 -24.055 -1.030 1.00 70.48 ? 128 ARG B CD 1 ATOM 2506 N NE . ARG B 1 114 ? 28.375 -25.324 -1.598 1.00 73.33 ? 128 ARG B NE 1 ATOM 2507 C CZ . ARG B 1 114 ? 29.412 -25.432 -2.425 1.00 74.24 ? 128 ARG B CZ 1 ATOM 2508 N NH1 . ARG B 1 114 ? 29.785 -26.623 -2.898 1.00 74.55 ? 128 ARG B NH1 1 ATOM 2509 N NH2 . ARG B 1 114 ? 30.083 -24.341 -2.768 1.00 73.31 ? 128 ARG B NH2 1 ATOM 2510 N N . ARG B 1 115 ? 22.856 -24.632 -0.736 1.00 65.59 ? 129 ARG B N 1 ATOM 2511 C CA . ARG B 1 115 ? 22.117 -25.438 0.243 1.00 66.76 ? 129 ARG B CA 1 ATOM 2512 C C . ARG B 1 115 ? 22.850 -26.699 0.722 1.00 66.51 ? 129 ARG B C 1 ATOM 2513 O O . ARG B 1 115 ? 23.483 -27.404 -0.062 1.00 66.73 ? 129 ARG B O 1 ATOM 2514 C CB . ARG B 1 115 ? 20.749 -25.832 -0.316 1.00 67.49 ? 129 ARG B CB 1 ATOM 2515 C CG . ARG B 1 115 ? 19.725 -26.188 0.757 1.00 70.00 ? 129 ARG B CG 1 ATOM 2516 C CD . ARG B 1 115 ? 18.362 -26.598 0.223 1.00 75.45 ? 129 ARG B CD 1 ATOM 2517 N NE . ARG B 1 115 ? 18.299 -28.036 -0.058 1.00 80.20 ? 129 ARG B NE 1 ATOM 2518 C CZ . ARG B 1 115 ? 17.234 -28.663 -0.552 1.00 82.49 ? 129 ARG B CZ 1 ATOM 2519 N NH1 . ARG B 1 115 ? 17.271 -29.976 -0.776 1.00 84.34 ? 129 ARG B NH1 1 ATOM 2520 N NH2 . ARG B 1 115 ? 16.130 -27.980 -0.824 1.00 83.36 ? 129 ARG B NH2 1 ATOM 2521 N N . LEU B 1 116 ? 22.724 -26.966 2.021 1.00 65.81 ? 130 LEU B N 1 ATOM 2522 C CA . LEU B 1 116 ? 23.391 -28.077 2.682 1.00 65.18 ? 130 LEU B CA 1 ATOM 2523 C C . LEU B 1 116 ? 22.484 -29.310 2.855 1.00 65.02 ? 130 LEU B C 1 ATOM 2524 O O . LEU B 1 116 ? 21.320 -29.206 3.302 1.00 65.06 ? 130 LEU B O 1 ATOM 2525 C CB . LEU B 1 116 ? 23.973 -27.619 4.027 1.00 65.22 ? 130 LEU B CB 1 ATOM 2526 C CG . LEU B 1 116 ? 25.226 -26.734 3.992 1.00 63.66 ? 130 LEU B CG 1 ATOM 2527 C CD1 . LEU B 1 116 ? 25.969 -26.761 5.329 1.00 61.85 ? 130 LEU B CD1 1 ATOM 2528 C CD2 . LEU B 1 116 ? 26.122 -27.190 2.872 1.00 62.58 ? 130 LEU B CD2 1 ATOM 2529 N N . GLY B 1 117 ? 23.034 -30.476 2.507 1.00 64.54 ? 131 GLY B N 1 ATOM 2530 C CA . GLY B 1 117 ? 22.318 -31.750 2.539 1.00 62.73 ? 131 GLY B CA 1 ATOM 2531 C C . GLY B 1 117 ? 22.616 -32.687 3.695 1.00 61.73 ? 131 GLY B C 1 ATOM 2532 O O . GLY B 1 117 ? 23.778 -32.882 4.097 1.00 61.81 ? 131 GLY B O 1 ATOM 2533 N N . ASN B 1 118 ? 21.551 -33.272 4.229 1.00 60.23 ? 132 ASN B N 1 ATOM 2534 C CA . ASN B 1 118 ? 21.694 -34.213 5.313 1.00 59.82 ? 132 ASN B CA 1 ATOM 2535 C C . ASN B 1 118 ? 22.963 -35.026 5.055 1.00 58.07 ? 132 ASN B C 1 ATOM 2536 O O . ASN B 1 118 ? 23.183 -35.518 3.942 1.00 57.80 ? 132 ASN B O 1 ATOM 2537 C CB . ASN B 1 118 ? 20.456 -35.110 5.434 1.00 59.88 ? 132 ASN B CB 1 ATOM 2538 C CG . ASN B 1 118 ? 20.372 -35.806 6.801 1.00 63.99 ? 132 ASN B CG 1 ATOM 2539 O OD1 . ASN B 1 118 ? 19.396 -36.504 7.106 1.00 67.86 ? 132 ASN B OD1 1 ATOM 2540 N ND2 . ASN B 1 118 ? 21.397 -35.602 7.638 1.00 65.55 ? 132 ASN B ND2 1 ATOM 2541 N N . GLY B 1 119 ? 23.827 -35.113 6.058 1.00 56.22 ? 133 GLY B N 1 ATOM 2542 C CA . GLY B 1 119 ? 25.047 -35.874 5.925 1.00 54.54 ? 133 GLY B CA 1 ATOM 2543 C C . GLY B 1 119 ? 26.373 -35.157 5.976 1.00 53.73 ? 133 GLY B C 1 ATOM 2544 O O . GLY B 1 119 ? 27.354 -35.766 6.368 1.00 54.16 ? 133 GLY B O 1 ATOM 2545 N N . VAL B 1 120 ? 26.445 -33.890 5.572 1.00 52.69 ? 134 VAL B N 1 ATOM 2546 C CA . VAL B 1 120 ? 27.737 -33.177 5.582 1.00 51.96 ? 134 VAL B CA 1 ATOM 2547 C C . VAL B 1 120 ? 28.430 -33.063 6.960 1.00 51.13 ? 134 VAL B C 1 ATOM 2548 O O . VAL B 1 120 ? 27.769 -32.933 7.976 1.00 50.87 ? 134 VAL B O 1 ATOM 2549 C CB . VAL B 1 120 ? 27.592 -31.748 5.001 1.00 52.40 ? 134 VAL B CB 1 ATOM 2550 C CG1 . VAL B 1 120 ? 28.983 -31.211 4.621 1.00 52.88 ? 134 VAL B CG1 1 ATOM 2551 C CG2 . VAL B 1 120 ? 26.635 -31.742 3.778 1.00 53.51 ? 134 VAL B CG2 1 ATOM 2552 N N . GLN B 1 121 ? 29.753 -33.092 7.013 1.00 50.16 ? 135 GLN B N 1 ATOM 2553 C CA . GLN B 1 121 ? 30.411 -33.002 8.307 1.00 50.33 ? 135 GLN B CA 1 ATOM 2554 C C . GLN B 1 121 ? 31.041 -31.654 8.639 1.00 49.98 ? 135 GLN B C 1 ATOM 2555 O O . GLN B 1 121 ? 32.082 -31.261 8.093 1.00 50.92 ? 135 GLN B O 1 ATOM 2556 C CB . GLN B 1 121 ? 31.422 -34.117 8.497 1.00 50.66 ? 135 GLN B CB 1 ATOM 2557 C CG . GLN B 1 121 ? 30.830 -35.528 8.288 1.00 52.97 ? 135 GLN B CG 1 ATOM 2558 C CD . GLN B 1 121 ? 30.032 -36.012 9.469 1.00 56.33 ? 135 GLN B CD 1 ATOM 2559 O OE1 . GLN B 1 121 ? 30.554 -36.063 10.592 1.00 59.61 ? 135 GLN B OE1 1 ATOM 2560 N NE2 . GLN B 1 121 ? 28.761 -36.357 9.237 1.00 56.14 ? 135 GLN B NE2 1 ATOM 2561 N N . CYS B 1 122 ? 30.423 -30.959 9.583 1.00 49.24 ? 136 CYS B N 1 ATOM 2562 C CA . CYS B 1 122 ? 30.877 -29.618 9.941 1.00 48.03 ? 136 CYS B CA 1 ATOM 2563 C C . CYS B 1 122 ? 31.509 -29.554 11.285 1.00 47.21 ? 136 CYS B C 1 ATOM 2564 O O . CYS B 1 122 ? 31.579 -30.539 12.026 1.00 46.94 ? 136 CYS B O 1 ATOM 2565 C CB . CYS B 1 122 ? 29.720 -28.635 9.952 1.00 46.84 ? 136 CYS B CB 1 ATOM 2566 S SG . CYS B 1 122 ? 28.819 -28.588 8.440 1.00 46.08 ? 136 CYS B SG 1 ATOM 2567 N N . LEU B 1 123 ? 31.932 -28.351 11.627 1.00 46.06 ? 137 LEU B N 1 ATOM 2568 C CA . LEU B 1 123 ? 32.553 -28.158 12.913 1.00 46.08 ? 137 LEU B CA 1 ATOM 2569 C C . LEU B 1 123 ? 31.956 -26.917 13.567 1.00 44.70 ? 137 LEU B C 1 ATOM 2570 O O . LEU B 1 123 ? 31.924 -25.858 12.961 1.00 44.52 ? 137 LEU B O 1 ATOM 2571 C CB . LEU B 1 123 ? 34.064 -28.029 12.744 1.00 45.59 ? 137 LEU B CB 1 ATOM 2572 C CG . LEU B 1 123 ? 34.850 -27.953 14.053 1.00 48.97 ? 137 LEU B CG 1 ATOM 2573 C CD1 . LEU B 1 123 ? 35.010 -29.305 14.760 1.00 51.35 ? 137 LEU B CD1 1 ATOM 2574 C CD2 . LEU B 1 123 ? 36.223 -27.362 13.785 1.00 50.82 ? 137 LEU B CD2 1 ATOM 2575 N N . ALA B 1 124 ? 31.481 -27.079 14.802 1.00 43.90 ? 138 ALA B N 1 ATOM 2576 C CA . ALA B 1 124 ? 30.934 -25.981 15.572 1.00 41.78 ? 138 ALA B CA 1 ATOM 2577 C C . ALA B 1 124 ? 31.940 -25.611 16.614 1.00 41.15 ? 138 ALA B C 1 ATOM 2578 O O . ALA B 1 124 ? 32.824 -26.402 16.924 1.00 40.64 ? 138 ALA B O 1 ATOM 2579 C CB . ALA B 1 124 ? 29.624 -26.370 16.176 1.00 42.18 ? 138 ALA B CB 1 ATOM 2580 N N . MET B 1 125 ? 31.841 -24.388 17.139 1.00 39.80 ? 139 MET B N 1 ATOM 2581 C CA . MET B 1 125 ? 32.781 -23.929 18.130 1.00 38.78 ? 139 MET B CA 1 ATOM 2582 C C . MET B 1 125 ? 32.180 -22.768 18.940 1.00 39.03 ? 139 MET B C 1 ATOM 2583 O O . MET B 1 125 ? 31.176 -22.179 18.532 1.00 39.50 ? 139 MET B O 1 ATOM 2584 C CB . MET B 1 125 ? 34.063 -23.456 17.439 1.00 38.08 ? 139 MET B CB 1 ATOM 2585 C CG . MET B 1 125 ? 33.832 -22.267 16.506 1.00 37.94 ? 139 MET B CG 1 ATOM 2586 S SD . MET B 1 125 ? 35.392 -21.868 15.703 1.00 42.79 ? 139 MET B SD 1 ATOM 2587 C CE . MET B 1 125 ? 34.909 -22.028 14.266 1.00 41.87 ? 139 MET B CE 1 ATOM 2588 N N . GLY B 1 126 ? 32.808 -22.456 20.066 1.00 38.86 ? 140 GLY B N 1 ATOM 2589 C CA . GLY B 1 126 ? 32.367 -21.378 20.952 1.00 40.29 ? 140 GLY B CA 1 ATOM 2590 C C . GLY B 1 126 ? 32.999 -21.459 22.339 1.00 41.41 ? 140 GLY B C 1 ATOM 2591 O O . GLY B 1 126 ? 33.600 -22.484 22.714 1.00 41.79 ? 140 GLY B O 1 ATOM 2592 N N . TRP B 1 127 ? 32.871 -20.374 23.113 1.00 41.87 ? 141 TRP B N 1 ATOM 2593 C CA . TRP B 1 127 ? 33.307 -20.345 24.504 1.00 41.58 ? 141 TRP B CA 1 ATOM 2594 C C . TRP B 1 127 ? 32.070 -20.494 25.400 1.00 42.38 ? 141 TRP B C 1 ATOM 2595 O O . TRP B 1 127 ? 32.103 -20.151 26.572 1.00 43.44 ? 141 TRP B O 1 ATOM 2596 C CB . TRP B 1 127 ? 33.954 -18.994 24.824 1.00 42.01 ? 141 TRP B CB 1 ATOM 2597 C CG . TRP B 1 127 ? 35.382 -18.799 24.379 1.00 39.60 ? 141 TRP B CG 1 ATOM 2598 C CD1 . TRP B 1 127 ? 36.532 -19.225 25.036 1.00 40.83 ? 141 TRP B CD1 1 ATOM 2599 C CD2 . TRP B 1 127 ? 35.831 -18.073 23.237 1.00 39.49 ? 141 TRP B CD2 1 ATOM 2600 N NE1 . TRP B 1 127 ? 37.651 -18.842 24.333 1.00 38.98 ? 141 TRP B NE1 1 ATOM 2601 C CE2 . TRP B 1 127 ? 37.252 -18.128 23.227 1.00 42.32 ? 141 TRP B CE2 1 ATOM 2602 C CE3 . TRP B 1 127 ? 35.184 -17.394 22.200 1.00 40.31 ? 141 TRP B CE3 1 ATOM 2603 C CZ2 . TRP B 1 127 ? 38.018 -17.507 22.231 1.00 39.07 ? 141 TRP B CZ2 1 ATOM 2604 C CZ3 . TRP B 1 127 ? 35.947 -16.793 21.201 1.00 41.08 ? 141 TRP B CZ3 1 ATOM 2605 C CH2 . TRP B 1 127 ? 37.347 -16.841 21.239 1.00 43.54 ? 141 TRP B CH2 1 ATOM 2606 N N . GLY B 1 128 ? 30.964 -20.976 24.848 1.00 43.12 ? 142 GLY B N 1 ATOM 2607 C CA . GLY B 1 128 ? 29.756 -21.172 25.622 1.00 44.52 ? 142 GLY B CA 1 ATOM 2608 C C . GLY B 1 128 ? 29.811 -22.188 26.753 1.00 46.36 ? 142 GLY B C 1 ATOM 2609 O O . GLY B 1 128 ? 30.837 -22.867 26.969 1.00 44.79 ? 142 GLY B O 1 ATOM 2610 N N . LEU B 1 129 ? 28.686 -22.268 27.456 1.00 48.24 ? 143 LEU B N 1 ATOM 2611 C CA . LEU B 1 129 ? 28.513 -23.096 28.628 1.00 51.87 ? 143 LEU B CA 1 ATOM 2612 C C . LEU B 1 129 ? 28.958 -24.534 28.396 1.00 54.55 ? 143 LEU B C 1 ATOM 2613 O O . LEU B 1 129 ? 28.484 -25.202 27.471 1.00 54.72 ? 143 LEU B O 1 ATOM 2614 C CB . LEU B 1 129 ? 27.025 -23.118 28.997 1.00 51.65 ? 143 LEU B CB 1 ATOM 2615 C CG . LEU B 1 129 ? 26.689 -22.933 30.471 1.00 52.00 ? 143 LEU B CG 1 ATOM 2616 C CD1 . LEU B 1 129 ? 27.163 -21.571 30.973 1.00 51.21 ? 143 LEU B CD1 1 ATOM 2617 C CD2 . LEU B 1 129 ? 25.203 -23.103 30.680 1.00 53.01 ? 143 LEU B CD2 1 ATOM 2618 N N . LEU B 1 130 ? 29.838 -25.023 29.264 1.00 57.21 ? 144 LEU B N 1 ATOM 2619 C CA . LEU B 1 130 ? 30.342 -26.377 29.141 1.00 59.82 ? 144 LEU B CA 1 ATOM 2620 C C . LEU B 1 130 ? 29.188 -27.347 29.391 1.00 62.22 ? 144 LEU B C 1 ATOM 2621 O O . LEU B 1 130 ? 29.261 -28.514 29.020 1.00 61.42 ? 144 LEU B O 1 ATOM 2622 C CB . LEU B 1 130 ? 31.477 -26.651 30.120 1.00 59.87 ? 144 LEU B CB 1 ATOM 2623 C CG . LEU B 1 130 ? 32.718 -27.213 29.429 1.00 59.60 ? 144 LEU B CG 1 ATOM 2624 C CD1 . LEU B 1 130 ? 32.895 -26.587 28.051 1.00 58.24 ? 144 LEU B CD1 1 ATOM 2625 C CD2 . LEU B 1 130 ? 33.950 -26.947 30.267 1.00 61.99 ? 144 LEU B CD2 1 ATOM 2626 N N . GLY B 1 131 ? 28.114 -26.855 30.009 1.00 65.00 ? 145 GLY B N 1 ATOM 2627 C CA . GLY B 1 131 ? 26.929 -27.660 30.273 1.00 68.73 ? 145 GLY B CA 1 ATOM 2628 C C . GLY B 1 131 ? 25.942 -27.170 31.343 1.00 71.47 ? 145 GLY B C 1 ATOM 2629 O O . GLY B 1 131 ? 24.721 -27.094 31.095 1.00 71.43 ? 145 GLY B O 1 ATOM 2630 N N . ARG B 1 132 ? 26.471 -26.841 32.528 1.00 74.02 ? 147 ARG B N 1 ATOM 2631 C CA . ARG B 1 132 ? 25.651 -26.514 33.704 1.00 76.41 ? 147 ARG B CA 1 ATOM 2632 C C . ARG B 1 132 ? 26.352 -27.030 34.986 1.00 77.58 ? 147 ARG B C 1 ATOM 2633 O O . ARG B 1 132 ? 25.904 -26.773 36.110 1.00 78.02 ? 147 ARG B O 1 ATOM 2634 C CB . ARG B 1 132 ? 24.280 -27.181 33.559 1.00 76.35 ? 147 ARG B CB 1 ATOM 2635 C CG . ARG B 1 132 ? 23.155 -26.586 34.370 1.00 77.73 ? 147 ARG B CG 1 ATOM 2636 C CD . ARG B 1 132 ? 22.141 -25.813 33.539 1.00 79.51 ? 147 ARG B CD 1 ATOM 2637 N NE . ARG B 1 132 ? 22.542 -24.423 33.331 1.00 80.86 ? 147 ARG B NE 1 ATOM 2638 C CZ . ARG B 1 132 ? 21.694 -23.434 33.064 1.00 81.85 ? 147 ARG B CZ 1 ATOM 2639 N NH1 . ARG B 1 132 ? 20.391 -23.677 32.962 1.00 81.13 ? 147 ARG B NH1 1 ATOM 2640 N NH2 . ARG B 1 132 ? 22.151 -22.197 32.896 1.00 83.15 ? 147 ARG B NH2 1 ATOM 2641 N N . ASN B 1 133 ? 27.426 -27.800 34.789 1.00 78.88 ? 148 ASN B N 1 ATOM 2642 C CA . ASN B 1 133 ? 28.275 -28.330 35.866 1.00 79.99 ? 148 ASN B CA 1 ATOM 2643 C C . ASN B 1 133 ? 29.639 -27.794 35.514 1.00 80.46 ? 148 ASN B C 1 ATOM 2644 O O . ASN B 1 133 ? 30.423 -28.432 34.795 1.00 80.56 ? 148 ASN B O 1 ATOM 2645 C CB . ASN B 1 133 ? 28.258 -29.852 35.891 1.00 80.09 ? 148 ASN B CB 1 ATOM 2646 C CG . ASN B 1 133 ? 26.868 -30.399 35.705 1.00 80.07 ? 148 ASN B CG 1 ATOM 2647 O OD1 . ASN B 1 133 ? 26.081 -30.477 36.655 1.00 80.85 ? 148 ASN B OD1 1 ATOM 2648 N ND2 . ASN B 1 133 ? 26.533 -30.731 34.465 1.00 79.49 ? 148 ASN B ND2 1 ATOM 2649 N N . ARG B 1 134 ? 29.869 -26.606 36.065 1.00 80.95 ? 149 ARG B N 1 ATOM 2650 C CA . ARG B 1 134 ? 30.916 -25.635 35.722 1.00 81.26 ? 149 ARG B CA 1 ATOM 2651 C C . ARG B 1 134 ? 30.338 -24.734 34.639 1.00 80.41 ? 149 ARG B C 1 ATOM 2652 O O . ARG B 1 134 ? 29.573 -25.169 33.775 1.00 80.25 ? 149 ARG B O 1 ATOM 2653 C CB . ARG B 1 134 ? 32.329 -26.175 35.401 1.00 81.85 ? 149 ARG B CB 1 ATOM 2654 C CG . ARG B 1 134 ? 32.468 -27.414 34.555 1.00 83.74 ? 149 ARG B CG 1 ATOM 2655 C CD . ARG B 1 134 ? 33.724 -28.195 34.908 1.00 87.53 ? 149 ARG B CD 1 ATOM 2656 N NE . ARG B 1 134 ? 33.500 -29.149 35.995 1.00 89.86 ? 149 ARG B NE 1 ATOM 2657 C CZ . ARG B 1 134 ? 34.353 -30.108 36.320 1.00 92.05 ? 149 ARG B CZ 1 ATOM 2658 N NH1 . ARG B 1 134 ? 35.500 -30.233 35.650 1.00 92.56 ? 149 ARG B NH1 1 ATOM 2659 N NH2 . ARG B 1 134 ? 34.061 -30.944 37.312 1.00 94.15 ? 149 ARG B NH2 1 ATOM 2660 N N . GLY B 1 135 ? 30.665 -23.461 34.738 1.00 79.84 ? 150 GLY B N 1 ATOM 2661 C CA . GLY B 1 135 ? 30.101 -22.490 33.844 1.00 78.81 ? 150 GLY B CA 1 ATOM 2662 C C . GLY B 1 135 ? 30.800 -22.437 32.514 1.00 78.20 ? 150 GLY B C 1 ATOM 2663 O O . GLY B 1 135 ? 31.098 -23.466 31.871 1.00 78.23 ? 150 GLY B O 1 ATOM 2664 N N . ILE B 1 136 ? 31.070 -21.202 32.114 1.00 77.07 ? 151 ILE B N 1 ATOM 2665 C CA . ILE B 1 136 ? 31.626 -20.928 30.808 1.00 75.67 ? 151 ILE B CA 1 ATOM 2666 C C . ILE B 1 136 ? 33.037 -21.484 30.589 1.00 74.41 ? 151 ILE B C 1 ATOM 2667 O O . ILE B 1 136 ? 33.778 -21.831 31.530 1.00 73.74 ? 151 ILE B O 1 ATOM 2668 C CB . ILE B 1 136 ? 31.491 -19.400 30.450 1.00 76.33 ? 151 ILE B CB 1 ATOM 2669 C CG1 . ILE B 1 136 ? 30.217 -19.142 29.625 1.00 75.35 ? 151 ILE B CG1 1 ATOM 2670 C CG2 . ILE B 1 136 ? 32.734 -18.874 29.706 1.00 76.51 ? 151 ILE B CG2 1 ATOM 2671 C CD1 . ILE B 1 136 ? 29.916 -17.678 29.377 1.00 75.95 ? 151 ILE B CD1 1 ATOM 2672 N N . ALA B 1 137 ? 33.347 -21.584 29.302 1.00 72.51 ? 152 ALA B N 1 ATOM 2673 C CA . ALA B 1 137 ? 34.608 -22.068 28.802 1.00 70.32 ? 152 ALA B CA 1 ATOM 2674 C C . ALA B 1 137 ? 35.725 -21.062 29.035 1.00 69.08 ? 152 ALA B C 1 ATOM 2675 O O . ALA B 1 137 ? 35.541 -19.850 28.905 1.00 69.19 ? 152 ALA B O 1 ATOM 2676 C CB . ALA B 1 137 ? 34.475 -22.318 27.324 1.00 70.38 ? 152 ALA B CB 1 ATOM 2677 N N . SER B 1 138 ? 36.901 -21.564 29.373 1.00 66.98 ? 153 SER B N 1 ATOM 2678 C CA . SER B 1 138 ? 38.078 -20.706 29.433 1.00 64.85 ? 153 SER B CA 1 ATOM 2679 C C . SER B 1 138 ? 38.696 -20.755 28.038 1.00 62.46 ? 153 SER B C 1 ATOM 2680 O O . SER B 1 138 ? 38.837 -19.731 27.379 1.00 61.87 ? 153 SER B O 1 ATOM 2681 C CB . SER B 1 138 ? 39.042 -21.191 30.512 1.00 65.09 ? 153 SER B CB 1 ATOM 2682 O OG . SER B 1 138 ? 38.915 -22.585 30.734 1.00 67.40 ? 153 SER B OG 1 ATOM 2683 N N . VAL B 1 139 ? 38.982 -21.972 27.579 1.00 59.56 ? 154 VAL B N 1 ATOM 2684 C CA . VAL B 1 139 ? 39.559 -22.238 26.262 1.00 56.74 ? 154 VAL B CA 1 ATOM 2685 C C . VAL B 1 139 ? 38.498 -22.494 25.175 1.00 54.52 ? 154 VAL B C 1 ATOM 2686 O O . VAL B 1 139 ? 37.514 -23.204 25.411 1.00 53.74 ? 154 VAL B O 1 ATOM 2687 C CB . VAL B 1 139 ? 40.399 -23.554 26.304 1.00 57.46 ? 154 VAL B CB 1 ATOM 2688 C CG1 . VAL B 1 139 ? 40.854 -23.959 24.895 1.00 58.35 ? 154 VAL B CG1 1 ATOM 2689 C CG2 . VAL B 1 139 ? 41.577 -23.426 27.234 1.00 57.41 ? 154 VAL B CG2 1 ATOM 2690 N N . LEU B 1 140 ? 38.710 -21.943 23.984 1.00 51.12 ? 155 LEU B N 1 ATOM 2691 C CA . LEU B 1 140 ? 37.796 -22.165 22.868 1.00 49.35 ? 155 LEU B CA 1 ATOM 2692 C C . LEU B 1 140 ? 37.597 -23.671 22.622 1.00 48.49 ? 155 LEU B C 1 ATOM 2693 O O . LEU B 1 140 ? 38.556 -24.417 22.587 1.00 48.55 ? 155 LEU B O 1 ATOM 2694 C CB . LEU B 1 140 ? 38.309 -21.495 21.585 1.00 47.79 ? 