{ "code": "SASDXV4", "status": "Published", "type_of_curve": "Single concentration", "angular_unit": "1/A", "project": { "title": "The role of kinase domain dimerization in EGFR activation", "publication": null, "status": "released", "submitted_date": "2025-03-16", "released_date": "2025-11-02" }, "pddf_data": "https://www.sasbdb.org/media/p_of_R_files/SASDXV4.out", "intensities_data": "https://www.sasbdb.org/media/intensities_files/SASDXV4.dat", "intensities_log_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDXV4_dat_img.png", "intensities_kratky_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDXV4_kratky_img.png", "pddf_plot": "https://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDXV4_pofr_img.png", "intensities_guinier_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDXV4_guinier_img.png", "sascif_data": "https://www.sasbdb.org/media/sascif/sascif_files/SASDXV4.sascif", "experiment": { "instrument": { "detector": { "type": "Rigaku HyPix - 3000", "name": "Rigaku PSAXS Nano", "resolution": 100.0 }, "name": "Yale University", "city": "New Haven", "country": "United States", "beamline_name": "Rigaku MicroMax-007HF", "beam_geometry": null, "type_of_source": "X-ray in house", "point_source": null, "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": "Receptor protein-tyrosine kinase (duplication mutant)", "short_name": "KDD", "sequence": "HHHHHHSSGVDLGTENLYFQSMGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLLVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQG", "organism": "Homo sapiens", "uniprot_code": "Q504U8", "uniprot_range_first": 651, "uniprot_range_last": 993, "oligomerization": "monomer", "molecular_type": "protein", "uniprot_sequence": "MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEV\nVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALA\nVLSNYDANKTGLKELPMRNLQGQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRG\nKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKY\nSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEF\nKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFL\nLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISG\nNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVS\nCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHY\nIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPS\nIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLR\nILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYV\nMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGM\nNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALES\nILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYM\nIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEE\nDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSF\nLQRYSSDPTGALTEDSIDDTFLPVPGEWLVWKQSCSSTSSTHSAAASLQCPSQVLPPASP\nEGETVADLQTQ", "mw": 79.594, "total_mw": 79.594, "number_molecules": 1, "complex_state": false, "deuteration": null, "molecule_source": "biological", "molecule_description": "EGFR kinase domain duplication mutant. The purified construct consists of amino acids 643-976 appended to amino acids 651-993 using mature protein numbering (UniProt Q504U8 numbering: 651-993 followed by a duplicated 643-977 region). The protein construct used for SAXS contains an additional N-terminal non-native 22 amino acid extension and polyhistidine tag (HHHHHHSSGVDLGTENLYFQSM)." } ], "buffer": { "name": "20 mM HEPES, 250 mM NaCl, 250 mM KCl", "concentration_unit": null, "comment": null, "additive": null, "concentration": null, "pka": null, "ph": 8.0, "deuteration": null }, "purity_method": null, "name": "EGFR kinase domain duplication mutant (KDD) at 2.6 mg/ml", "ext_coefficient": null, "contrast": null, "specific_vol": null, "dry_vol": null, "absorbption": null, "deuteration": null, "mixture": null }, "contributor": [ { "affiliation": [ { "short_name": null, "address": "New Haven, CT, USA", "full_name": "Yale University", "webpage": "https://www.yale.edu/" } ], "contributor_name": "Zaritza", "contributor_surname": "Petrova", "orcid": "https://orcid.org/0000-0002-4877-4676" } ], "concentration_method": null, "concentration_unit": null, "date": "2022-03-22", "storage_temperature": 4.0, "cell_temperature": 4.0, "exposure_time": 7200.0, "number_of_frames": 3, "wavelength": 0.1542, "sample_detector_distance": 0.491, "concentration_min": null, "concentration_max": 2.6, "sample_volume": null, "flow_rate": null, "s_min": 0.07, "s_max": 5.008, "total_exposure_time": null, "seccolumn": null }, "fits": [], "estimated_volume_method": null, "pddf_software": "ATSAS GNOM", "pddf_software_version": "5.0", "i0_calibration_standard": null, "description": null, "experiment_description": "SAXS data from solutions of EGFR kinase domain duplication mutant in 20 mM HEPES, 250 mM NaCl, 250 mM KCl, pH 8 were collected on the Rigaku MicroMax-007HF instrument (Yale University, New Haven, United States) using a Rigaku PSAXS Nano detector at a sample-detector distance of 0.5 m and at a wavelength of λ = 0.1542 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.60 mg/ml was measured at 4°C. Three successive 7200 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.", "tags": [], "intensity_unit": "arbitrary", "experimental_mw": 86.0, "experimental_mw_error": null, "guinier_i0_mw": 86.0, "guinier_i0_mw_error": null, "porod_mw": 101.0, "porod_mw_error": null, "pddf_i0": 0.2736, "pddf_i0_error": null, "guinier_i0": 0.278134, "guinier_i0_error": null, "pddf_rg": 4.87, "pddf_rg_error": null, "guinier_rg": 4.867, "guinier_rg_error": 0.663, "pddf_dmax": 16.4, "pddf_dmax_error": null, "porod_volume": 163.0, "porod_volume_error": null, "estimated_volume": null, "estimated_volume_error": null, "guinier_point_first": 2, "guinier_point_last": 25, "pddf_point_first": null, "pddf_point_last": null, "i0_calibration_standard_data": null, "intensities_log_log_plot": "SASDXV4_datloglog_img.png", "symmetry": null, "last_modified": "2025-11-02T21:11:43.418457+01:00", "bragg_peak": [] }