data_1UKM # _entry.id 1UKM # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.296 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 1UKM RCSB RCSB005932 WWPDB D_1000005932 # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 1UKM _pdbx_database_status.recvd_initial_deposition_date 2003-08-27 _pdbx_database_status.deposit_site PDBJ _pdbx_database_status.process_site PDBJ _pdbx_database_status.status_code_sf REL _pdbx_database_status.SG_entry . _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal _audit_author.identifier_ORCID 'Horii, K.' 1 ? 'Okuda, D.' 2 ? 'Morita, T.' 3 ? 'Mizuno, H.' 4 ? # loop_ _citation.id _citation.title _citation.journal_abbrev _citation.journal_volume _citation.page_first _citation.page_last _citation.year _citation.journal_id_ASTM _citation.country _citation.journal_id_ISSN _citation.journal_id_CSD _citation.book_publisher _citation.pdbx_database_id_PubMed _citation.pdbx_database_id_DOI primary 'Structural characterization of EMS16, an Antagonist of collagen receptor (GPIa/IIa) from the venom of Echis multisquamatus' Biochemistry 42 12497 12502 2003 BICHAW US 0006-2960 0033 ? 14580195 10.1021/bi034890h 1 ;Characterization and Preliminary Crystallographic Studies of EMS16, an Antagonist of Collagen Receptor (GPIa/IIa) from the Venom of Echis multisquamatus ; 'J.BIOCHEM.(TOKYO)' 134 19 23 2003 JOBIAO JA 0021-924X 0418 ? ? 10.1093/jb/mvg108 2 ;Isolation and characterization of EMS16, a C-lectin type protein from Echis multisquamatus venom, a potent and selective inhibitor of the alpha2beta1 integrin ; Biochemistry 39 9859 9867 2000 BICHAW US 0006-2960 0033 ? ? 10.1021/bi000428a # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal _citation_author.identifier_ORCID primary 'Horii, K.' 1 ? primary 'Okuda, D.' 2 ? primary 'Morita, T.' 3 ? primary 'Mizuno, H.' 4 ? 1 'Okuda, D.' 5 ? 1 'Horii, K.' 6 ? 1 'Mizuno, H.' 7 ? 1 'Morita, T.' 8 ? 2 'Marcinkiewicz, C.' 9 ? 2 'Lobb, R.R.' 10 ? 2 'Marcinkiewicz, M.M.' 11 ? 2 'Daniel, J.L.' 12 ? 2 'Smith, J.B.' 13 ? 2 'Dangelmaier, C.' 14 ? 2 'Weinreb, P.H.' 15 ? 2 'Beacham, D.A.' 16 ? 2 'Niewiarowski, S.' 17 ? # _cell.entry_id 1UKM _cell.length_a 46.570 _cell.length_b 59.933 _cell.length_c 115.743 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 4 _cell.pdbx_unique_axis ? # _symmetry.entry_id 1UKM _symmetry.space_group_name_H-M 'P 21 21 21' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 19 # 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 'EMS16 A chain' 15889.537 1 ? ? 'RESIDUES 1-134' ? 2 polymer nat 'EMS16 B chain' 15121.384 1 ? G43S 'RESIDUES 1-128' ? 3 non-polymer syn 'CHLORIDE ION' 35.453 1 ? ? ? ? 4 non-polymer syn GLYCEROL 92.094 4 ? ? ? ? 5 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 1 ? ? ? ? 6 water nat water 18.015 250 ? ? ? ? # loop_ _entity_name_com.entity_id _entity_name_com.name 1 'EMS16 subunit A' 2 'EMS16 subunit B' # loop_ _entity_poly.entity_id _entity_poly.type _entity_poly.nstd_linkage _entity_poly.nstd_monomer _entity_poly.pdbx_seq_one_letter_code _entity_poly.pdbx_seq_one_letter_code_can _entity_poly.pdbx_strand_id _entity_poly.pdbx_target_identifier 1 'polypeptide(L)' no no ;DFDCPSDWTAYDQHCYLAIGEPQNWYEAERFCTEQAKDGHLVSIQSREEGNFVAQLVSGFMHRSEIYVWIGLRDRREEQQ CNPEWNDGSKIIYVNWKEGESKMCQGLTKWTNFHDWNNINCEDLYPFVCKFSAV ; ;DFDCPSDWTAYDQHCYLAIGEPQNWYEAERFCTEQAKDGHLVSIQSREEGNFVAQLVSGFMHRSEIYVWIGLRDRREEQQ CNPEWNDGSKIIYVNWKEGESKMCQGLTKWTNFHDWNNINCEDLYPFVCKFSAV ; A ? 2 'polypeptide(L)' no no ;CPLGWSSFDQHCYKVFEPVKNWTEAEEICMQQHKGSRLASIHSSEEEAFVSKLASKALKFTSMWIGLNNPWKDCKWEWSD NARFDYKAWKRRPYCTVMVVKPDRIFWFTRGCEKSVSFVCKFLTDPAV ; ;CPLGWSSFDQHCYKVFEPVKNWTEAEEICMQQHKGSRLASIHSSEEEAFVSKLASKALKFTSMWIGLNNPWKDCKWEWSD NARFDYKAWKRRPYCTVMVVKPDRIFWFTRGCEKSVSFVCKFLTDPAV ; B ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ASP n 1 2 PHE n 1 3 ASP n 1 4 CYS n 1 5 PRO n 1 6 SER n 1 7 ASP n 1 8 TRP n 1 9 THR n 1 10 ALA n 1 11 TYR n 1 12 ASP n 1 13 GLN n 1 14 HIS n 1 15 CYS n 1 16 TYR n 1 17 LEU n 1 18 ALA n 1 19 ILE n 1 20 GLY n 1 21 GLU n 1 22 PRO n 1 23 GLN n 1 24 ASN n 1 25 TRP n 1 26 TYR n 1 27 GLU n 1 28 ALA n 1 29 GLU n 1 30 ARG n 1 31 PHE n 1 32 CYS n 1 33 THR n 1 34 GLU n 1 35 GLN n 1 36 ALA n 1 37 LYS n 1 38 ASP n 1 39 GLY n 1 40 HIS n 1 41 LEU n 1 42 VAL n 1 43 SER n 1 44 ILE n 1 45 GLN n 1 46 SER n 1 47 ARG n 1 48 GLU n 1 49 GLU n 1 50 GLY n 1 51 ASN n 1 52 PHE n 1 53 VAL n 1 54 ALA n 1 55 GLN n 1 56 LEU n 1 57 VAL n 1 58 SER n 1 59 GLY n 1 60 PHE n 1 61 MET n 1 62 HIS n 1 63 ARG n 1 64 SER n 1 65 GLU n 1 66 ILE n 1 67 TYR n 1 68 VAL n 1 69 TRP n 1 70 ILE n 1 71 GLY n 1 72 LEU n 1 73 ARG n 1 74 ASP n 1 75 ARG n 1 76 ARG n 1 77 GLU n 1 78 GLU n 1 79 GLN n 1 80 GLN n 1 81 CYS n 1 82 ASN n 1 83 PRO n 1 84 GLU n 1 85 TRP n 1 86 ASN n 1 87 ASP n 1 88 GLY n 1 89 SER n 1 90 LYS n 1 91 ILE n 1 92 ILE n 1 93 TYR n 1 94 VAL n 1 95 ASN n 1 96 TRP n 1 97 LYS n 1 98 GLU n 1 99 GLY n 1 100 GLU n 1 101 SER n 1 102 LYS n 1 103 MET n 1 104 CYS n 1 105 GLN n 1 106 GLY n 1 107 LEU n 1 108 THR n 1 109 LYS n 1 110 TRP n 1 111 THR n 1 112 ASN n 1 113 PHE n 1 114 HIS n 1 115 ASP n 1 116 TRP n 1 117 ASN n 1 118 ASN n 1 119 ILE n 1 120 ASN n 1 121 CYS n 1 122 GLU n 1 123 ASP n 1 124 LEU n 1 125 TYR n 1 126 PRO n 1 127 PHE n 1 128 VAL n 1 129 CYS n 1 130 LYS n 1 131 PHE n 1 132 SER n 1 133 ALA n 1 134 VAL n 2 1 CYS n 2 2 PRO n 2 3 LEU n 2 4 GLY n 2 5 TRP n 2 6 SER n 2 7 SER n 2 8 PHE n 2 9 ASP n 2 10 GLN n 2 11 HIS n 2 12 CYS n 2 13 TYR n 2 14 LYS n 2 15 VAL n 2 16 PHE n 2 17 GLU n 2 18 PRO n 2 19 VAL n 2 20 LYS n 2 21 ASN n 2 22 TRP n 2 23 THR n 2 24 GLU n 2 25 ALA n 2 26 GLU n 2 27 GLU n 2 28 ILE n 2 29 CYS n 2 30 MET n 2 31 GLN n 2 32 GLN n 2 33 HIS n 2 34 LYS n 2 35 GLY n 2 36 SER n 2 37 ARG n 2 38 LEU n 2 39 ALA n 2 40 SER n 2 41 ILE n 2 42 HIS n 2 43 SER n 2 44 SER n 2 45 GLU n 2 46 GLU n 2 47 GLU n 2 48 ALA n 2 49 PHE n 2 50 VAL n 2 51 SER n 2 52 LYS n 2 53 LEU n 2 54 ALA n 2 55 SER n 2 56 LYS n 2 57 ALA n 2 58 LEU n 2 59 LYS n 2 60 PHE n 2 61 THR n 2 62 SER n 2 63 MET n 2 64 TRP n 2 65 ILE n 2 66 GLY n 2 67 LEU n 2 68 ASN n 2 69 ASN n 2 70 PRO n 2 71 TRP n 2 72 LYS n 2 73 ASP n 2 74 CYS n 2 75 LYS n 2 76 TRP n 2 77 GLU n 2 78 TRP n 2 79 SER n 2 80 ASP n 2 81 ASN n 2 82 ALA n 2 83 ARG n 2 84 PHE n 2 85 ASP n 2 86 TYR n 2 87 LYS n 2 88 ALA n 2 89 TRP n 2 90 LYS n 2 91 ARG n 2 92 ARG n 2 93 PRO n 2 94 TYR n 2 95 CYS n 2 96 THR n 2 97 VAL n 2 98 MET n 2 99 VAL n 2 100 VAL n 2 101 LYS n 2 102 PRO n 2 103 ASP n 2 104 ARG n 2 105 ILE n 2 106 PHE n 2 107 TRP n 2 108 PHE n 2 109 THR n 2 110 ARG n 2 111 GLY n 2 112 CYS n 2 113 GLU n 2 114 LYS n 2 115 SER n 2 116 VAL n 2 117 SER n 2 118 PHE n 2 119 VAL n 2 120 CYS n 2 121 LYS n 2 122 PHE n 2 123 LEU n 2 124 THR n 2 125 ASP n 2 126 PRO n 2 127 ALA n 2 128 VAL n # loop_ _entity_src_nat.entity_id _entity_src_nat.pdbx_src_id _entity_src_nat.pdbx_alt_source_flag _entity_src_nat.pdbx_beg_seq_num _entity_src_nat.pdbx_end_seq_num _entity_src_nat.common_name _entity_src_nat.pdbx_organism_scientific _entity_src_nat.pdbx_ncbi_taxonomy_id _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 _entity_src_nat.pdbx_plasmid_name _entity_src_nat.pdbx_plasmid_details _entity_src_nat.details 1 1 sample ? ? ? 'Echis multisquamatus' 93050 Echis ? ? ? ? venom ? ? ? ? ? ? ? ? ? ? ? 2 1 sample ? ? ? 'Echis multisquamatus' 93050 Echis ? ? ? ? venom ? ? ? ? ? ? ? ? ? ? ? # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.pdbx_db_accession _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.pdbx_db_isoform 1 UNP Q7T2Q1_ECHML Q7T2Q1 1 ;DFDCPSDWTAYDQHCYLAIGEPQNWYEAERFCTEQAKDGHLVSIQSREEGNFVAQLVSGFMHRSEIYVWIGLRDRREEQQ CNPEWNDGSKIIYVNWKEGESKMCQGLTKWTNFHDWNNINCEDLYPFVCKFSAV ; 24 ? 2 UNP Q7T2Q0_ECHML Q7T2Q0 2 ;CPLGWSSFDQHCYKVFEPVKNWTEAEEICMQQHKGSRLASIHGSEEEAFVSKLASKALKFTSMWIGLNNPWKDCKWEWSD NARFDYKAWKRRPYCTVMVVKPDRIFWFTRGCEKSVSFVCKFLTDPAV ; 27 ? # 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 1UKM A 1 ? 134 ? Q7T2Q1 24 ? 157 ? 1 134 2 2 1UKM B 1 ? 128 ? Q7T2Q0 27 ? 154 ? 1 128 # _struct_ref_seq_dif.align_id 2 _struct_ref_seq_dif.pdbx_pdb_id_code 1UKM _struct_ref_seq_dif.mon_id SER _struct_ref_seq_dif.pdbx_pdb_strand_id B _struct_ref_seq_dif.seq_num 43 _struct_ref_seq_dif.pdbx_pdb_ins_code ? _struct_ref_seq_dif.pdbx_seq_db_name UNP _struct_ref_seq_dif.pdbx_seq_db_accession_code Q7T2Q0 _struct_ref_seq_dif.db_mon_id GLY _struct_ref_seq_dif.pdbx_seq_db_seq_num 69 _struct_ref_seq_dif.details 'SEE REMARK 999' _struct_ref_seq_dif.pdbx_auth_seq_num 43 _struct_ref_seq_dif.pdbx_ordinal 1 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight 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 CL non-polymer . 'CHLORIDE ION' ? 'Cl -1' 35.453 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 GOL non-polymer . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3' 92.094 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 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 1UKM _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.39 _exptl_crystal.density_percent_sol 48.10 _exptl_crystal.description ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 293 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 5.8 _exptl_crystal_grow.pdbx_details 'PEG8000, potassium dihydrogen phosphate, glycerol, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K' _exptl_crystal_grow.pdbx_pH_range ? # _diffrn.id 1 _diffrn.ambient_temp 120 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector 'IMAGE PLATE' _diffrn_detector.type 'RIGAKU RAXIS IV' _diffrn_detector.pdbx_collection_date 2002-08-12 _diffrn_detector.details 'Osmic confocal mirrors' # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'Osmic confocal' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.5418 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source 'ROTATING ANODE' _diffrn_source.type RIGAKU _diffrn_source.pdbx_synchrotron_site ? _diffrn_source.pdbx_synchrotron_beamline ? _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1.5418 # _reflns.entry_id 1UKM _reflns.observed_criterion_sigma_I 3.0 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 29.71 _reflns.d_resolution_high 1.90 _reflns.number_obs 26199 _reflns.number_all ? _reflns.percent_possible_obs 99.7 _reflns.pdbx_Rmerge_I_obs 0.031 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 16.1 _reflns.B_iso_Wilson_estimate 19.2 _reflns.pdbx_redundancy 3.6 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 1.90 _reflns_shell.d_res_low 1.97 _reflns_shell.percent_possible_all 99.7 _reflns_shell.Rmerge_I_obs 0.116 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 5.6 _reflns_shell.pdbx_redundancy 3.6 _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 1UKM _refine.ls_number_reflns_obs 26143 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 0.0 _refine.pdbx_data_cutoff_high_absF 1271064.40 _refine.pdbx_data_cutoff_low_absF 0.000000 _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 18.36 _refine.ls_d_res_high 1.90 _refine.ls_percent_reflns_obs 99.5 _refine.ls_R_factor_obs 0.196 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.196 _refine.ls_R_factor_R_free 0.233 _refine.ls_R_factor_R_free_error 0.006 _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.0 _refine.ls_number_reflns_R_free 1303 _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 27.7 _refine.aniso_B[1][1] 4.12 _refine.aniso_B[2][2] -1.31 _refine.aniso_B[3][3] -2.81 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details 'FLAT MODEL' _refine.solvent_model_param_ksol 0.394865 _refine.solvent_model_param_bsol 50.6729 _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details ? _refine.pdbx_starting_model 'PDB ENTRY 1BJ3' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model RESTRAINED _refine.pdbx_stereochemistry_target_values 'Engh & Huber' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML ? _refine.overall_SU_B ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_phase_error ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_analyze.entry_id 1UKM _refine_analyze.Luzzati_coordinate_error_obs 0.21 _refine_analyze.Luzzati_sigma_a_obs 0.14 _refine_analyze.Luzzati_d_res_low_obs 5.00 _refine_analyze.Luzzati_coordinate_error_free 0.26 _refine_analyze.Luzzati_sigma_a_free 0.21 _refine_analyze.Luzzati_d_res_low_free ? _refine_analyze.number_disordered_residues ? _refine_analyze.occupancy_sum_hydrogen ? _refine_analyze.occupancy_sum_non_hydrogen ? _refine_analyze.pdbx_Luzzati_d_res_high_obs ? _refine_analyze.pdbx_refine_id 'X-RAY DIFFRACTION' # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 2126 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 39 _refine_hist.number_atoms_solvent 250 _refine_hist.number_atoms_total 2415 _refine_hist.d_res_high 1.90 _refine_hist.d_res_low 18.36 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function c_bond_d 0.008 ? ? ? 'X-RAY DIFFRACTION' ? c_bond_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? c_bond_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? c_angle_d ? ? ? ? 'X-RAY DIFFRACTION' ? c_angle_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? c_angle_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? c_angle_deg 1.5 ? ? ? 'X-RAY DIFFRACTION' ? c_angle_deg_na ? ? ? ? 'X-RAY DIFFRACTION' ? c_angle_deg_prot ? ? ? ? 'X-RAY DIFFRACTION' ? c_dihedral_angle_d 22.8 ? ? ? 'X-RAY DIFFRACTION' ? c_dihedral_angle_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? c_dihedral_angle_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? c_improper_angle_d 0.81 ? ? ? 'X-RAY DIFFRACTION' ? c_improper_angle_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? c_improper_angle_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? c_mcbond_it 3.20 1.50 ? ? 'X-RAY DIFFRACTION' ? c_mcangle_it 3.84 2.00 ? ? 'X-RAY DIFFRACTION' ? c_scbond_it 4.66 2.00 ? ? 'X-RAY DIFFRACTION' ? c_scangle_it 6.27 2.50 ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_total_number_of_bins_used 6 _refine_ls_shell.d_res_high 1.90 _refine_ls_shell.d_res_low 2.02 _refine_ls_shell.number_reflns_R_work 4092 _refine_ls_shell.R_factor_R_work 0.274 _refine_ls_shell.percent_reflns_obs 100.0 _refine_ls_shell.R_factor_R_free 0.334 _refine_ls_shell.R_factor_R_free_error 0.023 _refine_ls_shell.percent_reflns_R_free 4.9 _refine_ls_shell.number_reflns_R_free 209 _refine_ls_shell.number_reflns_obs 4301 _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.number_reflns_all ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.R_factor_all ? # loop_ _pdbx_xplor_file.serial_no _pdbx_xplor_file.param_file _pdbx_xplor_file.topol_file _pdbx_xplor_file.pdbx_refine_id 1 PROTEIN_REP.PARAM PROTEIN.TOP 'X-RAY DIFFRACTION' 2 HETERO.PARAM HETERO.TOP 'X-RAY DIFFRACTION' 3 WATER_REP.PARAM WATER.TOP 'X-RAY DIFFRACTION' 4 ION.PARAM ION.TOP 'X-RAY DIFFRACTION' 5 CARBO_REP.PARAM CARBOHYDRATE.TOP 'X-RAY DIFFRACTION' # _struct.entry_id 1UKM _struct.title 'Crystal structure of EMS16, an Antagonist of collagen receptor integrin alpha2beta1 (GPIa/IIa)' _struct.pdbx_descriptor 'EMS16 A chain/EMS16 B chain' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 1UKM _struct_keywords.pdbx_keywords TOXIN _struct_keywords.text 'Domain swapping, C-type lectin, TOXIN' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 4 ? E N N 4 ? F N N 4 ? G N N 5 ? H N N 4 ? I N N 6 ? J N N 6 ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 ASN A 24 ? ALA A 36 ? ASN A 24 ALA A 36 1 ? 13 HELX_P HELX_P2 2 SER A 46 ? VAL A 57 ? SER A 46 VAL A 57 1 ? 12 HELX_P HELX_P3 3 SER A 58 ? ARG A 63 ? SER A 58 ARG A 63 5 ? 6 HELX_P HELX_P4 4 TRP A 110 ? ASN A 112 ? TRP A 110 ASN A 112 5 ? 3 HELX_P HELX_P5 5 ASN B 21 ? HIS B 33 ? ASN B 21 HIS B 33 1 ? 13 HELX_P HELX_P6 6 SER B 43 ? LEU B 58 ? SER B 43 LEU B 58 1 ? 16 # _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 4 SG ? ? ? 1_555 A CYS 15 SG ? ? A CYS 4 A CYS 15 1_555 ? ? ? ? ? ? ? 2.024 ? disulf2 disulf ? ? A CYS 32 SG ? ? ? 1_555 A CYS 129 SG ? ? A CYS 32 A CYS 129 1_555 ? ? ? ? ? ? ? 2.036 ? disulf3 disulf ? ? A CYS 81 SG ? ? ? 1_555 B CYS 74 SG ? ? A CYS 81 B CYS 74 1_555 ? ? ? ? ? ? ? 2.028 ? disulf4 disulf ? ? A CYS 104 SG ? ? ? 1_555 A CYS 121 SG ? ? A CYS 104 A CYS 121 1_555 ? ? ? ? ? ? ? 2.034 ? disulf5 disulf ? ? B CYS 1 SG ? ? ? 1_555 B CYS 12 SG ? ? B CYS 1 B CYS 12 1_555 ? ? ? ? ? ? ? 2.036 ? disulf6 disulf ? ? B CYS 29 SG ? ? ? 1_555 B CYS 120 SG ? ? B CYS 29 B CYS 120 1_555 ? ? ? ? ? ? ? 2.038 ? disulf7 disulf ? ? B CYS 95 SG ? ? ? 1_555 B CYS 112 SG ? ? B CYS 95 B CYS 112 1_555 ? ? ? ? ? ? ? 2.052 ? covale1 covale ? ? B ASN 21 ND2 ? ? ? 1_555 G NAG . C1 ? ? B ASN 21 B NAG 1022 1_555 ? ? ? ? ? ? ? 1.455 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 4 ? B ? 4 ? C ? 4 ? D ? 6 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? anti-parallel C 1 2 ? anti-parallel C 2 3 ? anti-parallel C 3 4 ? anti-parallel D 1 2 ? anti-parallel D 2 3 ? anti-parallel D 3 4 ? parallel D 4 5 ? anti-parallel D 5 6 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 THR A 9 ? TYR A 11 ? THR A 9 TYR A 11 A 2 HIS A 14 ? GLN A 23 ? HIS A 14 GLN A 23 A 3 TYR A 125 ? SER A 132 ? TYR A 125 SER A 132 A 4 HIS A 40 ? LEU A 41 ? HIS A 40 LEU A 41 B 1 TRP A 116 ? ILE A 119 ? TRP A 116 ILE A 119 B 2 CYS A 104 ? THR A 108 ? CYS A 104 THR A 108 B 3 TYR A 67 ? ASP A 74 ? TYR A 67 ASP A 74 B 4 TRP B 76 ? TRP B 78 ? TRP B 76 TRP B 78 C 1 SER B 6 ? PHE B 8 ? SER B 6 PHE B 8 C 2 HIS B 11 ? LYS B 20 ? HIS B 11 LYS B 20 C 3 VAL B 116 ? LEU B 123 ? VAL B 116 LEU B 123 C 4 ARG B 37 ? LEU B 38 ? ARG B 37 LEU B 38 D 1 SER B 6 ? PHE B 8 ? SER B 6 PHE B 8 D 2 HIS B 11 ? LYS B 20 ? HIS B 11 LYS B 20 D 3 VAL B 116 ? LEU B 123 ? VAL B 116 LEU B 123 D 4 SER B 62 ? ASN B 68 ? SER B 62 ASN B 68 D 5 TYR B 94 ? VAL B 100 ? TYR B 94 VAL B 100 D 6 ILE B 105 ? GLY B 111 ? ILE B 105 GLY B 111 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 N THR A 9 ? N THR A 9 O TYR A 16 ? O TYR A 16 A 2 3 N ILE A 19 ? N ILE A 19 O PHE A 127 ? O PHE A 127 A 3 4 O LYS A 130 ? O LYS A 130 N HIS A 40 ? N HIS A 40 B 1 2 O ILE A 119 ? O ILE A 119 N CYS A 104 ? N CYS A 104 B 2 3 O LEU A 107 ? O LEU A 107 N VAL A 68 ? N VAL A 68 B 3 4 N ARG A 73 ? N ARG A 73 O GLU B 77 ? O GLU B 77 C 1 2 N SER B 6 ? N SER B 6 O TYR B 13 ? O TYR B 13 C 2 3 N PHE B 16 ? N PHE B 16 O PHE B 118 ? O PHE B 118 C 3 4 O LYS B 121 ? O LYS B 121 N ARG B 37 ? N ARG B 37 D 1 2 N SER B 6 ? N SER B 6 O TYR B 13 ? O TYR B 13 D 2 3 N PHE B 16 ? N PHE B 16 O PHE B 118 ? O PHE B 118 D 3 4 O SER B 117 ? O SER B 117 N TRP B 64 ? N TRP B 64 D 4 5 N MET B 63 ? N MET B 63 O MET B 98 ? O MET B 98 D 5 6 N CYS B 95 ? N CYS B 95 O ARG B 110 ? O ARG B 110 # 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 ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG B 1022' AC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CL A 1304' AC3 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE GOL A 1300' AC4 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE GOL A 1301' AC5 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE GOL A 1302' AC6 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE GOL B 1303' # 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 4 ASN B 21 ? ASN B 21 . ? 1_555 ? 2 AC1 4 THR B 23 ? THR B 23 . ? 1_555 ? 3 AC1 4 GLU B 24 ? GLU B 24 . ? 1_555 ? 4 AC1 4 GLU B 113 ? GLU B 113 . ? 1_555 ? 5 AC2 4 TRP A 25 ? TRP A 25 . ? 1_555 ? 6 AC2 4 ARG A 73 ? ARG A 73 . ? 1_555 ? 7 AC2 4 ARG A 75 ? ARG A 75 . ? 1_555 ? 8 AC2 4 HOH I . ? HOH A 1339 . ? 1_555 ? 9 AC3 6 ARG A 76 ? ARG A 76 . ? 1_555 ? 10 AC3 6 GLU A 78 ? GLU A 78 . ? 1_555 ? 11 AC3 6 GLN A 80 ? GLN A 80 . ? 1_555 ? 12 AC3 6 CYS A 81 ? CYS A 81 . ? 1_555 ? 13 AC3 6 ASN A 82 ? ASN A 82 . ? 1_555 ? 14 AC3 6 HOH I . ? HOH A 1379 . ? 1_555 ? 15 AC4 3 LYS A 97 ? LYS A 97 . ? 1_555 ? 16 AC4 3 HOH I . ? HOH A 1338 . ? 1_555 ? 17 AC4 3 PHE B 106 ? PHE B 106 . ? 1_555 ? 18 AC5 5 CYS A 4 ? CYS A 4 . ? 1_555 ? 19 AC5 5 THR A 9 ? THR A 9 . ? 1_555 ? 20 AC5 5 ALA A 10 ? ALA A 10 . ? 1_555 ? 21 AC5 5 HOH I . ? HOH A 1428 . ? 1_555 ? 22 AC5 5 ARG B 92 ? ARG B 92 . ? 3_655 ? 23 AC6 6 LYS A 102 ? LYS A 102 . ? 1_555 ? 24 AC6 6 ASN A 117 ? ASN A 117 . ? 1_555 ? 25 AC6 6 HOH I . ? HOH A 1356 . ? 1_555 ? 26 AC6 6 ARG B 91 ? ARG B 91 . ? 1_555 ? 27 AC6 6 TYR B 94 ? TYR B 94 . ? 1_555 ? 28 AC6 6 HOH J . ? HOH B 1329 . ? 1_555 ? # _database_PDB_matrix.entry_id 1UKM _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 1UKM _atom_sites.fract_transf_matrix[1][1] 0.021473 _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] 0.016685 _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] 0.008640 _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 CL 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 . ASP A 1 3 ? 25.387 30.539 13.182 1.00 48.52 ? 3 ASP A N 1 ATOM 2 C CA . ASP A 1 3 ? 26.351 30.714 14.309 1.00 50.52 ? 3 ASP A CA 1 ATOM 3 C C . ASP A 1 3 ? 25.637 30.930 15.638 1.00 47.03 ? 3 ASP A C 1 ATOM 4 O O . ASP A 1 3 ? 24.412 31.042 15.691 1.00 51.89 ? 3 ASP A O 1 ATOM 5 C CB . ASP A 1 3 ? 27.271 31.921 14.063 1.00 46.90 ? 3 ASP A CB 1 ATOM 6 C CG . ASP A 1 3 ? 28.270 31.683 12.949 1.00 55.21 ? 3 ASP A CG 1 ATOM 7 O OD1 . ASP A 1 3 ? 29.353 32.323 12.975 1.00 47.59 ? 3 ASP A OD1 1 ATOM 8 O OD2 . ASP A 1 3 ? 27.970 30.867 12.048 1.00 47.99 ? 3 ASP A OD2 1 ATOM 9 N N . CYS A 1 4 ? 26.426 30.991 16.705 1.00 41.51 ? 4 CYS A N 1 ATOM 10 C CA . CYS A 1 4 ? 25.916 31.236 18.049 1.00 34.27 ? 4 CYS A CA 1 ATOM 11 C C . CYS A 1 4 ? 26.802 32.302 18.662 1.00 32.34 ? 4 CYS A C 1 ATOM 12 O O . CYS A 1 4 ? 27.968 32.436 18.292 1.00 27.55 ? 4 CYS A O 1 ATOM 13 C CB . CYS A 1 4 ? 25.981 29.961 18.895 1.00 31.13 ? 4 CYS A CB 1 ATOM 14 S SG . CYS A 1 4 ? 24.773 28.711 18.379 1.00 28.46 ? 4 CYS A SG 1 ATOM 15 N N . PRO A 1 5 ? 26.263 33.081 19.607 1.00 26.70 ? 5 PRO A N 1 ATOM 16 C CA . PRO A 1 5 ? 27.049 34.135 20.249 1.00 27.25 ? 5 PRO A CA 1 ATOM 17 C C . PRO A 1 5 ? 28.048 33.626 21.279 1.00 28.57 ? 5 PRO A C 1 ATOM 18 O O . PRO A 1 5 ? 27.921 32.511 21.801 1.00 25.04 ? 5 PRO A O 1 ATOM 19 C CB . PRO A 1 5 ? 25.980 34.999 20.903 1.00 28.99 ? 5 PRO A CB 1 ATOM 20 C CG . PRO A 1 5 ? 24.970 33.968 21.321 1.00 24.17 ? 5 PRO A CG 1 ATOM 21 C CD . PRO A 1 5 ? 24.872 33.095 20.098 1.00 28.15 ? 5 PRO A CD 1 ATOM 22 N N . SER A 1 6 ? 29.038 34.470 21.561 1.00 23.37 ? 6 SER A N 1 ATOM 23 C CA . SER A 1 6 ? 30.060 34.203 22.561 1.00 22.44 ? 6 SER A CA 1 ATOM 24 C C . SER A 1 6 ? 30.537 32.752 22.597 1.00 24.41 ? 6 SER A C 1 ATOM 25 O O . SER A 1 6 ? 31.058 32.242 21.605 1.00 22.96 ? 6 SER A O 1 ATOM 26 C CB . SER A 1 6 ? 29.520 34.622 23.935 1.00 23.75 ? 6 SER A CB 1 ATOM 27 O OG . SER A 1 6 ? 29.175 35.999 23.918 1.00 25.59 ? 6 SER A OG 1 ATOM 28 N N . ASP A 1 7 ? 30.368 32.104 23.748 1.00 22.86 ? 7 ASP A N 1 ATOM 29 C CA . ASP A 1 7 ? 30.785 30.718 23.905 1.00 24.74 ? 7 ASP A CA 1 ATOM 30 C C . ASP A 1 7 ? 29.646 29.690 23.815 1.00 26.30 ? 7 ASP A C 1 ATOM 31 O O . ASP A 1 7 ? 29.800 28.532 24.229 1.00 22.80 ? 7 ASP A O 1 ATOM 32 C CB . ASP A 1 7 ? 31.556 30.553 25.218 1.00 27.39 ? 7 ASP A CB 1 ATOM 33 C CG . ASP A 1 7 ? 30.797 31.098 26.436 1.00 28.93 ? 7 ASP A CG 1 ATOM 34 O OD1 . ASP A 1 7 ? 31.284 30.894 27.567 1.00 34.26 ? 7 ASP A OD1 1 ATOM 35 O OD2 . ASP A 1 7 ? 29.732 31.728 26.271 1.00 21.43 ? 7 ASP A OD2 1 ATOM 36 N N . TRP A 1 8 ? 28.511 30.098 23.259 1.00 20.14 ? 8 TRP A N 1 ATOM 37 C CA . TRP A 1 8 ? 27.384 29.180 23.109 1.00 19.57 ? 8 TRP A CA 1 ATOM 38 C C . TRP A 1 8 ? 27.716 28.178 21.997 1.00 25.84 ? 8 TRP A C 1 ATOM 39 O O . TRP A 1 8 ? 28.423 28.509 21.040 1.00 23.96 ? 8 TRP A O 1 ATOM 40 C CB . TRP A 1 8 ? 26.100 29.952 22.772 1.00 20.54 ? 8 TRP A CB 1 ATOM 41 C CG . TRP A 1 8 ? 25.572 30.791 23.922 1.00 27.04 ? 8 TRP A CG 1 ATOM 42 C CD1 . TRP A 1 8 ? 26.180 31.866 24.510 1.00 24.30 ? 8 TRP A CD1 1 ATOM 43 C CD2 . TRP A 1 8 ? 24.323 30.611 24.610 1.00 19.98 ? 8 TRP A CD2 1 ATOM 44 N NE1 . TRP A 1 8 ? 25.383 32.372 25.521 1.00 21.06 ? 8 TRP A NE1 1 ATOM 45 C CE2 . TRP A 1 8 ? 24.240 31.616 25.602 1.00 25.28 ? 8 TRP A CE2 1 ATOM 46 C CE3 . TRP A 1 8 ? 23.270 29.692 24.488 1.00 19.27 ? 8 TRP A CE3 1 ATOM 47 C CZ2 . TRP A 1 8 ? 23.145 31.728 26.464 1.00 19.10 ? 8 TRP A CZ2 1 ATOM 48 C CZ3 . TRP A 1 8 ? 22.173 29.802 25.353 1.00 20.65 ? 8 TRP A CZ3 1 ATOM 49 C CH2 . TRP A 1 8 ? 22.125 30.818 26.328 1.00 19.27 ? 8 TRP A CH2 1 ATOM 50 N N . THR A 1 9 ? 27.217 26.955 22.122 1.00 24.76 ? 9 THR A N 1 ATOM 51 C CA . THR A 1 9 ? 27.501 25.915 21.129 1.00 20.22 ? 9 THR A CA 1 ATOM 52 C C . THR A 1 9 ? 26.282 25.641 20.251 1.00 26.12 ? 9 THR A C 1 ATOM 53 O O . THR A 1 9 ? 25.153 25.542 20.745 1.00 19.86 ? 9 THR A O 1 ATOM 54 C CB . THR A 1 9 ? 27.943 24.606 21.828 1.00 18.74 ? 9 THR A CB 1 ATOM 55 O OG1 . THR A 1 9 ? 29.084 24.877 22.656 1.00 22.50 ? 9 THR A OG1 1 ATOM 56 C CG2 . THR A 1 9 ? 28.310 23.534 20.792 1.00 17.73 ? 9 THR A CG2 1 ATOM 57 N N . ALA A 1 10 ? 26.511 25.507 18.946 1.00 25.52 ? 10 ALA A N 1 ATOM 58 C CA . ALA A 1 10 ? 25.427 25.263 18.000 1.00 25.85 ? 10 ALA A CA 1 ATOM 59 C C . ALA A 1 10 ? 25.098 23.786 17.772 1.00 25.66 ? 10 ALA A C 1 ATOM 60 O O . ALA A 1 10 ? 25.973 22.926 17.833 1.00 26.34 ? 10 ALA A O 1 ATOM 61 C CB . ALA A 1 10 ? 25.759 25.928 16.652 1.00 30.28 ? 10 ALA A CB 1 ATOM 62 N N . TYR A 1 11 ? 23.819 23.516 17.523 1.00 24.33 ? 11 TYR A N 1 ATOM 63 C CA . TYR A 1 11 ? 23.323 22.175 17.233 1.00 24.60 ? 11 TYR A CA 1 ATOM 64 C C . TYR A 1 11 ? 21.924 22.301 16.660 1.00 28.41 ? 11 TYR A C 1 ATOM 65 O O . TYR A 1 11 ? 21.062 22.992 17.222 1.00 25.34 ? 11 TYR A O 1 ATOM 66 C CB . TYR A 1 11 ? 23.262 21.287 18.475 1.00 28.89 ? 11 TYR A CB 1 ATOM 67 C CG . TYR A 1 11 ? 22.651 19.922 18.191 1.00 29.81 ? 11 TYR A CG 1 ATOM 68 C CD1 . TYR A 1 11 ? 23.444 18.855 17.766 1.00 29.15 ? 11 TYR A CD1 1 ATOM 69 C CD2 . TYR A 1 11 ? 21.272 19.714 18.296 1.00 32.67 ? 11 TYR A CD2 1 ATOM 70 C CE1 . TYR A 1 11 ? 22.886 17.621 17.454 1.00 30.35 ? 11 TYR A CE1 1 ATOM 71 C CE2 . TYR A 1 11 ? 20.700 18.476 17.980 1.00 30.11 ? 11 TYR A CE2 1 ATOM 72 C CZ . TYR A 1 11 ? 21.518 17.436 17.559 1.00 35.26 ? 11 TYR A CZ 1 ATOM 73 O OH . TYR A 1 11 ? 20.976 16.208 17.246 1.00 31.42 ? 11 TYR A OH 1 ATOM 74 N N . ASP A 1 12 ? 21.714 21.637 15.527 1.00 30.82 ? 12 ASP A N 1 ATOM 75 C CA . ASP A 1 12 ? 20.433 21.635 14.838 1.00 33.61 ? 12 ASP A CA 1 ATOM 76 C C . ASP A 1 12 ? 19.684 22.960 14.882 1.00 30.88 ? 12 ASP A C 1 ATOM 77 O O . ASP A 1 12 ? 18.528 23.019 15.294 1.00 35.45 ? 12 ASP A O 1 ATOM 78 C CB . ASP A 1 12 ? 19.543 20.519 15.392 1.00 34.77 ? 12 ASP A CB 1 ATOM 79 C CG . ASP A 1 12 ? 18.236 20.383 14.625 1.00 48.38 ? 12 ASP A CG 1 ATOM 80 O OD1 . ASP A 1 12 ? 18.239 20.624 13.396 1.00 45.97 ? 12 ASP A OD1 1 ATOM 81 O OD2 . ASP A 1 12 ? 17.211 20.023 15.245 1.00 48.67 ? 12 ASP A OD2 1 ATOM 82 N N . GLN A 1 13 ? 20.357 24.025 14.465 1.00 35.87 ? 13 GLN A N 1 ATOM 83 C CA . GLN A 1 13 ? 19.760 25.356 14.409 1.00 33.06 ? 13 GLN A CA 1 ATOM 84 C C . GLN A 1 13 ? 19.439 26.026 15.747 1.00 34.94 ? 13 GLN A C 1 ATOM 85 O O . GLN A 1 13 ? 18.641 26.964 15.799 1.00 32.51 ? 13 GLN A O 1 ATOM 86 C CB . GLN A 1 13 ? 18.505 25.319 13.530 1.00 41.34 ? 13 GLN A CB 1 ATOM 87 C CG . GLN A 1 13 ? 18.796 24.869 12.101 1.00 49.72 ? 13 GLN A CG 1 ATOM 88 C CD . GLN A 1 13 ? 17.542 24.714 11.261 1.00 57.46 ? 13 GLN A CD 1 ATOM 89 O OE1 . GLN A 1 13 ? 16.662 23.913 11.579 1.00 63.32 ? 13 GLN A OE1 1 ATOM 90 N NE2 . GLN A 1 13 ? 17.455 25.482 10.179 1.00 59.85 ? 13 GLN A NE2 1 ATOM 91 N N . HIS A 1 14 ? 20.047 25.546 16.827 1.00 29.37 ? 14 HIS A N 1 ATOM 92 C CA . HIS A 1 14 ? 19.846 26.169 18.128 1.00 27.07 ? 14 HIS A CA 1 ATOM 93 C C . HIS A 1 14 ? 21.195 26.395 18.789 1.00 27.72 ? 14 HIS A C 1 ATOM 94 O O . HIS A 1 14 ? 22.208 25.829 18.359 1.00 22.03 ? 14 HIS A O 1 ATOM 95 C CB . HIS A 1 14 ? 18.960 25.299 19.023 1.00 24.23 ? 14 HIS A CB 1 ATOM 96 C CG . HIS A 1 14 ? 17.534 25.247 18.578 1.00 29.84 ? 14 HIS A CG 1 ATOM 97 N ND1 . HIS A 1 14 ? 17.130 24.539 17.467 1.00 29.36 ? 14 HIS A ND1 1 ATOM 98 C CD2 . HIS A 1 14 ? 16.423 25.847 19.069 1.00 25.90 ? 14 HIS A CD2 1 ATOM 99 C CE1 . HIS A 1 14 ? 15.831 24.705 17.293 1.00 29.36 ? 14 HIS A CE1 1 ATOM 100 N NE2 . HIS A 1 14 ? 15.378 25.494 18.250 1.00 26.52 ? 14 HIS A NE2 1 ATOM 101 N N . CYS A 1 15 ? 21.208 27.242 19.817 1.00 19.82 ? 15 CYS A N 1 ATOM 102 C CA . CYS A 1 15 ? 22.423 27.540 20.560 1.00 19.27 ? 15 CYS A CA 1 ATOM 103 C C . CYS A 1 15 ? 22.226 27.066 21.991 1.00 19.43 ? 15 CYS A C 1 ATOM 104 O O . CYS A 1 15 ? 21.150 27.243 22.558 1.00 18.90 ? 15 CYS A O 1 ATOM 105 C CB . CYS A 1 15 ? 22.705 29.040 20.532 1.00 21.19 ? 15 CYS A CB 1 ATOM 106 S SG . CYS A 1 15 ? 