155 LEU B CB 1 ATOM 2695 C CG . LEU B 1 140 ? 37.437 -21.724 20.341 1.00 46.81 ? 155 LEU B CG 1 ATOM 2696 C CD1 . LEU B 1 140 ? 36.130 -20.946 20.382 1.00 45.49 ? 155 LEU B CD1 1 ATOM 2697 C CD2 . LEU B 1 140 ? 38.184 -21.411 19.068 1.00 43.06 ? 155 LEU B CD2 1 ATOM 2698 N N . GLN B 1 141 ? 36.353 -24.101 22.489 1.00 47.58 ? 156 GLN B N 1 ATOM 2699 C CA . GLN B 1 141 ? 36.028 -25.499 22.228 1.00 47.09 ? 156 GLN B CA 1 ATOM 2700 C C . GLN B 1 141 ? 35.538 -25.691 20.799 1.00 46.36 ? 156 GLN B C 1 ATOM 2701 O O . GLN B 1 141 ? 35.114 -24.719 20.134 1.00 44.97 ? 156 GLN B O 1 ATOM 2702 C CB . GLN B 1 141 ? 34.927 -25.931 23.182 1.00 47.53 ? 156 GLN B CB 1 ATOM 2703 C CG . GLN B 1 141 ? 35.253 -25.652 24.622 1.00 47.14 ? 156 GLN B CG 1 ATOM 2704 C CD . GLN B 1 141 ? 36.273 -26.618 25.181 1.00 49.05 ? 156 GLN B CD 1 ATOM 2705 O OE1 . GLN B 1 141 ? 37.378 -26.219 25.583 1.00 46.87 ? 156 GLN B OE1 1 ATOM 2706 N NE2 . GLN B 1 141 ? 35.911 -27.887 25.221 1.00 47.76 ? 156 GLN B NE2 1 ATOM 2707 N N . GLU B 1 142 ? 35.609 -26.939 20.321 1.00 45.68 ? 157 GLU B N 1 ATOM 2708 C CA . GLU B 1 142 ? 35.107 -27.314 19.003 1.00 46.05 ? 157 GLU B CA 1 ATOM 2709 C C . GLU B 1 142 ? 34.366 -28.642 19.032 1.00 45.63 ? 157 GLU B C 1 ATOM 2710 O O . GLU B 1 142 ? 34.574 -29.453 19.912 1.00 45.89 ? 157 GLU B O 1 ATOM 2711 C CB . GLU B 1 142 ? 36.231 -27.370 17.973 1.00 47.22 ? 157 GLU B CB 1 ATOM 2712 C CG . GLU B 1 142 ? 37.471 -28.129 18.466 1.00 50.74 ? 157 GLU B CG 1 ATOM 2713 C CD . GLU B 1 142 ? 38.533 -28.240 17.403 1.00 52.77 ? 157 GLU B CD 1 ATOM 2714 O OE1 . GLU B 1 142 ? 39.274 -27.265 17.197 1.00 55.21 ? 157 GLU B OE1 1 ATOM 2715 O OE2 . GLU B 1 142 ? 38.617 -29.299 16.764 1.00 56.54 ? 157 GLU B OE2 1 ATOM 2716 N N . LEU B 1 143 ? 33.520 -28.878 18.043 1.00 44.47 ? 158 LEU B N 1 ATOM 2717 C CA . LEU B 1 143 ? 32.661 -30.038 18.087 1.00 44.32 ? 158 LEU B CA 1 ATOM 2718 C C . LEU B 1 143 ? 32.342 -30.507 16.711 1.00 43.27 ? 158 LEU B C 1 ATOM 2719 O O . LEU B 1 143 ? 31.877 -29.718 15.909 1.00 43.25 ? 158 LEU B O 1 ATOM 2720 C CB . LEU B 1 143 ? 31.349 -29.650 18.738 1.00 43.74 ? 158 LEU B CB 1 ATOM 2721 C CG . LEU B 1 143 ? 30.399 -30.799 18.972 1.00 44.28 ? 158 LEU B CG 1 ATOM 2722 C CD1 . LEU B 1 143 ? 31.154 -31.832 19.826 1.00 47.29 ? 158 LEU B CD1 1 ATOM 2723 C CD2 . LEU B 1 143 ? 29.141 -30.317 19.666 1.00 38.32 ? 158 LEU B CD2 1 ATOM 2724 N N . ASN B 1 144 ? 32.585 -31.782 16.422 1.00 43.24 ? 159 ASN B N 1 ATOM 2725 C CA . ASN B 1 144 ? 32.232 -32.323 15.103 1.00 41.95 ? 159 ASN B CA 1 ATOM 2726 C C . ASN B 1 144 ? 30.738 -32.527 15.101 1.00 39.47 ? 159 ASN B C 1 ATOM 2727 O O . ASN B 1 144 ? 30.223 -32.997 16.057 1.00 39.98 ? 159 ASN B O 1 ATOM 2728 C CB . ASN B 1 144 ? 32.953 -33.672 14.819 1.00 43.85 ? 159 ASN B CB 1 ATOM 2729 C CG . ASN B 1 144 ? 34.491 -33.535 14.672 1.00 48.65 ? 159 ASN B CG 1 ATOM 2730 O OD1 . ASN B 1 144 ? 35.195 -33.321 15.649 1.00 52.76 ? 159 ASN B OD1 1 ATOM 2731 N ND2 . ASN B 1 144 ? 34.998 -33.741 13.441 1.00 56.72 ? 159 ASN B ND2 1 ATOM 2732 N N . VAL B 1 145 ? 30.016 -32.154 14.064 1.00 38.31 ? 160 VAL B N 1 ATOM 2733 C CA . VAL B 1 145 ? 28.593 -32.406 14.090 1.00 39.09 ? 160 VAL B CA 1 ATOM 2734 C C . VAL B 1 145 ? 28.255 -32.750 12.700 1.00 38.35 ? 160 VAL B C 1 ATOM 2735 O O . VAL B 1 145 ? 29.112 -32.682 11.837 1.00 40.96 ? 160 VAL B O 1 ATOM 2736 C CB . VAL B 1 145 ? 27.743 -31.165 14.543 1.00 39.61 ? 160 VAL B CB 1 ATOM 2737 C CG1 . VAL B 1 145 ? 28.229 -30.644 15.884 1.00 38.14 ? 160 VAL B CG1 1 ATOM 2738 C CG2 . VAL B 1 145 ? 27.845 -30.078 13.520 1.00 39.86 ? 160 VAL B CG2 1 ATOM 2739 N N . THR B 1 146 ? 26.995 -33.043 12.451 1.00 38.31 ? 162 THR B N 1 ATOM 2740 C CA . THR B 1 146 ? 26.560 -33.414 11.156 1.00 37.82 ? 162 THR B CA 1 ATOM 2741 C C . THR B 1 146 ? 25.338 -32.639 10.785 1.00 38.42 ? 162 THR B C 1 ATOM 2742 O O . THR B 1 146 ? 24.435 -32.505 11.602 1.00 37.93 ? 162 THR B O 1 ATOM 2743 C CB . THR B 1 146 ? 26.121 -34.917 11.172 1.00 38.05 ? 162 THR B CB 1 ATOM 2744 O OG1 . THR B 1 146 ? 27.237 -35.736 11.543 1.00 37.19 ? 162 THR B OG1 1 ATOM 2745 C CG2 . THR B 1 146 ? 25.735 -35.313 9.746 1.00 38.53 ? 162 THR B CG2 1 ATOM 2746 N N . VAL B 1 147 ? 25.300 -32.148 9.545 1.00 38.28 ? 163 VAL B N 1 ATOM 2747 C CA . VAL B 1 147 ? 24.144 -31.403 9.045 1.00 38.78 ? 163 VAL B CA 1 ATOM 2748 C C . VAL B 1 147 ? 22.998 -32.305 8.983 1.00 38.76 ? 163 VAL B C 1 ATOM 2749 O O . VAL B 1 147 ? 23.136 -33.430 8.490 1.00 41.02 ? 163 VAL B O 1 ATOM 2750 C CB . VAL B 1 147 ? 24.385 -30.860 7.606 1.00 38.97 ? 163 VAL B CB 1 ATOM 2751 C CG1 . VAL B 1 147 ? 23.082 -30.293 6.974 1.00 37.59 ? 163 VAL B CG1 1 ATOM 2752 C CG2 . VAL B 1 147 ? 25.443 -29.831 7.602 1.00 38.64 ? 163 VAL B CG2 1 ATOM 2753 N N . VAL B 1 148 ? 21.845 -31.837 9.420 1.00 38.62 ? 164 VAL B N 1 ATOM 2754 C CA . VAL B 1 148 ? 20.651 -32.642 9.417 1.00 39.30 ? 164 VAL B CA 1 ATOM 2755 C C . VAL B 1 148 ? 19.433 -31.885 8.950 1.00 39.41 ? 164 VAL B C 1 ATOM 2756 O O . VAL B 1 148 ? 19.345 -30.650 9.149 1.00 40.23 ? 164 VAL B O 1 ATOM 2757 C CB . VAL B 1 148 ? 20.399 -33.103 10.857 1.00 41.51 ? 164 VAL B CB 1 ATOM 2758 C CG1 . VAL B 1 148 ? 18.926 -33.072 11.185 1.00 40.65 ? 164 VAL B CG1 1 ATOM 2759 C CG2 . VAL B 1 148 ? 21.071 -34.443 11.095 1.00 40.46 ? 164 VAL B CG2 1 ATOM 2760 N N . THR B 1 149 ? 18.461 -32.584 8.370 1.00 38.11 ? 165 THR B N 1 ATOM 2761 C CA . THR B 1 149 ? 17.235 -31.928 7.944 1.00 38.52 ? 165 THR B CA 1 ATOM 2762 C C . THR B 1 149 ? 16.061 -32.277 8.803 1.00 39.68 ? 165 THR B C 1 ATOM 2763 O O . THR B 1 149 ? 15.072 -31.533 8.844 1.00 40.41 ? 165 THR B O 1 ATOM 2764 C CB . THR B 1 149 ? 16.823 -32.244 6.456 1.00 39.75 ? 165 THR B CB 1 ATOM 2765 O OG1 . THR B 1 149 ? 17.290 -33.551 6.072 1.00 41.66 ? 165 THR B OG1 1 ATOM 2766 C CG2 . THR B 1 149 ? 17.478 -31.288 5.480 1.00 36.28 ? 165 THR B CG2 1 ATOM 2767 N N . SER B 1 150 ? 16.113 -33.431 9.471 1.00 39.59 ? 166 SER B N 1 ATOM 2768 C CA . SER B 1 150 ? 14.945 -33.818 10.260 1.00 40.08 ? 166 SER B CA 1 ATOM 2769 C C . SER B 1 150 ? 14.751 -32.780 11.399 1.00 38.81 ? 166 SER B C 1 ATOM 2770 O O . SER B 1 150 ? 15.718 -32.423 12.029 1.00 37.95 ? 166 SER B O 1 ATOM 2771 C CB . SER B 1 150 ? 15.142 -35.224 10.845 1.00 39.46 ? 166 SER B CB 1 ATOM 2772 O OG . SER B 1 150 ? 15.818 -36.088 9.923 1.00 43.02 ? 166 SER B OG 1 ATOM 2773 N N . LEU B 1 151 ? 13.507 -32.387 11.663 1.00 38.88 ? 167 LEU B N 1 ATOM 2774 C CA . LEU B 1 151 ? 13.163 -31.485 12.751 1.00 39.90 ? 167 LEU B CA 1 ATOM 2775 C C . LEU B 1 151 ? 13.885 -30.107 12.558 1.00 40.49 ? 167 LEU B C 1 ATOM 2776 O O . LEU B 1 151 ? 14.447 -29.553 13.490 1.00 39.71 ? 167 LEU B O 1 ATOM 2777 C CB . LEU B 1 151 ? 13.506 -32.119 14.131 1.00 39.26 ? 167 LEU B CB 1 ATOM 2778 C CG . LEU B 1 151 ? 12.789 -33.445 14.547 1.00 38.01 ? 167 LEU B CG 1 ATOM 2779 C CD1 . LEU B 1 151 ? 13.197 -33.983 15.940 1.00 34.50 ? 167 LEU B CD1 1 ATOM 2780 C CD2 . LEU B 1 151 ? 11.269 -33.357 14.428 1.00 36.83 ? 167 LEU B CD2 1 ATOM 2781 N N . CYS B 1 152 ? 13.914 -29.620 11.320 1.00 40.56 ? 168 CYS B N 1 ATOM 2782 C CA . CYS B 1 152 ? 14.596 -28.370 11.010 1.00 40.59 ? 168 CYS B CA 1 ATOM 2783 C C . CYS B 1 152 ? 13.755 -27.543 10.074 1.00 40.58 ? 168 CYS B C 1 ATOM 2784 O O . CYS B 1 152 ? 13.200 -28.075 9.120 1.00 39.55 ? 168 CYS B O 1 ATOM 2785 C CB . CYS B 1 152 ? 15.924 -28.658 10.340 1.00 40.17 ? 168 CYS B CB 1 ATOM 2786 S SG . CYS B 1 152 ? 17.045 -27.226 10.327 1.00 37.49 ? 168 CYS B SG 1 ATOM 2787 N N . ARG B 1 153 ? 13.626 -26.236 10.328 1.00 40.37 ? 177 ARG B N 1 ATOM 2788 C CA . ARG B 1 153 ? 12.864 -25.402 9.390 1.00 40.34 ? 177 ARG B CA 1 ATOM 2789 C C . ARG B 1 153 ? 13.684 -25.319 8.092 1.00 38.59 ? 177 ARG B C 1 ATOM 2790 O O . ARG B 1 153 ? 14.869 -25.483 8.136 1.00 36.95 ? 177 ARG B O 1 ATOM 2791 C CB . ARG B 1 153 ? 12.576 -23.989 10.007 1.00 40.74 ? 177 ARG B CB 1 ATOM 2792 C CG . ARG B 1 153 ? 12.387 -24.069 11.545 1.00 45.44 ? 177 ARG B CG 1 ATOM 2793 C CD . ARG B 1 153 ? 11.523 -23.011 12.291 1.00 50.76 ? 177 ARG B CD 1 ATOM 2794 N NE . ARG B 1 153 ? 12.171 -21.716 12.438 1.00 51.58 ? 177 ARG B NE 1 ATOM 2795 C CZ . ARG B 1 153 ? 12.138 -20.926 13.530 1.00 50.03 ? 177 ARG B CZ 1 ATOM 2796 N NH1 . ARG B 1 153 ? 11.526 -21.286 14.648 1.00 48.00 ? 177 ARG B NH1 1 ATOM 2797 N NH2 . ARG B 1 153 ? 12.740 -19.748 13.482 1.00 46.65 ? 177 ARG B NH2 1 ATOM 2798 N N . ARG B 1 154 ? 13.061 -25.103 6.928 1.00 39.26 ? 178 ARG B N 1 ATOM 2799 C CA . ARG B 1 154 ? 13.841 -24.883 5.703 1.00 40.32 ? 178 ARG B CA 1 ATOM 2800 C C . ARG B 1 154 ? 14.685 -23.570 5.827 1.00 39.95 ? 178 ARG B C 1 ATOM 2801 O O . ARG B 1 154 ? 15.771 -23.435 5.221 1.00 40.00 ? 178 ARG B O 1 ATOM 2802 C CB . ARG B 1 154 ? 12.921 -24.814 4.497 1.00 41.44 ? 178 ARG B CB 1 ATOM 2803 C CG . ARG B 1 154 ? 11.594 -25.507 4.738 1.00 47.69 ? 178 ARG B CG 1 ATOM 2804 C CD . ARG B 1 154 ? 10.586 -25.429 3.597 1.00 55.99 ? 178 ARG B CD 1 ATOM 2805 N NE . ARG B 1 154 ? 9.271 -25.833 4.114 1.00 62.90 ? 178 ARG B NE 1 ATOM 2806 C CZ . ARG B 1 154 ? 8.406 -25.003 4.689 1.00 65.39 ? 178 ARG B CZ 1 ATOM 2807 N NH1 . ARG B 1 154 ? 7.246 -25.461 5.149 1.00 68.26 ? 178 ARG B NH1 1 ATOM 2808 N NH2 . ARG B 1 154 ? 8.697 -23.708 4.802 1.00 67.49 ? 178 ARG B NH2 1 ATOM 2809 N N . SER B 1 155 ? 14.229 -22.679 6.722 1.00 38.20 ? 179 SER B N 1 ATOM 2810 C CA . SER B 1 155 ? 14.924 -21.416 7.025 1.00 38.03 ? 179 SER B CA 1 ATOM 2811 C C . SER B 1 155 ? 16.117 -21.481 7.983 1.00 37.50 ? 179 SER B C 1 ATOM 2812 O O . SER B 1 155 ? 16.557 -20.423 8.468 1.00 36.06 ? 179 SER B O 1 ATOM 2813 C CB . SER B 1 155 ? 13.940 -20.440 7.628 1.00 37.00 ? 179 SER B CB 1 ATOM 2814 O OG . SER B 1 155 ? 13.468 -20.955 8.873 1.00 37.71 ? 179 SER B OG 1 ATOM 2815 N N . ASN B 1 156 ? 16.576 -22.694 8.331 1.00 35.70 ? 180 ASN B N 1 ATOM 2816 C CA . ASN B 1 156 ? 17.751 -22.925 9.175 1.00 33.61 ? 180 ASN B CA 1 ATOM 2817 C C . ASN B 1 156 ? 18.664 -23.972 8.592 1.00 35.11 ? 180 ASN B C 1 ATOM 2818 O O . ASN B 1 156 ? 18.269 -24.795 7.762 1.00 34.10 ? 180 ASN B O 1 ATOM 2819 C CB . ASN B 1 156 ? 17.362 -23.490 10.569 1.00 35.16 ? 180 ASN B CB 1 ATOM 2820 C CG . ASN B 1 156 ? 16.874 -22.408 11.554 1.00 31.55 ? 180 ASN B CG 1 ATOM 2821 O OD1 . ASN B 1 156 ? 15.695 -22.350 11.918 1.00 30.68 ? 180 ASN B OD1 1 ATOM 2822 N ND2 . ASN B 1 156 ? 17.792 -21.556 11.970 1.00 33.51 ? 180 ASN B ND2 1 ATOM 2823 N N . VAL B 1 157 ? 19.908 -23.964 9.043 1.00 35.85 ? 181 VAL B N 1 ATOM 2824 C CA . VAL B 1 157 ? 20.792 -25.056 8.765 1.00 36.29 ? 181 VAL B CA 1 ATOM 2825 C C . VAL B 1 157 ? 20.855 -25.635 10.173 1.00 36.71 ? 181 VAL B C 1 ATOM 2826 O O . VAL B 1 157 ? 21.041 -24.881 11.150 1.00 33.64 ? 181 VAL B O 1 ATOM 2827 C CB . VAL B 1 157 ? 22.185 -24.636 8.389 1.00 34.94 ? 181 VAL B CB 1 ATOM 2828 C CG1 . VAL B 1 157 ? 23.127 -25.727 8.659 1.00 40.43 ? 181 VAL B CG1 1 ATOM 2829 C CG2 . VAL B 1 157 ? 22.299 -24.259 6.897 1.00 37.86 ? 181 VAL B CG2 1 ATOM 2830 N N . CYS B 1 158 ? 20.648 -26.947 10.287 1.00 36.97 ? 182 CYS B N 1 ATOM 2831 C CA . CYS B 1 158 ? 20.729 -27.588 11.613 1.00 37.52 ? 182 CYS B CA 1 ATOM 2832 C C . CYS B 1 158 ? 21.774 -28.703 11.710 1.00 38.15 ? 182 CYS B C 1 ATOM 2833 O O . CYS B 1 158 ? 22.198 -29.332 10.697 1.00 37.11 ? 182 CYS B O 1 ATOM 2834 C CB . CYS B 1 158 ? 19.394 -28.118 12.074 1.00 37.18 ? 182 CYS B CB 1 ATOM 2835 S SG . CYS B 1 158 ? 17.902 -27.124 12.169 1.00 35.15 ? 182 CYS B SG 1 ATOM 2836 N N . THR B 1 159 ? 22.222 -28.943 12.931 1.00 38.16 ? 183 THR B N 1 ATOM 2837 C CA . THR B 1 159 ? 23.204 -29.981 13.147 1.00 38.94 ? 183 THR B CA 1 ATOM 2838 C C . THR B 1 159 ? 22.804 -30.954 14.262 1.00 40.53 ? 183 THR B C 1 ATOM 2839 O O . THR B 1 159 ? 21.789 -30.763 14.938 1.00 39.81 ? 183 THR B O 1 ATOM 2840 C CB . THR B 1 159 ? 24.564 -29.388 13.421 1.00 38.18 ? 183 THR B CB 1 ATOM 2841 O OG1 . THR B 1 159 ? 24.547 -28.638 14.650 1.00 38.39 ? 183 THR B OG1 1 ATOM 2842 C CG2 . THR B 1 159 ? 24.884 -28.382 12.338 1.00 39.23 ? 183 THR B CG2 1 ATOM 2843 N N . LEU B 1 160 ? 23.626 -31.980 14.444 1.00 41.61 ? 184 LEU B N 1 ATOM 2844 C CA . LEU B 1 160 ? 23.347 -32.988 15.460 1.00 42.70 ? 184 LEU B CA 1 ATOM 2845 C C . LEU B 1 160 ? 24.549 -33.865 15.675 1.00 43.91 ? 184 LEU B C 1 ATOM 2846 O O . LEU B 1 160 ? 25.304 -34.223 14.712 1.00 43.83 ? 184 LEU B O 1 ATOM 2847 C CB . LEU B 1 160 ? 22.109 -33.821 15.138 1.00 40.52 ? 184 LEU B CB 1 ATOM 2848 C CG . LEU B 1 160 ? 21.887 -34.766 16.328 1.00 43.27 ? 184 LEU B CG 1 ATOM 2849 C CD1 . LEU B 1 160 ? 20.954 -34.195 17.407 1.00 38.04 ? 184 LEU B CD1 1 ATOM 2850 C CD2 . LEU B 1 160 ? 21.427 -36.211 15.843 1.00 43.24 ? 184 LEU B CD2 1 ATOM 2851 N N . VAL B 1 161 ? 24.797 -34.148 16.951 1.00 44.52 ? 185 VAL B N 1 ATOM 2852 C CA . VAL B 1 161 ? 25.876 -35.030 17.249 1.00 45.46 ? 185 VAL B CA 1 ATOM 2853 C C . VAL B 1 161 ? 25.237 -36.376 17.471 1.00 46.11 ? 185 VAL B C 1 ATOM 2854 O O . VAL B 1 161 ? 24.569 -36.605 18.480 1.00 46.51 ? 185 VAL B O 1 ATOM 2855 C CB . VAL B 1 161 ? 26.630 -34.635 18.453 1.00 45.24 ? 185 VAL B CB 1 ATOM 2856 C CG1 . VAL B 1 161 ? 27.712 -35.690 18.727 1.00 46.34 ? 185 VAL B CG1 1 ATOM 2857 C CG2 . VAL B 1 161 ? 27.212 -33.269 18.267 1.00 47.13 ? 185 VAL B CG2 1 ATOM 2858 N N . ARG B 1 162 ? 25.408 -37.248 16.494 1.00 46.31 ? 186 ARG B N 1 ATOM 2859 C CA . ARG B 1 162 ? 24.843 -38.581 16.582 1.00 46.40 ? 186 ARG B CA 1 ATOM 2860 C C . ARG B 1 162 ? 25.456 -39.435 17.682 1.00 45.65 ? 186 ARG B C 1 ATOM 2861 O O . ARG B 1 162 ? 26.687 -39.524 17.827 1.00 44.82 ? 186 ARG B O 1 ATOM 2862 C CB . ARG B 1 162 ? 25.105 -39.309 15.277 1.00 47.03 ? 186 ARG B CB 1 ATOM 2863 C CG . ARG B 1 162 ? 24.721 -38.548 14.047 1.00 45.81 ? 186 ARG B CG 1 ATOM 2864 C CD . ARG B 1 162 ? 24.158 -39.481 13.022 1.00 42.36 ? 186 ARG B CD 1 ATOM 2865 N NE . ARG B 1 162 ? 23.844 -38.824 11.769 1.00 40.56 ? 186 ARG B NE 1 ATOM 2866 C CZ . ARG B 1 162 ? 22.662 -38.364 11.493 1.00 40.29 ? 186 ARG B CZ 1 ATOM 2867 N NH1 . ARG B 1 162 ? 21.684 -38.485 12.400 1.00 41.28 ? 186 ARG B NH1 1 ATOM 2868 N NH2 . ARG B 1 162 ? 22.457 -37.744 10.342 1.00 39.11 ? 186 ARG B NH2 1 ATOM 2869 N N . GLY B 1 163 A 24.593 -40.093 18.437 1.00 45.39 ? 186 GLY B N 1 ATOM 2870 C CA . GLY B 1 163 A 25.065 -41.102 19.358 1.00 45.38 ? 186 GLY B CA 1 ATOM 2871 C C . GLY B 1 163 A 25.331 -40.669 20.769 1.00 46.14 ? 186 GLY B C 1 ATOM 2872 O O . GLY B 1 163 A 25.467 -41.489 21.657 1.00 46.36 ? 186 GLY B O 1 ATOM 2873 N N . ARG B 1 164 ? 25.478 -39.375 20.986 1.00 46.73 ? 187 ARG B N 1 ATOM 2874 C CA . ARG B 1 164 ? 25.645 -38.944 22.362 1.00 46.04 ? 187 ARG B CA 1 ATOM 2875 C C . ARG B 1 164 ? 24.934 -37.627 22.581 1.00 44.76 ? 187 ARG B C 1 ATOM 2876 O O . ARG B 1 164 ? 24.365 -37.079 21.664 1.00 43.83 ? 187 ARG B O 1 ATOM 2877 C CB . ARG B 1 164 ? 27.124 -38.863 22.766 1.00 47.03 ? 187 ARG B CB 1 ATOM 2878 C CG . ARG B 1 164 ? 28.089 -38.786 21.640 1.00 46.68 ? 187 ARG B CG 1 ATOM 2879 C CD . ARG B 1 164 ? 29.518 -38.586 22.107 1.00 49.50 ? 187 ARG B CD 1 ATOM 2880 N NE . ARG B 1 164 ? 30.112 -37.486 21.355 1.00 52.89 ? 187 ARG B NE 1 ATOM 2881 C CZ . ARG B 1 164 ? 30.631 -36.366 21.882 1.00 51.57 ? 187 ARG B CZ 1 ATOM 2882 N NH1 . ARG B 1 164 ? 30.709 -36.145 23.195 1.00 48.08 ? 187 ARG B NH1 1 ATOM 2883 N NH2 . ARG B 1 164 ? 31.087 -35.462 21.055 1.00 53.69 ? 