SASDCN3

Phosphoenolpyruvate-protein phosphotransferase

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2023-03-02T16:54:05.368462+01:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Phosphoenolpyruvate-protein phosphotransferase

Concentration— – 5.0 Buffer / pH20mM TRIS buffer, 100 mM NaCl, 10 mM DTT, 4 mM MgCl2, 1 mM EDTA / 7.4
Experimental temperature25.0 Facility / beamlineAdvanced Photon Source (APS), Argonne National Laboratory / 12-ID-C
Wavelength0.06199 nmExposure0.25 s × 20

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Phosphoenolpyruvate-protein phosphotransferase
View sequence
MISGILASPGIAFGKALLLKEDEIVIDRKKISADQVDQEVERFLSGRAKASAQLETIKTKAGETFGEEKEAIFEGHIMLLEDEELEQEIIALIKDKHMTADAAAHEVIEGQASALEELDDEYLKERAADVRDIGKRLLRNILGLKIIDLSAIQDEVILVAADLTPSETAQLNLKKVLGFITDAGGRTSHTSIMARSLELPAIVGTGSVTSQVKNDDYLILDAVNNQVYVNPTNEVIDKMRAVQEQVASEKAELAKLKDLPAITLDGHQVEVCANIGTVRDVEGAERNGAEGVGLYRTEFLFMDRDALPTEEEQFAAYKAVAEACGSQAVIVRTMDIGGDKELPYMNFPKEENPFLGWRAIRIAMDRREILRDQLRAILRASAFGKLRIMFPMIISVEEVRALRKEIEIYKQELRDEGKAFDESIEIGVMVETPAAATIARHLAKEVDFFSIGTNDLTQYTLAVDRGNDMISHLYQPMSPSVLNLIKQVIDASHAEGKWTGMCGELAGDERATLLLLGMGLDEFSMSAISIPRIKKIIRNTNFEDAKVLAEQALAQPTTDELMTLVNKFIEEKTIC
proteinEscherichia coliA0A037YGN31–575dimerMolecule count 263.561 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1187[3]0.014426–0.22082 1/AHas uncertainty columnMissing 00sasbdb/entries/n3/sasdcn3/source/SASDCN3.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)14.750.5Å
i0Guinier0.0290498——
mwExperimental128.0—kDa
mwPorod118.0—kDa
porod_volumePorod189.0—ų
rgGuinier4.10.06Å
rgP(r)4.20.02Å

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

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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 name20mM TRIS buffer, 100 mM NaCl, 10 mM DTT, 4 mM MgCl2, 1 mM EDTABuffer concentration—
pH7.4Additives—
Buffer description1 tablet of protease inhibitor cocktail (SigmaFAST S8830) was added
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2010-08-23Storage / measurement temperature— / 25.0
Exposure time0.25Frames20
Wavelength0.06199Sample-to-detector distance4.0
SourceX-ray synchrotronDetectorGold CCD
Facility / beamlineAdvanced Photon Source (APS), Argonne National Laboratory / 12-ID-C · Lemont, IL, USA
q range0.144 – 2.208Sample 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:159 field values
Field pathRaw value
codeSASDCN3
statusPublished
type_of_curveSingle concentration
angular_unit1/A
project.titleSolution structure of the 128 kDa enzyme I dimer from Escherichia coli and its 146 kDa complex with HPr using residual dipolar couplings and small- and wide-angle X-ray scattering.
project.publication.titleSolution structure of the 128 kDa enzyme I dimer from Escherichia coli and its 146 kDa complex with HPr using residual dipolar couplings and small- and wide-angle X-ray scattering.
