SASDFW3

Cytokine-like nuclear factor dehydrogenase domain, NPAC DH, plus native linker (NPAC delta-205)

Data type: SASBDB experimental data Status: Published Curve type: SEC-SAS Last updated: 2019-12-06T13:07:15.624532+01:00

The protein construct encompasses the dehydrogenase domain plus an additional upstream native-sequence amino acid linker (compare to the isolated dehydrogenase domain, SASDFV3, NPAC delta-261).

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Cytokine-like nuclear factor dehydrogenase domain, NPAC DH, plus native linker (NPAC delta-205)

Concentration— – 1.25 Buffer / pH15 mM HEPES, 200 mM NaCl / 7.3
Experimental temperature20.0 Facility / beamlineESRF / BM29
Wavelength0.1 nmExposure1.0 s × 222

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
NPAC linker+DH (delta-205)
View sequence
TASEPVKDADPHFHHFLLSQTEKPAVCYQAITKKLKICEEETGSTSIQAADSTAVNGSITPTDKKIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEKCDLFIQEGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPSGVLQGIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFLGEVGNAAKMMLIVNMVQGSFMATIAEGLTLAQVTGQSQQTLLDILNQGQLASIFLDQKCQNILQGNFKPDFYLKYIQKDLRLAIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRAYIH
proteinHomo sapiensQ49A26205–553tetramerMolecule count 437.438 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1593[3]0.07138524–2.852432 1/nmHas uncertainty columnMissing 086sasbdb/entries/w3/sasdfw3/source/SASDFW3.dat
▼

2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)11.36—nm
i0Guinier24.10.09arbitrary
i0P(r)24.0—arbitrary
mwExperimental160.0—kDa
mwPorod150.0—kDa
porod_volumePorod240.0—nm³
rgGuinier4.040.02nm
rgP(r)4.015—nm

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

This entry has no source fit record.