187 ARG B NH2 1 ATOM 2884 N N . GLN B 1 165 ? 24.949 -37.168 23.819 1.00 43.52 ? 188 GLN B N 1 ATOM 2885 C CA . GLN B 1 165 ? 24.354 -35.896 24.194 1.00 43.19 ? 188 GLN B CA 1 ATOM 2886 C C . GLN B 1 165 ? 25.437 -34.826 24.133 1.00 41.67 ? 188 GLN B C 1 ATOM 2887 O O . GLN B 1 165 ? 26.306 -34.764 24.983 1.00 40.77 ? 188 GLN B O 1 ATOM 2888 C CB . GLN B 1 165 ? 23.800 -36.002 25.613 1.00 43.36 ? 188 GLN B CB 1 ATOM 2889 C CG . GLN B 1 165 ? 22.434 -36.514 25.629 1.00 45.03 ? 188 GLN B CG 1 ATOM 2890 C CD . GLN B 1 165 ? 21.874 -36.659 27.025 1.00 52.70 ? 188 GLN B CD 1 ATOM 2891 O OE1 . GLN B 1 165 ? 20.665 -36.655 27.198 1.00 56.48 ? 188 GLN B OE1 1 ATOM 2892 N NE2 . GLN B 1 165 ? 22.741 -36.770 28.018 1.00 55.55 ? 188 GLN B NE2 1 ATOM 2893 N N . ALA B 1 166 A 25.389 -33.996 23.107 1.00 40.91 ? 188 ALA B N 1 ATOM 2894 C CA . ALA B 1 166 A 26.386 -32.972 22.937 1.00 39.43 ? 188 ALA B CA 1 ATOM 2895 C C . ALA B 1 166 A 25.889 -31.968 21.904 1.00 39.06 ? 188 ALA B C 1 ATOM 2896 O O . ALA B 1 166 A 25.019 -32.286 21.070 1.00 37.85 ? 188 ALA B O 1 ATOM 2897 C CB . ALA B 1 166 A 27.694 -33.576 22.520 1.00 40.05 ? 188 ALA B CB 1 ATOM 2898 N N . GLY B 1 167 ? 26.440 -30.749 21.962 1.00 37.62 ? 189 GLY B N 1 ATOM 2899 C CA . GLY B 1 167 ? 25.969 -29.681 21.068 1.00 35.92 ? 189 GLY B CA 1 ATOM 2900 C C . GLY B 1 167 ? 26.313 -28.303 21.618 1.00 35.33 ? 189 GLY B C 1 ATOM 2901 O O . GLY B 1 167 ? 27.118 -28.179 22.569 1.00 35.63 ? 189 GLY B O 1 ATOM 2902 N N . VAL B 1 168 ? 25.756 -27.272 20.996 1.00 34.05 ? 190 VAL B N 1 ATOM 2903 C CA . VAL B 1 168 ? 26.048 -25.890 21.412 1.00 33.44 ? 190 VAL B CA 1 ATOM 2904 C C . VAL B 1 168 ? 25.275 -25.490 22.672 1.00 33.91 ? 190 VAL B C 1 ATOM 2905 O O . VAL B 1 168 ? 24.146 -25.991 22.908 1.00 34.53 ? 190 VAL B O 1 ATOM 2906 C CB . VAL B 1 168 ? 25.704 -24.937 20.285 1.00 32.65 ? 190 VAL B CB 1 ATOM 2907 C CG1 . VAL B 1 168 ? 26.447 -25.320 19.061 1.00 32.54 ? 190 VAL B CG1 1 ATOM 2908 C CG2 . VAL B 1 168 ? 24.178 -24.968 20.008 1.00 31.06 ? 190 VAL B CG2 1 ATOM 2909 N N . CYS B 1 169 ? 25.853 -24.596 23.486 1.00 33.63 ? 191 CYS B N 1 ATOM 2910 C CA . CYS B 1 169 ? 25.122 -24.139 24.662 1.00 33.73 ? 191 CYS B CA 1 ATOM 2911 C C . CYS B 1 169 ? 25.141 -22.590 24.889 1.00 34.94 ? 191 CYS B C 1 ATOM 2912 O O . CYS B 1 169 ? 25.724 -21.851 24.061 1.00 33.29 ? 191 CYS B O 1 ATOM 2913 C CB . CYS B 1 169 ? 25.580 -24.928 25.893 1.00 33.19 ? 191 CYS B CB 1 ATOM 2914 S SG . CYS B 1 169 ? 24.307 -25.078 27.153 1.00 34.46 ? 191 CYS B SG 1 ATOM 2915 N N . PHE B 1 170 ? 24.489 -22.106 25.961 1.00 35.01 ? 192 PHE B N 1 ATOM 2916 C CA . PHE B 1 170 ? 24.442 -20.632 26.198 1.00 35.98 ? 192 PHE B CA 1 ATOM 2917 C C . PHE B 1 170 ? 25.858 -20.023 26.111 1.00 35.42 ? 192 PHE B C 1 ATOM 2918 O O . PHE B 1 170 ? 26.773 -20.460 26.785 1.00 33.95 ? 192 PHE B O 1 ATOM 2919 C CB . PHE B 1 170 ? 23.880 -20.258 27.575 1.00 37.33 ? 192 PHE B CB 1 ATOM 2920 C CG . PHE B 1 170 ? 22.598 -21.020 27.979 1.00 41.12 ? 192 PHE B CG 1 ATOM 2921 C CD1 . PHE B 1 170 ? 21.484 -21.090 27.157 1.00 46.75 ? 192 PHE B CD1 1 ATOM 2922 C CD2 . PHE B 1 170 ? 22.519 -21.609 29.221 1.00 46.89 ? 192 PHE B CD2 1 ATOM 2923 C CE1 . PHE B 1 170 ? 20.322 -21.791 27.573 1.00 48.90 ? 192 PHE B CE1 1 ATOM 2924 C CE2 . PHE B 1 170 ? 21.405 -22.251 29.640 1.00 49.52 ? 192 PHE B CE2 1 ATOM 2925 C CZ . PHE B 1 170 ? 20.304 -22.354 28.822 1.00 49.51 ? 192 PHE B CZ 1 ATOM 2926 N N . GLY B 1 171 ? 26.040 -19.017 25.271 1.00 35.05 ? 193 GLY B N 1 ATOM 2927 C CA . GLY B 1 171 ? 27.349 -18.430 25.169 1.00 33.97 ? 193 GLY B CA 1 ATOM 2928 C C . GLY B 1 171 ? 27.927 -18.803 23.832 1.00 34.67 ? 193 GLY B C 1 ATOM 2929 O O . GLY B 1 171 ? 28.899 -18.207 23.421 1.00 36.54 ? 193 GLY B O 1 ATOM 2930 N N . ASP B 1 172 ? 27.316 -19.732 23.112 1.00 34.01 ? 194 ASP B N 1 ATOM 2931 C CA . ASP B 1 172 ? 27.818 -20.087 21.777 1.00 33.29 ? 194 ASP B CA 1 ATOM 2932 C C . ASP B 1 172 ? 26.994 -19.393 20.701 1.00 33.21 ? 194 ASP B C 1 ATOM 2933 O O . ASP B 1 172 ? 27.422 -19.310 19.541 1.00 34.00 ? 194 ASP B O 1 ATOM 2934 C CB . ASP B 1 172 ? 27.794 -21.615 21.522 1.00 34.17 ? 194 ASP B CB 1 ATOM 2935 C CG . ASP B 1 172 ? 28.728 -22.366 22.399 1.00 32.46 ? 194 ASP B CG 1 ATOM 2936 O OD1 . ASP B 1 172 ? 29.911 -21.953 22.547 1.00 36.51 ? 194 ASP B OD1 1 ATOM 2937 O OD2 . ASP B 1 172 ? 28.381 -23.397 23.026 1.00 33.83 ? 194 ASP B OD2 1 ATOM 2938 N N . SER B 1 173 ? 25.800 -18.928 21.031 1.00 31.11 ? 195 SER B N 1 ATOM 2939 C CA . SER B 1 173 ? 25.036 -18.149 20.065 1.00 32.63 ? 195 SER B CA 1 ATOM 2940 C C . SER B 1 173 ? 25.955 -17.089 19.391 1.00 31.89 ? 195 SER B C 1 ATOM 2941 O O . SER B 1 173 ? 26.823 -16.551 20.048 1.00 31.61 ? 195 SER B O 1 ATOM 2942 C CB . SER B 1 173 ? 23.910 -17.381 20.772 1.00 32.68 ? 195 SER B CB 1 ATOM 2943 O OG . SER B 1 173 ? 22.826 -18.225 21.056 1.00 33.20 ? 195 SER B OG 1 ATOM 2944 N N . GLY B 1 174 ? 25.727 -16.829 18.105 1.00 33.02 ? 196 GLY B N 1 ATOM 2945 C CA . GLY B 1 174 ? 26.526 -15.950 17.258 1.00 31.98 ? 196 GLY B CA 1 ATOM 2946 C C . GLY B 1 174 ? 27.805 -16.593 16.691 1.00 33.47 ? 196 GLY B C 1 ATOM 2947 O O . GLY B 1 174 ? 28.466 -16.018 15.810 1.00 31.44 ? 196 GLY B O 1 ATOM 2948 N N . SER B 1 175 ? 28.154 -17.787 17.172 1.00 33.15 ? 197 SER B N 1 ATOM 2949 C CA . SER B 1 175 ? 29.393 -18.446 16.739 1.00 33.24 ? 197 SER B CA 1 ATOM 2950 C C . SER B 1 175 ? 29.183 -19.066 15.351 1.00 32.55 ? 197 SER B C 1 ATOM 2951 O O . SER B 1 175 ? 28.060 -19.406 14.999 1.00 34.64 ? 197 SER B O 1 ATOM 2952 C CB . SER B 1 175 ? 29.851 -19.490 17.750 1.00 34.12 ? 197 SER B CB 1 ATOM 2953 O OG . SER B 1 175 ? 29.836 -19.031 19.108 1.00 36.85 ? 197 SER B OG 1 ATOM 2954 N N . PRO B 1 176 ? 30.240 -19.242 14.578 1.00 31.51 ? 198 PRO B N 1 ATOM 2955 C CA . PRO B 1 176 ? 30.098 -19.740 13.189 1.00 32.57 ? 198 PRO B CA 1 ATOM 2956 C C . PRO B 1 176 ? 30.087 -21.292 13.188 1.00 34.48 ? 198 PRO B C 1 ATOM 2957 O O . PRO B 1 176 ? 30.623 -21.903 14.087 1.00 33.73 ? 198 PRO B O 1 ATOM 2958 C CB . PRO B 1 176 ? 31.413 -19.337 12.535 1.00 32.35 ? 198 PRO B CB 1 ATOM 2959 C CG . PRO B 1 176 ? 32.462 -19.314 13.709 1.00 30.06 ? 198 PRO B CG 1 ATOM 2960 C CD . PRO B 1 176 ? 31.643 -19.115 14.998 1.00 30.73 ? 198 PRO B CD 1 ATOM 2961 N N . LEU B 1 177 ? 29.497 -21.878 12.166 1.00 37.10 ? 199 LEU B N 1 ATOM 2962 C CA . LEU B 1 177 ? 29.554 -23.306 11.933 1.00 38.85 ? 199 LEU B CA 1 ATOM 2963 C C . LEU B 1 177 ? 30.388 -23.444 10.654 1.00 40.31 ? 199 LEU B C 1 ATOM 2964 O O . LEU B 1 177 ? 29.972 -22.954 9.634 1.00 40.64 ? 199 LEU B O 1 ATOM 2965 C CB . LEU B 1 177 ? 28.168 -23.808 11.625 1.00 38.54 ? 199 LEU B CB 1 ATOM 2966 C CG . LEU B 1 177 ? 28.153 -25.307 11.248 1.00 38.52 ? 199 LEU B CG 1 ATOM 2967 C CD1 . LEU B 1 177 ? 28.087 -26.140 12.504 1.00 35.00 ? 199 LEU B CD1 1 ATOM 2968 C CD2 . LEU B 1 177 ? 26.945 -25.584 10.389 1.00 37.30 ? 199 LEU B CD2 1 ATOM 2969 N N . VAL B 1 178 ? 31.532 -24.113 10.709 1.00 42.15 ? 200 VAL B N 1 ATOM 2970 C CA . VAL B 1 178 ? 32.404 -24.221 9.549 1.00 45.37 ? 200 VAL B CA 1 ATOM 2971 C C . VAL B 1 178 ? 32.144 -25.561 8.828 1.00 46.89 ? 200 VAL B C 1 ATOM 2972 O O . VAL B 1 178 ? 32.222 -26.599 9.452 1.00 47.23 ? 200 VAL B O 1 ATOM 2973 C CB . VAL B 1 178 ? 33.897 -24.216 10.014 1.00 45.35 ? 200 VAL B CB 1 ATOM 2974 C CG1 . VAL B 1 178 ? 34.851 -24.017 8.817 1.00 47.10 ? 200 VAL B CG1 1 ATOM 2975 C CG2 . VAL B 1 178 ? 34.136 -23.155 11.100 1.00 45.68 ? 200 VAL B CG2 1 ATOM 2976 N N . CYS B 1 179 ? 31.827 -25.536 7.535 1.00 48.85 ? 201 CYS B N 1 ATOM 2977 C CA . CYS B 1 179 ? 31.652 -26.774 6.747 1.00 49.47 ? 201 CYS B CA 1 ATOM 2978 C C . CYS B 1 179 ? 32.550 -26.731 5.483 1.00 51.39 ? 201 CYS B C 1 ATOM 2979 O O . CYS B 1 179 ? 32.432 -25.815 4.636 1.00 50.77 ? 201 CYS B O 1 ATOM 2980 C CB . CYS B 1 179 ? 30.199 -26.935 6.293 1.00 48.76 ? 201 CYS B CB 1 ATOM 2981 S SG . CYS B 1 179 ? 28.938 -26.751 7.573 1.00 47.30 ? 201 CYS B SG 1 ATOM 2982 N N . ASN B 1 180 ? 33.425 -27.728 5.328 1.00 52.78 ? 204 ASN B N 1 ATOM 2983 C CA . ASN B 1 180 ? 34.293 -27.761 4.157 1.00 53.64 ? 204 ASN B CA 1 ATOM 2984 C C . ASN B 1 180 ? 34.801 -26.350 3.867 1.00 53.62 ? 204 ASN B C 1 ATOM 2985 O O . ASN B 1 180 ? 34.650 -25.828 2.756 1.00 53.87 ? 204 ASN B O 1 ATOM 2986 C CB . ASN B 1 180 ? 33.523 -28.331 2.947 1.00 54.92 ? 204 ASN B CB 1 ATOM 2987 C CG . ASN B 1 180 ? 32.998 -29.755 3.202 1.00 55.87 ? 204 ASN B CG 1 ATOM 2988 O OD1 . ASN B 1 180 ? 33.606 -30.527 3.951 1.00 60.06 ? 204 ASN B OD1 1 ATOM 2989 N ND2 . ASN B 1 180 ? 31.866 -30.092 2.597 1.00 56.86 ? 204 ASN B ND2 1 ATOM 2990 N N . GLY B 1 181 ? 35.298 -25.706 4.923 1.00 53.07 ? 205 GLY B N 1 ATOM 2991 C CA . GLY B 1 181 ? 35.966 -24.427 4.824 1.00 51.66 ? 205 GLY B CA 1 ATOM 2992 C C . GLY B 1 181 ? 35.230 -23.099 4.842 1.00 49.73 ? 205 GLY B C 1 ATOM 2993 O O . GLY B 1 181 ? 35.894 -22.080 4.990 1.00 50.83 ? 205 GLY B O 1 ATOM 2994 N N . LEU B 1 182 ? 33.912 -23.093 4.632 1.00 47.66 ? 208 LEU B N 1 ATOM 2995 C CA . LEU B 1 182 ? 33.113 -21.861 4.551 1.00 45.13 ? 208 LEU B CA 1 ATOM 2996 C C . LEU B 1 182 ? 32.108 -21.774 5.716 1.00 43.15 ? 208 LEU B C 1 ATOM 2997 O O . LEU B 1 182 ? 31.644 -22.803 6.200 1.00 41.82 ? 208 LEU B O 1 ATOM 2998 C CB . LEU B 1 182 ? 32.274 -21.868 3.296 1.00 44.85 ? 208 LEU B CB 1 ATOM 2999 C CG . LEU B 1 182 ? 32.808 -22.724 2.143 1.00 46.94 ? 208 LEU B CG 1 ATOM 3000 C CD1 . LEU B 1 182 ? 31.880 -22.597 0.963 1.00 40.79 ? 208 LEU B CD1 1 ATOM 3001 C CD2 . LEU B 1 182 ? 34.217 -22.309 1.746 1.00 44.18 ? 208 LEU B CD2 1 ATOM 3002 N N . ILE B 1 183 ? 31.744 -20.547 6.107 1.00 40.53 ? 209 ILE B N 1 ATOM 3003 C CA . ILE B 1 183 ? 30.798 -20.314 7.202 1.00 37.26 ? 209 ILE B CA 1 ATOM 3004 C C . ILE B 1 183 ? 29.416 -20.572 6.715 1.00 36.80 ? 209 ILE B C 1 ATOM 3005 O O . ILE B 1 183 ? 28.833 -19.795 5.976 1.00 36.04 ? 209 ILE B O 1 ATOM 3006 C CB . ILE B 1 183 ? 30.837 -18.853 7.641 1.00 38.24 ? 209 ILE B CB 1 ATOM 3007 C CG1 . ILE B 1 183 ? 32.281 -18.451 7.939 1.00 34.17 ? 209 ILE B CG1 1 ATOM 3008 C CG2 . ILE B 1 183 ? 29.877 -18.649 8.856 1.00 34.19 ? 209 ILE B CG2 1 ATOM 3009 C CD1 . ILE B 1 183 ? 32.910 -19.390 8.857 1.00 35.84 ? 209 ILE B CD1 1 ATOM 3010 N N . HIS B 1 184 ? 28.853 -21.675 7.134 1.00 34.93 ? 210 HIS B N 1 ATOM 3011 C CA . HIS B 1 184 ? 27.577 -22.014 6.610 1.00 33.40 ? 210 HIS B CA 1 ATOM 3012 C C . HIS B 1 184 ? 26.487 -21.675 7.623 1.00 31.43 ? 210 HIS B C 1 ATOM 3013 O O . HIS B 1 184 ? 25.328 -21.592 7.289 1.00 31.33 ? 210 HIS B O 1 ATOM 3014 C CB . HIS B 1 184 ? 27.630 -23.508 6.204 1.00 34.55 ? 210 HIS B CB 1 ATOM 3015 C CG . HIS B 1 184 ? 27.906 -23.720 4.737 1.00 35.43 ? 210 HIS B CG 1 ATOM 3016 N ND1 . HIS B 1 184 ? 26.943 -23.546 3.773 1.00 34.99 ? 210 HIS B ND1 1 ATOM 3017 C CD2 . HIS B 1 184 ? 29.028 -24.096 4.076 1.00 36.28 ? 210 HIS B CD2 1 ATOM 3018 C CE1 . HIS B 1 184 ? 27.449 -23.784 2.581 1.00 35.90 ? 210 HIS B CE1 1 ATOM 3019 N NE2 . HIS B 1 184 ? 28.710 -24.138 2.736 1.00 35.39 ? 210 HIS B NE2 1 ATOM 3020 N N . GLY B 1 185 ? 26.895 -21.500 8.861 1.00 30.34 ? 211 GLY B N 1 ATOM 3021 C CA . GLY B 1 185 ? 25.961 -21.097 9.890 1.00 30.75 ? 211 GLY B CA 1 ATOM 3022 C C . GLY B 1 185 ? 26.479 -20.160 10.978 1.00 29.06 ? 211 GLY B C 1 ATOM 3023 O O . GLY B 1 185 ? 27.704 -20.068 11.224 1.00 30.89 ? 211 GLY B O 1 ATOM 3024 N N . ILE B 1 186 ? 25.523 -19.532 11.670 1.00 26.76 ? 212 ILE B N 1 ATOM 3025 C CA . ILE B 1 186 ? 25.751 -18.809 12.908 1.00 25.68 ? 212 ILE B CA 1 ATOM 3026 C C . ILE B 1 186 ? 24.751 -19.387 13.912 1.00 26.50 ? 212 ILE B C 1 ATOM 3027 O O . ILE B 1 186 ? 23.538 -19.352 13.692 1.00 24.56 ? 212 ILE B O 1 ATOM 3028 C CB . ILE B 1 186 ? 25.343 -17.285 12.765 1.00 26.40 ? 212 ILE B CB 1 ATOM 3029 C CG1 . ILE B 1 186 ? 26.029 -16.666 11.579 1.00 24.41 ? 212 ILE B CG1 1 ATOM 3030 C CG2 . ILE B 1 186 ? 25.637 -16.526 14.153 1.00 25.03 ? 212 ILE B CG2 1 ATOM 3031 C CD1 . ILE B 1 186 ? 25.202 -15.455 10.861 1.00 23.88 ? 212 ILE B CD1 1 ATOM 3032 N N . ALA B 1 187 ? 25.273 -19.798 15.050 1.00 28.60 ? 213 ALA B N 1 ATOM 3033 C CA . ALA B 1 187 ? 24.496 -20.497 16.083 1.00 29.46 ? 213 ALA B CA 1 ATOM 3034 C C . ALA B 1 187 ? 23.373 -19.630 16.607 1.00 30.32 ? 213 ALA B C 1 ATOM 3035 O O . ALA B 1 187 ? 23.626 -18.467 16.988 1.00 32.79 ? 213 ALA B O 1 ATOM 3036 C CB . ALA B 1 187 ? 25.421 -20.872 17.146 1.00 28.53 ? 213 ALA B CB 1 ATOM 3037 N N . SER B 1 188 ? 22.155 -20.147 16.607 1.00 28.06 ? 214 SER B N 1 ATOM 3038 C CA . SER B 1 188 ? 21.010 -19.350 16.894 1.00 28.19 ? 214 SER B CA 1 ATOM 3039 C C . SER B 1 188 ? 20.096 -19.835 18.040 1.00 29.82 ? 214 SER B C 1 ATOM 3040 O O . SER B 1 188 ? 19.730 -19.053 18.955 1.00 25.33 ? 214 SER B O 1 ATOM 3041 C CB . SER B 1 188 ? 20.196 -19.174 15.625 1.00 27.29 ? 214 SER B CB 1 ATOM 3042 O OG . SER B 1 188 ? 18.938 -18.547 15.823 1.00 27.08 ? 214 SER B OG 1 ATOM 3043 N N . PHE B 1 189 ? 19.664 -21.105 17.949 1.00 27.67 ? 215 PHE B N 1 ATOM 3044 C CA . PHE B 1 189 ? 18.860 -21.608 19.022 1.00 28.87 ? 215 PHE B CA 1 ATOM 3045 C C . PHE B 1 189 ? 19.032 -23.179 19.190 1.00 29.30 ? 215 PHE B C 1 ATOM 3046 O O . PHE B 1 189 ? 19.707 -23.850 18.349 1.00 30.87 ? 215 PHE B O 1 ATOM 3047 C CB . PHE B 1 189 ? 17.409 -21.104 18.918 1.00 27.64 ? 215 PHE B CB 1 ATOM 3048 C CG . PHE B 1 189 ? 16.609 -21.695 17.796 1.00 31.56 ? 215 PHE B CG 1 ATOM 3049 C CD1 . PHE B 1 189 ? 16.468 -21.011 16.589 1.00 31.09 ? 215 PHE B CD1 1 ATOM 3050 C CD2 . PHE B 1 189 ? 16.017 -22.963 17.934 1.00 30.76 ? 215 PHE B CD2 1 ATOM 3051 C CE1 . PHE B 1 189 ? 15.686 -21.544 15.544 1.00 36.45 ? 215 PHE B CE1 1 ATOM 3052 C CE2 . PHE B 1 189 ? 15.255 -23.517 16.904 1.00 39.16 ? 215 PHE B CE2 1 ATOM 3053 C CZ . PHE B 1 189 ? 15.079 -22.824 15.696 1.00 37.27 ? 215 PHE B CZ 1 ATOM 3054 N N . VAL B 1 190 ? 18.568 -23.679 20.321 1.00 29.92 ? 216 VAL B N 1 ATOM 3055 C CA . VAL B 1 190 ? 18.592 -25.128 20.691 1.00 29.74 ? 216 VAL B CA 1 ATOM 3056 C C . VAL B 1 190 ? 17.178 -25.409 21.223 1.00 31.97 ? 216 VAL B C 1 ATOM 3057 O O . VAL B 1 190 ? 16.465 -24.447 21.542 1.00 31.08 ? 216 VAL B O 1 ATOM 3058 C CB . VAL B 1 190 ? 19.682 -25.541 21.733 1.00 29.17 ? 216 VAL B CB 1 ATOM 3059 C CG1 . VAL B 1 190 ? 21.086 -25.366 21.265 1.00 25.56 ? 216 VAL B CG1 1 ATOM 3060 C CG2 . VAL B 1 190 ? 19.582 -24.847 23.118 1.00 28.97 ? 216 VAL B CG2 1 ATOM 3061 N N . ARG B 1 191 A 16.731 -26.699 21.274 1.00 31.82 ? 217 ARG B N 1 ATOM 3062 C CA . ARG B 1 191 A 15.396 -27.027 21.834 1.00 33.08 ? 217 ARG B CA 1 ATOM 3063 C C . ARG B 1 191 A 15.561 -28.213 22.813 1.00 32.98 ? 217 ARG B C 1 ATOM 3064 O O . ARG B 1 191 A 16.473 -29.003 22.633 1.00 30.69 ? 217 ARG B O 1 ATOM 3065 C CB . ARG B 1 191 A 14.428 -27.410 20.738 1.00 34.55 ? 217 ARG B CB 1 ATOM 3066 C CG . ARG B 1 191 A 13.661 -26.280 19.946 1.00 38.40 ? 217 ARG B CG 1 ATOM 3067 C CD . ARG B 1 191 A 13.268 -26.759 18.570 1.00 39.17 ? 217 ARG B CD 1 ATOM 3068 N NE . ARG B 1 191 A 14.521 -26.941 17.854 1.00 46.77 ? 217 ARG B NE 1 ATOM 3069 C CZ . ARG B 1 191 A 14.860 -27.954 17.044 1.00 46.86 ? 217 ARG B CZ 1 ATOM 3070 N NH1 . ARG B 1 191 A 14.030 -28.956 16.774 1.00 45.62 ? 217 ARG B NH1 1 ATOM 3071 N NH2 . ARG B 1 191 A 16.078 -27.955 16.508 1.00 48.64 ? 217 ARG B NH2 1 ATOM 3072 N N . GLY B 1 192 ? 14.725 -28.311 23.851 1.00 32.85 ? 218 GLY B N 1 ATOM 3073 C CA . GLY B 1 192 ? 