The following content comes directly from the SASBDB entry. Missing values are shown as “—”; SAXSdb does not infer undeclared units.
Every source field is expanded here, including empty values, list members and fields already shown above.
View the complete summary.json source
{
"code": "SASDXY7",
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"angular_unit": "1/nm",
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"title": "The N-Myc MB0-MBI region interacts specifically and dynamically with the N-lobe of Aurora kinase A.",
"publication": {
"title": "The N-Myc MB0-MBI region interacts specifically and dynamically with the N-lobe of Aurora kinase A.",
"author_list": "Hultman J, Morad V, Tanner E, Kenney TMG, Pietras Z, Khare LP, Derbyshire D, Resetca D, Arrowsmith CH, Aili D, Ekström S, Penn LZ, Wallner B, Ahlner A, Sunnerhagen M",
"journal": "Nat Commun",
"doi": "10.1038/s41467-026-69725-1",
"pmid": "41735282",
"published_date": "2026 Feb 24"
},
"status": "released",
"submitted_date": "2025-08-19",
"released_date": "2026-01-30"
},
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"name": "Pilatus 6M",
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},
"name": "PETRA III",
"city": "DESY; Hamburg",
"country": "Germany",
"beamline_name": "EMBL P12",
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"type_of_source": "X-ray synchrotron",
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{
"long_name": "N-myc proto-oncogene protein, residues 1-100",
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"sequence": "SMPSCSTSTMP GMICKNPDLE FDSLQPCFYP DEDDFYFGGP DSTPPGEDIW KKFELLPTPP\r\nLSPSRGFAEH SSEPPSWVTE MLLENELWGS PAEEDAFGLG",
"organism": "Homo sapiens",
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"oligomerization": "monomer",
"molecular_type": "protein",
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"molecule_source": "biological",
"molecule_description": ""
},
{
"long_name": "Aurora kinase A mutant C290A:C393A",
"short_name": "AurA C290A:C393A",
"sequence": "ESKKRQWALE DFEIGRPLGK GKFGNVYLAR EKQSKFILAL KVLFKAQLEK AGVEHQLRRE\r\nVEIQSHLRHP NILRLYGYFH DATRVYLILE YAPLGTVYRE LQKLSKFDEQ RTATYITELA\r\nNALSYCHSKR VIHRDIKPEN LLLGSAGELK IADFGWSVHA PSSRRTTLAG TLDYLPPEMI\r\nEGRMHDEKVD LWSLGVLCYE FLVGKPPFEA NTYQETYKRI SRVEFTFPDF VTEGARDLIS\r\nRLLKHNPSQR PMLREVLEHP WITANSSKPS NAQNKESASK QS",
"organism": "Homo sapiens",
"uniprot_code": "O14965",
"uniprot_range_first": 122,
"uniprot_range_last": 403,
"oligomerization": "monomer",
"molecular_type": "protein",
"uniprot_sequence": "MDRSKENCISGPVKATAPVGGPKRVLVTQQFPCQNPLPVNSGQAQRVLCPSNSSQRIPLQ\nAQKLVSSHKPVQNQKQKQLQATSVPHPVSRPLNNTQKSKQPLPSAPENNPEEELASKQKN\nEESKKRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRR\nEVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITEL\nANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLCGTLDYLPPEM\nIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLI\nSRLLKHNPSQRPMLREVLEHPWITANSSKPSNCQNKESASKQS",
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"complex_state": false,
"deuteration": null,
"molecule_source": "biological",
"molecule_description": ""
}
],
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"concentration_unit": null,
"comment": null,
"additive": null,
"concentration": null,
"pka": null,
"ph": 7.5,
"deuteration": null
},
"purity_method": null,
"name": "N-Myc proto-oncogene residues 1-100 in complex with Aurora kinase A mutant C290A:C393A",
"ext_coefficient": null,
"contrast": null,
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"dry_vol": null,
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"deuteration": null,
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},
"contributor": [
{
"affiliation": [
{
"short_name": null,
"address": null,
"full_name": "Linköping University ",
"webpage": null
}
],
"contributor_name": "Johanna",
"contributor_surname": "Hultman",
"orcid": "https://orcid.org/0009-0000-8066-228X"
}
],
"concentration_method": null,
"concentration_unit": null,
"date": "2022-12-09",
"storage_temperature": 10.0,
"cell_temperature": 20.0,
"exposure_time": 1.0,
"number_of_frames": 2100,
"wavelength": 0.12398,
"sample_detector_distance": 3.0,
"concentration_min": null,
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"s_min": 0.022,
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},
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"pddf_software": "ATSAS GNOM",
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"description": "Synchrotron SAXS data from solutions of the N-Myc proto-oncogen protein (residues 1-100) in complex with the kinase domain of Aurora kinase A (residues 122-403, containing a C290A:C393A double mutation) was collected in 20mM HEPES, 150mM NaCl, 5mM MgCl2, 3% v/v glycerol, 2mM TCEP, pH 7.5 on the EMBL P12 beam line at PETRA III (DESY, Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAXS was employed by injecting 70.00 μl sample of 12 mg/ml onto a GE Superdex 75 Increase 10/300 column with a flow rate of 0.70 ml/min at 20°C. 2100 successive 1 second frames were collected. The data was normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. Buffer subtraction was done using CHROMIXS and data analysis was done using the ATSAS suite. The experimental molecular weight was also determined from SEC-MALLS run in parallel to SEC-SAXS.",
"experiment_description": null,
"tags": [],
"intensity_unit": "1/cm",
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"pddf_rg": 2.916,
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"guinier_rg": 2.82,
"guinier_rg_error": 0.007,
"pddf_dmax": 11.4,
"pddf_dmax_error": null,
"porod_volume": 82.0,
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"estimated_volume": null,
"estimated_volume_error": null,
"guinier_point_first": 34,
"guinier_point_last": 158,
"pddf_point_first": null,
"pddf_point_last": null,
"i0_calibration_standard_data": null,
"intensities_log_log_plot": "SASDXY7_datloglog_img.png",
"symmetry": null,
"last_modified": "2026-02-25T14:53:49.468065+01:00",
"bragg_peak": []
}View the complete manifest.json source
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