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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 name15 mM HEPES, 200 mM NaClBuffer concentration—
pH7.3Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2018-01-26Storage / measurement temperature4.0 / 20.0
Exposure time1.0Frames222
Wavelength0.1Sample-to-detector distance2.87
SourceX-ray synchrotronDetectorPilatus 1M
Facility / beamlineESRF / BM29 · Grenoble, France
q range0.071 – 2.852Sample 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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pddf:source record
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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:134 field values
Field pathRaw value
codeSASDFW3
statusPublished
type_of_curveSEC-SAS
angular_unit1/nm
project.titleA Tail-Based Mechanism Drives Nucleosome Demethylation by the LSD2/NPAC Multimeric Complex.
project.publication.titleA Tail-Based Mechanism Drives Nucleosome Demethylation by the LSD2/NPAC Multimeric Complex.
project.publication.author_listMarabelli C, Marrocco B, Pilotto S, Chittori S, Picaud S, Marchese S, Ciossani G, Forneris F, Filippakopoulos P, Schoehn G, Rhodes D, Subramaniam S, Mattevi A
project.publication.journalCell Rep
project.publication.doi10.1016/j.celrep.2019.03.061
project.publication.pmid30970244
project.publication.published_date2019 Apr 9
project.statusreleased
project.submitted_date2019-03-12
project.released_date2019-04-16
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDFW3.out
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDFW3.dat
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experiment.instrument.detector.typeDectris
experiment.instrument.detector.namePilatus 1M
experiment.instrument.detector.resolution172.0
experiment.instrument.nameESRF
experiment.instrument.cityGrenoble
experiment.instrument.countryFrance
experiment.instrument.beamline_nameBM29
experiment.instrument.beam_geometry
experiment.instrument.type_of_sourceX-ray synchrotron
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_nameNPAC linker+DH (delta-205)
experiment.sample.molecule[0].short_nameNPAC delta205
experiment.sample.molecule[0].sequenceTASEPVKDADPHFHHFLLSQTEKPAVCYQAITKKLKICEEETGSTSIQAADSTAVNGSIT PTDKKIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEKCDLFIQEGARLGRTPAEVVSTC DITFACVSDPKAAKDLVLGPSGVLQGIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLE APVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFLGEVGNAAKMMLIVNMVQ GSFMATIAEGLTLAQVTGQSQQTLLDILNQGQLASIFLDQKCQNILQGNFKPDFYLKYIQ KDLRLAIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRAYIH
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeQ49A26
experiment.sample.molecule[0].uniprot_range_first205
experiment.sample.molecule[0].uniprot_range_last553
experiment.sample.molecule[0].oligomerizationtetramer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMAAVSLRLGDLVWGKLGRYPPWPGKIVNPPKDLKKPRGKKCFFVKFFGTEDHAWIKVEQL KPYHAHKEEMIKINKGKRFQQAVDAVEEFLRRAKGKDQTSSHNSSDDKNRRNSSEERSRP NSGDEKRKLSLSEGKVKKNMGEGKKRVSSGSSERGSKSPLKRAQEQSPRKRGRPPKDEKD LTIPESSTVKGMMAGPMAAFKWQPTASEPVKDADPHFHHFLLSQTEKPAVCYQAITKKLK ICEEETGSTSIQAADSTAVNGSITPTDKKIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTA EKCDLFIQEGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPSGVLQGIRPGKCYVDM STVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAM GKTSFFLGEVGNAAKMMLIVNMVQGSFMATIAEGLTLAQVTGQSQQTLLDILNQGQLASI FLDQKCQNILQGNFKPDFYLKYIQKDLRLAIALGDAVNHPTPMAAAANEVYKRAKALDQS DNDMSAVYRAYIH
experiment.sample.molecule[0].mw37.438
experiment.sample.molecule[0].total_mw149.752
experiment.sample.molecule[0].number_molecules4
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.name15 mM HEPES, 200 mM NaCl
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph7.3
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameCytokine-like nuclear factor dehydrogenase domain, NPAC DH, plus native linker (NPAC delta-205)
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].addressItaly
experiment.contributor[0].affiliation[0].full_nameUniversity of Pavia
experiment.contributor[0].affiliation[0].webpagehttp://wcm-3.unipv.it
experiment.contributor[0].contributor_nameFederico
experiment.contributor[0].contributor_surnameForneris
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2018-01-26
experiment.storage_temperature4.0
experiment.cell_temperature20.0
experiment.exposure_time1.0
experiment.number_of_frames222
experiment.wavelength0.1
experiment.sample_detector_distance2.87
experiment.concentration_minnull
experiment.concentration_max1.25
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.071
experiment.s_max2.852
experiment.total_exposure_timenull
experiment.seccolumnnull
fits[]
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionThe protein construct encompasses the dehydrogenase domain plus an additional upstream native-sequence amino acid linker (compare to the isolated dehydrogenase domain, SASDFV3, NPAC delta-261).
experiment_descriptionSynchrotron SAXS data from solutions of truncated cytokine-like nuclear factor (NPAC delta-205) in 15 mM HEPES, 200 mM NaCl, pH 7.3 were collected using size-exclusion chromatography SAXS (SEC-SAXS) on the BM29 beam line at the 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 (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). SEC-SAXS was performed at 20 °C using the following parameters: Column: Wyatt WTC-030N5; Flow rate: 0.25 mL/min; Sample injection concentration: 2 mg/mL; Injection volume: 50 μL. The data were collected through the SEC peak of the sample as a series of 222 x 1 second exposures. Each unsubtracted data frame was normalised to the intensity of the transmitted beam and radially averaged and the scattering of an appropriate solvent-blank was subtracted. The resulting subtracted frames were scaled and averaged to generate the final SAXS profile displayed in this entry.
tags[]
intensity_unitarbitrary
experimental_mw160.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw150.0
porod_mw_errornull
pddf_i024.0
pddf_i0_errornull
guinier_i024.1
guinier_i0_error0.09
pddf_rg4.015
pddf_rg_errornull
guinier_rg4.04
guinier_rg_error0.02
pddf_dmax11.36
pddf_dmax_errornull
porod_volume240.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first9
guinier_point_last61
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDFW3_datloglog_img.png
symmetrynull
last_modified2019-12-06T13:07:15.624532+01:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDFW3
statussuccess
started_at2026-08-11T14:09:18.059408+00:00
finished_at2026-08-11T14:09:26.038579+00:00
source_last_modified2019-12-06T13:07:15.624532+01:00
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View the complete summary.json source
{
  "code": "SASDFW3",
  "status": "Published",
  "type_of_curve": "SEC-SAS",