14.902 -29.357 24.857 1.00 32.94 ? 218 GLY B CA 1 ATOM 3074 C C . GLY B 1 192 ? 16.167 -29.131 25.676 1.00 34.20 ? 218 GLY B C 1 ATOM 3075 O O . GLY B 1 192 ? 16.768 -30.060 26.292 1.00 32.55 ? 218 GLY B O 1 ATOM 3076 N N . GLY B 1 193 ? 16.566 -27.850 25.758 1.00 31.77 ? 219 GLY B N 1 ATOM 3077 C CA . GLY B 1 193 ? 17.762 -27.539 26.492 1.00 31.75 ? 219 GLY B CA 1 ATOM 3078 C C . GLY B 1 193 ? 18.964 -27.878 25.655 1.00 31.07 ? 219 GLY B C 1 ATOM 3079 O O . GLY B 1 193 ? 18.855 -28.408 24.561 1.00 34.62 ? 219 GLY B O 1 ATOM 3080 N N . CYS B 1 194 ? 20.124 -27.603 26.174 1.00 32.37 ? 220 CYS B N 1 ATOM 3081 C CA . CYS B 1 194 ? 21.360 -27.910 25.502 1.00 31.55 ? 220 CYS B CA 1 ATOM 3082 C C . CYS B 1 194 ? 21.615 -29.433 25.516 1.00 33.11 ? 220 CYS B C 1 ATOM 3083 O O . CYS B 1 194 ? 21.317 -30.185 26.501 1.00 31.49 ? 220 CYS B O 1 ATOM 3084 C CB . CYS B 1 194 ? 22.549 -27.240 26.162 1.00 31.07 ? 220 CYS B CB 1 ATOM 3085 S SG . CYS B 1 194 ? 22.524 -25.387 26.417 1.00 30.32 ? 220 CYS B SG 1 ATOM 3086 N N . ALA B 1 195 ? 22.198 -29.855 24.418 1.00 33.07 ? 221 ALA B N 1 ATOM 3087 C CA . ALA B 1 195 ? 22.651 -31.230 24.302 1.00 32.92 ? 221 ALA B CA 1 ATOM 3088 C C . ALA B 1 195 ? 21.591 -32.222 24.725 1.00 32.69 ? 221 ALA B C 1 ATOM 3089 O O . ALA B 1 195 ? 21.927 -33.132 25.459 1.00 32.91 ? 221 ALA B O 1 ATOM 3090 C CB . ALA B 1 195 ? 23.820 -31.382 25.178 1.00 32.94 ? 221 ALA B CB 1 ATOM 3091 N N . SER B 1 196 ? 20.358 -32.068 24.246 1.00 32.86 ? 222 SER B N 1 ATOM 3092 C CA . SER B 1 196 ? 19.238 -32.958 24.567 1.00 33.89 ? 222 SER B CA 1 ATOM 3093 C C . SER B 1 196 ? 19.308 -34.426 23.981 1.00 37.14 ? 222 SER B C 1 ATOM 3094 O O . SER B 1 196 ? 18.741 -35.372 24.560 1.00 36.92 ? 222 SER B O 1 ATOM 3095 C CB . SER B 1 196 ? 17.941 -32.322 24.066 1.00 34.78 ? 222 SER B CB 1 ATOM 3096 O OG . SER B 1 196 ? 17.859 -32.264 22.614 1.00 31.11 ? 222 SER B OG 1 ATOM 3097 N N . GLY B 1 197 A 19.915 -34.577 22.799 1.00 37.47 ? 222 GLY B N 1 ATOM 3098 C CA . GLY B 1 197 A 19.995 -35.866 22.144 1.00 38.29 ? 222 GLY B CA 1 ATOM 3099 C C . GLY B 1 197 A 18.763 -36.068 21.321 1.00 38.74 ? 222 GLY B C 1 ATOM 3100 O O . GLY B 1 197 A 18.731 -36.957 20.474 1.00 40.69 ? 222 GLY B O 1 ATOM 3101 N N . LEU B 1 198 ? 17.763 -35.216 21.527 1.00 35.81 ? 223 LEU B N 1 ATOM 3102 C CA . LEU B 1 198 ? 16.501 -35.363 20.833 1.00 34.55 ? 223 LEU B CA 1 ATOM 3103 C C . LEU B 1 198 ? 16.317 -34.396 19.643 1.00 35.20 ? 223 LEU B C 1 ATOM 3104 O O . LEU B 1 198 ? 15.768 -34.796 18.619 1.00 35.54 ? 223 LEU B O 1 ATOM 3105 C CB . LEU B 1 198 ? 15.292 -35.245 21.802 1.00 32.61 ? 223 LEU B CB 1 ATOM 3106 C CG . LEU B 1 198 ? 15.249 -36.141 23.061 1.00 33.51 ? 223 LEU B CG 1 ATOM 3107 C CD1 . LEU B 1 198 ? 13.978 -35.846 23.934 1.00 30.03 ? 223 LEU B CD1 1 ATOM 3108 C CD2 . LEU B 1 198 ? 15.385 -37.690 22.725 1.00 30.64 ? 223 LEU B CD2 1 ATOM 3109 N N . TYR B 1 199 ? 16.839 -33.167 19.784 1.00 35.26 ? 224 TYR B N 1 ATOM 3110 C CA . TYR B 1 199 ? 16.618 -32.088 18.807 1.00 33.34 ? 224 TYR B CA 1 ATOM 3111 C C . TYR B 1 199 ? 17.918 -31.595 18.226 1.00 32.01 ? 224 TYR B C 1 ATOM 3112 O O . TYR B 1 199 ? 18.943 -31.574 18.915 1.00 31.55 ? 224 TYR B O 1 ATOM 3113 C CB . TYR B 1 199 ? 15.941 -30.977 19.525 1.00 34.43 ? 224 TYR B CB 1 ATOM 3114 C CG . TYR B 1 199 ? 14.551 -31.290 20.009 1.00 32.98 ? 224 TYR B CG 1 ATOM 3115 C CD1 . TYR B 1 199 ? 13.482 -31.254 19.154 1.00 34.73 ? 224 TYR B CD1 1 ATOM 3116 C CD2 . TYR B 1 199 ? 14.301 -31.542 21.340 1.00 35.76 ? 224 TYR B CD2 1 ATOM 3117 C CE1 . TYR B 1 199 ? 12.189 -31.490 19.611 1.00 37.73 ? 224 TYR B CE1 1 ATOM 3118 C CE2 . TYR B 1 199 ? 13.023 -31.798 21.801 1.00 35.90 ? 224 TYR B CE2 1 ATOM 3119 C CZ . TYR B 1 199 ? 11.982 -31.756 20.944 1.00 39.34 ? 224 TYR B CZ 1 ATOM 3120 O OH . TYR B 1 199 ? 10.705 -32.019 21.407 1.00 44.06 ? 224 TYR B OH 1 ATOM 3121 N N . PRO B 1 200 ? 17.935 -31.237 16.941 1.00 31.10 ? 225 PRO B N 1 ATOM 3122 C CA . PRO B 1 200 ? 19.191 -30.771 16.362 1.00 30.90 ? 225 PRO B CA 1 ATOM 3123 C C . PRO B 1 200 ? 19.383 -29.273 16.788 1.00 30.69 ? 225 PRO B C 1 ATOM 3124 O O . PRO B 1 200 ? 18.401 -28.658 17.202 1.00 29.70 ? 225 PRO B O 1 ATOM 3125 C CB . PRO B 1 200 ? 18.964 -30.907 14.856 1.00 31.04 ? 225 PRO B CB 1 ATOM 3126 C CG . PRO B 1 200 ? 17.530 -30.671 14.671 1.00 31.16 ? 225 PRO B CG 1 ATOM 3127 C CD . PRO B 1 200 ? 16.850 -31.255 15.959 1.00 31.12 ? 225 PRO B CD 1 ATOM 3128 N N . ASP B 1 201 ? 20.607 -28.779 16.753 1.00 29.13 ? 226 ASP B N 1 ATOM 3129 C CA . ASP B 1 201 ? 20.870 -27.359 17.024 1.00 30.41 ? 226 ASP B CA 1 ATOM 3130 C C . ASP B 1 201 ? 20.548 -26.619 15.749 1.00 31.49 ? 226 ASP B C 1 ATOM 3131 O O . ASP B 1 201 ? 20.678 -27.188 14.644 1.00 29.94 ? 226 ASP B O 1 ATOM 3132 C CB . ASP B 1 201 ? 22.314 -27.138 17.437 1.00 28.92 ? 226 ASP B CB 1 ATOM 3133 C CG . ASP B 1 201 ? 22.631 -27.854 18.693 1.00 28.22 ? 226 ASP B CG 1 ATOM 3134 O OD1 . ASP B 1 201 ? 23.825 -28.044 18.982 1.00 26.04 ? 226 ASP B OD1 1 ATOM 3135 O OD2 . ASP B 1 201 ? 21.703 -28.205 19.478 1.00 23.70 ? 226 ASP B OD2 1 ATOM 3136 N N . ALA B 1 202 ? 20.134 -25.359 15.886 1.00 31.02 ? 227 ALA B N 1 ATOM 3137 C CA . ALA B 1 202 ? 19.726 -24.552 14.720 1.00 29.95 ? 227 ALA B CA 1 ATOM 3138 C C . ALA B 1 202 ? 20.634 -23.306 14.522 1.00 32.33 ? 227 ALA B C 1 ATOM 3139 O O . ALA B 1 202 ? 20.936 -22.541 15.492 1.00 28.76 ? 227 ALA B O 1 ATOM 3140 C CB . ALA B 1 202 ? 18.251 -24.172 14.813 1.00 28.64 ? 227 ALA B CB 1 ATOM 3141 N N . PHE B 1 203 ? 21.091 -23.153 13.271 1.00 32.13 ? 228 PHE B N 1 ATOM 3142 C CA . PHE B 1 203 ? 22.037 -22.107 12.898 1.00 32.31 ? 228 PHE B CA 1 ATOM 3143 C C . PHE B 1 203 ? 21.402 -21.299 11.796 1.00 32.29 ? 228 PHE B C 1 ATOM 3144 O O . PHE B 1 203 ? 20.709 -21.813 10.935 1.00 33.92 ? 228 PHE B O 1 ATOM 3145 C CB . PHE B 1 203 ? 23.381 -22.654 12.417 1.00 32.62 ? 228 PHE B CB 1 ATOM 3146 C CG . PHE B 1 203 ? 24.119 -23.522 13.428 1.00 34.44 ? 228 PHE B CG 1 ATOM 3147 C CD1 . PHE B 1 203 ? 25.319 -23.082 13.979 1.00 33.16 ? 228 PHE B CD1 1 ATOM 3148 C CD2 . PHE B 1 203 ? 23.650 -24.795 13.782 1.00 35.11 ? 228 PHE B CD2 1 ATOM 3149 C CE1 . PHE B 1 203 ? 26.045 -23.858 14.829 1.00 34.57 ? 228 PHE B CE1 1 ATOM 3150 C CE2 . PHE B 1 203 ? 24.352 -25.579 14.708 1.00 30.39 ? 228 PHE B CE2 1 ATOM 3151 C CZ . PHE B 1 203 ? 25.547 -25.144 15.208 1.00 32.94 ? 228 PHE B CZ 1 ATOM 3152 N N . ALA B 1 204 ? 21.553 -19.981 11.874 1.00 30.70 ? 229 ALA B N 1 ATOM 3153 C CA . ALA B 1 204 ? 21.089 -19.158 10.813 1.00 29.70 ? 229 ALA B CA 1 ATOM 3154 C C . ALA B 1 204 ? 21.884 -19.547 9.563 1.00 28.03 ? 229 ALA B C 1 ATOM 3155 O O . ALA B 1 204 ? 23.115 -19.723 9.575 1.00 29.53 ? 229 ALA B O 1 ATOM 3156 C CB . ALA B 1 204 ? 21.339 -17.605 11.173 1.00 29.88 ? 229 ALA B CB 1 ATOM 3157 N N . PRO B 1 205 ? 21.172 -19.604 8.488 1.00 26.94 ? 230 PRO B N 1 ATOM 3158 C CA . PRO B 1 205 ? 21.677 -20.056 7.179 1.00 28.97 ? 230 PRO B CA 1 ATOM 3159 C C . PRO B 1 205 ? 22.509 -19.037 6.396 1.00 29.59 ? 230 PRO B C 1 ATOM 3160 O O . PRO B 1 205 ? 21.927 -18.380 5.595 1.00 31.14 ? 230 PRO B O 1 ATOM 3161 C CB . PRO B 1 205 ? 20.392 -20.309 6.401 1.00 28.10 ? 230 PRO B CB 1 ATOM 3162 C CG . PRO B 1 205 ? 19.331 -19.696 7.109 1.00 28.53 ? 230 PRO B CG 1 ATOM 3163 C CD . PRO B 1 205 ? 19.770 -19.225 8.468 1.00 26.38 ? 230 PRO B CD 1 ATOM 3164 N N . VAL B 1 206 ? 23.811 -18.977 6.551 1.00 32.04 ? 231 VAL B N 1 ATOM 3165 C CA . VAL B 1 206 ? 24.552 -17.820 6.029 1.00 34.36 ? 231 VAL B CA 1 ATOM 3166 C C . VAL B 1 206 ? 24.417 -17.621 4.517 1.00 35.45 ? 231 VAL B C 1 ATOM 3167 O O . VAL B 1 206 ? 24.227 -16.465 4.014 1.00 34.26 ? 231 VAL B O 1 ATOM 3168 C CB . VAL B 1 206 ? 25.988 -17.936 6.428 1.00 33.31 ? 231 VAL B CB 1 ATOM 3169 C CG1 . VAL B 1 206 ? 26.835 -16.908 5.711 1.00 35.58 ? 231 VAL B CG1 1 ATOM 3170 C CG2 . VAL B 1 206 ? 26.095 -17.806 7.957 1.00 37.53 ? 231 VAL B CG2 1 ATOM 3171 N N . ALA B 1 207 ? 24.441 -18.763 3.826 1.00 35.81 ? 232 ALA B N 1 ATOM 3172 C CA . ALA B 1 207 ? 24.318 -18.840 2.366 1.00 37.14 ? 232 ALA B CA 1 ATOM 3173 C C . ALA B 1 207 ? 23.076 -18.182 1.840 1.00 37.73 ? 232 ALA B C 1 ATOM 3174 O O . ALA B 1 207 ? 23.056 -17.693 0.708 1.00 39.12 ? 232 ALA B O 1 ATOM 3175 C CB . ALA B 1 207 ? 24.380 -20.334 1.907 1.00 37.46 ? 232 ALA B CB 1 ATOM 3176 N N . GLN B 1 208 ? 22.060 -18.074 2.684 1.00 37.90 ? 233 GLN B N 1 ATOM 3177 C CA . GLN B 1 208 ? 20.836 -17.355 2.287 1.00 38.88 ? 233 GLN B CA 1 ATOM 3178 C C . GLN B 1 208 ? 20.867 -15.725 2.307 1.00 39.44 ? 233 GLN B C 1 ATOM 3179 O O . GLN B 1 208 ? 19.952 -15.085 1.797 1.00 39.98 ? 233 GLN B O 1 ATOM 3180 C CB . GLN B 1 208 ? 19.651 -17.835 3.126 1.00 39.66 ? 233 GLN B CB 1 ATOM 3181 C CG . GLN B 1 208 ? 19.290 -19.377 2.976 1.00 42.29 ? 233 GLN B CG 1 ATOM 3182 C CD . GLN B 1 208 ? 17.925 -19.737 3.630 1.00 47.10 ? 233 GLN B CD 1 ATOM 3183 O OE1 . GLN B 1 208 ? 17.203 -18.855 4.084 1.00 49.94 ? 233 GLN B OE1 1 ATOM 3184 N NE2 . GLN B 1 208 ? 17.606 -21.028 3.709 1.00 48.29 ? 233 GLN B NE2 1 ATOM 3185 N N . PHE B 1 209 ? 21.927 -15.149 2.872 1.00 38.67 ? 234 PHE B N 1 ATOM 3186 C CA . PHE B 1 209 ? 22.085 -13.686 3.153 1.00 38.71 ? 234 PHE B CA 1 ATOM 3187 C C . PHE B 1 209 ? 23.337 -13.172 2.430 1.00 40.02 ? 234 PHE B C 1 ATOM 3188 O O . PHE B 1 209 ? 23.773 -11.998 2.567 1.00 38.74 ? 234 PHE B O 1 ATOM 3189 C CB . PHE B 1 209 ? 22.257 -13.471 4.681 1.00 37.63 ? 234 PHE B CB 1 ATOM 3190 C CG . PHE B 1 209 ? 21.029 -13.805 5.443 1.00 36.40 ? 234 PHE B CG 1 ATOM 3191 C CD1 . PHE B 1 209 ? 20.944 -14.991 6.151 1.00 37.34 ? 234 PHE B CD1 1 ATOM 3192 C CD2 . PHE B 1 209 ? 19.920 -12.999 5.352 1.00 35.42 ? 234 PHE B CD2 1 ATOM 3193 C CE1 . PHE B 1 209 ? 19.763 -15.342 6.795 1.00 35.92 ? 234 PHE B CE1 1 ATOM 3194 C CE2 . PHE B 1 209 ? 18.752 -13.330 5.974 1.00 36.24 ? 234 PHE B CE2 1 ATOM 3195 C CZ . PHE B 1 209 ? 18.671 -14.527 6.700 1.00 38.28 ? 234 PHE B CZ 1 ATOM 3196 N N . VAL B 1 210 ? 23.924 -14.088 1.647 1.00 40.40 ? 235 VAL B N 1 ATOM 3197 C CA . VAL B 1 210 ? 25.165 -13.769 0.936 1.00 40.47 ? 235 VAL B CA 1 ATOM 3198 C C . VAL B 1 210 ? 25.242 -12.476 0.126 1.00 39.54 ? 235 VAL B C 1 ATOM 3199 O O . VAL B 1 210 ? 26.165 -11.731 0.332 1.00 40.12 ? 235 VAL B O 1 ATOM 3200 C CB . VAL B 1 210 ? 25.694 -14.936 0.104 1.00 41.10 ? 235 VAL B CB 1 ATOM 3201 C CG1 . VAL B 1 210 ? 26.822 -14.447 -0.789 1.00 39.75 ? 235 VAL B CG1 1 ATOM 3202 C CG2 . VAL B 1 210 ? 26.241 -15.922 1.042 1.00 42.91 ? 235 VAL B CG2 1 ATOM 3203 N N . ASN B 1 211 ? 24.324 -12.273 -0.809 1.00 39.25 ? 236 ASN B N 1 ATOM 3204 C CA . ASN B 1 211 ? 24.366 -11.060 -1.621 1.00 38.89 ? 236 ASN B CA 1 ATOM 3205 C C . ASN B 1 211 ? 24.091 -9.845 -0.732 1.00 39.23 ? 236 ASN B C 1 ATOM 3206 O O . ASN B 1 211 ? 24.641 -8.744 -0.971 1.00 38.37 ? 236 ASN B O 1 ATOM 3207 C CB . ASN B 1 211 ? 23.376 -11.138 -2.761 1.00 37.99 ? 236 ASN B CB 1 ATOM 3208 C CG . ASN B 1 211 ? 23.663 -12.330 -3.671 1.00 36.54 ? 236 ASN B CG 1 ATOM 3209 O OD1 . ASN B 1 211 ? 22.805 -12.777 -4.340 1.00 33.55 ? 236 ASN B OD1 1 ATOM 3210 N ND2 . ASN B 1 211 ? 24.900 -12.815 -3.675 1.00 31.43 ? 236 ASN B ND2 1 ATOM 3211 N N . TRP B 1 212 ? 23.254 -10.021 0.291 1.00 37.88 ? 237 TRP B N 1 ATOM 3212 C CA . TRP B 1 212 ? 23.005 -8.908 1.195 1.00 37.47 ? 237 TRP B CA 1 ATOM 3213 C C . TRP B 1 212 ? 24.264 -8.562 1.934 1.00 36.31 ? 237 TRP B C 1 ATOM 3214 O O . TRP B 1 212 ? 24.616 -7.322 2.027 1.00 37.29 ? 237 TRP B O 1 ATOM 3215 C CB . TRP B 1 212 ? 21.973 -9.261 2.234 1.00 36.38 ? 237 TRP B CB 1 ATOM 3216 C CG . TRP B 1 212 ? 21.836 -8.228 3.335 1.00 38.24 ? 237 TRP B CG 1 ATOM 3217 C CD1 . TRP B 1 212 ? 21.362 -6.955 3.224 1.00 41.96 ? 237 TRP B CD1 1 ATOM 3218 C CD2 . TRP B 1 212 ? 22.113 -8.427 4.714 1.00 34.52 ? 237 TRP B CD2 1 ATOM 3219 N NE1 . TRP B 1 212 ? 21.335 -6.341 4.454 1.00 36.28 ? 237 TRP B NE1 1 ATOM 3220 C CE2 . TRP B 1 212 ? 21.790 -7.229 5.389 1.00 36.48 ? 237 TRP B CE2 1 ATOM 3221 C CE3 . TRP B 1 212 ? 22.584 -9.519 5.459 1.00 33.27 ? 237 TRP B CE3 1 ATOM 3222 C CZ2 . TRP B 1 212 ? 21.911 -7.095 6.774 1.00 37.50 ? 237 TRP B CZ2 1 ATOM 3223 C CZ3 . TRP B 1 212 ? 22.721 -9.398 6.796 1.00 36.45 ? 237 TRP B CZ3 1 ATOM 3224 C CH2 . TRP B 1 212 ? 22.394 -8.164 7.468 1.00 36.98 ? 237 TRP B CH2 1 ATOM 3225 N N . ILE B 1 213 ? 24.903 -9.558 2.518 1.00 35.42 ? 238 ILE B N 1 ATOM 3226 C CA . ILE B 1 213 ? 26.129 -9.337 3.245 1.00 34.38 ? 238 ILE B CA 1 ATOM 3227 C C . ILE B 1 213 ? 27.084 -8.642 2.289 1.00 37.82 ? 238 ILE B C 1 ATOM 3228 O O . ILE B 1 213 ? 27.552 -7.508 2.539 1.00 38.01 ? 238 ILE B O 1 ATOM 3229 C CB . ILE B 1 213 ? 26.723 -10.610 3.791 1.00 34.10 ? 238 ILE B CB 1 ATOM 3230 C CG1 . ILE B 1 213 ? 25.906 -11.116 4.991 1.00 31.68 ? 238 ILE B CG1 1 ATOM 3231 C CG2 . ILE B 1 213 ? 28.150 -10.399 4.306 1.00 30.92 ? 238 ILE B CG2 1 ATOM 3232 C CD1 . ILE B 1 213 ? 26.189 -12.581 5.345 1.00 28.87 ? 238 ILE B CD1 1 ATOM 3233 N N . ASP B 1 214 ? 27.358 -9.299 1.167 1.00 36.89 ? 239 ASP B N 1 ATOM 3234 C CA . ASP B 1 214 ? 28.196 -8.603 0.193 1.00 37.37 ? 239 ASP B CA 1 ATOM 3235 C C . ASP B 1 214 ? 27.796 -7.157 -0.169 1.00 35.35 ? 239 ASP B C 1 ATOM 3236 O O . ASP B 1 214 ? 28.661 -6.426 -0.402 1.00 34.13 ? 239 ASP B O 1 ATOM 3237 C CB . ASP B 1 214 ? 28.415 -9.426 -1.105 1.00 37.10 ? 239 ASP B CB 1 ATOM 3238 C CG . ASP B 1 214 ? 29.309 -10.677 -0.878 1.00 40.83 ? 239 ASP B CG 1 ATOM 3239 O OD1 . ASP B 1 214 ? 29.138 -11.691 -1.614 1.00 41.47 ? 239 ASP B OD1 1 ATOM 3240 O OD2 . ASP B 1 214 ? 30.193 -10.702 -0.007 1.00 40.64 ? 239 ASP B OD2 1 ATOM 3241 N N . SER B 1 215 ? 26.532 -6.799 -0.293 1.00 36.43 ? 240 SER B N 1 ATOM 3242 C CA . SER B 1 215 ? 26.208 -5.438 -0.678 1.00 37.60 ? 240 SER B CA 1 ATOM 3243 C C . SER B 1 215 ? 26.667 -4.437 0.365 1.00 37.78 ? 240 SER B C 1 ATOM 3244 O O . SER B 1 215 ? 26.540 -3.241 0.186 1.00 38.99 ? 240 SER B O 1 ATOM 3245 C CB . SER B 1 215 ? 24.690 -5.268 -0.843 1.00 39.45 ? 240 SER B CB 1 ATOM 3246 O OG . SER B 1 215 ? 24.019 -5.353 0.417 1.00 42.72 ? 240 SER B OG 1 ATOM 3247 N N . ILE B 1 216 ? 27.179 -4.973 1.463 1.00 36.22 ? 241 ILE B N 1 ATOM 3248 C CA . ILE B 1 216 ? 27.627 -4.228 2.616 1.00 33.70 ? 241 ILE B CA 1 ATOM 3249 C C . ILE B 1 216 ? 29.137 -4.227 2.824 1.00 33.12 ? 241 ILE B C 1 ATOM 3250 O O . ILE B 1 216 ? 29.716 -3.206 3.240 1.00 34.56 ? 241 ILE B O 1 ATOM 3251 C CB . ILE B 1 216 ? 26.984 -4.802 3.942 1.00 33.97 ? 241 ILE B CB 1 ATOM 3252 C CG1 . ILE B 1 216 ? 25.506 -4.524 4.093 1.00 29.38 ? 241 ILE B CG1 1 ATOM 3253 C CG2 . ILE B 1 216 ? 27.724 -4.326 5.173 1.00 31.72 ? 241 ILE B CG2 1 ATOM 3254 C CD1 . ILE B 1 216 ? 24.930 -5.374 5.241 1.00 32.22 ? 241 ILE B CD1 1 ATOM 3255 N N . ILE B 1 217 ? 29.816 -5.344 2.640 1.00 31.85 ? 242 ILE B N 1 ATOM 3256 C CA . ILE B 1 217 ? 31.232 -5.334 3.019 1.00 31.27 ? 242 ILE B CA 1 ATOM 3257 C C . ILE B 1 217 ? 32.157 -5.173 1.815 1.00 32.94 ? 242 ILE B C 1 ATOM 3258 O O . ILE B 1 217 ? 33.369 -5.036 1.975 1.00 32.35 ? 242 ILE B O 1 ATOM 3259 C CB . ILE B 1 217 ? 31.619 -6.626 3.765 1.00 32.41 ? 242 ILE B CB 1 ATOM 3260 C CG1 . ILE B 1 217 ? 31.402 -7.795 2.792 1.00 32.58 ? 242 ILE B CG1 1 ATOM 3261 C CG2 . ILE B 1 217 ? 30.777 -6.835 5.097 1.00 29.07 ? 242 ILE B CG2 1 ATOM 3262 C CD1 . ILE B 1 217 ? 31.804 -9.119 3.314 1.00 32.94 ? 242 ILE B CD1 1 ATOM 3263 N N . GLN B 1 218 ? 31.593 -5.213 0.612 1.00 34.52 ? 