SASDY96

Chordin fragment aa.168-650

Data type: SASBDB experimental data Status: Published Curve type: SEC-SAS Last updated: 2026-06-15T09:04:33.907949+02:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Chordin fragment aa.168-650

Concentration— – 9.0 Buffer / pH25 mM HEPES, 150 mM NaCl / 7.5
Experimental temperature15.0 Facility / beamlineDiamond Light Source / B21
Wavelength0.09464 nmExposure1.0 s × 600

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Chordin fragment aa.168-650
View sequence
APLAGHTDFVALLTGPRSQAVARARVSLLRSSLRFSISYRRLDRPTRIRFSDSNGSVLFEHPAAPTQDGLVCGVWRAVPRLSLRLLRAEQLHVALVTLTHPSGEVWGPLIRHRALAAETFSAILTLEGPPQQGVGGITLLTLSDTEDSLHFLLLFRGLLEPRSGGLTQVPLRLQILHQGQLLRELQANVSAQEPGFAEVLPNLTVQEMDWLVLGELQMALEWAGRPGLRISGHIAARKSCDVLQSVLCGADALIPVQTGAAGSASLTLLGNGSLIYQVQVVGTSSEVVAMTLETKPQRRDQRTVLCHMAGLQPGGHTAVGICPGLGARGAHMLLQNELFLNVGTKDFPDGELRGHVAALPYCGHSARHDTLPVPLAGALVLPPVKSQAAGHAWLSLDTHCHLHYEVLLAGLGGSEQGTVTAHLLGPPGTPGPRRLLKGFYGSEAQGVVKDLEPELLRHLAKGMASLLITTKGSPRGELRGQVHIANQCELVPRGSHHHHHH
proteinHomo sapiensQ9H2X0168–644monomerMolecule count 153.6 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
12573[3]0.0045–0.34 1/AHas uncertainty columnMissing 044sasbdb/entries/96/sasdy96/source/SASDY96.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)10.57—Å
i0Guinier0.115845—1/cm
i0P(r)0.1159—1/cm
mwExperimental61.3—kDa
mwPorod66.0—kDa
porod_volumePorod106.0—ų
rgGuinier2.9620.02Å
rgP(r)2.98—Å

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

▼

3. Source Fits and Models Source Fits & Models

Fit 1 · MultiFoXS main.af0ac5f

χ²: 2.054974CorMap p: 0.0Unit: 1/A
ModelName / TypeSoftwareSymmetryModel MWPDB DeclarationSource file
1—atomicMultiFoXS multi_state_model_2_1_1.datC150.99—Model Image
2—atomicMultiFoXS multi_state_model_2_1_1.datC150.99—Model Image

Fit 2 · MultiFoXS main.af0ac5f

χ²: 2.277442CorMap p: 0.0Unit: 1/A
ModelName / TypeSoftwareSymmetryModel MWPDB DeclarationSource file
1—atomicMultiFoXS main.af0ac5fC150.99—Model Image
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4. Source File Index Source Files

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5. Experiment Description and Publication Experiment & Publication

▼

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 name25 mM HEPES, 150 mM NaClBuffer concentration—
pH7.5Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2024-07-26Storage / measurement temperature-80.0 / 15.0
Exposure time1.0Frames600
Wavelength0.09464Sample-to-detector distance3.6883
SourceX-ray synchrotronDetectorEiger 4M
Facility / beamlineDiamond Light Source / B21 · Didcot, UK
q range0.045 – 3.4Sample volume / flow rate50.0 / 0.07

