SASDFQ4

Domain-stapled mutant of Pro-Matrix metalloproteinase-1 (proMMP-1 S243C, S318C)

Data type: SASBDB experimental data Status: Published Curve type: SEC-SAS Last updated: 2021-09-27T16:14:08.329705+02:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Domain-stapled mutant of Pro-Matrix metalloproteinase-1 (proMMP-1 S243C, S318C)

Concentration0.0 – 5.6 Buffer / pH50 mM Tris-HCl, 150 mM Sodium chloride, 10 mM Calcium chloride / 7.4
Experimental temperature25.0 Facility / beamlineDiamond Light Source / B21
Wavelength0.1 nmExposure3.0 s × 28

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Pro-matrix metalloproteinase-1 (Interstitial collagenase) (proMMP-1 S243C, S318C)
View sequence
MFPATLETQEQDVDLVQKYLEKYYNLKNDGRQVEKRRNSGPVVEKLKQMQEFFGLKVTGKPDAETLKVMKQPRCGVPDVAQFVLTEGNPRWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTNNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSYTFCGDVQLAQDDIDGIQAIYGRSQNPVQPIGPQTPKACDSKLTFDAITTIRGEVMFFKDRFYMRTNPFYPEVELNFICVFWPQLPNGLEAAYEFADRDEVRFFKGNKYWAVQGQNVLHGYPKDIYSSFGFPRTVKHIDAALSEENTGKTYFFVANKYWRYDEYKRSMDPGYPKMIAHDFPGIGHKVDAVFMKDGFFYFFHGTRQYKFDPKTKRILTLQKANSWFNCRKN
proteinHomo sapiensP0395620–469monomerMolecule count 152.007 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
11458[3]0.003278562–0.4037659 1/AHas uncertainty columnMissing 042sasbdb/entries/q4/sasdfq4/source/SASDFQ4.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)8.9—Å
i0Guinier0.010295.1e-05arbitrary
i0P(r)0.01028—arbitrary
mwExperimental39.35—kDa
mwPorod38.0—kDa
porod_volumePorod61.0—ų
rgGuinier2.6940.021Å
rgP(r)2.71—Å