243 GLN B N 1 ATOM 3264 C CA . GLN B 1 218 ? 32.399 -5.108 -0.610 1.00 36.89 ? 243 GLN B CA 1 ATOM 3265 C C . GLN B 1 218 ? 32.205 -3.736 -1.296 1.00 38.02 ? 243 GLN B C 1 ATOM 3266 O O . GLN B 1 218 ? 31.073 -3.278 -1.512 1.00 39.32 ? 243 GLN B O 1 ATOM 3267 C CB . GLN B 1 218 ? 31.996 -6.167 -1.615 1.00 36.06 ? 243 GLN B CB 1 ATOM 3268 C CG . GLN B 1 218 ? 32.370 -7.652 -1.272 1.00 37.26 ? 243 GLN B CG 1 ATOM 3269 C CD . GLN B 1 218 ? 32.137 -8.563 -2.441 1.00 37.83 ? 243 GLN B CD 1 ATOM 3270 O OE1 . GLN B 1 218 ? 31.128 -8.439 -3.165 1.00 39.33 ? 243 GLN B OE1 1 ATOM 3271 N NE2 . GLN B 1 218 ? 33.049 -9.480 -2.646 1.00 39.37 ? 243 GLN B NE2 1 ATOM 3272 O OXT . GLN B 1 218 ? 33.177 -3.129 -1.707 1.00 39.76 ? 243 GLN B OXT 1 HETATM 3273 O O3 . 151 C 2 . ? 17.630 13.215 24.721 1.00 34.23 ? 400 151 A O3 1 HETATM 3274 C C2 . 151 C 2 . ? 18.260 12.771 23.753 1.00 34.83 ? 400 151 A C2 1 HETATM 3275 N N1 . 151 C 2 . ? 17.818 11.732 22.962 1.00 31.63 ? 400 151 A N1 1 HETATM 3276 C C26 . 151 C 2 . ? 18.699 10.896 22.177 1.00 35.38 ? 400 151 A C26 1 HETATM 3277 C C28 . 151 C 2 . ? 17.869 9.614 21.895 1.00 32.52 ? 400 151 A C28 1 HETATM 3278 C C29 . 151 C 2 . ? 16.779 9.759 22.939 1.00 32.56 ? 400 151 A C29 1 HETATM 3279 N N2 . 151 C 2 . ? 17.406 9.400 24.167 1.00 37.44 ? 400 151 A N2 1 HETATM 3280 S S1 . 151 C 2 . ? 16.398 8.901 25.457 1.00 41.01 ? 400 151 A S1 1 HETATM 3281 C C3 . 151 C 2 . ? 14.757 8.446 24.987 1.00 41.47 ? 400 151 A C3 1 HETATM 3282 O O1 . 151 C 2 . ? 17.261 7.845 26.079 1.00 45.77 ? 400 151 A O1 1 HETATM 3283 O O2 . 151 C 2 . ? 16.307 10.115 26.384 1.00 47.00 ? 400 151 A O2 1 HETATM 3284 C C8 . 151 C 2 . ? 16.456 11.270 22.947 1.00 30.00 ? 400 151 A C8 1 HETATM 3285 C C7 . 151 C 2 . ? 15.661 11.640 21.689 1.00 28.97 ? 400 151 A C7 1 HETATM 3286 C C27 . 151 C 2 . ? 15.298 13.144 21.502 1.00 28.33 ? 400 151 A C27 1 HETATM 3287 C C1 . 151 C 2 . ? 14.465 13.568 22.717 1.00 31.16 ? 400 151 A C1 1 HETATM 3288 C C17 . 151 C 2 . ? 14.550 13.321 20.168 1.00 25.50 ? 400 151 A C17 1 HETATM 3289 C C30 . 151 C 2 . ? 14.365 10.791 21.665 1.00 28.80 ? 400 151 A C30 1 HETATM 3290 O O5 . 151 C 2 . ? 13.370 10.848 22.429 1.00 27.71 ? 400 151 A O5 1 HETATM 3291 C C4 . 151 C 2 . ? 19.557 13.194 23.586 1.00 35.11 ? 400 151 A C4 1 HETATM 3292 N N3 . 151 C 2 . ? 20.288 13.279 22.356 1.00 37.87 ? 400 151 A N3 1 HETATM 3293 C C5 . 151 C 2 . ? 21.558 13.657 22.874 1.00 37.85 ? 400 151 A C5 1 HETATM 3294 O O4 . 151 C 2 . ? 21.620 13.797 24.246 1.00 39.59 ? 400 151 A O4 1 HETATM 3295 C C6 . 151 C 2 . ? 20.371 13.465 24.690 1.00 37.78 ? 400 151 A C6 1 HETATM 3296 C C9 . 151 C 2 . ? 22.726 13.916 21.986 1.00 40.25 ? 400 151 A C9 1 HETATM 3297 N N4 . 151 C 2 . ? 23.498 12.739 21.641 1.00 45.14 ? 400 151 A N4 1 HETATM 3298 C C11 . 151 C 2 . ? 22.972 11.921 20.544 1.00 41.97 ? 400 151 A C11 1 HETATM 3299 C C13 . 151 C 2 . ? 23.741 12.376 19.310 1.00 44.12 ? 400 151 A C13 1 HETATM 3300 C C14 . 151 C 2 . ? 25.129 12.409 19.918 1.00 44.99 ? 400 151 A C14 1 HETATM 3301 C C12 . 151 C 2 . ? 24.870 13.124 21.254 1.00 45.61 ? 400 151 A C12 1 HETATM 3302 C C1 . NAG D 3 . ? 2.018 25.699 10.984 1.00 48.25 ? 401 NAG A C1 1 HETATM 3303 C C2 . NAG D 3 . ? 1.697 26.969 10.170 1.00 54.09 ? 401 NAG A C2 1 HETATM 3304 C C3 . NAG D 3 . ? 0.324 26.782 9.550 1.00 54.07 ? 401 NAG A C3 1 HETATM 3305 C C4 . NAG D 3 . ? 0.429 25.544 8.672 1.00 51.84 ? 401 NAG A C4 1 HETATM 3306 C C5 . NAG D 3 . ? 0.813 24.344 9.538 1.00 49.89 ? 401 NAG A C5 1 HETATM 3307 C C6 . NAG D 3 . ? 0.836 23.078 8.675 1.00 48.60 ? 401 NAG A C6 1 HETATM 3308 C C7 . NAG D 3 . ? 2.753 28.993 11.035 1.00 55.98 ? 401 NAG A C7 1 HETATM 3309 C C8 . NAG D 3 . ? 2.500 30.291 11.753 1.00 60.15 ? 401 NAG A C8 1 HETATM 3310 N N2 . NAG D 3 . ? 1.676 28.226 10.917 1.00 53.29 ? 401 NAG A N2 1 HETATM 3311 O O3 . NAG D 3 . ? 0.021 27.935 8.794 1.00 57.49 ? 401 NAG A O3 1 HETATM 3312 O O4 . NAG D 3 . ? -0.803 25.325 8.037 1.00 52.68 ? 401 NAG A O4 1 HETATM 3313 O O5 . NAG D 3 . ? 2.107 24.606 10.089 1.00 48.66 ? 401 NAG A O5 1 HETATM 3314 O O6 . NAG D 3 . ? 1.990 23.128 7.851 1.00 44.76 ? 401 NAG A O6 1 HETATM 3315 O O7 . NAG D 3 . ? 3.886 28.694 10.626 1.00 54.64 ? 401 NAG A O7 1 HETATM 3316 C C1 . FUC E 4 . ? 1.784 22.397 6.630 1.00 46.19 ? 402 FUC A C1 1 HETATM 3317 C C2 . FUC E 4 . ? 3.049 22.494 5.813 1.00 45.93 ? 402 FUC A C2 1 HETATM 3318 C C3 . FUC E 4 . ? 4.211 21.686 6.383 1.00 44.48 ? 402 FUC A C3 1 HETATM 3319 C C4 . FUC E 4 . ? 3.782 20.278 6.604 1.00 47.27 ? 402 FUC A C4 1 HETATM 3320 C C5 . FUC E 4 . ? 2.543 20.368 7.496 1.00 46.43 ? 402 FUC A C5 1 HETATM 3321 C C6 . FUC E 4 . ? 2.019 18.999 7.849 1.00 48.59 ? 402 FUC A C6 1 HETATM 3322 O O2 . FUC E 4 . ? 3.444 23.847 5.892 1.00 48.31 ? 402 FUC A O2 1 HETATM 3323 O O3 . FUC E 4 . ? 5.329 21.712 5.546 1.00 43.27 ? 402 FUC A O3 1 HETATM 3324 O O4 . FUC E 4 . ? 3.608 19.596 5.354 1.00 47.58 ? 402 FUC A O4 1 HETATM 3325 O O5 . FUC E 4 . ? 1.491 21.047 6.866 1.00 47.58 ? 402 FUC A O5 1 HETATM 3326 C C1 . NAG F 3 . ? -0.769 -9.311 16.704 1.00 49.88 ? 411 NAG A C1 1 HETATM 3327 C C2 . NAG F 3 . ? -1.959 -10.309 16.803 1.00 55.32 ? 411 NAG A C2 1 HETATM 3328 C C3 . NAG F 3 . ? -3.043 -9.831 17.785 1.00 55.42 ? 411 NAG A C3 1 HETATM 3329 C C4 . NAG F 3 . ? -2.449 -9.623 19.168 1.00 56.24 ? 411 NAG A C4 1 HETATM 3330 C C5 . NAG F 3 . ? -1.413 -8.538 18.892 1.00 55.14 ? 411 NAG A C5 1 HETATM 3331 C C6 . NAG F 3 . ? -0.864 -7.925 20.169 1.00 57.76 ? 411 NAG A C6 1 HETATM 3332 C C7 . NAG F 3 . ? -2.220 -11.520 14.660 1.00 52.98 ? 411 NAG A C7 1 HETATM 3333 C C8 . NAG F 3 . ? -1.159 -12.467 15.143 1.00 52.64 ? 411 NAG A C8 1 HETATM 3334 N N2 . NAG F 3 . ? -2.608 -10.573 15.527 1.00 54.86 ? 411 NAG A N2 1 HETATM 3335 O O3 . NAG F 3 . ? -4.098 -10.749 17.827 1.00 59.16 ? 411 NAG A O3 1 HETATM 3336 O O4 . NAG F 3 . ? -3.412 -9.295 20.177 1.00 58.33 ? 411 NAG A O4 1 HETATM 3337 O O5 . NAG F 3 . ? -0.385 -9.055 18.059 1.00 51.00 ? 411 NAG A O5 1 HETATM 3338 O O6 . NAG F 3 . ? -0.695 -8.915 21.138 1.00 60.18 ? 411 NAG A O6 1 HETATM 3339 O O7 . NAG F 3 . ? -2.693 -11.597 13.512 1.00 50.80 ? 411 NAG A O7 1 HETATM 3340 C C1 . FUC G 4 . ? -0.285 -8.266 22.357 1.00 62.71 ? 412 FUC A C1 1 HETATM 3341 C C2 . FUC G 4 . ? -0.196 -9.294 23.474 1.00 63.62 ? 412 FUC A C2 1 HETATM 3342 C C3 . FUC G 4 . ? 0.668 -10.386 22.848 1.00 64.36 ? 412 FUC A C3 1 HETATM 3343 C C4 . FUC G 4 . ? 2.064 -9.769 22.793 1.00 63.28 ? 412 FUC A C4 1 HETATM 3344 C C5 . FUC G 4 . ? 2.034 -8.581 21.846 1.00 62.99 ? 412 FUC A C5 1 HETATM 3345 C C6 . FUC G 4 . ? 3.370 -7.842 21.913 1.00 61.29 ? 412 FUC A C6 1 HETATM 3346 O O2 . FUC G 4 . ? -1.485 -9.686 23.856 1.00 64.89 ? 412 FUC A O2 1 HETATM 3347 O O3 . FUC G 4 . ? 0.655 -11.642 23.502 1.00 66.18 ? 412 FUC A O3 1 HETATM 3348 O O4 . FUC G 4 . ? 2.435 -9.264 24.060 1.00 60.64 ? 412 FUC A O4 1 HETATM 3349 O O5 . FUC G 4 . ? 0.991 -7.680 22.208 1.00 63.33 ? 412 FUC A O5 1 HETATM 3350 O O3 . 151 H 2 . ? 19.078 -21.528 24.767 1.00 36.82 ? 400 151 B O3 1 HETATM 3351 C C2 . 151 H 2 . ? 18.448 -21.011 23.904 1.00 34.39 ? 400 151 B C2 1 HETATM 3352 N N1 . 151 H 2 . ? 18.881 -19.911 23.190 1.00 37.31 ? 400 151 B N1 1 HETATM 3353 C C26 . 151 H 2 . ? 18.035 -19.101 22.328 1.00 35.60 ? 400 151 B C26 1 HETATM 3354 C C28 . 151 H 2 . ? 18.838 -17.798 22.263 1.00 41.59 ? 400 151 B C28 1 HETATM 3355 C C29 . 151 H 2 . ? 19.952 -17.916 23.297 1.00 40.29 ? 400 151 B C29 1 HETATM 3356 N N2 . 151 H 2 . ? 19.283 -17.706 24.537 1.00 47.77 ? 400 151 B N2 1 HETATM 3357 S S1 . 151 H 2 . ? 20.113 -17.304 25.988 1.00 52.41 ? 400 151 B S1 1 HETATM 3358 C C3 . 151 H 2 . ? 19.099 -17.842 27.376 1.00 53.82 ? 400 151 B C3 1 HETATM 3359 O O1 . 151 H 2 . ? 21.506 -17.930 25.940 1.00 51.52 ? 400 151 B O1 1 HETATM 3360 O O2 . 151 H 2 . ? 20.157 -15.790 25.793 1.00 52.92 ? 400 151 B O2 1 HETATM 3361 C C8 . 151 H 2 . ? 20.240 -19.409 23.299 1.00 36.52 ? 400 151 B C8 1 HETATM 3362 C C7 . 151 H 2 . ? 21.053 -19.729 22.064 1.00 33.75 ? 400 151 B C7 1 HETATM 3363 C C27 . 151 H 2 . ? 21.369 -21.216 21.841 1.00 30.50 ? 400 151 B C27 1 HETATM 3364 C C1 . 151 H 2 . ? 22.175 -21.638 23.077 1.00 31.28 ? 400 151 B C1 1 HETATM 3365 C C17 . 151 H 2 . ? 22.285 -21.358 20.601 1.00 28.76 ? 400 151 B C17 1 HETATM 3366 C C30 . 151 H 2 . ? 22.312 -18.844 22.184 1.00 27.81 ? 400 151 B C30 1 HETATM 3367 O O5 . 151 H 2 . ? 23.294 -18.922 22.901 1.00 26.24 ? 400 151 B O5 1 HETATM 3368 C C4 . 151 H 2 . ? 17.195 -21.423 23.649 1.00 33.58 ? 400 151 B C4 1 HETATM 3369 N N3 . 151 H 2 . ? 16.753 -21.554 22.306 1.00 33.16 ? 400 151 B N3 1 HETATM 3370 C C5 . 151 H 2 . ? 15.404 -21.870 22.566 1.00 28.63 ? 400 151 B C5 1 HETATM 3371 O O4 . 151 H 2 . ? 15.050 -21.973 23.888 1.00 32.43 ? 400 151 B O4 1 HETATM 3372 C C6 . 151 H 2 . ? 16.171 -21.656 24.586 1.00 33.74 ? 400 151 B C6 1 HETATM 3373 C C9 . 151 H 2 . ? 14.537 -22.137 21.406 1.00 29.58 ? 400 151 B C9 1 HETATM 3374 N N4 . 151 H 2 . ? 13.478 -21.205 21.158 1.00 34.47 ? 400 151 B N4 1 HETATM 3375 C C11 . 151 H 2 . ? 13.896 -19.892 20.594 1.00 32.54 ? 400 151 B C11 1 HETATM 3376 C C13 . 151 H 2 . ? 13.558 -20.027 19.126 1.00 35.93 ? 400 151 B C13 1 HETATM 3377 C C14 . 151 H 2 . ? 12.317 -20.936 19.089 1.00 39.85 ? 400 151 B C14 1 HETATM 3378 C C12 . 151 H 2 . ? 12.387 -21.781 20.374 1.00 33.48 ? 400 151 B C12 1 HETATM 3379 C C1 . NAG I 3 . ? 36.426 -33.575 13.224 1.00 63.12 ? 401 NAG B C1 1 HETATM 3380 C C2 . NAG I 3 . ? 36.923 -34.849 12.526 1.00 69.02 ? 401 NAG B C2 1 HETATM 3381 C C3 . NAG I 3 . ? 38.362 -34.703 11.996 1.00 70.61 ? 401 NAG B C3 1 HETATM 3382 C C4 . NAG I 3 . ? 38.602 -33.401 11.216 1.00 70.39 ? 401 NAG B C4 1 HETATM 3383 C C5 . NAG I 3 . ? 37.924 -32.213 11.876 1.00 68.50 ? 401 NAG B C5 1 HETATM 3384 C C6 . NAG I 3 . ? 37.925 -31.040 10.888 1.00 69.13 ? 401 NAG B C6 1 HETATM 3385 C C7 . NAG I 3 . ? 35.873 -36.994 13.186 1.00 69.75 ? 401 NAG B C7 1 HETATM 3386 C C8 . NAG I 3 . ? 35.972 -38.177 14.110 1.00 69.45 ? 401 NAG B C8 1 HETATM 3387 N N2 . NAG I 3 . ? 36.826 -36.053 13.347 1.00 68.23 ? 401 NAG B N2 1 HETATM 3388 O O3 . NAG I 3 . ? 38.621 -35.780 11.119 1.00 72.98 ? 401 NAG B O3 1 HETATM 3389 O O4 . NAG I 3 . ? 39.987 -33.132 11.064 1.00 70.99 ? 401 NAG B O4 1 HETATM 3390 O O5 . NAG I 3 . ? 36.594 -32.570 12.224 1.00 66.77 ? 401 NAG B O5 1 HETATM 3391 O O6 . NAG I 3 . ? 36.810 -31.079 10.001 1.00 68.25 ? 401 NAG B O6 1 HETATM 3392 O O7 . NAG I 3 . ? 34.945 -36.948 12.360 1.00 66.72 ? 401 NAG B O7 1 HETATM 3393 C C1 . FUC J 4 . ? 37.077 -30.379 8.753 1.00 66.69 ? 402 FUC B C1 1 HETATM 3394 C C2 . FUC J 4 . ? 35.885 -30.402 7.785 1.00 66.77 ? 402 FUC B C2 1 HETATM 3395 C C3 . FUC J 4 . ? 34.781 -29.407 8.150 1.00 64.56 ? 402 FUC B C3 1 HETATM 3396 C C4 . FUC J 4 . ? 35.331 -28.012 8.381 1.00 65.09 ? 402 FUC B C4 1 HETATM 3397 C C5 . FUC J 4 . ? 36.537 -28.102 9.307 1.00 66.56 ? 402 FUC B C5 1 HETATM 3398 C C6 . FUC J 4 . ? 37.207 -26.749 9.428 1.00 67.73 ? 402 FUC B C6 1 HETATM 3399 O O2 . FUC J 4 . ? 35.322 -31.695 7.709 1.00 66.49 ? 402 FUC B O2 1 HETATM 3400 O O3 . FUC J 4 . ? 33.842 -29.375 7.106 1.00 62.52 ? 402 FUC B O3 1 HETATM 3401 O O4 . FUC J 4 . ? 35.671 -27.390 7.157 1.00 65.24 ? 402 FUC B O4 1 HETATM 3402 O O5 . FUC J 4 . ? 37.508 -29.034 8.868 1.00 68.37 ? 402 FUC B O5 1 HETATM 3403 C C1 . NAG K 3 . ? 38.082 1.230 18.822 1.00 50.74 ? 411 NAG B C1 1 HETATM 3404 C C2 . NAG K 3 . ? 39.315 2.155 18.958 1.00 55.00 ? 411 NAG B C2 1 HETATM 3405 C C3 . NAG K 3 . ? 40.313 1.739 20.057 1.00 55.60 ? 411 NAG B C3 1 HETATM 3406 C C4 . NAG K 3 . ? 39.569 1.556 21.364 1.00 57.41 ? 411 NAG B C4 1 HETATM 3407 C C5 . NAG K 3 . ? 38.558 0.453 21.079 1.00 55.65 ? 411 NAG B C5 1 HETATM 3408 C C6 . NAG K 3 . ? 37.795 0.063 22.335 1.00 58.61 ? 411 NAG B C6 1 HETATM 3409 C C7 . NAG K 3 . ? 39.989 3.360 16.890 1.00 57.96 ? 411 NAG B C7 1 HETATM 3410 C C8 . NAG K 3 . ? 38.984 4.430 17.202 1.00 57.79 ? 411 NAG B C8 1 HETATM 3411 N N2 . NAG K 3 . ? 39.987 2.270 17.674 1.00 55.17 ? 411 NAG B N2 1 HETATM 3412 O O3 . NAG K 3 . ? 41.247 2.748 20.306 1.00 56.02 ? 411 NAG B O3 1 HETATM 3413 O O4 . NAG K 3 . ? 40.458 1.320 22.460 1.00 58.85 ? 411 NAG B O4 1 HETATM 3414 O O5 . NAG K 3 . ? 37.616 0.877 20.101 1.00 51.66 ? 411 NAG B O5 1 HETATM 3415 O O6 . NAG K 3 . ? 37.436 1.181 23.098 1.00 61.62 ? 411 NAG B O6 1 HETATM 3416 O O7 . NAG K 3 . ? 40.779 3.501 15.926 1.00 58.72 ? 411 NAG B O7 1 HETATM 3417 C C1 . FUC L 4 . ? 37.324 0.676 24.427 1.00 66.77 ? 412 FUC B C1 1 HETATM 3418 C C2 . FUC L 4 . ? 37.111 1.826 25.392 1.00 67.70 ? 412 FUC B C2 1 HETATM 3419 C C3 . FUC L 4 . ? 36.093 2.695 24.683 1.00 68.86 ? 412 FUC B C3 1 HETATM 3420 C C4 . FUC L 4 . ? 34.825 1.846 24.598 1.00 69.48 ? 412 FUC B C4 1 HETATM 3421 C C5 . FUC L 4 . ? 35.105 0.556 23.824 1.00 69.37 ? 412 FUC B C5 1 HETATM 3422 C C6 . FUC L 4 . ? 33.871 -0.349 23.773 1.00 69.82 ? 412 FUC B C6 1 HETATM 3423 O O2 . FUC L 4 . ? 38.332 2.483 25.615 1.00 71.28 ? 412 FUC B O2 1 HETATM 3424 O O3 . FUC L 4 . ? 35.829 3.902 25.351 1.00 70.26 ? 412 FUC B O3 1 HETATM 3425 O O4 . FUC L 4 . ? 34.379 1.492 25.891 1.00 68.35 ? 412 FUC B O4 1 HETATM 3426 O O5 . FUC L 4 . ? 36.183 -0.139 24.424 1.00 68.83 ? 412 FUC B O5 1 HETATM 3427 O O . HOH M 5 . ? 4.340 15.994 23.315 1.00 29.54 ? 2001 HOH A O 1 HETATM 3428 O O . HOH M 5 . ? 4.604 22.688 26.128 1.00 38.98 ? 2002 HOH A O 1 HETATM 3429 O O . HOH M 5 . ? 2.581 26.188 19.149 1.00 44.64 ? 2003 HOH A O 1 HETATM 3430 O O . HOH M 5 . ? -3.399 23.316 22.815 1.00 55.26 ? 2004 HOH A O 1 HETATM 3431 O O . HOH M 5 . ? -3.577 21.642 16.616 1.00 52.18 ? 2005 HOH A O 1 HETATM 3432 O O . HOH M 5 . ? -4.130 19.254 14.397 1.00 44.61 ? 2006 HOH A O 1 HETATM 3433 O O . HOH M 5 . ? -4.399 20.103 10.105 1.00 49.38 ? 2007 HOH A O 1 HETATM 3434 O O . HOH M 5 . ? -3.208 14.181 7.703 1.00 45.85 ? 2008 HOH A O 1 HETATM 3435 O O . HOH M 5 . ? -4.610 16.919 9.299 1.00 45.91 ? 2009 HOH A O 1 HETATM 3436 O O . HOH M 5 . ? -3.660 11.698 14.498 1.00 41.32 ? 2010 HOH A O 1 HETATM 3437 O O . HOH M 5 . ? 8.218 1.167 30.562 1.00 51.73 ? 2011 HOH A O 1 HETATM 3438 O O . HOH M 5 . ? 10.952 1.866 27.355 1.00 38.83 ? 2012 HOH A O 1 HETATM 3439 O O . HOH M 5 . ? -1.229 -8.290 28.775 1.00 58.64 ? 2013 HOH A O 1 HETATM 3440 O O . HOH M 5 . ? 14.968 4.953 23.800 1.00 52.11 ? 2014 HOH A O 1 HETATM 3441 O O . HOH M 5 . ? 14.031 7.253 22.945 1.00 32.23 ? 2015 HOH A O 1 HETATM 3442 O O . HOH M 5 . ? 20.605 -1.531 18.663 1.00 42.57 ? 2016 HOH A O 1 HETATM 3443 O O . HOH M 5 . ? -4.831 -0.083 0.773 1.00 96.40 ? 2017 HOH A O 1 HETATM 3444 O O . HOH M 5 . ? 8.236 2.673 28.446 1.00 43.72 ? 2018 HOH A O 1 HETATM 3445 O O . HOH M 5 . ? 4.014 -11.307 18.898 1.00 42.29 ? 2019 HOH A O 1 HETATM 3446 O O . HOH M 5 . ? 5.868 5.206 29.660 0.50 45.01 ? 2020 HOH A O 1 HETATM 3447 O O . HOH M 5 . ? 7.972 7.186 29.670 0.50 31.95 ? 2021 HOH A O 1 HETATM 3448 O O . HOH M 5 . ? 8.659 5.161 28.740 1.00 33.60 ? 2022 HOH A O 1 HETATM 3449 O O . HOH M 5 . ? 1.436 5.520 28.010 1.00 47.12 ? 2023 HOH A O 1 HETATM 3450 O O . HOH M 5 . ? 5.256 7.308 28.434 1.00 51.87 ? 2024 HOH A O 1 HETATM 3451 O O . HOH M 5 . ? 8.469 7.607 12.050 1.00 27.73 ? 2025 HOH A O 1 HETATM 3452 O O . HOH M 5 . ? 4.895 4.835 2.746 1.00 38.51 ? 2026 HOH A O 1 HETATM 3453 O O . HOH M 5 . ? 4.666 -7.719 3.071 1.00 50.38 ? 2027 HOH A O 1 HETATM 3454 O O . HOH M 5 . ? 