22.998 29.583 18.811 1.00 27.68 ? 15 CYS A SG 1 ATOM 107 N N . TYR A 1 16 ? 23.277 26.495 22.567 1.00 19.80 ? 16 TYR A N 1 ATOM 108 C CA . TYR A 1 16 ? 23.219 25.956 23.922 1.00 17.94 ? 16 TYR A CA 1 ATOM 109 C C . TYR A 1 16 ? 24.389 26.429 24.774 1.00 18.94 ? 16 TYR A C 1 ATOM 110 O O . TYR A 1 16 ? 25.464 26.716 24.256 1.00 19.61 ? 16 TYR A O 1 ATOM 111 C CB . TYR A 1 16 ? 23.280 24.428 23.872 1.00 16.17 ? 16 TYR A CB 1 ATOM 112 C CG . TYR A 1 16 ? 22.255 23.767 23.004 1.00 20.60 ? 16 TYR A CG 1 ATOM 113 C CD1 . TYR A 1 16 ? 22.306 23.881 21.613 1.00 26.33 ? 16 TYR A CD1 1 ATOM 114 C CD2 . TYR A 1 16 ? 21.238 22.998 23.570 1.00 20.72 ? 16 TYR A CD2 1 ATOM 115 C CE1 . TYR A 1 16 ? 21.365 23.242 20.806 1.00 25.14 ? 16 TYR A CE1 1 ATOM 116 C CE2 . TYR A 1 16 ? 20.301 22.361 22.780 1.00 14.11 ? 16 TYR A CE2 1 ATOM 117 C CZ . TYR A 1 16 ? 20.366 22.487 21.399 1.00 24.11 ? 16 TYR A CZ 1 ATOM 118 O OH . TYR A 1 16 ? 19.425 21.866 20.622 1.00 22.46 ? 16 TYR A OH 1 ATOM 119 N N . LEU A 1 17 ? 24.192 26.466 26.090 1.00 14.90 ? 17 LEU A N 1 ATOM 120 C CA . LEU A 1 17 ? 25.261 26.869 26.987 1.00 17.25 ? 17 LEU A CA 1 ATOM 121 C C . LEU A 1 17 ? 25.077 26.167 28.324 1.00 21.52 ? 17 LEU A C 1 ATOM 122 O O . LEU A 1 17 ? 23.974 26.170 28.875 1.00 19.16 ? 17 LEU A O 1 ATOM 123 C CB . LEU A 1 17 ? 25.253 28.393 27.205 1.00 20.77 ? 17 LEU A CB 1 ATOM 124 C CG . LEU A 1 17 ? 26.313 28.929 28.183 1.00 23.87 ? 17 LEU A CG 1 ATOM 125 C CD1 . LEU A 1 17 ? 27.708 28.678 27.613 1.00 25.44 ? 17 LEU A CD1 1 ATOM 126 C CD2 . LEU A 1 17 ? 26.110 30.430 28.417 1.00 24.17 ? 17 LEU A CD2 1 ATOM 127 N N . ALA A 1 18 ? 26.143 25.544 28.825 1.00 19.23 ? 18 ALA A N 1 ATOM 128 C CA . ALA A 1 18 ? 26.069 24.865 30.117 1.00 17.06 ? 18 ALA A CA 1 ATOM 129 C C . ALA A 1 18 ? 26.429 25.885 31.199 1.00 20.80 ? 18 ALA A C 1 ATOM 130 O O . ALA A 1 18 ? 27.433 26.594 31.085 1.00 20.06 ? 18 ALA A O 1 ATOM 131 C CB . ALA A 1 18 ? 27.041 23.680 30.155 1.00 18.32 ? 18 ALA A CB 1 ATOM 132 N N . ILE A 1 19 ? 25.611 25.971 32.245 1.00 17.81 ? 19 ILE A N 1 ATOM 133 C CA . ILE A 1 19 ? 25.867 26.926 33.322 1.00 15.57 ? 19 ILE A CA 1 ATOM 134 C C . ILE A 1 19 ? 26.283 26.185 34.599 1.00 17.09 ? 19 ILE A C 1 ATOM 135 O O . ILE A 1 19 ? 25.507 25.396 35.144 1.00 19.67 ? 19 ILE A O 1 ATOM 136 C CB . ILE A 1 19 ? 24.593 27.777 33.611 1.00 22.53 ? 19 ILE A CB 1 ATOM 137 C CG1 . ILE A 1 19 ? 24.159 28.538 32.351 1.00 20.50 ? 19 ILE A CG1 1 ATOM 138 C CG2 . ILE A 1 19 ? 24.869 28.767 34.738 1.00 22.48 ? 19 ILE A CG2 1 ATOM 139 C CD1 . ILE A 1 19 ? 25.181 29.540 31.844 1.00 31.42 ? 19 ILE A CD1 1 ATOM 140 N N . GLY A 1 20 ? 27.493 26.461 35.081 1.00 16.13 ? 20 GLY A N 1 ATOM 141 C CA . GLY A 1 20 ? 28.007 25.794 36.271 1.00 20.42 ? 20 GLY A CA 1 ATOM 142 C C . GLY A 1 20 ? 27.500 26.238 37.633 1.00 22.84 ? 20 GLY A C 1 ATOM 143 O O . GLY A 1 20 ? 27.454 25.421 38.564 1.00 24.88 ? 20 GLY A O 1 ATOM 144 N N . GLU A 1 21 ? 27.124 27.509 37.775 1.00 20.06 ? 21 GLU A N 1 ATOM 145 C CA . GLU A 1 21 ? 26.611 28.008 39.059 1.00 25.94 ? 21 GLU A CA 1 ATOM 146 C C . GLU A 1 21 ? 25.230 27.404 39.331 1.00 18.44 ? 21 GLU A C 1 ATOM 147 O O . GLU A 1 21 ? 24.278 27.664 38.596 1.00 23.80 ? 21 GLU A O 1 ATOM 148 C CB . GLU A 1 21 ? 26.510 29.534 39.036 1.00 29.23 ? 21 GLU A CB 1 ATOM 149 C CG . GLU A 1 21 ? 27.803 30.257 39.387 1.00 53.54 ? 21 GLU A CG 1 ATOM 150 C CD . GLU A 1 21 ? 28.188 30.101 40.854 1.00 59.73 ? 21 GLU A CD 1 ATOM 151 O OE1 . GLU A 1 21 ? 28.523 28.967 41.273 1.00 63.54 ? 21 GLU A OE1 1 ATOM 152 O OE2 . GLU A 1 21 ? 28.153 31.117 41.590 1.00 63.62 ? 21 GLU A OE2 1 ATOM 153 N N . PRO A 1 22 ? 25.095 26.615 40.408 1.00 18.90 ? 22 PRO A N 1 ATOM 154 C CA . PRO A 1 22 ? 23.798 25.993 40.708 1.00 20.41 ? 22 PRO A CA 1 ATOM 155 C C . PRO A 1 22 ? 22.680 26.936 41.133 1.00 23.89 ? 22 PRO A C 1 ATOM 156 O O . PRO A 1 22 ? 22.911 27.894 41.879 1.00 17.81 ? 22 PRO A O 1 ATOM 157 C CB . PRO A 1 22 ? 24.142 24.960 41.786 1.00 15.95 ? 22 PRO A CB 1 ATOM 158 C CG . PRO A 1 22 ? 25.316 25.577 42.486 1.00 26.60 ? 22 PRO A CG 1 ATOM 159 C CD . PRO A 1 22 ? 26.137 26.170 41.355 1.00 22.55 ? 22 PRO A CD 1 ATOM 160 N N . GLN A 1 23 ? 21.474 26.635 40.649 1.00 18.66 ? 23 GLN A N 1 ATOM 161 C CA . GLN A 1 23 ? 20.254 27.401 40.928 1.00 17.56 ? 23 GLN A CA 1 ATOM 162 C C . GLN A 1 23 ? 19.103 26.397 41.014 1.00 15.90 ? 23 GLN A C 1 ATOM 163 O O . GLN A 1 23 ? 19.251 25.265 40.554 1.00 16.74 ? 23 GLN A O 1 ATOM 164 C CB . GLN A 1 23 ? 19.977 28.355 39.763 1.00 19.27 ? 23 GLN A CB 1 ATOM 165 C CG . GLN A 1 23 ? 20.964 29.490 39.656 1.00 28.60 ? 23 GLN A CG 1 ATOM 166 C CD . GLN A 1 23 ? 20.586 30.640 40.553 1.00 41.32 ? 23 GLN A CD 1 ATOM 167 O OE1 . GLN A 1 23 ? 20.620 30.527 41.781 1.00 40.98 ? 23 GLN A OE1 1 ATOM 168 N NE2 . GLN A 1 23 ? 20.198 31.756 39.943 1.00 44.39 ? 23 GLN A NE2 1 ATOM 169 N N . ASN A 1 24 ? 17.963 26.778 41.592 1.00 14.72 ? 24 ASN A N 1 ATOM 170 C CA . ASN A 1 24 ? 16.862 25.821 41.619 1.00 16.20 ? 24 ASN A CA 1 ATOM 171 C C . ASN A 1 24 ? 16.233 25.859 40.225 1.00 13.83 ? 24 ASN A C 1 ATOM 172 O O . ASN A 1 24 ? 16.638 26.677 39.382 1.00 17.04 ? 24 ASN A O 1 ATOM 173 C CB . ASN A 1 24 ? 15.839 26.088 42.761 1.00 14.88 ? 24 ASN A CB 1 ATOM 174 C CG . ASN A 1 24 ? 14.987 27.347 42.575 1.00 19.92 ? 24 ASN A CG 1 ATOM 175 O OD1 . ASN A 1 24 ? 14.711 27.794 41.463 1.00 16.68 ? 24 ASN A OD1 1 ATOM 176 N ND2 . ASN A 1 24 ? 14.515 27.894 43.705 1.00 15.62 ? 24 ASN A ND2 1 ATOM 177 N N . TRP A 1 25 ? 15.289 24.975 39.949 1.00 13.68 ? 25 TRP A N 1 ATOM 178 C CA . TRP A 1 25 ? 14.710 24.924 38.597 1.00 15.32 ? 25 TRP A CA 1 ATOM 179 C C . TRP A 1 25 ? 14.126 26.259 38.119 1.00 16.76 ? 25 TRP A C 1 ATOM 180 O O . TRP A 1 25 ? 14.374 26.699 36.980 1.00 14.20 ? 25 TRP A O 1 ATOM 181 C CB . TRP A 1 25 ? 13.637 23.820 38.522 1.00 15.66 ? 25 TRP A CB 1 ATOM 182 C CG . TRP A 1 25 ? 13.174 23.534 37.124 1.00 14.63 ? 25 TRP A CG 1 ATOM 183 C CD1 . TRP A 1 25 ? 13.615 22.528 36.291 1.00 14.09 ? 25 TRP A CD1 1 ATOM 184 C CD2 . TRP A 1 25 ? 12.219 24.288 36.371 1.00 15.05 ? 25 TRP A CD2 1 ATOM 185 N NE1 . TRP A 1 25 ? 12.990 22.621 35.075 1.00 16.39 ? 25 TRP A NE1 1 ATOM 186 C CE2 . TRP A 1 25 ? 12.134 23.694 35.090 1.00 15.94 ? 25 TRP A CE2 1 ATOM 187 C CE3 . TRP A 1 25 ? 11.427 25.417 36.654 1.00 16.78 ? 25 TRP A CE3 1 ATOM 188 C CZ2 . TRP A 1 25 ? 11.290 24.190 34.082 1.00 16.62 ? 25 TRP A CZ2 1 ATOM 189 C CZ3 . TRP A 1 25 ? 10.580 25.912 35.648 1.00 16.33 ? 25 TRP A CZ3 1 ATOM 190 C CH2 . TRP A 1 25 ? 10.522 25.298 34.379 1.00 14.76 ? 25 TRP A CH2 1 ATOM 191 N N . TYR A 1 26 ? 13.356 26.913 38.981 1.00 15.43 ? 26 TYR A N 1 ATOM 192 C CA . TYR A 1 26 ? 12.735 28.187 38.610 1.00 15.01 ? 26 TYR A CA 1 ATOM 193 C C . TYR A 1 26 ? 13.762 29.279 38.302 1.00 17.84 ? 26 TYR A C 1 ATOM 194 O O . TYR A 1 26 ? 13.612 30.028 37.329 1.00 16.84 ? 26 TYR A O 1 ATOM 195 C CB . TYR A 1 26 ? 11.806 28.677 39.734 1.00 18.46 ? 26 TYR A CB 1 ATOM 196 C CG . TYR A 1 26 ? 10.856 27.607 40.233 1.00 19.06 ? 26 TYR A CG 1 ATOM 197 C CD1 . TYR A 1 26 ? 9.781 27.179 39.449 1.00 18.85 ? 26 TYR A CD1 1 ATOM 198 C CD2 . TYR A 1 26 ? 11.061 26.985 41.467 1.00 17.00 ? 26 TYR A CD2 1 ATOM 199 C CE1 . TYR A 1 26 ? 8.938 26.162 39.874 1.00 26.23 ? 26 TYR A CE1 1 ATOM 200 C CE2 . TYR A 1 26 ? 10.219 25.963 41.899 1.00 22.91 ? 26 TYR A CE2 1 ATOM 201 C CZ . TYR A 1 26 ? 9.161 25.559 41.095 1.00 22.35 ? 26 TYR A CZ 1 ATOM 202 O OH . TYR A 1 26 ? 8.331 24.550 41.514 1.00 25.07 ? 26 TYR A OH 1 ATOM 203 N N . GLU A 1 27 ? 14.792 29.376 39.141 1.00 16.24 ? 27 GLU A N 1 ATOM 204 C CA . GLU A 1 27 ? 15.838 30.385 38.974 1.00 15.26 ? 27 GLU A CA 1 ATOM 205 C C . GLU A 1 27 ? 16.672 30.101 37.721 1.00 15.99 ? 27 GLU A C 1 ATOM 206 O O . GLU A 1 27 ? 17.143 31.028 37.050 1.00 17.32 ? 27 GLU A O 1 ATOM 207 C CB . GLU A 1 27 ? 16.759 30.391 40.194 1.00 17.49 ? 27 GLU A CB 1 ATOM 208 C CG . GLU A 1 27 ? 16.112 30.811 41.498 1.00 22.97 ? 27 GLU A CG 1 ATOM 209 C CD . GLU A 1 27 ? 16.996 30.479 42.707 1.00 35.03 ? 27 GLU A CD 1 ATOM 210 O OE1 . GLU A 1 27 ? 16.977 31.277 43.668 1.00 38.00 ? 27 GLU A OE1 1 ATOM 211 O OE2 . GLU A 1 27 ? 17.698 29.420 42.708 1.00 23.82 ? 27 GLU A OE2 1 ATOM 212 N N . ALA A 1 28 ? 16.867 28.821 37.419 1.00 16.05 ? 28 ALA A N 1 ATOM 213 C CA . ALA A 1 28 ? 17.636 28.423 36.233 1.00 15.11 ? 28 ALA A CA 1 ATOM 214 C C . ALA A 1 28 ? 16.860 28.820 34.969 1.00 17.42 ? 28 ALA A C 1 ATOM 215 O O . ALA A 1 28 ? 17.421 29.409 34.021 1.00 19.06 ? 28 ALA A O 1 ATOM 216 C CB . ALA A 1 28 ? 17.893 26.914 36.268 1.00 13.48 ? 28 ALA A CB 1 ATOM 217 N N . GLU A 1 29 ? 15.568 28.512 34.953 1.00 14.01 ? 29 GLU A N 1 ATOM 218 C CA . GLU A 1 29 ? 14.713 28.876 33.820 1.00 14.02 ? 29 GLU A CA 1 ATOM 219 C C . GLU A 1 29 ? 14.734 30.399 33.640 1.00 19.27 ? 29 GLU A C 1 ATOM 220 O O . GLU A 1 29 ? 14.886 30.905 32.525 1.00 18.84 ? 29 GLU A O 1 ATOM 221 C CB . GLU A 1 29 ? 13.273 28.406 34.078 1.00 15.43 ? 29 GLU A CB 1 ATOM 222 C CG . GLU A 1 29 ? 12.220 28.988 33.123 1.00 15.99 ? 29 GLU A CG 1 ATOM 223 C CD . GLU A 1 29 ? 12.385 28.547 31.672 1.00 22.28 ? 29 GLU A CD 1 ATOM 224 O OE1 . GLU A 1 29 ? 11.723 29.150 30.801 1.00 22.66 ? 29 GLU A OE1 1 ATOM 225 O OE2 . GLU A 1 29 ? 13.151 27.594 31.389 1.00 21.25 ? 29 GLU A OE2 1 ATOM 226 N N . ARG A 1 30 ? 14.588 31.135 34.740 1.00 17.62 ? 30 ARG A N 1 ATOM 227 C CA . ARG A 1 30 ? 14.583 32.596 34.651 1.00 17.47 ? 30 ARG A CA 1 ATOM 228 C C . ARG A 1 30 ? 15.919 33.086 34.091 1.00 19.62 ? 30 ARG A C 1 ATOM 229 O O . ARG A 1 30 ? 15.951 33.935 33.203 1.00 21.09 ? 30 ARG A O 1 ATOM 230 C CB . ARG A 1 30 ? 14.307 33.233 36.028 1.00 20.78 ? 30 ARG A CB 1 ATOM 231 C CG . ARG A 1 30 ? 14.421 34.761 36.020 1.00 23.05 ? 30 ARG A CG 1 ATOM 232 C CD . ARG A 1 30 ? 14.050 35.375 37.357 1.00 34.97 ? 30 ARG A CD 1 ATOM 233 N NE . ARG A 1 30 ? 12.622 35.231 37.623 1.00 50.52 ? 30 ARG A NE 1 ATOM 234 C CZ . ARG A 1 30 ? 11.667 35.971 37.063 1.00 57.69 ? 30 ARG A CZ 1 ATOM 235 N NH1 . ARG A 1 30 ? 11.977 36.932 36.197 1.00 59.04 ? 30 ARG A NH1 1 ATOM 236 N NH2 . ARG A 1 30 ? 10.393 35.740 37.361 1.00 59.52 ? 30 ARG A NH2 1 ATOM 237 N N . PHE A 1 31 ? 17.018 32.541 34.602 1.00 16.50 ? 31 PHE A N 1 ATOM 238 C CA . PHE A 1 31 ? 18.345 32.915 34.129 1.00 18.65 ? 31 PHE A CA 1 ATOM 239 C C . PHE A 1 31 ? 18.398 32.729 32.608 1.00 21.16 ? 31 PHE A C 1 ATOM 240 O O . PHE A 1 31 ? 18.823 33.624 31.876 1.00 20.59 ? 31 PHE A O 1 ATOM 241 C CB . PHE A 1 31 ? 19.405 32.027 34.796 1.00 19.85 ? 31 PHE A CB 1 ATOM 242 C CG . PHE A 1 31 ? 20.817 32.332 34.379 1.00 17.99 ? 31 PHE A CG 1 ATOM 243 C CD1 . PHE A 1 31 ? 21.630 33.137 35.167 1.00 26.98 ? 31 PHE A CD1 1 ATOM 244 C CD2 . PHE A 1 31 ? 21.349 31.778 33.217 1.00 25.38 ? 31 PHE A CD2 1 ATOM 245 C CE1 . PHE A 1 31 ? 22.964 33.383 34.808 1.00 30.49 ? 31 PHE A CE1 1 ATOM 246 C CE2 . PHE A 1 31 ? 22.679 32.018 32.847 1.00 25.36 ? 31 PHE A CE2 1 ATOM 247 C CZ . PHE A 1 31 ? 23.485 32.821 33.649 1.00 30.90 ? 31 PHE A CZ 1 ATOM 248 N N . CYS A 1 32 ? 17.972 31.563 32.129 1.00 15.77 ? 32 CYS A N 1 ATOM 249 C CA . CYS A 1 32 ? 17.992 31.322 30.686 1.00 18.68 ? 32 CYS A CA 1 ATOM 250 C C . CYS A 1 32 ? 17.141 32.347 29.947 1.00 19.69 ? 32 CYS A C 1 ATOM 251 O O . CYS A 1 32 ? 17.503 32.782 28.856 1.00 22.09 ? 32 CYS A O 1 ATOM 252 C CB . CYS A 1 32 ? 17.481 29.922 30.353 1.00 15.37 ? 32 CYS A CB 1 ATOM 253 S SG . CYS A 1 32 ? 18.523 28.568 30.989 1.00 16.00 ? 32 CYS A SG 1 ATOM 254 N N . THR A 1 33 ? 16.001 32.727 30.510 1.00 16.33 ? 33 THR A N 1 ATOM 255 C CA . THR A 1 33 ? 15.166 33.722 29.830 1.00 16.47 ? 33 THR A CA 1 ATOM 256 C C . THR A 1 33 ? 15.834 35.098 29.856 1.00 20.65 ? 33 THR A C 1 ATOM 257 O O . THR A 1 33 ? 15.603 35.934 28.967 1.00 21.89 ? 33 THR A O 1 ATOM 258 C CB . THR A 1 33 ? 13.774 33.897 30.477 1.00 18.15 ? 33 THR A CB 1 ATOM 259 O OG1 . THR A 1 33 ? 13.918 34.546 31.740 1.00 17.59 ? 33 THR A OG1 1 ATOM 260 C CG2 . THR A 1 33 ? 13.067 32.556 30.633 1.00 17.50 ? 33 THR A CG2 1 ATOM 261 N N . GLU A 1 34 ? 16.669 35.352 30.858 1.00 19.84 ? 34 GLU A N 1 ATOM 262 C CA . GLU A 1 34 ? 17.313 36.666 30.943 1.00 23.07 ? 34 GLU A CA 1 ATOM 263 C C . GLU A 1 34 ? 18.634 36.776 30.204 1.00 27.76 ? 34 GLU A C 1 ATOM 264 O O . GLU A 1 34 ? 18.978 37.846 29.699 1.00 25.70 ? 34 GLU A O 1 ATOM 265 C CB . GLU A 1 34 ? 17.552 37.059 32.404 1.00 20.99 ? 34 GLU A CB 1 ATOM 266 C CG . GLU A 1 34 ? 16.303 37.066 33.253 1.00 23.31 ? 34 GLU A CG 1 ATOM 267 C CD . GLU A 1 34 ? 16.605 37.313 34.718 1.00 34.38 ? 34 GLU A CD 1 ATOM 268 O OE1 . GLU A 1 34 ? 17.656 36.835 35.200 1.00 38.18 ? 34 GLU A OE1 1 ATOM 269 O OE2 . GLU A 1 34 ? 15.780 37.967 35.393 1.00 38.18 ? 34 GLU A OE2 1 ATOM 270 N N . GLN A 1 35 ? 19.375 35.677 30.130 1.00 23.24 ? 35 GLN A N 1 ATOM 271 C CA . GLN A 1 35 ? 20.689 35.715 29.500 1.00 25.05 ? 35 GLN A CA 1 ATOM 272 C C . GLN A 1 35 ? 20.739 35.413 28.011 1.00 22.97 ? 35 GLN A C 1 ATOM 273 O O . GLN A 1 35 ? 21.814 35.481 27.403 1.00 26.15 ? 35 GLN A O 1 ATOM 274 C CB . GLN A 1 35 ? 21.642 34.780 30.247 1.00 25.12 ? 35 GLN A CB 1 ATOM 275 C CG . GLN A 1 35 ? 21.788 35.113 31.723 1.00 30.20 ? 35 GLN A CG 1 ATOM 276 C CD . GLN A 1 35 ? 22.509 36.432 31.956 1.00 37.88 ? 35 GLN A CD 1 ATOM 277 O OE1 . GLN A 1 35 ? 23.487 36.737 31.276 1.00 32.35 ? 35 GLN A OE1 1 ATOM 278 N NE2 . GLN A 1 35 ? 22.040 37.211 32.935 1.00 27.23 ? 35 GLN A NE2 1 ATOM 279 N N . ALA A 1 36 ? 19.594 35.087 27.415 1.00 23.09 ? 36 ALA A N 1 ATOM 280 C CA . ALA A 1 36 ? 19.566 34.808 25.986 1.00 24.98 ? 36 ALA A CA 1 ATOM 281 C C . ALA A 1 36 ? 18.239 35.242 25.395 1.00 20.28 ? 36 ALA A C 1 ATOM 282 O O . ALA A 1 36 ? 17.200 35.113 26.035 1.00 25.49 ? 36 ALA A O 1 ATOM 283 C CB . ALA A 1 36 ? 19.795 33.303 25.723 1.00 23.02 ? 36 ALA A CB 1 ATOM 284 N N . LYS A 1 37 ? 18.263 35.753 24.167 1.00 24.25 ? 37 LYS A N 1 ATOM 285 C CA . LYS A 1 37 ? 17.008 36.180 23.534 1.00 24.65 ? 37 LYS A CA 1 ATOM 286 C C . LYS A 1 37 ? 16.086 34.978 23.363 1.00 21.96 ? 37 LYS A C 1 ATOM 287 O O . LYS A 1 37 ? 16.425 34.042 22.651 1.00 24.69 ? 37 LYS A O 1 ATOM 288 C CB . LYS A 1 37 ? 17.267 36.819 22.159 1.00 25.88 ? 37 LYS A CB 1 ATOM 289 C CG . LYS A 1 37 ? 16.002 37.432 21.541 1.00 27.24 ? 37 LYS A CG 1 ATOM 290 C CD . LYS A 1 37 ? 16.237 38.089 20.183 1.00 39.90 ? 37 LYS A CD 1 ATOM 291 C CE . LYS A 1 37 ? 16.491 37.054 19.090 1.00 45.75 ? 37 LYS A CE 1 ATOM 292 N NZ . LYS A 1 37 ? 16.442 37.660 17.729 1.00 51.84 ? 37 LYS A NZ 1 ATOM 293 N N . ASP A 1 38 ? 14.924 35.004 24.017 1.00 27.12 ? 38 ASP A N 1 ATOM 294 C CA . ASP A 1 38 ? 13.957 33.892 23.934 1.00 29.64 ? 38 ASP A CA 1 ATOM 295 C C . ASP A 1 38 ? 14.552 32.588 24.484 1.00 27.85 ? 38 ASP A C 1 ATOM 296 O O . ASP A 1 38 ? 14.194 31.484 24.038 1.00 24.56 ? 38 ASP A O 1 ATOM 297 C CB . ASP A 1 38 ? 13.512 33.679 22.481 1.00 29.60 ? 38 ASP A CB 1 ATOM 298 C CG . ASP A 1 38 ? 12.830 34.902 21.899 1.00 39.00 ? 38 ASP A CG 1 ATOM 299 O OD1 . ASP A 1 38 ? 13.038 35.190 20.700 1.00 46.08 ? 38 ASP A OD1 1 ATOM 300 O OD2 . ASP A 1 38 ? 12.078 35.572 22.640 1.00 38.89 ? 38 ASP A OD2 1 ATOM 301 N N . GLY A 1 39 ? 15.464 32.725 25.447 1.00 26.14 ? 39 GLY A N 1 ATOM 302 C CA . GLY A 1 39 ? 16.101 31.565 26.049 1.00 20.53 ? 39 GLY A CA 1 ATOM 303 C C . GLY A 1 39 ? 15.225 30.845 27.064 1.00 20.42 ? 39 GLY A C 1 ATOM 304 O O . GLY A 1 39 ? 14.302 31.431 27.625 1.00 15.95 ? 39 GLY A O 1 ATOM 305 N N . HIS A 1 40 ? 15.525 29.567 27.283 1.00 20.93 ? 40 HIS A N 1 ATOM 306 C CA . HIS A 1 40 ? 14.816 28.717 28.236 1.00 15.50 ? 40 HIS A CA 1 ATOM 307 C C . HIS A 1 40 ? 15.759 27.592 28.621 1.00 17.63 ? 40 HIS A C 1 ATOM 308 O O . HIS A 1 40 ? 16.767 27.365 27.958 1.00 21.40 ? 40 HIS A O 1 ATOM 309 C CB . HIS A 1 40 ? 13.602 28.049 27.578 1.00 18.25 ? 40 HIS A CB 1 ATOM 310 C CG . HIS A 1 40 ? 12.504 28.999 27.212 1.00 18.23 ? 40 HIS A CG 1 ATOM 311 N ND1 . HIS A 1 40 ? 11.677 29.575 28.153 1.00 21.16 ? 40 HIS A ND1 1 ATOM 312 C CD2 . HIS A 1 40 ? 12.111 29.493 26.012 1.00 24.23 ? 40 HIS A CD2 1 ATOM 313 C CE1 . HIS A 1 40 ? 10.820 30.382 27.550 1.00 26.09 ? 40 HIS A CE1 1 ATOM 314 N NE2 . HIS A 1 40 ? 11.062 30.350 26.251 1.00 24.28 ? 40 HIS A NE2 1 ATOM 315 N N . LEU A 1 41 ? 15.432 26.891 29.701 1.00 14.15 ? 41 LEU A N 1 ATOM 316 C CA . LEU A 1 41 ? 16.205 25.717 30.070 1.00 15.13 ? 41 LEU A CA 1 ATOM 317 C C . LEU A 1 41 ? 16.049 24.831 28.839 1.00 20.07 ? 41 LEU A C 1 ATOM 318 O O . LEU A 1 41 ? 15.028 24.884 28.146 1.00 19.89 ? 41 LEU A O 1 ATOM 319 C CB . LEU A 1 41 ? 15.578 25.009 31.274 1.00 13.18 ? 41 LEU A CB 1 ATOM 320 C CG . LEU A 1 41 ? 16.014 25.509 32.645 1.00 12.36 ? 41 LEU A CG 1 ATOM 321 C CD1 . LEU A 1 41 ? 15.065 24.937 33.713 1.00 13.72 ? 41 LEU A CD1 1 ATOM 322 C CD2 . LEU A 1 41 ? 17.461 25.090 32.926 1.00 15.63 ? 41 LEU A CD2 1 ATOM 323 N N . VAL A 1 42 ? 17.042 23.995 28.586 1.00 18.38 ? 42 VAL A N 1 ATOM 324 C CA . VAL A 1 42 ? 17.033 23.138 27.407 1.00 18.59 ? 42 VAL A CA 1 ATOM 325 C C . VAL A 1 42 ? 15.859 22.167 27.294 1.00 23.57 ? 42 VAL A C 1 ATOM 326 O O . VAL A 1 42 ? 15.383 21.641 28.294 1.00 22.18 ? 42 VAL A O 1 ATOM 327 C CB . VAL A 1 42 ? 18.354 22.339 27.334 1.00 16.86 ? 42 VAL A CB 1 ATOM 328 C CG1 . VAL A 1 42 ? 18.458 21.390 28.535 1.00 14.87 ? 42 VAL A CG1 1 ATOM 329 C CG2 . VAL A 1 42 ? 18.440 21.564 26.011 1.00 20.11 ? 42 VAL A CG2 1 ATOM 330 N N . SER A 1 43 ? 15.353 21.991 26.072 1.00 18.98 ? 43 SER A N 1 ATOM 331 C CA . SER A 1 43 ? 14.307 21.007 25.824 1.00 20.19 ? 43 SER A CA 1 ATOM 332 C C . SER A 1 43 ? 15.067 19.976 24.977 1.00 23.81 ? 43 SER A C 1 ATOM 333 O O . SER A 1 43 ? 15.870 20.338 24.112 1.00 19.97 ? 43 SER A O 1 ATOM 334 C CB . SER A 1 43 ? 13.110 21.611 25.071 1.00 23.39 ? 43 SER A CB 1 ATOM 335 O OG . SER A 1 43 ? 13.479 22.174 23.830 1.00 23.60 ? 43 SER A OG 1 ATOM 336 N N . ILE A 1 44 ? 14.850 18.694 25.253 1.00 22.65 ? 44 ILE A N 1 ATOM 337 C CA . ILE A 1 44 ? 15.554 17.635 24.554 1.00 17.12 ? 44 ILE A CA 1 ATOM 338 C C . ILE A 1 44 ? 14.482 16.810 23.861 1.00 28.25 ? 44 ILE A C 1 ATOM 339 O O . ILE A 1 44 ? 13.686 16.114 24.500 1.00 21.74 ? 44 ILE A O 1 ATOM 340 C CB . ILE A 1 44 ? 16.374 16.814 25.563 1.00 18.12 ? 44 ILE A CB 1 ATOM 341 C CG1 . ILE A 1 44 ? 17.386 17.747 26.241 1.00 21.58 ? 44 ILE A CG1 1 ATOM 342 C CG2 . ILE A 1 44 ? 17.093 15.663 24.881 1.00 12.82 ? 44 ILE A CG2 1 ATOM 343 C CD1 . ILE A 1 44 ? 18.313 17.067 27.248 1.00 20.69 ? 44 ILE A CD1 1 ATOM 344 N N . GLN A 1 45 ? 14.464 16.905 22.538 1.00 26.60 ? 45 GLN A N 1 ATOM 345 C CA . GLN A 1 45 ? 13.424 16.261 21.758 1.00 30.78 ? 45 GLN A CA 1 ATOM 346 C C . GLN A 1 45 ? 13.808 15.027 20.958 1.00 34.52 ? 45 GLN A C 1 ATOM 347 O O . GLN A 1 45 ? 12.995 14.501 20.193 1.00 35.31 ? 45 GLN A O 1 ATOM 348 C CB . GLN A 1 45 ? 12.781 17.335 20.863 1.00 28.20 ? 45 GLN A CB 1 ATOM 349 C CG . GLN A 1 45 ? 12.164 18.464 21.699 1.00 33.94 ? 45 GLN A CG 1 ATOM 350 C CD . GLN A 1 45 ? 11.866 19.731 20.915 1.00 37.90 ? 45 GLN A CD 1 ATOM 351 O OE1 . GLN A 1 45 ? 11.200 19.694 19.878 1.00 39.99 ? 45 GLN A OE1 1 ATOM 352 N NE2 . GLN A 1 45 ? 12.343 20.867 21.421 1.00 23.53 ? 45 GLN A NE2 1 ATOM 353 N N . SER A 1 46 ? 15.030 14.548 21.149 1.00 27.38 ? 46 SER A N 1 ATOM 354 C CA . SER A 1 46 ? 15.466 13.357 20.444 1.00 29.67 ? 46 SER A CA 1 ATOM 355 C C . SER A 1 46 ? 16.710 12.795 21.091 1.00 29.37 ? 46 SER A C 1 ATOM 356 O O . SER A 1 46 ? 17.421 13.494 21.824 1.00 28.62 ? 46 SER A O 1 ATOM 357 C CB . SER A 1 46 ? 15.761 13.676 18.978 1.00 32.54 ? 46 SER A CB 1 ATOM 358 O OG . SER A 1 46 ? 16.978 14.396 18.866 1.00 30.78 ? 46 SER A OG 1 ATOM 359 N N . ARG A 1 47 ? 16.968 11.522 20.819 1.00 30.18 ? 47 ARG A N 1 ATOM 360 C CA . ARG A 1 47 ? 18.134 10.841 21.347 1.00 31.55 ? 47 ARG A CA 1 ATOM 361 C C . ARG A 1 47 ? 19.420 11.541 20.899 1.00 29.76 ? 47 ARG A C 1 ATOM 362 O O . ARG A 1 47 ? 20.387 11.641 21.662 1.00 23.98 ? 47 ARG A O 1 ATOM 363 C CB . ARG A 1 47 ? 18.138 9.387 20.869 1.00 39.77 ? 47 ARG A CB 1 ATOM 364 C CG . ARG A 1 47 ? 19.182 8.516 21.540 1.00 49.92 ? 47 ARG A CG 1 ATOM 365 C CD . ARG A 1 47 ? 19.083 7.078 21.049 1.00 55.40 ? 47 ARG A CD 1 ATOM 366 N NE . ARG A 1 47 ? 17.719 6.559 21.144 1.00 56.81 ? 47 ARG A NE 1 ATOM 367 C CZ . ARG A 1 47 ? 17.008 6.498 22.269 1.00 62.66 ? 47 ARG A CZ 1 ATOM 368 N NH1 . ARG A 1 47 ? 15.773 6.007 22.249 1.00 58.51 ? 47 ARG A NH1 1 ATOM 369 N NH2 . ARG A 1 47 ? 17.527 6.925 23.416 1.00 61.28 ? 47 ARG A NH2 1 ATOM 370 N N . GLU A 1 48 ? 19.430 12.024 19.660 1.00 28.78 ? 48 GLU A N 1 ATOM 371 C CA . GLU A 1 48 ? 20.606 12.708 19.116 1.00 29.14 ? 48 GLU A CA 1 ATOM 372 C C . GLU A 1 48 ? 20.888 13.997 19.880 1.00 25.54 ? 48 GLU A C 1 ATOM 373 O O . GLU A 1 48 ? 22.031 14.272 20.250 1.00 24.56 ? 48 GLU A O 1 ATOM 374 C CB . GLU A 1 48 ? 20.404 13.035 17.628 1.00 34.19 ? 48 GLU A CB 1 ATOM 375 C CG . GLU A 1 48 ? 20.371 11.819 16.698 1.00 42.85 ? 48 GLU A CG 1 ATOM 376 C CD . GLU A 1 48 ? 19.226 10.867 16.999 1.00 47.36 ? 48 GLU A CD 1 ATOM 377 O OE1 . GLU A 1 48 ? 18.089 11.343 17.221 1.00 46.94 ? 48 GLU A OE1 1 ATOM 378 O OE2 . GLU A 1 48 ? 19.460 9.638 17.002 1.00 58.94 ? 48 GLU A OE2 1 ATOM 379 N N . GLU A 1 49 ? 19.847 14.788 20.106 1.00 24.15 ? 49 GLU A N 1 ATOM 380 C CA . GLU A 1 49 ? 20.016 16.036 20.845 1.00 24.35 ? 49 GLU A CA 1 ATOM 381 C C . GLU A 1 49 ? 20.500 15.693 22.252 1.00 20.83 ? 49 GLU A C 1 ATOM 382 O O . GLU A 1 49 ? 21.303 16.422 22.840 1.00 22.89 ? 49 GLU A O 1 ATOM 383 C CB . GLU A 1 49 ? 18.695 16.805 20.920 1.00 21.64 ? 49 GLU A CB 1 ATOM 384 C CG . GLU A 1 49 ? 18.839 18.210 21.527 1.00 19.97 ? 49 GLU A CG 1 ATOM 385 C CD . GLU A 1 49 ? 17.572 19.041 21.411 1.00 26.26 ? 49 GLU A CD 1 ATOM 386 O OE1 . GLU A 1 49 ? 17.644 20.277 21.628 1.00 20.60 ? 49 GLU A OE1 1 ATOM 387 O OE2 . GLU A 1 49 ? 16.502 18.461 21.109 1.00 22.60 ? 49 GLU A OE2 1 ATOM 388 N N . GLY A 1 50 ? 20.000 14.581 22.798 1.00 20.52 ? 50 GLY A N 1 ATOM 389 C CA . GLY A 1 50 ? 20.424 14.168 24.129 1.00 19.83 ? 50 GLY A CA 1 ATOM 390 C C . GLY A 1 50 ? 21.910 13.836 24.207 1.00 19.99 ? 50 GLY A C 1 ATOM 391 O O . GLY A 1 50 ? 22.580 14.144 25.197 1.00 16.87 ? 50 GLY A O 1 ATOM 392 N N . ASN A 1 51 ? 22.437 13.197 23.166 1.00 22.57 ? 51 ASN A N 1 ATOM 393 C CA . ASN A 1 51 ? 23.854 12.863 23.146 1.00 21.62 ? 51 ASN A CA 1 ATOM 394 C C . ASN A 1 51 ? 24.680 14.138 23.041 1.00 19.58 ? 51 ASN A C 1 ATOM 395 O O . ASN A 1 51 ? 25.752 14.260 23.646 1.00 20.31 ? 51 ASN A O 1 ATOM 396 C CB . ASN A 1 51 ? 24.170 11.930 21.973 1.00 28.06 ? 51 ASN A CB 1 ATOM 397 C CG . ASN A 1 51 ? 23.605 10.547 22.177 1.00 34.99 ? 51 ASN A CG 1 ATOM 398 O OD1 . ASN A 1 51 ? 23.525 10.065 23.311 1.00 31.12 ? 51 ASN A OD1 1 ATOM 399 N ND2 . ASN A 1 51 ? 23.221 9.889 21.085 1.00 31.08 ? 51 ASN A ND2 1 ATOM 400 N N . PHE A 1 52 ? 24.178 15.086 22.263 1.00 21.42 ? 52 PHE A N 1 ATOM 401 C CA . PHE A 1 52 ? 24.872 16.360 22.114 1.00 21.33 ? 52 PHE A CA 1 ATOM 402 C C . PHE A 1 52 ? 24.904 17.065 23.474 1.00 19.04 ? 52 PHE A C 1 ATOM 403 O O . PHE A 1 52 ? 25.950 17.537 23.916 1.00 20.67 ? 52 PHE A O 1 ATOM 404 C CB . PHE A 1 52 ? 24.144 17.254 21.112 1.00 22.61 ? 52 PHE A CB 1 ATOM 405 C CG . PHE A 1 52 ? 24.549 18.699 21.199 1.00 21.60 ? 52 PHE A CG 1 ATOM 406 C CD1 . PHE A 1 52 ? 25.778 19.120 20.708 1.00 24.13 ? 52 PHE A CD1 1 ATOM 407 C CD2 . PHE A 1 52 ? 23.729 19.623 21.852 1.00 21.48 ? 52 PHE A CD2 1 ATOM 408 C CE1 . PHE A 1 52 ? 26.198 20.441 20.864 1.00 27.40 ? 52 PHE A CE1 1 ATOM 409 C CE2 . PHE A 1 52 ? 24.139 20.942 22.013 1.00 21.01 ? 52 PHE A CE2 1 ATOM 410 C CZ . PHE A 1 52 ? 25.378 21.349 21.518 1.00 21.00 ? 52 PHE A CZ 1 ATOM 411 N N . VAL A 1 53 ? 23.752 17.134 24.142 1.00 16.91 ? 53 VAL A N 1 ATOM 412 C CA . VAL A 1 53 ? 23.704 17.817 25.442 1.00 17.02 ? 53 VAL A CA 1 ATOM 413 C C . VAL A 1 53 ? 24.579 17.105 26.471 1.00 17.46 ? 53 VAL A C 1 ATOM 414 O O . VAL A 1 53 ? 25.261 17.747 27.278 1.00 17.94 ? 53 VAL A O 1 ATOM 415 C CB . VAL A 1 53 ? 22.247 17.930 25.946 1.00 16.00 ? 53 VAL A CB 1 ATOM 416 C CG1 . VAL A 1 53 ? 22.208 18.586 27.334 1.00 15.69 ? 53 VAL A CG1 1 ATOM 417 C CG2 . VAL A 1 53 ? 21.435 18.772 24.963 1.00 15.48 ? 53 VAL A CG2 1 ATOM 418 N N . ALA A 1 54 ? 24.583 15.772 26.441 1.00 18.46 ? 54 ALA A N 1 ATOM 419 C CA . ALA A 1 54 ? 25.411 15.021 27.373 1.00 17.18 ? 54 ALA A CA 1 ATOM 420 C C . ALA A 1 54 ? 26.891 15.374 27.148 1.00 20.69 ? 54 ALA A C 1 ATOM 421 O O . ALA A 1 54 ? 27.660 15.516 28.099 1.00 19.80 ? 54 ALA A O 1 ATOM 422 C CB . ALA A 1 54 ? 25.190 13.519 27.177 1.00 20.87 ? 54 ALA A CB 1 ATOM 423 N N . GLN A 1 55 ? 27.299 15.491 25.889 1.00 21.69 ? 55 GLN A N 1 ATOM 424 C CA . GLN A 1 55 ? 28.691 15.850 25.593 1.00 25.19 ? 55 GLN A CA 1 ATOM 425 C C . GLN A 1 55 ? 28.939 17.296 26.045 1.00 21.42 ? 55 GLN A C 1 ATOM 426 O O . GLN A 1 55 ? 30.005 17.632 26.563 1.00 21.02 ? 55 GLN A O 1 ATOM 427 C CB . GLN A 1 55 ? 28.960 15.708 24.091 1.00 31.56 ? 55 GLN A CB 1 ATOM 428 C CG . GLN A 1 55 ? 30.408 15.935 23.692 1.00 48.28 ? 55 GLN A CG 1 ATOM 429 C CD . GLN A 1 55 ? 31.363 14.985 24.403 1.00 53.87 ? 55 GLN A CD 1 ATOM 430 O OE1 . GLN A 1 55 ? 31.203 13.763 24.344 1.00 53.65 ? 55 GLN A OE1 1 ATOM 431 N NE2 . GLN A 1 55 ? 32.364 15.545 25.077 1.00 52.38 ? 55 GLN A NE2 1 ATOM 432 N N . LEU A 1 56 ? 27.941 18.153 25.867 1.00 26.22 ? 56 LEU A N 1 ATOM 433 C CA . LEU A 1 56 ? 28.090 19.555 26.267 1.00 20.23 ? 56 LEU A CA 1 ATOM 434 C C . LEU A 1 56 ? 28.352 19.692 27.766 1.00 21.98 ? 56 LEU A C 1 ATOM 435 O O . LEU A 1 56 ? 29.078 20.596 28.205 1.00 22.15 ? 56 LEU A O 1 ATOM 436 C CB . LEU A 1 56 ? 26.832 20.341 25.904 1.00 21.82 ? 56 LEU A CB 1 ATOM 437 C CG . LEU A 1 56 ? 26.925 21.850 26.183 1.00 26.34 ? 56 LEU A CG 1 ATOM 438 C CD1 . LEU A 1 56 ? 27.802 22.511 25.111 1.00 23.26 ? 56 LEU A CD1 1 ATOM 439 C CD2 . LEU A 1 56 ? 25.524 22.465 26.188 1.00 22.55 ? 56 LEU A CD2 1 ATOM 440 N N . VAL A 1 57 ? 27.758 18.808 28.566 1.00 19.33 ? 57 VAL A N 1 ATOM 441 C CA . VAL A 1 57 ? 27.943 18.894 30.012 1.00 20.39 ? 57 VAL A CA 1 ATOM 442 C C . VAL A 1 57 ? 28.923 17.862 30.558 1.00 23.93 ? 57 VAL A C 1 ATOM 443 O O . VAL A 1 57 ? 28.991 17.652 31.765 1.00 22.51 ? 57 VAL A O 1 ATOM 444 C CB . VAL A 1 57 ? 26.589 18.759 30.777 1.00 21.15 ? 57 VAL A CB 1 ATOM 445 C CG1 . VAL A 1 57 ? 25.615 19.834 30.290 1.00 20.93 ? 57 VAL A CG1 1 ATOM 446 C CG2 . VAL A 1 57 ? 25.986 17.373 30.563 1.00 18.52 ? 57 VAL A CG2 1 ATOM 447 N N . SER A 1 58 ? 29.689 17.230 29.670 1.00 20.52 ? 58 SER A N 1 ATOM 448 C CA . SER A 1 58 ? 30.656 16.218 30.100 1.00 24.84 ? 58 SER A CA 1 ATOM 449 C C . SER A 1 58 ? 31.622 16.747 31.158 1.00 23.41 ? 58 SER A C 1 ATOM 450 O O . SER A 1 58 ? 32.154 15.987 31.955 1.00 23.82 ? 58 SER A O 1 ATOM 451 C CB . SER A 1 58 ? 31.448 15.686 28.900 1.00 29.11 ? 58 SER A CB 1 ATOM 452 O OG . SER A 1 58 ? 32.162 16.724 28.252 1.00 32.49 ? 58 SER A OG 1 ATOM 453 N N . GLY A 1 59 ? 31.837 18.058 31.183 1.00 25.43 ? 59 GLY A N 1 ATOM 454 C CA . GLY A 1 59 ? 32.731 18.612 32.179 1.00 26.05 ? 59 GLY A CA 1 ATOM 455 C C . GLY A 1 59 ? 32.193 18.525 33.596 1.00 30.73 ? 59 GLY A C 1 ATOM 456 O O . GLY A 1 59 ? 32.966 18.531 34.560 1.00 35.68 ? 59 GLY A O 1 ATOM 457 N N . PHE A 1 60 ? 30.872 18.440 33.735 1.00 23.25 ? 60 PHE A N 1 ATOM 458 C CA . PHE A 1 60 ? 30.268 18.360 35.061 1.00 27.21 ? 60 PHE A CA 1 ATOM 459 C C . PHE A 1 60 ? 30.398 16.951 35.659 1.00 30.29 ? 60 PHE A C 1 ATOM 460 O O . PHE A 1 60 ? 30.014 16.733 36.800 1.00 32.18 ? 60 PHE A O 1 ATOM 461 C CB . PHE A 1 60 ? 28.787 18.762 35.012 1.00 22.39 ? 60 PHE A CB 1 ATOM 462 C CG . PHE A 1 60 ? 28.542 20.189 34.583 1.00 27.68 ? 60 PHE A CG 1 ATOM 463 C CD1 . PHE A 1 60 ? 27.312 20.554 34.035 1.00 25.68 ? 60 PHE A CD1 1 ATOM 464 C CD2 . PHE A 1 60 ? 29.515 21.171 34.752 1.00 33.44 ? 60 PHE A CD2 1 ATOM 465 C CE1 . PHE A 1 60 ? 27.049 21.872 33.665 1.00 27.88 ? 60 PHE A CE1 1 ATOM 466 C CE2 . PHE A 1 60 ? 29.262 22.500 34.383 1.00 32.49 ? 60 PHE A CE2 1 ATOM 467 C CZ . PHE A 1 60 ? 28.025 22.850 33.839 1.00 28.54 ? 60 PHE A CZ 1 ATOM 468 N N . MET A 1 61 ? 30.930 15.993 34.899 1.00 32.21 ? 61 MET A N 1 ATOM 469 C CA . MET A 1 61 ? 31.091 14.641 35.443 1.00 36.80 ? 61 MET A CA 1 ATOM 470 C C . MET A 1 61 ? 32.080 14.613 36.609 1.00 44.87 ? 61 MET A C 1 ATOM 471 O O . MET A 1 61 ? 32.036 13.716 37.450 1.00 46.36 ? 61 MET A O 1 ATOM 472 C CB . MET A 1 61 ? 31.572 13.658 34.373 1.00 34.33 ? 61 MET A CB 1 ATOM 473 C CG . MET A 1 61 ? 30.490 13.160 33.425 1.00 38.36 ? 61 MET A CG 1 ATOM 474 S SD . MET A 1 61 ? 29.028 12.498 34.273 1.00 39.42 ? 61 MET A SD 1 ATOM 475 C CE . MET A 1 61 ? 29.625 10.880 34.873 1.00 27.99 ? 61 MET A CE 1 ATOM 476 N N . HIS A 1 62 ? 