{"code":"SASDC48","status":"Published","type_of_curve":"Single concentration","angular_unit":"1/A","project":{"title":"Disulfide isomerase activity of the dynamic, trimeric <b><i>Proteus mirabilis</i></b> ScsC protein is primed by the tandem immunoglobulin-fold domain of ScsB.","publication":{"title":"Disulfide isomerase activity of the dynamic, trimeric <b><i>Proteus mirabilis</i></b> ScsC protein is primed by the tandem immunoglobulin-fold domain of ScsB.","author_list":"Furlong EJ, Choudhury HG, Kurth F, Duff AP, Whitten AE, Martin JL","journal":"J Biol Chem","doi":"10.1074/jbc.RA118.001860","pmid":"29491145","published_date":"2018 Apr 20"},"status":"released","submitted_date":"2017-10-05","released_date":"2018-02-21"},"pddf_data":"https://www.sasbdb.org/media/p_of_R_files/SASDC48.out","intensities_data":"https://www.sasbdb.org/media/intensities_files/SASDC48.dat","intensities_log_plot":"https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDC48_dat_img.png","intensities_kratky_plot":"https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDC48_kratky_img.png","pddf_plot":"https://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDC48_pofr_img.png","intensities_guinier_plot":"https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDC48_guinier_img.png","sascif_data":"https://www.sasbdb.org/media/sascif/sascif_files/SASDC48.sascif","experiment":{"instrument":{"detector":{"type":"Dectris","name":"Pilatus 1M","resolution":172.0},"name":"Australian  Synchrotron","city":"Melbourne","country":"Australia","beamline_name":"SAXS/WAXS","beam_geometry":"Point","type_of_source":"X-ray synchrotron","point_source":true,"line_collimation":null,"sample_path_length":null,"line_collimation_slitlength":null,"line_collimation_integrationwidth":null,"xray_energy":null,"beam_profile_ah":null,"beam_profile_al":null},"sample":{"molecule":[{"long_name":"DsbA-like protein","short_name":"ScsC","sequence":"SNAALNAAQEKEVRALVRDTLVSNPEILEEAIMALQTKKADEQQAQFRQALASEHDALYNDAASPRIGAKDAKLVLVSFTDYNCPYCKRFDPLLEKITEQYPDVAVIIKPLPFKGESSAKASQAVLSVWKEDPKAFLALHQRLMQKKTMLDNASIEDAMKSTNTSKIKLTDDSLKTLQNNLELSRKLGIQGTPATVIGDTILPGAVDYDQLEIIVKEQLAKVKK","organism":"Proteus mirabilis","uniprot_code":"C2LPE2","uniprot_range_first":22,"uniprot_range_last":243,"oligomerization":"trimer","molecular_type":"protein","uniprot_sequence":null,"mw":24.768,"total_mw":74.304,"number_molecules":3,"complex_state":false,"deuteration":null,"molecule_source":"biological","molecule_description":null},{"long_name":"Putative metal resistance protein","short_name":"ScsB","sequence":"MHHHHHHSSGVDLGTENLYFQSNADTGWLTMPDNDHAQVRATADKSSTGDVKILLEVQLAPGWKTYWRSPGEGGVAPEINWTQSVSDMIWHWPSPSAFDVAGIHTQGYDKEVVFPIELKSVDSDNLNGVLTLSTCSNVCILTDYSLNLDLNEPAPADFEWQYNQAMAKVPVTSGLISAVSSDYRNSQLTLSLQREQGDWHQPNIYLDPPQGMLYGIPQLTAKGDHLSVTVDVTDDWGDAAGDITGKALSFVVTDDGYSRQVNDTIGQGDSASLPTADS","organism":"Proteus mirabilis","uniprot_code":"B4EV20","uniprot_range_first":22,"uniprot_range_last":275,"oligomerization":"monomer","molecular_type":"protein","uniprot_sequence":"MVRSFLIALMLMLFSLSSLAADTGWLTMPDNDHAQVRATADKSSTGDVKILLEVQLAPGW\nKTYWRSPGEGGVAPEINWTQSVSDMIWHWPSPSAFDVAGIHTQGYDKEVVFPIELKSVDS\nDNLNGVLTLSTCSNVCILTDYSLNLDLNEPAPADFEWQYNQAMAKVPVTSGLISAVSSDY\nRNSQLTLSLQREQGDWHQPNIYLDPPQGMLYGIPQLTAKGDHLSVTVDVTDDWGDAAGDI\nTGKALSFVVTDDGYSRQVNDTIGQGDSASLPTADSGVGLWSILAFALLGGLILNLMPCVL\nPVLAMKLGSILHIEKRDTGAIRKQFSVSVVGILVSFWALALFMTVLRYSQEAIGWGIQFQ\nSPWFIGFMVLITAIFTANLFGLFELRLSSNMNTKIATAGGQGYSRHFWEGAFATLLATPC\nSAPFLGTAVAYALIAPLSELWLIFTALGLGMSLPWIMVAMFPSIAKVLPKPGKWMNRLRV\nVLGFMMLLSCIWLITLLIPHFGIGIVAAIFVAIALILLFAIAKHYGKKTLFASMVITLIL\nGGTSYLFIAQPDTQTLAGQDHVNWQPLSEEAIHQALAENKRVFIDVTADWCVTCKANKYN\nVLLRDDVQKALSEPDVVALRGDWTKPSEQITQFLKQRGQVAVPFNQIYGPCNKEGEILPP\nLLNKDLMLTILSEAKGAQ","mw":30.343,"total_mw":30.343,"number_molecules":1,"complex_state":false,"deuteration":null,"molecule_source":"biological","molecule_description":null}],"buffer":{"name":"10mM HEPES, 150mM