31.741 11.081 12.498 1.00 48.72 ? 2028 HOH A O 1 HETATM 3455 O O . HOH M 5 . ? 15.806 6.944 20.848 1.00 29.49 ? 2029 HOH A O 1 HETATM 3456 O O . HOH M 5 . ? 20.186 -3.256 20.720 1.00 35.54 ? 2030 HOH A O 1 HETATM 3457 O O . HOH M 5 . ? 16.434 2.000 23.681 1.00 42.57 ? 2031 HOH A O 1 HETATM 3458 O O . HOH M 5 . ? 16.029 0.917 28.175 1.00 45.14 ? 2032 HOH A O 1 HETATM 3459 O O . HOH M 5 . ? 6.506 -6.902 19.550 1.00 30.42 ? 2033 HOH A O 1 HETATM 3460 O O . HOH M 5 . ? 12.391 -4.213 27.792 1.00 32.41 ? 2034 HOH A O 1 HETATM 3461 O O . HOH M 5 . ? 10.499 -7.888 29.038 1.00 50.82 ? 2035 HOH A O 1 HETATM 3462 O O . HOH M 5 . ? -4.316 3.098 1.210 1.00 64.19 ? 2036 HOH A O 1 HETATM 3463 O O . HOH M 5 . ? 5.510 -10.571 20.666 1.00 44.20 ? 2037 HOH A O 1 HETATM 3464 O O . HOH M 5 . ? -2.421 5.617 13.513 1.00 34.75 ? 2038 HOH A O 1 HETATM 3465 O O . HOH M 5 . ? -2.889 8.584 15.461 1.00 37.42 ? 2039 HOH A O 1 HETATM 3466 O O . HOH M 5 . ? -4.525 11.458 16.804 1.00 41.50 ? 2040 HOH A O 1 HETATM 3467 O O . HOH M 5 . ? -1.614 5.805 17.232 1.00 35.52 ? 2041 HOH A O 1 HETATM 3468 O O . HOH M 5 . ? -6.576 14.391 29.311 1.00 48.60 ? 2042 HOH A O 1 HETATM 3469 O O . HOH M 5 . ? -8.444 5.623 31.760 1.00 58.17 ? 2043 HOH A O 1 HETATM 3470 O O . HOH M 5 . ? -9.204 14.339 24.322 1.00 55.93 ? 2044 HOH A O 1 HETATM 3471 O O . HOH M 5 . ? -11.418 6.108 29.783 1.00 62.29 ? 2045 HOH A O 1 HETATM 3472 O O . HOH M 5 . ? 27.984 14.742 8.263 1.00 48.93 ? 2046 HOH A O 1 HETATM 3473 O O . HOH M 5 . ? -9.704 1.839 14.169 1.00 43.27 ? 2047 HOH A O 1 HETATM 3474 O O . HOH M 5 . ? -3.793 0.697 23.407 1.00 48.13 ? 2048 HOH A O 1 HETATM 3475 O O . HOH M 5 . ? -6.745 -4.085 13.532 1.00 43.65 ? 2049 HOH A O 1 HETATM 3476 O O . HOH M 5 . ? -6.542 -4.456 18.300 1.00 45.59 ? 2050 HOH A O 1 HETATM 3477 O O . HOH M 5 . ? 6.863 -9.349 18.886 1.00 33.23 ? 2051 HOH A O 1 HETATM 3478 O O . HOH M 5 . ? 4.857 -10.883 16.058 1.00 36.87 ? 2052 HOH A O 1 HETATM 3479 O O . HOH M 5 . ? 5.260 -14.585 7.869 1.00 54.82 ? 2053 HOH A O 1 HETATM 3480 O O . HOH M 5 . ? 4.670 -12.946 14.574 1.00 41.21 ? 2054 HOH A O 1 HETATM 3481 O O . HOH M 5 . ? 12.110 -10.437 4.851 1.00 63.27 ? 2055 HOH A O 1 HETATM 3482 O O . HOH M 5 . ? 20.511 -3.236 16.651 1.00 41.96 ? 2056 HOH A O 1 HETATM 3483 O O . HOH M 5 . ? 18.192 -0.885 17.497 1.00 32.47 ? 2057 HOH A O 1 HETATM 3484 O O . HOH M 5 . ? 20.055 -3.827 6.009 1.00 43.15 ? 2058 HOH A O 1 HETATM 3485 O O . HOH M 5 . ? 20.762 1.260 1.501 1.00 57.03 ? 2059 HOH A O 1 HETATM 3486 O O . HOH M 5 . ? 17.849 25.257 28.908 1.00 51.97 ? 2060 HOH A O 1 HETATM 3487 O O . HOH M 5 . ? 25.485 2.051 5.138 1.00 47.55 ? 2061 HOH A O 1 HETATM 3488 O O . HOH M 5 . ? 21.627 2.400 20.838 1.00 38.64 ? 2062 HOH A O 1 HETATM 3489 O O . HOH M 5 . ? 30.661 6.689 15.255 1.00 34.94 ? 2063 HOH A O 1 HETATM 3490 O O . HOH M 5 . ? 23.200 4.330 21.671 1.00 44.31 ? 2064 HOH A O 1 HETATM 3491 O O . HOH M 5 . ? 28.634 12.403 12.058 1.00 64.80 ? 2065 HOH A O 1 HETATM 3492 O O . HOH M 5 . ? 20.426 10.820 13.642 1.00 28.91 ? 2066 HOH A O 1 HETATM 3493 O O . HOH M 5 . ? 31.132 8.836 11.684 1.00 53.01 ? 2067 HOH A O 1 HETATM 3494 O O . HOH M 5 . ? 19.817 9.468 11.392 1.00 29.27 ? 2068 HOH A O 1 HETATM 3495 O O . HOH M 5 . ? 19.444 1.799 10.464 1.00 25.50 ? 2069 HOH A O 1 HETATM 3496 O O . HOH M 5 . ? 3.370 -8.680 7.827 1.00 46.05 ? 2070 HOH A O 1 HETATM 3497 O O . HOH M 5 . ? 9.704 -9.460 4.952 1.00 48.76 ? 2071 HOH A O 1 HETATM 3498 O O . HOH M 5 . ? -6.937 -1.998 4.790 1.00 49.91 ? 2072 HOH A O 1 HETATM 3499 O O . HOH M 5 . ? -12.648 0.829 10.211 1.00 50.70 ? 2073 HOH A O 1 HETATM 3500 O O . HOH M 5 . ? -13.839 5.924 7.588 1.00 51.26 ? 2074 HOH A O 1 HETATM 3501 O O . HOH M 5 . ? -5.331 8.443 14.363 1.00 34.97 ? 2075 HOH A O 1 HETATM 3502 O O . HOH M 5 . ? -11.095 7.309 5.136 1.00 47.47 ? 2076 HOH A O 1 HETATM 3503 O O . HOH M 5 . ? -4.002 4.830 3.923 1.00 43.78 ? 2077 HOH A O 1 HETATM 3504 O O . HOH M 5 . ? 17.376 4.290 0.230 1.00 38.81 ? 2078 HOH A O 1 HETATM 3505 O O . HOH M 5 . ? 13.408 18.409 -2.598 1.00 52.82 ? 2079 HOH A O 1 HETATM 3506 O O . HOH M 5 . ? 18.780 16.715 4.396 1.00 49.04 ? 2080 HOH A O 1 HETATM 3507 O O . HOH M 5 . ? 16.282 17.738 -4.039 1.00 51.67 ? 2081 HOH A O 1 HETATM 3508 O O . HOH M 5 . ? 19.983 28.334 8.845 1.00 51.45 ? 2082 HOH A O 1 HETATM 3509 O O . HOH M 5 . ? 10.990 30.030 6.445 1.00 54.39 ? 2083 HOH A O 1 HETATM 3510 O O . HOH M 5 . ? 6.204 25.387 10.331 1.00 39.84 ? 2084 HOH A O 1 HETATM 3511 O O . HOH M 5 . ? 10.082 24.069 29.461 1.00 57.28 ? 2085 HOH A O 1 HETATM 3512 O O . HOH M 5 . ? 16.458 18.281 28.637 1.00 38.74 ? 2086 HOH A O 1 HETATM 3513 O O . HOH M 5 . ? -1.961 13.068 31.388 1.00 40.04 ? 2087 HOH A O 1 HETATM 3514 O O . HOH M 5 . ? 3.390 21.092 23.609 1.00 33.90 ? 2088 HOH A O 1 HETATM 3515 O O . HOH M 5 . ? 4.185 25.907 16.461 1.00 42.45 ? 2089 HOH A O 1 HETATM 3516 O O . HOH M 5 . ? 9.732 28.048 13.339 1.00 46.59 ? 2090 HOH A O 1 HETATM 3517 O O . HOH M 5 . ? 18.724 20.185 7.541 1.00 34.59 ? 2091 HOH A O 1 HETATM 3518 O O . HOH M 5 . ? 20.964 26.776 13.259 1.00 51.55 ? 2092 HOH A O 1 HETATM 3519 O O . HOH M 5 . ? 22.792 17.000 12.971 1.00 29.08 ? 2093 HOH A O 1 HETATM 3520 O O . HOH M 5 . ? 23.249 11.672 11.719 1.00 38.89 ? 2094 HOH A O 1 HETATM 3521 O O . HOH M 5 . ? 20.820 14.698 5.463 1.00 55.51 ? 2095 HOH A O 1 HETATM 3522 O O . HOH M 5 . ? 21.776 9.742 9.400 1.00 29.76 ? 2096 HOH A O 1 HETATM 3523 O O . HOH M 5 . ? 27.519 12.528 9.473 1.00 46.85 ? 2097 HOH A O 1 HETATM 3524 O O . HOH M 5 . ? 21.133 19.148 7.112 1.00 30.53 ? 2098 HOH A O 1 HETATM 3525 O O . HOH M 5 . ? 12.574 21.834 16.375 1.00 29.91 ? 2099 HOH A O 1 HETATM 3526 O O . HOH M 5 . ? 13.242 24.002 17.885 1.00 30.04 ? 2100 HOH A O 1 HETATM 3527 O O . HOH M 5 . ? 18.390 29.043 12.437 1.00 47.68 ? 2101 HOH A O 1 HETATM 3528 O O . HOH M 5 . ? 13.142 31.213 7.993 1.00 46.74 ? 2102 HOH A O 1 HETATM 3529 O O . HOH M 5 . ? 6.702 29.478 23.996 1.00 53.59 ? 2103 HOH A O 1 HETATM 3530 O O . HOH M 5 . ? 13.586 27.191 20.136 1.00 40.57 ? 2104 HOH A O 1 HETATM 3531 O O . HOH M 5 . ? 10.869 31.010 25.128 1.00 41.91 ? 2105 HOH A O 1 HETATM 3532 O O . HOH M 5 . ? 11.516 8.771 23.144 1.00 35.39 ? 2106 HOH A O 1 HETATM 3533 O O . HOH M 5 . ? 5.856 10.186 20.175 1.00 24.76 ? 2107 HOH A O 1 HETATM 3534 O O . HOH M 5 . ? 8.410 14.892 15.354 1.00 25.54 ? 2108 HOH A O 1 HETATM 3535 O O . HOH M 5 . ? 1.840 11.984 4.743 1.00 45.56 ? 2109 HOH A O 1 HETATM 3536 O O . HOH M 5 . ? 14.286 13.359 4.052 1.00 28.44 ? 2110 HOH A O 1 HETATM 3537 O O . HOH M 5 . ? 13.943 15.419 2.977 1.00 46.27 ? 2111 HOH A O 1 HETATM 3538 O O . HOH M 5 . ? 16.534 8.278 18.826 1.00 23.73 ? 2112 HOH A O 1 HETATM 3539 O O . HOH M 5 . ? 23.905 17.929 15.245 1.00 47.06 ? 2113 HOH A O 1 HETATM 3540 O O . HOH M 5 . ? 21.423 24.306 26.439 1.00 39.12 ? 2114 HOH A O 1 HETATM 3541 O O . HOH M 5 . ? 24.824 17.713 24.725 1.00 45.06 ? 2115 HOH A O 1 HETATM 3542 O O . HOH M 5 . ? 20.428 17.301 25.020 1.00 32.43 ? 2116 HOH A O 1 HETATM 3543 O O . HOH M 5 . ? 17.453 21.848 22.375 1.00 26.57 ? 2117 HOH A O 1 HETATM 3544 O O . HOH M 5 . ? 14.016 21.551 28.595 1.00 45.92 ? 2118 HOH A O 1 HETATM 3545 O O . HOH M 5 . ? 17.323 22.749 27.202 1.00 32.77 ? 2119 HOH A O 1 HETATM 3546 O O . HOH M 5 . ? 19.846 26.570 26.802 1.00 40.14 ? 2120 HOH A O 1 HETATM 3547 O O . HOH M 5 . ? 15.168 24.749 20.966 1.00 30.36 ? 2121 HOH A O 1 HETATM 3548 O O . HOH M 5 . ? 16.341 30.061 18.929 1.00 32.01 ? 2122 HOH A O 1 HETATM 3549 O O . HOH M 5 . ? 21.727 29.024 17.586 1.00 44.02 ? 2123 HOH A O 1 HETATM 3550 O O . HOH M 5 . ? 15.655 22.882 19.089 1.00 28.11 ? 2124 HOH A O 1 HETATM 3551 O O . HOH M 5 . ? 20.158 18.160 17.637 1.00 38.21 ? 2125 HOH A O 1 HETATM 3552 O O . HOH M 5 . ? 17.437 20.267 19.697 1.00 29.94 ? 2126 HOH A O 1 HETATM 3553 O O . HOH M 5 . ? 14.361 20.197 21.663 1.00 21.84 ? 2127 HOH A O 1 HETATM 3554 O O . HOH M 5 . ? 18.160 6.694 -6.928 1.00 51.58 ? 2128 HOH A O 1 HETATM 3555 O O . HOH M 5 . ? 17.988 -4.246 5.707 1.00 31.62 ? 2129 HOH A O 1 HETATM 3556 O O . HOH M 5 . ? 8.010 4.821 -0.323 1.00 58.51 ? 2130 HOH A O 1 HETATM 3557 O O . HOH M 5 . ? 11.890 -6.040 -2.748 1.00 41.47 ? 2131 HOH A O 1 HETATM 3558 O O . HOH M 5 . ? 5.817 -6.967 -5.063 1.00 50.37 ? 2132 HOH A O 1 HETATM 3559 O O . HOH M 5 . ? 6.279 -7.009 1.330 1.00 51.64 ? 2133 HOH A O 1 HETATM 3560 O O . HOH M 5 . ? 15.235 13.913 26.348 1.00 38.48 ? 2134 HOH A O 1 HETATM 3561 O O . HOH M 5 . ? 25.173 11.062 24.083 1.00 50.37 ? 2135 HOH A O 1 HETATM 3562 O O . HOH M 5 . ? 17.558 14.672 26.319 1.00 46.85 ? 2136 HOH A O 1 HETATM 3563 O O . HOH M 5 . ? -4.212 -7.899 21.877 1.00 59.98 ? 2137 HOH A O 1 HETATM 3564 O O . HOH M 5 . ? 1.567 -11.436 18.871 1.00 42.54 ? 2138 HOH A O 1 HETATM 3565 O O . HOH N 5 . ? 33.238 -29.037 25.307 1.00 39.18 ? 2001 HOH B O 1 HETATM 3566 O O . HOH N 5 . ? 49.607 -19.461 17.562 1.00 56.33 ? 2002 HOH B O 1 HETATM 3567 O O . HOH N 5 . ? 41.230 -19.628 16.861 1.00 56.24 ? 2003 HOH B O 1 HETATM 3568 O O . HOH N 5 . ? 38.725 -14.058 19.141 1.00 45.88 ? 2004 HOH B O 1 HETATM 3569 O O . HOH N 5 . ? 23.250 -11.194 27.065 1.00 42.13 ? 2005 HOH B O 1 HETATM 3570 O O . HOH N 5 . ? 17.966 -3.755 18.437 1.00 48.19 ? 2006 HOH B O 1 HETATM 3571 O O . HOH N 5 . ? 13.372 -7.956 29.897 1.00 56.80 ? 2007 HOH B O 1 HETATM 3572 O O . HOH N 5 . ? 22.495 -0.098 19.860 1.00 40.64 ? 2008 HOH B O 1 HETATM 3573 O O . HOH N 5 . ? 33.487 3.713 20.587 1.00 51.40 ? 2009 HOH B O 1 HETATM 3574 O O . HOH N 5 . ? 34.400 -14.138 29.847 1.00 45.67 ? 2010 HOH B O 1 HETATM 3575 O O . HOH N 5 . ? 33.612 -12.777 3.455 1.00 52.04 ? 2011 HOH B O 1 HETATM 3576 O O . HOH N 5 . ? 31.176 3.552 5.184 1.00 53.42 ? 2012 HOH B O 1 HETATM 3577 O O . HOH N 5 . ? 35.529 -1.503 4.621 1.00 50.98 ? 2013 HOH B O 1 HETATM 3578 O O . HOH N 5 . ? 35.178 0.667 9.817 1.00 37.94 ? 2014 HOH B O 1 HETATM 3579 O O . HOH N 5 . ? 13.622 -9.982 0.409 1.00 58.33 ? 2015 HOH B O 1 HETATM 3580 O O . HOH N 5 . ? 19.377 -7.312 17.532 1.00 31.44 ? 2016 HOH B O 1 HETATM 3581 O O . HOH N 5 . ? 21.077 -14.775 21.097 1.00 45.09 ? 2017 HOH B O 1 HETATM 3582 O O . HOH N 5 . ? 23.208 -11.082 24.337 1.00 42.63 ? 2018 HOH B O 1 HETATM 3583 O O . HOH N 5 . ? 16.967 -4.863 20.664 1.00 35.62 ? 2019 HOH B O 1 HETATM 3584 O O . HOH N 5 . ? 14.123 -6.138 29.462 1.00 47.14 ? 2020 HOH B O 1 HETATM 3585 O O . HOH N 5 . ? 19.442 -8.729 26.843 1.00 41.11 ? 2021 HOH B O 1 HETATM 3586 O O . HOH N 5 . ? 23.621 -4.303 28.422 1.00 39.54 ? 2022 HOH B O 1 HETATM 3587 O O . HOH N 5 . ? 21.935 -0.547 22.582 1.00 48.52 ? 2023 HOH B O 1 HETATM 3588 O O . HOH N 5 . ? 28.045 3.142 27.323 1.00 60.04 ? 2024 HOH B O 1 HETATM 3589 O O . HOH N 5 . ? 26.367 10.074 22.564 1.00 70.91 ? 2025 HOH B O 1 HETATM 3590 O O . HOH N 5 . ? 31.487 2.809 22.253 1.00 52.36 ? 2026 HOH B O 1 HETATM 3591 O O . HOH N 5 . ? 22.148 7.752 22.819 1.00 57.30 ? 2027 HOH B O 1 HETATM 3592 O O . HOH N 5 . ? 30.485 -1.318 21.057 1.00 35.74 ? 2028 HOH B O 1 HETATM 3593 O O . HOH N 5 . ? 40.020 -13.641 15.999 1.00 51.20 ? 2029 HOH B O 1 HETATM 3594 O O . HOH N 5 . ? 40.431 -16.749 18.095 1.00 45.88 ? 2030 HOH B O 1 HETATM 3595 O O . HOH N 5 . ? 41.893 -19.598 19.112 1.00 59.60 ? 2031 HOH B O 1 HETATM 3596 O O . HOH N 5 . ? 49.201 -6.908 31.953 1.00 53.77 ? 2032 HOH B O 1 HETATM 3597 O O . HOH N 5 . ? 48.377 -15.163 23.945 1.00 55.05 ? 2033 HOH B O 1 HETATM 3598 O O . HOH N 5 . ? 26.681 -42.144 8.842 1.00 49.42 ? 2034 HOH B O 1 HETATM 3599 O O . HOH N 5 . ? 19.614 -33.540 28.869 1.00 49.81 ? 2035 HOH B O 1 HETATM 3600 O O . HOH N 5 . ? 30.018 1.282 20.165 1.00 36.24 ? 2036 HOH B O 1 HETATM 3601 O O . HOH N 5 . ? 32.622 4.842 16.163 1.00 39.67 ? 2037 HOH B O 1 HETATM 3602 O O . HOH N 5 . ? 31.956 4.373 7.368 1.00 58.36 ? 2038 HOH B O 1 HETATM 3603 O O . HOH N 5 . ? 28.565 5.145 4.454 1.00 59.27 ? 2039 HOH B O 1 HETATM 3604 O O . HOH N 5 . ? 16.942 -4.613 16.455 1.00 37.29 ? 2040 HOH B O 1 HETATM 3605 O O . HOH N 5 . ? 17.340 -9.601 1.225 1.00 45.17 ? 2041 HOH B O 1 HETATM 3606 O O . HOH N 5 . ? 12.757 -32.306 26.048 1.00 44.95 ? 2042 HOH B O 1 HETATM 3607 O O . HOH N 5 . ? 15.290 -10.462 20.277 1.00 39.77 ? 2043 HOH B O 1 HETATM 3608 O O . HOH N 5 . ? 6.884 -14.365 13.909 1.00 45.38 ? 2044 HOH B O 1 HETATM 3609 O O . HOH N 5 . ? 13.204 -12.139 21.160 1.00 41.28 ? 2045 HOH B O 1 HETATM 3610 O O . HOH N 5 . ? 17.035 -19.089 13.609 1.00 31.14 ? 2046 HOH B O 1 HETATM 3611 O O . HOH N 5 . ? 36.345 -0.998 -1.800 1.00 51.22 ? 2047 HOH B O 1 HETATM 3612 O O . HOH N 5 . ? 20.483 -16.277 19.097 1.00 32.24 ? 2048 HOH B O 1 HETATM 3613 O O . HOH N 5 . ? 18.608 -17.477 11.417 1.00 28.83 ? 2049 HOH B O 1 HETATM 3614 O O . HOH N 5 . ? 18.846 -10.006 10.501 1.00 23.08 ? 2050 HOH B O 1 HETATM 3615 O O . HOH N 5 . ? 30.355 0.917 5.977 1.00 50.72 ? 2051 HOH B O 1 HETATM 3616 O O . HOH N 5 . ? 39.046 4.043 12.306 1.00 55.66 ? 2052 HOH B O 1 HETATM 3617 O O . HOH N 5 . ? 42.374 0.844 12.356 1.00 64.46 ? 2053 HOH B O 1 HETATM 3618 O O . HOH N 5 . ? 50.378 -8.234 13.293 1.00 55.41 ? 2054 HOH B O 1 HETATM 3619 O O . HOH N 5 . ? 42.912 -16.648 16.606 1.00 45.85 ? 2055 HOH B O 1 HETATM 3620 O O . HOH N 5 . ? 48.384 -14.520 7.037 1.00 51.73 ? 2056 HOH B O 1 HETATM 3621 O O . HOH N 5 . ? 35.427 -15.620 0.149 1.00 51.61 ? 2057 HOH B O 1 HETATM 3622 O O . HOH N 5 . ? 37.446 -14.289 2.244 1.00 45.04 ? 2058 HOH B O 1 HETATM 3623 O O . HOH N 5 . ? 25.246 -17.543 -6.258 1.00 58.00 ? 2059 HOH B O 1 HETATM 3624 O O . HOH N 5 . ? 22.970 -17.515 -5.988 1.00 58.86 ? 2060 HOH B O 1 HETATM 3625 O O . HOH N 5 . ? 21.164 -27.657 5.346 1.00 40.93 ? 2061 HOH B O 1 HETATM 3626 O O . HOH N 5 . ? 18.236 -36.269 8.781 1.00 42.34 ? 2062 HOH B O 1 HETATM 3627 O O . HOH N 5 . ? 29.364 -22.991 16.550 1.00 26.06 ? 2063 HOH B O 1 HETATM 3628 O O . HOH N 5 . ? 32.802 -23.871 24.987 1.00 44.59 ? 2064 HOH B O 1 HETATM 3629 O O . HOH N 5 . ? 36.590 -29.907 27.624 1.00 51.46 ? 2065 HOH B O 1 HETATM 3630 O O . HOH N 5 . ? 27.942 -36.809 14.463 1.00 51.99 ? 2066 HOH B O 1 HETATM 3631 O O . HOH N 5 . ? 19.793 -28.202 7.947 1.00 32.28 ? 2067 HOH B O 1 HETATM 3632 O O . HOH N 5 . ? 16.058 -17.771 9.009 1.00 33.16 ? 2068 HOH B O 1 HETATM 3633 O O . HOH N 5 . ? 14.951 -25.038 12.706 1.00 28.89 ? 2069 HOH B O 1 HETATM 3634 O O . HOH N 5 . ? 17.493 -27.394 7.157 1.00 38.84 ? 2070 HOH B O 1 HETATM 3635 O O . HOH N 5 . ? 25.141 -29.755 17.007 1.00 30.88 ? 2071 HOH B O 1 HETATM 3636 O O . HOH N 5 . ? 19.144 -36.804 12.154 1.00 52.40 ? 2072 HOH B O 1 HETATM 3637 O O . HOH N 5 . ? 25.162 -38.927 8.295 1.00 56.52 ? 2073 HOH B O 1 HETATM 3638 O O . HOH N 5 . ? 18.679 -38.376 14.434 1.00 46.54 ? 2074 HOH B O 1 HETATM 3639 O O . HOH N 5 . ? 21.266 -39.633 14.803 1.00 50.11 ? 2075 HOH B O 1 HETATM 3640 O O . HOH N 5 . ? 20.550 -37.312 9.622 1.00 39.54 ? 2076 HOH B O 1 HETATM 3641 O O . HOH N 5 . ? 19.534 -36.501 30.178 1.00 58.49 ? 2077 HOH B O 1 HETATM 3642 O O . HOH N 5 . ? 23.909 -31.856 18.811 1.00 34.95 ? 2078 HOH B O 1 HETATM 3643 O O . HOH N 5 . ? 22.158 -32.773 21.511 1.00 36.84 ? 2079 HOH B O 1 HETATM 3644 O O . HOH N 5 . ? 22.818 -28.275 22.205 1.00 26.98 ? 2080 HOH B O 1 HETATM 3645 O O . HOH N 5 . ? 30.927 -18.354 21.663 1.00 40.43 ? 2081 HOH B O 1 HETATM 3646 O O . HOH N 5 . ? 29.366 -15.835 13.324 1.00 30.20 ? 2082 HOH B O 1 HETATM 3647 O O . HOH N 5 . ? 24.320 -21.424 4.721 1.00 38.53 ? 