32.970 15.596 36.661 1.00 48.14 ? 62 HIS A N 1 ATOM 477 C CA . HIS A 1 62 ? 33.965 15.644 37.722 1.00 56.32 ? 62 HIS A CA 1 ATOM 478 C C . HIS A 1 62 ? 33.444 16.321 38.986 1.00 59.60 ? 62 HIS A C 1 ATOM 479 O O . HIS A 1 62 ? 33.986 16.119 40.073 1.00 62.92 ? 62 HIS A O 1 ATOM 480 C CB . HIS A 1 62 ? 35.218 16.368 37.229 1.00 60.68 ? 62 HIS A CB 1 ATOM 481 C CG . HIS A 1 62 ? 35.777 15.811 35.955 1.00 66.59 ? 62 HIS A CG 1 ATOM 482 N ND1 . HIS A 1 62 ? 35.063 15.791 34.776 1.00 69.77 ? 62 HIS A ND1 1 ATOM 483 C CD2 . HIS A 1 62 ? 36.985 15.270 35.673 1.00 68.14 ? 62 HIS A CD2 1 ATOM 484 C CE1 . HIS A 1 62 ? 35.808 15.262 33.821 1.00 69.83 ? 62 HIS A CE1 1 ATOM 485 N NE2 . HIS A 1 62 ? 36.979 14.939 34.339 1.00 70.00 ? 62 HIS A NE2 1 ATOM 486 N N . ARG A 1 63 ? 32.391 17.120 38.850 1.00 57.17 ? 63 ARG A N 1 ATOM 487 C CA . ARG A 1 63 ? 31.835 17.809 40.007 1.00 56.56 ? 63 ARG A CA 1 ATOM 488 C C . ARG A 1 63 ? 30.968 16.891 40.850 1.00 54.12 ? 63 ARG A C 1 ATOM 489 O O . ARG A 1 63 ? 30.595 15.801 40.425 1.00 55.29 ? 63 ARG A O 1 ATOM 490 C CB . ARG A 1 63 ? 31.011 19.014 39.570 1.00 58.85 ? 63 ARG A CB 1 ATOM 491 C CG . ARG A 1 63 ? 31.782 20.020 38.751 1.00 59.52 ? 63 ARG A CG 1 ATOM 492 C CD . ARG A 1 63 ? 30.968 21.282 38.606 1.00 61.93 ? 63 ARG A CD 1 ATOM 493 N NE . ARG A 1 63 ? 31.583 22.228 37.683 1.00 64.17 ? 63 ARG A NE 1 ATOM 494 C CZ . ARG A 1 63 ? 31.133 23.461 37.486 1.00 62.29 ? 63 ARG A CZ 1 ATOM 495 N NH1 . ARG A 1 63 ? 31.744 24.262 36.624 1.00 60.29 ? 63 ARG A NH1 1 ATOM 496 N NH2 . ARG A 1 63 ? 30.074 23.892 38.161 1.00 64.44 ? 63 ARG A NH2 1 ATOM 497 N N . SER A 1 64 ? 30.636 17.354 42.047 1.00 54.09 ? 64 SER A N 1 ATOM 498 C CA . SER A 1 64 ? 29.819 16.584 42.971 1.00 55.11 ? 64 SER A CA 1 ATOM 499 C C . SER A 1 64 ? 28.324 16.512 42.631 1.00 51.55 ? 64 SER A C 1 ATOM 500 O O . SER A 1 64 ? 27.659 15.556 43.019 1.00 51.19 ? 64 SER A O 1 ATOM 501 C CB . SER A 1 64 ? 30.000 17.133 44.387 1.00 57.38 ? 64 SER A CB 1 ATOM 502 O OG . SER A 1 64 ? 29.808 18.535 44.409 1.00 62.64 ? 64 SER A OG 1 ATOM 503 N N . GLU A 1 65 ? 27.793 17.507 41.917 1.00 44.21 ? 65 GLU A N 1 ATOM 504 C CA . GLU A 1 65 ? 26.368 17.497 41.561 1.00 40.54 ? 65 GLU A CA 1 ATOM 505 C C . GLU A 1 65 ? 25.970 16.274 40.732 1.00 35.84 ? 65 GLU A C 1 ATOM 506 O O . GLU A 1 65 ? 26.591 15.967 39.707 1.00 28.52 ? 65 GLU A O 1 ATOM 507 C CB . GLU A 1 65 ? 25.978 18.761 40.790 1.00 42.28 ? 65 GLU A CB 1 ATOM 508 C CG . GLU A 1 65 ? 25.725 19.996 41.659 1.00 51.95 ? 65 GLU A CG 1 ATOM 509 C CD . GLU A 1 65 ? 26.994 20.746 42.008 1.00 55.30 ? 65 GLU A CD 1 ATOM 510 O OE1 . GLU A 1 65 ? 26.893 21.870 42.551 1.00 48.77 ? 65 GLU A OE1 1 ATOM 511 O OE2 . GLU A 1 65 ? 28.093 20.215 41.740 1.00 58.87 ? 65 GLU A OE2 1 ATOM 512 N N . ILE A 1 66 ? 24.912 15.592 41.154 1.00 22.64 ? 66 ILE A N 1 ATOM 513 C CA . ILE A 1 66 ? 24.489 14.409 40.433 1.00 24.73 ? 66 ILE A CA 1 ATOM 514 C C . ILE A 1 66 ? 23.424 14.646 39.375 1.00 20.47 ? 66 ILE A C 1 ATOM 515 O O . ILE A 1 66 ? 23.068 13.718 38.651 1.00 18.98 ? 66 ILE A O 1 ATOM 516 C CB . ILE A 1 66 ? 24.023 13.299 41.399 1.00 32.21 ? 66 ILE A CB 1 ATOM 517 C CG1 . ILE A 1 66 ? 22.670 13.650 42.007 1.00 35.65 ? 66 ILE A CG1 1 ATOM 518 C CG2 . ILE A 1 66 ? 25.062 13.122 42.504 1.00 37.88 ? 66 ILE A CG2 1 ATOM 519 C CD1 . ILE A 1 66 ? 22.131 12.568 42.924 1.00 45.72 ? 66 ILE A CD1 1 ATOM 520 N N . TYR A 1 67 ? 22.924 15.882 39.283 1.00 17.16 ? 67 TYR A N 1 ATOM 521 C CA . TYR A 1 67 ? 21.925 16.248 38.279 1.00 15.71 ? 67 TYR A CA 1 ATOM 522 C C . TYR A 1 67 ? 22.259 17.591 37.631 1.00 16.33 ? 67 TYR A C 1 ATOM 523 O O . TYR A 1 67 ? 23.000 18.411 38.189 1.00 16.59 ? 67 TYR A O 1 ATOM 524 C CB . TYR A 1 67 ? 20.530 16.386 38.901 1.00 16.19 ? 67 TYR A CB 1 ATOM 525 C CG . TYR A 1 67 ? 20.037 15.144 39.587 1.00 13.33 ? 67 TYR A CG 1 ATOM 526 C CD1 . TYR A 1 67 ? 19.735 14.001 38.852 1.00 13.97 ? 67 TYR A CD1 1 ATOM 527 C CD2 . TYR A 1 67 ? 19.871 15.110 40.977 1.00 20.23 ? 67 TYR A CD2 1 ATOM 528 C CE1 . TYR A 1 67 ? 19.277 12.843 39.477 1.00 20.85 ? 67 TYR A CE1 1 ATOM 529 C CE2 . TYR A 1 67 ? 19.411 13.953 41.618 1.00 23.68 ? 67 TYR A CE2 1 ATOM 530 C CZ . TYR A 1 67 ? 19.119 12.829 40.858 1.00 20.77 ? 67 TYR A CZ 1 ATOM 531 O OH . TYR A 1 67 ? 18.675 11.683 41.462 1.00 24.54 ? 67 TYR A OH 1 ATOM 532 N N . VAL A 1 68 ? 21.679 17.781 36.454 1.00 15.23 ? 68 VAL A N 1 ATOM 533 C CA . VAL A 1 68 ? 21.793 18.996 35.654 1.00 16.54 ? 68 VAL A CA 1 ATOM 534 C C . VAL A 1 68 ? 20.359 19.317 35.193 1.00 17.35 ? 68 VAL A C 1 ATOM 535 O O . VAL A 1 68 ? 19.733 18.505 34.514 1.00 16.67 ? 68 VAL A O 1 ATOM 536 C CB . VAL A 1 68 ? 22.663 18.754 34.394 1.00 14.02 ? 68 VAL A CB 1 ATOM 537 C CG1 . VAL A 1 68 ? 22.622 20.004 33.495 1.00 15.12 ? 68 VAL A CG1 1 ATOM 538 C CG2 . VAL A 1 68 ? 24.094 18.441 34.801 1.00 15.53 ? 68 VAL A CG2 1 ATOM 539 N N . TRP A 1 69 ? 19.833 20.491 35.537 1.00 16.41 ? 69 TRP A N 1 ATOM 540 C CA . TRP A 1 69 ? 18.462 20.835 35.139 1.00 16.09 ? 69 TRP A CA 1 ATOM 541 C C . TRP A 1 69 ? 18.188 20.903 33.639 1.00 18.02 ? 69 TRP A C 1 ATOM 542 O O . TRP A 1 69 ? 19.030 21.386 32.872 1.00 16.34 ? 69 TRP A O 1 ATOM 543 C CB . TRP A 1 69 ? 18.067 22.217 35.680 1.00 12.35 ? 69 TRP A CB 1 ATOM 544 C CG . TRP A 1 69 ? 17.857 22.325 37.155 1.00 14.12 ? 69 TRP A CG 1 ATOM 545 C CD1 . TRP A 1 69 ? 18.444 23.235 38.006 1.00 13.80 ? 69 TRP A CD1 1 ATOM 546 C CD2 . TRP A 1 69 ? 16.952 21.557 37.952 1.00 13.64 ? 69 TRP A CD2 1 ATOM 547 N NE1 . TRP A 1 69 ? 17.953 23.073 39.282 1.00 17.00 ? 69 TRP A NE1 1 ATOM 548 C CE2 . TRP A 1 69 ? 17.035 22.051 39.278 1.00 16.43 ? 69 TRP A CE2 1 ATOM 549 C CE3 . TRP A 1 69 ? 16.070 20.500 37.677 1.00 12.79 ? 69 TRP A CE3 1 ATOM 550 C CZ2 . TRP A 1 69 ? 16.269 21.522 40.327 1.00 16.64 ? 69 TRP A CZ2 1 ATOM 551 C CZ3 . TRP A 1 69 ? 15.309 19.978 38.721 1.00 13.06 ? 69 TRP A CZ3 1 ATOM 552 C CH2 . TRP A 1 69 ? 15.417 20.491 40.028 1.00 16.57 ? 69 TRP A CH2 1 ATOM 553 N N . ILE A 1 70 ? 17.004 20.437 33.236 1.00 16.08 ? 70 ILE A N 1 ATOM 554 C CA . ILE A 1 70 ? 16.533 20.575 31.856 1.00 18.59 ? 70 ILE A CA 1 ATOM 555 C C . ILE A 1 70 ? 15.148 21.225 32.044 1.00 14.60 ? 70 ILE A C 1 ATOM 556 O O . ILE A 1 70 ? 14.626 21.260 33.167 1.00 14.91 ? 70 ILE A O 1 ATOM 557 C CB . ILE A 1 70 ? 16.431 19.237 31.071 1.00 15.16 ? 70 ILE A CB 1 ATOM 558 C CG1 . ILE A 1 70 ? 15.427 18.292 31.728 1.00 19.91 ? 70 ILE A CG1 1 ATOM 559 C CG2 . ILE A 1 70 ? 17.815 18.615 30.945 1.00 19.00 ? 70 ILE A CG2 1 ATOM 560 C CD1 . ILE A 1 70 ? 15.237 17.001 30.943 1.00 21.14 ? 70 ILE A CD1 1 ATOM 561 N N . GLY A 1 71 ? 14.554 21.750 30.974 1.00 16.27 ? 71 GLY A N 1 ATOM 562 C CA . GLY A 1 71 ? 13.291 22.459 31.132 1.00 15.10 ? 71 GLY A CA 1 ATOM 563 C C . GLY A 1 71 ? 11.999 21.681 31.259 1.00 15.44 ? 71 GLY A C 1 ATOM 564 O O . GLY A 1 71 ? 10.944 22.190 30.889 1.00 17.20 ? 71 GLY A O 1 ATOM 565 N N . LEU A 1 72 ? 12.055 20.474 31.814 1.00 16.42 ? 72 LEU A N 1 ATOM 566 C CA . LEU A 1 72 ? 10.852 19.648 31.920 1.00 17.68 ? 72 LEU A CA 1 ATOM 567 C C . LEU A 1 72 ? 10.302 19.602 33.332 1.00 18.23 ? 72 LEU A C 1 ATOM 568 O O . LEU A 1 72 ? 11.041 19.366 34.281 1.00 18.47 ? 72 LEU A O 1 ATOM 569 C CB . LEU A 1 72 ? 11.168 18.219 31.482 1.00 21.91 ? 72 LEU A CB 1 ATOM 570 C CG . LEU A 1 72 ? 9.979 17.287 31.249 1.00 18.17 ? 72 LEU A CG 1 ATOM 571 C CD1 . LEU A 1 72 ? 9.209 17.733 29.991 1.00 16.85 ? 72 LEU A CD1 1 ATOM 572 C CD2 . LEU A 1 72 ? 10.487 15.872 31.068 1.00 15.82 ? 72 LEU A CD2 1 ATOM 573 N N . ARG A 1 73 ? 9.005 19.830 33.476 1.00 17.06 ? 73 ARG A N 1 ATOM 574 C CA . ARG A 1 73 ? 8.387 19.754 34.796 1.00 21.10 ? 73 ARG A CA 1 ATOM 575 C C . ARG A 1 73 ? 6.879 19.584 34.699 1.00 19.64 ? 73 ARG A C 1 ATOM 576 O O . ARG A 1 73 ? 6.290 19.792 33.638 1.00 18.31 ? 73 ARG A O 1 ATOM 577 C CB . ARG A 1 73 ? 8.670 21.024 35.613 1.00 18.99 ? 73 ARG A CB 1 ATOM 578 C CG . ARG A 1 73 ? 7.824 22.240 35.201 1.00 24.02 ? 73 ARG A CG 1 ATOM 579 C CD . ARG A 1 73 ? 8.019 23.459 36.153 1.00 20.28 ? 73 ARG A CD 1 ATOM 580 N NE . ARG A 1 73 ? 7.346 24.649 35.636 1.00 21.86 ? 73 ARG A NE 1 ATOM 581 C CZ . ARG A 1 73 ? 6.392 25.332 36.267 1.00 27.58 ? 73 ARG A CZ 1 ATOM 582 N NH1 . ARG A 1 73 ? 5.847 26.397 35.680 1.00 25.05 ? 73 ARG A NH1 1 ATOM 583 N NH2 . ARG A 1 73 ? 5.988 24.974 37.481 1.00 23.82 ? 73 ARG A NH2 1 ATOM 584 N N . ASP A 1 74 ? 6.260 19.185 35.810 1.00 18.10 ? 74 ASP A N 1 ATOM 585 C CA . ASP A 1 74 ? 4.802 19.074 35.859 1.00 19.91 ? 74 ASP A CA 1 ATOM 586 C C . ASP A 1 74 ? 4.419 20.360 36.591 1.00 21.14 ? 74 ASP A C 1 ATOM 587 O O . ASP A 1 74 ? 4.810 20.572 37.743 1.00 20.15 ? 74 ASP A O 1 ATOM 588 C CB . ASP A 1 74 ? 4.364 17.840 36.644 1.00 17.03 ? 74 ASP A CB 1 ATOM 589 C CG . ASP A 1 74 ? 2.852 17.693 36.692 1.00 18.42 ? 74 ASP A CG 1 ATOM 590 O OD1 . ASP A 1 74 ? 2.334 16.639 36.265 1.00 20.58 ? 74 ASP A OD1 1 ATOM 591 O OD2 . ASP A 1 74 ? 2.192 18.632 37.164 1.00 21.53 ? 74 ASP A OD2 1 ATOM 592 N N . ARG A 1 75 ? 3.667 21.218 35.910 1.00 19.26 ? 75 ARG A N 1 ATOM 593 C CA . ARG A 1 75 ? 3.279 22.529 36.425 1.00 19.92 ? 75 ARG A CA 1 ATOM 594 C C . ARG A 1 75 ? 2.163 22.620 37.457 1.00 23.08 ? 75 ARG A C 1 ATOM 595 O O . ARG A 1 75 ? 1.799 23.724 37.861 1.00 21.16 ? 75 ARG A O 1 ATOM 596 C CB . ARG A 1 75 ? 2.895 23.437 35.256 1.00 23.20 ? 75 ARG A CB 1 ATOM 597 C CG . ARG A 1 75 ? 3.921 23.469 34.136 1.00 27.80 ? 75 ARG A CG 1 ATOM 598 C CD . ARG A 1 75 ? 3.473 24.368 32.994 1.00 25.22 ? 75 ARG A CD 1 ATOM 599 N NE . ARG A 1 75 ? 4.426 24.309 31.882 1.00 24.82 ? 75 ARG A NE 1 ATOM 600 C CZ . ARG A 1 75 ? 4.252 24.913 30.712 1.00 30.50 ? 75 ARG A CZ 1 ATOM 601 N NH1 . ARG A 1 75 ? 5.176 24.804 29.761 1.00 29.02 ? 75 ARG A NH1 1 ATOM 602 N NH2 . ARG A 1 75 ? 3.152 25.622 30.494 1.00 22.82 ? 75 ARG A NH2 1 ATOM 603 N N . ARG A 1 76 ? 1.613 21.499 37.898 1.00 23.33 ? 76 ARG A N 1 ATOM 604 C CA . ARG A 1 76 ? 0.515 21.592 38.859 1.00 20.66 ? 76 ARG A CA 1 ATOM 605 C C . ARG A 1 76 ? 0.880 22.178 40.223 1.00 24.58 ? 76 ARG A C 1 ATOM 606 O O . ARG A 1 76 ? 2.046 22.274 40.596 1.00 23.32 ? 76 ARG A O 1 ATOM 607 C CB . ARG A 1 76 ? -0.134 20.225 39.048 1.00 23.90 ? 76 ARG A CB 1 ATOM 608 C CG . ARG A 1 76 ? 0.675 19.242 39.864 1.00 27.48 ? 76 ARG A CG 1 ATOM 609 C CD . ARG A 1 76 ? -0.009 17.903 39.828 1.00 23.20 ? 76 ARG A CD 1 ATOM 610 N NE . ARG A 1 76 ? 0.160 17.259 38.523 1.00 20.65 ? 76 ARG A NE 1 ATOM 611 C CZ . ARG A 1 76 ? -0.614 16.278 38.067 1.00 24.13 ? 76 ARG A CZ 1 ATOM 612 N NH1 . ARG A 1 76 ? -1.632 15.828 38.800 1.00 26.59 ? 76 ARG A NH1 1 ATOM 613 N NH2 . ARG A 1 76 ? -0.359 15.726 36.888 1.00 22.16 ? 76 ARG A NH2 1 ATOM 614 N N . GLU A 1 77 ? -0.137 22.561 40.985 1.00 22.48 ? 77 GLU A N 1 ATOM 615 C CA . GLU A 1 77 ? 0.109 23.122 42.304 1.00 25.12 ? 77 GLU A CA 1 ATOM 616 C C . GLU A 1 77 ? 0.416 22.024 43.325 1.00 21.57 ? 77 GLU A C 1 ATOM 617 O O . GLU A 1 77 ? 1.124 22.258 44.302 1.00 20.16 ? 77 GLU A O 1 ATOM 618 C CB . GLU A 1 77 ? -1.119 23.905 42.755 1.00 28.42 ? 77 GLU A CB 1 ATOM 619 C CG . GLU A 1 77 ? -1.009 24.519 44.127 1.00 45.98 ? 77 GLU A CG 1 ATOM 620 C CD . GLU A 1 77 ? -2.318 25.156 44.563 1.00 59.54 ? 77 GLU A CD 1 ATOM 621 O OE1 . GLU A 1 77 ? -2.832 26.024 43.820 1.00 62.57 ? 77 GLU A OE1 1 ATOM 622 O OE2 . GLU A 1 77 ? -2.834 24.788 45.643 1.00 63.51 ? 77 GLU A OE2 1 ATOM 623 N N . GLU A 1 78 ? -0.141 20.836 43.094 1.00 20.19 ? 78 GLU A N 1 ATOM 624 C CA . GLU A 1 78 ? 0.035 19.697 43.995 1.00 19.19 ? 78 GLU A CA 1 ATOM 625 C C . GLU A 1 78 ? 1.467 19.174 44.040 1.00 21.48 ? 78 GLU A C 1 ATOM 626 O O . GLU A 1 78 ? 2.227 19.355 43.092 1.00 18.52 ? 78 GLU A O 1 ATOM 627 C CB . GLU A 1 78 ? -0.911 18.565 43.588 1.00 18.94 ? 78 GLU A CB 1 ATOM 628 C CG . GLU A 1 78 ? -2.395 18.847 43.859 1.00 25.51 ? 78 GLU A CG 1 ATOM 629 C CD . GLU A 1 78 ? -3.066 19.679 42.770 1.00 32.85 ? 78 GLU A CD 1 ATOM 630 O OE1 . GLU A 1 78 ? -4.266 19.991 42.930 1.00 31.80 ? 78 GLU A OE1 1 ATOM 631 O OE2 . GLU A 1 78 ? -2.407 20.016 41.754 1.00 28.40 ? 78 GLU A OE2 1 ATOM 632 N N . GLN A 1 79 ? 1.820 18.484 45.125 1.00 18.01 ? 79 GLN A N 1 ATOM 633 C CA . GLN A 1 79 ? 3.176 17.959 45.282 1.00 19.54 ? 79 GLN A CA 1 ATOM 634 C C . GLN A 1 79 ? 3.472 16.626 44.608 1.00 15.36 ? 79 GLN A C 1 ATOM 635 O O . GLN A 1 79 ? 4.587 16.105 44.702 1.00 17.98 ? 79 GLN A O 1 ATOM 636 C CB . GLN A 1 79 ? 3.520 17.869 46.771 1.00 18.89 ? 79 GLN A CB 1 ATOM 637 C CG . GLN A 1 79 ? 3.693 19.245 47.408 1.00 25.40 ? 79 GLN A CG 1 ATOM 638 C CD . GLN A 1 79 ? 3.678 19.184 48.916 1.00 33.25 ? 79 GLN A CD 1 ATOM 639 O OE1 . GLN A 1 79 ? 4.438 18.441 49.522 1.00 27.08 ? 79 GLN A OE1 1 ATOM 640 N NE2 . GLN A 1 79 ? 2.797 19.966 49.531 1.00 46.13 ? 79 GLN A NE2 1 ATOM 641 N N . GLN A 1 80 ? 2.480 16.055 43.945 1.00 17.32 ? 80 GLN A N 1 ATOM 642 C CA . GLN A 1 80 ? 2.686 14.791 43.239 1.00 16.90 ? 80 GLN A CA 1 ATOM 643 C C . GLN A 1 80 ? 1.573 14.674 42.200 1.00 18.08 ? 80 GLN A C 1 ATOM 644 O O . GLN A 1 80 ? 0.679 15.508 42.167 1.00 19.44 ? 80 GLN A O 1 ATOM 645 C CB . GLN A 1 80 ? 2.664 13.591 44.200 1.00 17.49 ? 80 GLN A CB 1 ATOM 646 C CG . GLN A 1 80 ? 1.333 13.354 44.928 1.00 18.65 ? 80 GLN A CG 1 ATOM 647 C CD . GLN A 1 80 ? 0.993 14.452 45.913 1.00 20.73 ? 80 GLN A CD 1 ATOM 648 O OE1 . GLN A 1 80 ? 1.812 14.825 46.760 1.00 17.94 ? 80 GLN A OE1 1 ATOM 649 N NE2 . GLN A 1 80 ? -0.227 14.974 45.820 1.00 17.12 ? 80 GLN A NE2 1 ATOM 650 N N . CYS A 1 81 ? 1.629 13.640 41.370 1.00 18.58 ? 81 CYS A N 1 ATOM 651 C CA . CYS A 1 81 ? 0.663 13.484 40.288 1.00 17.75 ? 81 CYS A CA 1 ATOM 652 C C . CYS A 1 81 ? -0.497 12.509 40.473 1.00 20.87 ? 81 CYS A C 1 ATOM 653 O O . CYS A 1 81 ? -1.612 12.772 40.002 1.00 19.65 ? 81 CYS A O 1 ATOM 654 C CB . CYS A 1 81 ? 1.404 13.095 39.005 1.00 22.56 ? 81 CYS A CB 1 ATOM 655 S SG . CYS A 1 81 ? 2.969 14.001 38.718 1.00 23.11 ? 81 CYS A SG 1 ATOM 656 N N . ASN A 1 82 ? -0.227 11.379 41.113 1.00 18.29 ? 82 ASN A N 1 ATOM 657 C CA . ASN A 1 82 ? -1.242 10.344 41.295 1.00 21.73 ? 82 ASN A CA 1 ATOM 658 C C . ASN A 1 82 ? -2.471 10.933 41.980 1.00 22.94 ? 82 ASN A C 1 ATOM 659 O O . ASN A 1 82 ? -2.379 11.465 43.079 1.00 22.97 ? 82 ASN A O 1 ATOM 660 C CB . ASN A 1 82 ? -0.667 9.203 42.124 1.00 19.30 ? 82 ASN A CB 1 ATOM 661 C CG . ASN A 1 82 ? -1.472 7.940 41.988 1.00 22.44 ? 82 ASN A CG 1 ATOM 662 O OD1 . ASN A 1 82 ? -2.664 7.993 41.701 1.00 22.09 ? 82 ASN A OD1 1 ATOM 663 N ND2 . ASN A 1 82 ? -0.830 6.794 42.204 1.00 20.19 ? 82 ASN A ND2 1 ATOM 664 N N . PRO A 1 83 ? -3.645 10.851 41.337 1.00 25.52 ? 83 PRO A N 1 ATOM 665 C CA . PRO A 1 83 ? -4.836 11.420 41.974 1.00 23.07 ? 83 PRO A CA 1 ATOM 666 C C . PRO A 1 83 ? -5.476 10.621 43.102 1.00 18.76 ? 83 PRO A C 1 ATOM 667 O O . PRO A 1 83 ? -6.243 11.179 43.880 1.00 25.09 ? 83 PRO A O 1 ATOM 668 C CB . PRO A 1 83 ? -5.791 11.609 40.798 1.00 32.05 ? 83 PRO A CB 1 ATOM 669 C CG . PRO A 1 83 ? -5.479 10.421 39.943 1.00 29.37 ? 83 PRO A CG 1 ATOM 670 C CD . PRO A 1 83 ? -3.955 10.346 39.985 1.00 25.36 ? 83 PRO A CD 1 ATOM 671 N N . GLU A 1 84 ? -5.160 9.335 43.211 1.00 20.80 ? 84 GLU A N 1 ATOM 672 C CA . GLU A 1 84 ? -5.792 8.508 44.238 1.00 23.64 ? 84 GLU A CA 1 ATOM 673 C C . GLU A 1 84 ? -4.913 7.542 45.006 1.00 25.19 ? 84 GLU A C 1 ATOM 674 O O . GLU A 1 84 ? -3.882 7.079 44.514 1.00 24.97 ? 84 GLU A O 1 ATOM 675 C CB . GLU A 1 84 ? -6.930 7.681 43.610 1.00 23.87 ? 84 GLU A CB 1 ATOM 676 C CG . GLU A 1 84 ? -7.982 8.509 42.893 1.00 25.93 ? 84 GLU A CG 1 ATOM 677 C CD . GLU A 1 84 ? -9.146 7.675 42.375 1.00 35.73 ? 84 GLU A CD 1 ATOM 678 O OE1 . GLU A 1 84 ? -8.985 6.444 42.212 1.00 34.65 ? 84 GLU A OE1 1 ATOM 679 O OE2 . GLU A 1 84 ? -10.219 8.259 42.118 1.00 32.76 ? 84 GLU A OE2 1 ATOM 680 N N . TRP A 1 85 ? -5.348 7.224 46.224 1.00 19.14 ? 85 TRP A N 1 ATOM 681 C CA . TRP A 1 85 ? -4.653 6.239 47.024 1.00 22.64 ? 85 TRP A CA 1 ATOM 682 C C . TRP A 1 85 ? -5.001 4.878 46.427 1.00 24.19 ? 85 TRP A C 1 ATOM 683 O O . TRP A 1 85 ? -5.890 4.773 45.590 1.00 28.87 ? 85 TRP A O 1 ATOM 684 C CB . TRP A 1 85 ? -5.143 6.252 48.482 1.00 20.71 ? 85 TRP A CB 1 ATOM 685 C CG . TRP A 1 85 ? -4.739 7.449 49.240 1.00 20.41 ? 85 TRP A CG 1 ATOM 686 C CD1 . TRP A 1 85 ? -5.407 8.631 49.326 1.00 19.38 ? 85 TRP A CD1 1 ATOM 687 C CD2 . TRP A 1 85 ? -3.566 7.584 50.045 1.00 19.74 ? 85 TRP A CD2 1 ATOM 688 N NE1 . TRP A 1 85 ? -4.723 9.499 50.145 1.00 19.60 ? 85 TRP A NE1 1 ATOM 689 C CE2 . TRP A 1 85 ? -3.588 8.879 50.597 1.00 17.40 ? 85 TRP A CE2 1 ATOM 690 C CE3 . TRP A 1 85 ? -2.495 6.730 50.354 1.00 20.42 ? 85 TRP A CE3 1 ATOM 691 C CZ2 . TRP A 1 85 ? -2.575 9.350 51.444 1.00 18.33 ? 85 TRP A CZ2 1 ATOM 692 C CZ3 . TRP A 1 85 ? -1.487 7.194 51.195 1.00 26.21 ? 85 TRP A CZ3 1 ATOM 693 C CH2 . TRP A 1 85 ? -1.535 8.492 51.731 1.00 19.53 ? 85 TRP A CH2 1 ATOM 694 N N . ASN A 1 86 ? -4.300 3.847 46.883 1.00 22.89 ? 86 ASN A N 1 ATOM 695 C CA . ASN A 1 86 ? -4.526 2.480 46.453 1.00 23.30 ? 86 ASN A CA 1 ATOM 696 C C . ASN A 1 86 ? -6.008 2.101 46.616 1.00 32.30 ? 86 ASN A C 1 ATOM 697 O O . ASN A 1 86 ? -6.565 1.364 45.796 1.00 27.11 ? 86 ASN A O 1 ATOM 698 C CB . ASN A 1 86 ? -3.660 1.542 47.297 1.00 22.60 ? 86 ASN A CB 1 ATOM 699 C CG . ASN A 1 86 ? -3.994 1.614 48.798 1.00 25.43 ? 86 ASN A CG 1 ATOM 700 O OD1 . ASN A 1 86 ? -4.528 2.612 49.283 1.00 22.38 ? 86 ASN A OD1 1 ATOM 701 N ND2 . ASN A 1 86 ? -3.660 0.563 49.530 1.00 20.58 ? 86 ASN A ND2 1 ATOM 702 N N . ASP A 1 87 ? -6.651 2.629 47.655 1.00 25.99 ? 87 ASP A N 1 ATOM 703 C CA . ASP A 1 87 ? -8.053 2.302 47.918 1.00 31.00 ? 87 ASP A CA 1 ATOM 704 C C . ASP A 1 87 ? -9.093 3.144 47.183 1.00 30.83 ? 87 ASP A C 1 ATOM 705 O O . ASP A 1 87 ? -10.291 3.037 47.460 1.00 28.36 ? 87 ASP A O 1 ATOM 706 C CB . ASP A 1 87 ? -8.322 2.331 49.433 1.00 25.78 ? 87 ASP A CB 1 ATOM 707 C CG . ASP A 1 87 ? -8.146 3.718 50.057 1.00 29.68 ? 87 ASP A CG 1 ATOM 708 O OD1 . ASP A 1 87 ? -7.920 3.775 51.288 1.00 26.49 ? 87 ASP A OD1 1 ATOM 709 O OD2 . ASP A 1 87 ? -8.246 4.741 49.343 1.00 28.26 ? 87 ASP A OD2 1 ATOM 710 N N . GLY A 1 88 ? -8.641 3.980 46.248 1.00 28.04 ? 88 GLY A N 1 ATOM 711 C CA . GLY A 1 88 ? -9.570 4.809 45.492 1.00 25.93 ? 88 GLY A CA 1 ATOM 712 C C . GLY A 1 88 ? -9.864 6.196 46.040 1.00 28.53 ? 88 GLY A C 1 ATOM 713 O O . GLY A 1 88 ? -10.390 7.041 45.314 1.00 28.31 ? 88 GLY A O 1 ATOM 714 N N . SER A 1 89 ? -9.559 6.445 47.315 1.00 24.33 ? 89 SER A N 1 ATOM 715 C CA . SER A 1 89 ? -9.820 7.767 47.877 1.00 21.22 ? 89 SER A CA 1 ATOM 716 C C . SER A 1 89 ? -8.875 8.800 47.278 1.00 25.82 ? 89 SER A C 1 ATOM 717 O O . SER A 1 89 ? -7.786 8.464 46.808 1.00 22.77 ? 89 SER A O 1 ATOM 718 C CB . SER A 1 89 ? -9.681 7.764 49.407 1.00 28.23 ? 89 SER A CB 1 ATOM 719 O OG . SER A 1 89 ? -8.413 7.293 49.826 1.00 23.28 ? 89 SER A OG 1 ATOM 720 N N . LYS A 1 90 ? -9.300 10.057 47.289 1.00 25.00 ? 90 LYS A N 1 ATOM 721 C CA . LYS A 1 90 ? -8.498 11.139 46.726 1.00 28.45 ? 90 LYS A CA 1 ATOM 722 C C . LYS A 1 90 ? -7.273 11.474 47.559 1.00 27.75 ? 90 LYS A C 1 ATOM 723 O O . LYS A 1 90 ? -7.305 11.437 48.794 1.00 22.27 ? 90 LYS A O 1 ATOM 724 C CB . LYS A 1 90 ? -9.345 12.403 46.587 1.00 30.71 ? 90 LYS A CB 1 ATOM 725 C CG . LYS A 1 90 ? -10.585 12.232 45.727 1.00 39.19 ? 90 LYS A CG 1 ATOM 726 C CD . LYS A 1 90 ? -10.224 11.801 44.317 1.00 45.57 ? 90 LYS A CD 1 ATOM 727 C CE . LYS A 1 90 ? -11.474 11.653 43.450 1.00 53.18 ? 90 LYS A CE 1 ATOM 728 N NZ . LYS A 1 90 ? -11.148 11.168 42.080 1.00 55.63 ? 90 LYS A NZ 1 ATOM 729 N N . ILE A 1 91 ? -6.180 11.786 46.879 1.00 22.64 ? 91 ILE A N 1 ATOM 730 C CA . ILE A 1 91 ? -4.972 12.184 47.585 1.00 23.09 ? 91 ILE A CA 1 ATOM 731 C C . ILE A 1 91 ? -5.089 13.697 47.747 1.00 23.34 ? 91 ILE A C 1 ATOM 732 O O . ILE A 1 91 ? -5.151 14.437 46.766 1.00 23.35 ? 91 ILE A O 1 ATOM 733 C CB . ILE A 1 91 ? -3.701 11.848 46.780 1.00 18.69 ? 91 ILE A CB 1 ATOM 734 C CG1 . ILE A 1 91 ? -3.426 10.340 46.861 1.00 19.97 ? 91 ILE A CG1 1 ATOM 735 C CG2 . ILE A 1 91 ? -2.525 12.669 47.309 1.00 20.03 ? 91 ILE A CG2 1 ATOM 736 C CD1 . ILE A 1 91 ? -2.369 9.843 45.912 1.00 27.15 ? 91 ILE A CD1 1 ATOM 737 N N . ILE A 1 92 ? -5.163 14.150 48.990 1.00 21.01 ? 92 ILE A N 1 ATOM 738 C CA . ILE A 1 92 ? -5.261 15.576 49.285 1.00 20.96 ? 92 ILE A CA 1 ATOM 739 C C . ILE A 1 92 ? -4.175 15.804 50.328 1.00 20.80 ? 92 ILE A C 1 ATOM 740 O O . ILE A 1 92 ? -3.145 16.386 50.035 1.00 21.97 ? 92 ILE A O 1 ATOM 741 C CB . ILE A 1 92 ? -6.648 15.934 49.874 1.00 21.65 ? 92 ILE A CB 1 ATOM 742 C CG1 . ILE A 1 92 ? -7.749 15.544 48.880 1.00 24.07 ? 92 ILE A CG1 1 ATOM 743 C CG2 . ILE A 1 92 ? -6.726 17.431 50.161 1.00 26.06 ? 92 ILE A CG2 1 ATOM 744 C CD1 . ILE A 1 92 ? -7.855 16.469 47.700 1.00 21.59 ? 92 ILE A CD1 1 ATOM 745 N N . TYR A 1 93 ? -4.404 15.326 51.544 1.00 17.90 ? 93 TYR A N 1 ATOM 746 C CA . TYR A 1 93 ? -3.394 15.451 52.581 1.00 19.45 ? 93 TYR A CA 1 ATOM 747 C C . TYR A 1 93 ? -2.177 14.607 52.215 1.00 19.14 ? 93 TYR A C 1 ATOM 748 O O . TYR A 1 93 ? -2.317 13.414 51.882 1.00 16.05 ? 93 TYR A O 1 ATOM 749 C CB . TYR A 1 93 ? -3.917 14.930 53.920 1.00 18.02 ? 93 TYR A CB 1 ATOM 750 C CG . TYR A 1 93 ? -2.856 14.920 55.009 1.00 16.71 ? 93 TYR A CG 1 ATOM 751 C CD1 . TYR A 1 93 ? -2.523 16.094 55.689 1.00 19.49 ? 93 TYR A CD1 1 ATOM 752 C CD2 . TYR A 1 93 ? -2.163 13.752 55.333 1.00 16.49 ? 93 TYR A CD2 1 ATOM 753 C CE1 . TYR A 1 93 ? -1.531 16.106 56.670 1.00 22.39 ? 93 TYR A CE1 1 ATOM 754 C CE2 . TYR A 1 93 ? -1.151 13.758 56.315 1.00 16.58 ? 93 TYR A CE2 1 ATOM 755 C CZ . TYR A 1 93 ? -0.852 14.948 56.975 1.00 20.82 ? 93 TYR A CZ 1 ATOM 756 O OH . TYR A 1 93 ? 0.127 14.991 57.944 1.00 19.68 ? 93 TYR A OH 1 ATOM 757 N N . VAL A 1 94 ? -0.994 15.226 52.266 1.00 18.20 ? 94 VAL A N 1 ATOM 758 C CA . VAL A 1 94 ? 0.276 14.524 52.046 1.00 17.07 ? 94 VAL A CA 1 ATOM 759 C C . VAL A 1 94 ? 1.281 15.111 53.039 1.00 16.25 ? 94 VAL A C 1 ATOM 760 O O . VAL A 1 94 ? 1.101 16.230 53.545 1.00 16.29 ? 94 VAL A O 1 ATOM 761 C CB . VAL A 1 94 ? 0.834 14.675 50.610 1.00 14.46 ? 94 VAL A CB 1 ATOM 762 C CG1 . VAL A 1 94 ? -0.118 14.008 49.617 1.00 14.32 ? 94 VAL A CG1 1 ATOM 763 C CG2 . VAL A 1 94 ? 1.039 16.155 50.276 1.00 13.22 ? 94 VAL A CG2 1 ATOM 764 N N . ASN A 1 95 ? 2.323 14.349 53.338 1.00 13.70 ? 95 ASN A N 1 ATOM 765 C CA . ASN A 1 95 ? 3.334 14.797 54.298 1.00 9.84 ? 95 ASN A CA 1 ATOM 766 C C . ASN A 1 95 ? 4.734 14.355 53.873 1.00 14.15 ? 95 ASN A C 1 ATOM 767 O O . ASN A 1 95 ? 5.389 13.587 54.563 1.00 17.98 ? 95 ASN A O 1 ATOM 768 C CB . ASN A 1 95 ? 2.990 14.241 55.676 1.00 14.17 ? 95 ASN A CB 1 ATOM 769 C CG . ASN A 1 95 ? 3.978 14.682 56.747 1.00 15.96 ? 95 ASN A CG 1 ATOM 770 O OD1 . ASN A 1 95 ? 4.574 15.734 56.639 1.00 18.11 ? 95 ASN A OD1 1 ATOM 771 N ND2 . ASN A 1 95 ? 4.123 13.883 57.793 1.00 18.95 ? 95 ASN A ND2 1 ATOM 772 N N . TRP A 1 96 ? 5.194 14.862 52.734 1.00 16.97 ? 96 TRP A N 1 ATOM 773 C CA . TRP A 1 96 ? 6.517 14.499 52.227 1.00 13.65 ? 96 TRP A CA 1 ATOM 774 C C . TRP A 1 96 ? 7.616 15.166 53.019 1.00 14.88 ? 96 TRP A C 1 ATOM 775 O O . TRP A 1 96 ? 7.477 16.308 53.453 1.00 16.39 ? 96 TRP A O 1 ATOM 776 C CB . TRP A 1 96 ? 6.668 14.918 50.756 1.00 12.70 ? 96 TRP A CB 1 ATOM 777 C CG . TRP A 1 96 ? 5.656 14.274 49.847 1.00 14.05 ? 96 TRP A CG 1 ATOM 778 C CD1 . TRP A 1 96 ? 4.643 14.892 49.183 1.00 11.71 ? 96 TRP A CD1 1 ATOM 779 C CD2 . TRP A 1 96 ? 5.552 12.876 49.536 1.00 13.71 ? 96 TRP A CD2 1 ATOM 780 N NE1 . TRP A 1 96 ? 3.904 13.969 48.477 1.00 18.85 ? 96 TRP A NE1 1 ATOM 781 C CE2 . TRP A 1 96 ? 4.440 12.722 48.678 1.00 15.72 ? 96 TRP A CE2 1 ATOM 782 C CE3 . TRP A 1 96 ? 6.288 11.740 49.906 1.00 16.22 ? 96 TRP A CE3 1 ATOM 783 C CZ2 . TRP A 1 96 ? 4.041 11.473 48.180 1.00 17.37 ? 96 TRP A CZ2 1 ATOM 784 C CZ3 . TRP A 1 96 ? 5.890 10.492 49.411 1.00 19.90 ? 96 TRP A CZ3 1 ATOM 785 C CH2 . TRP A 1 96 ? 4.777 10.370 48.561 1.00 15.37 ? 96 TRP A CH2 1 ATOM 786 N N . LYS A 1 97 ? 8.710 14.446 53.219 1.00 15.41 ? 97 LYS A N 1 ATOM 787 C CA . LYS A 1 97 ? 9.879 15.003 53.892 1.00 15.87 ? 97 LYS A CA 1 ATOM 788 C C . LYS A 1 97 ? 10.405 16.041 52.915 1.00 16.90 ? 97 LYS A C 1 ATOM 789 O O . LYS A 1 97 ? 10.103 15.973 51.709 1.00 14.70 ? 97 LYS A O 1 ATOM 790 C CB . LYS A 1 97 ? 10.958 13.917 54.062 1.00 13.96 ? 97 LYS A CB 1 ATOM 791 C CG . LYS A 1 97 ? 12.132 14.318 54.925 1.00 20.04 ? 97 LYS A CG 1 ATOM 792 C CD . LYS A 1 97 ? 13.227 13.242 54.864 1.00 14.62 ? 97 LYS A CD 1 ATOM 793 C CE . LYS A 1 97 ? 14.336 13.523 55.863 1.00 20.61 ? 97 LYS A CE 1 ATOM 794 N NZ . LYS A 1 97 ? 15.443 12.533 55.778 1.00 20.66 ? 97 LYS A NZ 1 ATOM 795 N N . GLU A 1 98 ? 11.176 17.006 53.417 1.00 18.90 ? 98 GLU A N 1 ATOM 796 C CA . GLU A 1 98 ? 11.761 18.014 52.541 1.00 18.28 ? 98 GLU A CA 1 ATOM 797 C C . GLU A 1 98 ? 12.515 17.258 51.448 1.00 20.39 ? 98 GLU A C 1 ATOM 798 O O . GLU A 1 98 ? 13.169 16.254 51.722 1.00 16.98 ? 98 GLU A O 1 ATOM 799 C CB . GLU A 1 98 ? 12.726 18.928 53.321 1.00 21.96 ? 98 GLU A CB 1 ATOM 800 C CG . GLU A 1 98 ? 13.814 18.185 54.150 1.00 18.61 ? 98 GLU A CG 1 ATOM 801 C CD . GLU A 1 98 ? 13.322 17.753 55.526 1.00 22.24 ? 98 GLU A CD 1 ATOM 802 O OE1 . GLU A 1 98 ? 14.142 17.269 56.343 1.00 21.58 ? 98 GLU A OE1 1 ATOM 803 O OE2 . GLU A 1 98 ? 12.109 17.899 55.807 1.00 21.42 ? 98 GLU A OE2 1 ATOM 804 N N . GLY A 1 99 ? 12.364 17.698 50.203 1.00 16.55 ? 99 GLY A N 1 ATOM 805 C CA . GLY A 1 99 ? 13.060 17.052 49.102 1.00 17.10 ? 99 GLY A CA 1 ATOM 806 C C . GLY A 1 99 ? 12.359 15.872 48.463 1.00 22.35 ? 99 GLY A C 1 ATOM 807 O O . GLY A 1 99 ? 12.792 15.397 47.410 1.00 18.49 ? 99 GLY A O 1 ATOM 808 N N . GLU A 1 100 ? 11.274 15.395 49.070 1.00 18.49 ? 100 GLU A N 1 ATOM 809 C CA . GLU A 1 100 ? 10.575 14.228 48.535 1.00 15.23 ? 100 GLU A CA 1 ATOM 810 C C . GLU A 1 100 ? 9.463 14.509 47.536 1.00 13.43 ? 100 GLU A C 1 ATOM 811 O O . GLU A 1 100 ? 8.892 13.581 46.985 1.00 19.03 ? 100 GLU A O 1 ATOM 812 C CB . GLU A 1 100 ? 10.075 13.337 49.681 1.00 17.17 ? 100 GLU A CB 1 ATOM 813 C CG . GLU A 1 100 ? 11.248 12.725 50.503 1.00 16.43 ? 100 GLU A CG 1 ATOM 814 C CD . GLU A 1 100 ? 12.090 11.735 49.696 1.00 30.26 ? 100 GLU A CD 1 ATOM 815 O OE1 . GLU A 1 100 ? 13.326 11.691 49.885 1.00 23.54 ? 100 GLU A OE1 1 ATOM 816 O OE2 . GLU A 1 100 ? 11.518 10.986 48.883 1.00 21.79 ? 100 GLU A OE2 1 ATOM 817 N N . SER A 1 101 ? 9.120 15.782 47.329 1.00 11.96 ? 101 SER A N 1 ATOM 818 C CA . SER A 1 101 ? 8.149 16.124 46.283 1.00 14.34 ? 101 SER A CA 1 ATOM 819 C C . SER A 1 101 ? 9.092 16.388 45.090 1.00 17.35 ? 101 SER A C 1 ATOM 820 O O . SER A 1 101 ? 9.930 17.294 45.167 1.00 15.75 ? 101 SER A O 1 ATOM 821 C CB . SER A 1 101 ? 7.395 17.418 46.609 1.00 14.93 ? 101 SER A CB 1 ATOM 822 O OG . SER A 1 101 ? 6.646 17.832 45.467 1.00 17.16 ? 101 SER A OG 1 ATOM 823 N N . LYS A 1 102 ? 8.967 15.622 44.008 1.00 15.63 ? 102 LYS A N 1 ATOM 824 C CA . LYS A 1 102 ? 9.882 15.759 42.862 1.00 14.44 ? 102 LYS A CA 1 ATOM 825 C C . LYS A 1 102 ? 9.119 15.965 41.572 1.00 16.74 ? 102 LYS A C 1 ATOM 826 O O . LYS A 1 102 ? 8.744 15.015 40.888 1.00 18.18 ? 102 LYS A O 1 ATOM 827 C CB . LYS A 1 102 ? 10.764 14.510 42.781 1.00 18.69 ? 102 LYS A CB 1 ATOM 828 C CG . LYS A 1 102 ? 11.472 14.227 44.118 1.00 15.95 ? 102 LYS A CG 1 ATOM 829 C CD . LYS A 1 102 ? 12.269 12.912 44.103 1.00 22.40 ? 102 LYS A CD 1 ATOM 830 C CE . LYS A 1 102 ? 12.976 12.688 45.442 1.00 22.05 ? 102 LYS A CE 1 ATOM 831 N NZ . LYS A 1 102 ? 13.666 11.375 45.486 1.00 26.58 ? 102 LYS A NZ 1 ATOM 832 N N . MET A 1 103 ? 8.932 17.231 41.227 1.00 15.40 ? 103 MET A N 1 ATOM 833 C CA . MET A 1 103 ? 8.141 17.572 40.064 1.00 15.01 ? 103 MET A CA 1 ATOM 834 C C . MET A 1 103 ? 8.874 18.238 38.901 1.00 17.23 ? 103 MET A C 1 ATOM 835 O O . MET A 1 103 ? 8.238 18.632 37.917 1.00 15.04 ? 103 MET A O 1 ATOM 836 C CB . MET A 1 103 ? 6.991 18.446 40.533 1.00 16.76 ? 103 MET A CB 1 ATOM 837 C CG . MET A 1 103 ? 6.101 17.747 41.563 1.00 14.62 ? 103 MET A CG 1 ATOM 838 S SD . MET A 1 103 ? 5.126 16.405 40.804 1.00 19.96 ? 103 MET A SD 1 ATOM 839 C CE . MET A 1 103 ? 3.632 17.397 40.384 1.00 19.82 ? 103 MET A CE 1 ATOM 840 N N . CYS A 1 104 ? 10.197 18.356 39.020 1.00 13.92 ? 104 CYS A N 1 ATOM 841 C CA . CYS A 1 104 ? 11.048 18.957 37.968 1.00 17.38 ? 104 CYS A CA 1 ATOM 842 C C . CYS A 1 104 ? 12.068 17.901 37.550 1.00 15.39 ? 104 CYS A C 1 ATOM 843 O O . CYS A 1 104 ? 12.398 17.011 38.333 1.00 16.51 ? 104 CYS A O 1 ATOM 844 C CB . CYS A 1 104 ? 11.793 20.191 38.501 1.00 16.95 ? 104 CYS A CB 1 ATOM 845 S SG . CYS A 1 104 ? 10.708 21.625 38.851 1.00 16.96 ? 104 CYS A SG 1 ATOM 846 N N . GLN A 1 105 ? 12.604 18.018 36.339 1.00 15.08 ? 105 GLN A N 1 ATOM 847 C CA . GLN A 1 105 ? 