NaCl","concentration_unit":null,"comment":null,"additive":null,"concentration":null,"pka":null,"ph":7.5,"deuteration":null},"purity_method":null,"name":"ScsC-ScsBalpha complex","ext_coefficient":null,"contrast":null,"specific_vol":null,"dry_vol":null,"absorbption":null,"deuteration":null,"mixture":null},"contributor":[{"affiliation":[{"short_name":"ANSTO","address":"Kirrawee DC, NSW 2232, Australia","full_name":"Australian Nuclear Science and Technology Organisation","webpage":""}],"contributor_name":"Andrew","contributor_surname":"Whitten","orcid":null}],"concentration_method":null,"concentration_unit":null,"date":"2016-11-02","storage_temperature":4.0,"cell_temperature":10.0,"exposure_time":1.0,"number_of_frames":13,"wavelength":0.1033,"sample_detector_distance":2.68,"concentration_min":0.56,"concentration_max":4.5,"sample_volume":null,"flow_rate":null,"s_min":0.105,"s_max":2.999,"total_exposure_time":null,"seccolumn":null},"fits":[{"models":[{"model_plot":"https://www.sasbdb.org/media/pdb_file/images/SASDC48_fit1_model1_img.png","software":"SASREF","pdb_link":[],"model_title":null,"type_of_model":"atomic","software_version":"7.d","model_data":"https://www.sasbdb.org/media/pdb_file/SASDC48_fit1_model1.pdb","model_mw":99.99,"bead_radius":1.9,"log":"https://www.sasbdb.org/media/log_files/run1_ZoMbNC2.log","symmetry":"P1","comment":"Overall symmetry is P1, but the ScsC component possesses P3 symmetry","user":111}],"fit_unit":"1/A","fit_plot":"https://www.sasbdb.org/media/fitting_files/scattering_plots/SASDC48_fit1_fit_img.png","software":"SASREF","chi_square_value":1.7956,"p_value":0.0,"fit_residual_plot":"SASDC48_fit1_fitresiduals_img.png","fit_data":"https://www.sasbdb.org/media/fitting_files/SASDC48_fit1.fit","fit_log":"https://www.sasbdb.org/media/fitting_files/log_files/run1_ZTJcGes.log","software_version":"7.d","description":null}],"estimated_volume_method":null,"pddf_software":"ATSAS GNOM","pddf_software_version":"4.6","i0_calibration_standard":null,"description":null,"experiment_description":"X-ray synchrotron radiation scattering data from solutions of Suppressor of Copper Sensitivity C protein (ScsC) complexed with the alpha domain of the Suppressor of Copper Sensitivity B protein from Proteus mirabilis in 10 mM HEPES 100mM NaCl, pH 7.5 were collected on the SAXS/WAXS beam line of the Australian Synchrotron (Melbourne, Australia) using a 2D Photon counting Pilatus 1M-W pixel detector (s = 4π sin θ/λ, where 2θ is the scattering angle). Thirteen successive 1 second frames were collected across solute concentrations of 0.56-4.50 mg/ml. The SAXS data displayed this entry was derived from a 0.56 mg/ml sample. The data were normalized to the intensity of the transmitted beam and radially averaged and the scattering of the solvent-blank was subtracted. Small-angle neutron scattering data with contrast variation were also collected on the QUOKKA instrument at the Australian Nuclear Science and Technology Organisation at a solute concentration of ~5.0 mg/ml. A rigid-body model was co-refined against the SAXS and SANS data using using SASREF (v 7.d), and this model is shown, together with the X-ray data and correspond fit. Details of the SANS data collection, corresponding fits, and additional analysis are contained in a downloadable zip archive.","tags":[],"intensity_unit":"1/cm","experimental_mw":95.0,"experimental_mw_error":null,"guinier_i0_mw":95.0,"guinier_i0_mw_error":5.0,"porod_mw":119.0,"porod_mw_error":null,"pddf_i0":0.04026,"pddf_i0_error":0.0001,"guinier_i0":0.04057,"guinier_i0_error":0.00012,"pddf_rg":3.87,"pddf_rg_error":0.01,"guinier_rg":3.92,"guinier_rg_error":0.02,"pddf_dmax":11.5,"pddf_dmax_error":3.0,"porod_volume":145.0,"porod_volume_error":null,"estimated_volume":null,"estimated_volume_error":null,"guinier_point_first":1,"guinier_point_last":30,"pddf_point_first":null,"pddf_point_last":null,"i0_calibration_standard_data":null,"intensities_log_log_plot":"SASDC48_datloglog_img.png","symmetry":null,"last_modified":"2020-06-15T11:36:42.269791+02:00","bragg_peak":[]}