SASDDN6

Human stress-inducible heat shock 70 kDa protein 1, Hsp70 (Hspa1a) T204A mutant dimer, in the presence of ATP

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2019-12-06T13:07:15.624532+01:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Human stress-inducible heat shock 70 kDa protein 1, Hsp70 (Hspa1a) T204A mutant dimer, in the presence of ATP

Concentration— – 2.5 Buffer / pH50mM HEPES, 150mM KCH3COO, 2mM MgCl2 / 7.5
Experimental temperature4.0 Facility / beamlineCEITEC / Rigaku BioSAXS-1000
Wavelength0.154 nmExposure3600.0 s × —

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Heat shock 70 kDa protein 1
View sequence
MSYYHHHHHHLESTSLYKKAGFGSENLYFQSMAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGAFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGILNVTATDKSTGKANKITITNDKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDEGLKGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELEQVCNPIISGLYQGAGGPGPGGFGAQGPKGGSGSGPTIEEVD
proteinHomo sapiensP0DMV8—–—dimerMolecule count 273.74 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1430[3]0.0137969–0.631377 1/AHas uncertainty columnMissing 048sasbdb/entries/n6/sasddn6/source/SASDDN6.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)11.56—Å
i0Guinier0.760.011arbitrary
i0P(r)0.74570.0058arbitrary
mwExperimental148.0—kDa
mwPorod155.0—kDa
porod_volumePorod248.0—ų
rgGuinier4.010.077Å
rgP(r)3.970.2Å

These values are reported by SASBDB; SAXSdb did not recalculate them from the experimental curve.

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3. Source Fits and Models Source Fits & Models

Fit 1 · CRYSOL 2.8.3

χ²: 1.15CorMap p: 0.489949Unit: 1/A
ModelName / TypeSoftwareSymmetryModel MWPDB DeclarationSource file
1—atomicMODELLER —148.5—Model Image
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4. Source File Index Source Files

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5. Experiment Description and Publication Experiment & Publication

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6. Complete Source Record Complete Source Record

The following content comes directly from the SASBDB entry. Missing values are shown as “—”; SAXSdb does not infer undeclared units.

Open the original SASBDB entry

Buffer and Sample Properties

Buffer name50mM HEPES, 150mM KCH3COO, 2mM MgCl2Buffer concentration—
pH7.5Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2018-02-20Storage / measurement temperature4.0 / 4.0
Exposure time3600.0Frames—
Wavelength0.154Sample-to-detector distance0.48
SourceX-ray in houseDetectorPilatus 100K
Facility / beamlineCEITEC / Rigaku BioSAXS-1000 · Brno, Czech Republic
q range0.138 – 6.314Sample volume / flow rate— / —

Original SASBDB Plots

Experimental I(q)
Experimental I(q)
Experimental I(q), log-log
Experimental I(q), log-log
Guinier plot
Guinier plot
Kratky plot
Kratky plot
P(r) plot
P(r) plot

Downloadable Files

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full_entry_zip:source record and ZIP contents (4 items)
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All source fields (unfiltered)

Every source field is expanded here, including empty values, list members and fields already shown above.