13.541 17.005 35.871 1.00 15.48 ? 105 GLN A CA 1 ATOM 848 C C . GLN A 1 105 ? 14.941 17.495 35.527 1.00 17.00 ? 105 GLN A C 1 ATOM 849 O O . GLN A 1 105 ? 15.129 18.646 35.136 1.00 14.77 ? 105 GLN A O 1 ATOM 850 C CB . GLN A 1 105 ? 12.928 16.287 34.659 1.00 17.07 ? 105 GLN A CB 1 ATOM 851 C CG . GLN A 1 105 ? 11.588 15.643 34.994 1.00 18.65 ? 105 GLN A CG 1 ATOM 852 C CD . GLN A 1 105 ? 11.426 14.230 34.445 1.00 17.00 ? 105 GLN A CD 1 ATOM 853 O OE1 . GLN A 1 105 ? 10.354 13.623 34.568 1.00 22.83 ? 105 GLN A OE1 1 ATOM 854 N NE2 . GLN A 1 105 ? 12.476 13.703 33.842 1.00 11.85 ? 105 GLN A NE2 1 ATOM 855 N N . GLY A 1 106 ? 15.910 16.594 35.687 1.00 16.90 ? 106 GLY A N 1 ATOM 856 C CA . GLY A 1 106 ? 17.302 16.877 35.375 1.00 16.31 ? 106 GLY A CA 1 ATOM 857 C C . GLY A 1 106 ? 18.023 15.661 34.796 1.00 19.03 ? 106 GLY A C 1 ATOM 858 O O . GLY A 1 106 ? 17.550 14.532 34.948 1.00 15.13 ? 106 GLY A O 1 ATOM 859 N N . LEU A 1 107 ? 19.158 15.890 34.127 1.00 14.83 ? 107 LEU A N 1 ATOM 860 C CA . LEU A 1 107 ? 19.975 14.818 33.543 1.00 14.65 ? 107 LEU A CA 1 ATOM 861 C C . LEU A 1 107 ? 20.668 14.099 34.689 1.00 17.77 ? 107 LEU A C 1 ATOM 862 O O . LEU A 1 107 ? 21.016 14.739 35.662 1.00 14.92 ? 107 LEU A O 1 ATOM 863 C CB . LEU A 1 107 ? 21.042 15.425 32.626 1.00 18.04 ? 107 LEU A CB 1 ATOM 864 C CG . LEU A 1 107 ? 20.494 16.313 31.507 1.00 15.82 ? 107 LEU A CG 1 ATOM 865 C CD1 . LEU A 1 107 ? 21.672 16.930 30.748 1.00 15.67 ? 107 LEU A CD1 1 ATOM 866 C CD2 . LEU A 1 107 ? 19.638 15.480 30.552 1.00 16.91 ? 107 LEU A CD2 1 ATOM 867 N N . THR A 1 108 ? 20.906 12.793 34.574 1.00 18.54 ? 108 THR A N 1 ATOM 868 C CA . THR A 1 108 ? 21.527 12.058 35.681 1.00 16.95 ? 108 THR A CA 1 ATOM 869 C C . THR A 1 108 ? 22.996 11.715 35.493 1.00 21.11 ? 108 THR A C 1 ATOM 870 O O . THR A 1 108 ? 23.406 11.201 34.451 1.00 17.18 ? 108 THR A O 1 ATOM 871 C CB . THR A 1 108 ? 20.737 10.751 35.995 1.00 15.64 ? 108 THR A CB 1 ATOM 872 O OG1 . THR A 1 108 ? 20.873 9.815 34.911 1.00 18.86 ? 108 THR A OG1 1 ATOM 873 C CG2 . THR A 1 108 ? 19.251 11.081 36.144 1.00 20.18 ? 108 THR A CG2 1 ATOM 874 N N . LYS A 1 109 ? 23.791 11.997 36.519 1.00 17.20 ? 109 LYS A N 1 ATOM 875 C CA . LYS A 1 109 ? 25.221 11.724 36.455 1.00 21.84 ? 109 LYS A CA 1 ATOM 876 C C . LYS A 1 109 ? 25.565 10.253 36.220 1.00 23.38 ? 109 LYS A C 1 ATOM 877 O O . LYS A 1 109 ? 26.544 9.947 35.541 1.00 21.15 ? 109 LYS A O 1 ATOM 878 C CB . LYS A 1 109 ? 25.907 12.199 37.734 1.00 25.61 ? 109 LYS A CB 1 ATOM 879 C CG . LYS A 1 109 ? 27.419 12.059 37.682 1.00 27.43 ? 109 LYS A CG 1 ATOM 880 C CD . LYS A 1 109 ? 28.062 12.573 38.965 1.00 32.69 ? 109 LYS A CD 1 ATOM 881 C CE . LYS A 1 109 ? 29.577 12.471 38.902 1.00 35.19 ? 109 LYS A CE 1 ATOM 882 N NZ . LYS A 1 109 ? 30.201 12.915 40.167 1.00 35.82 ? 109 LYS A NZ 1 ATOM 883 N N . TRP A 1 110 ? 24.759 9.347 36.765 1.00 20.77 ? 110 TRP A N 1 ATOM 884 C CA . TRP A 1 110 ? 25.009 7.911 36.608 1.00 27.28 ? 110 TRP A CA 1 ATOM 885 C C . TRP A 1 110 ? 24.982 7.420 35.169 1.00 24.13 ? 110 TRP A C 1 ATOM 886 O O . TRP A 1 110 ? 25.594 6.405 34.839 1.00 25.71 ? 110 TRP A O 1 ATOM 887 C CB . TRP A 1 110 ? 23.992 7.116 37.423 1.00 31.14 ? 110 TRP A CB 1 ATOM 888 C CG . TRP A 1 110 ? 23.954 7.551 38.822 1.00 44.33 ? 110 TRP A CG 1 ATOM 889 C CD1 . TRP A 1 110 ? 22.948 8.229 39.442 1.00 48.63 ? 110 TRP A CD1 1 ATOM 890 C CD2 . TRP A 1 110 ? 25.009 7.425 39.779 1.00 54.19 ? 110 TRP A CD2 1 ATOM 891 N NE1 . TRP A 1 110 ? 23.312 8.541 40.732 1.00 58.82 ? 110 TRP A NE1 1 ATOM 892 C CE2 . TRP A 1 110 ? 24.574 8.059 40.965 1.00 58.08 ? 110 TRP A CE2 1 ATOM 893 C CE3 . TRP A 1 110 ? 26.283 6.840 39.750 1.00 57.34 ? 110 TRP A CE3 1 ATOM 894 C CZ2 . TRP A 1 110 ? 25.369 8.125 42.116 1.00 59.99 ? 110 TRP A CZ2 1 ATOM 895 C CZ3 . TRP A 1 110 ? 27.075 6.905 40.894 1.00 62.12 ? 110 TRP A CZ3 1 ATOM 896 C CH2 . TRP A 1 110 ? 26.612 7.544 42.062 1.00 60.81 ? 110 TRP A CH2 1 ATOM 897 N N . THR A 1 111 ? 24.249 8.120 34.316 1.00 21.50 ? 111 THR A N 1 ATOM 898 C CA . THR A 1 111 ? 24.159 7.748 32.912 1.00 19.45 ? 111 THR A CA 1 ATOM 899 C C . THR A 1 111 ? 24.945 8.741 32.068 1.00 18.12 ? 111 THR A C 1 ATOM 900 O O . THR A 1 111 ? 24.664 8.907 30.889 1.00 17.94 ? 111 THR A O 1 ATOM 901 C CB . THR A 1 111 ? 22.698 7.745 32.427 1.00 26.78 ? 111 THR A CB 1 ATOM 902 O OG1 . THR A 1 111 ? 22.142 9.063 32.564 1.00 20.01 ? 111 THR A OG1 1 ATOM 903 C CG2 . THR A 1 111 ? 21.879 6.772 33.247 1.00 20.92 ? 111 THR A CG2 1 ATOM 904 N N . ASN A 1 112 ? 25.938 9.376 32.681 1.00 17.01 ? 112 ASN A N 1 ATOM 905 C CA . ASN A 1 112 ? 26.765 10.384 32.013 1.00 19.94 ? 112 ASN A CA 1 ATOM 906 C C . ASN A 1 112 ? 25.880 11.480 31.438 1.00 17.86 ? 112 ASN A C 1 ATOM 907 O O . ASN A 1 112 ? 26.140 12.025 30.356 1.00 17.66 ? 112 ASN A O 1 ATOM 908 C CB . ASN A 1 112 ? 27.645 9.760 30.908 1.00 18.22 ? 112 ASN A CB 1 ATOM 909 C CG . ASN A 1 112 ? 28.753 8.862 31.474 1.00 25.32 ? 112 ASN A CG 1 ATOM 910 O OD1 . ASN A 1 112 ? 29.188 9.036 32.617 1.00 24.81 ? 112 ASN A OD1 1 ATOM 911 N ND2 . ASN A 1 112 ? 29.224 7.913 30.666 1.00 29.64 ? 112 ASN A ND2 1 ATOM 912 N N . PHE A 1 113 ? 24.818 11.794 32.176 1.00 18.70 ? 113 PHE A N 1 ATOM 913 C CA . PHE A 1 113 ? 23.865 12.839 31.798 1.00 17.45 ? 113 PHE A CA 1 ATOM 914 C C . PHE A 1 113 ? 23.028 12.608 30.548 1.00 19.06 ? 113 PHE A C 1 ATOM 915 O O . PHE A 1 113 ? 22.745 13.535 29.785 1.00 17.11 ? 113 PHE A O 1 ATOM 916 C CB . PHE A 1 113 ? 24.586 14.200 31.728 1.00 17.99 ? 113 PHE A CB 1 ATOM 917 C CG . PHE A 1 113 ? 25.187 14.629 33.051 1.00 20.96 ? 113 PHE A CG 1 ATOM 918 C CD1 . PHE A 1 113 ? 26.537 14.972 33.154 1.00 21.24 ? 113 PHE A CD1 1 ATOM 919 C CD2 . PHE A 1 113 ? 24.408 14.647 34.207 1.00 22.37 ? 113 PHE A CD2 1 ATOM 920 C CE1 . PHE A 1 113 ? 27.106 15.324 34.391 1.00 21.84 ? 113 PHE A CE1 1 ATOM 921 C CE2 . PHE A 1 113 ? 24.966 14.998 35.455 1.00 18.27 ? 113 PHE A CE2 1 ATOM 922 C CZ . PHE A 1 113 ? 26.314 15.335 35.545 1.00 20.84 ? 113 PHE A CZ 1 ATOM 923 N N . HIS A 1 114 ? 22.605 11.358 30.359 1.00 20.57 ? 114 HIS A N 1 ATOM 924 C CA . HIS A 1 114 ? 21.760 10.984 29.238 1.00 14.22 ? 114 HIS A CA 1 ATOM 925 C C . HIS A 1 114 ? 20.305 10.792 29.673 1.00 19.27 ? 114 HIS A C 1 ATOM 926 O O . HIS A 1 114 ? 19.403 11.316 29.037 1.00 18.26 ? 114 HIS A O 1 ATOM 927 C CB . HIS A 1 114 ? 22.256 9.685 28.606 1.00 19.21 ? 114 HIS A CB 1 ATOM 928 C CG . HIS A 1 114 ? 23.516 9.852 27.817 1.00 17.74 ? 114 HIS A CG 1 ATOM 929 N ND1 . HIS A 1 114 ? 23.517 10.234 26.495 1.00 25.82 ? 114 HIS A ND1 1 ATOM 930 C CD2 . HIS A 1 114 ? 24.814 9.704 28.168 1.00 12.61 ? 114 HIS A CD2 1 ATOM 931 C CE1 . HIS A 1 114 ? 24.763 10.312 26.061 1.00 20.00 ? 114 HIS A CE1 1 ATOM 932 N NE2 . HIS A 1 114 ? 25.569 9.996 27.056 1.00 20.68 ? 114 HIS A NE2 1 ATOM 933 N N . ASP A 1 115 ? 20.082 10.015 30.732 1.00 17.21 ? 115 ASP A N 1 ATOM 934 C CA . ASP A 1 115 ? 18.721 9.784 31.211 1.00 15.46 ? 115 ASP A CA 1 ATOM 935 C C . ASP A 1 115 ? 18.259 10.933 32.094 1.00 19.38 ? 115 ASP A C 1 ATOM 936 O O . ASP A 1 115 ? 19.073 11.733 32.551 1.00 18.42 ? 115 ASP A O 1 ATOM 937 C CB . ASP A 1 115 ? 18.641 8.470 32.003 1.00 14.00 ? 115 ASP A CB 1 ATOM 938 C CG . ASP A 1 115 ? 18.613 7.245 31.095 1.00 24.22 ? 115 ASP A CG 1 ATOM 939 O OD1 . ASP A 1 115 ? 18.683 6.120 31.629 1.00 20.15 ? 115 ASP A OD1 1 ATOM 940 O OD2 . ASP A 1 115 ? 18.513 7.419 29.856 1.00 19.25 ? 115 ASP A OD2 1 ATOM 941 N N . TRP A 1 116 ? 16.948 11.017 32.314 1.00 17.41 ? 116 TRP A N 1 ATOM 942 C CA . TRP A 1 116 ? 16.396 12.083 33.138 1.00 17.22 ? 116 TRP A CA 1 ATOM 943 C C . TRP A 1 116 ? 15.743 11.524 34.378 1.00 16.00 ? 116 TRP A C 1 ATOM 944 O O . TRP A 1 116 ? 15.264 10.390 34.381 1.00 16.48 ? 116 TRP A O 1 ATOM 945 C CB . TRP A 1 116 ? 15.311 12.854 32.392 1.00 15.83 ? 116 TRP A CB 1 ATOM 946 C CG . TRP A 1 116 ? 15.624 13.215 30.982 1.00 16.31 ? 116 TRP A CG 1 ATOM 947 C CD1 . TRP A 1 116 ? 16.849 13.344 30.418 1.00 19.43 ? 116 TRP A CD1 1 ATOM 948 C CD2 . TRP A 1 116 ? 14.670 13.495 29.956 1.00 18.59 ? 116 TRP A CD2 1 ATOM 949 N NE1 . TRP A 1 116 ? 16.724 13.685 29.087 1.00 18.94 ? 116 TRP A NE1 1 ATOM 950 C CE2 . TRP A 1 116 ? 15.395 13.785 28.778 1.00 19.00 ? 116 TRP A CE2 1 ATOM 951 C CE3 . TRP A 1 116 ? 13.268 13.531 29.916 1.00 18.31 ? 116 TRP A CE3 1 ATOM 952 C CZ2 . TRP A 1 116 ? 14.766 14.103 27.565 1.00 24.19 ? 116 TRP A CZ2 1 ATOM 953 C CZ3 . TRP A 1 116 ? 12.635 13.847 28.705 1.00 23.34 ? 116 TRP A CZ3 1 ATOM 954 C CH2 . TRP A 1 116 ? 13.392 14.128 27.546 1.00 25.01 ? 116 TRP A CH2 1 ATOM 955 N N . ASN A 1 117 ? 15.712 12.314 35.435 1.00 14.80 ? 117 ASN A N 1 ATOM 956 C CA . ASN A 1 117 ? 15.022 11.868 36.636 1.00 13.31 ? 117 ASN A CA 1 ATOM 957 C C . ASN A 1 117 ? 14.221 13.029 37.223 1.00 18.79 ? 117 ASN A C 1 ATOM 958 O O . ASN A 1 117 ? 14.637 14.187 37.082 1.00 17.40 ? 117 ASN A O 1 ATOM 959 C CB . ASN A 1 117 ? 16.012 11.361 37.685 1.00 14.43 ? 117 ASN A CB 1 ATOM 960 C CG . ASN A 1 117 ? 15.296 10.701 38.853 1.00 25.64 ? 117 ASN A CG 1 ATOM 961 O OD1 . ASN A 1 117 ? 14.205 10.156 38.670 1.00 16.42 ? 117 ASN A OD1 1 ATOM 962 N ND2 . ASN A 1 117 ? 15.899 10.736 40.045 1.00 22.99 ? 117 ASN A ND2 1 ATOM 963 N N . ASN A 1 118 ? 13.074 12.748 37.849 1.00 15.84 ? 118 ASN A N 1 ATOM 964 C CA . ASN A 1 118 ? 12.315 13.839 38.471 1.00 12.01 ? 118 ASN A CA 1 ATOM 965 C C . ASN A 1 118 ? 12.925 14.058 39.862 1.00 16.00 ? 118 ASN A C 1 ATOM 966 O O . ASN A 1 118 ? 13.169 13.110 40.611 1.00 16.86 ? 118 ASN A O 1 ATOM 967 C CB . ASN A 1 118 ? 10.809 13.541 38.533 1.00 14.31 ? 118 ASN A CB 1 ATOM 968 C CG . ASN A 1 118 ? 10.478 12.250 39.245 1.00 18.76 ? 118 ASN A CG 1 ATOM 969 O OD1 . ASN A 1 118 ? 10.961 11.180 38.869 1.00 15.31 ? 118 ASN A OD1 1 ATOM 970 N ND2 . ASN A 1 118 ? 9.619 12.338 40.267 1.00 16.50 ? 118 ASN A ND2 1 ATOM 971 N N . ILE A 1 119 ? 13.196 15.314 40.190 1.00 13.48 ? 119 ILE A N 1 ATOM 972 C CA . ILE A 1 119 ? 13.832 15.655 41.458 1.00 15.46 ? 119 ILE A CA 1 ATOM 973 C C . ILE A 1 119 ? 13.198 16.914 42.064 1.00 17.15 ? 119 ILE A C 1 ATOM 974 O O . ILE A 1 119 ? 12.345 17.539 41.450 1.00 15.89 ? 119 ILE A O 1 ATOM 975 C CB . ILE A 1 119 ? 15.328 15.893 41.227 1.00 19.05 ? 119 ILE A CB 1 ATOM 976 C CG1 . ILE A 1 119 ? 15.515 17.009 40.203 1.00 19.27 ? 119 ILE A CG1 1 ATOM 977 C CG2 . ILE A 1 119 ? 15.992 14.603 40.665 1.00 18.10 ? 119 ILE A CG2 1 ATOM 978 C CD1 . ILE A 1 119 ? 16.934 17.113 39.665 1.00 29.31 ? 119 ILE A CD1 1 ATOM 979 N N . ASN A 1 120 ? 13.641 17.291 43.257 1.00 16.49 ? 120 ASN A N 1 ATOM 980 C CA . ASN A 1 120 ? 13.099 18.453 43.952 1.00 18.65 ? 120 ASN A CA 1 ATOM 981 C C . ASN A 1 120 ? 13.380 19.780 43.226 1.00 15.36 ? 120 ASN A C 1 ATOM 982 O O . ASN A 1 120 ? 14.532 20.188 43.084 1.00 18.92 ? 120 ASN A O 1 ATOM 983 C CB . ASN A 1 120 ? 13.678 18.489 45.374 1.00 18.91 ? 120 ASN A CB 1 ATOM 984 C CG . ASN A 1 120 ? 13.203 19.684 46.162 1.00 17.97 ? 120 ASN A CG 1 ATOM 985 O OD1 . ASN A 1 120 ? 12.197 20.295 45.823 1.00 21.20 ? 120 ASN A OD1 1 ATOM 986 N ND2 . ASN A 1 120 ? 13.915 20.011 47.237 1.00 24.33 ? 120 ASN A ND2 1 ATOM 987 N N . CYS A 1 121 ? 12.322 20.448 42.775 1.00 17.17 ? 121 CYS A N 1 ATOM 988 C CA . CYS A 1 121 ? 12.439 21.726 42.065 1.00 14.94 ? 121 CYS A CA 1 ATOM 989 C C . CYS A 1 121 ? 13.239 22.788 42.837 1.00 17.14 ? 121 CYS A C 1 ATOM 990 O O . CYS A 1 121 ? 13.850 23.665 42.234 1.00 18.06 ? 121 CYS A O 1 ATOM 991 C CB . CYS A 1 121 ? 11.042 22.292 41.784 1.00 13.03 ? 121 CYS A CB 1 ATOM 992 S SG . CYS A 1 121 ? 9.967 21.270 40.712 1.00 18.14 ? 121 CYS A SG 1 ATOM 993 N N . GLU A 1 122 ? 13.229 22.717 44.169 1.00 14.38 ? 122 GLU A N 1 ATOM 994 C CA . GLU A 1 122 ? 13.959 23.703 44.976 1.00 15.94 ? 122 GLU A CA 1 ATOM 995 C C . GLU A 1 122 ? 15.443 23.413 45.194 1.00 17.61 ? 122 GLU A C 1 ATOM 996 O O . GLU A 1 122 ? 16.177 24.260 45.700 1.00 17.22 ? 122 GLU A O 1 ATOM 997 C CB . GLU A 1 122 ? 13.255 23.897 46.320 1.00 17.91 ? 122 GLU A CB 1 ATOM 998 C CG . GLU A 1 122 ? 12.036 24.795 46.196 1.00 19.89 ? 122 GLU A CG 1 ATOM 999 C CD . GLU A 1 122 ? 11.294 24.953 47.505 1.00 31.91 ? 122 GLU A CD 1 ATOM 1000 O OE1 . GLU A 1 122 ? 10.609 25.983 47.659 1.00 22.06 ? 122 GLU A OE1 1 ATOM 1001 O OE2 . GLU A 1 122 ? 11.395 24.054 48.369 1.00 23.55 ? 122 GLU A OE2 1 ATOM 1002 N N . ASP A 1 123 ? 15.881 22.220 44.801 1.00 16.72 ? 123 ASP A N 1 ATOM 1003 C CA . ASP A 1 123 ? 17.280 21.835 44.927 1.00 16.74 ? 123 ASP A CA 1 ATOM 1004 C C . ASP A 1 123 ? 18.142 22.672 43.961 1.00 17.71 ? 123 ASP A C 1 ATOM 1005 O O . ASP A 1 123 ? 17.648 23.150 42.941 1.00 16.72 ? 123 ASP A O 1 ATOM 1006 C CB . ASP A 1 123 ? 17.436 20.352 44.592 1.00 27.19 ? 123 ASP A CB 1 ATOM 1007 C CG . ASP A 1 123 ? 17.906 19.540 45.772 1.00 41.78 ? 123 ASP A CG 1 ATOM 1008 O OD1 . ASP A 1 123 ? 17.134 19.419 46.742 1.00 48.99 ? 123 ASP A OD1 1 ATOM 1009 O OD2 . ASP A 1 123 ? 19.047 19.028 45.730 1.00 47.49 ? 123 ASP A OD2 1 ATOM 1010 N N . LEU A 1 124 ? 19.424 22.829 44.276 1.00 17.96 ? 124 LEU A N 1 ATOM 1011 C CA . LEU A 1 124 ? 20.333 23.631 43.449 1.00 13.71 ? 124 LEU A CA 1 ATOM 1012 C C . LEU A 1 124 ? 21.250 22.776 42.584 1.00 16.43 ? 124 LEU A C 1 ATOM 1013 O O . LEU A 1 124 ? 21.992 21.920 43.092 1.00 17.14 ? 124 LEU A O 1 ATOM 1014 C CB . LEU A 1 124 ? 21.180 24.533 44.347 1.00 14.73 ? 124 LEU A CB 1 ATOM 1015 C CG . LEU A 1 124 ? 20.373 25.322 45.395 1.00 22.20 ? 124 LEU A CG 1 ATOM 1016 C CD1 . LEU A 1 124 ? 21.341 26.104 46.305 1.00 20.68 ? 124 LEU A CD1 1 ATOM 1017 C CD2 . LEU A 1 124 ? 19.390 26.256 44.700 1.00 16.07 ? 124 LEU A CD2 1 ATOM 1018 N N . TYR A 1 125 ? 21.218 23.025 41.279 1.00 14.69 ? 125 TYR A N 1 ATOM 1019 C CA . TYR A 1 125 ? 22.037 22.259 40.326 1.00 11.88 ? 125 TYR A CA 1 ATOM 1020 C C . TYR A 1 125 ? 22.458 23.122 39.164 1.00 16.52 ? 125 TYR A C 1 ATOM 1021 O O . TYR A 1 125 ? 21.843 24.149 38.891 1.00 17.07 ? 125 TYR A O 1 ATOM 1022 C CB . TYR A 1 125 ? 21.232 21.103 39.727 1.00 11.52 ? 125 TYR A CB 1 ATOM 1023 C CG . TYR A 1 125 ? 20.916 20.033 40.729 1.00 18.38 ? 125 TYR A CG 1 ATOM 1024 C CD1 . TYR A 1 125 ? 21.934 19.240 41.262 1.00 25.85 ? 125 TYR A CD1 1 ATOM 1025 C CD2 . TYR A 1 125 ? 19.616 19.851 41.197 1.00 22.38 ? 125 TYR A CD2 1 ATOM 1026 C CE1 . TYR A 1 125 ? 21.663 18.288 42.250 1.00 20.47 ? 125 TYR A CE1 1 ATOM 1027 C CE2 . TYR A 1 125 ? 19.340 18.897 42.190 1.00 19.41 ? 125 TYR A CE2 1 ATOM 1028 C CZ . TYR A 1 125 ? 20.367 18.132 42.704 1.00 21.35 ? 125 TYR A CZ 1 ATOM 1029 O OH . TYR A 1 125 ? 20.108 17.206 43.689 1.00 34.56 ? 125 TYR A OH 1 ATOM 1030 N N . PRO A 1 126 ? 23.526 22.709 38.469 1.00 16.97 ? 126 PRO A N 1 ATOM 1031 C CA . PRO A 1 126 ? 24.005 23.453 37.307 1.00 19.36 ? 126 PRO A CA 1 ATOM 1032 C C . PRO A 1 126 ? 22.924 23.159 36.256 1.00 16.22 ? 126 PRO A C 1 ATOM 1033 O O . PRO A 1 126 ? 22.047 22.325 36.495 1.00 14.52 ? 126 PRO A O 1 ATOM 1034 C CB . PRO A 1 126 ? 25.357 22.793 36.998 1.00 18.01 ? 126 PRO A CB 1 ATOM 1035 C CG . PRO A 1 126 ? 25.200 21.415 37.508 1.00 19.41 ? 126 PRO A CG 1 ATOM 1036 C CD . PRO A 1 126 ? 24.420 21.582 38.793 1.00 20.30 ? 126 PRO A CD 1 ATOM 1037 N N . PHE A 1 127 ? 22.976 23.813 35.103 1.00 14.53 ? 127 PHE A N 1 ATOM 1038 C CA . PHE A 1 127 ? 21.928 23.615 34.110 1.00 11.76 ? 127 PHE A CA 1 ATOM 1039 C C . PHE A 1 127 ? 22.348 23.979 32.692 1.00 15.21 ? 127 PHE A C 1 ATOM 1040 O O . PHE A 1 127 ? 23.486 24.389 32.454 1.00 17.48 ? 127 PHE A O 1 ATOM 1041 C CB . PHE A 1 127 ? 20.694 24.447 34.497 1.00 12.04 ? 127 PHE A CB 1 ATOM 1042 C CG . PHE A 1 127 ? 21.000 25.913 34.775 1.00 15.66 ? 127 PHE A CG 1 ATOM 1043 C CD1 . PHE A 1 127 ? 20.711 26.899 33.826 1.00 14.87 ? 127 PHE A CD1 1 ATOM 1044 C CD2 . PHE A 1 127 ? 21.554 26.300 35.990 1.00 15.70 ? 127 PHE A CD2 1 ATOM 1045 C CE1 . PHE A 1 127 ? 20.973 28.263 34.093 1.00 17.68 ? 127 PHE A CE1 1 ATOM 1046 C CE2 . PHE A 1 127 ? 21.821 27.653 36.270 1.00 20.60 ? 127 PHE A CE2 1 ATOM 1047 C CZ . PHE A 1 127 ? 21.531 28.632 35.322 1.00 17.52 ? 127 PHE A CZ 1 ATOM 1048 N N . VAL A 1 128 ? 21.428 23.804 31.747 1.00 14.16 ? 128 VAL A N 1 ATOM 1049 C CA . VAL A 1 128 ? 21.718 24.136 30.361 1.00 12.32 ? 128 VAL A CA 1 ATOM 1050 C C . VAL A 1 128 ? 20.627 25.006 29.763 1.00 13.42 ? 128 VAL A C 1 ATOM 1051 O O . VAL A 1 128 ? 19.440 24.698 29.896 1.00 16.82 ? 128 VAL A O 1 ATOM 1052 C CB . VAL A 1 128 ? 21.833 22.858 29.496 1.00 14.19 ? 128 VAL A CB 1 ATOM 1053 C CG1 . VAL A 1 128 ? 22.069 23.240 28.027 1.00 18.96 ? 128 VAL A CG1 1 ATOM 1054 C CG2 . VAL A 1 128 ? 22.966 21.965 30.042 1.00 13.89 ? 128 VAL A CG2 1 ATOM 1055 N N . CYS A 1 129 ? 21.038 26.084 29.084 1.00 17.27 ? 129 CYS A N 1 ATOM 1056 C CA . CYS A 1 129 ? 20.107 26.988 28.429 1.00 14.09 ? 129 CYS A CA 1 ATOM 1057 C C . CYS A 1 129 ? 20.153 26.708 26.935 1.00 15.62 ? 129 CYS A C 1 ATOM 1058 O O . CYS A 1 129 ? 21.144 26.192 26.429 1.00 16.36 ? 129 CYS A O 1 ATOM 1059 C CB . CYS A 1 129 ? 20.490 28.456 28.653 1.00 16.60 ? 129 CYS A CB 1 ATOM 1060 S SG . CYS A 1 129 ? 20.404 29.049 30.376 1.00 18.23 ? 129 CYS A SG 1 ATOM 1061 N N . LYS A 1 130 ? 19.082 27.082 26.249 1.00 15.82 ? 130 LYS A N 1 ATOM 1062 C CA . LYS A 1 130 ? 18.930 26.863 24.817 1.00 17.08 ? 130 LYS A CA 1 ATOM 1063 C C . LYS A 1 130 ? 18.078 27.974 24.221 1.00 20.23 ? 130 LYS A C 1 ATOM 1064 O O . LYS A 1 130 ? 17.172 28.493 24.877 1.00 17.05 ? 130 LYS A O 1 ATOM 1065 C CB . LYS A 1 130 ? 18.231 25.515 24.603 1.00 18.24 ? 130 LYS A CB 1 ATOM 1066 C CG . LYS A 1 130 ? 17.716 25.220 23.189 1.00 16.40 ? 130 LYS A CG 1 ATOM 1067 C CD . LYS A 1 130 ? 16.978 23.877 23.174 1.00 17.70 ? 130 LYS A CD 1 ATOM 1068 C CE . LYS A 1 130 ? 16.369 23.548 21.804 1.00 20.54 ? 130 LYS A CE 1 ATOM 1069 N NZ . LYS A 1 130 ? 15.710 22.198 21.791 1.00 19.80 ? 130 LYS A NZ 1 ATOM 1070 N N . PHE A 1 131 ? 18.394 28.375 22.990 1.00 20.24 ? 131 PHE A N 1 ATOM 1071 C CA . PHE A 1 131 ? 17.559 29.358 22.303 1.00 18.66 ? 131 PHE A CA 1 ATOM 1072 C C . PHE A 1 131 ? 17.714 29.147 20.807 1.00 26.63 ? 131 PHE A C 1 ATOM 1073 O O . PHE A 1 131 ? 18.661 28.501 20.357 1.00 19.07 ? 131 PHE A O 1 ATOM 1074 C CB . PHE A 1 131 ? 17.866 30.820 22.706 1.00 22.41 ? 131 PHE A CB 1 ATOM 1075 C CG . PHE A 1 131 ? 19.157 31.380 22.152 1.00 21.13 ? 131 PHE A CG 1 ATOM 1076 C CD1 . PHE A 1 131 ? 20.342 31.275 22.868 1.00 23.55 ? 131 PHE A CD1 1 ATOM 1077 C CD2 . PHE A 1 131 ? 19.170 32.064 20.940 1.00 30.63 ? 131 PHE A CD2 1 ATOM 1078 C CE1 . PHE A 1 131 ? 21.528 31.849 22.391 1.00 22.82 ? 131 PHE A CE1 1 ATOM 1079 C CE2 . PHE A 1 131 ? 20.350 32.639 20.451 1.00 26.37 ? 131 PHE A CE2 1 ATOM 1080 C CZ . PHE A 1 131 ? 21.524 32.535 21.173 1.00 25.75 ? 131 PHE A CZ 1 ATOM 1081 N N . SER A 1 132 ? 16.755 29.652 20.042 1.00 30.86 ? 132 SER A N 1 ATOM 1082 C CA . SER A 1 132 ? 16.784 29.494 18.597 1.00 36.93 ? 132 SER A CA 1 ATOM 1083 C C . SER A 1 132 ? 17.617 30.575 17.937 1.00 42.51 ? 132 SER A C 1 ATOM 1084 O O . SER A 1 132 ? 17.476 31.759 18.248 1.00 36.80 ? 132 SER A O 1 ATOM 1085 C CB . SER A 1 132 ? 15.363 29.534 18.035 1.00 41.94 ? 132 SER A CB 1 ATOM 1086 O OG . SER A 1 132 ? 15.390 29.527 16.617 1.00 47.45 ? 132 SER A OG 1 ATOM 1087 N N . ALA A 1 133 ? 18.494 30.160 17.030 1.00 49.03 ? 133 ALA A N 1 ATOM 1088 C CA . ALA A 1 133 ? 19.338 31.103 16.313 1.00 53.57 ? 133 ALA A CA 1 ATOM 1089 C C . ALA A 1 133 ? 18.536 31.658 15.135 1.00 56.62 ? 133 ALA A C 1 ATOM 1090 O O . ALA A 1 133 ? 17.657 30.925 14.632 1.00 57.34 ? 133 ALA A O 1 ATOM 1091 C CB . ALA A 1 133 ? 20.597 30.398 15.817 1.00 53.91 ? 133 ALA A CB 1 ATOM 1092 N N . CYS B 2 1 ? -13.150 -3.900 66.586 1.00 32.40 ? 1 CYS B N 1 ATOM 1093 C CA . CYS B 2 1 ? -12.210 -4.575 65.646 1.00 32.22 ? 1 CYS B CA 1 ATOM 1094 C C . CYS B 2 1 ? -11.779 -5.944 66.161 1.00 35.54 ? 1 CYS B C 1 ATOM 1095 O O . CYS B 2 1 ? -11.828 -6.210 67.360 1.00 33.83 ? 1 CYS B O 1 ATOM 1096 C CB . CYS B 2 1 ? -10.954 -3.714 65.441 1.00 28.56 ? 1 CYS B CB 1 ATOM 1097 S SG . CYS B 2 1 ? -11.256 -2.049 64.764 1.00 29.42 ? 1 CYS B SG 1 ATOM 1098 N N . PRO B 2 2 ? -11.338 -6.832 65.255 1.00 35.79 ? 2 PRO B N 1 ATOM 1099 C CA . PRO B 2 2 ? -10.894 -8.167 65.654 1.00 35.63 ? 2 PRO B CA 1 ATOM 1100 C C . PRO B 2 2 ? -9.590 -8.134 66.433 1.00 41.26 ? 2 PRO B C 1 ATOM 1101 O O . PRO B 2 2 ? -8.852 -7.137 66.408 1.00 33.46 ? 2 PRO B O 1 ATOM 1102 C CB . PRO B 2 2 ? -10.749 -8.900 64.321 1.00 41.08 ? 2 PRO B CB 1 ATOM 1103 C CG . PRO B 2 2 ? -10.409 -7.812 63.370 1.00 36.72 ? 2 PRO B CG 1 ATOM 1104 C CD . PRO B 2 2 ? -11.346 -6.704 63.787 1.00 37.22 ? 2 PRO B CD 1 ATOM 1105 N N . LEU B 2 3 ? -9.320 -9.240 67.119 1.00 36.52 ? 3 LEU B N 1 ATOM 1106 C CA . LEU B 2 3 ? -8.123 -9.398 67.928 1.00 42.64 ? 3 LEU B CA 1 ATOM 1107 C C . LEU B 2 3 ? -6.888 -8.966 67.147 1.00 38.67 ? 3 LEU B C 1 ATOM 1108 O O . LEU B 2 3 ? -6.689 -9.385 66.007 1.00 39.25 ? 3 LEU B O 1 ATOM 1109 C CB . LEU B 2 3 ? -7.981 -10.864 68.351 1.00 42.04 ? 3 LEU B CB 1 ATOM 1110 C CG . LEU B 2 3 ? -6.885 -11.267 69.340 1.00 46.98 ? 3 LEU B CG 1 ATOM 1111 C CD1 . LEU B 2 3 ? -7.068 -10.527 70.658 1.00 47.47 ? 3 LEU B CD1 1 ATOM 1112 C CD2 . LEU B 2 3 ? -6.950 -12.774 69.564 1.00 47.04 ? 3 LEU B CD2 1 ATOM 1113 N N . GLY B 2 4 ? -6.069 -8.119 67.762 1.00 34.24 ? 4 GLY B N 1 ATOM 1114 C CA . GLY B 2 4 ? -4.855 -7.663 67.111 1.00 30.15 ? 4 GLY B CA 1 ATOM 1115 C C . GLY B 2 4 ? -5.014 -6.384 66.315 1.00 27.48 ? 4 GLY B C 1 ATOM 1116 O O . GLY B 2 4 ? -4.023 -5.757 65.945 1.00 28.85 ? 4 GLY B O 1 ATOM 1117 N N . TRP B 2 5 ? -6.253 -5.999 66.036 1.00 27.67 ? 5 TRP B N 1 ATOM 1118 C CA . TRP B 2 5 ? -6.511 -4.772 65.290 1.00 26.07 ? 5 TRP B CA 1 ATOM 1119 C C . TRP B 2 5 ? -6.958 -3.653 66.224 1.00 30.58 ? 5 TRP B C 1 ATOM 1120 O O . TRP B 2 5 ? -7.687 -3.890 67.187 1.00 27.23 ? 5 TRP B O 1 ATOM 1121 C CB . TRP B 2 5 ? -7.575 -5.012 64.225 1.00 26.86 ? 5 TRP B CB 1 ATOM 1122 C CG . TRP B 2 5 ? -7.112 -5.950 63.147 1.00 32.99 ? 5 TRP B CG 1 ATOM 1123 C CD1 . TRP B 2 5 ? -6.851 -7.287 63.274 1.00 33.27 ? 5 TRP B CD1 1 ATOM 1124 C CD2 . TRP B 2 5 ? -6.818 -5.610 61.787 1.00 30.38 ? 5 TRP B CD2 1 ATOM 1125 N NE1 . TRP B 2 5 ? -6.407 -7.801 62.071 1.00 36.69 ? 5 TRP B NE1 1 ATOM 1126 C CE2 . TRP B 2 5 ? -6.378 -6.793 61.143 1.00 35.56 ? 5 TRP B CE2 1 ATOM 1127 C CE3 . TRP B 2 5 ? -6.878 -4.420 61.051 1.00 23.22 ? 5 TRP B CE3 1 ATOM 1128 C CZ2 . TRP B 2 5 ? -6.003 -6.817 59.793 1.00 35.16 ? 5 TRP B CZ2 1 ATOM 1129 C CZ3 . TRP B 2 5 ? -6.504 -4.445 59.705 1.00 26.03 ? 5 TRP B CZ3 1 ATOM 1130 C CH2 . TRP B 2 5 ? -6.073 -5.635 59.095 1.00 29.96 ? 5 TRP B CH2 1 ATOM 1131 N N . SER B 2 6 ? -6.525 -2.432 65.922 1.00 23.64 ? 6 SER B N 1 ATOM 1132 C CA . SER B 2 6 ? -6.855 -1.267 66.734 1.00 19.59 ? 6 SER B CA 1 ATOM 1133 C C . SER B 2 6 ? -7.894 -0.386 66.046 1.00 21.72 ? 6 SER B C 1 ATOM 1134 O O . SER B 2 6 ? -7.869 -0.218 64.832 1.00 25.02 ? 6 SER B O 1 ATOM 1135 C CB . SER B 2 6 ? -5.578 -0.480 67.010 1.00 20.01 ? 6 SER B CB 1 ATOM 1136 O OG . SER B 2 6 ? -4.633 -1.307 67.677 1.00 21.16 ? 6 SER B OG 1 ATOM 1137 N N . SER B 2 7 ? -8.795 0.191 66.836 1.00 21.32 ? 7 SER B N 1 ATOM 1138 C CA . SER B 2 7 ? -9.877 1.013 66.309 1.00 20.16 ? 7 SER B CA 1 ATOM 1139 C C . SER B 2 7 ? -9.621 2.513 66.302 1.00 26.25 ? 7 SER B C 1 ATOM 1140 O O . SER B 2 7 ? -9.132 3.070 67.280 1.00 24.40 ? 7 SER B O 1 ATOM 1141 C CB . SER B 2 7 ? -11.153 0.746 67.116 1.00 23.22 ? 7 SER B CB 1 ATOM 1142 O OG . SER B 2 7 ? -12.196 1.636 66.742 1.00 26.17 ? 7 SER B OG 1 ATOM 1143 N N . PHE B 2 8 ? -9.951 3.159 65.190 1.00 18.74 ? 8 PHE B N 1 ATOM 1144 C CA . PHE B 2 8 ? -9.815 4.605 65.088 1.00 22.40 ? 8 PHE B CA 1 ATOM 1145 C C . PHE B 2 8 ? -10.842 5.093 64.079 1.00 23.53 ? 8 PHE B C 1 ATOM 1146 O O . PHE B 2 8 ? -10.831 4.676 62.922 1.00 23.24 ? 8 PHE B O 1 ATOM 1147 C CB . PHE B 2 8 ? -8.416 5.014 64.628 1.00 18.01 ? 8 PHE B CB 1 ATOM 1148 C CG . PHE B 2 8 ? -8.189 6.502 64.644 1.00 20.05 ? 8 PHE B CG 1 ATOM 1149 C CD1 . PHE B 2 8 ? -7.940 7.171 65.842 1.00 22.99 ? 8 PHE B CD1 1 ATOM 1150 C CD2 . PHE B 2 8 ? -8.215 7.233 63.459 1.00 19.09 ? 8 PHE B CD2 1 ATOM 1151 C CE1 . PHE B 2 8 ? -7.716 8.556 65.860 1.00 28.18 ? 8 PHE B CE1 1 ATOM 1152 C CE2 . PHE B 2 8 ? -7.994 8.609 63.465 1.00 26.84 ? 8 PHE B CE2 1 ATOM 1153 C CZ . PHE B 2 8 ? -7.744 9.271 64.664 1.00 23.30 ? 8 PHE B CZ 1 ATOM 1154 N N . ASP B 2 9 ? -11.753 5.942 64.536 1.00 23.72 ? 9 ASP B N 1 ATOM 1155 C CA . ASP B 2 9 ? -12.780 6.501 63.663 1.00 29.89 ? 9 ASP B CA 1 ATOM 1156 C C . ASP B 2 9 ? -13.399 5.497 62.674 1.00 34.65 ? 9 ASP B C 1 ATOM 1157 O O . ASP B 2 9 ? -13.273 5.650 61.449 1.00 28.49 ? 9 ASP B O 1 ATOM 1158 C CB . ASP B 2 9 ? -12.181 7.680 62.901 1.00 33.05 ? 9 ASP B CB 1 ATOM 1159 C CG . ASP B 2 9 ? -13.189 8.383 62.034 1.00 46.42 ? 9 ASP B CG 1 ATOM 1160 O OD1 . ASP B 2 9 ? -14.244 8.787 62.568 1.00 48.75 ? 9 ASP B OD1 1 ATOM 1161 O OD2 . ASP B 2 9 ? -12.917 8.534 60.822 1.00 49.63 ? 9 ASP B OD2 1 ATOM 1162 N N . GLN B 2 10 ? -14.048 4.465 63.209 1.00 28.69 ? 10 GLN B N 1 ATOM 1163 C CA . GLN B 2 10 ? -14.712 3.456 62.384 1.00 33.44 ? 10 GLN B CA 1 ATOM 1164 C C . GLN B 2 10 ? -13.835 2.571 61.502 1.00 33.67 ? 10 GLN B C 1 ATOM 1165 O O . GLN B 2 10 ? -14.358 1.807 60.685 1.00 30.91 ? 10 GLN B O 1 ATOM 1166 C CB . GLN B 2 10 ? -15.781 4.126 61.518 1.00 37.86 ? 10 GLN B CB 1 ATOM 1167 C CG . GLN B 2 10 ? -16.931 4.708 62.322 1.00 47.93 ? 10 GLN B CG 1 ATOM 1168 C CD . GLN B 2 10 ? -17.923 5.464 61.459 1.00 55.20 ? 10 GLN B CD 1 ATOM 1169 O OE1 . GLN B 2 10 ? -18.979 5.877 61.931 1.00 63.72 ? 10 GLN B OE1 1 ATOM 1170 N NE2 . GLN B 2 10 ? -17.581 5.657 60.189 1.00 63.26 ? 10 GLN B NE2 1 ATOM 1171 N N . HIS B 2 11 ? -12.514 2.676 61.643 1.00 25.71 ? 11 HIS B N 1 ATOM 1172 C CA . HIS B 2 11 ? -11.614 1.830 60.867 1.00 26.74 ? 11 HIS B CA 1 ATOM 1173 C C . HIS B 2 11 ? -10.766 0.983 61.787 1.00 26.52 ? 11 HIS B C 1 ATOM 1174 O O . HIS B 2 11 ? -10.590 1.290 62.972 1.00 28.57 ? 11 HIS B O 1 ATOM 1175 C CB . HIS B 2 11 ? -10.701 2.654 59.955 1.00 24.27 ? 11 HIS B CB 1 ATOM 1176 C CG . HIS B 2 11 ? -11.418 3.271 58.798 1.00 28.53 ? 11 HIS B CG 1 ATOM 1177 N ND1 . HIS B 2 11 ? -12.255 4.358 58.935 1.00 27.70 ? 11 HIS B ND1 1 ATOM 1178 C CD2 . HIS B 2 11 ? -11.455 2.927 57.486 1.00 22.04 ? 11 HIS B CD2 1 ATOM 1179 C CE1 . HIS B 2 11 ? -12.775 4.660 57.758 1.00 32.94 ? 11 HIS B CE1 1 ATOM 1180 N NE2 . HIS B 2 11 ? -12.307 3.807 56.863 1.00 28.19 ? 11 HIS B NE2 1 ATOM 1181 N N . CYS B 2 12 ? -10.250 -0.101 61.237 1.00 25.41 ? 12 CYS B N 1 ATOM 1182 C CA . CYS B 2 12 ? -9.413 -1.006 61.987 1.00 24.95 ? 12 CYS B CA 1 ATOM 1183 C C . CYS B 2 12 ? -8.015 -1.042 61.370 1.00 28.64 ? 12 CYS B C 1 ATOM 1184 O O . CYS B 2 12 ? -7.850 -1.198 60.149 1.00 29.15 ? 12 CYS B O 1 ATOM 1185 C CB . CYS B 2 12 ? -10.048 -2.388 62.000 1.00 26.97 ? 12 CYS B CB 1 ATOM 1186 S SG . CYS B 2 12 ? -11.688 -2.379 62.802 1.00 28.14 ? 12 CYS B SG 1 ATOM 1187 N N . TYR B 2 13 ? -7.011 -0.900 62.225 1.00 21.20 ? 13 TYR B N 1 ATOM 1188 C CA . TYR B 2 13 ? -5.623 -0.873 61.782 1.00 24.64 ? 13 TYR B CA 1 ATOM 1189 C C . TYR B 2 13 ? -4.757 -1.921 62.442 1.00 25.98 ? 13 TYR B C 1 ATOM 1190 O O . TYR B 2 13 ? -5.000 -2.315 63.587 1.00 27.34 ? 13 TYR B O 1 ATOM 1191 C CB . TYR B 2 13 ? -4.995 0.497 62.084 1.00 22.75 ? 13 TYR B CB 1 ATOM 1192 C CG . TYR B 2 13 ? -5.749 1.677 61.540 1.00 22.61 ? 13 TYR B CG 1 ATOM 1193 C CD1 . TYR B 2 13 ? -6.953 2.095 62.113 1.00 21.24 ? 13 TYR B CD1 1 ATOM 1194 C CD2 . TYR B 2 13 ? -5.253 2.398 60.457 1.00 19.21 ? 13 TYR B CD2 1 ATOM 1195 C CE1 . TYR B 2 13 ? -7.638 3.209 61.620 1.00 18.65 ? 13 TYR B CE1 1 ATOM 1196 C CE2 . TYR B 2 13 ? -5.936 3.506 59.958 1.00 16.30 ? 13 TYR B CE2 1 ATOM 1197 C CZ . TYR B 2 13 ? -7.118 3.908 60.540 1.00 19.32 ? 13 TYR B CZ 1 ATOM 1198 O OH . TYR B 2 13 ? -7.764 5.022 60.033 1.00 22.66 ? 13 TYR B OH 1 ATOM 1199 N N . LYS B 2 14 ? -3.725 -2.354 61.724 1.00 23.06 ? 14 LYS B N 1 ATOM 1200 C CA . LYS B 2 14 ? -2.782 -3.321 62.262 1.00 24.04 ? 14 LYS B CA 1 ATOM 1201 C C . LYS B 2 14 ? -1.442 -3.227 61.550 1.00 22.82 ? 14 LYS B C 1 ATOM 1202 O O . LYS B 2 14 ? -1.380 -3.249 60.326 1.00 23.24 ? 14 LYS B O 1 ATOM 1203 C CB . LYS B 2 14 ? -3.328 -4.750 62.136 1.00 29.83 ? 14 LYS B CB 1 ATOM 1204 C CG . LYS B 2 14 ? -2.344 -5.786 62.661 1.00 29.00 ? 14 LYS B CG 1 ATOM 1205 C CD . LYS B 2 14 ? -2.885 -7.197 62.534 1.00 35.41 ? 14 LYS B CD 1 ATOM 1206 C CE . LYS B 2 14 ? -1.827 -8.216 62.917 1.00 33.30 ? 14 LYS B CE 1 ATOM 1207 N NZ . LYS B 2 14 ? -2.300 -9.614 62.667 1.00 41.59 ? 14 LYS B NZ 1 ATOM 1208 N N . VAL B 2 15 ? -0.373 -3.121 62.326 1.00 22.60 ? 15 VAL B N 1 ATOM 1209 C CA . VAL B 2 15 ? 0.975 -3.028 61.782 1.00 28.21 ? 15 VAL B CA 1 ATOM 1210 C C . VAL B 2 15 ? 