查看完整 summary.json 原文
{
"code": "SASDB36",
"status": "Published",
"type_of_curve": "Single concentration",
"angular_unit": "1/nm",
"project": {
"title": "Structural basis of myelin-associated glycoprotein adhesion and signalling.",
"publication": {
"title": "Structural basis of myelin-associated glycoprotein adhesion and signalling.",
"author_list": "Pronker MF, Lemstra S, Snijder J, Heck AJ, Thies-Weesie DM, Pasterkamp RJ, Janssen BJ",
"journal": "Nat Commun",
"doi": "10.1038/ncomms13584",
"pmid": "27922006",
"published_date": "2016 Dec 6"
},
"status": "released",
"submitted_date": "2016-07-24",
"released_date": "2016-12-13"
},
"pddf_data": "https://www.sasbdb.org/media/p_of_R_files/SASDB36.out",
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"experiment": {
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"name": "Pilatus 1M",
"resolution": 172.0
},
"name": "ESRF",
"city": "Grenoble",
"country": "France",
"beamline_name": "BM29",
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"type_of_source": "X-ray synchrotron",
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},
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{
"long_name": "Myelin-associated glycoprotein (20-508; N406Q mutant)",
"short_name": "MAG",
"sequence": "GHWGAWMPSTISAFEGTCVSIPCRFDFPDELRPAVVHGVWY\r\nFNSPYPKNYPPVVFKSRTQVVHESFQGRSRLLGDLGLRNCTLLLSTLSPELGGKYYFRGD\r\nLGGYNQYTFSEHSVLDIVNTPNIVVPPEVVAGTEVEVSCMVPDNCPELRPELSWLGHEGL\r\nGEPTVLGRLREDEGTWVQVSLLHFVPTREANGHRLGCQAAFPNTTLQFEGYASLDVKYPP\r\nVIVEMNSSVEAIEGSHVSLLCGADSNPPPLLTWMRDGMVLREAVAKSLYLDLEEVTPGED\r\nGVYACLAENAYGQDNRTVELSVMYAPWKPTVNGTVVAVEGETVSILCSTQSNPDPILTIF\r\nKEKQILATVIYESQLQLELPAVTPEDDGEYWCVAENQYGQRATAFQ\r\nLSVEFAPIILLESH\r\nCAAARDTVQCLCVVKSNPEPSVAFELPSRNVTVNETEREFVYSERSGLLLTSILTIRGQA\r\nQAPPRVICTSRNLYGTQSLELPFQGAHR",
"organism": "Mus musculus",
"uniprot_code": "P20917",
"uniprot_range_first": 20,
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"oligomerization": "monomer",
"molecular_type": "protein",
"uniprot_sequence": "MIFLATLPLFWIMISASRGGHWGAWMPSTISAFEGTCVSIPCRFDFPDELRPAVVHGVWY\nFNSPYPKNYPPVVFKSRTQVVHESFQGRSRLLGDLGLRNCTLLLSTLSPELGGKYYFRGD\nLGGYNQYTFSEHSVLDIVNTPNIVVPPEVVAGTEVEVSCMVPDNCPELRPELSWLGHEGL\nGEPTVLGRLREDEGTWVQVSLLHFVPTREANGHRLGCQAAFPNTTLQFEGYASLDVKYPP\nVIVEMNSSVEAIEGSHVSLLCGADSNPPPLLTWMRDGMVLREAVAKSLYLDLEEVTPGED\nGVYACLAENAYGQDNRTVELSVMYAPWKPTVNGTVVAVEGETVSILCSTQSNPDPILTIF\nKEKQILATVIYESQLQLELPAVTPEDDGEYWCVAENQYGQRATAFNLSVEFAPIILLESH\nCAAARDTVQCLCVVKSNPEPSVAFELPSRNVTVNETEREFVYSERSGLLLTSILTIRGQA\nQAPPRVICTSRNLYGTQSLELPFQGAHRLMWAKIGPVGAVVAFAILIAIVCYITQTRRKK\nNVTESSSFSGGDNPHVLYSPEFRISGAPDKYESEKQRLGSERRLLGLRGESPELDLSYSH\nSDLGKRPTKDSYTLTEELAEYAEIRVK",
"mw": 53.978,
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"number_molecules": 1,
"complex_state": false,
"deuteration": null,
"molecule_source": "biological",
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}
],
"buffer": {
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"concentration_unit": "mM",
"comment": null,
"additive": "150 mM NaCl",
"concentration": 20.0,
"pka": null,
"ph": 7.5,
"deuteration": null
},
"purity_method": null,
"name": "Glycosylated myelin-associated glycoprotein full extracellular domain (Ig1-5) N406Q mutant",
"ext_coefficient": null,
"contrast": null,
"specific_vol": null,
"dry_vol": null,
"absorbption": null,
"deuteration": null,
"mixture": null
},
"contributor": [
{
"affiliation": [
{
"short_name": null,
"address": "Utrecht, Netherlands",
"full_name": "Utrecht University",
"webpage": "http://www.uu.nl/"
}
],
"contributor_name": "Matti",
"contributor_surname": "Pronker",
"orcid": null
}
],
"concentration_method": null,
"concentration_unit": null,
"date": "2016-02-05",
"storage_temperature": 20.0,
"cell_temperature": 20.0,
"exposure_time": 1.0,
"number_of_frames": 9,
"wavelength": 0.0992,
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"concentration_min": null,
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},
"fits": [
{
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"software": "PDB (Protein Data Bank)",
"pdb_link": [
{
"pdb_code": "5lfu",
"ext_code": "5LFU",
"ext_type": "pdb",
"difference_with_model": "derived"
}
],
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"log": null,
"symmetry": "",
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}
],
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"software": null,
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"fit_data": "https://www.sasbdb.org/media/fitting_files/SASDB36_fit1.fit",
"fit_log": null,
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}
],
"estimated_volume_method": null,
"pddf_software": "ATSAS GNOM",
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"i0_calibration_standard": null,
"description": "Myelin-associated glycoprotein (MAG) full extracellular domain (immunoglobulin domains 1-5) with an N406Q mutation that should, based on the crystal structure, enhance MAG dimerization by removing an N-linked glycan that clashes with its symmetry mate.",
"experiment_description": "Synchrotron SAXS data from solutions of glycosylated myelin-associated glycoprotein (full extracellular domain (Ig1-5) N406Q mutant) in HEPES, pH 7.5 were collected on the BM29 camera on the storage ring ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4π sin θ/λ and 2θ is the scattering angle). One solute concentration of 2.12 mg/ml was measured at 20°C. Nine successive 1 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 and the different curves were scaled for protein concentration.",
"tags": [],
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"experimental_mw": 63.7,
"experimental_mw_error": null,
"guinier_i0_mw": 82.0,
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"pddf_dmax": 25.6,
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"porod_volume": 193.23,
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"estimated_volume": null,
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"guinier_point_first": 13,
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"i0_calibration_standard_data": null,
"intensities_log_log_plot": "SASDB36_datloglog_img.png",
"symmetry": null,
"last_modified": "2019-12-06T13:07:15.624532+01:00",
"bragg_peak": []
}查看完整 manifest.json 原文
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"started_at": "2026-08-11T16:36:57.415859+00:00",
"finished_at": "2026-08-11T16:37:07.122935+00:00",
"source_last_modified": "2019-12-06T13:07:15.624532+01:00",
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