summary.json:156 field values
Field pathRaw value
codeSASDDN6
statusPublished
type_of_curveSingle concentration
angular_unit1/A
project.titleHuman stress-inducible Hsp70 has a high propensity to form ATP-dependent antiparallel dimers that are differentially regulated by co-chaperone binding.
project.publication.titleHuman stress-inducible Hsp70 has a high propensity to form ATP-dependent antiparallel dimers that are differentially regulated by co-chaperone binding.
project.publication.author_listTrcka F, Durech M, Vankova P, Chmelik J, Martinkova V, Hausner J, Kadek A, Marcoux J, Klumpler T, Vojtesek B, Muller P, Man P
project.publication.journalMol Cell Proteomics
project.publication.doi10.1074/mcp.RA118.001044
project.publication.pmid30459217
project.publication.published_date2018 Nov 20
project.statusreleased
project.submitted_date2018-05-17
project.released_date2018-11-30
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDDN6.out
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDDN6.dat
intensities_log_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDDN6_dat_img.png
intensities_kratky_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDDN6_kratky_img.png
pddf_plothttps://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDDN6_pofr_img.png
intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDDN6_guinier_img.png
sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDDN6.sascif
experiment.instrument.detector.typenull
experiment.instrument.detector.namePilatus 100K
experiment.instrument.detector.resolution172.0
experiment.instrument.nameCEITEC
experiment.instrument.cityBrno
experiment.instrument.countryCzech Republic
experiment.instrument.beamline_nameRigaku BioSAXS-1000
experiment.instrument.beam_geometry
experiment.instrument.type_of_sourceX-ray in house
experiment.instrument.point_sourcenull
experiment.instrument.line_collimationnull
experiment.instrument.sample_path_lengthnull
experiment.instrument.line_collimation_slitlengthnull
experiment.instrument.line_collimation_integrationwidthnull
experiment.instrument.xray_energynull
experiment.instrument.beam_profile_ahnull
experiment.instrument.beam_profile_alnull
experiment.sample.molecule[0].long_nameHeat shock 70 kDa protein 1
experiment.sample.molecule[0].short_nameHSPA1A_T204A
experiment.sample.molecule[0].sequenceMSYYHHHHHHLESTSLYKKAGFGSENLYFQSMAKAAAIGI DLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTER LIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKH WPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKE IAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNV LRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGAFDVSI LTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEFKRKH KKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFE GIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKLDKA QIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAV AYGAAVQAAILMGDKSENVQDLLLLDVAPLSLGLETAGGV MTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAM TKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGILNVT ATDKSTGKANKITITNDKGRLSKEEIERMVQEAEKYKAED EVQRERVSAKNALESYAFNMKSAVEDEGLKGKISEADKKK VLDKCQEVISWLDANTLAEKDEFEHKRKELEQVCNPIISG LYQGAGGPGPGGFGAQGPKGGSGSGPTIEEVD
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeP0DMV8
experiment.sample.molecule[0].uniprot_range_firstnull
experiment.sample.molecule[0].uniprot_range_lastnull
experiment.sample.molecule[0].oligomerizationdimer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVA LNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEIS SMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAA IAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNH FVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRA RFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLN KSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVAPLSLGLETAGGVMTALIKRNSTI PTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDI DANGILNVTATDKSTGKANKITITNDKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKN ALESYAFNMKSAVEDEGLKGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELE QVCNPIISGLYQGAGGPGPGGFGAQGPKGGSGSGPTIEEVD
experiment.sample.molecule[0].mw73.74
experiment.sample.molecule[0].total_mw147.48
experiment.sample.molecule[0].number_molecules2
experiment.sample.molecule[0].complex_stateFalse
experiment.sample.molecule[0].deuterationnull
experiment.sample.molecule[0].molecule_sourcebiological
experiment.sample.molecule[0].molecule_descriptionnull
experiment.sample.buffer.name50mM HEPES, 150mM KCH3COO, 2mM MgCl2
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph7.5
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameHuman stress-inducible heat shock 70 kDa protein 1, Hsp70 (Hspa1a) T204A mutant dimer, in the presence of ATP
experiment.sample.ext_coefficientnull
experiment.sample.contrastnull
experiment.sample.specific_volnull
experiment.sample.dry_volnull
experiment.sample.absorbptionnull
experiment.sample.deuterationnull
experiment.sample.mixturenull
experiment.contributor[0].affiliation[0].short_namenull
experiment.contributor[0].affiliation[0].addressnull
experiment.contributor[0].affiliation[0].full_nameCEITEC - Central European Institute of Technology, Masaryk University
experiment.contributor[0].affiliation[0].webpagehttps://www.ceitec.eu/
experiment.contributor[0].contributor_nameTomas