1.624 -4.410 61.742 1.00 31.74 ? 15 VAL B C 1 ATOM 1211 O O . VAL B 2 15 ? 1.571 -5.162 62.723 1.00 26.29 ? 15 VAL B O 1 ATOM 1212 C CB . VAL B 2 15 ? 1.865 -2.095 62.647 1.00 27.33 ? 15 VAL B CB 1 ATOM 1213 C CG1 . VAL B 2 15 ? 3.292 -2.048 62.088 1.00 26.43 ? 15 VAL B CG1 1 ATOM 1214 C CG2 . VAL B 2 15 ? 1.269 -0.689 62.688 1.00 22.41 ? 15 VAL B CG2 1 ATOM 1215 N N . PHE B 2 16 ? 2.243 -4.737 60.609 1.00 25.84 ? 16 PHE B N 1 ATOM 1216 C CA . PHE B 2 16 ? 2.918 -6.025 60.434 1.00 31.17 ? 16 PHE B CA 1 ATOM 1217 C C . PHE B 2 16 ? 4.425 -5.805 60.352 1.00 32.94 ? 16 PHE B C 1 ATOM 1218 O O . PHE B 2 16 ? 4.889 -5.039 59.505 1.00 33.08 ? 16 PHE B O 1 ATOM 1219 C CB . PHE B 2 16 ? 2.423 -6.707 59.156 1.00 26.41 ? 16 PHE B CB 1 ATOM 1220 C CG . PHE B 2 16 ? 0.984 -7.138 59.211 1.00 34.70 ? 16 PHE B CG 1 ATOM 1221 C CD1 . PHE B 2 16 ? -0.043 -6.209 59.119 1.00 30.84 ? 16 PHE B CD1 1 ATOM 1222 C CD2 . PHE B 2 16 ? 0.654 -8.483 59.352 1.00 40.81 ? 16 PHE B CD2 1 ATOM 1223 C CE1 . PHE B 2 16 ? -1.379 -6.607 59.166 1.00 31.31 ? 16 PHE B CE1 1 ATOM 1224 C CE2 . PHE B 2 16 ? -0.680 -8.893 59.401 1.00 34.50 ? 16 PHE B CE2 1 ATOM 1225 C CZ . PHE B 2 16 ? -1.698 -7.955 59.307 1.00 33.11 ? 16 PHE B CZ 1 ATOM 1226 N N . GLU B 2 17 ? 5.194 -6.470 61.216 1.00 25.89 ? 17 GLU B N 1 ATOM 1227 C CA . GLU B 2 17 ? 6.646 -6.285 61.211 1.00 32.76 ? 17 GLU B CA 1 ATOM 1228 C C . GLU B 2 17 ? 7.441 -6.981 60.097 1.00 32.61 ? 17 GLU B C 1 ATOM 1229 O O . GLU B 2 17 ? 8.295 -6.358 59.470 1.00 33.87 ? 17 GLU B O 1 ATOM 1230 C CB . GLU B 2 17 ? 7.244 -6.666 62.570 1.00 31.92 ? 17 GLU B CB 1 ATOM 1231 C CG . GLU B 2 17 ? 8.632 -6.061 62.815 1.00 41.22 ? 17 GLU B CG 1 ATOM 1232 C CD . GLU B 2 17 ? 9.070 -6.132 64.275 1.00 56.93 ? 17 GLU B CD 1 ATOM 1233 O OE1 . GLU B 2 17 ? 10.014 -5.398 64.660 1.00 56.29 ? 17 GLU B OE1 1 ATOM 1234 O OE2 . GLU B 2 17 ? 8.472 -6.925 65.036 1.00 62.79 ? 17 GLU B OE2 1 ATOM 1235 N N . PRO B 2 18 ? 7.176 -8.272 59.830 1.00 38.36 ? 18 PRO B N 1 ATOM 1236 C CA . PRO B 2 18 ? 7.930 -8.964 58.770 1.00 32.82 ? 18 PRO B CA 1 ATOM 1237 C C . PRO B 2 18 ? 7.930 -8.205 57.438 1.00 33.27 ? 18 PRO B C 1 ATOM 1238 O O . PRO B 2 18 ? 6.891 -8.067 56.784 1.00 32.95 ? 18 PRO B O 1 ATOM 1239 C CB . PRO B 2 18 ? 7.229 -10.320 58.680 1.00 39.52 ? 18 PRO B CB 1 ATOM 1240 C CG . PRO B 2 18 ? 6.758 -10.540 60.111 1.00 34.36 ? 18 PRO B CG 1 ATOM 1241 C CD . PRO B 2 18 ? 6.184 -9.174 60.442 1.00 35.13 ? 18 PRO B CD 1 ATOM 1242 N N . VAL B 2 19 ? 9.107 -7.733 57.037 1.00 30.60 ? 19 VAL B N 1 ATOM 1243 C CA . VAL B 2 19 ? 9.261 -6.952 55.808 1.00 32.46 ? 19 VAL B CA 1 ATOM 1244 C C . VAL B 2 19 ? 8.798 -7.642 54.526 1.00 34.37 ? 19 VAL B C 1 ATOM 1245 O O . VAL B 2 19 ? 8.941 -8.854 54.362 1.00 33.04 ? 19 VAL B O 1 ATOM 1246 C CB . VAL B 2 19 ? 10.727 -6.498 55.639 1.00 33.47 ? 19 VAL B CB 1 ATOM 1247 C CG1 . VAL B 2 19 ? 11.147 -5.675 56.847 1.00 34.80 ? 19 VAL B CG1 1 ATOM 1248 C CG2 . VAL B 2 19 ? 11.640 -7.708 55.486 1.00 34.26 ? 19 VAL B CG2 1 ATOM 1249 N N . LYS B 2 20 ? 8.246 -6.850 53.613 1.00 27.41 ? 20 LYS B N 1 ATOM 1250 C CA . LYS B 2 20 ? 7.733 -7.344 52.335 1.00 28.61 ? 20 LYS B CA 1 ATOM 1251 C C . LYS B 2 20 ? 7.792 -6.191 51.332 1.00 27.41 ? 20 LYS B C 1 ATOM 1252 O O . LYS B 2 20 ? 7.844 -5.036 51.747 1.00 31.36 ? 20 LYS B O 1 ATOM 1253 C CB . LYS B 2 20 ? 6.271 -7.764 52.494 1.00 28.92 ? 20 LYS B CB 1 ATOM 1254 C CG . LYS B 2 20 ? 6.017 -8.873 53.509 1.00 35.97 ? 20 LYS B CG 1 ATOM 1255 C CD . LYS B 2 20 ? 6.468 -10.217 52.952 1.00 40.24 ? 20 LYS B CD 1 ATOM 1256 C CE . LYS B 2 20 ? 6.028 -11.366 53.840 1.00 48.22 ? 20 LYS B CE 1 ATOM 1257 N NZ . LYS B 2 20 ? 6.396 -12.681 53.243 1.00 56.63 ? 20 LYS B NZ 1 ATOM 1258 N N . ASN B 2 21 ? 7.786 -6.485 50.031 1.00 31.08 ? 21 ASN B N 1 ATOM 1259 C CA . ASN B 2 21 ? 7.784 -5.404 49.041 1.00 31.33 ? 21 ASN B CA 1 ATOM 1260 C C . ASN B 2 21 ? 6.352 -4.897 49.008 1.00 26.94 ? 21 ASN B C 1 ATOM 1261 O O . ASN B 2 21 ? 5.459 -5.551 49.548 1.00 26.69 ? 21 ASN B O 1 ATOM 1262 C CB . ASN B 2 21 ? 8.254 -5.873 47.642 1.00 30.61 ? 21 ASN B CB 1 ATOM 1263 C CG . ASN B 2 21 ? 7.358 -6.938 47.022 1.00 30.67 ? 21 ASN B CG 1 ATOM 1264 O OD1 . ASN B 2 21 ? 6.140 -6.909 47.170 1.00 28.57 ? 21 ASN B OD1 1 ATOM 1265 N ND2 . ASN B 2 21 ? 7.972 -7.863 46.286 1.00 41.30 ? 21 ASN B ND2 1 ATOM 1266 N N . TRP B 2 22 ? 6.123 -3.735 48.395 1.00 25.41 ? 22 TRP B N 1 ATOM 1267 C CA . TRP B 2 22 ? 4.792 -3.131 48.372 1.00 25.61 ? 22 TRP B CA 1 ATOM 1268 C C . TRP B 2 22 ? 3.634 -3.995 47.877 1.00 27.14 ? 22 TRP B C 1 ATOM 1269 O O . TRP B 2 22 ? 2.563 -4.016 48.491 1.00 25.06 ? 22 TRP B O 1 ATOM 1270 C CB . TRP B 2 22 ? 4.802 -1.836 47.546 1.00 26.56 ? 22 TRP B CB 1 ATOM 1271 C CG . TRP B 2 22 ? 3.643 -0.925 47.841 1.00 23.57 ? 22 TRP B CG 1 ATOM 1272 C CD1 . TRP B 2 22 ? 3.618 0.104 48.756 1.00 25.25 ? 22 TRP B CD1 1 ATOM 1273 C CD2 . TRP B 2 22 ? 2.341 -0.954 47.244 1.00 24.82 ? 22 TRP B CD2 1 ATOM 1274 N NE1 . TRP B 2 22 ? 2.387 0.709 48.754 1.00 21.03 ? 22 TRP B NE1 1 ATOM 1275 C CE2 . TRP B 2 22 ? 1.583 0.081 47.838 1.00 22.19 ? 22 TRP B CE2 1 ATOM 1276 C CE3 . TRP B 2 22 ? 1.737 -1.755 46.262 1.00 25.53 ? 22 TRP B CE3 1 ATOM 1277 C CZ2 . TRP B 2 22 ? 0.254 0.335 47.484 1.00 25.82 ? 22 TRP B CZ2 1 ATOM 1278 C CZ3 . TRP B 2 22 ? 0.416 -1.502 45.909 1.00 25.04 ? 22 TRP B CZ3 1 ATOM 1279 C CH2 . TRP B 2 22 ? -0.311 -0.466 46.519 1.00 25.86 ? 22 TRP B CH2 1 ATOM 1280 N N . THR B 2 23 ? 3.817 -4.697 46.765 1.00 25.88 ? 23 THR B N 1 ATOM 1281 C CA . THR B 2 23 ? 2.719 -5.498 46.225 1.00 30.28 ? 23 THR B CA 1 ATOM 1282 C C . THR B 2 23 ? 2.342 -6.704 47.084 1.00 27.78 ? 23 THR B C 1 ATOM 1283 O O . THR B 2 23 ? 1.159 -7.037 47.207 1.00 31.52 ? 23 THR B O 1 ATOM 1284 C CB . THR B 2 23 ? 3.022 -5.982 44.779 1.00 33.98 ? 23 THR B CB 1 ATOM 1285 O OG1 . THR B 2 23 ? 4.315 -6.592 44.739 1.00 32.22 ? 23 THR B OG1 1 ATOM 1286 C CG2 . THR B 2 23 ? 2.990 -4.815 43.811 1.00 31.08 ? 23 THR B CG2 1 ATOM 1287 N N . GLU B 2 24 ? 3.329 -7.367 47.669 1.00 26.92 ? 24 GLU B N 1 ATOM 1288 C CA . GLU B 2 24 ? 3.005 -8.508 48.505 1.00 33.10 ? 24 GLU B CA 1 ATOM 1289 C C . GLU B 2 24 ? 2.397 -8.009 49.819 1.00 34.05 ? 24 GLU B C 1 ATOM 1290 O O . GLU B 2 24 ? 1.551 -8.677 50.404 1.00 31.15 ? 24 GLU B O 1 ATOM 1291 C CB . GLU B 2 24 ? 4.235 -9.397 48.737 1.00 38.50 ? 24 GLU B CB 1 ATOM 1292 C CG . GLU B 2 24 ? 5.447 -8.762 49.386 1.00 44.59 ? 24 GLU B CG 1 ATOM 1293 C CD . GLU B 2 24 ? 6.685 -9.656 49.261 1.00 50.98 ? 24 GLU B CD 1 ATOM 1294 O OE1 . GLU B 2 24 ? 6.516 -10.895 49.190 1.00 55.44 ? 24 GLU B OE1 1 ATOM 1295 O OE2 . GLU B 2 24 ? 7.823 -9.132 49.241 1.00 44.23 ? 24 GLU B OE2 1 ATOM 1296 N N . ALA B 2 25 ? 2.792 -6.816 50.255 1.00 27.04 ? 25 ALA B N 1 ATOM 1297 C CA . ALA B 2 25 ? 2.238 -6.250 51.484 1.00 29.99 ? 25 ALA B CA 1 ATOM 1298 C C . ALA B 2 25 ? 0.767 -5.933 51.244 1.00 29.79 ? 25 ALA B C 1 ATOM 1299 O O . ALA B 2 25 ? -0.085 -6.167 52.112 1.00 34.37 ? 25 ALA B O 1 ATOM 1300 C CB . ALA B 2 25 ? 2.994 -4.982 51.874 1.00 29.80 ? 25 ALA B CB 1 ATOM 1301 N N . GLU B 2 26 ? 0.464 -5.408 50.060 1.00 24.90 ? 26 GLU B N 1 ATOM 1302 C CA . GLU B 2 26 ? -0.907 -5.069 49.712 1.00 27.48 ? 26 GLU B CA 1 ATOM 1303 C C . GLU B 2 26 ? -1.744 -6.352 49.667 1.00 32.56 ? 26 GLU B C 1 ATOM 1304 O O . GLU B 2 26 ? -2.884 -6.391 50.149 1.00 28.76 ? 26 GLU B O 1 ATOM 1305 C CB . GLU B 2 26 ? -0.949 -4.365 48.350 1.00 21.94 ? 26 GLU B CB 1 ATOM 1306 C CG . GLU B 2 26 ? -2.357 -4.034 47.833 1.00 24.11 ? 26 GLU B CG 1 ATOM 1307 C CD . GLU B 2 26 ? -2.964 -2.796 48.477 1.00 29.16 ? 26 GLU B CD 1 ATOM 1308 O OE1 . GLU B 2 26 ? -2.764 -2.596 49.698 1.00 30.56 ? 26 GLU B OE1 1 ATOM 1309 O OE2 . GLU B 2 26 ? -3.653 -2.027 47.766 1.00 25.24 ? 26 GLU B OE2 1 ATOM 1310 N N . GLU B 2 27 ? -1.173 -7.404 49.087 1.00 33.96 ? 27 GLU B N 1 ATOM 1311 C CA . GLU B 2 27 ? -1.883 -8.675 48.984 1.00 37.91 ? 27 GLU B CA 1 ATOM 1312 C C . GLU B 2 27 ? -2.164 -9.237 50.366 1.00 35.09 ? 27 GLU B C 1 ATOM 1313 O O . GLU B 2 27 ? -3.286 -9.665 50.658 1.00 33.88 ? 27 GLU B O 1 ATOM 1314 C CB . GLU B 2 27 ? -1.068 -9.683 48.165 1.00 44.89 ? 27 GLU B CB 1 ATOM 1315 C CG . GLU B 2 27 ? -0.932 -9.295 46.700 1.00 56.32 ? 27 GLU B CG 1 ATOM 1316 C CD . GLU B 2 27 ? -0.285 -10.377 45.860 1.00 61.47 ? 27 GLU B CD 1 ATOM 1317 O OE1 . GLU B 2 27 ? 0.863 -10.770 46.164 1.00 63.14 ? 27 GLU B OE1 1 ATOM 1318 O OE2 . GLU B 2 27 ? -0.929 -10.830 44.892 1.00 62.99 ? 27 GLU B OE2 1 ATOM 1319 N N . ILE B 2 28 ? -1.137 -9.230 51.209 1.00 31.46 ? 28 ILE B N 1 ATOM 1320 C CA . ILE B 2 28 ? -1.257 -9.721 52.573 1.00 37.45 ? 28 ILE B CA 1 ATOM 1321 C C . ILE B 2 28 ? -2.348 -8.958 53.322 1.00 40.70 ? 28 ILE B C 1 ATOM 1322 O O . ILE B 2 28 ? -3.082 -9.544 54.119 1.00 35.85 ? 28 ILE B O 1 ATOM 1323 C CB . ILE B 2 28 ? 0.080 -9.594 53.334 1.00 33.93 ? 28 ILE B CB 1 ATOM 1324 C CG1 . ILE B 2 28 ? 1.117 -10.529 52.710 1.00 30.24 ? 28 ILE B CG1 1 ATOM 1325 C CG2 . ILE B 2 28 ? -0.123 -9.931 54.815 1.00 37.86 ? 28 ILE B CG2 1 ATOM 1326 C CD1 . ILE B 2 28 ? 2.466 -10.523 53.400 1.00 30.93 ? 28 ILE B CD1 1 ATOM 1327 N N . CYS B 2 29 ? -2.463 -7.656 53.069 1.00 36.61 ? 29 CYS B N 1 ATOM 1328 C CA . CYS B 2 29 ? -3.497 -6.874 53.733 1.00 33.15 ? 29 CYS B CA 1 ATOM 1329 C C . CYS B 2 29 ? -4.868 -7.324 53.252 1.00 37.28 ? 29 CYS B C 1 ATOM 1330 O O . CYS B 2 29 ? -5.791 -7.514 54.053 1.00 32.84 ? 29 CYS B O 1 ATOM 1331 C CB . CYS B 2 29 ? -3.353 -5.379 53.446 1.00 32.88 ? 29 CYS B CB 1 ATOM 1332 S SG . CYS B 2 29 ? -2.058 -4.472 54.357 1.00 27.78 ? 29 CYS B SG 1 ATOM 1333 N N . MET B 2 30 ? -5.009 -7.492 51.940 1.00 31.65 ? 30 MET B N 1 ATOM 1334 C CA . MET B 2 30 ? -6.291 -7.906 51.387 1.00 34.95 ? 30 MET B CA 1 ATOM 1335 C C . MET B 2 30 ? -6.741 -9.271 51.923 1.00 34.18 ? 30 MET B C 1 ATOM 1336 O O . MET B 2 30 ? -7.942 -9.532 52.048 1.00 34.49 ? 30 MET B O 1 ATOM 1337 C CB . MET B 2 30 ? -6.224 -7.932 49.854 1.00 38.97 ? 30 MET B CB 1 ATOM 1338 C CG . MET B 2 30 ? -6.022 -6.559 49.221 1.00 44.81 ? 30 MET B CG 1 ATOM 1339 S SD . MET B 2 30 ? -6.003 -6.599 47.405 1.00 42.58 ? 30 MET B SD 1 ATOM 1340 C CE . MET B 2 30 ? -4.591 -7.598 47.154 1.00 41.69 ? 30 MET B CE 1 ATOM 1341 N N . GLN B 2 31 ? -5.776 -10.127 52.248 1.00 32.70 ? 31 GLN B N 1 ATOM 1342 C CA . GLN B 2 31 ? -6.062 -11.461 52.769 1.00 36.23 ? 31 GLN B CA 1 ATOM 1343 C C . GLN B 2 31 ? -6.566 -11.452 54.209 1.00 39.53 ? 31 GLN B C 1 ATOM 1344 O O . GLN B 2 31 ? -7.386 -12.293 54.588 1.00 37.38 ? 31 GLN B O 1 ATOM 1345 C CB . GLN B 2 31 ? -4.811 -12.334 52.714 1.00 39.64 ? 31 GLN B CB 1 ATOM 1346 C CG . GLN B 2 31 ? -4.335 -12.700 51.323 1.00 44.88 ? 31 GLN B CG 1 ATOM 1347 C CD . GLN B 2 31 ? -2.988 -13.384 51.357 1.00 49.01 ? 31 GLN B CD 1 ATOM 1348 O OE1 . GLN B 2 31 ? -2.449 -13.775 50.325 1.00 59.74 ? 31 GLN B OE1 1 ATOM 1349 N NE2 . GLN B 2 31 ? -2.432 -13.528 52.553 1.00 56.02 ? 31 GLN B NE2 1 ATOM 1350 N N . GLN B 2 32 ? -6.064 -10.514 55.010 1.00 35.81 ? 32 GLN B N 1 ATOM 1351 C CA . GLN B 2 32 ? -6.447 -10.417 56.420 1.00 37.73 ? 32 GLN B CA 1 ATOM 1352 C C . GLN B 2 32 ? -7.919 -10.111 56.691 1.00 37.82 ? 32 GLN B C 1 ATOM 1353 O O . GLN B 2 32 ? -8.450 -10.500 57.735 1.00 41.97 ? 32 GLN B O 1 ATOM 1354 C CB . GLN B 2 32 ? -5.601 -9.354 57.130 1.00 39.52 ? 32 GLN B CB 1 ATOM 1355 C CG . GLN B 2 32 ? -4.114 -9.522 56.956 1.00 40.55 ? 32 GLN B CG 1 ATOM 1356 C CD . GLN B 2 32 ? -3.627 -10.883 57.386 1.00 45.86 ? 32 GLN B CD 1 ATOM 1357 O OE1 . GLN B 2 32 ? -3.708 -11.241 58.559 1.00 48.39 ? 32 GLN B OE1 1 ATOM 1358 N NE2 . GLN B 2 32 ? -3.118 -11.654 56.437 1.00 49.84 ? 32 GLN B NE2 1 ATOM 1359 N N . HIS B 2 33 ? -8.588 -9.419 55.779 1.00 34.21 ? 33 HIS B N 1 ATOM 1360 C CA . HIS B 2 33 ? -9.980 -9.078 56.028 1.00 33.13 ? 33 HIS B CA 1 ATOM 1361 C C . HIS B 2 33 ? -10.601 -8.377 54.829 1.00 38.38 ? 33 HIS B C 1 ATOM 1362 O O . HIS B 2 33 ? -9.893 -7.819 53.992 1.00 35.94 ? 33 HIS B O 1 ATOM 1363 C CB . HIS B 2 33 ? -10.033 -8.166 57.261 1.00 40.19 ? 33 HIS B CB 1 ATOM 1364 C CG . HIS B 2 33 ? -11.404 -7.969 57.826 1.00 36.63 ? 33 HIS B CG 1 ATOM 1365 N ND1 . HIS B 2 33 ? -12.381 -7.241 57.182 1.00 39.08 ? 33 HIS B ND1 1 ATOM 1366 C CD2 . HIS B 2 33 ? -11.949 -8.379 58.995 1.00 38.36 ? 33 HIS B CD2 1 ATOM 1367 C CE1 . HIS B 2 33 ? -13.469 -7.210 57.931 1.00 39.05 ? 33 HIS B CE1 1 ATOM 1368 N NE2 . HIS B 2 33 ? -13.233 -7.893 59.036 1.00 37.96 ? 33 HIS B NE2 1 ATOM 1369 N N . LYS B 2 34 ? -11.926 -8.400 54.751 1.00 36.53 ? 34 LYS B N 1 ATOM 1370 C CA . LYS B 2 34 ? -12.626 -7.753 53.649 1.00 40.49 ? 34 LYS B CA 1 ATOM 1371 C C . LYS B 2 34 ? -12.448 -6.240 53.710 1.00 40.78 ? 34 LYS B C 1 ATOM 1372 O O . LYS B 2 34 ? -12.589 -5.635 54.773 1.00 44.06 ? 34 LYS B O 1 ATOM 1373 C CB . LYS B 2 34 ? -14.120 -8.100 53.679 1.00 42.11 ? 34 LYS B CB 1 ATOM 1374 C CG . LYS B 2 34 ? -14.892 -7.544 52.484 1.00 56.56 ? 34 LYS B CG 1 ATOM 1375 C CD . LYS B 2 34 ? -16.155 -8.348 52.164 1.00 61.52 ? 34 LYS B CD 1 ATOM 1376 C CE . LYS B 2 34 ? -17.238 -8.177 53.219 1.00 67.28 ? 34 LYS B CE 1 ATOM 1377 N NZ . LYS B 2 34 ? -18.503 -8.865 52.816 1.00 66.23 ? 34 LYS B NZ 1 ATOM 1378 N N . GLY B 2 35 ? -12.133 -5.636 52.566 1.00 37.62 ? 35 GLY B N 1 ATOM 1379 C CA . GLY B 2 35 ? -11.946 -4.197 52.510 1.00 34.42 ? 35 GLY B CA 1 ATOM 1380 C C . GLY B 2 35 ? -10.619 -3.705 53.070 1.00 30.56 ? 35 GLY B C 1 ATOM 1381 O O . GLY B 2 35 ? -10.406 -2.495 53.195 1.00 30.02 ? 35 GLY B O 1 ATOM 1382 N N . SER B 2 36 ? -9.727 -4.635 53.398 1.00 26.71 ? 36 SER B N 1 ATOM 1383 C CA . SER B 2 36 ? -8.412 -4.303 53.958 1.00 26.79 ? 36 SER B CA 1 ATOM 1384 C C . SER B 2 36 ? -7.335 -4.103 52.885 1.00 36.14 ? 36 SER B C 1 ATOM 1385 O O . SER B 2 36 ? -7.187 -4.916 51.969 1.00 28.32 ? 36 SER B O 1 ATOM 1386 C CB . SER B 2 36 ? -7.966 -5.416 54.909 1.00 27.20 ? 36 SER B CB 1 ATOM 1387 O OG . SER B 2 36 ? -6.639 -5.231 55.377 1.00 29.78 ? 36 SER B OG 1 ATOM 1388 N N . ARG B 2 37 ? -6.580 -3.015 53.006 1.00 30.91 ? 37 ARG B N 1 ATOM 1389 C CA . ARG B 2 37 ? -5.502 -2.711 52.065 1.00 29.82 ? 37 ARG B CA 1 ATOM 1390 C C . ARG B 2 37 ? -4.472 -1.907 52.842 1.00 30.82 ? 37 ARG B C 1 ATOM 1391 O O . ARG B 2 37 ? -4.704 -1.567 54.002 1.00 21.42 ? 37 ARG B O 1 ATOM 1392 C CB . ARG B 2 37 ? -6.020 -1.861 50.899 1.00 33.03 ? 37 ARG B CB 1 ATOM 1393 C CG . ARG B 2 37 ? -7.200 -2.457 50.135 1.00 39.68 ? 37 ARG B CG 1 ATOM 1394 C CD . ARG B 2 37 ? -7.721 -1.495 49.069 1.00 46.97 ? 37 ARG B CD 1 ATOM 1395 N NE . ARG B 2 37 ? -6.960 -1.587 47.827 1.00 52.08 ? 37 ARG B NE 1 ATOM 1396 C CZ . ARG B 2 37 ? -7.082 -2.580 46.952 1.00 53.80 ? 37 ARG B CZ 1 ATOM 1397 N NH1 . ARG B 2 37 ? -6.346 -2.591 45.852 1.00 56.24 ? 37 ARG B NH1 1 ATOM 1398 N NH2 . ARG B 2 37 ? -7.950 -3.555 47.169 1.00 58.79 ? 37 ARG B NH2 1 ATOM 1399 N N . LEU B 2 38 ? -3.331 -1.620 52.224 1.00 22.57 ? 38 LEU B N 1 ATOM 1400 C CA . LEU B 2 38 ? -2.318 -0.818 52.895 1.00 21.41 ? 38 LEU B CA 1 ATOM 1401 C C . LEU B 2 38 ? -3.037 0.489 53.224 1.00 20.13 ? 38 LEU B C 1 ATOM 1402 O O . LEU B 2 38 ? -3.834 0.984 52.431 1.00 19.69 ? 38 LEU B O 1 ATOM 1403 C CB . LEU B 2 38 ? -1.113 -0.595 51.965 1.00 19.91 ? 38 LEU B CB 1 ATOM 1404 C CG . LEU B 2 38 ? -0.143 -1.780 51.835 1.00 26.57 ? 38 LEU B CG 1 ATOM 1405 C CD1 . LEU B 2 38 ? 0.865 -1.540 50.691 1.00 25.73 ? 38 LEU B CD1 1 ATOM 1406 C CD2 . LEU B 2 38 ? 0.595 -1.986 53.162 1.00 25.25 ? 38 LEU B CD2 1 ATOM 1407 N N . ALA B 2 39 ? -2.761 1.051 54.394 1.00 19.90 ? 39 ALA B N 1 ATOM 1408 C CA . ALA B 2 39 ? -3.461 2.249 54.816 1.00 20.58 ? 39 ALA B CA 1 ATOM 1409 C C . ALA B 2 39 ? -3.247 3.538 54.056 1.00 21.95 ? 39 ALA B C 1 ATOM 1410 O O . ALA B 2 39 ? -2.116 3.944 53.788 1.00 24.51 ? 39 ALA B O 1 ATOM 1411 C CB . ALA B 2 39 ? -3.193 2.506 56.312 1.00 17.79 ? 39 ALA B CB 1 ATOM 1412 N N . SER B 2 40 ? -4.356 4.178 53.711 1.00 16.90 ? 40 SER B N 1 ATOM 1413 C CA . SER B 2 40 ? -4.295 5.491 53.096 1.00 18.16 ? 40 SER B CA 1 ATOM 1414 C C . SER B 2 40 ? -4.242 6.380 54.360 1.00 22.35 ? 40 SER B C 1 ATOM 1415 O O . SER B 2 40 ? -4.740 5.990 55.418 1.00 22.94 ? 40 SER B O 1 ATOM 1416 C CB . SER B 2 40 ? -5.560 5.766 52.269 1.00 25.08 ? 40 SER B CB 1 ATOM 1417 O OG . SER B 2 40 ? -6.747 5.529 53.012 1.00 28.02 ? 40 SER B OG 1 ATOM 1418 N N . ILE B 2 41 ? -3.620 7.546 54.265 1.00 20.11 ? 41 ILE B N 1 ATOM 1419 C CA . ILE B 2 41 ? -3.487 8.452 55.408 1.00 16.56 ? 41 ILE B CA 1 ATOM 1420 C C . ILE B 2 41 ? -4.106 9.775 54.969 1.00 21.40 ? 41 ILE B C 1 ATOM 1421 O O . ILE B 2 41 ? -3.515 10.523 54.189 1.00 20.19 ? 41 ILE B O 1 ATOM 1422 C CB . ILE B 2 41 ? -1.995 8.633 55.755 1.00 18.04 ? 41 ILE B CB 1 ATOM 1423 C CG1 . ILE B 2 41 ? -1.369 7.265 56.034 1.00 17.44 ? 41 ILE B CG1 1 ATOM 1424 C CG2 . ILE B 2 41 ? -1.827 9.562 56.952 1.00 13.63 ? 41 ILE B CG2 1 ATOM 1425 C CD1 . ILE B 2 41 ? -1.908 6.559 57.297 1.00 20.54 ? 41 ILE B CD1 1 ATOM 1426 N N . HIS B 2 42 ? -5.284 10.085 55.505 1.00 14.50 ? 42 HIS B N 1 ATOM 1427 C CA . HIS B 2 42 ? -6.010 11.263 55.079 1.00 15.17 ? 42 HIS B CA 1 ATOM 1428 C C . HIS B 2 42 ? -5.896 12.545 55.873 1.00 18.49 ? 42 HIS B C 1 ATOM 1429 O O . HIS B 2 42 ? -6.422 13.575 55.458 1.00 17.52 ? 42 HIS B O 1 ATOM 1430 C CB . HIS B 2 42 ? -7.489 10.895 54.925 1.00 23.06 ? 42 HIS B CB 1 ATOM 1431 C CG . HIS B 2 42 ? -7.748 9.872 53.861 1.00 29.47 ? 42 HIS B CG 1 ATOM 1432 N ND1 . HIS B 2 42 ? -8.591 8.797 54.049 1.00 31.54 ? 42 HIS B ND1 1 ATOM 1433 C CD2 . HIS B 2 42 ? -7.297 9.775 52.587 1.00 31.17 ? 42 HIS B CD2 1 ATOM 1434 C CE1 . HIS B 2 42 ? -8.646 8.083 52.939 1.00 33.62 ? 42 HIS B CE1 1 ATOM 1435 N NE2 . HIS B 2 42 ? -7.871 8.656 52.035 1.00 30.54 ? 42 HIS B NE2 1 ATOM 1436 N N . SER B 2 43 ? -5.224 12.510 57.010 1.00 15.60 ? 43 SER B N 1 ATOM 1437 C CA . SER B 2 43 ? -5.088 13.732 57.792 1.00 15.28 ? 43 SER B CA 1 ATOM 1438 C C . SER B 2 43 ? -3.957 13.563 58.785 1.00 15.27 ? 43 SER B C 1 ATOM 1439 O O . SER B 2 43 ? -3.485 12.451 59.008 1.00 16.97 ? 43 SER B O 1 ATOM 1440 C CB . SER B 2 43 ? -6.374 14.022 58.569 1.00 15.85 ? 43 SER B CB 1 ATOM 1441 O OG . SER B 2 43 ? -6.611 12.997 59.514 1.00 17.40 ? 43 SER B OG 1 ATOM 1442 N N . SER B 2 44 ? -3.528 14.659 59.402 1.00 17.33 ? 44 SER B N 1 ATOM 1443 C CA . SER B 2 44 ? -2.451 14.539 60.376 1.00 17.53 ? 44 SER B CA 1 ATOM 1444 C C . SER B 2 44 ? -2.939 13.764 61.595 1.00 19.54 ? 44 SER B C 1 ATOM 1445 O O . SER B 2 44 ? -2.149 13.101 62.269 1.00 16.76 ? 44 SER B O 1 ATOM 1446 C CB . SER B 2 44 ? -1.936 15.922 60.799 1.00 24.51 ? 44 SER B CB 1 ATOM 1447 O OG . SER B 2 44 ? -2.969 16.697 61.359 1.00 25.65 ? 44 SER B OG 1 ATOM 1448 N N . GLU B 2 45 ? -4.242 13.823 61.883 1.00 15.74 ? 45 GLU B N 1 ATOM 1449 C CA . GLU B 2 45 ? -4.761 13.095 63.036 1.00 16.68 ? 45 GLU B CA 1 ATOM 1450 C C . GLU B 2 45 ? -4.717 11.592 62.788 1.00 16.21 ? 45 GLU B C 1 ATOM 1451 O O . GLU B 2 45 ? -4.311 10.811 63.670 1.00 14.80 ? 45 GLU B O 1 ATOM 1452 C CB . GLU B 2 45 ? -6.196 13.532 63.371 1.00 24.50 ? 45 GLU B CB 1 ATOM 1453 C CG . GLU B 2 45 ? -6.322 14.957 63.906 1.00 25.71 ? 45 GLU B CG 1 ATOM 1454 C CD . GLU B 2 45 ? -6.275 16.022 62.825 1.00 25.47 ? 45 GLU B CD 1 ATOM 1455 O OE1 . GLU B 2 45 ? -6.432 15.698 61.627 1.00 21.66 ? 45 GLU B OE1 1 ATOM 1456 O OE2 . GLU B 2 45 ? -6.103 17.211 63.173 1.00 32.11 ? 45 GLU B OE2 1 ATOM 1457 N N . GLU B 2 46 ? -5.123 11.166 61.591 1.00 16.78 ? 46 GLU B N 1 ATOM 1458 C CA . GLU B 2 46 ? -5.064 9.743 61.299 1.00 14.42 ? 46 GLU B CA 1 ATOM 1459 C C . GLU B 2 46 ? -3.594 9.332 61.295 1.00 17.76 ? 46 GLU B C 1 ATOM 1460 O O . GLU B 2 46 ? -3.220 8.264 61.785 1.00 17.21 ? 46 GLU B O 1 ATOM 1461 C CB . GLU B 2 46 ? -5.691 9.429 59.929 1.00 16.62 ? 46 GLU B CB 1 ATOM 1462 C CG . GLU B 2 46 ? -5.576 7.952 59.542 1.00 16.71 ? 46 GLU B CG 1 ATOM 1463 C CD . GLU B 2 46 ? -6.390 7.587 58.305 1.00 18.35 ? 46 GLU B CD 1 ATOM 1464 O OE1 . GLU B 2 46 ? -6.680 8.484 57.484 1.00 20.43 ? 46 GLU B OE1 1 ATOM 1465 O OE2 . GLU B 2 46 ? -6.733 6.393 58.150 1.00 19.11 ? 46 GLU B OE2 1 ATOM 1466 N N . GLU B 2 47 ? -2.759 10.196 60.731 1.00 16.90 ? 47 GLU B N 1 ATOM 1467 C CA . GLU B 2 47 ? -1.336 9.919 60.658 1.00 13.67 ? 47 GLU B CA 1 ATOM 1468 C C . GLU B 2 47 ? -0.714 9.723 62.034 1.00 16.56 ? 47 GLU B C 1 ATOM 1469 O O . GLU B 2 47 ? 0.083 8.794 62.252 1.00 15.90 ? 47 GLU B O 1 ATOM 1470 C CB . GLU B 2 47 ? -0.626 11.061 59.918 1.00 16.11 ? 47 GLU B CB 1 ATOM 1471 C CG . GLU B 2 47 ? 0.878 10.883 59.796 1.00 15.10 ? 47 GLU B CG 1 ATOM 1472 C CD . GLU B 2 47 ? 1.512 12.024 59.027 1.00 20.35 ? 47 GLU B CD 1 ATOM 1473 O OE1 . GLU B 2 47 ? 1.352 13.184 59.454 1.00 23.47 ? 47 GLU B OE1 1 ATOM 1474 O OE2 . GLU B 2 47 ? 2.166 11.760 58.001 1.00 19.92 ? 47 GLU B OE2 1 ATOM 1475 N N . ALA B 2 48 ? -1.083 10.589 62.974 1.00 18.35 ? 48 ALA B N 1 ATOM 1476 C CA . ALA B 2 48 ? -0.528 10.512 64.321 1.00 19.41 ? 48 ALA B CA 1 ATOM 1477 C C . ALA B 2 48 ? -0.875 9.186 64.989 1.00 21.78 ? 48 ALA B C 1 ATOM 1478 O O . ALA B 2 48 ? -0.020 8.544 65.614 1.00 20.47 ? 48 ALA B O 1 ATOM 1479 C CB . ALA B 2 48 ? -1.041 11.691 65.166 1.00 20.15 ? 48 ALA B CB 1 ATOM 1480 N N . PHE B 2 49 ? -2.136 8.779 64.863 1.00 15.73 ? 49 PHE B N 1 ATOM 1481 C CA . PHE B 2 49 ? -2.585 7.531 65.460 1.00 18.74 ? 49 PHE B CA 1 ATOM 1482 C C . PHE B 2 49 ? -1.817 6.355 64.871 1.00 15.06 ? 49 PHE B C 1 ATOM 1483 O O . PHE B 2 49 ? -1.238 5.544 65.594 1.00 16.47 ? 49 PHE B O 1 ATOM 1484 C CB . PHE B 2 49 ? -4.071 7.325 65.194 1.00 19.27 ? 49 PHE B CB 1 ATOM 1485 C CG . PHE B 2 49 ? -4.560 5.974 65.595 1.00 19.60 ? 49 PHE B CG 1 ATOM 1486 C CD1 . PHE B 2 49 ? -4.808 5.682 66.937 1.00 21.51 ? 49 PHE B CD1 1 ATOM 1487 C CD2 . PHE B 2 49 ? -4.762 4.985 64.638 1.00 16.74 ? 49 PHE B CD2 1 ATOM 1488 C CE1 . PHE B 2 49 ? -5.257 4.415 67.321 1.00 25.54 ? 49 PHE B CE1 1 ATOM 1489 C CE2 . PHE B 2 49 ? -5.208 3.715 65.011 1.00 22.60 ? 49 PHE B CE2 1 ATOM 1490 C CZ . PHE B 2 49 ? -5.456 3.433 66.359 1.00 22.46 ? 49 PHE B CZ 1 ATOM 1491 N N . VAL B 2 50 ? -1.823 6.252 63.547 1.00 14.44 ? 50 VAL B N 1 ATOM 1492 C CA . VAL B 2 50 ? -1.100 5.163 62.907 1.00 16.02 ? 50 VAL B CA 1 ATOM 1493 C C . VAL B 2 50 ? 0.378 5.166 63.307 1.00 19.37 ? 50 VAL B C 1 ATOM 1494 O O . VAL B 2 50 ? 0.993 4.113 63.462 1.00 17.96 ? 50 VAL B O 1 ATOM 1495 C CB . VAL B 2 50 ? -1.231 5.251 61.376 1.00 19.57 ? 50 VAL B CB 1 ATOM 1496 C CG1 . VAL B 2 50 ? -0.330 4.218 60.708 1.00 20.18 ? 50 VAL B CG1 1 ATOM 1497 C CG2 . VAL B 2 50 ? -2.685 4.991 60.988 1.00 19.98 ? 50 VAL B CG2 1 ATOM 1498 N N . SER B 2 51 ? 0.958 6.347 63.480 1.00 20.06 ? 51 SER B N 1 ATOM 1499 C CA . SER B 2 51 ? 2.360 6.410 63.881 1.00 22.42 ? 51 SER B CA 1 ATOM 1500 C C . SER B 2 51 ? 2.616 5.838 65.271 1.00 22.29 ? 51 SER B C 1 ATOM 1501 O O . SER B 2 51 ? 3.572 5.077 65.465 1.00 20.29 ? 51 SER B O 1 ATOM 1502 C CB . SER B 2 51 ? 2.867 7.850 63.821 1.00 23.96 ? 51 SER B CB 1 ATOM 1503 O OG . SER B 2 51 ? 3.004 8.248 62.467 1.00 28.10 ? 51 SER B OG 1 ATOM 1504 N N . LYS B 2 52 ? 1.776 6.194 66.240 1.00 18.96 ? 52 LYS B N 1 ATOM 1505 C CA . LYS B 2 52 ? 1.960 5.690 67.598 1.00 24.85 ? 52 LYS B CA 1 ATOM 1506 C C . LYS B 2 52 ? 1.758 4.188 67.606 1.00 22.43 ? 52 LYS B C 1 ATOM 1507 O O . LYS B 2 52 ? 2.408 3.455 68.350 1.00 22.07 ? 52 LYS B O 1 ATOM 1508 C CB . LYS B 2 52 ? 0.967 6.325 68.569 1.00 25.68 ? 52 LYS B CB 1 ATOM 1509 C CG . LYS B 2 52 ? 1.141 7.807 68.803 1.00 39.25 ? 52 LYS B CG 1 ATOM 1510 C CD . LYS B 2 52 ? 0.084 8.282 69.794 1.00 42.14 ? 52 LYS B CD 1 ATOM 1511 C CE . LYS B 2 52 ? -0.180 9.768 69.679 1.00 47.67 ? 52 LYS B CE 1 ATOM 1512 N NZ . LYS B 2 52 ? -1.389 10.119 70.460 1.00 35.75 ? 52 LYS B NZ 1 ATOM 1513 N N . LEU B 2 53 ? 0.838 3.736 66.772 1.00 19.12 ? 53 LEU B N 1 ATOM 1514 C CA . LEU B 2 53 ? 0.553 2.317 66.666 1.00 22.21 ? 53 LEU B CA 1 ATOM 1515 C C . LEU B 2 53 ? 1.792 1.583 66.153 1.00 25.16 ? 53 LEU B C 1 ATOM 1516 O O . LEU B 2 53 ? 2.168 0.520 66.662 1.00 22.89 ? 53 LEU B O 1 ATOM 1517 C CB . LEU B 2 53 ? -0.615 2.100 65.704 1.00 21.56 ? 53 LEU B CB 1 ATOM 1518 C CG . LEU B 2 53 ? -1.198 0.692 65.682 1.00 22.85 ? 53 LEU B CG 1 ATOM 1519 C CD1 . LEU B 2 53 ? -1.721 0.325 67.084 1.00 20.35 ? 53 LEU B CD1 1 ATOM 1520 C CD2 . LEU B 2 53 ? -2.317 0.636 64.649 1.00 23.87 ? 53 LEU B CD2 1 ATOM 1521 N N . ALA B 2 54 ? 2.433 2.161 65.145 1.00 23.41 ? 54 ALA B N 1 ATOM 1522 C CA . ALA B 2 54 ? 3.622 1.559 64.558 1.00 22.48 ? 54 ALA B CA 1 ATOM 1523 C C . ALA B 2 54 ? 4.773 1.507 65.551 1.00 25.80 ? 54 ALA B C 1 ATOM 1524 O O . ALA B 2 54 ? 5.527 0.541 65.582 1.00 27.28 ? 54 ALA B O 1 ATOM 1525 C CB . ALA B 2 54 ? 4.047 2.348 63.327 1.00 29.51 ? 54 ALA B CB 1 ATOM 1526 N N . SER B 2 55 ? 4.917 2.555 66.351 1.00 21.93 ? 55 SER B N 1 ATOM 1527 C CA . SER B 2 55 ? 5.994 2.603 67.332 1.00 22.28 ? 55 SER B CA 1 ATOM 1528 C C . SER B 2 55 ? 5.931 1.454 68.321 1.00 23.55 ? 55 SER B C 1 ATOM 1529 O O . SER B 2 55 ? 6.960 1.020 68.842 1.00 26.58 ? 55 SER B O 1 ATOM 1530 C CB . SER B 2 55 ? 5.970 3.931 68.090 1.00 26.52 ? 55 SER B CB 1 ATOM 1531 O OG . SER B 2 55 ? 6.379 4.994 67.246 1.00 29.40 ? 55 SER B OG 1 ATOM 1532 N N . LYS B 2 56 ? 4.729 0.960 68.586 1.00 23.86 ? 56 LYS B N 1 ATOM 1533 C CA . LYS B 2 56 ? 4.566 -0.156 69.519 1.00 24.19 ? 56 LYS B CA 1 ATOM 1534 C C . LYS B 2 56 ? 4.950 -1.471 68.853 1.00 27.43 ? 56 LYS B C 1 ATOM 1535 O O . LYS B 2 56 ? 5.459 -2.378 69.499 1.00 25.00 ? 56 LYS B O 1 ATOM 1536 C CB . LYS B 2 56 ? 3.111 -0.250 69.980 1.00 24.84 ? 56 LYS B CB 1 ATOM 1537 C CG . LYS B 2 56 ? 2.594 1.013 70.651 1.00 26.83 ? 56 LYS B CG 1 ATOM 1538 C CD . LYS B 2 56 ? 1.183 0.808 71.196 1.00 34.15 ? 56 LYS B CD 1 ATOM 1539 C CE . LYS B 2 56 ? 1.190 -0.149 72.360 1.00 35.60 ? 56 LYS B CE 1 ATOM 1540 N NZ . LYS B 2 56 ? -0.199 -0.373 72.849 1.00 45.21 ? 56 LYS B NZ 1 ATOM 1541 N N . ALA B 2 57 ? 4.712 -1.563 67.548 1.00 25.15 ? 57 ALA B N 1 ATOM 1542 C CA . ALA B 2 57 ? 4.997 -2.793 66.820 1.00 29.21 ? 57 ALA B CA 1 ATOM 1543 C C . ALA B 2 57 ? 6.347 -2.889 66.115 1.00 31.65 ? 57 ALA B C 1 ATOM 1544 O O . ALA B 2 57 ? 6.822 -3.992 65.858 1.00 30.33 ? 57 ALA B O 1 ATOM 1545 C CB . ALA B 2 57 ? 3.879 -3.053 65.809 1.00 29.20 ? 57 ALA B CB 1 ATOM 1546 N N . LEU B 2 58 ? 6.971 -1.756 65.811 1.00 26.74 ? 58 LEU B N 1 ATOM 1547 C CA . LEU B 2 58 ? 8.232 -1.777 65.068 1.00 30.50 ? 58 LEU B CA 1 ATOM 1548 C C . LEU B 2 58 ? 9.446 -1.173 65.767 1.00 33.15 ? 58 LEU B C 1 ATOM 1549 O O . LEU B 2 58 ? 9.376 -0.068 66.292 1.00 34.04 ? 58 LEU B O 1 ATOM 1550 C CB . LEU B 2 58 ? 8.038 -1.046 63.732 1.00 23.65 ? 58 LEU B CB 1 ATOM 1551 C CG . LEU B 2 58 ? 6.771 -1.333 62.925 1.00 25.47 ? 58 LEU B CG 1 ATOM 1552 C CD1 . LEU B 2 58 ? 6.724 -0.422 61.683 1.00 26.72 ? 58 LEU B CD1 1 ATOM 1553 C CD2 . LEU B 2 58 ? 6.749 -2.795 62.520 1.00 27.54 ? 58 LEU B CD2 1 ATOM 1554 N N . LYS B 2 59 ? 10.562 -1.900 65.767 1.00 35.65 ? 59 LYS B N 1 ATOM 1555 C CA . LYS B 2 59 ? 11.791 -1.380 66.355 1.00 34.63 ? 59 LYS B CA 1 ATOM 1556 C C . LYS B 2 59 ? 12.282 -0.295 65.388 1.00 34.00 ? 59 LYS B C 1 ATOM 1557 O O . LYS B 2 59 ? 12.700 0.789 65.810 1.00 34.20 ? 59 LYS B O 1 ATOM 1558 C CB . LYS B 2 59 ? 12.846 -2.480 66.477 1.00 39.55 ? 59 LYS B CB 1 ATOM 1559 C CG . LYS B 2 59 ? 14.193 -1.973 66.989 1.00 51.49 ? 59 LYS B CG 1 ATOM 1560 C CD . LYS B 2 59 ? 15.240 -3.083 67.001 1.00 57.99 ? 59 LYS B CD 1 ATOM 1561 C CE . LYS B 2 59 ? 16.582 -2.584 67.525 1.00 60.53 ? 59 LYS B CE 1 ATOM 1562 N NZ . LYS B 2 59 ? 17.630 -3.643 67.441 1.00 62.99 ? 59 LYS B NZ 1 ATOM 1563 N N . PHE B 2 60 ? 12.238 -0.604 64.091 1.00 30.87 ? 60 PHE B N 1 ATOM 1564 C CA . PHE B 2 60 ? 12.626 0.356 63.047 1.00 28.82 ? 60 PHE B CA 1 ATOM 1565 C C . PHE B 2 60 ? 11.294 0.832 62.467 1.00 21.32 ? 60 PHE B C 1 ATOM 1566 O O . PHE B 2 60 ? 10.687 0.174 61.621 1.00 20.33 ? 60 PHE B O 1 ATOM 1567 C CB . PHE B 2 60 ? 13.492 -0.320 61.983 1.00 36.09 ? 60 PHE B CB 1 ATOM 1568 C CG . PHE B 2 60 ? 14.736 -0.942 62.540 1.00 41.25 ? 60 PHE B CG 1 ATOM 1569 C CD1 . PHE B 2 60 ? 14.760 -2.286 62.891 1.00 48.30 ? 60 PHE B CD1 1 ATOM 1570 C CD2 . PHE B 2 60 ? 15.864 -0.167 62.787 1.00 48.58 ? 60 PHE B CD2 1 ATOM 1571 C CE1 . PHE B 2 60 ? 15.887 -2.848 63.486 1.00 54.23 ? 60 PHE B CE1 1 ATOM 1572 C CE2 . PHE B 2 60 ? 16.997 -0.719 63.383 1.00 50.21 ? 60 PHE B CE2 1 ATOM 1573 C CZ . PHE B 2 60 ? 17.008 -2.060 63.733 1.00 55.35 ? 60 PHE B CZ 1 ATOM 1574 N N . THR B 2 61 ? 10.848 1.987 62.939 1.00 24.73 ? 61 THR B N 1 ATOM 1575 C CA . THR B 2 61 ? 9.547 2.497 62.555 1.00 25.23 ? 61 THR B CA 1 ATOM 1576 C C . THR B 2 61 ? 9.361 3.146 61.196 1.00 25.63 ? 61 THR B C 1 ATOM 1577 O O . THR B 2 61 ? 9.112 4.348 61.092 1.00 25.16 ? 61 THR B O 1 ATOM 1578 C CB . THR B 2 61 ? 