project.publication.author_listSchwieters CD, Suh JY, Grishaev A, Ghirlando R, Takayama Y, Clore GM
project.publication.journalJ Am Chem Soc
project.publication.doi10.1021/ja105485b
project.publication.pmid20731394
project.publication.published_date2010 Sep 22
project.statusreleased
project.submitted_date2017-05-23
project.released_date2017-05-23
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDCN3.out
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experiment.instrument.detector.typenull
experiment.instrument.detector.nameGold CCD
experiment.instrument.detector.resolutionnull
experiment.instrument.nameAdvanced Photon Source (APS), Argonne National Laboratory
experiment.instrument.cityLemont, IL
experiment.instrument.countryUSA
experiment.instrument.beamline_name12-ID-C
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_namePhosphoenolpyruvate-protein phosphotransferase
experiment.sample.molecule[0].short_nameEnzyme I
experiment.sample.molecule[0].sequenceMISGILASPGIAFGKALLLKEDEIVIDRKKISADQVDQEVERFLSGRAKASAQLETIKTKAGETFGEEKEAIFEGHIMLLEDEELEQEIIALIKDKHMTADAAAHEVIEGQASALEELDDEYLKERAADVRDIGKRLLRNILGLKIIDLSAIQDEVILVAADLTPSETAQLNLKKVLGFITDAGGRTSHTSIMARSLELPAIVGTGSVTSQVKNDDYLILDAVNNQVYVNPTNEVIDKMRAVQEQVASEKAELAKLKDLPAITLDGHQVEVCANIGTVRDVEGAERNGAEGVGLYRTEFLFMDRDALPTEEEQFAAYKAVAEACGSQAVIVRTMDIGGDKELPYMNFPKEENPFLGWRAIRIAMDRREILRDQLRAILRASAFGKLRIMFPMIISVEEVRALRKEIEIYKQELRDEGKAFDESIEIGVMVETPAAATIARHLAKEVDFFSIGTNDLTQYTLAVDRGNDMISHLYQPMSPSVLNLIKQVIDASHAEGKWTGMCGELAGDERATLLLLGMGLDEFSMSAISIPRIKKIIRNTNFEDAKVLAEQALAQPTTDELMTLVNKFIEEKTIC
experiment.sample.molecule[0].organismEscherichia coli
experiment.sample.molecule[0].uniprot_codeA0A037YGN3
experiment.sample.molecule[0].uniprot_range_first1
experiment.sample.molecule[0].uniprot_range_last575
experiment.sample.molecule[0].oligomerizationdimer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMISGILASPGIAFGKALLLKEDEIVIDRKKISADQVDQEVERFLSGRAKASAQLETIKTK AGETFGEEKEAIFEGHIMLLEDEELEQEIIALIKDKHMTADAAAHEVIEGQASALEELDD EYLKERAADVRDIGKRLLRNILGLKIIDLSAIQDEVILVAADLTPSETAQLNLKKVLGFI TDAGGRTSHTSIMARSLELPAIVGTGSVTSQVKNDDYLILDAVNNQVYVNPTNEVIDKMR AVQEQVASEKAELAKLKDLPAITLDGHQVEVCANIGTVRDVEGAERNGAEGVGLYRTEFL FMDRDALPTEEEQFAAYKAVAEACGSQAVIVRTMDIGGDKELPYMNFPKEENPFLGWRAI RIAMDRREILRDQLRAILRASAFGKLRIMFPMIISVEEVRALRKEIEIYKQELRDEGKAF DESIEIGVMVETPAAATIARHLAKEVDFFSIGTNDLTQYTLAVDRGNDMISHLYQPMSPS VLNLIKQVIDASHAEGKWTGMCGELAGDERATLLLLGMGLDEFSMSAISIPRIKKIIRNT NFEDAKVLAEQALAQPTTDELMTLVNKFIEEKTIC
experiment.sample.molecule[0].mw63.561
experiment.sample.molecule[0].total_mw127.122
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.name20mM TRIS buffer, 100 mM NaCl, 10 mM DTT, 4 mM MgCl2, 1 mM EDTA
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.comment1 tablet of protease inhibitor cocktail (SigmaFAST S8830) was added
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.namePhosphoenolpyruvate-protein phosphotransferase
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_nameEBI
experiment.contributor[0].affiliation[0].addressHinxton, UK
experiment.contributor[0].affiliation[0].full_nameEMBL-EBI
experiment.contributor[0].affiliation[0].webpagehttp://www.ebi.ac.uk/
experiment.contributor[0].contributor_nameMihaly
experiment.contributor[0].contributor_surnameVaradi
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2010-08-23
experiment.storage_temperaturenull
experiment.cell_temperature25.0
experiment.exposure_time0.25
experiment.number_of_frames20
experiment.wavelength0.06199
experiment.sample_detector_distance4.0
experiment.concentration_minnull
experiment.concentration_max5.0
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.144
experiment.s_max2.208
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].models[0].softwarePDB (Protein Data Bank)