experiment.contributor[0].contributor_surnameKlumpler
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2018-02-20
experiment.storage_temperature4.0
experiment.cell_temperature4.0
experiment.exposure_time3600.0
experiment.number_of_framesnull
experiment.wavelength0.154
experiment.sample_detector_distance0.48
experiment.concentration_minnull
experiment.concentration_max2.5
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.138
experiment.s_max6.314
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].models[0].softwareMODELLER
fits[0].models[0].pdb_link[]
fits[0].models[0].model_titlenull
fits[0].models[0].type_of_modelatomic
fits[0].models[0].software_versionnull
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fits[0].models[0].model_mw148.5
fits[0].models[0].bead_radiusnull
fits[0].models[0].lognull
fits[0].models[0].symmetrynull
fits[0].models[0].commentnull
fits[0].models[0].user195
fits[0].fit_unit1/A
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fits[0].softwareCRYSOL
fits[0].chi_square_value1.15
fits[0].p_value0.489949
fits[0].fit_residual_plotSASDDN6_fit1_fitresiduals_img.png
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fits[0].fit_lognull
fits[0].software_version2.8.3
fits[0].descriptionnull
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version5
i0_calibration_standardnull
descriptionnull
experiment_descriptionSAXS data from solutions of human stress-induced heat shock 70 kDa protein 1 ,Hsp70, (Hspa1a T204A mutant), with ATP in 50mM HEPES; 150mM KCH3COO; 2mM MgCl2, pH 7.5, were collected on a Rigaku BioSAXS-1000 instrument at CEITEC (Brno, Czech Republic) using a Pilatus 100K detector at a sample-detector distance of 0.5 m and at a wavelength of λ = 0.154 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.50 mg/ml was measured at 4°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
tags[]
intensity_unitarbitrary
experimental_mw148.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw155.0
porod_mw_errornull
pddf_i00.7457
pddf_i0_error0.0058
guinier_i00.76
guinier_i0_error0.011
pddf_rg3.97
pddf_rg_error0.2
guinier_rg4.01
guinier_rg_error0.077
pddf_dmax11.56
pddf_dmax_errornull
porod_volume248.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first2
guinier_point_last14
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDDN6_datloglog_img.png
symmetrynull
last_modified2019-12-06T13:07:15.624532+01:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDDN6
statussuccess
started_at2026-08-11T15:13:01.844679+00:00
finished_at2026-08-11T15:13:11.618171+00:00
source_last_modified2019-12-06T13:07:15.624532+01:00
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View the complete summary.json source
{
  "code": "SASDDN6",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "project": {
    "title": "Human stress-inducible Hsp70 has a high propensity to form ATP-dependent antiparallel dimers that are differentially regulated by co-chaperone binding.",
    "publication": {
      "title": "Human stress-inducible Hsp70 has a high propensity to form ATP-dependent antiparallel dimers that are differentially regulated by co-chaperone binding.",
      "author_list": "Trcka F, Durech M, Vankova P, Chmelik J, Martinkova V, Hausner J, Kadek A, Marcoux J, Klumpler T, Vojtesek B, Muller P, Man P",
      "journal": "Mol Cell Proteomics",
      "doi": "10.1074/mcp.RA118.001044",
      "pmid": "30459217",
      "published_date": "2018 Nov 20"
    },
    "status": "released",
    "submitted_date": "2018-05-17",
    "released_date": "2018-11-30"
  },
  "pddf_data": "https://www.sasbdb.org/media/p_of_R_files/SASDDN6.out",
  "intensities_data": "https://www.sasbdb.org/media/intensities_files/SASDDN6.dat",
  "intensities_log_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDDN6_dat_img.png",
  "intensities_kratky_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDDN6_kratky_img.png",
  "pddf_plot": "https://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDDN6_pofr_img.png",
  "intensities_guinier_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDDN6_guinier_img.png",
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  "experiment": {
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      "country": "Czech Republic",
      "beamline_name": "Rigaku BioSAXS-1000",
      "beam_geometry": "",
      "type_of_source": "X-ray in house",
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      "xray_energy": null,
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    },
    "sample": {
      "molecule": [
        {
          "long_name": "Heat shock 70 kDa protein 1",
          "short_name": "HSPA1A_T204A",
          "sequence": "MSYYHHHHHHLESTSLYKKAGFGSENLYFQSMAKAAAIGI\r\nDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTER\r\nLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKH\r\nWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKE\r\nIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNV\r\nLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGAFDVSI\r\nLTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEFKRKH\r\nKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFE\r\nGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKLDKA\r\nQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAV\r\nAYGAAVQAAILMGDKSENVQDLLLLDVAPLSLGLETAGGV\r\nMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAM\r\nTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGILNVT\r\nATDKSTGKANKITITNDKGRLSKEEIERMVQEAEKYKAED\r\nEVQRERVSAKNALESYAFNMKSAVEDEGLKGKISEADKKK\r\nVLDKCQEVISWLDANTLAEKDEFEHKRKELEQVCNPIISG\r\nLYQGAGGPGPGGFGAQGPKGGSGSGPTIEEVD",