  "angular_unit": "1/nm",
  "project": {
    "title": "A Tail-Based Mechanism Drives Nucleosome Demethylation by the LSD2/NPAC Multimeric Complex.",
    "publication": {
      "title": "A Tail-Based Mechanism Drives Nucleosome Demethylation by the LSD2/NPAC Multimeric Complex.",
      "author_list": "Marabelli C, Marrocco B, Pilotto S, Chittori S, Picaud S, Marchese S, Ciossani G, Forneris F, Filippakopoulos P, Schoehn G, Rhodes D, Subramaniam S, Mattevi A",
      "journal": "Cell Rep",
      "doi": "10.1016/j.celrep.2019.03.061",
      "pmid": "30970244",
      "published_date": "2019 Apr 9"
    },
    "status": "released",
    "submitted_date": "2019-03-12",
    "released_date": "2019-04-16"
  },
  "pddf_data": "https://www.sasbdb.org/media/p_of_R_files/SASDFW3.out",
  "intensities_data": "https://www.sasbdb.org/media/intensities_files/SASDFW3.dat",
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  "intensities_kratky_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDFW3_kratky_img.png",
  "pddf_plot": "https://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDFW3_pofr_img.png",
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  "experiment": {
    "instrument": {
      "detector": {
        "type": "Dectris",
        "name": "Pilatus 1M",
        "resolution": 172.0
      },
      "name": "ESRF",
      "city": "Grenoble",
      "country": "France",
      "beamline_name": "BM29",
      "beam_geometry": "",
      "type_of_source": "X-ray synchrotron",
      "point_source": null,
      "line_collimation": null,
      "sample_path_length": null,
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      "line_collimation_integrationwidth": null,
      "xray_energy": null,
      "beam_profile_ah": null,
      "beam_profile_al": null
    },
    "sample": {
      "molecule": [
        {
          "long_name": "NPAC linker+DH (delta-205)",
          "short_name": "NPAC delta205",
          "sequence": "TASEPVKDADPHFHHFLLSQTEKPAVCYQAITKKLKICEEETGSTSIQAADSTAVNGSIT\r\nPTDKKIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEKCDLFIQEGARLGRTPAEVVSTC\r\nDITFACVSDPKAAKDLVLGPSGVLQGIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLE\r\nAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFLGEVGNAAKMMLIVNMVQ\r\nGSFMATIAEGLTLAQVTGQSQQTLLDILNQGQLASIFLDQKCQNILQGNFKPDFYLKYIQ\r\nKDLRLAIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRAYIH",
          "organism": "Homo sapiens",
          "uniprot_code": "Q49A26",
          "uniprot_range_first": 205,
          "uniprot_range_last": 553,
          "oligomerization": "tetramer",
          "molecular_type": "protein",
          "uniprot_sequence": "MAAVSLRLGDLVWGKLGRYPPWPGKIVNPPKDLKKPRGKKCFFVKFFGTEDHAWIKVEQL\nKPYHAHKEEMIKINKGKRFQQAVDAVEEFLRRAKGKDQTSSHNSSDDKNRRNSSEERSRP\nNSGDEKRKLSLSEGKVKKNMGEGKKRVSSGSSERGSKSPLKRAQEQSPRKRGRPPKDEKD\nLTIPESSTVKGMMAGPMAAFKWQPTASEPVKDADPHFHHFLLSQTEKPAVCYQAITKKLK\nICEEETGSTSIQAADSTAVNGSITPTDKKIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTA\nEKCDLFIQEGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPSGVLQGIRPGKCYVDM\nSTVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAM\nGKTSFFLGEVGNAAKMMLIVNMVQGSFMATIAEGLTLAQVTGQSQQTLLDILNQGQLASI\nFLDQKCQNILQGNFKPDFYLKYIQKDLRLAIALGDAVNHPTPMAAAANEVYKRAKALDQS\nDNDMSAVYRAYIH",
          "mw": 37.438,
          "total_mw": 149.752,
          "number_molecules": 4,
          "complex_state": false,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": null
        }
      ],
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        "concentration_unit": null,
        "comment": null,
        "additive": null,
        "concentration": null,
        "pka": null,
        "ph": 7.3,
        "deuteration": null
      },
      "purity_method": null,
      "name": "Cytokine-like nuclear factor dehydrogenase domain, NPAC DH, plus native linker (NPAC delta-205)",
      "ext_coefficient": null,
      "contrast": null,
      "specific_vol": null,
      "dry_vol": null,
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      "deuteration": null,
      "mixture": null
    },
    "contributor": [
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          {
            "short_name": null,
            "address": "Italy",
            "full_name": "University of Pavia",
            "webpage": "http://wcm-3.unipv.it"
          }
        ],
        "contributor_name": "Federico",
        "contributor_surname": "Forneris",
        "orcid": null
      }
    ],
    "concentration_method": null,
    "concentration_unit": null,
    "date": "2018-01-26",
    "storage_temperature": 4.0,
    "cell_temperature": 20.0,
    "exposure_time": 1.0,
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    "wavelength": 0.1,
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    "concentration_min": null,
    "concentration_max": 1.25,
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    "seccolumn": null
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  "pddf_software": "ATSAS GNOM",
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  "i0_calibration_standard": null,
  "description": "The protein construct encompasses the dehydrogenase domain plus an additional upstream native-sequence amino acid linker (compare to the isolated dehydrogenase domain, SASDFV3, NPAC delta-261).",
  "experiment_description": "Synchrotron SAXS data from solutions of truncated cytokine-like nuclear factor (NPAC delta-205) in 15 mM HEPES, 200 mM NaCl, pH 7.3 were collected using size-exclusion chromatography SAXS (SEC-SAXS) on the BM29 beam line at the 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 (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). SEC-SAXS was performed at 20 °C using the following parameters: Column: Wyatt WTC-030N5; Flow rate: 0.25 mL/min; Sample injection concentration: 2 mg/mL; Injection volume: 50 μL. The data were collected through the SEC peak of the sample as a series of 222 x 1 second exposures. Each unsubtracted data frame was normalised to the intensity of the transmitted beam and radially averaged and the scattering of an appropriate solvent-blank was subtracted. The resulting subtracted frames were scaled and averaged to generate the final SAXS profile displayed in this entry.",
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  "guinier_i0_mw_error": null,
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  "pddf_dmax": 11.36,
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  "estimated_volume_error": null,
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  "guinier_point_last": 61,
  "pddf_point_first": null,
  "pddf_point_last": null,
  "i0_calibration_standard_data": null,
  "intensities_log_log_plot": "SASDFW3_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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