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 name50 mM Tris-HCl, 150 mM Sodium chloride, 10 mM Calcium chlorideBuffer concentration—
pH7.4Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2015-05-21Storage / measurement temperature4.0 / 25.0
Exposure time3.0Frames28
Wavelength0.1Sample-to-detector distance3.9
SourceX-ray synchrotronDetectorPilatus 2M
Facility / beamlineDiamond Light Source / B21 · Didcot, UK
q range0.033 – 4.038Sample 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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sascif:source record
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summary: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:129 field values
Field pathRaw value
codeSASDFQ4
statusPublished
type_of_curveSEC-SAS
angular_unit1/A
project.titleConformationally constrained mutant of human matrix metalloproteinase-1
project.publicationnull
project.statusreleased
project.submitted_date2019-03-26
project.released_date2021-09-27
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDFQ4.out
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDFQ4.dat
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pddf_plothttps://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDFQ4_pofr_img.png
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experiment.instrument.detector.typenull
experiment.instrument.detector.namePilatus 2M
experiment.instrument.detector.resolutionnull
experiment.instrument.nameDiamond Light Source
experiment.instrument.cityDidcot
experiment.instrument.countryUK
experiment.instrument.beamline_nameB21
experiment.instrument.beam_geometry1 x 5 mm
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_namePro-matrix metalloproteinase-1 (Interstitial collagenase) (proMMP-1 S243C, S318C)
experiment.sample.molecule[0].short_nameProMMP-1 (S243C, S31
experiment.sample.molecule[0].sequenceMFPATLETQEQDVDLVQKYLEKYYNLKNDGRQVEKRRNSGPV VEKLKQMQEFFGLKVTGKPDAETLKVMKQPRCGVPDVAQFVLTEGNPRWEQTHLTYRIEN YTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGN LAHAFQPGPGIGGDAHFDEDERWTNNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSY TFCGDVQLAQDDIDGIQAIYGRSQNPVQPIGPQTPKACDSKLTFDAITTIRGEVMFFKDR FYMRTNPFYPEVELNFICVFWPQLPNGLEAAYEFADRDEVRFFKGNKYWAVQGQNVLHGY PKDIYSSFGFPRTVKHIDAALSEENTGKTYFFVANKYWRYDEYKRSMDPGYPKMIAHDFP GIGHKVDAVFMKDGFFYFFHGTRQYKFDPKTKRILTLQKANSWFNCRKN
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeP03956
experiment.sample.molecule[0].uniprot_range_first20
experiment.sample.molecule[0].uniprot_range_last469
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMHSFPPLLLLLFWGVVSHSFPATLETQEQDVDLVQKYLEKYYNLKNDGRQVEKRRNSGPV VEKLKQMQEFFGLKVTGKPDAETLKVMKQPRCGVPDVAQFVLTEGNPRWEQTHLTYRIEN YTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGN LAHAFQPGPGIGGDAHFDEDERWTNNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSY TFSGDVQLAQDDIDGIQAIYGRSQNPVQPIGPQTPKACDSKLTFDAITTIRGEVMFFKDR FYMRTNPFYPEVELNFISVFWPQLPNGLEAAYEFADRDEVRFFKGNKYWAVQGQNVLHGY PKDIYSSFGFPRTVKHIDAALSEENTGKTYFFVANKYWRYDEYKRSMDPGYPKMIAHDFP GIGHKVDAVFMKDGFFYFFHGTRQYKFDPKTKRILTLQKANSWFNCRKN
experiment.sample.molecule[0].mw52.007
experiment.sample.molecule[0].total_mw52.007
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_descriptionnull
experiment.sample.buffer.name50 mM Tris-HCl, 150 mM Sodium chloride, 10 mM Calcium chloride
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph7.4
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameDomain-stapled mutant of Pro-Matrix metalloproteinase-1 (proMMP-1 S243C, S318C)
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].addressPortsmouth, UK
experiment.contributor[0].affiliation[0].full_nameUniversity of Portsmouth
experiment.contributor[0].affiliation[0].webpagehttps://www.port.ac.uk
experiment.contributor[0].contributor_nameRob
experiment.contributor[0].contributor_surnameHolland
experiment.contributor[0].orcid
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2015-05-21
experiment.storage_temperature4.0
experiment.cell_temperature25.0
experiment.exposure_time3.0
experiment.number_of_frames28
experiment.wavelength0.1
experiment.sample_detector_distance3.9
experiment.concentration_min0.0
experiment.concentration_max5.6
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.033
experiment.s_max4.038
experiment.total_exposure_timenull
experiment.seccolumnnull
fits[]
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionnull
experiment_descriptionSynchrotron SAXS data from solutions of the domain-stapled mutant of pro-matrix metalloproteinase-1 (proMMP-1 S243C, S318C) in 50 mM Tris-HCl, 150 mM NaCl, 10 mM CaCl2, pH 7.4 were collected using size-exclusion chromatography SAXS (SEC-SAXS) on the B21 beam line at the Diamond Light Source (Oxfordshire, UK) using a Pilatus 2M detector at a sample-detector distance of 3.9 m and at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). SEC-SAXS was performed at 25 °C using the following parameters: Shodex Kw-403 analytical SEC column; Flow rate: 0.2 mL/min; Sample injection concentration: 5.6 mg/mL; Injection volume: 50 μL. The data were collected through the SEC peak of the sample as a series of 28 x 3 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_mw39.35
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw38.0
porod_mw_errornull
pddf_i00.01028
pddf_i0_errornull
guinier_i00.01029
guinier_i0_error5.1e-05
pddf_rg2.71
pddf_rg_errornull
guinier_rg2.694
guinier_rg_error0.021
pddf_dmax8.9
pddf_dmax_errornull
porod_volume61.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first35
guinier_point_last164
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDFQ4_datloglog_img.png
symmetrynull
last_modified2021-09-27T16:14:08.329705+02:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDFQ4