2083 HOH B O 1 HETATM 3648 O O . HOH N 5 . ? 14.713 -26.427 14.798 1.00 44.93 ? 2084 HOH B O 1 HETATM 3649 O O . HOH N 5 . ? 18.930 -30.679 27.499 1.00 32.39 ? 2085 HOH B O 1 HETATM 3650 O O . HOH N 5 . ? 15.118 -32.383 26.355 1.00 34.42 ? 2086 HOH B O 1 HETATM 3651 O O . HOH N 5 . ? 15.741 -25.034 24.767 1.00 31.66 ? 2087 HOH B O 1 HETATM 3652 O O . HOH N 5 . ? 20.387 -26.933 29.218 1.00 45.06 ? 2088 HOH B O 1 HETATM 3653 O O . HOH N 5 . ? 19.526 -29.980 22.141 1.00 26.04 ? 2089 HOH B O 1 HETATM 3654 O O . HOH N 5 . ? 18.410 -38.155 24.296 1.00 53.65 ? 2090 HOH B O 1 HETATM 3655 O O . HOH N 5 . ? 20.649 -37.997 19.114 1.00 36.33 ? 2091 HOH B O 1 HETATM 3656 O O . HOH N 5 . ? 17.654 -37.513 17.314 1.00 40.01 ? 2092 HOH B O 1 HETATM 3657 O O . HOH N 5 . ? 17.164 -34.654 26.892 1.00 43.24 ? 2093 HOH B O 1 HETATM 3658 O O . HOH N 5 . ? 16.827 -34.940 16.167 1.00 41.87 ? 2094 HOH B O 1 HETATM 3659 O O . HOH N 5 . ? 19.381 -28.361 20.116 1.00 27.34 ? 2095 HOH B O 1 HETATM 3660 O O . HOH N 5 . ? 21.714 -30.913 19.397 1.00 28.32 ? 2096 HOH B O 1 HETATM 3661 O O . HOH N 5 . ? 21.212 -12.217 1.222 1.00 71.16 ? 2097 HOH B O 1 HETATM 3662 O O . HOH N 5 . ? 25.941 -8.144 -3.466 1.00 45.57 ? 2098 HOH B O 1 HETATM 3663 O O . HOH N 5 . ? 26.826 -12.214 -3.323 1.00 49.15 ? 2099 HOH B O 1 HETATM 3664 O O . HOH N 5 . ? 32.289 -12.393 -0.279 1.00 53.95 ? 2100 HOH B O 1 HETATM 3665 O O . HOH N 5 . ? 28.356 -7.139 -3.176 1.00 41.42 ? 2101 HOH B O 1 HETATM 3666 O O . HOH N 5 . ? 28.574 -0.524 3.963 1.00 54.24 ? 2102 HOH B O 1 HETATM 3667 O O . HOH N 5 . ? 34.379 -1.501 -2.557 1.00 50.50 ? 2103 HOH B O 1 HETATM 3668 O O . HOH N 5 . ? 13.408 -24.949 25.177 1.00 41.78 ? 2104 HOH B O 1 HETATM 3669 O O . HOH N 5 . ? 17.981 -23.736 25.945 1.00 41.17 ? 2105 HOH B O 1 HETATM 3670 O O . HOH N 5 . ? 43.680 1.228 21.159 1.00 53.28 ? 2106 HOH B O 1 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ILE 1 16 16 ILE ILE A . n A 1 2 VAL 2 17 17 VAL VAL A . n A 1 3 GLY 3 18 18 GLY GLY A . n A 1 4 GLY 4 19 19 GLY GLY A . n A 1 5 ARG 5 20 20 ARG ARG A . n A 1 6 ARG 6 21 21 ARG ARG A . n A 1 7 ALA 7 22 22 ALA ALA A . n A 1 8 ARG 8 23 23 ARG ARG A . n A 1 9 PRO 9 24 24 PRO PRO A . n A 1 10 HIS 10 25 25 HIS HIS A . n A 1 11 ALA 11 26 26 ALA ALA A . n A 1 12 TRP 12 27 27 TRP TRP A . n A 1 13 PRO 13 28 28 PRO PRO A . n A 1 14 PHE 14 29 29 PHE PHE A . n A 1 15 MET 15 30 30 MET MET A . n A 1 16 VAL 16 31 31 VAL VAL A . n A 1 17 SER 17 32 32 SER SER A . n A 1 18 LEU 18 33 33 LEU LEU A . n A 1 19 GLN 19 34 34 GLN GLN A . n A 1 20 LEU 20 35 35 LEU LEU A . n A 1 21 ARG 21 36 36 ARG ARG A . n A 1 22 GLY 22 38 38 GLY GLY A . n A 1 23 GLY 23 39 39 GLY GLY A . n A 1 24 HIS 24 40 40 HIS HIS A . n A 1 25 PHE 25 41 41 PHE PHE A . n A 1 26 CYS 26 42 42 CYS CYS A . n A 1 27 GLY 27 43 43 GLY GLY A . n A 1 28 ALA 28 44 44 ALA ALA A . n A 1 29 THR 29 45 45 THR THR A . n A 1 30 LEU 30 46 46 LEU LEU A . n A 1 31 ILE 31 47 47 ILE ILE A . n A 1 32 ALA 32 48 48 ALA ALA A . n A 1 33 PRO 33 49 49 PRO PRO A . n A 1 34 ASN 34 50 50 ASN ASN A . n A 1 35 PHE 35 51 51 PHE PHE A . n A 1 36 VAL 36 52 52 VAL VAL A . n A 1 37 MET 37 53 53 MET MET A . n A 1 38 SER 38 54 54 SER SER A . n A 1 39 ALA 39 55 55 ALA ALA A . n A 1 40 ALA 40 56 56 ALA ALA A . n A 1 41 HIS 41 57 57 HIS HIS A . n A 1 42 CYS 42 58 58 CYS CYS A . n A 1 43 VAL 43 59 59 VAL VAL A . n A 1 44 ALA 44 60 60 ALA ALA A . n A 1 45 ASN 45 61 61 ASN ASN A . n A 1 46 VAL 46 62 62 VAL VAL A . n A 1 47 ASN 47 62 62 ASN ASN A A n A 1 48 VAL 48 62 62 VAL VAL A B n A 1 49 ARG 49 63 63 ARG ARG A . n A 1 50 ALA 50 64 64 ALA ALA A . n A 1 51 VAL 51 65 65 VAL VAL A . n A 1 52 ARG 52 65 65 ARG ARG A A n A 1 53 VAL 53 66 66 VAL VAL A . n A 1 54 VAL 54 67 67 VAL VAL A . n A 1 55 LEU 55 68 68 LEU LEU A . n A 1 56 GLY 56 69 69 GLY GLY A . n A 1 57 ALA 57 70 70 ALA ALA A . n A 1 58 HIS 58 71 71 HIS HIS A . n A 1 59 ASN 59 72 72 ASN ASN A . n A 1 60 LEU 60 73 73 LEU LEU A . n A 1 61 SER 61 74 74 SER SER A . n A 1 62 ARG 62 75 75 ARG ARG A . n A 1 63 ARG 63 76 76 ARG ARG A . n A 1 64 GLU 64 77 77 GLU GLU A . n A 1 65 PRO 65 78 78 PRO PRO A . n A 1 66 THR 66 79 79 THR THR A . n A 1 67 ARG 67 80 80 ARG ARG A . n A 1 68 GLN 68 81 81 GLN GLN A . n A 1 69 VAL 69 82 82 VAL VAL A . n A 1 70 PHE 70 83 83 PHE PHE A . n A 1 71 ALA 71 84 84 ALA ALA A . n A 1 72 VAL 72 85 85 VAL VAL A . n A 1 73 GLN 73 86 86 GLN GLN A . n A 1 74 ARG 74 87 87 ARG ARG A . n A 1 75 ILE 75 88 88 ILE ILE A . n A 1 76 PHE 76 89 89 PHE PHE A . n A 1 77 GLU 77 90 90 GLU GLU A . n A 1 78 ASN 78 91 91 ASN ASN A . n A 1 79 GLY 79 92 92 GLY GLY A . n A 1 80 TYR 80 94 94 TYR TYR A . n A 1 81 ASP 81 95 95 ASP ASP A . n A 1 82 PRO 82 98 98 PRO PRO A . n A 1 83 VAL 83 99 99 VAL VAL A . n A 1 84 ASN 84 99 99 ASN ASN A A n A 1 85 LEU 85 99 99 LEU LEU A B n A 1 86 LEU 86 100 100 LEU LEU A . n A 1 87 ASN 87 101 101 ASN ASN A . n A 1 88 ASP 88 102 102 ASP ASP A . n A 1 89 ILE 89 103 103 ILE ILE A . n A 1 90 VAL 90 104 104 VAL VAL A . n A 1 91 ILE 91 105 105 ILE ILE A . n A 1 92 LEU 92 106 106 LEU LEU A . n A 1 93 GLN 93 107 107 GLN GLN A . n A 1 94 LEU 94 108 108 LEU LEU A . n A 1 95 ASN 95 109 109 ASN ASN A . n A 1 96 GLY 96 110 110 GLY GLY A . n A 1 97 SER 97 111 111 SER SER A . n A 1 98 ALA 98 112 112 ALA ALA A . n A 1 99 THR 99 113 113 THR THR A . n A 1 100 ILE 100 114 114 ILE ILE A . n A 1 101 ASN 101 115 115 ASN ASN A . n A 1 102 ALA 102 116 116 ALA ALA A . n A 1 103 ASN 103 117 117 ASN ASN A . n A 1 104 VAL 104 118 118 VAL VAL A . n A 1 105 GLN 105 119 119 GLN GLN A . n A 1 106 VAL 106 120 120 VAL VAL A . n A 1 107 ALA 107 121 121 ALA ALA A . n A 1 108 GLN 108 122 122 GLN GLN A . n A 1 109 LEU 109 123 123 LEU LEU A . n A 1 110 PRO 110 124 124 PRO PRO A . n A 1 111 ALA 111 125 125 ALA ALA A . n A 1 112 GLN 112 126 126 GLN GLN A . n A 1 113 GLY 113 127 127 GLY GLY A . n A 1 114 ARG 114 128 128 ARG ARG A . n A 1 115 ARG 115 129 129 ARG ARG A . n A 1 116 LEU 116 130 130 LEU LEU A . n A 1 117 GLY 117 131 131 GLY GLY A . n A 1 118 ASN 118 132 132 ASN ASN A . n A 1 119 GLY 119 133 133 GLY GLY A . n A 1 120 VAL 120 134 134 VAL VAL A . n A 1 121 GLN 121 135 135 GLN GLN A . n A 1 122 CYS 122 136 136 CYS CYS A . n A 1 123 LEU 123 137 137 LEU LEU A . n A 1 124 ALA 124 138 138 ALA ALA A . n A 1 125 MET 125 139 139 MET MET A . n A 1 126 GLY 126 140 140 GLY GLY A . n A 1 127 TRP 127 141 141 TRP TRP A . n A 1 128 GLY 128 142 142 GLY GLY A . n A 1 129 LEU 129 143 143 LEU LEU A . n A 1 130 LEU 130 144 144 LEU LEU A . n A 1 131 GLY 131 145 145 GLY GLY A . n A 1 132 ARG 132 147 147 ARG ARG A . n A 1 133 ASN 133 148 148 ASN ASN A . n A 1 134 ARG 134 149 149 ARG ARG A . n A 1 135 GLY 135 150 150 GLY GLY A . n A 1 136 ILE 136 151 151 ILE ILE A . n A 1 137 ALA 137 152 152 ALA ALA A . n A 1 138 SER 138 153 153 SER SER A . n A 1 139 VAL 139 154 154 VAL VAL A . n A 1 140 LEU 140 155 155 LEU LEU A . n A 1 141 GLN 141 156 156 GLN GLN A . n A 1 142 GLU 142 157 157 GLU GLU A . n A 1 143 LEU 143 158 158 LEU LEU A . n A 1 144 ASN 144 159 159 ASN ASN A . n A 1 145 VAL 145 160 160 VAL VAL A . n A 1 146 THR 146 162 162 THR THR A . n A 1 147 VAL 147 163 163 VAL VAL A . n A 1 148 VAL 148 164 164 VAL VAL A . n A 1 149 THR 149 165 165 THR THR A . n A 1 150 SER 150 166 166 SER SER A . n A 1 151 LEU 151 167 167 LEU LEU A . n A 1 152 CYS 152 168 168 CYS CYS A . n A 1 153 ARG 153 177 177 ARG ARG A . n A 1 154 ARG 154 178 178 ARG ARG A . n A 1 155 SER 155 179 179 SER SER A . n A 1 156 ASN 156 180 180 ASN ASN A . n A 1 157 VAL 157 181 181 VAL VAL A . n A 1 158 CYS 158 182 182 CYS CYS A . n A 1 159 THR 159 183 183 THR THR A . n A 1 160 LEU 160 184 184 LEU LEU A . n A 1 161 VAL 161 185 185 VAL VAL A . n A 1 162 ARG 162 186 186 ARG ARG A . n A 1 163 GLY 163 186 186 GLY GLY A A n A 1 164 ARG 164 187 187 ARG ARG A . n A 1 165 GLN 165 188 188 GLN GLN A . n A 1 166 ALA 166 188 188 ALA ALA A A n A 1 167 GLY 167 189 189 GLY GLY A . n A 1 168 VAL 168 190 190 VAL VAL A . n A 1 169 CYS 169 191 191 CYS CYS A . n A 1 170 PHE 170 192 192 PHE PHE A . n A 1 171 GLY 171 193 193 GLY GLY A . n A 1 172 ASP 172 194 194 ASP ASP A . n A 1 173 SER 173 195 195 SER SER A . n A 1 174 GLY 174 196 196 GLY GLY A . n A 1 175 SER 175 197 197 SER SER A . n A 1 176 PRO 176 198 198 PRO PRO A . n A 1 177 LEU 177 199 199 LEU LEU A . n A 1 178 VAL 178 200 200 VAL VAL A . n A 1 179 CYS 179 201 201 CYS CYS A . n A 1 180 ASN 180 204 204 ASN ASN A . n A 1 181 GLY 181 205 205 GLY GLY A . n A 1 182 LEU 182 208 208 LEU LEU A . n A 1 183 ILE 183 209 209 ILE ILE A . n A 1 184 HIS 184 210 210 HIS HIS A . n A 1 185 GLY 185 211 211 GLY GLY A . n A 1 186 ILE 186 212 212 ILE ILE A . n A 1 187 ALA 187 213 213 ALA ALA A . n A 1 188 SER 188 214 214 SER SER A . n A 1 189 PHE 189 215 215 PHE PHE A . n A 1 190 VAL 190 216 216 VAL VAL A . n A 1 191 ARG 191 217 217 ARG ARG A A n A 1 192 GLY 192 218 218 GLY GLY A . n A 1 193 GLY 193 219 219 GLY GLY A . n A 1 194 CYS 194 220 220 CYS CYS A . n A 1 195 ALA 195 221 221 ALA ALA A . n A 1 196 SER 196 222 222 SER SER A . n A 1 197 GLY 197 222 222 GLY GLY A A n A 1 198 LEU 198 223 223 LEU LEU A . n A 1 199 TYR 199 224 224 TYR TYR A . n A 1 200 PRO 200 225 225 PRO PRO A . n A 1 201 ASP 201 226 226 ASP ASP A . n A 1 202 ALA 202 227 227 ALA ALA A . n A 1 203 PHE 203 228 228 PHE PHE A . n A 1 204 ALA 204 229 229 ALA ALA A . n A 1 205 PRO 205 230 230 PRO PRO A . n A 1 206 VAL 206 231 231 VAL VAL A . n A 1 207 ALA 207 232 232 ALA ALA A . n A 1 208 GLN 208 233 233 GLN GLN A . n A 1 209 PHE 209 234 234 PHE PHE A . n A 1 210 VAL 210 235 235 VAL VAL A . n A 1 211 ASN 211 236 236 ASN ASN A . n A 1 212 TRP 212 237 237 TRP TRP A . n A 1 213 ILE 213 238 238 ILE ILE A . n A 1 214 ASP 214 239 239 ASP ASP A . n A 1 215 SER 215 240 240 SER SER A . n A 1 216 ILE 216 241 241 ILE ILE A . n A 1 217 ILE 217 242 242 ILE ILE A . n A 1 218 GLN 218 243 243 GLN GLN A . n B 1 1 ILE 1 16 16 ILE ILE B . n B 1 2 VAL 2 17 17 VAL VAL B . n B 1 3 GLY 3 18 18 GLY GLY B . n B 1 4 GLY 4 19 19 GLY GLY B . n B 1 5 ARG 5 20 20 ARG ARG B . n B 1 6 ARG 6 21 21 ARG ARG B . n B 1 7 ALA 7 22 22 ALA ALA B . n B 1 8 ARG 8 23 23 ARG ARG B . n B 1 9 PRO 9 24 24 PRO PRO B . n B 1 10 HIS 10 25 25 HIS HIS B . n B 1 11 ALA 11 26 26 ALA ALA B . n B 1 12 TRP 12 27 27 TRP TRP B . n B 1 13 PRO 13 28 28 PRO PRO B . n B 1 14 PHE 14 29 29 PHE PHE B . n B 1 15 MET 15 30 30 MET MET B . n B 1 16 VAL 16 31 31 VAL VAL B . n B 1 17 SER 17 32 32 SER SER B . n B 1 18 LEU 18 33 33 LEU LEU B . n B 1 19 GLN 19 34 34 GLN GLN B . n B 1 20 LEU 20 35 35 LEU LEU B . n B 1 21 ARG 21 36 36 ARG ARG B . n B 1 22 GLY 22 38 38 GLY GLY B . n B 1 23 GLY 23 39 39 GLY GLY B . n B 1 24 HIS 24 40 40 HIS HIS B . n B 1 25 PHE 25 41 41 PHE PHE B . n B 1 26 CYS 26 42 42 CYS CYS B . n B 1 27 GLY 27 43 43 GLY GLY B . n B 1 28 ALA 28 44 44 ALA ALA B . n B 1 29 THR 29 45 45 THR THR B . n B 1 30 LEU 30 46 46 LEU LEU B . n B 1 31 ILE 31 47 47 ILE ILE B . n B 1 32 ALA 32 48 48 ALA ALA B . n B 1 33 PRO 33 49 49 PRO PRO B . n B 1 34 ASN 34 50 50 ASN ASN B . n B 1 35 PHE 35 51 51 PHE PHE B . n B 1 36 VAL 36 52 52 VAL VAL B . n B 1 37 MET 37 53 53 MET MET B . n B 1 38 SER 38 54 54 SER SER B . n B 1 39 ALA 39 55 55 ALA ALA B . n B 1 40 ALA 40 56 56 ALA ALA B . n B 1 41 HIS 41 57 57 HIS HIS B . n B 1 42 CYS 42 58 58 CYS CYS B . n B 1 43 VAL 43 59 59 VAL VAL B . n B 1 44 ALA 44 60 60 ALA ALA B . n B 1 45 ASN 45 61 61 ASN ASN B . n B 1 46 VAL 46 62 62 VAL VAL B . n B 1 47 ASN 47 62 62 ASN ASN B A n B 1 48 VAL 48 62 62 VAL VAL B B n B 1 49 ARG 49 63 63 ARG ARG B . n B 1 50 ALA 50 64 64 ALA ALA B . n B 1 51 VAL 51 65 65 VAL VAL B . n B 1 52 ARG 52 65 65 ARG ARG B A n B 1 53 VAL 53 66 66 VAL VAL B . n B 1 54 VAL 54 67 67 VAL VAL B . n B 1 55 LEU 55 68 68 LEU LEU B . n B 1 56 GLY 56 69 69 GLY GLY B . n B 1 57 ALA 57 70 70 ALA ALA B . n B 1 58 HIS 58 71 71 HIS HIS B . n B 1 59 ASN 59 72 72 ASN ASN B . n B 1 60 LEU 60 73 73 LEU LEU B . n B 1 61 SER 61 74 74 SER SER B . n B 1 62 ARG 62 75 75 ARG ARG B . n B 1 63 ARG 63 76 76 ARG ARG B . n B 1 64 GLU 64 77 77 GLU GLU B . n B 1 65 PRO 65 78 78 PRO PRO B . n B 1 66 THR 66 79 79 THR THR B . n B 1 67 ARG 67 80 80 ARG ARG B . n B 1 68 GLN 68 81 81 GLN GLN B . n B 1 69 VAL 69 82 82 VAL VAL B . n B 1 70 PHE 70 83 83 PHE PHE B . n B 1 71 ALA 71 84 84 ALA ALA B . n B 1 72 VAL 72 85 85 VAL VAL B . n B 1 73 GLN 73 86 86 GLN GLN B . n B 1 74 ARG 74 87 87 ARG ARG B . n B 1 75 ILE 75 88 88 ILE ILE B . n B 1 76 PHE 76 89 89 PHE PHE B . n B 1 77 GLU 77 90 90 GLU GLU B . n B 1 78 ASN 78 91 91 ASN ASN B . n B 1 79 GLY 79 92 92 GLY GLY B . n B 1 80 TYR 80 94 94 TYR TYR B . n B 1 81 ASP 81 95 95 ASP ASP B . n B 1 82 PRO 82 98 98 PRO PRO B . n B 1 83 VAL 83 99 99 VAL VAL B . n B 1 84 ASN 84 99 99 ASN ASN B A n B 1 85 LEU 85 99 99 LEU LEU B B n B 1 86 LEU 86 100 100 LEU LEU B . n B 1 87 ASN 87 101 101 ASN ASN B . n B 1 88 ASP 88 102 102 ASP ASP B . n B 1 89 ILE 89 103 103 ILE ILE B . n B 1 90 VAL 90 104 104 VAL VAL B . n B 1 91 ILE 91 105 105 ILE ILE B . n B 1 92 LEU 92 106 106 LEU LEU B . n B 1 93 GLN 93 107 107 GLN GLN B . n B 1 94 LEU 94 108 108 LEU LEU B . n B 1 95 ASN 95 109 109 ASN ASN B . n B 1 96 GLY 96 110 110 GLY GLY B . n B 1 97 SER 97 111 111 SER SER B . n B 1 98 ALA 98 112 112 ALA ALA B . n B 1 99 THR 99 113 113 THR THR B . n B 1 100 ILE 100 114 114 ILE ILE B . n B 1 101 ASN 101 115 115 ASN ASN B . n B 1 102 ALA 102 116 116 ALA ALA B . n B 1 103 ASN 103 117 117 ASN ASN B . n B 1 104 VAL 104 118 118 VAL VAL B . n B 1 105 GLN 105 119 119 GLN GLN B . n B 1 106 VAL 106 120 120 VAL VAL B . n B 1 107 ALA 107 121 121 ALA ALA B . n B 1 108 GLN 108 122 122 GLN GLN B . n B 1 109 LEU 109 123 123 LEU LEU B . n B 1 110 PRO 110 124 124 PRO PRO B . n B 1 111 ALA 111 125 125 ALA ALA B . n B 1 112 GLN 112 126 126 GLN GLN B . n B 1 113 GLY 113 127 127 GLY GLY B . n B 1 114 ARG 114 128 128 ARG ARG B . n B 1 115 ARG 115 129 129 ARG ARG B . n B 1 116 LEU 116 130 130 LEU LEU B . n B 1 117 GLY 117 131 131 GLY GLY B . n B 1 118 ASN 118 132 132 ASN ASN B . n B 1 119 GLY 119 133 133 GLY GLY B . n B 1 120 VAL 120 134 134 VAL VAL B . n B 1 121 GLN 121 135 135 GLN GLN B . n B 1 122 CYS 122 136 136 CYS CYS B . n B 1 123 LEU 123 137 137 LEU LEU B . n B 1 124 ALA 124 138 138 ALA ALA B . n B 1 125 MET 125 139 139 MET MET B . n B 1 126 GLY 126 140 140 GLY GLY B . n B 1 127 TRP 127 141 141 TRP TRP B . n B 1 128 GLY 128 142 142 GLY GLY B . n B 1 129 LEU 129 143 143 LEU LEU B . n B 1 130 LEU 130 144 144 LEU LEU B . n B 1 131 GLY 131 145 145 GLY GLY B . n B 1 132 ARG 132 147 147 ARG ARG B . n B 1 133 ASN 133 148 148 ASN ASN B . n B 1 134 ARG 134 149 149 ARG ARG B . n B 1 135 GLY 135 150 150 GLY GLY B . n B 1 136 ILE 136 151 151 ILE ILE B . n B 1 137 ALA 137 152 152 ALA ALA B . n B 1 138 SER 138 153 153 SER SER B . n B 1 139 VAL 139 154 154 VAL VAL B . n B 1 140 LEU 140 155 155 LEU LEU B . n B 1 141 GLN 141 156 156 GLN GLN B . n B 1 142 GLU 142 157 157 GLU GLU B . n B 1 143 LEU 143 158 158 LEU LEU B . n B 1 144 ASN 144 159 159 ASN ASN B . n B 1 145 VAL 145 160 160 VAL VAL B . n B 1 146 THR 146 162 162 THR THR B . n B 1 147 VAL 147 163 163 VAL VAL B . n B 1 148 VAL 148 164 164 VAL VAL B . n B 1 149 THR 149 165 165 THR THR B . n B 1 150 SER 150 166 166 SER SER B . n B 1 151 LEU 151 167 167 LEU LEU B . n B 1 152 CYS 152 168 168 CYS CYS B . n B 1 153 ARG 