9.016 3.448 63.628 1.00 28.94 ? 61 THR B CB 1 ATOM 1579 O OG1 . THR B 2 61 ? 9.370 2.945 64.920 1.00 33.88 ? 61 THR B OG1 1 ATOM 1580 C CG2 . THR B 2 61 ? 7.490 3.527 63.543 1.00 26.85 ? 61 THR B CG2 1 ATOM 1581 N N . SER B 2 62 ? 9.472 2.329 60.158 1.00 22.85 ? 62 SER B N 1 ATOM 1582 C CA . SER B 2 62 ? 9.258 2.773 58.791 1.00 21.34 ? 62 SER B CA 1 ATOM 1583 C C . SER B 2 62 ? 8.252 1.774 58.236 1.00 22.71 ? 62 SER B C 1 ATOM 1584 O O . SER B 2 62 ? 8.360 0.571 58.503 1.00 24.52 ? 62 SER B O 1 ATOM 1585 C CB . SER B 2 62 ? 10.569 2.722 58.002 1.00 21.45 ? 62 SER B CB 1 ATOM 1586 O OG . SER B 2 62 ? 11.448 3.714 58.494 1.00 26.86 ? 62 SER B OG 1 ATOM 1587 N N . MET B 2 63 ? 7.267 2.247 57.477 1.00 17.98 ? 63 MET B N 1 ATOM 1588 C CA . MET B 2 63 ? 6.264 1.325 56.949 1.00 18.67 ? 63 MET B CA 1 ATOM 1589 C C . MET B 2 63 ? 5.648 1.770 55.641 1.00 18.18 ? 63 MET B C 1 ATOM 1590 O O . MET B 2 63 ? 5.488 2.959 55.391 1.00 21.72 ? 63 MET B O 1 ATOM 1591 C CB . MET B 2 63 ? 5.125 1.156 57.972 1.00 22.15 ? 63 MET B CB 1 ATOM 1592 C CG . MET B 2 63 ? 4.204 2.373 58.054 1.00 25.10 ? 63 MET B CG 1 ATOM 1593 S SD . MET B 2 63 ? 3.400 2.637 59.695 1.00 29.36 ? 63 MET B SD 1 ATOM 1594 C CE . MET B 2 63 ? 4.683 3.638 60.461 1.00 28.08 ? 63 MET B CE 1 ATOM 1595 N N . TRP B 2 64 ? 5.300 0.805 54.798 1.00 19.22 ? 64 TRP B N 1 ATOM 1596 C CA . TRP B 2 64 ? 4.637 1.128 53.548 1.00 18.04 ? 64 TRP B CA 1 ATOM 1597 C C . TRP B 2 64 ? 3.239 1.652 53.871 1.00 22.47 ? 64 TRP B C 1 ATOM 1598 O O . TRP B 2 64 ? 2.592 1.161 54.807 1.00 18.94 ? 64 TRP B O 1 ATOM 1599 C CB . TRP B 2 64 ? 4.407 -0.124 52.690 1.00 22.55 ? 64 TRP B CB 1 ATOM 1600 C CG . TRP B 2 64 ? 5.577 -0.774 52.018 1.00 30.44 ? 64 TRP B CG 1 ATOM 1601 C CD1 . TRP B 2 64 ? 5.917 -2.102 52.082 1.00 26.01 ? 64 TRP B CD1 1 ATOM 1602 C CD2 . TRP B 2 64 ? 6.487 -0.173 51.081 1.00 26.96 ? 64 TRP B CD2 1 ATOM 1603 N NE1 . TRP B 2 64 ? 6.976 -2.362 51.238 1.00 27.73 ? 64 TRP B NE1 1 ATOM 1604 C CE2 . TRP B 2 64 ? 7.346 -1.197 50.616 1.00 22.45 ? 64 TRP B CE2 1 ATOM 1605 C CE3 . TRP B 2 64 ? 6.658 1.130 50.587 1.00 24.04 ? 64 TRP B CE3 1 ATOM 1606 C CZ2 . TRP B 2 64 ? 8.370 -0.959 49.680 1.00 20.03 ? 64 TRP B CZ2 1 ATOM 1607 C CZ3 . TRP B 2 64 ? 7.677 1.369 49.652 1.00 22.54 ? 64 TRP B CZ3 1 ATOM 1608 C CH2 . TRP B 2 64 ? 8.518 0.325 49.212 1.00 28.68 ? 64 TRP B CH2 1 ATOM 1609 N N . ILE B 2 65 ? 2.787 2.668 53.139 1.00 16.65 ? 65 ILE B N 1 ATOM 1610 C CA . ILE B 2 65 ? 1.411 3.108 53.270 1.00 15.99 ? 65 ILE B CA 1 ATOM 1611 C C . ILE B 2 65 ? 0.801 2.924 51.866 1.00 17.67 ? 65 ILE B C 1 ATOM 1612 O O . ILE B 2 65 ? 1.513 2.528 50.947 1.00 20.47 ? 65 ILE B O 1 ATOM 1613 C CB . ILE B 2 65 ? 1.250 4.538 53.817 1.00 15.12 ? 65 ILE B CB 1 ATOM 1614 C CG1 . ILE B 2 65 ? 2.097 5.544 53.036 1.00 18.35 ? 65 ILE B CG1 1 ATOM 1615 C CG2 . ILE B 2 65 ? 1.579 4.512 55.321 1.00 13.90 ? 65 ILE B CG2 1 ATOM 1616 C CD1 . ILE B 2 65 ? 1.771 7.002 53.437 1.00 16.16 ? 65 ILE B CD1 1 ATOM 1617 N N . GLY B 2 66 ? -0.486 3.207 51.693 1.00 18.27 ? 66 GLY B N 1 ATOM 1618 C CA . GLY B 2 66 ? -1.144 2.940 50.421 1.00 19.77 ? 66 GLY B CA 1 ATOM 1619 C C . GLY B 2 66 ? -0.917 3.783 49.182 1.00 21.46 ? 66 GLY B C 1 ATOM 1620 O O . GLY B 2 66 ? -1.781 3.835 48.309 1.00 23.57 ? 66 GLY B O 1 ATOM 1621 N N . LEU B 2 67 ? 0.236 4.422 49.072 1.00 22.78 ? 67 LEU B N 1 ATOM 1622 C CA . LEU B 2 67 ? 0.485 5.250 47.903 1.00 24.78 ? 67 LEU B CA 1 ATOM 1623 C C . LEU B 2 67 ? 1.565 4.652 47.008 1.00 22.94 ? 67 LEU B C 1 ATOM 1624 O O . LEU B 2 67 ? 2.764 4.827 47.261 1.00 23.37 ? 67 LEU B O 1 ATOM 1625 C CB . LEU B 2 67 ? 0.876 6.655 48.365 1.00 28.23 ? 67 LEU B CB 1 ATOM 1626 C CG . LEU B 2 67 ? 0.574 7.862 47.473 1.00 37.13 ? 67 LEU B CG 1 ATOM 1627 C CD1 . LEU B 2 67 ? 1.009 9.126 48.181 1.00 42.21 ? 67 LEU B CD1 1 ATOM 1628 C CD2 . LEU B 2 67 ? 1.277 7.729 46.152 1.00 39.15 ? 67 LEU B CD2 1 ATOM 1629 N N . ASN B 2 68 ? 1.139 3.915 45.980 1.00 22.72 ? 68 ASN B N 1 ATOM 1630 C CA . ASN B 2 68 ? 2.067 3.319 45.014 1.00 24.34 ? 68 ASN B CA 1 ATOM 1631 C C . ASN B 2 68 ? 2.147 4.290 43.840 1.00 23.95 ? 68 ASN B C 1 ATOM 1632 O O . ASN B 2 68 ? 1.136 4.757 43.333 1.00 25.69 ? 68 ASN B O 1 ATOM 1633 C CB . ASN B 2 68 ? 1.573 1.952 44.506 1.00 30.59 ? 68 ASN B CB 1 ATOM 1634 C CG . ASN B 2 68 ? 2.455 1.380 43.379 1.00 44.09 ? 68 ASN B CG 1 ATOM 1635 O OD1 . ASN B 2 68 ? 2.707 2.046 42.366 1.00 43.55 ? 68 ASN B OD1 1 ATOM 1636 N ND2 . ASN B 2 68 ? 2.913 0.136 43.550 1.00 39.28 ? 68 ASN B ND2 1 ATOM 1637 N N . ASN B 2 69 ? 3.369 4.594 43.433 1.00 23.63 ? 69 ASN B N 1 ATOM 1638 C CA . ASN B 2 69 ? 3.642 5.509 42.339 1.00 17.12 ? 69 ASN B CA 1 ATOM 1639 C C . ASN B 2 69 ? 3.081 6.919 42.428 1.00 19.52 ? 69 ASN B C 1 ATOM 1640 O O . ASN B 2 69 ? 2.074 7.267 41.799 1.00 19.73 ? 69 ASN B O 1 ATOM 1641 C CB . ASN B 2 69 ? 3.230 4.905 40.999 1.00 26.43 ? 69 ASN B CB 1 ATOM 1642 C CG . ASN B 2 69 ? 3.828 5.669 39.823 1.00 32.21 ? 69 ASN B CG 1 ATOM 1643 O OD1 . ASN B 2 69 ? 4.813 6.400 39.985 1.00 32.46 ? 69 ASN B OD1 1 ATOM 1644 N ND2 . ASN B 2 69 ? 3.250 5.495 38.638 1.00 30.86 ? 69 ASN B ND2 1 ATOM 1645 N N . PRO B 2 70 ? 3.758 7.779 43.186 1.00 21.87 ? 70 PRO B N 1 ATOM 1646 C CA . PRO B 2 70 ? 3.239 9.142 43.276 1.00 19.03 ? 70 PRO B CA 1 ATOM 1647 C C . PRO B 2 70 ? 3.307 9.880 41.931 1.00 21.29 ? 70 PRO B C 1 ATOM 1648 O O . PRO B 2 70 ? 2.669 10.909 41.745 1.00 16.57 ? 70 PRO B O 1 ATOM 1649 C CB . PRO B 2 70 ? 4.124 9.778 44.358 1.00 22.51 ? 70 PRO B CB 1 ATOM 1650 C CG . PRO B 2 70 ? 5.361 8.927 44.383 1.00 26.93 ? 70 PRO B CG 1 ATOM 1651 C CD . PRO B 2 70 ? 4.836 7.539 44.163 1.00 22.65 ? 70 PRO B CD 1 ATOM 1652 N N . TRP B 2 71 ? 4.077 9.337 40.994 1.00 19.52 ? 71 TRP B N 1 ATOM 1653 C CA . TRP B 2 71 ? 4.231 9.967 39.689 1.00 23.37 ? 71 TRP B CA 1 ATOM 1654 C C . TRP B 2 71 ? 3.462 9.266 38.582 1.00 25.95 ? 71 TRP B C 1 ATOM 1655 O O . TRP B 2 71 ? 3.923 9.150 37.444 1.00 24.19 ? 71 TRP B O 1 ATOM 1656 C CB . TRP B 2 71 ? 5.717 10.074 39.362 1.00 22.24 ? 71 TRP B CB 1 ATOM 1657 C CG . TRP B 2 71 ? 6.393 10.846 40.441 1.00 19.17 ? 71 TRP B CG 1 ATOM 1658 C CD1 . TRP B 2 71 ? 6.166 12.160 40.762 1.00 23.37 ? 71 TRP B CD1 1 ATOM 1659 C CD2 . TRP B 2 71 ? 7.303 10.346 41.419 1.00 17.52 ? 71 TRP B CD2 1 ATOM 1660 N NE1 . TRP B 2 71 ? 6.874 12.500 41.884 1.00 18.18 ? 71 TRP B NE1 1 ATOM 1661 C CE2 . TRP B 2 71 ? 7.581 11.407 42.310 1.00 17.18 ? 71 TRP B CE2 1 ATOM 1662 C CE3 . TRP B 2 71 ? 7.914 9.102 41.635 1.00 19.02 ? 71 TRP B CE3 1 ATOM 1663 C CZ2 . TRP B 2 71 ? 8.442 11.262 43.407 1.00 20.18 ? 71 TRP B CZ2 1 ATOM 1664 C CZ3 . TRP B 2 71 ? 8.770 8.960 42.721 1.00 18.60 ? 71 TRP B CZ3 1 ATOM 1665 C CH2 . TRP B 2 71 ? 9.025 10.035 43.594 1.00 21.62 ? 71 TRP B CH2 1 ATOM 1666 N N . LYS B 2 72 ? 2.277 8.788 38.939 1.00 24.81 ? 72 LYS B N 1 ATOM 1667 C CA . LYS B 2 72 ? 1.392 8.155 37.983 1.00 25.80 ? 72 LYS B CA 1 ATOM 1668 C C . LYS B 2 72 ? 0.571 9.300 37.388 1.00 23.85 ? 72 LYS B C 1 ATOM 1669 O O . LYS B 2 72 ? 0.095 10.173 38.113 1.00 24.42 ? 72 LYS B O 1 ATOM 1670 C CB . LYS B 2 72 ? 0.468 7.171 38.698 1.00 29.34 ? 72 LYS B CB 1 ATOM 1671 C CG . LYS B 2 72 ? -0.595 6.554 37.804 1.00 35.03 ? 72 LYS B CG 1 ATOM 1672 C CD . LYS B 2 72 ? -1.602 5.770 38.632 1.00 37.55 ? 72 LYS B CD 1 ATOM 1673 C CE . LYS B 2 72 ? -2.728 5.228 37.761 1.00 46.79 ? 72 LYS B CE 1 ATOM 1674 N NZ . LYS B 2 72 ? -3.760 4.517 38.573 1.00 44.75 ? 72 LYS B NZ 1 ATOM 1675 N N . ASP B 2 73 ? 0.433 9.314 36.066 1.00 27.78 ? 73 ASP B N 1 ATOM 1676 C CA . ASP B 2 73 ? -0.348 10.345 35.386 1.00 28.15 ? 73 ASP B CA 1 ATOM 1677 C C . ASP B 2 73 ? 0.181 11.775 35.492 1.00 26.69 ? 73 ASP B C 1 ATOM 1678 O O . ASP B 2 73 ? -0.602 12.722 35.588 1.00 25.70 ? 73 ASP B O 1 ATOM 1679 C CB . ASP B 2 73 ? -1.798 10.312 35.884 1.00 39.63 ? 73 ASP B CB 1 ATOM 1680 C CG . ASP B 2 73 ? -2.535 9.045 35.462 1.00 46.14 ? 73 ASP B CG 1 ATOM 1681 O OD1 . ASP B 2 73 ? -3.650 8.812 35.972 1.00 50.75 ? 73 ASP B OD1 1 ATOM 1682 O OD2 . ASP B 2 73 ? -2.005 8.289 34.617 1.00 47.85 ? 73 ASP B OD2 1 ATOM 1683 N N . CYS B 2 74 ? 1.497 11.948 35.501 1.00 22.81 ? 74 CYS B N 1 ATOM 1684 C CA . CYS B 2 74 ? 2.036 13.305 35.529 1.00 26.42 ? 74 CYS B CA 1 ATOM 1685 C C . CYS B 2 74 ? 1.841 13.888 34.129 1.00 27.98 ? 74 CYS B C 1 ATOM 1686 O O . CYS B 2 74 ? 1.613 13.154 33.170 1.00 23.88 ? 74 CYS B O 1 ATOM 1687 C CB . CYS B 2 74 ? 3.531 13.311 35.828 1.00 27.25 ? 74 CYS B CB 1 ATOM 1688 S SG . CYS B 2 74 ? 3.986 12.749 37.488 1.00 26.49 ? 74 CYS B SG 1 ATOM 1689 N N . LYS B 2 75 ? 1.941 15.205 34.023 1.00 26.33 ? 75 LYS B N 1 ATOM 1690 C CA . LYS B 2 75 ? 1.816 15.901 32.750 1.00 28.45 ? 75 LYS B CA 1 ATOM 1691 C C . LYS B 2 75 ? 3.121 16.680 32.579 1.00 25.58 ? 75 LYS B C 1 ATOM 1692 O O . LYS B 2 75 ? 3.229 17.826 33.008 1.00 22.11 ? 75 LYS B O 1 ATOM 1693 C CB . LYS B 2 75 ? 0.627 16.857 32.805 1.00 29.59 ? 75 LYS B CB 1 ATOM 1694 C CG . LYS B 2 75 ? 0.327 17.590 31.514 1.00 36.81 ? 75 LYS B CG 1 ATOM 1695 C CD . LYS B 2 75 ? -0.951 18.395 31.662 1.00 44.36 ? 75 LYS B CD 1 ATOM 1696 C CE . LYS B 2 75 ? -1.282 19.172 30.398 1.00 52.24 ? 75 LYS B CE 1 ATOM 1697 N NZ . LYS B 2 75 ? -0.254 20.209 30.119 1.00 56.13 ? 75 LYS B NZ 1 ATOM 1698 N N . TRP B 2 76 ? 4.119 16.042 31.979 1.00 23.74 ? 76 TRP B N 1 ATOM 1699 C CA . TRP B 2 76 ? 5.411 16.694 31.780 1.00 25.46 ? 76 TRP B CA 1 ATOM 1700 C C . TRP B 2 76 ? 5.357 17.692 30.626 1.00 23.99 ? 76 TRP B C 1 ATOM 1701 O O . TRP B 2 76 ? 4.907 17.365 29.530 1.00 25.72 ? 76 TRP B O 1 ATOM 1702 C CB . TRP B 2 76 ? 6.498 15.642 31.517 1.00 23.67 ? 76 TRP B CB 1 ATOM 1703 C CG . TRP B 2 76 ? 6.595 14.588 32.600 1.00 22.59 ? 76 TRP B CG 1 ATOM 1704 C CD1 . TRP B 2 76 ? 6.293 13.254 32.482 1.00 28.79 ? 76 TRP B CD1 1 ATOM 1705 C CD2 . TRP B 2 76 ? 6.997 14.785 33.965 1.00 19.67 ? 76 TRP B CD2 1 ATOM 1706 N NE1 . TRP B 2 76 ? 6.484 12.614 33.690 1.00 24.23 ? 76 TRP B NE1 1 ATOM 1707 C CE2 . TRP B 2 76 ? 6.917 13.531 34.614 1.00 20.90 ? 76 TRP B CE2 1 ATOM 1708 C CE3 . TRP B 2 76 ? 7.417 15.899 34.702 1.00 19.03 ? 76 TRP B CE3 1 ATOM 1709 C CZ2 . TRP B 2 76 ? 7.240 13.365 35.959 1.00 21.03 ? 76 TRP B CZ2 1 ATOM 1710 C CZ3 . TRP B 2 76 ? 7.736 15.731 36.043 1.00 15.77 ? 76 TRP B CZ3 1 ATOM 1711 C CH2 . TRP B 2 76 ? 7.649 14.475 36.658 1.00 19.41 ? 76 TRP B CH2 1 ATOM 1712 N N . GLU B 2 77 ? 5.812 18.912 30.883 1.00 21.35 ? 77 GLU B N 1 ATOM 1713 C CA . GLU B 2 77 ? 5.834 19.958 29.864 1.00 21.75 ? 77 GLU B CA 1 ATOM 1714 C C . GLU B 2 77 ? 7.188 20.661 29.801 1.00 22.42 ? 77 GLU B C 1 ATOM 1715 O O . GLU B 2 77 ? 7.859 20.824 30.824 1.00 21.10 ? 77 GLU B O 1 ATOM 1716 C CB . GLU B 2 77 ? 4.774 21.014 30.166 1.00 25.79 ? 77 GLU B CB 1 ATOM 1717 C CG . GLU B 2 77 ? 3.365 20.490 30.208 1.00 23.69 ? 77 GLU B CG 1 ATOM 1718 C CD . GLU B 2 77 ? 2.364 21.609 30.382 1.00 28.97 ? 77 GLU B CD 1 ATOM 1719 O OE1 . GLU B 2 77 ? 1.753 21.697 31.466 1.00 26.30 ? 77 GLU B OE1 1 ATOM 1720 O OE2 . GLU B 2 77 ? 2.202 22.405 29.433 1.00 24.47 ? 77 GLU B OE2 1 ATOM 1721 N N . TRP B 2 78 ? 7.579 21.085 28.603 1.00 20.61 ? 78 TRP B N 1 ATOM 1722 C CA . TRP B 2 78 ? 8.837 21.806 28.419 1.00 20.00 ? 78 TRP B CA 1 ATOM 1723 C C . TRP B 2 78 ? 8.575 23.301 28.664 1.00 20.03 ? 78 TRP B C 1 ATOM 1724 O O . TRP B 2 78 ? 7.557 23.838 28.216 1.00 22.82 ? 78 TRP B O 1 ATOM 1725 C CB . TRP B 2 78 ? 9.363 21.625 26.976 1.00 17.83 ? 78 TRP B CB 1 ATOM 1726 C CG . TRP B 2 78 ? 9.795 20.228 26.625 1.00 18.91 ? 78 TRP B CG 1 ATOM 1727 C CD1 . TRP B 2 78 ? 9.204 19.380 25.720 1.00 23.06 ? 78 TRP B CD1 1 ATOM 1728 C CD2 . TRP B 2 78 ? 10.914 19.516 27.168 1.00 17.61 ? 78 TRP B CD2 1 ATOM 1729 N NE1 . TRP B 2 78 ? 9.893 18.189 25.670 1.00 22.70 ? 78 TRP B NE1 1 ATOM 1730 C CE2 . TRP B 2 78 ? 10.944 18.244 26.549 1.00 20.80 ? 78 TRP B CE2 1 ATOM 1731 C CE3 . TRP B 2 78 ? 11.891 19.827 28.124 1.00 23.20 ? 78 TRP B CE3 1 ATOM 1732 C CZ2 . TRP B 2 78 ? 11.914 17.284 26.854 1.00 21.01 ? 78 TRP B CZ2 1 ATOM 1733 C CZ3 . TRP B 2 78 ? 12.863 18.867 28.432 1.00 17.46 ? 78 TRP B CZ3 1 ATOM 1734 C CH2 . TRP B 2 78 ? 12.863 17.609 27.793 1.00 20.93 ? 78 TRP B CH2 1 ATOM 1735 N N . SER B 2 79 ? 9.491 23.984 29.346 1.00 19.18 ? 79 SER B N 1 ATOM 1736 C CA . SER B 2 79 ? 9.302 25.413 29.600 1.00 17.97 ? 79 SER B CA 1 ATOM 1737 C C . SER B 2 79 ? 9.252 26.237 28.303 1.00 22.41 ? 79 SER B C 1 ATOM 1738 O O . SER B 2 79 ? 8.726 27.355 28.299 1.00 20.15 ? 79 SER B O 1 ATOM 1739 C CB . SER B 2 79 ? 10.416 25.963 30.505 1.00 18.66 ? 79 SER B CB 1 ATOM 1740 O OG . SER B 2 79 ? 11.689 25.841 29.894 1.00 19.05 ? 79 SER B OG 1 ATOM 1741 N N . ASP B 2 80 ? 9.801 25.714 27.208 1.00 19.89 ? 80 ASP B N 1 ATOM 1742 C CA . ASP B 2 80 ? 9.738 26.476 25.959 1.00 18.69 ? 80 ASP B CA 1 ATOM 1743 C C . ASP B 2 80 ? 8.479 26.083 25.177 1.00 25.69 ? 80 ASP B C 1 ATOM 1744 O O . ASP B 2 80 ? 8.272 26.503 24.043 1.00 22.65 ? 80 ASP B O 1 ATOM 1745 C CB . ASP B 2 80 ? 10.997 26.266 25.099 1.00 16.49 ? 80 ASP B CB 1 ATOM 1746 C CG . ASP B 2 80 ? 11.194 24.822 24.662 1.00 21.28 ? 80 ASP B CG 1 ATOM 1747 O OD1 . ASP B 2 80 ? 10.256 23.992 24.774 1.00 23.17 ? 80 ASP B OD1 1 ATOM 1748 O OD2 . ASP B 2 80 ? 12.306 24.519 24.183 1.00 25.48 ? 80 ASP B OD2 1 ATOM 1749 N N . ASN B 2 81 ? 7.650 25.266 25.813 1.00 23.23 ? 81 ASN B N 1 ATOM 1750 C CA . ASN B 2 81 ? 6.391 24.784 25.259 1.00 27.77 ? 81 ASN B CA 1 ATOM 1751 C C . ASN B 2 81 ? 6.461 23.910 24.021 1.00 27.92 ? 81 ASN B C 1 ATOM 1752 O O . ASN B 2 81 ? 5.466 23.751 23.317 1.00 30.38 ? 81 ASN B O 1 ATOM 1753 C CB . ASN B 2 81 ? 5.432 25.953 25.024 1.00 27.48 ? 81 ASN B CB 1 ATOM 1754 C CG . ASN B 2 81 ? 4.861 26.489 26.322 1.00 28.23 ? 81 ASN B CG 1 ATOM 1755 O OD1 . ASN B 2 81 ? 4.285 25.738 27.112 1.00 26.18 ? 81 ASN B OD1 1 ATOM 1756 N ND2 . ASN B 2 81 ? 5.018 27.789 26.553 1.00 28.87 ? 81 ASN B ND2 1 ATOM 1757 N N . ALA B 2 82 ? 7.629 23.340 23.759 1.00 24.49 ? 82 ALA B N 1 ATOM 1758 C CA . ALA B 2 82 ? 7.785 22.425 22.634 1.00 24.96 ? 82 ALA B CA 1 ATOM 1759 C C . ALA B 2 82 ? 6.912 21.237 23.020 1.00 30.87 ? 82 ALA B C 1 ATOM 1760 O O . ALA B 2 82 ? 6.635 21.035 24.201 1.00 28.80 ? 82 ALA B O 1 ATOM 1761 C CB . ALA B 2 82 ? 9.227 21.985 22.497 1.00 20.89 ? 82 ALA B CB 1 ATOM 1762 N N . ARG B 2 83 ? 6.473 20.456 22.041 1.00 30.48 ? 83 ARG B N 1 ATOM 1763 C CA . ARG B 2 83 ? 5.622 19.312 22.335 1.00 35.48 ? 83 ARG B CA 1 ATOM 1764 C C . ARG B 2 83 ? 6.375 18.219 23.087 1.00 31.43 ? 83 ARG B C 1 ATOM 1765 O O . ARG B 2 83 ? 7.536 17.928 22.787 1.00 27.55 ? 83 ARG B O 1 ATOM 1766 C CB . ARG B 2 83 ? 5.056 18.733 21.037 1.00 40.76 ? 83 ARG B CB 1 ATOM 1767 C CG . ARG B 2 83 ? 4.232 17.478 21.236 1.00 47.94 ? 83 ARG B CG 1 ATOM 1768 C CD . ARG B 2 83 ? 4.123 16.699 19.937 1.00 57.21 ? 83 ARG B CD 1 ATOM 1769 N NE . ARG B 2 83 ? 3.658 15.332 20.156 1.00 61.40 ? 83 ARG B NE 1 ATOM 1770 C CZ . ARG B 2 83 ? 3.799 14.351 19.271 1.00 64.94 ? 83 ARG B CZ 1 ATOM 1771 N NH1 . ARG B 2 83 ? 3.347 13.134 19.546 1.00 62.18 ? 83 ARG B NH1 1 ATOM 1772 N NH2 . ARG B 2 83 ? 4.403 14.587 18.112 1.00 64.65 ? 83 ARG B NH2 1 ATOM 1773 N N . PHE B 2 84 ? 5.717 17.613 24.070 1.00 30.36 ? 84 PHE B N 1 ATOM 1774 C CA . PHE B 2 84 ? 6.348 16.537 24.820 1.00 31.98 ? 84 PHE B CA 1 ATOM 1775 C C . PHE B 2 84 ? 6.062 15.205 24.143 1.00 33.50 ? 84 PHE B C 1 ATOM 1776 O O . PHE B 2 84 ? 4.909 14.796 24.022 1.00 35.03 ? 84 PHE B O 1 ATOM 1777 C CB . PHE B 2 84 ? 5.834 16.486 26.261 1.00 29.34 ? 84 PHE B CB 1 ATOM 1778 C CG . PHE B 2 84 ? 6.471 15.404 27.084 1.00 31.87 ? 84 PHE B CG 1 ATOM 1779 C CD1 . PHE B 2 84 ? 7.833 15.442 27.369 1.00 26.92 ? 84 PHE B CD1 1 ATOM 1780 C CD2 . PHE B 2 84 ? 5.718 14.333 27.554 1.00 28.13 ? 84 PHE B CD2 1 ATOM 1781 C CE1 . PHE B 2 84 ? 8.437 14.427 28.111 1.00 27.60 ? 84 PHE B CE1 1 ATOM 1782 C CE2 . PHE B 2 84 ? 6.315 13.311 28.298 1.00 33.42 ? 84 PHE B CE2 1 ATOM 1783 C CZ . PHE B 2 84 ? 7.677 13.360 28.576 1.00 29.76 ? 84 PHE B CZ 1 ATOM 1784 N N . ASP B 2 85 ? 7.116 14.539 23.693 1.00 33.18 ? 85 ASP B N 1 ATOM 1785 C CA . ASP B 2 85 ? 6.995 13.237 23.035 1.00 33.26 ? 85 ASP B CA 1 ATOM 1786 C C . ASP B 2 85 ? 8.197 12.393 23.436 1.00 29.94 ? 85 ASP B C 1 ATOM 1787 O O . ASP B 2 85 ? 8.080 11.466 24.250 1.00 34.61 ? 85 ASP B O 1 ATOM 1788 C CB . ASP B 2 85 ? 6.951 13.404 21.513 1.00 37.00 ? 85 ASP B CB 1 ATOM 1789 C CG . ASP B 2 85 ? 6.885 12.072 20.787 1.00 40.34 ? 85 ASP B CG 1 ATOM 1790 O OD1 . ASP B 2 85 ? 6.183 11.162 21.279 1.00 37.62 ? 85 ASP B OD1 1 ATOM 1791 O OD2 . ASP B 2 85 ? 7.528 11.938 19.727 1.00 41.89 ? 85 ASP B OD2 1 ATOM 1792 N N . TYR B 2 86 ? 9.356 12.712 22.869 1.00 26.00 ? 86 TYR B N 1 ATOM 1793 C CA . TYR B 2 86 ? 10.568 11.993 23.225 1.00 27.17 ? 86 TYR B CA 1 ATOM 1794 C C . TYR B 2 86 ? 10.786 12.142 24.730 1.00 23.61 ? 86 TYR B C 1 ATOM 1795 O O . TYR B 2 86 ? 10.586 13.218 25.290 1.00 23.11 ? 86 TYR B O 1 ATOM 1796 C CB . TYR B 2 86 ? 11.791 12.581 22.518 1.00 25.39 ? 86 TYR B CB 1 ATOM 1797 C CG . TYR B 2 86 ? 13.080 11.924 22.951 1.00 21.64 ? 86 TYR B CG 1 ATOM 1798 C CD1 . TYR B 2 86 ? 13.419 10.654 22.488 1.00 24.86 ? 86 TYR B CD1 1 ATOM 1799 C CD2 . TYR B 2 86 ? 13.933 12.538 23.871 1.00 24.27 ? 86 TYR B CD2 1 ATOM 1800 C CE1 . TYR B 2 86 ? 14.571 10.004 22.928 1.00 25.20 ? 86 TYR B CE1 1 ATOM 1801 C CE2 . TYR B 2 86 ? 15.093 11.899 24.326 1.00 19.84 ? 86 TYR B CE2 1 ATOM 1802 C CZ . TYR B 2 86 ? 15.402 10.625 23.842 1.00 26.69 ? 86 TYR B CZ 1 ATOM 1803 O OH . TYR B 2 86 ? 16.537 9.967 24.244 1.00 25.77 ? 86 TYR B OH 1 ATOM 1804 N N . LYS B 2 87 ? 11.191 11.069 25.388 1.00 21.93 ? 87 LYS B N 1 ATOM 1805 C CA . LYS B 2 87 ? 11.456 11.171 26.811 1.00 27.42 ? 87 LYS B CA 1 ATOM 1806 C C . LYS B 2 87 ? 12.500 10.155 27.241 1.00 30.29 ? 87 LYS B C 1 ATOM 1807 O O . LYS B 2 87 ? 12.541 9.029 26.737 1.00 28.83 ? 87 LYS B O 1 ATOM 1808 C CB . LYS B 2 87 ? 10.173 10.975 27.621 1.00 33.74 ? 87 LYS B CB 1 ATOM 1809 C CG . LYS B 2 87 ? 9.669 9.550 27.691 1.00 38.37 ? 87 LYS B CG 1 ATOM 1810 C CD . LYS B 2 87 ? 8.706 9.387 28.864 1.00 45.46 ? 87 LYS B CD 1 ATOM 1811 C CE . LYS B 2 87 ? 8.062 8.011 28.869 1.00 49.37 ? 87 LYS B CE 1 ATOM 1812 N NZ . LYS B 2 87 ? 7.180 7.833 27.684 1.00 57.05 ? 87 LYS B NZ 1 ATOM 1813 N N . ALA B 2 88 ? 13.362 10.570 28.161 1.00 23.76 ? 88 ALA B N 1 ATOM 1814 C CA . ALA B 2 88 ? 14.384 9.687 28.682 1.00 20.90 ? 88 ALA B CA 1 ATOM 1815 C C . ALA B 2 88 ? 14.176 9.527 30.186 1.00 18.60 ? 88 ALA B C 1 ATOM 1816 O O . ALA B 2 88 ? 15.109 9.189 30.913 1.00 19.21 ? 88 ALA B O 1 ATOM 1817 C CB . ALA B 2 88 ? 15.769 10.249 28.396 1.00 21.97 ? 88 ALA B CB 1 ATOM 1818 N N . TRP B 2 89 ? 12.951 9.771 30.646 1.00 20.14 ? 89 TRP B N 1 ATOM 1819 C CA . TRP B 2 89 ? 12.611 9.610 32.059 1.00 15.35 ? 89 TRP B CA 1 ATOM 1820 C C . TRP B 2 89 ? 12.197 8.150 32.181 1.00 21.82 ? 89 TRP B C 1 ATOM 1821 O O . TRP B 2 89 ? 11.167 7.753 31.625 1.00 24.21 ? 89 TRP B O 1 ATOM 1822 C CB . TRP B 2 89 ? 11.432 10.505 32.436 1.00 15.57 ? 89 TRP B CB 1 ATOM 1823 C CG . TRP B 2 89 ? 10.981 10.339 33.856 1.00 17.82 ? 89 TRP B CG 1 ATOM 1824 C CD1 . TRP B 2 89 ? 11.733 10.523 34.989 1.00 19.16 ? 89 TRP B CD1 1 ATOM 1825 C CD2 . TRP B 2 89 ? 9.666 10.002 34.298 1.00 17.60 ? 89 TRP B CD2 1 ATOM 1826 N NE1 . TRP B 2 89 ? 10.958 10.326 36.113 1.00 19.14 ? 89 TRP B NE1 1 ATOM 1827 C CE2 . TRP B 2 89 ? 9.684 10.008 35.715 1.00 18.72 ? 89 TRP B CE2 1 ATOM 1828 C CE3 . TRP B 2 89 ? 8.465 9.697 33.633 1.00 23.65 ? 89 TRP B CE3 1 ATOM 1829 C CZ2 . TRP B 2 89 ? 8.549 9.725 36.479 1.00 18.54 ? 89 TRP B CZ2 1 ATOM 1830 C CZ3 . TRP B 2 89 ? 7.330 9.413 34.397 1.00 25.55 ? 89 TRP B CZ3 1 ATOM 1831 C CH2 . TRP B 2 89 ? 7.384 9.432 35.804 1.00 24.38 ? 89 TRP B CH2 1 ATOM 1832 N N . LYS B 2 90 ? 12.979 7.366 32.913 1.00 19.35 ? 90 LYS B N 1 ATOM 1833 C CA . LYS B 2 90 ? 12.715 5.931 33.041 1.00 25.39 ? 90 LYS B CA 1 ATOM 1834 C C . LYS B 2 90 ? 12.680 5.427 34.478 1.00 26.19 ? 90 LYS B C 1 ATOM 1835 O O . LYS B 2 90 ? 13.170 4.332 34.778 1.00 21.77 ? 90 LYS B O 1 ATOM 1836 C CB . LYS B 2 90 ? 13.784 5.147 32.266 1.00 23.85 ? 90 LYS B CB 1 ATOM 1837 C CG . LYS B 2 90 ? 13.976 5.596 30.827 1.00 25.65 ? 90 LYS B CG 1 ATOM 1838 C CD . LYS B 2 90 ? 15.301 5.055 30.278 1.00 28.55 ? 90 LYS B CD 1 ATOM 1839 C CE . LYS B 2 90 ? 15.673 5.692 28.949 1.00 34.09 ? 90 LYS B CE 1 ATOM 1840 N NZ . LYS B 2 90 ? 17.040 5.290 28.530 1.00 26.34 ? 90 LYS B NZ 1 ATOM 1841 N N . ARG B 2 91 ? 12.110 6.229 35.366 1.00 24.09 ? 91 ARG B N 1 ATOM 1842 C CA . ARG B 2 91 ? 11.995 5.849 36.764 1.00 21.39 ? 91 ARG B CA 1 ATOM 1843 C C . ARG B 2 91 ? 11.067 4.622 36.912 1.00 20.79 ? 91 ARG B C 1 ATOM 1844 O O . ARG B 2 91 ? 9.953 4.607 36.395 1.00 19.62 ? 91 ARG B O 1 ATOM 1845 C CB . ARG B 2 91 ? 11.485 7.073 37.554 1.00 26.18 ? 91 ARG B CB 1 ATOM 1846 C CG . ARG B 2 91 ? 10.508 6.812 38.674 1.00 35.84 ? 91 ARG B CG 1 ATOM 1847 C CD . ARG B 2 91 ? 11.043 7.183 40.045 1.00 30.90 ? 91 ARG B CD 1 ATOM 1848 N NE . ARG B 2 91 ? 11.529 8.559 40.236 1.00 23.17 ? 91 ARG B NE 1 ATOM 1849 C CZ . ARG B 2 91 ? 12.201 8.913 41.325 1.00 20.96 ? 91 ARG B CZ 1 ATOM 1850 N NH1 . ARG B 2 91 ? 12.652 10.154 41.500 1.00 24.00 ? 91 ARG B NH1 1 ATOM 1851 N NH2 . ARG B 2 91 ? 12.418 7.993 42.263 1.00 20.94 ? 91 ARG B NH2 1 ATOM 1852 N N . ARG B 2 92 ? 11.549 3.583 37.592 1.00 20.78 ? 92 ARG B N 1 ATOM 1853 C CA . ARG B 2 92 ? 10.759 2.369 37.812 1.00 21.87 ? 92 ARG B CA 1 ATOM 1854 C C . ARG B 2 92 ? 9.704 2.704 38.870 1.00 26.96 ? 92 ARG B C 1 ATOM 1855 O O . ARG B 2 92 ? 9.736 3.785 39.457 1.00 21.28 ? 92 ARG B O 1 ATOM 1856 C CB . ARG B 2 92 ? 11.653 1.241 38.336 1.00 26.15 ? 92 ARG B CB 1 ATOM 1857 C CG . ARG B 2 92 ? 12.161 1.443 39.775 1.00 18.45 ? 92 ARG B CG 1 ATOM 1858 C CD . ARG B 2 92 ? 13.158 0.332 40.156 1.00 23.94 ? 92 ARG B CD 1 ATOM 1859 N NE . ARG B 2 92 ? 13.630 0.382 41.543 1.00 24.22 ? 92 ARG B NE 1 ATOM 1860 C CZ . ARG B 2 92 ? 14.510 1.262 42.019 1.00 26.46 ? 92 ARG B CZ 1 ATOM 1861 N NH1 . ARG B 2 92 ? 15.032 2.193 41.229 1.00 24.41 ? 92 ARG B NH1 1 ATOM 1862 N NH2 . ARG B 2 92 ? 14.888 1.198 43.288 1.00 23.89 ? 92 ARG B NH2 1 ATOM 1863 N N . PRO B 2 93 ? 8.761 1.786 39.126 1.00 24.53 ? 93 PRO B N 1 ATOM 1864 C CA . PRO B 2 93 ? 7.740 2.082 40.139 1.00 27.65 ? 93 PRO B CA 1 ATOM 1865 C C . PRO B 2 93 ? 8.309 2.333 41.536 1.00 27.28 ? 93 PRO B C 1 ATOM 1866 O O . PRO B 2 93 ? 9.091 1.536 42.059 1.00 21.25 ? 93 PRO B O 1 ATOM 1867 C CB . PRO B 2 93 ? 6.843 0.844 40.095 1.00 29.08 ? 93 PRO B CB 1 ATOM 1868 C CG . PRO B 2 93 ? 6.913 0.452 38.641 1.00 31.44 ? 93 PRO B CG 1 ATOM 1869 C CD . PRO B 2 93 ? 8.404 0.570 38.368 1.00 25.54 ? 93 PRO B CD 1 ATOM 1870 N N . TYR B 2 94 ? 7.931 3.466 42.127 1.00 24.74 ? 94 TYR B N 1 ATOM 1871 C CA . TYR B 2 94 ? 8.366 3.802 43.477 1.00 18.06 ? 94 TYR B CA 1 ATOM 1872 C C . TYR B 2 94 ? 7.112 3.832 44.353 1.00 17.42 ? 94 TYR B C 1 ATOM 1873 O O . TYR B 2 94 ? 6.027 4.175 43.889 1.00 21.35 ? 94 TYR B O 1 ATOM 1874 C CB . TYR B 2 94 ? 9.061 5.168 43.520 1.00 16.84 ? 94 TYR B CB 1 ATOM 1875 C CG . TYR B 2 94 ? 10.568 5.076 43.430 1.00 20.15 ? 94 TYR B CG 1 ATOM 1876 C CD1 . TYR B 2 94 ? 11.194 4.635 42.258 1.00 21.78 ? 94 TYR B CD1 1 ATOM 1877 C CD2 . TYR B 2 94 ? 11.371 5.415 44.516 1.00 22.95 ? 94 TYR B CD2 1 ATOM 1878 C CE1 . TYR B 2 94 ? 12.579 4.539 42.177 1.00 19.70 ? 94 TYR B CE1 1 ATOM 1879 C CE2 . TYR B 2 94 ? 12.754 5.319 44.447 1.00 24.31 ? 94 TYR B CE2 1 ATOM 1880 C CZ . TYR B 2 94 ? 13.356 4.877 43.268 1.00 24.66 ? 94 TYR B CZ 1 ATOM 1881 O OH . TYR B 2 94 ? 14.733 4.779 43.186 1.00 25.04 ? 94 TYR B OH 1 ATOM 1882 N N . CYS B 2 95 ? 7.290 3.506 45.622 1.00 22.29 ? 95 CYS B N 1 ATOM 1883 C CA . CYS B 2 95 ? 6.180 3.433 46.560 1.00 21.61 ? 95 CYS B CA 1 ATOM 1884 C C . CYS B 2 95 ? 6.461 4.283 47.801 1.00 20.06 ? 95 CYS B C 1 ATOM 1885 O O . CYS B 2 95 ? 7.610 4.647 48.072 1.00 21.73 ? 95 CYS B O 1 ATOM 1886 C CB . CYS B 2 95 ? 5.936 1.950 46.899 1.00 25.20 ? 95 CYS B CB 1 ATOM 1887 S SG . CYS B 2 95 ? 5.082 1.022 45.554 1.00 23.92 ? 95 CYS B SG 1 ATOM 1888 N N . THR B 2 96 ? 5.413 4.588 48.561 1.00 22.24 ? 96 THR B N 1 ATOM 1889 C CA . THR B 2 96 ? 5.550 5.461 49.726 1.00 17.12 ? 96 THR B CA 1 ATOM 1890 C C . THR B 2 96 ? 5.733 4.829 51.104 1.00 18.00 ? 96 THR B C 1 ATOM 1891 O O . THR B 2 96 ? 4.946 3.970 51.524 1.00 18.35 ? 96 THR B O 1 ATOM 1892 C CB . THR B 2 96 ? 4.353 6.405 49.788 1.00 21.29 ? 96 THR B CB 1 ATOM 1893 O OG1 . THR B 2 96 ? 4.119 6.956 48.486 1.00 18.77 ? 96 THR B OG1 1 ATOM 1894 C CG2 . THR B 2 96 ? 4.623 7.527 50.758 1.00 20.12 ? 96 THR B CG2 1 ATOM 1895 N N . VAL B 2 97 ? 6.762 5.299 51.811 1.00 16.89 ? 97 VAL B N 1 ATOM 1896 C CA . VAL B 2 97 ? 7.099 4.829 53.154 1.00 19.32 ? 97 VAL B CA 1 ATOM 1897 C C . VAL B 2 97 ? 6.850 5.934 54.178 1.00 21.97 ? 97 VAL B C 1 ATOM 1898 O O . VAL B 2 97 ? 7.270 7.072 53.975 1.00 18.52 ? 97 VAL B O 1 ATOM 1899 C CB . VAL B 2 97 ? 8.604 4.436 53.249 1.00 20.00 ? 97 VAL B CB 1 ATOM 1900 C CG1 . VAL B 2 97 ? 9.002 4.197 54.685 1.00 19.31 ? 97 VAL B CG1 1 ATOM 1901 C CG2 . VAL B 2 97 ? 8.870 3.190 52.427 1.00 21.70 ? 97 VAL B CG2 1 ATOM 1902 N N . MET B 2 98 ? 6.153 5.607 55.265 1.00 16.11 ? 98 MET B N 1 ATOM 1903 C CA . MET B 2 98 ? 5.926 6.597 56.304 1.00 11.75 ? 98 MET B CA 1 ATOM 1904 C C . MET B 2 98 ? 6.953 6.307 57.388 1.00 17.41 ? 98 MET B C 1 ATOM 1905 O O . MET B 2 98 ? 7.082 5.171 57.841 1.00 20.93 ? 98 MET B O 1 ATOM 1906 C CB . MET B 2 98 ? 4.506 6.481 56.880 1.00 16.43 ? 98 MET B CB 1 ATOM 1907 C CG . MET B 2 98 ? 4.217 7.481 57.982 1.00 19.68 ? 98 MET B CG 1 ATOM 1908 S SD . MET B 2 98 ? 2.409 7.509 58.292 1.00 25.76 ? 98 MET B SD 1 ATOM 1909 C CE . MET B 2 98 ? 2.293 6.213 59.352 1.00 20.57 ? 98 MET B CE 1 ATOM 1910 N N . VAL B 2 99 ? 7.690 7.336 57.793 1.00 20.08 ? 99 VAL B N 1 ATOM 1911 C CA . VAL B 2 99 ? 8.715 7.180 58.813 1.00 21.31 ? 99 VAL B CA 1 ATOM 1912 C C . VAL B 2 99 ? 8.342 7.945 60.066 1.00 19.67 ? 99 VAL B C 1 ATOM 1913 O O . VAL B 2 99 ? 7.907 9.101 59.996 1.00 18.58 ? 99 VAL B O 1 ATOM 1914 C CB . VAL B 2 99 ? 10.098 7.705 58.309 1.00 19.94 ? 99 VAL B CB 1 ATOM 1915 C CG1 . VAL B 2 99 ? 11.167 7.519 59.393 1.00 22.58 ? 99 VAL B CG1 1 ATOM 1916 C CG2 . VAL B 2 99 ? 10.485 6.968 57.056 1.00 23.04 ? 99 VAL B CG2 1 ATOM 1917 N N . VAL B 2 100 ? 8.517 7.288 61.207 1.00 19.50 ? 100 VAL B N 1 ATOM 1918 C CA . VAL B 2 100 ? 8.225 7.886 62.493 1.00 19.33 ? 100 VAL B CA 1 ATOM 1919 C C . VAL B 2 100 ? 9.513 8.170 63.250 1.00 23.28 ? 100 VAL B C 1 ATOM 1920 O O . VAL B 2 100 ? 10.259 7.251 63.587 1.00 21.69 ? 100 VAL B O 1 ATOM 1921 C CB . VAL B 2 100 ? 7.344 6.955 63.361 1.00 18.87 ? 100 VAL B CB 1 ATOM 1922 C CG1 . VAL B 2 100 ? 7.035 7.628 64.683 1.00 20.88 ? 100 VAL B CG1 1 ATOM 1923 C CG2 . VAL B 2 100 ? 6.052 6.629 62.625 1.00 17.32 ? 100 VAL B CG2 1 ATOM 1924 N N . LYS B 2 101 ? 9.772 9.448 63.495 1.00 23.14 ? 101 LYS B N 1 ATOM 1925 C CA . LYS B 2 101 ? 10.961 9.876 64.229 1.00 25.12 ? 101 LYS B CA 1 ATOM 1926 C C . LYS B 2 101 ? 10.502 10.375 65.601 1.00 26.55 ? 101 LYS B C 1 ATOM 1927 O O . LYS B 2 101 ? 9.305 10.558 65.839 1.00 23.77 ? 101 LYS B O 1 ATOM 1928 C CB . LYS B 2 101 ? 11.692 11.002 63.468 1.00 26.58 ? 101 LYS B CB 1 ATOM 1929 C CG . LYS B 2 101 ? 12.414 10.544 62.190 1.00 25.66 ? 101 LYS B CG 1 ATOM 1930 C CD . LYS B 2 101 ? 13.424 9.444 62.509 1.00 36.61 ? 101 LYS B CD 1 ATOM 1931 C CE . LYS B 2 101 ? 14.113 8.896 61.260 1.00 47.44 ? 101 LYS B CE 1 ATOM 1932 N NZ . LYS B 2 101 ? 14.978 9.897 60.569 1.00 51.50 ? 101 LYS B NZ 1 ATOM 1933 N N . PRO B 2 102 ? 11.445 10.608 66.522 1.00 25.75 ? 102 PRO B N 1 ATOM 1934 C CA . PRO B 2 102 ? 11.045 11.084 67.852 1.00 28.19 ? 102 PRO B CA 1 ATOM 1935 C C . PRO B 2 102 ? 10.430 12.472 67.829 1.00 28.68 ? 102 PRO B C 1 ATOM 1936 O O . PRO B 2 102 ? 9.594 12.801 68.667 1.00 31.29 ? 102 PRO B O 1 ATOM 1937 C CB . PRO B 2 102 ? 12.362 11.057 68.642 1.00 24.27 ? 102 PRO B CB 1 ATOM 1938 C CG . PRO B 2 102 ? 13.121 9.923 67.983 1.00 25.09 ? 102 PRO B CG 1 ATOM 1939 C CD . PRO B 2 102 ? 12.861 10.195 66.510 1.00 25.17 ? 102 PRO B CD 1 ATOM 1940 N N . ASP B 2 103 ? 10.842 13.283 66.860 1.00 29.44 ? 103 ASP B N 1 ATOM 1941 C CA . ASP B 2 103 ? 10.368 14.654 66.769 1.00 31.77 ? 103 ASP B CA 1 ATOM 1942 C C . ASP B 2 103 ? 9.400 14.925 65.623 1.00 33.55 ? 103 ASP B C 1 ATOM 1943 O O . ASP B 2 103 ? 8.896 16.041 65.495 1.00 28.05 ? 103 ASP B O 1 ATOM 1944 C CB . ASP B 2 103 ? 11.568 15.591 66.636 1.00 37.07 ? 103 ASP B CB 1 ATOM 1945 C CG . ASP B 2 103 ? 12.287 15.431 65.310 1.00 39.52 ? 103 ASP B CG 1 ATOM 1946 O OD1 . ASP B 2 103 ? 12.536 14.279 64.876 1.00 38.75 ? 103 ASP B OD1 1 ATOM 1947 O OD2 . ASP B 2 103 ? 12.616 16.469 64.703 1.00 46.27 ? 103 ASP B OD2 1 ATOM 1948 N N . ARG B 2 104 ? 