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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summarysasbdb/entries/96/sasdy96/source/summary.jsondownloaded9403b18351cd7bab0134ab6919f4faa80816b405d3f4aa1bb4934cf02cc64021f9a1DownloadView source fileSource site
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full_entry_zip:source record and ZIP contents (7 items)
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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:192 field values
Field pathRaw value
codeSASDY96
statusPublished
type_of_curveSEC-SAS
angular_unit1/A
project.titleStructural and biophysical analysis of the four CHRD domains of human chordin reveals a novel binding site for glycosaminoglycans.
project.publication.titleStructural and biophysical analysis of the four CHRD domains of human chordin reveals a novel binding site for glycosaminoglycans.
project.publication.author_listSnee M, Birchenough HL, Becker MH, Popplewell JF, Ashe HL, Baldock C
project.publication.journalJ Biol Chem
project.publication.doi10.1016/j.jbc.2026.113248
project.publication.pmid42285510
project.publication.published_date2026 Jun 12
project.statusreleased
project.submitted_date2026-01-27
project.released_date2026-06-15
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experiment.instrument.detector.typenull
experiment.instrument.detector.nameEiger 4M
experiment.instrument.detector.resolution75.0
experiment.instrument.nameDiamond Light Source
experiment.instrument.cityDidcot
experiment.instrument.countryUK
experiment.instrument.beamline_nameB21
experiment.instrument.beam_geometrynull
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_nameChordin fragment aa.168-650
experiment.sample.molecule[0].short_namenull
experiment.sample.molecule[0].sequenceAPLAGHTDFVALLTGPRSQAVARARVSLLRSSLRFSISYRRLDRPTRIRFSDSNGSVLFEHPAAPTQDGLVCGVWRAVPRLSLRLLRAEQLHVALVTLTHPSGEVWGPLIRHRALAAETFSAILTLEGPPQQGVGGITLLTLSDTEDSLHFLLLFRGLLEPRSGGLTQVPLRLQILHQGQLLRELQANVSAQEPGFAEVLPNLTVQEMDWLVLGELQMALEWAGRPGLRISGHIAARKSCDVLQSVLCGADALIPVQTGAAGSASLTLLGNGSLIYQVQVVGTSSEVVAMTLETKPQRRDQRTVLCHMAGLQPGGHTAVGICPGLGARGAHMLLQNELFLNVGTKDFPDGELRGHVAALPYCGHSARHDTLPVPLAGALVLPPVKSQAAGHAWLSLDTHCHLHYEVLLAGLGGSEQGTVTAHLLGPPGTPGPRRLLKGFYGSEAQGVVKDLEPELLRHLAKGMASLLITTKGSPRGELRGQVHIANQCELVPRGSHHHHHH
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeQ9H2X0
experiment.sample.molecule[0].uniprot_range_first168
experiment.sample.molecule[0].uniprot_range_last644
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMPSLPAPPAPLLLLGLLLLGSRPARGAGPEPPVLPIRSEKEPLPVRGAAGCTFGGKVYAL DETWHPDLGEPFGVMRCVLCACEAPQWGRRTRGPGRVSCKNIKPECPTPACGQPRQLPGH CCQTCPQERSSSERQPSGLSFEYPRDPEHRSYSDRGEPGAEERARGDGHTDFVALLTGPR SQAVARARVSLLRSSLRFSISYRRLDRPTRIRFSDSNGSVLFEHPAAPTQDGLVCGVWRA VPRLSLRLLRAEQLHVALVTLTHPSGEVWGPLIRHRALAAETFSAILTLEGPPQQGVGGI TLLTLSDTEDSLHFLLLFRGLLEPRSGGLTQVPLRLQILHQGQLLRELQANVSAQEPGFA EVLPNLTVQEMDWLVLGELQMALEWAGRPGLRISGHIAARKSCDVLQSVLCGADALIPVQ TGAAGSASLTLLGNGSLIYQVQVVGTSSEVVAMTLETKPQRRDQRTVLCHMAGLQPGGHT AVGICPGLGARGAHMLLQNELFLNVGTKDFPDGELRGHVAALPYCGHSARHDTLPVPLAG ALVLPPVKSQAAGHAWLSLDTHCHLHYEVLLAGLGGSEQGTVTAHLLGPPGTPGPRRLLK GFYGSEAQGVVKDLEPELLRHLAKGMASLMITTKGSPRGELRGQVHIANQCEVGGLRLEA AGAEGVRALGAPDTASAAPPVVPGLPALAPAKPGGPGRPRDPNTCFFEGQQRPHGARWAP NYDPLCSLCTCQRRTVICDPVVCPPPSCPHPVQAPDQCCPVCPEKQDVRDLPGLPRSRDP GEGCYFDGDRSWRAAGTRWHPVVPPFGLIKCAVCTCKGGTGEVHCEKVQCPRLACAQPVR VNPTDCCKQCPVGSGAHPQLGDPMQADGPRGCRFAGQWFPESQSWHPSVPPFGEMSCITC RCGAGVPHCERDDCSLPLSCGSGKESRCCSRCTAHRRPAPETRTDPELEKEAEGS
experiment.sample.molecule[0].mw53.6
experiment.sample.molecule[0].total_mw53.6