153 177 177 ARG ARG B . n B 1 154 ARG 154 178 178 ARG ARG B . n B 1 155 SER 155 179 179 SER SER B . n B 1 156 ASN 156 180 180 ASN ASN B . n B 1 157 VAL 157 181 181 VAL VAL B . n B 1 158 CYS 158 182 182 CYS CYS B . n B 1 159 THR 159 183 183 THR THR B . n B 1 160 LEU 160 184 184 LEU LEU B . n B 1 161 VAL 161 185 185 VAL VAL B . n B 1 162 ARG 162 186 186 ARG ARG B . n B 1 163 GLY 163 186 186 GLY GLY B A n B 1 164 ARG 164 187 187 ARG ARG B . n B 1 165 GLN 165 188 188 GLN GLN B . n B 1 166 ALA 166 188 188 ALA ALA B A n B 1 167 GLY 167 189 189 GLY GLY B . n B 1 168 VAL 168 190 190 VAL VAL B . n B 1 169 CYS 169 191 191 CYS CYS B . n B 1 170 PHE 170 192 192 PHE PHE B . n B 1 171 GLY 171 193 193 GLY GLY B . n B 1 172 ASP 172 194 194 ASP ASP B . n B 1 173 SER 173 195 195 SER SER B . n B 1 174 GLY 174 196 196 GLY GLY B . n B 1 175 SER 175 197 197 SER SER B . n B 1 176 PRO 176 198 198 PRO PRO B . n B 1 177 LEU 177 199 199 LEU LEU B . n B 1 178 VAL 178 200 200 VAL VAL B . n B 1 179 CYS 179 201 201 CYS CYS B . n B 1 180 ASN 180 204 204 ASN ASN B . n B 1 181 GLY 181 205 205 GLY GLY B . n B 1 182 LEU 182 208 208 LEU LEU B . n B 1 183 ILE 183 209 209 ILE ILE B . n B 1 184 HIS 184 210 210 HIS HIS B . n B 1 185 GLY 185 211 211 GLY GLY B . n B 1 186 ILE 186 212 212 ILE ILE B . n B 1 187 ALA 187 213 213 ALA ALA B . n B 1 188 SER 188 214 214 SER SER B . n B 1 189 PHE 189 215 215 PHE PHE B . n B 1 190 VAL 190 216 216 VAL VAL B . n B 1 191 ARG 191 217 217 ARG ARG B A n B 1 192 GLY 192 218 218 GLY GLY B . n B 1 193 GLY 193 219 219 GLY GLY B . n B 1 194 CYS 194 220 220 CYS CYS B . n B 1 195 ALA 195 221 221 ALA ALA B . n B 1 196 SER 196 222 222 SER SER B . n B 1 197 GLY 197 222 222 GLY GLY B A n B 1 198 LEU 198 223 223 LEU LEU B . n B 1 199 TYR 199 224 224 TYR TYR B . n B 1 200 PRO 200 225 225 PRO PRO B . n B 1 201 ASP 201 226 226 ASP ASP B . n B 1 202 ALA 202 227 227 ALA ALA B . n B 1 203 PHE 203 228 228 PHE PHE B . n B 1 204 ALA 204 229 229 ALA ALA B . n B 1 205 PRO 205 230 230 PRO PRO B . n B 1 206 VAL 206 231 231 VAL VAL B . n B 1 207 ALA 207 232 232 ALA ALA B . n B 1 208 GLN 208 233 233 GLN GLN B . n B 1 209 PHE 209 234 234 PHE PHE B . n B 1 210 VAL 210 235 235 VAL VAL B . n B 1 211 ASN 211 236 236 ASN ASN B . n B 1 212 TRP 212 237 237 TRP TRP B . n B 1 213 ILE 213 238 238 ILE ILE B . n B 1 214 ASP 214 239 239 ASP ASP B . n B 1 215 SER 215 240 240 SER SER B . n B 1 216 ILE 216 241 241 ILE ILE B . n B 1 217 ILE 217 242 242 ILE ILE B . n B 1 218 GLN 218 243 243 GLN GLN B . 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 C 2 151 1 400 400 151 151 A . D 3 NAG 1 401 401 NAG NAG A . E 4 FUC 2 402 402 FUC FUC A . F 3 NAG 1 411 411 NAG NAG A . G 4 FUC 2 412 412 FUC FUC A . H 2 151 1 400 400 151 151 B . I 3 NAG 1 401 401 NAG NAG B . J 4 FUC 2 402 402 FUC FUC B . K 3 NAG 1 411 411 NAG NAG B . L 4 FUC 2 412 412 FUC FUC B . M 5 HOH 1 2001 2001 HOH HOH A . M 5 HOH 2 2002 2002 HOH HOH A . M 5 HOH 3 2003 2003 HOH HOH A . M 5 HOH 4 2004 2004 HOH HOH A . M 5 HOH 5 2005 2005 HOH HOH A . M 5 HOH 6 2006 2006 HOH HOH A . M 5 HOH 7 2007 2007 HOH HOH A . M 5 HOH 8 2008 2008 HOH HOH A . M 5 HOH 9 2009 2009 HOH HOH A . M 5 HOH 10 2010 2010 HOH HOH A . M 5 HOH 11 2011 2011 HOH HOH A . M 5 HOH 12 2012 2012 HOH HOH A . M 5 HOH 13 2013 2013 HOH HOH A . M 5 HOH 14 2014 2014 HOH HOH A . M 5 HOH 15 2015 2015 HOH HOH A . M 5 HOH 16 2016 2016 HOH HOH A . M 5 HOH 17 2017 2017 HOH HOH A . M 5 HOH 18 2018 2018 HOH HOH A . M 5 HOH 19 2019 2019 HOH HOH A . M 5 HOH 20 2020 2020 HOH HOH A . M 5 HOH 21 2021 2021 HOH HOH A . M 5 HOH 22 2022 2022 HOH HOH A . M 5 HOH 23 2023 2023 HOH HOH A . M 5 HOH 24 2024 2024 HOH HOH A . M 5 HOH 25 2025 2025 HOH HOH A . M 5 HOH 26 2026 2026 HOH HOH A . M 5 HOH 27 2027 2027 HOH HOH A . M 5 HOH 28 2028 2028 HOH HOH A . M 5 HOH 29 2029 2029 HOH HOH A . M 5 HOH 30 2030 2030 HOH HOH A . M 5 HOH 31 2031 2031 HOH HOH A . M 5 HOH 32 2032 2032 HOH HOH A . M 5 HOH 33 2033 2033 HOH HOH A . M 5 HOH 34 2034 2034 HOH HOH A . M 5 HOH 35 2035 2035 HOH HOH A . M 5 HOH 36 2036 2036 HOH HOH A . M 5 HOH 37 2037 2037 HOH HOH A . M 5 HOH 38 2038 2038 HOH HOH A . M 5 HOH 39 2039 2039 HOH HOH A . M 5 HOH 40 2040 2040 HOH HOH A . M 5 HOH 41 2041 2041 HOH HOH A . M 5 HOH 42 2042 2042 HOH HOH A . M 5 HOH 43 2043 2043 HOH HOH A . M 5 HOH 44 2044 2044 HOH HOH A . M 5 HOH 45 2045 2045 HOH HOH A . M 5 HOH 46 2046 2046 HOH HOH A . M 5 HOH 47 2047 2047 HOH HOH A . M 5 HOH 48 2048 2048 HOH HOH A . M 5 HOH 49 2049 2049 HOH HOH A . M 5 HOH 50 2050 2050 HOH HOH A . M 5 HOH 51 2051 2051 HOH HOH A . M 5 HOH 52 2052 2052 HOH HOH A . M 5 HOH 53 2053 2053 HOH HOH A . M 5 HOH 54 2054 2054 HOH HOH A . M 5 HOH 55 2055 2055 HOH HOH A . M 5 HOH 56 2056 2056 HOH HOH A . M 5 HOH 57 2057 2057 HOH HOH A . M 5 HOH 58 2058 2058 HOH HOH A . M 5 HOH 59 2059 2059 HOH HOH A . M 5 HOH 60 2060 2060 HOH HOH A . M 5 HOH 61 2061 2061 HOH HOH A . M 5 HOH 62 2062 2062 HOH HOH A . M 5 HOH 63 2063 2063 HOH HOH A . M 5 HOH 64 2064 2064 HOH HOH A . M 5 HOH 65 2065 2065 HOH HOH A . M 5 HOH 66 2066 2066 HOH HOH A . M 5 HOH 67 2067 2067 HOH HOH A . M 5 HOH 68 2068 2068 HOH HOH A . M 5 HOH 69 2069 2069 HOH HOH A . M 5 HOH 70 2070 2070 HOH HOH A . M 5 HOH 71 2071 2071 HOH HOH A . M 5 HOH 72 2072 2072 HOH HOH A . M 5 HOH 73 2073 2073 HOH HOH A . M 5 HOH 74 2074 2074 HOH HOH A . M 5 HOH 75 2075 2075 HOH HOH A . M 5 HOH 76 2076 2076 HOH HOH A . M 5 HOH 77 2077 2077 HOH HOH A . M 5 HOH 78 2078 2078 HOH HOH A . M 5 HOH 79 2079 2079 HOH HOH A . M 5 HOH 80 2080 2080 HOH HOH A . M 5 HOH 81 2081 2081 HOH HOH A . M 5 HOH 82 2082 2082 HOH HOH A . M 5 HOH 83 2083 2083 HOH HOH A . M 5 HOH 84 2084 2084 HOH HOH A . M 5 HOH 85 2085 2085 HOH HOH A . M 5 HOH 86 2086 2086 HOH HOH A . M 5 HOH 87 2087 2087 HOH HOH A . M 5 HOH 88 2088 2088 HOH HOH A . M 5 HOH 89 2089 2089 HOH HOH A . M 5 HOH 90 2090 2090 HOH HOH A . M 5 HOH 91 2091 2091 HOH HOH A . M 5 HOH 92 2092 2092 HOH HOH A . M 5 HOH 93 2093 2093 HOH HOH A . M 5 HOH 94 2094 2094 HOH HOH A . M 5 HOH 95 2095 2095 HOH HOH A . M 5 HOH 96 2096 2096 HOH HOH A . M 5 HOH 97 2097 2097 HOH HOH A . M 5 HOH 98 2098 2098 HOH HOH A . M 5 HOH 99 2099 2099 HOH HOH A . M 5 HOH 100 2100 2100 HOH HOH A . M 5 HOH 101 2101 2101 HOH HOH A . M 5 HOH 102 2102 2102 HOH HOH A . M 5 HOH 103 2103 2103 HOH HOH A . M 5 HOH 104 2104 2104 HOH HOH A . M 5 HOH 105 2105 2105 HOH HOH A . M 5 HOH 106 2106 2106 HOH HOH A . M 5 HOH 107 2107 2107 HOH HOH A . M 5 HOH 108 2108 2108 HOH HOH A . M 5 HOH 109 2109 2109 HOH HOH A . M 5 HOH 110 2110 2110 HOH HOH A . M 5 HOH 111 2111 2111 HOH HOH A . M 5 HOH 112 2112 2112 HOH HOH A . M 5 HOH 113 2113 2113 HOH HOH A . M 5 HOH 114 2114 2114 HOH HOH A . M 5 HOH 115 2115 2115 HOH HOH A . M 5 HOH 116 2116 2116 HOH HOH A . M 5 HOH 117 2117 2117 HOH HOH A . M 5 HOH 118 2118 2118 HOH HOH A . M 5 HOH 119 2119 2119 HOH HOH A . M 5 HOH 120 2120 2120 HOH HOH A . M 5 HOH 121 2121 2121 HOH HOH A . M 5 HOH 122 2122 2122 HOH HOH A . M 5 HOH 123 2123 2123 HOH HOH A . M 5 HOH 124 2124 2124 HOH HOH A . M 5 HOH 125 2125 2125 HOH HOH A . M 5 HOH 126 2126 2126 HOH HOH A . M 5 HOH 127 2127 2127 HOH HOH A . M 5 HOH 128 2128 2128 HOH HOH A . M 5 HOH 129 2129 2129 HOH HOH A . M 5 HOH 130 2130 2130 HOH HOH A . M 5 HOH 131 2131 2131 HOH HOH A . M 5 HOH 132 2132 2132 HOH HOH A . M 5 HOH 133 2133 2133 HOH HOH A . M 5 HOH 134 2134 2134 HOH HOH A . M 5 HOH 135 2135 2135 HOH HOH A . M 5 HOH 136 2136 2136 HOH HOH A . M 5 HOH 137 2137 2137 HOH HOH A . M 5 HOH 138 2138 2138 HOH HOH A . N 5 HOH 1 2001 2001 HOH HOH B . N 5 HOH 2 2002 2002 HOH HOH B . N 5 HOH 3 2003 2003 HOH HOH B . N 5 HOH 4 2004 2004 HOH HOH B . N 5 HOH 5 2005 2005 HOH HOH B . N 5 HOH 6 2006 2006 HOH HOH B . N 5 HOH 7 2007 2007 HOH HOH B . N 5 HOH 8 2008 2008 HOH HOH B . N 5 HOH 9 2009 2009 HOH HOH B . N 5 HOH 10 2010 2010 HOH HOH B . N 5 HOH 11 2011 2011 HOH HOH B . N 5 HOH 12 2012 2012 HOH HOH B . N 5 HOH 13 2013 2013 HOH HOH B . N 5 HOH 14 2014 2014 HOH HOH B . N 5 HOH 15 2015 2015 HOH HOH B . N 5 HOH 16 2016 2016 HOH HOH B . N 5 HOH 17 2017 2017 HOH HOH B . N 5 HOH 18 2018 2018 HOH HOH B . N 5 HOH 19 2019 2019 HOH HOH B . N 5 HOH 20 2020 2020 HOH HOH B . N 5 HOH 21 2021 2021 HOH HOH B . N 5 HOH 22 2022 2022 HOH HOH B . N 5 HOH 23 2023 2023 HOH HOH B . N 5 HOH 24 2024 2024 HOH HOH B . N 5 HOH 25 2025 2025 HOH HOH B . N 5 HOH 26 2026 2026 HOH HOH B . N 5 HOH 27 2027 2027 HOH HOH B . N 5 HOH 28 2028 2028 HOH HOH B . N 5 HOH 29 2029 2029 HOH HOH B . N 5 HOH 30 2030 2030 HOH HOH B . N 5 HOH 31 2031 2031 HOH HOH B . N 5 HOH 32 2032 2032 HOH HOH B . N 5 HOH 33 2033 2033 HOH HOH B . N 5 HOH 34 2034 2034 HOH HOH B . N 5 HOH 35 2035 2035 HOH HOH B . N 5 HOH 36 2036 2036 HOH HOH B . N 5 HOH 37 2037 2037 HOH HOH B . N 5 HOH 38 2038 2038 HOH HOH B . N 5 HOH 39 2039 2039 HOH HOH B . N 5 HOH 40 2040 2040 HOH HOH B . N 5 HOH 41 2041 2041 HOH HOH B . N 5 HOH 42 2042 2042 HOH HOH B . N 5 HOH 43 2043 2043 HOH HOH B . N 5 HOH 44 2044 2044 HOH HOH B . N 5 HOH 45 2045 2045 HOH HOH B . N 5 HOH 46 2046 2046 HOH HOH B . N 5 HOH 47 2047 2047 HOH HOH B . N 5 HOH 48 2048 2048 HOH HOH B . N 5 HOH 49 2049 2049 HOH HOH B . N 5 HOH 50 2050 2050 HOH HOH B . N 5 HOH 51 2051 2051 HOH HOH B . N 5 HOH 52 2052 2052 HOH HOH B . N 5 HOH 53 2053 2053 HOH HOH B . N 5 HOH 54 2054 2054 HOH HOH B . N 5 HOH 55 2055 2055 HOH HOH B . N 5 HOH 56 2056 2056 HOH HOH B . N 5 HOH 57 2057 2057 HOH HOH B . N 5 HOH 58 2058 2058 HOH HOH B . N 5 HOH 59 2059 2059 HOH HOH B . N 5 HOH 60 2060 2060 HOH HOH B . N 5 HOH 61 2061 2061 HOH HOH B . N 5 HOH 62 2062 2062 HOH HOH B . N 5 HOH 63 2063 2063 HOH HOH B . N 5 HOH 64 2064 2064 HOH HOH B . N 5 HOH 65 2065 2065 HOH HOH B . N 5 HOH 66 2066 2066 HOH HOH B . N 5 HOH 67 2067 2067 HOH HOH B . N 5 HOH 68 2068 2068 HOH HOH B . N 5 HOH 69 2069 2069 HOH HOH B . N 5 HOH 70 2070 2070 HOH HOH B . N 5 HOH 71 2071 2071 HOH HOH B . N 5 HOH 72 2072 2072 HOH HOH B . N 5 HOH 73 2073 2073 HOH HOH B . N 5 HOH 74 2074 2074 HOH HOH B . N 5 HOH 75 2075 2075 HOH HOH B . N 5 HOH 76 2076 2076 HOH HOH B . N 5 HOH 77 2077 2077 HOH HOH B . N 5 HOH 78 2078 2078 HOH HOH B . N 5 HOH 79 2079 2079 HOH HOH B . N 5 HOH 80 2080 2080 HOH HOH B . N 5 HOH 81 2081 2081 HOH HOH B . N 5 HOH 82 2082 2082 HOH HOH B . N 5 HOH 83 2083 2083 HOH HOH B . N 5 HOH 84 2084 2084 HOH HOH B . N 5 HOH 85 2085 2085 HOH HOH B . N 5 HOH 86 2086 2086 HOH HOH B . N 5 HOH 87 2087 2087 HOH HOH B . N 5 HOH 88 2088 2088 HOH HOH B . N 5 HOH 89 2089 2089 HOH HOH B . N 5 HOH 90 2090 2090 HOH HOH B . N 5 HOH 91 2091 2091 HOH HOH B . N 5 HOH 92 2092 2092 HOH HOH B . N 5 HOH 93 2093 2093 HOH HOH B . N 5 HOH 94 2094 2094 HOH HOH B . N 5 HOH 95 2095 2095 HOH HOH B . N 5 HOH 96 2096 2096 HOH HOH B . N 5 HOH 97 2097 2097 HOH HOH B . N 5 HOH 98 2098 2098 HOH HOH B . N 5 HOH 99 2099 2099 HOH HOH B . N 5 HOH 100 2100 2100 HOH HOH B . N 5 HOH 101 2101 2101 HOH HOH B . N 5 HOH 102 2102 2102 HOH HOH B . N 5 HOH 103 2103 2103 HOH HOH B . N 5 HOH 104 2104 2104 HOH HOH B . N 5 HOH 105 2105 2105 HOH HOH B . N 5 HOH 106 2106 2106 HOH HOH B . # 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 95 A ASN 109 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 144 A ASN 159 ? ASN 'GLYCOSYLATION SITE' 3 B ASN 95 B ASN 109 ? ASN 'GLYCOSYLATION SITE' 4 B ASN 144 B ASN 159 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details dimeric _pdbx_struct_assembly.oligomeric_count 2 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N # 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)' 1650 ? 1 MORE -19.0 ? 1 'SSA (A^2)' 22370 ? # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2002-08-29 2 'Structure model' 1 1 2011-09-14 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Derived calculations' 2 2 'Structure model' 'Non-polymer description' 3 2 'Structure model' Other 4 2 'Structure model' 'Structure summary' 5 2 'Structure model' 'Version format compliance' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement . ? 1 DENZO 'data reduction' . ? 2 SCALEPACK 'data scaling' . ? 3 AMoRE phasing . ? 4 # _pdbx_database_remark.id 700 _pdbx_database_remark.text ; SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 14-STRANDED BARREL THIS IS REPRESENTED BY A 15-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. ; # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 NH1 A ARG 147 ? ? O A HOH 2086 ? ? 1.53 2 1 NE2 B GLN 122 ? ? O B HOH 2058 ? ? 1.74 3 1 CD B GLN 122 ? ? O B HOH 2058 ? ? 1.89 4 1 OE1 B GLN 122 ? ? O B HOH 2058 ? ? 1.91 5 1 O B ALA 60 ? ? O B HOH 2019 ? ? 1.96 6 1 OG A SER 153 ? ? O A HOH 2087 ? ? 1.97 7 1 OD1 A ASN 132 ? ? O A HOH 2082 ? ? 2.01 8 1 O B HOH 2007 ? ? O B HOH 2020 ? ? 2.01 9 1 OE1 B GLN 122 ? ? O B HOH 2057 ? ? 2.03 10 1 ND2 B ASN 236 ? ? O B HOH 2099 ? ? 2.05 11 1 OD1 B ASN 132 ? ? O B HOH 2062 ? ? 2.05 12 1 NH2 B ARG 186 ? ? O B HOH 2076 ? ? 2.08 13 1 O A ARG 178 ? ? O A HOH 2095 ? ? 2.13 14 1 OD2 A ASP 226 ? ? O A HOH 2126 ? ? 2.13 15 1 O A HOH 2058 ? ? O A HOH 2129 ? ? 2.13 16 1 OD1 B ASN 72 ? ? OG B SER 74 ? ? 2.13 17 1 O3 A 151 400 ? ? O A HOH 2136 ? ? 2.16 18 1 O B HOH 2047 ? ? O B HOH 2103 ? ? 2.17 19 1 O A HOH 2135 ? ? O B HOH 2025 ? ? 2.17 20 1 OXT B GLN 243 ? ? O B HOH 2103 ? ? 2.19 # loop_ _pdbx_validate_symm_contact.id _pdbx_validate_symm_contact.PDB_model_num _pdbx_validate_symm_contact.auth_atom_id_1 _pdbx_validate_symm_contact.auth_asym_id_1 _pdbx_validate_symm_contact.auth_comp_id_1 _pdbx_validate_symm_contact.auth_seq_id_1 _pdbx_validate_symm_contact.PDB_ins_code_1 _pdbx_validate_symm_contact.label_alt_id_1 _pdbx_validate_symm_contact.site_symmetry_1 _pdbx_validate_symm_contact.auth_atom_id_2 _pdbx_validate_symm_contact.auth_asym_id_2 _pdbx_validate_symm_contact.auth_comp_id_2 _pdbx_validate_symm_contact.auth_seq_id_2 _pdbx_validate_symm_contact.PDB_ins_code_2 _pdbx_validate_symm_contact.label_alt_id_2 _pdbx_validate_symm_contact.site_symmetry_2 _pdbx_validate_symm_contact.dist 1 1 O A HOH 2042 ? ? 1_555 O B HOH 2020 ? ? 7_555 1.60 2 1 NH2 A ARG 147 ? ? 1_555 NH2 A ARG 147 ? ? 7_555 1.71 3 1 O B HOH 2057 ? ? 1_555 O B HOH 2057 ? ? 5_655 2.00 4 1 O A HOH 2042 ? ? 1_555 O B HOH 2007 ? ? 7_555 2.03 # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 CA A CYS 182 ? ? CB A CYS 182 ? ? SG A CYS 182 ? ? 127.26 114.20 13.06 1.10 N 2 1 CA B LEU 100 ? ? CB B LEU 100 ? ? CG B LEU 100 ? ? 133.22 115.30 17.92 2.30 N 3 1 CA B CYS 182 ? ? CB B CYS 182 ? ? SG B CYS 182 ? ? 123.86 114.20 9.66 1.10 N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 HIS A 71 ? ? -127.73 -67.61 2 1 ASN A 115 ? ? -159.32 -159.94 3 1 ARG A 128 ? ? -66.28 92.38 4 1 ARG A 147 ? ? 140.63 2.18 5 1 ARG A 149 ? ? 69.74 141.48 6 1 SER A 214 ? ? -122.17 -58.24 7 1 PRO B 24 ? ? -30.28 113.60 8 1 ARG B 36 ? ? 72.86 -133.07 9 1 ASN B 61 ? ? -140.14 59.07 10 1 HIS B 71 ? ? -139.21 -44.52 11 1 ASN B 115 ? ? -140.95 -158.27 12 1 ASN B 132 ? ? -37.11 129.32 13 1 ARG B 147 ? ? 144.87 -8.46 14 1 ARG B 149 ? ? 89.34 141.22 15 1 SER B 214 ? ? -124.64 -53.30 # _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 6.84 _pdbx_distant_solvent_atoms.neighbor_ligand_distance . # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 ;(2S)-3-METHYL-2-((2R,3S)-3-[(METHYLSULFONYL)AMINO]-1-{[2-(PYRROLIDIN-1-YLMETHYL)-1,3-OXAZOL-4-YL]CARBONYL}PYRROLIDIN-2-YL)BUTANOIC ACID ; 151 3 N-ACETYL-D-GLUCOSAMINE NAG 4 ALPHA-L-FUCOSE FUC 5 water HOH #