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fits[0].models[0].pdb_link[0].ext_code2KX9
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fits[0].models[0].software_version
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fits[0].models[0].model_mw126.6
fits[0].models[0].bead_radius1.9
fits[0].models[0].lognull
fits[0].models[0].symmetry
fits[0].models[0].comment
fits[0].models[0].user107
fits[0].fit_unit1/A
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fits[0].softwareCRYSOL
fits[0].chi_square_value0.341
fits[0].p_value0.0
fits[0].fit_residual_plotSASDCN3_fit1_fitresiduals_img.png
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fits[0].software_version2.8.3
fits[0].descriptionnull
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_versionnull
i0_calibration_standardnull
descriptionnull
experiment_descriptionSynchrotron SAXS data from a solution of Phosphoenolpyruvate-protein phosphotransferase in 20 mM TRIS buffer, pH 7.4, 100 mM NaCl, 10 mM DTT, 4 mM MgCl2, 1 mM EDTA, and 1 tablet of protease inhibitor cocktail (SigmaFAST S8830) were acquired at the beamline 12ID-C at the Advanced Photon Source (APS, Argonne, IL, USA). One solute concentration of 5 mg/ml (corresponding to ∼40 μM dimer) was measured at 25°C using a Gold CCD detector at a sample-detector distance of 4 m and at a wavelength of λ = 0.06199 nm (s = 4π sin θ/λ, where 2θ is the scattering angle). 20 successive 0.25 second frames were collected. To prevent radiation damage, volumes of 150 μL of samples and buffers were oscillated during data collection using a flow-though setup. Individual data frames were masked, corrected for the detector sensitivity, radially integrated and normalized by the corresponding incident beam intensities. The final 1D scattering profiles and their uncertainties were calculated as means and standard deviations over the 20 individual frames. The buffer data were then subtracted from the scattering profiles.
tags[]
intensity_unitnull
experimental_mw128.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw118.0
porod_mw_errornull
pddf_i0null
pddf_i0_errornull
guinier_i00.0290498
guinier_i0_errornull
pddf_rg4.2
pddf_rg_error0.02
guinier_rg4.1
guinier_rg_error0.06
pddf_dmax14.75
pddf_dmax_error0.5
porod_volume189.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_firstnull
guinier_point_lastnull
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDCN3_datloglog_img.png
symmetrynull
last_modified2023-03-02T16:54:05.368462+01:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDCN3
statussuccess
started_at2026-08-11T14:03:54.557538+00:00
finished_at2026-08-11T14:04:05.204096+00:00
source_last_modified2023-03-02T16:54:05.368462+01:00
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View the complete summary.json source
{
  "code": "SASDCN3",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "project": {
    "title": "Solution structure of the 128 kDa enzyme I dimer from Escherichia coli and its 146 kDa complex with HPr using residual dipolar couplings and small- and wide-angle X-ray scattering.",
    "publication": {
      "title": "Solution structure of the 128 kDa enzyme I dimer from Escherichia coli and its 146 kDa complex with HPr using residual dipolar couplings and small- and wide-angle X-ray scattering.",
      "author_list": "Schwieters CD, Suh JY, Grishaev A, Ghirlando R, Takayama Y, Clore GM",
      "journal": "J Am Chem Soc",
      "doi": "10.1021/ja105485b",
      "pmid": "20731394",
      "published_date": "2010 Sep 22"
    },
    "status": "released",
    "submitted_date": "2017-05-23",
    "released_date": "2017-05-23"
  },
  "pddf_data": "https://www.sasbdb.org/media/p_of_R_files/SASDCN3.out",
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  "pddf_plot": "https://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDCN3_pofr_img.png",