9.151 13.925 64.784 1.00 25.95 ? 104 ARG B N 1 ATOM 1949 C CA . ARG B 2 104 ? 8.233 14.125 63.673 1.00 25.44 ? 104 ARG B CA 1 ATOM 1950 C C . ARG B 2 104 ? 7.997 12.882 62.853 1.00 17.92 ? 104 ARG B C 1 ATOM 1951 O O . ARG B 2 104 ? 8.637 11.848 63.052 1.00 22.71 ? 104 ARG B O 1 ATOM 1952 C CB . ARG B 2 104 ? 8.757 15.198 62.731 1.00 23.35 ? 104 ARG B CB 1 ATOM 1953 C CG . ARG B 2 104 ? 10.064 14.810 62.069 1.00 24.67 ? 104 ARG B CG 1 ATOM 1954 C CD . ARG B 2 104 ? 10.205 15.569 60.778 1.00 40.04 ? 104 ARG B CD 1 ATOM 1955 N NE . ARG B 2 104 ? 11.539 15.462 60.216 1.00 28.62 ? 104 ARG B NE 1 ATOM 1956 C CZ . ARG B 2 104 ? 11.873 15.918 59.014 1.00 30.38 ? 104 ARG B CZ 1 ATOM 1957 N NH1 . ARG B 2 104 ? 10.965 16.499 58.237 1.00 23.31 ? 104 ARG B NH1 1 ATOM 1958 N NH2 . ARG B 2 104 ? 13.131 15.827 58.607 1.00 23.84 ? 104 ARG B NH2 1 ATOM 1959 N N . ILE B 2 105 ? 7.075 13.027 61.907 1.00 19.87 ? 105 ILE B N 1 ATOM 1960 C CA . ILE B 2 105 ? 6.692 11.959 60.990 1.00 17.82 ? 105 ILE B CA 1 ATOM 1961 C C . ILE B 2 105 ? 6.836 12.536 59.588 1.00 18.25 ? 105 ILE B C 1 ATOM 1962 O O . ILE B 2 105 ? 6.501 13.701 59.360 1.00 18.08 ? 105 ILE B O 1 ATOM 1963 C CB . ILE B 2 105 ? 5.200 11.571 61.208 1.00 18.01 ? 105 ILE B CB 1 ATOM 1964 C CG1 . ILE B 2 105 ? 4.992 11.070 62.643 1.00 17.59 ? 105 ILE B CG1 1 ATOM 1965 C CG2 . ILE B 2 105 ? 4.760 10.517 60.178 1.00 20.06 ? 105 ILE B CG2 1 ATOM 1966 C CD1 . ILE B 2 105 ? 3.508 11.167 63.111 1.00 22.98 ? 105 ILE B CD1 1 ATOM 1967 N N . PHE B 2 106 ? 7.330 11.741 58.640 1.00 17.03 ? 106 PHE B N 1 ATOM 1968 C CA . PHE B 2 106 ? 7.437 12.234 57.269 1.00 16.42 ? 106 PHE B CA 1 ATOM 1969 C C . PHE B 2 106 ? 7.349 11.052 56.331 1.00 14.46 ? 106 PHE B C 1 ATOM 1970 O O . PHE B 2 106 ? 7.485 9.906 56.759 1.00 18.90 ? 106 PHE B O 1 ATOM 1971 C CB . PHE B 2 106 ? 8.758 12.995 57.047 1.00 20.73 ? 106 PHE B CB 1 ATOM 1972 C CG . PHE B 2 106 ? 9.992 12.144 57.198 1.00 20.50 ? 106 PHE B CG 1 ATOM 1973 C CD1 . PHE B 2 106 ? 10.345 11.216 56.216 1.00 20.50 ? 106 PHE B CD1 1 ATOM 1974 C CD2 . PHE B 2 106 ? 10.807 12.279 58.321 1.00 27.55 ? 106 PHE B CD2 1 ATOM 1975 C CE1 . PHE B 2 106 ? 11.508 10.422 56.348 1.00 18.54 ? 106 PHE B CE1 1 ATOM 1976 C CE2 . PHE B 2 106 ? 11.968 11.492 58.465 1.00 23.27 ? 106 PHE B CE2 1 ATOM 1977 C CZ . PHE B 2 106 ? 12.311 10.568 57.476 1.00 21.10 ? 106 PHE B CZ 1 ATOM 1978 N N . TRP B 2 107 ? 7.103 11.329 55.059 1.00 15.63 ? 107 TRP B N 1 ATOM 1979 C CA . TRP B 2 107 ? 7.007 10.265 54.068 1.00 14.28 ? 107 TRP B CA 1 ATOM 1980 C C . TRP B 2 107 ? 8.129 10.449 53.052 1.00 18.77 ? 107 TRP B C 1 ATOM 1981 O O . TRP B 2 107 ? 8.567 11.575 52.793 1.00 18.26 ? 107 TRP B O 1 ATOM 1982 C CB . TRP B 2 107 ? 5.693 10.339 53.276 1.00 14.94 ? 107 TRP B CB 1 ATOM 1983 C CG . TRP B 2 107 ? 4.399 10.389 54.047 1.00 20.44 ? 107 TRP B CG 1 ATOM 1984 C CD1 . TRP B 2 107 ? 4.212 10.227 55.391 1.00 20.70 ? 107 TRP B CD1 1 ATOM 1985 C CD2 . TRP B 2 107 ? 3.104 10.635 53.486 1.00 13.22 ? 107 TRP B CD2 1 ATOM 1986 N NE1 . TRP B 2 107 ? 2.868 10.365 55.700 1.00 16.60 ? 107 TRP B NE1 1 ATOM 1987 C CE2 . TRP B 2 107 ? 2.172 10.615 54.547 1.00 21.75 ? 107 TRP B CE2 1 ATOM 1988 C CE3 . TRP B 2 107 ? 2.643 10.873 52.187 1.00 19.42 ? 107 TRP B CE3 1 ATOM 1989 C CZ2 . TRP B 2 107 ? 0.807 10.822 54.348 1.00 20.14 ? 107 TRP B CZ2 1 ATOM 1990 C CZ3 . TRP B 2 107 ? 1.277 11.081 51.985 1.00 20.26 ? 107 TRP B CZ3 1 ATOM 1991 C CH2 . TRP B 2 107 ? 0.379 11.054 53.063 1.00 21.76 ? 107 TRP B CH2 1 ATOM 1992 N N . PHE B 2 108 ? 8.599 9.341 52.495 1.00 15.71 ? 108 PHE B N 1 ATOM 1993 C CA . PHE B 2 108 ? 9.598 9.397 51.436 1.00 17.09 ? 108 PHE B CA 1 ATOM 1994 C C . PHE B 2 108 ? 9.323 8.213 50.518 1.00 19.37 ? 108 PHE B C 1 ATOM 1995 O O . PHE B 2 108 ? 8.498 7.348 50.843 1.00 21.00 ? 108 PHE B O 1 ATOM 1996 C CB . PHE B 2 108 ? 11.042 9.422 51.984 1.00 19.62 ? 108 PHE B CB 1 ATOM 1997 C CG . PHE B 2 108 ? 11.582 8.090 52.421 1.00 18.86 ? 108 PHE B CG 1 ATOM 1998 C CD1 . PHE B 2 108 ? 11.084 7.442 53.540 1.00 23.73 ? 108 PHE B CD1 1 ATOM 1999 C CD2 . PHE B 2 108 ? 12.641 7.511 51.721 1.00 15.88 ? 108 PHE B CD2 1 ATOM 2000 C CE1 . PHE B 2 108 ? 11.638 6.225 53.964 1.00 24.95 ? 108 PHE B CE1 1 ATOM 2001 C CE2 . PHE B 2 108 ? 13.197 6.299 52.139 1.00 27.17 ? 108 PHE B CE2 1 ATOM 2002 C CZ . PHE B 2 108 ? 12.694 5.662 53.258 1.00 23.29 ? 108 PHE B CZ 1 ATOM 2003 N N . THR B 2 109 ? 9.970 8.168 49.364 1.00 17.85 ? 109 THR B N 1 ATOM 2004 C CA . THR B 2 109 ? 9.705 7.084 48.429 1.00 16.47 ? 109 THR B CA 1 ATOM 2005 C C . THR B 2 109 ? 10.864 6.107 48.280 1.00 20.66 ? 109 THR B C 1 ATOM 2006 O O . THR B 2 109 ? 12.022 6.469 48.450 1.00 19.55 ? 109 THR B O 1 ATOM 2007 C CB . THR B 2 109 ? 9.375 7.633 47.019 1.00 22.90 ? 109 THR B CB 1 ATOM 2008 O OG1 . THR B 2 109 ? 10.439 8.490 46.584 1.00 18.17 ? 109 THR B OG1 1 ATOM 2009 C CG2 . THR B 2 109 ? 8.063 8.410 47.028 1.00 23.41 ? 109 THR B CG2 1 ATOM 2010 N N . ARG B 2 110 ? 10.528 4.859 47.971 1.00 22.41 ? 110 ARG B N 1 ATOM 2011 C CA . ARG B 2 110 ? 11.525 3.821 47.750 1.00 25.89 ? 110 ARG B CA 1 ATOM 2012 C C . ARG B 2 110 ? 11.033 2.911 46.639 1.00 23.19 ? 110 ARG B C 1 ATOM 2013 O O . ARG B 2 110 ? 9.835 2.843 46.384 1.00 21.70 ? 110 ARG B O 1 ATOM 2014 C CB . ARG B 2 110 ? 11.748 3.001 49.019 1.00 23.12 ? 110 ARG B CB 1 ATOM 2015 C CG . ARG B 2 110 ? 12.530 3.740 50.062 1.00 31.76 ? 110 ARG B CG 1 ATOM 2016 C CD . ARG B 2 110 ? 13.731 2.924 50.457 1.00 44.99 ? 110 ARG B CD 1 ATOM 2017 N NE . ARG B 2 110 ? 13.410 2.002 51.527 1.00 40.59 ? 110 ARG B NE 1 ATOM 2018 C CZ . ARG B 2 110 ? 14.102 0.901 51.798 1.00 46.65 ? 110 ARG B CZ 1 ATOM 2019 N NH1 . ARG B 2 110 ? 15.158 0.573 51.063 1.00 41.55 ? 110 ARG B NH1 1 ATOM 2020 N NH2 . ARG B 2 110 ? 13.746 0.139 52.821 1.00 40.94 ? 110 ARG B NH2 1 ATOM 2021 N N . GLY B 2 111 ? 11.962 2.229 45.966 1.00 25.35 ? 111 GLY B N 1 ATOM 2022 C CA . GLY B 2 111 ? 11.570 1.314 44.911 1.00 17.81 ? 111 GLY B CA 1 ATOM 2023 C C . GLY B 2 111 ? 10.531 0.373 45.510 1.00 21.01 ? 111 GLY B C 1 ATOM 2024 O O . GLY B 2 111 ? 10.702 -0.092 46.627 1.00 23.94 ? 111 GLY B O 1 ATOM 2025 N N . CYS B 2 112 ? 9.461 0.098 44.778 1.00 22.17 ? 112 CYS B N 1 ATOM 2026 C CA . CYS B 2 112 ? 8.405 -0.759 45.297 1.00 25.03 ? 112 CYS B CA 1 ATOM 2027 C C . CYS B 2 112 ? 8.902 -2.186 45.563 1.00 32.66 ? 112 CYS B C 1 ATOM 2028 O O . CYS B 2 112 ? 8.260 -2.953 46.288 1.00 30.51 ? 112 CYS B O 1 ATOM 2029 C CB . CYS B 2 112 ? 7.225 -0.781 44.321 1.00 23.13 ? 112 CYS B CB 1 ATOM 2030 S SG . CYS B 2 112 ? 6.406 0.827 43.999 1.00 25.75 ? 112 CYS B SG 1 ATOM 2031 N N . GLU B 2 113 ? 10.056 -2.526 44.996 1.00 28.93 ? 113 GLU B N 1 ATOM 2032 C CA . GLU B 2 113 ? 10.635 -3.857 45.160 1.00 30.33 ? 113 GLU B CA 1 ATOM 2033 C C . GLU B 2 113 ? 11.360 -4.014 46.495 1.00 29.16 ? 113 GLU B C 1 ATOM 2034 O O . GLU B 2 113 ? 11.699 -5.131 46.893 1.00 29.58 ? 113 GLU B O 1 ATOM 2035 C CB . GLU B 2 113 ? 11.622 -4.155 44.022 1.00 27.47 ? 113 GLU B CB 1 ATOM 2036 C CG . GLU B 2 113 ? 13.003 -3.523 44.204 1.00 25.63 ? 113 GLU B CG 1 ATOM 2037 C CD . GLU B 2 113 ? 13.050 -2.016 43.899 1.00 21.59 ? 113 GLU B CD 1 ATOM 2038 O OE1 . GLU B 2 113 ? 14.091 -1.400 44.205 1.00 23.73 ? 113 GLU B OE1 1 ATOM 2039 O OE2 . GLU B 2 113 ? 12.070 -1.460 43.360 1.00 27.48 ? 113 GLU B OE2 1 ATOM 2040 N N . LYS B 2 114 ? 11.613 -2.904 47.185 1.00 25.02 ? 114 LYS B N 1 ATOM 2041 C CA . LYS B 2 114 ? 12.303 -2.971 48.472 1.00 25.42 ? 114 LYS B CA 1 ATOM 2042 C C . LYS B 2 114 ? 11.385 -3.648 49.499 1.00 28.51 ? 114 LYS B C 1 ATOM 2043 O O . LYS B 2 114 ? 10.181 -3.758 49.278 1.00 30.13 ? 114 LYS B O 1 ATOM 2044 C CB . LYS B 2 114 ? 12.675 -1.565 48.959 1.00 31.79 ? 114 LYS B CB 1 ATOM 2045 C CG . LYS B 2 114 ? 13.618 -0.803 48.036 1.00 32.83 ? 114 LYS B CG 1 ATOM 2046 C CD . LYS B 2 114 ? 15.014 -1.420 48.006 1.00 33.74 ? 114 LYS B CD 1 ATOM 2047 C CE . LYS B 2 114 ? 15.932 -0.634 47.076 1.00 35.47 ? 114 LYS B CE 1 ATOM 2048 N NZ . LYS B 2 114 ? 17.326 -1.168 47.071 1.00 40.27 ? 114 LYS B NZ 1 ATOM 2049 N N . SER B 2 115 ? 11.955 -4.106 50.611 1.00 25.58 ? 115 SER B N 1 ATOM 2050 C CA . SER B 2 115 ? 11.168 -4.774 51.649 1.00 31.65 ? 115 SER B CA 1 ATOM 2051 C C . SER B 2 115 ? 11.054 -3.879 52.870 1.00 25.86 ? 115 SER B C 1 ATOM 2052 O O . SER B 2 115 ? 12.056 -3.465 53.442 1.00 26.12 ? 115 SER B O 1 ATOM 2053 C CB . SER B 2 115 ? 11.807 -6.107 52.039 1.00 37.25 ? 115 SER B CB 1 ATOM 2054 O OG . SER B 2 115 ? 11.657 -7.060 51.003 1.00 35.52 ? 115 SER B OG 1 ATOM 2055 N N . VAL B 2 116 ? 9.814 -3.602 53.258 1.00 25.99 ? 116 VAL B N 1 ATOM 2056 C CA . VAL B 2 116 ? 9.518 -2.725 54.385 1.00 21.98 ? 116 VAL B CA 1 ATOM 2057 C C . VAL B 2 116 ? 8.358 -3.300 55.209 1.00 19.41 ? 116 VAL B C 1 ATOM 2058 O O . VAL B 2 116 ? 7.536 -4.043 54.689 1.00 23.29 ? 116 VAL B O 1 ATOM 2059 C CB . VAL B 2 116 ? 9.063 -1.331 53.854 1.00 22.72 ? 116 VAL B CB 1 ATOM 2060 C CG1 . VAL B 2 116 ? 8.864 -0.363 54.996 1.00 19.46 ? 116 VAL B CG1 1 ATOM 2061 C CG2 . VAL B 2 116 ? 10.073 -0.801 52.838 1.00 24.74 ? 116 VAL B CG2 1 ATOM 2062 N N . SER B 2 117 ? 8.291 -2.952 56.488 1.00 23.38 ? 117 SER B N 1 ATOM 2063 C CA . SER B 2 117 ? 7.173 -3.399 57.309 1.00 21.45 ? 117 SER B CA 1 ATOM 2064 C C . SER B 2 117 ? 5.998 -2.602 56.751 1.00 28.34 ? 117 SER B C 1 ATOM 2065 O O . SER B 2 117 ? 6.201 -1.711 55.925 1.00 26.61 ? 117 SER B O 1 ATOM 2066 C CB . SER B 2 117 ? 7.404 -3.049 58.770 1.00 25.81 ? 117 SER B CB 1 ATOM 2067 O OG . SER B 2 117 ? 8.464 -3.816 59.308 1.00 28.22 ? 117 SER B OG 1 ATOM 2068 N N . PHE B 2 118 ? 4.776 -2.890 57.188 1.00 18.20 ? 118 PHE B N 1 ATOM 2069 C CA . PHE B 2 118 ? 3.631 -2.179 56.632 1.00 19.76 ? 118 PHE B CA 1 ATOM 2070 C C . PHE B 2 118 ? 2.471 -2.086 57.596 1.00 23.22 ? 118 PHE B C 1 ATOM 2071 O O . PHE B 2 118 ? 2.517 -2.662 58.679 1.00 22.41 ? 118 PHE B O 1 ATOM 2072 C CB . PHE B 2 118 ? 3.152 -2.859 55.341 1.00 18.97 ? 118 PHE B CB 1 ATOM 2073 C CG . PHE B 2 118 ? 2.890 -4.338 55.482 1.00 25.20 ? 118 PHE B CG 1 ATOM 2074 C CD1 . PHE B 2 118 ? 3.944 -5.242 55.558 1.00 25.78 ? 118 PHE B CD1 1 ATOM 2075 C CD2 . PHE B 2 118 ? 1.583 -4.826 55.508 1.00 24.89 ? 118 PHE B CD2 1 ATOM 2076 C CE1 . PHE B 2 118 ? 3.705 -6.624 55.657 1.00 29.14 ? 118 PHE B CE1 1 ATOM 2077 C CE2 . PHE B 2 118 ? 1.331 -6.202 55.608 1.00 29.11 ? 118 PHE B CE2 1 ATOM 2078 C CZ . PHE B 2 118 ? 2.400 -7.098 55.682 1.00 30.00 ? 118 PHE B CZ 1 ATOM 2079 N N . VAL B 2 119 ? 1.438 -1.357 57.191 1.00 20.92 ? 119 VAL B N 1 ATOM 2080 C CA . VAL B 2 119 ? 0.250 -1.193 58.020 1.00 23.47 ? 119 VAL B CA 1 ATOM 2081 C C . VAL B 2 119 ? -1.012 -1.342 57.171 1.00 25.13 ? 119 VAL B C 1 ATOM 2082 O O . VAL B 2 119 ? -1.110 -0.758 56.092 1.00 25.75 ? 119 VAL B O 1 ATOM 2083 C CB . VAL B 2 119 ? 0.253 0.191 58.726 1.00 21.52 ? 119 VAL B CB 1 ATOM 2084 C CG1 . VAL B 2 119 ? 0.349 1.318 57.682 1.00 20.61 ? 119 VAL B CG1 1 ATOM 2085 C CG2 . VAL B 2 119 ? -1.021 0.344 59.581 1.00 22.57 ? 119 VAL B CG2 1 ATOM 2086 N N . CYS B 2 120 ? -1.972 -2.130 57.662 1.00 23.73 ? 120 CYS B N 1 ATOM 2087 C CA . CYS B 2 120 ? -3.229 -2.361 56.947 1.00 23.73 ? 120 CYS B CA 1 ATOM 2088 C C . CYS B 2 120 ? -4.405 -1.618 57.584 1.00 24.94 ? 120 CYS B C 1 ATOM 2089 O O . CYS B 2 120 ? -4.392 -1.319 58.784 1.00 25.78 ? 120 CYS B O 1 ATOM 2090 C CB . CYS B 2 120 ? -3.570 -3.851 56.925 1.00 26.77 ? 120 CYS B CB 1 ATOM 2091 S SG . CYS B 2 120 ? -2.286 -4.976 56.318 1.00 25.49 ? 120 CYS B SG 1 ATOM 2092 N N . LYS B 2 121 ? -5.437 -1.373 56.786 1.00 21.27 ? 121 LYS B N 1 ATOM 2093 C CA . LYS B 2 121 ? -6.611 -0.638 57.234 1.00 20.45 ? 121 LYS B CA 1 ATOM 2094 C C . LYS B 2 121 ? -7.890 -1.060 56.508 1.00 27.14 ? 121 LYS B C 1 ATOM 2095 O O . LYS B 2 121 ? -7.871 -1.381 55.314 1.00 23.53 ? 121 LYS B O 1 ATOM 2096 C CB . LYS B 2 121 ? -6.340 0.860 57.007 1.00 24.43 ? 121 LYS B CB 1 ATOM 2097 C CG . LYS B 2 121 ? -7.541 1.805 56.986 1.00 22.29 ? 121 LYS B CG 1 ATOM 2098 C CD . LYS B 2 121 ? -7.059 3.188 56.516 1.00 28.18 ? 121 LYS B CD 1 ATOM 2099 C CE . LYS B 2 121 ? -8.192 4.156 56.195 1.00 27.94 ? 121 LYS B CE 1 ATOM 2100 N NZ . LYS B 2 121 ? -7.658 5.492 55.768 1.00 24.11 ? 121 LYS B NZ 1 ATOM 2101 N N . PHE B 2 122 ? -9.002 -1.086 57.234 1.00 20.97 ? 122 PHE B N 1 ATOM 2102 C CA . PHE B 2 122 ? -10.278 -1.420 56.618 1.00 29.34 ? 122 PHE B CA 1 ATOM 2103 C C . PHE B 2 122 ? -11.416 -0.798 57.402 1.00 31.08 ? 122 PHE B C 1 ATOM 2104 O O . PHE B 2 122 ? -11.272 -0.530 58.601 1.00 27.84 ? 122 PHE B O 1 ATOM 2105 C CB . PHE B 2 122 ? -10.444 -2.943 56.474 1.00 28.59 ? 122 PHE B CB 1 ATOM 2106 C CG . PHE B 2 122 ? -10.641 -3.685 57.776 1.00 30.77 ? 122 PHE B CG 1 ATOM 2107 C CD1 . PHE B 2 122 ? -11.853 -3.628 58.458 1.00 29.49 ? 122 PHE B CD1 1 ATOM 2108 C CD2 . PHE B 2 122 ? -9.630 -4.495 58.283 1.00 29.78 ? 122 PHE B CD2 1 ATOM 2109 C CE1 . PHE B 2 122 ? -12.057 -4.375 59.623 1.00 27.00 ? 122 PHE B CE1 1 ATOM 2110 C CE2 . PHE B 2 122 ? -9.821 -5.245 59.446 1.00 32.95 ? 122 PHE B CE2 1 ATOM 2111 C CZ . PHE B 2 122 ? -11.031 -5.187 60.115 1.00 22.48 ? 122 PHE B CZ 1 ATOM 2112 N N . LEU B 2 123 ? -12.521 -0.526 56.706 1.00 24.97 ? 123 LEU B N 1 ATOM 2113 C CA . LEU B 2 123 ? -13.711 0.074 57.298 1.00 32.55 ? 123 LEU B CA 1 ATOM 2114 C C . LEU B 2 123 ? -14.458 -0.986 58.096 1.00 39.14 ? 123 LEU B C 1 ATOM 2115 O O . LEU B 2 123 ? -14.832 -2.030 57.565 1.00 33.32 ? 123 LEU B O 1 ATOM 2116 C CB . LEU B 2 123 ? -14.623 0.638 56.203 1.00 34.90 ? 123 LEU B CB 1 ATOM 2117 C CG . LEU B 2 123 ? -15.924 1.323 56.653 1.00 41.49 ? 123 LEU B CG 1 ATOM 2118 C CD1 . LEU B 2 123 ? -15.604 2.480 57.581 1.00 41.77 ? 123 LEU B CD1 1 ATOM 2119 C CD2 . LEU B 2 123 ? -16.699 1.824 55.442 1.00 41.47 ? 123 LEU B CD2 1 ATOM 2120 N N . THR B 2 124 ? -14.670 -0.717 59.377 1.00 39.56 ? 124 THR B N 1 ATOM 2121 C CA . THR B 2 124 ? -15.358 -1.666 60.240 1.00 44.39 ? 124 THR B CA 1 ATOM 2122 C C . THR B 2 124 ? -16.777 -1.963 59.742 1.00 42.50 ? 124 THR B C 1 ATOM 2123 O O . THR B 2 124 ? -17.169 -3.149 59.790 1.00 46.11 ? 124 THR B O 1 ATOM 2124 C CB . THR B 2 124 ? -15.406 -1.151 61.696 1.00 43.36 ? 124 THR B CB 1 ATOM 2125 O OG1 . THR B 2 124 ? -15.876 -2.198 62.552 1.00 54.10 ? 124 THR B OG1 1 ATOM 2126 C CG2 . THR B 2 124 ? -16.331 0.054 61.815 1.00 44.29 ? 124 THR B CG2 1 HETATM 2127 CL CL . CL C 3 . ? 7.415 26.324 32.705 1.00 26.62 ? 1304 CL A CL 1 HETATM 2128 C C1 . GOL D 4 . ? -2.961 14.779 43.644 1.00 18.64 ? 1300 GOL A C1 1 HETATM 2129 O O1 . GOL D 4 . ? -1.790 13.979 43.765 1.00 24.57 ? 1300 GOL A O1 1 HETATM 2130 C C2 . GOL D 4 . ? -3.244 15.131 42.191 1.00 27.12 ? 1300 GOL A C2 1 HETATM 2131 O O2 . GOL D 4 . ? -2.156 15.853 41.654 1.00 26.41 ? 1300 GOL A O2 1 HETATM 2132 C C3 . GOL D 4 . ? -4.521 15.942 42.103 1.00 27.10 ? 1300 GOL A C3 1 HETATM 2133 O O3 . GOL D 4 . ? -4.815 16.263 40.748 1.00 36.35 ? 1300 GOL A O3 1 HETATM 2134 C C1 . GOL E 4 . ? 14.728 8.709 54.674 1.00 39.77 ? 1301 GOL A C1 1 HETATM 2135 O O1 . GOL E 4 . ? 14.583 10.098 54.456 1.00 29.99 ? 1301 GOL A O1 1 HETATM 2136 C C2 . GOL E 4 . ? 15.287 8.419 56.065 1.00 53.03 ? 1301 GOL A C2 1 HETATM 2137 O O2 . GOL E 4 . ? 16.709 8.464 56.045 1.00 49.28 ? 1301 GOL A O2 1 HETATM 2138 C C3 . GOL E 4 . ? 14.768 7.068 56.543 1.00 53.72 ? 1301 GOL A C3 1 HETATM 2139 O O3 . GOL E 4 . ? 15.197 6.756 57.866 1.00 61.38 ? 1301 GOL A O3 1 HETATM 2140 C C1 . GOL F 4 . ? 28.712 28.265 16.944 1.00 50.54 ? 1302 GOL A C1 1 HETATM 2141 O O1 . GOL F 4 . ? 29.026 29.644 16.897 1.00 48.72 ? 1302 GOL A O1 1 HETATM 2142 C C2 . GOL F 4 . ? 29.773 27.472 17.698 1.00 47.19 ? 1302 GOL A C2 1 HETATM 2143 O O2 . GOL F 4 . ? 31.030 27.602 17.051 1.00 56.84 ? 1302 GOL A O2 1 HETATM 2144 C C3 . GOL F 4 . ? 29.355 26.023 17.780 1.00 40.60 ? 1302 GOL A C3 1 HETATM 2145 O O3 . GOL F 4 . ? 30.295 25.248 18.509 1.00 52.91 ? 1302 GOL A O3 1 HETATM 2146 C C1 . NAG G 5 . ? 7.248 -8.715 45.355 1.00 48.41 ? 1022 NAG B C1 1 HETATM 2147 C C2 . NAG G 5 . ? 7.763 -8.486 43.924 1.00 52.60 ? 1022 NAG B C2 1 HETATM 2148 C C3 . NAG G 5 . ? 6.979 -9.377 42.968 1.00 56.78 ? 1022 NAG B C3 1 HETATM 2149 C C4 . NAG G 5 . ? 7.183 -10.819 43.386 1.00 55.85 ? 1022 NAG B C4 1 HETATM 2150 C C5 . NAG G 5 . ? 6.681 -10.994 44.823 1.00 58.42 ? 1022 NAG B C5 1 HETATM 2151 C C6 . NAG G 5 . ? 6.884 -12.406 45.337 1.00 57.51 ? 1022 NAG B C6 1 HETATM 2152 C C7 . NAG G 5 . ? 8.633 -6.399 43.095 1.00 56.50 ? 1022 NAG B C7 1 HETATM 2153 C C8 . NAG G 5 . ? 8.389 -4.945 42.726 1.00 58.63 ? 1022 NAG B C8 1 HETATM 2154 N N2 . NAG G 5 . ? 7.596 -7.094 43.552 1.00 55.07 ? 1022 NAG B N2 1 HETATM 2155 O O3 . NAG G 5 . ? 7.447 -9.187 41.641 1.00 58.05 ? 1022 NAG B O3 1 HETATM 2156 O O4 . NAG G 5 . ? 6.466 -11.682 42.513 1.00 61.62 ? 1022 NAG B O4 1 HETATM 2157 O O5 . NAG G 5 . ? 7.414 -10.103 45.713 1.00 52.86 ? 1022 NAG B O5 1 HETATM 2158 O O6 . NAG G 5 . ? 8.155 -12.550 45.956 1.00 59.65 ? 1022 NAG B O6 1 HETATM 2159 O O7 . NAG G 5 . ? 9.760 -6.884 42.964 1.00 56.79 ? 1022 NAG B O7 1 HETATM 2160 C C1 . GOL H 4 . ? 15.701 7.300 45.228 1.00 59.44 ? 1303 GOL B C1 1 HETATM 2161 O O1 . GOL H 4 . ? 16.402 6.107 44.902 1.00 55.46 ? 1303 GOL B O1 1 HETATM 2162 C C2 . GOL H 4 . ? 16.262 8.551 44.519 1.00 60.57 ? 1303 GOL B C2 1 HETATM 2163 O O2 . GOL H 4 . ? 16.837 9.408 45.501 1.00 65.54 ? 1303 GOL B O2 1 HETATM 2164 C C3 . GOL H 4 . ? 15.122 9.240 43.790 1.00 59.02 ? 1303 GOL B C3 1 HETATM 2165 O O3 . GOL H 4 . ? 15.501 10.440 43.127 1.00 41.64 ? 1303 GOL B O3 1 HETATM 2166 O O . HOH I 6 . ? 0.042 18.698 47.395 1.00 17.48 ? 1305 HOH A O 1 HETATM 2167 O O . HOH I 6 . ? 16.301 12.131 58.608 1.00 22.28 ? 1306 HOH A O 1 HETATM 2168 O O . HOH I 6 . ? 17.161 29.143 45.544 1.00 18.68 ? 1307 HOH A O 1 HETATM 2169 O O . HOH I 6 . ? 4.123 17.519 51.953 1.00 18.72 ? 1308 HOH A O 1 HETATM 2170 O O . HOH I 6 . ? 6.572 12.470 46.056 1.00 14.98 ? 1309 HOH A O 1 HETATM 2171 O O . HOH I 6 . ? 21.407 14.695 27.513 1.00 15.71 ? 1310 HOH A O 1 HETATM 2172 O O . HOH I 6 . ? -6.509 2.144 52.810 1.00 23.66 ? 1311 HOH A O 1 HETATM 2173 O O . HOH I 6 . ? 6.400 14.231 43.997 1.00 16.67 ? 1312 HOH A O 1 HETATM 2174 O O . HOH I 6 . ? 15.476 7.745 34.539 1.00 20.12 ? 1313 HOH A O 1 HETATM 2175 O O . HOH I 6 . ? -4.208 16.885 46.041 1.00 22.12 ? 1314 HOH A O 1 HETATM 2176 O O . HOH I 6 . ? 14.588 27.771 24.016 1.00 25.03 ? 1315 HOH A O 1 HETATM 2177 O O . HOH I 6 . ? 9.531 19.312 43.275 1.00 17.01 ? 1316 HOH A O 1 HETATM 2178 O O . HOH I 6 . ? 18.933 13.284 27.357 1.00 20.00 ? 1317 HOH A O 1 HETATM 2179 O O . HOH I 6 . ? 28.274 13.786 29.964 1.00 22.44 ? 1318 HOH A O 1 HETATM 2180 O O . HOH I 6 . ? 28.707 26.126 24.848 1.00 19.36 ? 1319 HOH A O 1 HETATM 2181 O O . HOH I 6 . ? -1.891 16.821 47.563 1.00 22.91 ? 1320 HOH A O 1 HETATM 2182 O O . HOH I 6 . ? 20.071 4.207 30.510 1.00 25.42 ? 1321 HOH A O 1 HETATM 2183 O O . HOH I 6 . ? 18.939 7.880 35.401 1.00 28.55 ? 1322 HOH A O 1 HETATM 2184 O O . HOH I 6 . ? 28.615 25.229 27.404 1.00 24.23 ? 1323 HOH A O 1 HETATM 2185 O O . HOH I 6 . ? 12.381 29.710 44.354 1.00 29.07 ? 1324 HOH A O 1 HETATM 2186 O O . HOH I 6 . ? 16.172 17.882 48.296 1.00 25.20 ? 1325 HOH A O 1 HETATM 2187 O O . HOH I 6 . ? 29.315 28.334 33.922 1.00 27.41 ? 1326 HOH A O 1 HETATM 2188 O O . HOH I 6 . ? -1.230 18.300 52.686 1.00 29.65 ? 1327 HOH A O 1 HETATM 2189 O O . HOH I 6 . ? 18.919 8.666 27.167 1.00 22.73 ? 1328 HOH A O 1 HETATM 2190 O O . HOH I 6 . ? 4.672 20.688 42.681 1.00 24.57 ? 1329 HOH A O 1 HETATM 2191 O O . HOH I 6 . ? 9.804 30.672 31.850 1.00 29.55 ? 1330 HOH A O 1 HETATM 2192 O O . HOH I 6 . ? -4.777 12.204 51.177 1.00 20.94 ? 1331 HOH A O 1 HETATM 2193 O O . HOH I 6 . ? 10.862 32.197 34.048 1.00 26.24 ? 1332 HOH A O 1 HETATM 2194 O O . HOH I 6 . ? 0.292 19.553 35.312 1.00 23.94 ? 1333 HOH A O 1 HETATM 2195 O O . HOH I 6 . ? 11.153 30.878 36.474 1.00 22.69 ? 1334 HOH A O 1 HETATM 2196 O O . HOH I 6 . ? -6.467 13.874 44.258 1.00 22.72 ? 1335 HOH A O 1 HETATM 2197 O O . HOH I 6 . ? 12.523 33.414 26.936 1.00 22.80 ? 1336 HOH A O 1 HETATM 2198 O O . HOH I 6 . ? 12.235 21.825 49.077 1.00 32.76 ? 1337 HOH A O 1 HETATM 2199 O O . HOH I 6 . ? 14.985 10.908 51.953 1.00 27.65 ? 1338 HOH A O 1 HETATM 2200 O O . HOH I 6 . ? 8.331 29.027 33.802 1.00 24.30 ? 1339 HOH A O 1 HETATM 2201 O O . HOH I 6 . ? 10.268 11.051 46.832 1.00 25.72 ? 1340 HOH A O 1 HETATM 2202 O O . HOH I 6 . ? 30.182 22.982 27.618 1.00 27.32 ? 1341 HOH A O 1 HETATM 2203 O O . HOH I 6 . ? 18.729 12.648 57.114 1.00 27.30 ? 1342 HOH A O 1 HETATM 2204 O O . HOH I 6 . ? 30.271 29.942 19.975 1.00 24.96 ? 1343 HOH A O 1 HETATM 2205 O O . HOH I 6 . ? 23.756 30.247 37.776 1.00 25.50 ? 1344 HOH A O 1 HETATM 2206 O O . HOH I 6 . ? -2.695 22.829 39.870 1.00 31.42 ? 1345 HOH A O 1 HETATM 2207 O O . HOH I 6 . ? 15.199 11.432 47.935 1.00 29.93 ? 1346 HOH A O 1 HETATM 2208 O O . HOH I 6 . ? 13.928 35.741 26.922 1.00 26.91 ? 1347 HOH A O 1 HETATM 2209 O O . HOH I 6 . ? 32.144 33.423 19.371 1.00 24.77 ? 1348 HOH A O 1 HETATM 2210 O O . HOH I 6 . ? 8.727 24.022 44.233 1.00 28.42 ? 1349 HOH A O 1 HETATM 2211 O O . HOH I 6 . ? 4.686 21.626 40.240 1.00 25.48 ? 1350 HOH A O 1 HETATM 2212 O O . HOH I 6 . ? 7.165 20.506 44.123 1.00 42.50 ? 1351 HOH A O 1 HETATM 2213 O O . HOH I 6 . ? 14.739 7.775 37.199 1.00 32.70 ? 1352 HOH A O 1 HETATM 2214 O O . HOH I 6 . ? 14.415 30.549 21.476 1.00 30.95 ? 1353 HOH A O 1 HETATM 2215 O O . HOH I 6 . ? -11.579 10.688 48.840 1.00 30.85 ? 1354 HOH A O 1 HETATM 2216 O O . HOH I 6 . ? -4.573 6.052 40.860 1.00 30.54 ? 1355 HOH A O 1 HETATM 2217 O O . HOH I 6 . ? 18.113 11.657 44.093 1.00 38.46 ? 1356 HOH A O 1 HETATM 2218 O O . HOH I 6 . ? 1.440 17.581 58.374 1.00 43.96 ? 1357 HOH A O 1 HETATM 2219 O O . HOH I 6 . ? 18.218 32.334 45.624 1.00 37.72 ? 1358 HOH A O 1 HETATM 2220 O O . HOH I 6 . ? -2.177 18.480 35.171 1.00 28.62 ? 1359 HOH A O 1 HETATM 2221 O O . HOH I 6 . ? 15.883 15.304 47.586 1.00 32.75 ? 1360 HOH A O 1 HETATM 2222 O O . HOH I 6 . ? 18.061 7.784 38.132 1.00 38.56 ? 1361 HOH A O 1 HETATM 2223 O O . HOH I 6 . ? 28.800 29.000 31.368 1.00 32.11 ? 1362 HOH A O 1 HETATM 2224 O O . HOH I 6 . ? 31.078 20.715 30.162 1.00 35.31 ? 1363 HOH A O 1 HETATM 2225 O O . HOH I 6 . ? 0.736 26.196 31.978 1.00 40.42 ? 1364 HOH A O 1 HETATM 2226 O O . HOH I 6 . ? 20.237 30.160 45.469 1.00 34.63 ? 1365 HOH A O 1 HETATM 2227 O O . HOH I 6 . ? 14.684 27.321 21.323 1.00 33.15 ? 1366 HOH A O 1 HETATM 2228 O O . HOH I 6 . ? -2.603 13.272 37.546 1.00 35.21 ? 1367 HOH A O 1 HETATM 2229 O O . HOH I 6 . ? 10.579 18.414 47.937 1.00 33.69 ? 1368 HOH A O 1 HETATM 2230 O O . HOH I 6 . ? 14.877 10.120 19.453 1.00 41.60 ? 1369 HOH A O 1 HETATM 2231 O O . HOH I 6 . ? 10.810 20.054 50.106 1.00 33.52 ? 1370 HOH A O 1 HETATM 2232 O O . HOH I 6 . ? 1.493 18.060 55.476 1.00 32.09 ? 1371 HOH A O 1 HETATM 2233 O O . HOH I 6 . ? 20.906 10.446 24.591 1.00 27.92 ? 1372 HOH A O 1 HETATM 2234 O O . HOH I 6 . ? 1.554 18.848 52.335 1.00 28.18 ? 1373 HOH A O 1 HETATM 2235 O O . HOH I 6 . ? 18.084 11.089 54.815 1.00 27.26 ? 1374 HOH A O 1 HETATM 2236 O O . HOH I 6 . ? 15.161 21.502 18.907 1.00 41.46 ? 1375 HOH A O 1 HETATM 2237 O O . HOH I 6 . ? 28.269 18.659 22.651 1.00 30.54 ? 1376 HOH A O 1 HETATM 2238 O O . HOH I 6 . ? 10.213 34.125 28.612 1.00 28.73 ? 1377 HOH A O 1 HETATM 2239 O O . HOH I 6 . ? 14.612 14.189 50.301 1.00 34.35 ? 1378 HOH A O 1 HETATM 2240 O O . HOH I 6 . ? -3.894 18.689 39.806 1.00 34.46 ? 1379 HOH A O 1 HETATM 2241 O O . HOH I 6 . ? 9.034 25.819 49.840 1.00 40.62 ? 1380 HOH A O 1 HETATM 2242 O O . HOH I 6 . ? 24.468 35.853 28.721 1.00 38.90 ? 1381 HOH A O 1 HETATM 2243 O O . HOH I 6 . ? 16.139 33.841 19.775 1.00 37.62 ? 1382 HOH A O 1 HETATM 2244 O O . HOH I 6 . ? 24.368 14.095 18.583 1.00 38.61 ? 1383 HOH A O 1 HETATM 2245 O O . HOH I 6 . ? -2.494 4.560 43.490 1.00 35.21 ? 1384 HOH A O 1 HETATM 2246 O O . HOH I 6 . ? 30.930 22.724 23.324 1.00 32.47 ? 1385 HOH A O 1 HETATM 2247 O O . HOH I 6 . ? 16.044 17.028 18.669 1.00 42.79 ? 1386 HOH A O 1 HETATM 2248 O O . HOH I 6 . ? -2.559 15.608 34.823 1.00 40.79 ? 1387 HOH A O 1 HETATM 2249 O O . HOH I 6 . ? 15.616 15.568 44.712 1.00 41.02 ? 1388 HOH A O 1 HETATM 2250 O O . HOH I 6 . ? 28.925 33.647 16.104 1.00 37.67 ? 1389 HOH A O 1 HETATM 2251 O O . HOH I 6 . ? -5.636 18.682 44.649 1.00 31.84 ? 1390 HOH A O 1 HETATM 2252 O O . HOH I 6 . ? 10.986 32.936 38.253 1.00 42.22 ? 1391 HOH A O 1 HETATM 2253 O O . HOH I 6 . ? 20.889 7.830 25.590 1.00 35.00 ? 1392 HOH A O 1 HETATM 2254 O O . HOH I 6 . ? -1.819 21.401 46.844 1.00 49.62 ? 1393 HOH A O 1 HETATM 2255 O O . HOH I 6 . ? 28.724 22.738 17.257 1.00 34.37 ? 1394 HOH A O 1 HETATM 2256 O O . HOH I 6 . ? 14.117 7.722 20.311 1.00 41.24 ? 1395 HOH A O 1 HETATM 2257 O O . HOH I 6 . ? 7.119 30.013 37.973 1.00 42.56 ? 1396 HOH A O 1 HETATM 2258 O O . HOH I 6 . ? 28.286 29.723 36.087 1.00 41.12 ? 1397 HOH A O 1 HETATM 2259 O O . HOH I 6 . ? 20.468 10.706 58.014 1.00 36.67 ? 1398 HOH A O 1 HETATM 2260 O O . HOH I 6 . ? 5.158 18.175 54.446 1.00 46.62 ? 1399 HOH A O 1 HETATM 2261 O O . HOH I 6 . ? 23.688 20.396 13.763 1.00 46.26 ? 1400 HOH A O 1 HETATM 2262 O O . HOH I 6 . ? -3.105 21.737 37.438 1.00 33.55 ? 1401 HOH A O 1 HETATM 2263 O O . HOH I 6 . ? 10.166 28.013 45.550 1.00 36.79 ? 1402 HOH A O 1 HETATM 2264 O O . HOH I 6 . ? 3.882 23.507 43.931 1.00 46.37 ? 1403 HOH A O 1 HETATM 2265 O O . HOH I 6 . ? 17.750 33.383 38.295 1.00 32.50 ? 1404 HOH A O 1 HETATM 2266 O O . HOH I 6 . ? 26.949 20.379 17.049 1.00 40.51 ? 1405 HOH A O 1 HETATM 2267 O O . HOH I 6 . ? 31.777 23.559 25.623 1.00 43.27 ? 1406 HOH A O 1 HETATM 2268 O O . HOH I 6 . ? 31.926 8.356 33.066 1.00 43.76 ? 1407 HOH A O 1 HETATM 2269 O O . HOH I 6 . ? 15.920 8.850 50.629 1.00 41.59 ? 1408 HOH A O 1 HETATM 2270 O O . HOH I 6 . ? 6.130 33.869 26.605 1.00 48.00 ? 1409 HOH A O 1 HETATM 2271 O O . HOH I 6 . ? 6.918 23.320 39.524 1.00 46.03 ? 1410 HOH A O 1 HETATM 2272 O O . HOH I 6 . ? 20.212 36.709 35.045 1.00 39.23 ? 1411 HOH A O 1 HETATM 2273 O O . HOH I 6 . ? 10.162 36.026 31.038 1.00 44.32 ? 1412 HOH A O 1 HETATM 2274 O O . HOH I 6 . ? 23.848 15.960 43.688 1.00 44.29 ? 1413 HOH A O 1 HETATM 2275 O O . HOH I 6 . ? 26.322 31.775 36.280 1.00 44.42 ? 1414 HOH A O 1 HETATM 2276 O O . HOH I 6 . ? 10.339 15.421 21.581 1.00 40.41 ? 1415 HOH A O 1 HETATM 2277 O O . HOH I 6 . ? 10.091 21.739 46.786 1.00 38.92 ? 1416 HOH A O 1 HETATM 2278 O O . HOH I 6 . ? 26.794 11.463 24.159 1.00 44.31 ? 1417 HOH A O 1 HETATM 2279 O O . HOH I 6 . ? 30.261 20.110 23.196 1.00 49.11 ? 1418 HOH A O 1 HETATM 2280 O O . HOH I 6 . ? 28.997 12.853 42.592 1.00 44.80 ? 1419 HOH A O 1 HETATM 2281 O O . HOH I 6 . ? -5.330 3.373 42.765 1.00 52.85 ? 1420 HOH A O 1 HETATM 2282 O O . HOH I 6 . ? 8.239 18.599 50.621 1.00 50.67 ? 1421 HOH A O 1 HETATM 2283 O O . HOH I 6 . ? -0.851 22.150 35.721 1.00 40.84 ? 1422 HOH A O 1 HETATM 2284 O O . HOH I 6 . ? 32.942 12.646 40.647 1.00 48.96 ? 1423 HOH A O 1 HETATM 2285 O O . HOH I 6 . ? 16.852 19.642 17.922 1.00 39.40 ? 1424 HOH A O 1 HETATM 2286 O O . HOH I 6 . ? 32.700 22.415 31.686 1.00 49.30 ? 1425 HOH A O 1 HETATM 2287 O O . HOH I 6 . ? -10.186 4.342 52.799 1.00 47.88 ? 1426 HOH A O 1 HETATM 2288 O O . HOH I 6 . ? -3.815 19.219 37.325 1.00 36.18 ? 1427 HOH A O 1 HETATM 2289 O O . HOH I 6 . ? 31.292 25.871 21.151 1.00 41.67 ? 1428 HOH A O 1 HETATM 2290 O O . HOH I 6 . ? 12.212 31.533 42.479 1.00 45.79 ? 1429 HOH A O 1 HETATM 2291 O O . HOH I 6 . ? 10.311 31.814 24.004 1.00 46.29 ? 1430 HOH A O 1 HETATM 2292 O O . HOH I 6 . ? 20.660 5.778 23.727 1.00 51.17 ? 1431 HOH A O 1 HETATM 2293 O O . HOH I 6 . ? -7.860 17.622 43.290 1.00 55.20 ? 1432 HOH A O 1 HETATM 2294 O O . HOH I 6 . ? 7.466 31.854 27.577 1.00 46.42 ? 1433 HOH A O 1 HETATM 2295 O O . HOH I 6 . ? 12.814 6.879 23.540 1.00 49.83 ? 1434 HOH A O 1 HETATM 2296 O O . HOH I 6 . ? 8.877 32.059 29.814 1.00 38.87 ? 1435 HOH A O 1 HETATM 2297 O O . HOH I 6 . ? 15.920 9.659 16.769 1.00 46.05 ? 1436 HOH A O 1 HETATM 2298 O O . HOH I 6 . ? 30.317 36.015 17.854 1.00 50.91 ? 1437 HOH A O 1 HETATM 2299 O O . HOH I 6 . ? 5.893 30.509 34.013 1.00 55.85 ? 1438 HOH A O 1 HETATM 2300 O O . HOH I 6 . ? 9.073 29.143 36.265 1.00 30.43 ? 1439 HOH A O 1 HETATM 2301 O O . HOH I 6 . ? 20.391 4.015 27.586 1.00 51.65 ? 1440 HOH A O 1 HETATM 2302 O O . HOH I 6 . ? 3.393 26.506 38.121 1.00 54.49 ? 1441 HOH A O 1 HETATM 2303 O O . HOH I 6 . ? 31.412 27.362 28.343 1.00 50.45 ? 1442 HOH A O 1 HETATM 2304 O O . HOH I 6 . ? 30.684 25.371 31.448 1.00 52.11 ? 1443 HOH A O 1 HETATM 2305 O O . HOH I 6 . ? -12.674 8.764 45.158 1.00 53.19 ? 1444 HOH A O 1 HETATM 2306 O O . HOH I 6 . ? -2.671 19.296 50.837 1.00 48.21 ? 