          "organism": "Homo sapiens",
          "uniprot_code": "P0DMV8",
          "uniprot_range_first": null,
          "uniprot_range_last": null,
          "oligomerization": "dimer",
          "molecular_type": "protein",
          "uniprot_sequence": "MAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVA\nLNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEIS\nSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAA\nIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNH\nFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRA\nRFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLN\nKSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVAPLSLGLETAGGVMTALIKRNSTI\nPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDI\nDANGILNVTATDKSTGKANKITITNDKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKN\nALESYAFNMKSAVEDEGLKGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELE\nQVCNPIISGLYQGAGGPGPGGFGAQGPKGGSGSGPTIEEVD",
          "mw": 73.74,
          "total_mw": 147.48,
          "number_molecules": 2,
          "complex_state": false,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": null
        }
      ],
      "buffer": {
        "name": "50mM HEPES, 150mM KCH3COO, 2mM MgCl2",
        "concentration_unit": null,
        "comment": null,
        "additive": null,
        "concentration": null,
        "pka": null,
        "ph": 7.5,
        "deuteration": null
      },
      "purity_method": null,
      "name": "Human stress-inducible heat shock 70 kDa protein 1, Hsp70 (Hspa1a) T204A mutant dimer, in the presence of ATP",
      "ext_coefficient": null,
      "contrast": null,
      "specific_vol": null,
      "dry_vol": null,
      "absorbption": null,
      "deuteration": null,
      "mixture": null
    },
    "contributor": [
      {
        "affiliation": [
          {
            "short_name": null,
            "address": null,
            "full_name": "CEITEC - Central European Institute of Technology, Masaryk University",
            "webpage": "https://www.ceitec.eu/"
          }
        ],
        "contributor_name": "Tomas",
        "contributor_surname": "Klumpler",
        "orcid": null
      }
    ],
    "concentration_method": null,
    "concentration_unit": null,
    "date": "2018-02-20",
    "storage_temperature": 4.0,
    "cell_temperature": 4.0,
    "exposure_time": 3600.0,
    "number_of_frames": null,
    "wavelength": 0.154,
    "sample_detector_distance": 0.48,
    "concentration_min": null,
    "concentration_max": 2.5,
    "sample_volume": null,
    "flow_rate": null,
    "s_min": 0.138,
    "s_max": 6.314,
    "total_exposure_time": null,
    "seccolumn": null
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      "models": [
        {
          "model_plot": "https://www.sasbdb.org/media/pdb_file/images/SASDDN6_fit1_model1_img.png",
          "software": "MODELLER",
          "pdb_link": [],
          "model_title": null,
          "type_of_model": "atomic",
          "software_version": null,
          "model_data": "https://www.sasbdb.org/media/pdb_file/SASDDN6_fit1_model1.pdb",
          "model_mw": 148.5,
          "bead_radius": null,
          "log": null,
          "symmetry": null,
          "comment": null,
          "user": 195
        }
      ],
      "fit_unit": "1/A",
      "fit_plot": "https://www.sasbdb.org/media/fitting_files/scattering_plots/SASDDN6_fit1_fit_img.png",
      "software": "CRYSOL",
      "chi_square_value": 1.15,
      "p_value": 0.489949,
      "fit_residual_plot": "SASDDN6_fit1_fitresiduals_img.png",
      "fit_data": "https://www.sasbdb.org/media/fitting_files/SASDDN6_fit1.fit",
      "fit_log": null,
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      "description": null
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  "i0_calibration_standard": null,
  "description": null,
  "experiment_description": "SAXS data from solutions of human stress-induced heat shock 70 kDa protein 1 ,Hsp70, (Hspa1a T204A mutant), with ATP in 50mM HEPES; 150mM KCH3COO; 2mM MgCl2, pH 7.5, were collected on a Rigaku BioSAXS-1000 instrument at CEITEC (Brno, Czech Republic) using a Pilatus 100K detector at a sample-detector distance of 0.5 m and at a wavelength of λ = 0.154 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.50 mg/ml was measured at 4°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.",
  "tags": [],
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  "guinier_i0_mw_error": null,
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  "pddf_dmax": 11.56,
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  "estimated_volume_error": null,
  "guinier_point_first": 2,
  "guinier_point_last": 14,
  "pddf_point_first": null,
  "pddf_point_last": null,
  "i0_calibration_standard_data": null,
  "intensities_log_log_plot": "SASDDN6_datloglog_img.png",
  "symmetry": null,
  "last_modified": "2019-12-06T13:07:15.624532+01:00",
  "bragg_peak": []
}
View the complete manifest.json source
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