experiment.sample.molecule[0].number_molecules1
experiment.sample.molecule[0].complex_stateFalse
experiment.sample.molecule[0].deuterationnull
experiment.sample.molecule[0].molecule_sourcebiological
experiment.sample.molecule[0].molecule_description
experiment.sample.buffer.name25 mM HEPES, 150 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.ph7.5
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameChordin fragment aa.168-650
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].addressManchester, UK
experiment.contributor[0].affiliation[0].full_nameUniversity of Manchester
experiment.contributor[0].affiliation[0].webpagehttp://www.manchester.ac.uk/
experiment.contributor[0].contributor_nameMark H.
experiment.contributor[0].contributor_surnameBecker
experiment.contributor[0].orcidhttps://orcid.org/0000-0003-3474-2419
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2024-07-26
experiment.storage_temperature-80.0
experiment.cell_temperature15.0
experiment.exposure_time1.0
experiment.number_of_frames600
experiment.wavelength0.09464
experiment.sample_detector_distance3.6883
experiment.concentration_minnull
experiment.concentration_max9.0
experiment.sample_volume50.0
experiment.flow_rate0.07
experiment.s_min0.045
experiment.s_max3.4
experiment.total_exposure_timenull
experiment.seccolumn48
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fits[0].p_value0.0
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pddf_software_version5.0
i0_calibration_standardnull
descriptionnull
experiment_descriptionnull
tags[]
intensity_unit1/cm
experimental_mw61.3
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw66.0
porod_mw_errornull
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guinier_i00.115845
guinier_i0_errornull
pddf_rg2.98
pddf_rg_errornull
guinier_rg2.962
guinier_rg_error0.02
pddf_dmax10.57
pddf_dmax_errornull
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porod_volume_errornull
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estimated_volume_errornull
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guinier_point_last302
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i0_calibration_standard_datanull
intensities_log_log_plotSASDY96_datloglog_img.png
symmetrynull
last_modified2026-06-15T09:04:33.907949+02:00
bragg_peak[]
manifest.json:34 field values
Field pathRaw value
codeSASDY96
statussuccess
started_at2026-08-11T15:04:47.188051+00:00
finished_at2026-08-11T15:04:56.131829+00:00
source_last_modified2026-06-15T09:04:33.907949+02:00
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View the complete summary.json source
{
  "code": "SASDY96",
  "status": "Published",
  "type_of_curve": "SEC-SAS",
  "angular_unit": "1/A",
  "project": {
    "title": "Structural and biophysical analysis of the four CHRD domains of human chordin reveals a novel binding site for glycosaminoglycans.",
    "publication": {
      "title": "Structural and biophysical analysis of the four CHRD domains of human chordin reveals a novel binding site for glycosaminoglycans.",
      "author_list": "Snee M, Birchenough HL, Becker MH, Popplewell JF, Ashe HL, Baldock C",
      "journal": "J Biol Chem",
      "doi": "10.1016/j.jbc.2026.113248",
      "pmid": "42285510",
      "published_date": "2026 Jun 12"
    },
    "status": "released",
    "submitted_date": "2026-01-27",
    "released_date": "2026-06-15"
  },
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View the complete manifest.json source
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