statussuccess
started_at2026-08-11T14:28:38.841024+00:00
finished_at2026-08-11T14:28:47.844242+00:00
source_last_modified2021-09-27T16:14:08.329705+02:00
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View the complete summary.json source
{
  "code": "SASDFQ4",
  "status": "Published",
  "type_of_curve": "SEC-SAS",
  "angular_unit": "1/A",
  "project": {
    "title": "Conformationally constrained mutant of human matrix metalloproteinase-1",
    "publication": null,
    "status": "released",
    "submitted_date": "2019-03-26",
    "released_date": "2021-09-27"
  },
  "pddf_data": "https://www.sasbdb.org/media/p_of_R_files/SASDFQ4.out",
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  "intensities_log_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDFQ4_dat_img.png",
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  "pddf_plot": "https://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDFQ4_pofr_img.png",
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  "experiment": {
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        "name": "Pilatus 2M",
        "resolution": null
      },
      "name": "Diamond Light Source",
      "city": "Didcot",
      "country": "UK",
      "beamline_name": "B21",
      "beam_geometry": "1 x 5 mm",
      "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,
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    },
    "sample": {
      "molecule": [
        {
          "long_name": "Pro-matrix metalloproteinase-1 (Interstitial collagenase) (proMMP-1 S243C, S318C)",
          "short_name": "ProMMP-1 (S243C, S31",
          "sequence": "MFPATLETQEQDVDLVQKYLEKYYNLKNDGRQVEKRRNSGPV\r\nVEKLKQMQEFFGLKVTGKPDAETLKVMKQPRCGVPDVAQFVLTEGNPRWEQTHLTYRIEN\r\nYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGN\r\nLAHAFQPGPGIGGDAHFDEDERWTNNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSY\r\nTFCGDVQLAQDDIDGIQAIYGRSQNPVQPIGPQTPKACDSKLTFDAITTIRGEVMFFKDR\r\nFYMRTNPFYPEVELNFICVFWPQLPNGLEAAYEFADRDEVRFFKGNKYWAVQGQNVLHGY\r\nPKDIYSSFGFPRTVKHIDAALSEENTGKTYFFVANKYWRYDEYKRSMDPGYPKMIAHDFP\r\nGIGHKVDAVFMKDGFFYFFHGTRQYKFDPKTKRILTLQKANSWFNCRKN",
          "organism": "Homo sapiens",
          "uniprot_code": "P03956",
          "uniprot_range_first": 20,
          "uniprot_range_last": 469,
          "oligomerization": "monomer",
          "molecular_type": "protein",
          "uniprot_sequence": "MHSFPPLLLLLFWGVVSHSFPATLETQEQDVDLVQKYLEKYYNLKNDGRQVEKRRNSGPV\nVEKLKQMQEFFGLKVTGKPDAETLKVMKQPRCGVPDVAQFVLTEGNPRWEQTHLTYRIEN\nYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGN\nLAHAFQPGPGIGGDAHFDEDERWTNNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSY\nTFSGDVQLAQDDIDGIQAIYGRSQNPVQPIGPQTPKACDSKLTFDAITTIRGEVMFFKDR\nFYMRTNPFYPEVELNFISVFWPQLPNGLEAAYEFADRDEVRFFKGNKYWAVQGQNVLHGY\nPKDIYSSFGFPRTVKHIDAALSEENTGKTYFFVANKYWRYDEYKRSMDPGYPKMIAHDFP\nGIGHKVDAVFMKDGFFYFFHGTRQYKFDPKTKRILTLQKANSWFNCRKN",
          "mw": 52.007,
          "total_mw": 52.007,
          "number_molecules": 1,
          "complex_state": false,
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          "molecule_source": "biological",
          "molecule_description": null
        }
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        "concentration_unit": null,
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        "concentration": null,
        "pka": null,
        "ph": 7.4,
        "deuteration": null
      },
      "purity_method": null,
      "name": "Domain-stapled mutant of Pro-Matrix metalloproteinase-1 (proMMP-1 S243C, S318C)",
      "ext_coefficient": null,
      "contrast": null,
      "specific_vol": null,
      "dry_vol": null,
      "absorbption": null,
      "deuteration": null,
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    },
    "contributor": [
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        "affiliation": [
          {
            "short_name": null,
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            "webpage": "https://www.port.ac.uk"
          }
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        "orcid": ""
      }
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    "concentration_unit": null,
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    "cell_temperature": 25.0,
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    "wavelength": 0.1,
    "sample_detector_distance": 3.9,
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  "description": null,
  "experiment_description": "Synchrotron SAXS data from solutions of the domain-stapled mutant of pro-matrix metalloproteinase-1 (proMMP-1 S243C, S318C) in 50 mM Tris-HCl, 150 mM NaCl, 10 mM CaCl2, pH 7.4 were collected using size-exclusion chromatography SAXS (SEC-SAXS) on the B21 beam line at the Diamond Light Source (Oxfordshire, UK) using a Pilatus 2M detector at a sample-detector distance of 3.9 m and at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). SEC-SAXS was performed at 25 °C using the following parameters: Shodex Kw-403 analytical SEC column; Flow rate: 0.2 mL/min; Sample injection concentration: 5.6 mg/mL; Injection volume: 50 μL. The data were collected through the SEC peak of the sample as a series of 28 x 3 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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  "i0_calibration_standard_data": null,
  "intensities_log_log_plot": "SASDFQ4_datloglog_img.png",
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  "last_modified": "2021-09-27T16:14:08.329705+02:00",
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}
View the complete manifest.json source
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