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  "experiment": {
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      "country": "USA",
      "beamline_name": "12-ID-C",
      "beam_geometry": null,
      "type_of_source": "X-ray synchrotron",
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      "beam_profile_ah": null,
      "beam_profile_al": null
    },
    "sample": {
      "molecule": [
        {
          "long_name": "Phosphoenolpyruvate-protein phosphotransferase",
          "short_name": "Enzyme I",
          "sequence": "MISGILASPGIAFGKALLLKEDEIVIDRKKISADQVDQEVERFLSGRAKASAQLETIKTKAGETFGEEKEAIFEGHIMLLEDEELEQEIIALIKDKHMTADAAAHEVIEGQASALEELDDEYLKERAADVRDIGKRLLRNILGLKIIDLSAIQDEVILVAADLTPSETAQLNLKKVLGFITDAGGRTSHTSIMARSLELPAIVGTGSVTSQVKNDDYLILDAVNNQVYVNPTNEVIDKMRAVQEQVASEKAELAKLKDLPAITLDGHQVEVCANIGTVRDVEGAERNGAEGVGLYRTEFLFMDRDALPTEEEQFAAYKAVAEACGSQAVIVRTMDIGGDKELPYMNFPKEENPFLGWRAIRIAMDRREILRDQLRAILRASAFGKLRIMFPMIISVEEVRALRKEIEIYKQELRDEGKAFDESIEIGVMVETPAAATIARHLAKEVDFFSIGTNDLTQYTLAVDRGNDMISHLYQPMSPSVLNLIKQVIDASHAEGKWTGMCGELAGDERATLLLLGMGLDEFSMSAISIPRIKKIIRNTNFEDAKVLAEQALAQPTTDELMTLVNKFIEEKTIC",
          "organism": "Escherichia coli",
          "uniprot_code": "A0A037YGN3",
          "uniprot_range_first": 1,
          "uniprot_range_last": 575,
          "oligomerization": "dimer",
          "molecular_type": "protein",
          "uniprot_sequence": "MISGILASPGIAFGKALLLKEDEIVIDRKKISADQVDQEVERFLSGRAKASAQLETIKTK\nAGETFGEEKEAIFEGHIMLLEDEELEQEIIALIKDKHMTADAAAHEVIEGQASALEELDD\nEYLKERAADVRDIGKRLLRNILGLKIIDLSAIQDEVILVAADLTPSETAQLNLKKVLGFI\nTDAGGRTSHTSIMARSLELPAIVGTGSVTSQVKNDDYLILDAVNNQVYVNPTNEVIDKMR\nAVQEQVASEKAELAKLKDLPAITLDGHQVEVCANIGTVRDVEGAERNGAEGVGLYRTEFL\nFMDRDALPTEEEQFAAYKAVAEACGSQAVIVRTMDIGGDKELPYMNFPKEENPFLGWRAI\nRIAMDRREILRDQLRAILRASAFGKLRIMFPMIISVEEVRALRKEIEIYKQELRDEGKAF\nDESIEIGVMVETPAAATIARHLAKEVDFFSIGTNDLTQYTLAVDRGNDMISHLYQPMSPS\nVLNLIKQVIDASHAEGKWTGMCGELAGDERATLLLLGMGLDEFSMSAISIPRIKKIIRNT\nNFEDAKVLAEQALAQPTTDELMTLVNKFIEEKTIC",
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          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": null
        }
      ],
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        "concentration_unit": null,
        "comment": "1 tablet of protease inhibitor cocktail (SigmaFAST S8830) was added",
        "additive": null,
        "concentration": null,
        "pka": null,
        "ph": 7.4,
        "deuteration": null
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      "name": "Phosphoenolpyruvate-protein phosphotransferase",
      "ext_coefficient": null,
      "contrast": null,
      "specific_vol": null,
      "dry_vol": null,
      "absorbption": null,
      "deuteration": null,
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    },
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        "affiliation": [
          {
            "short_name": "EBI",
            "address": "Hinxton, UK",
            "full_name": "EMBL-EBI",
            "webpage": "http://www.ebi.ac.uk/"
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        "contributor_surname": "Varadi",
        "orcid": null
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    "concentration_unit": null,
    "date": "2010-08-23",
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    "cell_temperature": 25.0,
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    "wavelength": 0.06199,
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              "difference_with_model": "identical"
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  "last_modified": "2023-03-02T16:54:05.368462+01:00",
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}
View the complete manifest.json source
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