1445 HOH A O 1 HETATM 2307 O O . HOH J 6 . ? 10.362 -1.247 57.871 1.00 18.25 ? 1304 HOH B O 1 HETATM 2308 O O . HOH J 6 . ? 14.691 25.265 25.332 1.00 17.92 ? 1305 HOH B O 1 HETATM 2309 O O . HOH J 6 . ? 18.426 11.128 25.665 1.00 25.44 ? 1306 HOH B O 1 HETATM 2310 O O . HOH J 6 . ? -7.599 3.104 69.580 1.00 17.07 ? 1307 HOH B O 1 HETATM 2311 O O . HOH J 6 . ? 5.345 20.890 26.667 1.00 27.52 ? 1308 HOH B O 1 HETATM 2312 O O . HOH J 6 . ? -4.641 11.576 66.295 1.00 20.08 ? 1309 HOH B O 1 HETATM 2313 O O . HOH J 6 . ? -0.637 -2.957 65.178 1.00 28.47 ? 1310 HOH B O 1 HETATM 2314 O O . HOH J 6 . ? 7.097 23.391 31.601 1.00 21.85 ? 1311 HOH B O 1 HETATM 2315 O O . HOH J 6 . ? -8.730 -0.546 69.711 1.00 23.29 ? 1312 HOH B O 1 HETATM 2316 O O . HOH J 6 . ? 11.545 -8.493 58.921 1.00 37.35 ? 1313 HOH B O 1 HETATM 2317 O O . HOH J 6 . ? -3.576 -1.680 45.080 1.00 26.48 ? 1314 HOH B O 1 HETATM 2318 O O . HOH J 6 . ? 0.616 13.546 62.389 1.00 23.40 ? 1315 HOH B O 1 HETATM 2319 O O . HOH J 6 . ? 12.223 23.970 27.804 1.00 17.12 ? 1316 HOH B O 1 HETATM 2320 O O . HOH J 6 . ? -6.708 13.721 52.647 1.00 19.19 ? 1317 HOH B O 1 HETATM 2321 O O . HOH J 6 . ? -3.175 -3.225 66.341 1.00 22.74 ? 1318 HOH B O 1 HETATM 2322 O O . HOH J 6 . ? -1.252 2.991 45.169 1.00 25.59 ? 1319 HOH B O 1 HETATM 2323 O O . HOH J 6 . ? 0.628 -5.403 65.231 1.00 29.26 ? 1320 HOH B O 1 HETATM 2324 O O . HOH J 6 . ? 2.258 20.175 33.554 1.00 24.67 ? 1321 HOH B O 1 HETATM 2325 O O . HOH J 6 . ? 14.731 2.731 46.560 1.00 23.89 ? 1322 HOH B O 1 HETATM 2326 O O . HOH J 6 . ? 10.007 -1.090 41.530 1.00 26.52 ? 1323 HOH B O 1 HETATM 2327 O O . HOH J 6 . ? 3.803 10.087 34.853 1.00 30.55 ? 1324 HOH B O 1 HETATM 2328 O O . HOH J 6 . ? 9.807 15.584 24.268 1.00 24.08 ? 1325 HOH B O 1 HETATM 2329 O O . HOH J 6 . ? -8.500 0.171 53.403 1.00 28.08 ? 1326 HOH B O 1 HETATM 2330 O O . HOH J 6 . ? 6.991 5.774 40.448 1.00 28.49 ? 1327 HOH B O 1 HETATM 2331 O O . HOH J 6 . ? 3.719 22.985 27.122 1.00 29.25 ? 1328 HOH B O 1 HETATM 2332 O O . HOH J 6 . ? 12.623 8.700 45.111 1.00 27.79 ? 1329 HOH B O 1 HETATM 2333 O O . HOH J 6 . ? 13.247 24.752 21.726 1.00 27.86 ? 1330 HOH B O 1 HETATM 2334 O O . HOH J 6 . ? 11.245 -3.223 63.182 1.00 36.28 ? 1331 HOH B O 1 HETATM 2335 O O . HOH J 6 . ? 3.920 -8.117 63.247 1.00 39.21 ? 1332 HOH B O 1 HETATM 2336 O O . HOH J 6 . ? 14.847 14.385 60.144 1.00 36.89 ? 1333 HOH B O 1 HETATM 2337 O O . HOH J 6 . ? 0.958 -1.802 67.168 1.00 26.15 ? 1334 HOH B O 1 HETATM 2338 O O . HOH J 6 . ? 2.854 15.310 60.557 1.00 33.55 ? 1335 HOH B O 1 HETATM 2339 O O . HOH J 6 . ? 7.902 16.193 59.144 1.00 28.26 ? 1336 HOH B O 1 HETATM 2340 O O . HOH J 6 . ? 12.102 1.819 34.568 1.00 27.63 ? 1337 HOH B O 1 HETATM 2341 O O . HOH J 6 . ? -3.201 8.740 68.932 1.00 29.62 ? 1338 HOH B O 1 HETATM 2342 O O . HOH J 6 . ? 13.561 8.894 48.205 1.00 32.94 ? 1339 HOH B O 1 HETATM 2343 O O . HOH J 6 . ? 5.444 7.352 68.253 1.00 31.61 ? 1340 HOH B O 1 HETATM 2344 O O . HOH J 6 . ? -9.412 8.316 57.035 1.00 39.85 ? 1341 HOH B O 1 HETATM 2345 O O . HOH J 6 . ? 3.394 13.539 30.570 1.00 33.78 ? 1342 HOH B O 1 HETATM 2346 O O . HOH J 6 . ? 6.593 11.147 66.170 1.00 30.17 ? 1343 HOH B O 1 HETATM 2347 O O . HOH J 6 . ? -10.348 6.196 55.079 1.00 40.09 ? 1344 HOH B O 1 HETATM 2348 O O . HOH J 6 . ? 14.838 5.996 48.137 1.00 34.30 ? 1345 HOH B O 1 HETATM 2349 O O . HOH J 6 . ? 2.561 -6.047 67.295 1.00 39.66 ? 1346 HOH B O 1 HETATM 2350 O O . HOH J 6 . ? 13.408 -6.729 48.707 1.00 38.33 ? 1347 HOH B O 1 HETATM 2351 O O . HOH J 6 . ? 14.513 13.065 62.480 1.00 30.32 ? 1348 HOH B O 1 HETATM 2352 O O . HOH J 6 . ? 10.605 -2.459 60.263 1.00 36.83 ? 1349 HOH B O 1 HETATM 2353 O O . HOH J 6 . ? -1.711 -6.883 66.220 1.00 33.40 ? 1350 HOH B O 1 HETATM 2354 O O . HOH J 6 . ? 12.723 5.420 62.356 1.00 48.59 ? 1351 HOH B O 1 HETATM 2355 O O . HOH J 6 . ? 4.997 15.434 62.083 1.00 33.68 ? 1352 HOH B O 1 HETATM 2356 O O . HOH J 6 . ? 9.327 4.979 67.070 1.00 33.39 ? 1353 HOH B O 1 HETATM 2357 O O . HOH J 6 . ? 10.724 8.376 23.964 1.00 29.07 ? 1354 HOH B O 1 HETATM 2358 O O . HOH J 6 . ? -12.296 -0.838 53.948 1.00 31.82 ? 1355 HOH B O 1 HETATM 2359 O O . HOH J 6 . ? -13.441 0.928 64.549 1.00 35.15 ? 1356 HOH B O 1 HETATM 2360 O O . HOH J 6 . ? -10.631 1.515 54.490 1.00 35.21 ? 1357 HOH B O 1 HETATM 2361 O O . HOH J 6 . ? 12.216 1.872 54.526 1.00 33.64 ? 1358 HOH B O 1 HETATM 2362 O O . HOH J 6 . ? -2.457 0.781 43.971 1.00 34.33 ? 1359 HOH B O 1 HETATM 2363 O O . HOH J 6 . ? 12.437 -0.631 35.161 1.00 39.56 ? 1360 HOH B O 1 HETATM 2364 O O . HOH J 6 . ? 1.676 7.420 34.288 1.00 38.64 ? 1361 HOH B O 1 HETATM 2365 O O . HOH J 6 . ? 7.053 28.308 30.299 1.00 36.39 ? 1362 HOH B O 1 HETATM 2366 O O . HOH J 6 . ? -9.824 -0.513 51.021 1.00 33.79 ? 1363 HOH B O 1 HETATM 2367 O O . HOH J 6 . ? 17.837 2.894 29.322 1.00 34.01 ? 1364 HOH B O 1 HETATM 2368 O O . HOH J 6 . ? 4.593 9.443 66.768 1.00 31.69 ? 1365 HOH B O 1 HETATM 2369 O O . HOH J 6 . ? -2.785 15.893 64.448 1.00 40.08 ? 1366 HOH B O 1 HETATM 2370 O O . HOH J 6 . ? -0.895 -6.506 45.168 1.00 44.42 ? 1367 HOH B O 1 HETATM 2371 O O . HOH J 6 . ? 7.254 20.806 19.297 1.00 47.96 ? 1368 HOH B O 1 HETATM 2372 O O . HOH J 6 . ? 5.776 10.472 25.186 1.00 44.21 ? 1369 HOH B O 1 HETATM 2373 O O . HOH J 6 . ? 2.558 22.150 23.917 1.00 52.25 ? 1370 HOH B O 1 HETATM 2374 O O . HOH J 6 . ? -0.771 22.808 32.169 1.00 45.09 ? 1371 HOH B O 1 HETATM 2375 O O . HOH J 6 . ? 9.725 1.567 68.633 1.00 38.72 ? 1372 HOH B O 1 HETATM 2376 O O . HOH J 6 . ? -3.385 13.900 66.624 1.00 37.85 ? 1373 HOH B O 1 HETATM 2377 O O . HOH J 6 . ? 4.470 -2.009 41.395 1.00 47.81 ? 1374 HOH B O 1 HETATM 2378 O O . HOH J 6 . ? -9.431 -3.179 69.223 1.00 42.61 ? 1375 HOH B O 1 HETATM 2379 O O . HOH J 6 . ? -14.511 -0.680 52.437 1.00 40.59 ? 1376 HOH B O 1 HETATM 2380 O O . HOH J 6 . ? -4.787 18.119 65.127 1.00 39.00 ? 1377 HOH B O 1 HETATM 2381 O O . HOH J 6 . ? -2.185 3.558 40.963 1.00 46.78 ? 1378 HOH B O 1 HETATM 2382 O O . HOH J 6 . ? -9.475 -5.351 50.182 1.00 43.14 ? 1379 HOH B O 1 HETATM 2383 O O . HOH J 6 . ? -8.620 -10.865 61.109 1.00 50.29 ? 1380 HOH B O 1 HETATM 2384 O O . HOH J 6 . ? 2.000 10.109 66.563 1.00 38.34 ? 1381 HOH B O 1 HETATM 2385 O O . HOH J 6 . ? -8.177 -11.551 64.305 1.00 38.66 ? 1382 HOH B O 1 HETATM 2386 O O . HOH J 6 . ? -10.217 6.170 60.634 1.00 40.40 ? 1383 HOH B O 1 HETATM 2387 O O . HOH J 6 . ? 11.017 -7.744 46.106 1.00 35.77 ? 1384 HOH B O 1 HETATM 2388 O O . HOH J 6 . ? 8.981 17.565 20.644 1.00 38.79 ? 1385 HOH B O 1 HETATM 2389 O O . HOH J 6 . ? 14.680 17.952 64.716 1.00 46.32 ? 1386 HOH B O 1 HETATM 2390 O O . HOH J 6 . ? 3.653 1.799 39.743 1.00 43.87 ? 1387 HOH B O 1 HETATM 2391 O O . HOH J 6 . ? 4.407 15.100 64.693 1.00 48.09 ? 1388 HOH B O 1 HETATM 2392 O O . HOH J 6 . ? 1.440 26.445 27.974 1.00 48.38 ? 1389 HOH B O 1 HETATM 2393 O O . HOH J 6 . ? -10.215 -11.284 52.601 1.00 48.09 ? 1390 HOH B O 1 HETATM 2394 O O . HOH J 6 . ? -12.899 3.958 54.222 1.00 48.86 ? 1391 HOH B O 1 HETATM 2395 O O . HOH J 6 . ? -14.497 -1.790 65.946 1.00 45.05 ? 1392 HOH B O 1 HETATM 2396 O O . HOH J 6 . ? 13.245 3.370 60.526 1.00 50.59 ? 1393 HOH B O 1 HETATM 2397 O O . HOH J 6 . ? 5.504 2.890 71.886 1.00 39.99 ? 1394 HOH B O 1 HETATM 2398 O O . HOH J 6 . ? -11.915 -2.891 69.058 1.00 38.76 ? 1395 HOH B O 1 HETATM 2399 O O . HOH J 6 . ? 7.791 5.780 38.030 1.00 42.39 ? 1396 HOH B O 1 HETATM 2400 O O . HOH J 6 . ? 9.642 -1.518 35.783 1.00 49.55 ? 1397 HOH B O 1 HETATM 2401 O O . HOH J 6 . ? -15.038 -4.898 50.266 1.00 43.82 ? 1398 HOH B O 1 HETATM 2402 O O . HOH J 6 . ? 3.691 4.173 70.445 1.00 45.50 ? 1399 HOH B O 1 HETATM 2403 O O . HOH J 6 . ? 8.696 6.459 31.959 1.00 47.24 ? 1400 HOH B O 1 HETATM 2404 O O . HOH J 6 . ? 1.816 13.894 28.456 1.00 47.42 ? 1401 HOH B O 1 HETATM 2405 O O . HOH J 6 . ? 18.314 -2.129 49.690 1.00 46.55 ? 1402 HOH B O 1 HETATM 2406 O O . HOH J 6 . ? 14.198 1.133 58.174 1.00 46.97 ? 1403 HOH B O 1 HETATM 2407 O O . HOH J 6 . ? -16.251 6.782 57.877 1.00 52.52 ? 1404 HOH B O 1 HETATM 2408 O O . HOH J 6 . ? 15.336 -3.966 51.094 1.00 41.45 ? 1405 HOH B O 1 HETATM 2409 O O . HOH J 6 . ? 5.553 -13.833 55.762 1.00 49.12 ? 1406 HOH B O 1 HETATM 2410 O O . HOH J 6 . ? 1.751 14.261 64.502 1.00 35.44 ? 1407 HOH B O 1 HETATM 2411 O O . HOH J 6 . ? 9.412 -1.524 69.956 1.00 55.84 ? 1408 HOH B O 1 HETATM 2412 O O . HOH J 6 . ? -12.865 -6.154 49.763 1.00 50.07 ? 1409 HOH B O 1 HETATM 2413 O O . HOH J 6 . ? 12.923 17.953 62.169 1.00 45.25 ? 1410 HOH B O 1 HETATM 2414 O O . HOH J 6 . ? 8.801 29.461 23.244 1.00 50.99 ? 1411 HOH B O 1 HETATM 2415 O O . HOH J 6 . ? -7.696 -14.871 53.565 1.00 51.25 ? 1412 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 ASP 1 1 ? ? ? A . n A 1 2 PHE 2 2 ? ? ? A . n A 1 3 ASP 3 3 3 ASP ASP A . n A 1 4 CYS 4 4 4 CYS CYS A . n A 1 5 PRO 5 5 5 PRO PRO A . n A 1 6 SER 6 6 6 SER SER A . n A 1 7 ASP 7 7 7 ASP ASP A . n A 1 8 TRP 8 8 8 TRP TRP A . n A 1 9 THR 9 9 9 THR THR A . n A 1 10 ALA 10 10 10 ALA ALA A . n A 1 11 TYR 11 11 11 TYR TYR A . n A 1 12 ASP 12 12 12 ASP ASP A . n A 1 13 GLN 13 13 13 GLN GLN A . n A 1 14 HIS 14 14 14 HIS HIS A . n A 1 15 CYS 15 15 15 CYS CYS A . n A 1 16 TYR 16 16 16 TYR TYR A . n A 1 17 LEU 17 17 17 LEU LEU A . n A 1 18 ALA 18 18 18 ALA ALA A . n A 1 19 ILE 19 19 19 ILE ILE A . n A 1 20 GLY 20 20 20 GLY GLY A . n A 1 21 GLU 21 21 21 GLU GLU A . n A 1 22 PRO 22 22 22 PRO PRO A . n A 1 23 GLN 23 23 23 GLN GLN A . n A 1 24 ASN 24 24 24 ASN ASN A . n A 1 25 TRP 25 25 25 TRP TRP A . n A 1 26 TYR 26 26 26 TYR TYR A . n A 1 27 GLU 27 27 27 GLU GLU A . n A 1 28 ALA 28 28 28 ALA ALA A . n A 1 29 GLU 29 29 29 GLU GLU A . n A 1 30 ARG 30 30 30 ARG ARG A . n A 1 31 PHE 31 31 31 PHE PHE A . n A 1 32 CYS 32 32 32 CYS CYS A . n A 1 33 THR 33 33 33 THR THR A . n A 1 34 GLU 34 34 34 GLU GLU A . n A 1 35 GLN 35 35 35 GLN GLN A . n A 1 36 ALA 36 36 36 ALA ALA A . n A 1 37 LYS 37 37 37 LYS LYS A . n A 1 38 ASP 38 38 38 ASP ASP A . n A 1 39 GLY 39 39 39 GLY GLY A . n A 1 40 HIS 40 40 40 HIS HIS A . n A 1 41 LEU 41 41 41 LEU LEU A . n A 1 42 VAL 42 42 42 VAL VAL A . n A 1 43 SER 43 43 43 SER SER A . n A 1 44 ILE 44 44 44 ILE ILE A . n A 1 45 GLN 45 45 45 GLN GLN A . n A 1 46 SER 46 46 46 SER SER A . n A 1 47 ARG 47 47 47 ARG ARG A . n A 1 48 GLU 48 48 48 GLU GLU A . n A 1 49 GLU 49 49 49 GLU GLU A . n A 1 50 GLY 50 50 50 GLY GLY A . n A 1 51 ASN 51 51 51 ASN ASN A . n A 1 52 PHE 52 52 52 PHE PHE A . n A 1 53 VAL 53 53 53 VAL VAL A . n A 1 54 ALA 54 54 54 ALA ALA A . n A 1 55 GLN 55 55 55 GLN GLN A . n A 1 56 LEU 56 56 56 LEU LEU A . n A 1 57 VAL 57 57 57 VAL VAL A . n A 1 58 SER 58 58 58 SER SER A . n A 1 59 GLY 59 59 59 GLY GLY A . n A 1 60 PHE 60 60 60 PHE PHE A . n A 1 61 MET 61 61 61 MET MET A . n A 1 62 HIS 62 62 62 HIS HIS A . n A 1 63 ARG 63 63 63 ARG ARG A . n A 1 64 SER 64 64 64 SER SER A . n A 1 65 GLU 65 65 65 GLU GLU A . n A 1 66 ILE 66 66 66 ILE ILE A . n A 1 67 TYR 67 67 67 TYR TYR A . n A 1 68 VAL 68 68 68 VAL VAL A . n A 1 69 TRP 69 69 69 TRP TRP A . n A 1 70 ILE 70 70 70 ILE ILE A . n A 1 71 GLY 71 71 71 GLY GLY A . n A 1 72 LEU 72 72 72 LEU LEU A . n A 1 73 ARG 73 73 73 ARG ARG A . n A 1 74 ASP 74 74 74 ASP ASP A . n A 1 75 ARG 75 75 75 ARG ARG A . n A 1 76 ARG 76 76 76 ARG ARG A . n A 1 77 GLU 77 77 77 GLU GLU A . n A 1 78 GLU 78 78 78 GLU GLU A . n A 1 79 GLN 79 79 79 GLN GLN A . n A 1 80 GLN 80 80 80 GLN GLN A . n A 1 81 CYS 81 81 81 CYS CYS A . n A 1 82 ASN 82 82 82 ASN ASN A . n A 1 83 PRO 83 83 83 PRO PRO A . n A 1 84 GLU 84 84 84 GLU GLU A . n A 1 85 TRP 85 85 85 TRP TRP A . n A 1 86 ASN 86 86 86 ASN ASN A . n A 1 87 ASP 87 87 87 ASP ASP A . n A 1 88 GLY 88 88 88 GLY GLY A . n A 1 89 SER 89 89 89 SER SER A . n A 1 90 LYS 90 90 90 LYS LYS A . n A 1 91 ILE 91 91 91 ILE ILE A . n A 1 92 ILE 92 92 92 ILE ILE A . n A 1 93 TYR 93 93 93 TYR TYR A . n A 1 94 VAL 94 94 94 VAL VAL A . n A 1 95 ASN 95 95 95 ASN ASN A . n A 1 96 TRP 96 96 96 TRP TRP A . n A 1 97 LYS 97 97 97 LYS LYS A . n A 1 98 GLU 98 98 98 GLU GLU A . n A 1 99 GLY 99 99 99 GLY GLY A . n A 1 100 GLU 100 100 100 GLU GLU A . n A 1 101 SER 101 101 101 SER SER A . n A 1 102 LYS 102 102 102 LYS LYS A . n A 1 103 MET 103 103 103 MET MET A . n A 1 104 CYS 104 104 104 CYS CYS A . n A 1 105 GLN 105 105 105 GLN GLN A . n A 1 106 GLY 106 106 106 GLY GLY A . n A 1 107 LEU 107 107 107 LEU LEU A . n A 1 108 THR 108 108 108 THR THR A . n A 1 109 LYS 109 109 109 LYS LYS A . n A 1 110 TRP 110 110 110 TRP TRP A . n A 1 111 THR 111 111 111 THR THR A . n A 1 112 ASN 112 112 112 ASN ASN A . n A 1 113 PHE 113 113 113 PHE PHE A . n A 1 114 HIS 114 114 114 HIS HIS A . n A 1 115 ASP 115 115 115 ASP ASP A . n A 1 116 TRP 116 116 116 TRP TRP A . n A 1 117 ASN 117 117 117 ASN ASN A . n A 1 118 ASN 118 118 118 ASN ASN A . n A 1 119 ILE 119 119 119 ILE ILE A . n A 1 120 ASN 120 120 120 ASN ASN A . n A 1 121 CYS 121 121 121 CYS CYS A . n A 1 122 GLU 122 122 122 GLU GLU A . n A 1 123 ASP 123 123 123 ASP ASP A . n A 1 124 LEU 124 124 124 LEU LEU A . n A 1 125 TYR 125 125 125 TYR TYR A . n A 1 126 PRO 126 126 126 PRO PRO A . n A 1 127 PHE 127 127 127 PHE PHE A . n A 1 128 VAL 128 128 128 VAL VAL A . n A 1 129 CYS 129 129 129 CYS CYS A . n A 1 130 LYS 130 130 130 LYS LYS A . n A 1 131 PHE 131 131 131 PHE PHE A . n A 1 132 SER 132 132 132 SER SER A . n A 1 133 ALA 133 133 133 ALA ALA A . n A 1 134 VAL 134 134 ? ? ? A . n B 2 1 CYS 1 1 1 CYS CYS B . n B 2 2 PRO 2 2 2 PRO PRO B . n B 2 3 LEU 3 3 3 LEU LEU B . n B 2 4 GLY 4 4 4 GLY GLY B . n B 2 5 TRP 5 5 5 TRP TRP B . n B 2 6 SER 6 6 6 SER SER B . n B 2 7 SER 7 7 7 SER SER B . n B 2 8 PHE 8 8 8 PHE PHE B . n B 2 9 ASP 9 9 9 ASP ASP B . n B 2 10 GLN 10 10 10 GLN GLN B . n B 2 11 HIS 11 11 11 HIS HIS B . n B 2 12 CYS 12 12 12 CYS CYS B . n B 2 13 TYR 13 13 13 TYR TYR B . n B 2 14 LYS 14 14 14 LYS LYS B . n B 2 15 VAL 15 15 15 VAL VAL B . n B 2 16 PHE 16 16 16 PHE PHE B . n B 2 17 GLU 17 17 17 GLU GLU B . n B 2 18 PRO 18 18 18 PRO PRO B . n B 2 19 VAL 19 19 19 VAL VAL B . n B 2 20 LYS 20 20 20 LYS LYS B . n B 2 21 ASN 21 21 21 ASN ASN B . n B 2 22 TRP 22 22 22 TRP TRP B . n B 2 23 THR 23 23 23 THR THR B . n B 2 24 GLU 24 24 24 GLU GLU B . n B 2 25 ALA 25 25 25 ALA ALA B . n B 2 26 GLU 26 26 26 GLU GLU B . n B 2 27 GLU 27 27 27 GLU GLU B . n B 2 28 ILE 28 28 28 ILE ILE B . n B 2 29 CYS 29 29 29 CYS CYS B . n B 2 30 MET 30 30 30 MET MET B . n B 2 31 GLN 31 31 31 GLN GLN B . n B 2 32 GLN 32 32 32 GLN GLN B . n B 2 33 HIS 33 33 33 HIS HIS B . n B 2 34 LYS 34 34 34 LYS LYS B . n B 2 35 GLY 35 35 35 GLY GLY B . n B 2 36 SER 36 36 36 SER SER B . n B 2 37 ARG 37 37 37 ARG ARG B . n B 2 38 LEU 38 38 38 LEU LEU B . n B 2 39 ALA 39 39 39 ALA ALA B . n B 2 40 SER 40 40 40 SER SER B . n B 2 41 ILE 41 41 41 ILE ILE B . n B 2 42 HIS 42 42 42 HIS HIS B . n B 2 43 SER 43 43 43 SER SER B . n B 2 44 SER 44 44 44 SER SER B . n B 2 45 GLU 45 45 45 GLU GLU B . n B 2 46 GLU 46 46 46 GLU GLU B . n B 2 47 GLU 47 47 47 GLU GLU B . n B 2 48 ALA 48 48 48 ALA ALA B . n B 2 49 PHE 49 49 49 PHE PHE B . n B 2 50 VAL 50 50 50 VAL VAL B . n B 2 51 SER 51 51 51 SER SER B . n B 2 52 LYS 52 52 52 LYS LYS B . n B 2 53 LEU 53 53 53 LEU LEU B . n B 2 54 ALA 54 54 54 ALA ALA B . n B 2 55 SER 55 55 55 SER SER B . n B 2 56 LYS 56 56 56 LYS LYS B . n B 2 57 ALA 57 57 57 ALA ALA B . n B 2 58 LEU 58 58 58 LEU LEU B . n B 2 59 LYS 59 59 59 LYS LYS B . n B 2 60 PHE 60 60 60 PHE PHE B . n B 2 61 THR 61 61 61 THR THR B . n B 2 62 SER 62 62 62 SER SER B . n B 2 63 MET 63 63 63 MET MET B . n B 2 64 TRP 64 64 64 TRP TRP B . n B 2 65 ILE 65 65 65 ILE ILE B . n B 2 66 GLY 66 66 66 GLY GLY B . n B 2 67 LEU 67 67 67 LEU LEU B . n B 2 68 ASN 68 68 68 ASN ASN B . n B 2 69 ASN 69 69 69 ASN ASN B . n B 2 70 PRO 70 70 70 PRO PRO B . n B 2 71 TRP 71 71 71 TRP TRP B . n B 2 72 LYS 72 72 72 LYS LYS B . n B 2 73 ASP 73 73 73 ASP ASP B . n B 2 74 CYS 74 74 74 CYS CYS B . n B 2 75 LYS 75 75 75 LYS LYS B . n B 2 76 TRP 76 76 76 TRP TRP B . n B 2 77 GLU 77 77 77 GLU GLU B . n B 2 78 TRP 78 78 78 TRP TRP B . n B 2 79 SER 79 79 79 SER SER B . n B 2 80 ASP 80 80 80 ASP ASP B . n B 2 81 ASN 81 81 81 ASN ASN B . n B 2 82 ALA 82 82 82 ALA ALA B . n B 2 83 ARG 83 83 83 ARG ARG B . n B 2 84 PHE 84 84 84 PHE PHE B . n B 2 85 ASP 85 85 85 ASP ASP B . n B 2 86 TYR 86 86 86 TYR TYR B . n B 2 87 LYS 87 87 87 LYS LYS B . n B 2 88 ALA 88 88 88 ALA ALA B . n B 2 89 TRP 89 89 89 TRP TRP B . n B 2 90 LYS 90 90 90 LYS LYS B . n B 2 91 ARG 91 91 91 ARG ARG B . n B 2 92 ARG 92 92 92 ARG ARG B . n B 2 93 PRO 93 93 93 PRO PRO B . n B 2 94 TYR 94 94 94 TYR TYR B . n B 2 95 CYS 95 95 95 CYS CYS B . n B 2 96 THR 96 96 96 THR THR B . n B 2 97 VAL 97 97 97 VAL VAL B . n B 2 98 MET 98 98 98 MET MET B . n B 2 99 VAL 99 99 99 VAL VAL B . n B 2 100 VAL 100 100 100 VAL VAL B . n B 2 101 LYS 101 101 101 LYS LYS B . n B 2 102 PRO 102 102 102 PRO PRO B . n B 2 103 ASP 103 103 103 ASP ASP B . n B 2 104 ARG 104 104 104 ARG ARG B . n B 2 105 ILE 105 105 105 ILE ILE B . n B 2 106 PHE 106 106 106 PHE PHE B . n B 2 107 TRP 107 107 107 TRP TRP B . n B 2 108 PHE 108 108 108 PHE PHE B . n B 2 109 THR 109 109 109 THR THR B . n B 2 110 ARG 110 110 110 ARG ARG B . n B 2 111 GLY 111 111 111 GLY GLY B . n B 2 112 CYS 112 112 112 CYS CYS B . n B 2 113 GLU 113 113 113 GLU GLU B . n B 2 114 LYS 114 114 114 LYS LYS B . n B 2 115 SER 115 115 115 SER SER B . n B 2 116 VAL 116 116 116 VAL VAL B . n B 2 117 SER 117 117 117 SER SER B . n B 2 118 PHE 118 118 118 PHE PHE B . n B 2 119 VAL 119 119 119 VAL VAL B . n B 2 120 CYS 120 120 120 CYS CYS B . n B 2 121 LYS 121 121 121 LYS LYS B . n B 2 122 PHE 122 122 122 PHE PHE B . n B 2 123 LEU 123 123 123 LEU LEU B . n B 2 124 THR 124 124 124 THR THR B . n B 2 125 ASP 125 125 ? ? ? B . n B 2 126 PRO 126 126 ? ? ? B . n B 2 127 ALA 127 127 ? ? ? B . n B 2 128 VAL 128 128 ? ? ? 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 3 CL 1 1304 1304 CL CL A . D 4 GOL 1 1300 1300 GOL CRY A . E 4 GOL 1 1301 1301 GOL CRY A . F 4 GOL 1 1302 1302 GOL CRY A . G 5 NAG 1 1022 1022 NAG NAG B . H 4 GOL 1 1303 1303 GOL CRY B . I 6 HOH 1 1305 1 HOH HOH A . I 6 HOH 2 1306 2 HOH HOH A . I 6 HOH 3 1307 3 HOH HOH A . I 6 HOH 4 1308 4 HOH HOH A . I 6 HOH 5 1309 7 HOH HOH A . I 6 HOH 6 1310 8 HOH HOH A . I 6 HOH 7 1311 9 HOH HOH A . I 6 HOH 8 1312 10 HOH HOH A . I 6 HOH 9 1313 11 HOH HOH A . I 6 HOH 10 1314 12 HOH HOH A . I 6 HOH 11 1315 13 HOH HOH A . I 6 HOH 12 1316 14 HOH HOH A . I 6 HOH 13 1317 15 HOH HOH A . I 6 HOH 14 1318 17 HOH HOH A . I 6 HOH 15 1319 19 HOH HOH A . I 6 HOH 16 1320 22 HOH HOH A . I 6 HOH 17 1321 24 HOH HOH A . I 6 HOH 18 1322 28 HOH HOH A . I 6 HOH 19 1323 29 HOH HOH A . I 6 HOH 20 1324 31 HOH HOH A . I 6 HOH 21 1325 32 HOH HOH A . I 6 HOH 22 1326 33 HOH HOH A . I 6 HOH 23 1327 34 HOH HOH A . I 6 HOH 24 1328 37 HOH HOH A . I 6 HOH 25 1329 42 HOH HOH A . I 6 HOH 26 1330 45 HOH HOH A . I 6 HOH 27 1331 46 HOH HOH A . I 6 HOH 28 1332 47 HOH HOH A . I 6 HOH 29 1333 48 HOH HOH A . I 6 HOH 30 1334 49 HOH HOH A . I 6 HOH 31 1335 50 HOH HOH A . I 6 HOH 32 1336 51 HOH HOH A . I 6 HOH 33 1337 52 HOH HOH A . I 6 HOH 34 1338 53 HOH HOH A . I 6 HOH 35 1339 54 HOH HOH A . I 6 HOH 36 1340 55 HOH HOH A . I 6 HOH 37 1341 56 HOH HOH A . I 6 HOH 38 1342 57 HOH HOH A . I 6 HOH 39 1343 58 HOH HOH A . I 6 HOH 40 1344 60 HOH HOH A . I 6 HOH 41 1345 63 HOH HOH A . I 6 HOH 42 1346 65 HOH HOH A . I 6 HOH 43 1347 68 HOH HOH A . I 6 HOH 44 1348 69 HOH HOH A . I 6 HOH 45 1349 75 HOH HOH A . I 6 HOH 46 1350 77 HOH HOH A . I 6 HOH 47 1351 80 HOH HOH A . I 6 HOH 48 1352 83 HOH HOH A . I 6 HOH 49 1353 87 HOH HOH A . I 6 HOH 50 1354 88 HOH HOH A . I 6 HOH 51 1355 89 HOH HOH A . I 6 HOH 52 1356 90 HOH HOH A . I 6 HOH 53 1357 91 HOH HOH A . I 6 HOH 54 1358 92 HOH HOH A . I 6 HOH 55 1359 93 HOH HOH A . I 6 HOH 56 1360 94 HOH HOH A . I 6 HOH 57 1361 96 HOH HOH A . I 6 HOH 58 1362 97 HOH HOH A . I 6 HOH 59 1363 99 HOH HOH A . I 6 HOH 60 1364 101 HOH HOH A . I 6 HOH 61 1365 103 HOH HOH A . I 6 HOH 62 1366 105 HOH HOH A . I 6 HOH 63 1367 106 HOH HOH A . I 6 HOH 64 1368 107 HOH HOH A . I 6 HOH 65 1369 109 HOH HOH A . I 6 HOH 66 1370 110 HOH HOH A . I 6 HOH 67 1371 111 HOH HOH A . I 6 HOH 68 1372 112 HOH HOH A . I 6 HOH 69 1373 113 HOH HOH A . I 6 HOH 70 1374 114 HOH HOH A . I 6 HOH 71 1375 117 HOH HOH A . I 6 HOH 72 1376 121 HOH HOH A . I 6 HOH 73 1377 125 HOH HOH A . I 6 HOH 74 1378 126 HOH HOH A . I 6 HOH 75 1379 127 HOH HOH A . I 6 HOH 76 1380 129 HOH HOH A . I 6 HOH 77 1381 131 HOH HOH A . I 6 HOH 78 1382 132 HOH HOH A . I 6 HOH 79 1383 133 HOH HOH A . I 6 HOH 80 1384 134 HOH HOH A . I 6 HOH 81 1385 137 HOH HOH A . I 6 HOH 82 1386 139 HOH HOH A . I 6 HOH 83 1387 140 HOH HOH A . I 6 HOH 84 1388 144 HOH HOH A . I 6 HOH 85 1389 145 HOH HOH A . I 6 HOH 86 1390 147 HOH HOH A . I 6 HOH 87 1391 148 HOH HOH A . I 6 HOH 88 1392 149 HOH HOH A . I 6 HOH 89 1393 152 HOH HOH A . I 6 HOH 90 1394 153 HOH HOH A . I 6 HOH 91 1395 154 HOH HOH A . I 6 HOH 92 1396 155 HOH HOH A . I 6 HOH 93 1397 156 HOH HOH A . I 6 HOH 94 1398 159 HOH HOH A . I 6 HOH 95 1399 161 HOH HOH A . I 6 HOH 96 1400 162 HOH HOH A . I 6 HOH 97 1401 164 HOH HOH A . I 6 HOH 98 1402 166 HOH HOH A . I 6 HOH 99 1403 167 HOH HOH A . I 6 HOH 100 1404 168 HOH HOH A . I 6 HOH 101 1405 169 HOH HOH A . I 6 HOH 102 1406 171 HOH HOH A . I 6 HOH 103 1407 172 HOH HOH A . I 6 HOH 104 1408 173 HOH HOH A . I 6 HOH 105 1409 174 HOH HOH A . I 6 HOH 106 1410 176 HOH HOH A . I 6 HOH 107 1411 184 HOH HOH A . I 6 HOH 108 1412 185 HOH HOH A . I 6 HOH 109 1413 187 HOH HOH A . I 6 HOH 110 1414 188 HOH HOH A . I 6 HOH 111 1415 189 HOH HOH A . I 6 HOH 112 1416 190 HOH HOH A . I 6 HOH 113 1417 191 HOH HOH A . I 6 HOH 114 1418 192 HOH HOH A . I 6 HOH 115 1419 196 HOH HOH A . I 6 HOH 116 1420 198 HOH HOH A . I 6 HOH 117 1421 202 HOH HOH A . I 6 HOH 118 1422 206 HOH HOH A . I 6 HOH 119 1423 207 HOH HOH A . I 6 HOH 120 1424 208 HOH HOH A . I 6 HOH 121 1425 212 HOH HOH A . I 6 HOH 122 1426 214 HOH HOH A . I 6 HOH 123 1427 215 HOH HOH A . I 6 HOH 124 1428 220 HOH HOH A . I 6 HOH 125 1429 222 HOH HOH A . I 6 HOH 126 1430 224 HOH HOH A . I 6 HOH 127 1431 227 HOH HOH A . I 6 HOH 128 1432 229 HOH HOH A . I 6 HOH 129 1433 230 HOH HOH A . I 6 HOH 130 1434 231 HOH HOH A . I 6 HOH 131 1435 232 HOH HOH A . I 6 HOH 132 1436 235 HOH HOH A . I 6 HOH 133 1437 236 HOH HOH A . I 6 HOH 134 1438 238 HOH HOH A . I 6 HOH 135 1439 240 HOH HOH A . I 6 HOH 136 1440 241 HOH HOH A . I 6 HOH 137 1441 242 HOH HOH A . I 6 HOH 138 1442 243 HOH HOH A . I 6 HOH 139 1443 246 HOH HOH A . I 6 HOH 140 1444 248 HOH HOH A . I 6 HOH 141 1445 249 HOH HOH A . J 6 HOH 1 1304 5 HOH HOH B . J 6 HOH 2 1305 6 HOH HOH B . J 6 HOH 3 1306 16 HOH HOH B . J 6 HOH 4 1307 18 HOH HOH B . J 6 HOH 5 1308 20 HOH HOH B . J 6 HOH 6 1309 21 HOH HOH B . J 6 HOH 7 1310 23 HOH HOH B . J 6 HOH 8 1311 25 HOH HOH B . J 6 HOH 9 1312 26 HOH HOH B . J 6 HOH 10 1313 27 HOH HOH B . J 6 HOH 11 1314 30 HOH HOH B . J 6 HOH 12 1315 35 HOH HOH B . J 6 HOH 13 1316 36 HOH HOH B . J 6 HOH 14 1317 38 HOH HOH B . J 6 HOH 15 1318 39 HOH HOH B . J 6 HOH 16 1319 40 HOH HOH B . J 6 HOH 17 1320 41 HOH HOH B . J 6 HOH 18 1321 43 HOH HOH B . J 6 HOH 19 1322 44 HOH HOH B . J 6 HOH 20 1323 59 HOH HOH B . J 6 HOH 21 1324 61 HOH HOH B . J 6 HOH 22 1325 62 HOH HOH B . J 6 HOH 23 1326 64 HOH HOH B . J 6 HOH 24 1327 66 HOH HOH B . J 6 HOH 25 1328 67 HOH HOH B . J 6 HOH 26 1329 70 HOH HOH B . J 6 HOH 27 1330 71 HOH HOH B . J 6 HOH 28 1331 72 HOH HOH B . J 6 HOH 29 1332 73 HOH HOH B . J 6 HOH 30 1333 74 HOH HOH B . J 6 HOH 31 1334 76 HOH HOH B . J 6 HOH 32 1335 78 HOH HOH B . J 6 HOH 33 1336 79 HOH HOH B . J 6 HOH 34 1337 81 HOH HOH B . J 6 HOH 35 1338 82 HOH HOH B . J 6 HOH 36 1339 84 HOH HOH B . J 6 HOH 37 1340 85 HOH HOH B . J 6 HOH 38 1341 86 HOH HOH B . J 6 HOH 39 1342 95 HOH HOH B . J 6 HOH 40 1343 98 HOH HOH B . J 6 HOH 41 1344 100 HOH HOH B . J 6 HOH 42 1345 102 HOH HOH B . J 6 HOH 43 1346 104 HOH HOH B . J 6 HOH 44 1347 108 HOH HOH B . J 6 HOH 45 1348 115 HOH HOH B . J 6 HOH 46 1349 116 HOH HOH B . J 6 HOH 47 1350 118 HOH HOH B . J 6 HOH 48 1351 119 HOH HOH B . J 6 HOH 49 1352 120 HOH HOH B . J 6 HOH 50 1353 122 HOH HOH B . J 6 HOH 51 1354 123 HOH HOH B . J 6 HOH 52 1355 124 HOH HOH B . J 6 HOH 53 1356 128 HOH HOH B . J 6 HOH 54 1357 130 HOH HOH B . J 6 HOH 55 1358 135 HOH HOH B . J 6 HOH 56 1359 136 HOH HOH B . J 6 HOH 57 1360 138 HOH HOH B . J 6 HOH 58 1361 141 HOH HOH B . J 6 HOH 59 1362 142 HOH HOH B . J 6 HOH 60 1363 143 HOH HOH B . J 6 HOH 61 1364 146 HOH HOH B . J 6 HOH 62 1365 150 HOH HOH B . J 6 HOH 63 1366 151 HOH HOH B . J 6 HOH 64 1367 157 HOH HOH B . J 6 HOH 65 1368 158 HOH HOH B . J 6 HOH 66 1369 160 HOH HOH B . J 6 HOH 67 1370 163 HOH HOH B . J 6 HOH 68 1371 165 HOH HOH B . J 6 HOH 69 1372 170 HOH HOH B . J 6 HOH 70 1373 175 HOH HOH B . J 6 HOH 71 1374 177 HOH HOH B . J 6 HOH 72 1375 178 HOH HOH B . J 6 HOH 73 1376 179 HOH HOH B . J 6 HOH 74 1377 180 HOH HOH B . J 6 HOH 75 1378 181 HOH HOH B . J 6 HOH 76 1379 182 HOH HOH B . J 6 HOH 77 1380 183 HOH HOH B . J 6 HOH 78 1381 186 HOH HOH B . J 6 HOH 79 1382 193 HOH HOH B . J 6 HOH 80 1383 194 HOH HOH B . J 6 HOH 81 1384 195 HOH HOH B . J 6 HOH 82 1385 197 HOH HOH B . J 6 HOH 83 1386 199 HOH HOH B . J 6 HOH 84 1387 200 HOH HOH B . J 6 HOH 85 1388 201 HOH HOH B . J 6 HOH 86 1389 203 HOH HOH B . J 6 HOH 87 1390 204 HOH HOH B . J 6 HOH 88 1391 205 HOH HOH B . J 6 HOH 89 1392 209 HOH HOH B . J 6 HOH 90 1393 210 HOH HOH B . J 6 HOH 91 1394 211 HOH HOH B . J 6 HOH 92 1395 213 HOH HOH B . J 6 HOH 93 1396 216 HOH HOH B . J 6 HOH 94 1397 217 HOH HOH B . J 6 HOH 95 1398 218 HOH HOH B . J 6 HOH 96 1399 219 HOH HOH B . J 6 HOH 97 1400 221 HOH HOH B . J 6 HOH 98 1401 223 HOH HOH B . J 6 HOH 99 1402 225 HOH HOH B . J 6 HOH 100 1403 226 HOH HOH B . J 6 HOH 101 1404 228 HOH HOH B . J 6 HOH 102 1405 233 HOH HOH B . J 6 HOH 103 1406 234 HOH HOH B . J 6 HOH 104 1407 237 HOH HOH B . J 6 HOH 105 1408 239 HOH HOH B . J 6 HOH 106 1409 244 HOH HOH B . J 6 HOH 107 1410 245 HOH HOH B . J 6 HOH 108 1411 247 HOH HOH B . J 6 HOH 109 1412 250 HOH HOH B . # _pdbx_struct_mod_residue.id 1 _pdbx_struct_mod_residue.label_asym_id B _pdbx_struct_mod_residue.label_comp_id ASN _pdbx_struct_mod_residue.label_seq_id 21 _pdbx_struct_mod_residue.auth_asym_id B _pdbx_struct_mod_residue.auth_comp_id ASN _pdbx_struct_mod_residue.auth_seq_id 21 _pdbx_struct_mod_residue.PDB_ins_code ? _pdbx_struct_mod_residue.parent_comp_id ASN _pdbx_struct_mod_residue.details '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 # 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)' 5110 ? 1 MORE -21 ? 1 'SSA (A^2)' 12930 ? # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2003-11-04 2 'Structure model' 1 1 2008-04-27 3 'Structure model' 1 2 2011-07-13 4 'Structure model' 1 3 2017-10-04 5 'Structure model' 1 4 2018-07-25 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Version format compliance' 2 3 'Structure model' 'Non-polymer description' 3 3 'Structure model' 'Version format compliance' 4 4 'Structure model' 'Refinement description' 5 5 'Structure model' 'Data collection' 6 5 'Structure model' 'Database references' 7 5 'Structure model' 'Structure summary' # loop_ _pdbx_audit_revision_category.ordinal _pdbx_audit_revision_category.revision_ordinal _pdbx_audit_revision_category.data_content_type _pdbx_audit_revision_category.category 1 4 'Structure model' software 2 5 'Structure model' pdbx_entry_details 3 5 'Structure model' struct_ref_seq_dif # _pdbx_audit_revision_item.ordinal 1 _pdbx_audit_revision_item.revision_ordinal 5 _pdbx_audit_revision_item.data_content_type 'Structure model' _pdbx_audit_revision_item.item '_struct_ref_seq_dif.details' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal CNS refinement 1.1 ? 1 AMoRE phasing . ? 2 # _pdbx_entry_details.compound_details ? _pdbx_entry_details.entry_id 1UKM _pdbx_entry_details.nonpolymer_details ? _pdbx_entry_details.sequence_details 'The sequence database UNP Q7T2Q0 reports there is a conflict as Experimental Information.' _pdbx_entry_details.source_details ? # 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 SER A 6 ? ? 39.00 -120.32 2 1 ASP A 12 ? ? 37.04 53.70 3 1 ILE A 92 ? ? -129.85 -72.42 4 1 ASN B 69 ? ? 56.67 80.10 5 1 ASP B 85 ? ? -144.14 -74.29 # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A ASP 1 ? A ASP 1 2 1 Y 1 A PHE 2 ? A PHE 2 3 1 Y 1 A VAL 134 ? A VAL 134 4 1 Y 1 B ASP 125 ? B ASP 125 5 1 Y 1 B PRO 126 ? B PRO 126 6 1 Y 1 B ALA 127 ? B ALA 127 7 1 Y 1 B VAL 128 ? B VAL 128 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 3 'CHLORIDE ION' CL 4 GLYCEROL GOL 5 N-ACETYL-D-GLUCOSAMINE NAG 6 water HOH #