SASDB27

Chimeric EcRHH-RcPutA: The E.coli Proline utilization A RHH domain fused to R.capsulatus PutA

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2026-05-18T10:07:55.648439+02:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Chimeric EcRHH-RcPutA: The E.coli Proline utilization A RHH domain fused to R.capsulatus PutA

Concentration— – 6.0 Buffer / pH50 mM Tris, 200 mM NaCl, 0.5 mM Tris(3-hydroxypropyl)phosphine / 7.5
Experimental temperature20.0 Facility / beamlineAdvanced Light Source (ALS) / 12.3.1 (SIBYLS)
Wavelength0.1 nmExposure0.5 s × 2

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Proline utilization A
View sequence
MGSSHHHHHHSSGLVPRGSHMGTTTMGVKLDDATRERIKSAATRIDRTPHWLIKQAIFSYLEQLENSDTLPEHMTDLSALGPKAKFAPEAEVLQALVAQAALPQPQLDRIAARGADLVARIRAEAKPSLMEHFLAQYGLSTREGVALMCLAEAMLRVPDTATIDALIEDKIAPSDWGKHLGTAASSLVNASTWALMLTGKVLDDGAGGIAGTLRGAMRRLGEPVIRAAVGQAMREMGRQFVLGETIEKALERAEKREAEGYTFSYDMLGEAALTAADAERYRLAYAQAITAIGKAATRGSIAANPGISIKLSALHPRYEVAQEARVMAELVPVVRDLARAAARAGIALHIDAEEQDRLALSLRVMAAVIADPETAGWEGFGAVVQAYGKRAGAAIDALAAMARAAGRRINIRLVKGAYWDAEMKRAQVEGHPGFPLFTSKTGTDVAYICLAAKLFGLNDCIYPQFATHNAHTVAAVLEMAAGRPFEFQRLHGMGARLHDIVLRETGGRCRIYAPVGAHRDLLAYLVRRLLENGANSSFVNQIVNESVPPAEVAACPFAALPTARAPRGLLAPADLFGAGRVNAQGFDLSDPEVLARIEAARDVTLPDAAPIVAGPVSGTLRPVRNPATGAVVAQVTEADAATVALALDAAQVWSAPAATRAAVLCRAADLYEENFGPIFAALAQEAGKTLGDAVSELREAVDFLRYYAAEGAADTRPPRGAVVAISPWNFPLAIFTGQVAAALMAGNAVLAKPAEQTPIIAALAVRLLHQAGVPETALQLLPGDGPTVGAALTRDPRVAGVVFTGSTETAQIIARAMAAHLAPGTPLIAETGGLNAMVVDSTALPEQAVRDVVASAFRSAGQRCSALRCLYVQDDIAPHLIGMLKGAMEELVSGDPARLSTDVGPVIDAEAKAGIETYLAANKARILHRSTAPEGGHFVAPALLQVGGIADLEREIFGPVLHLATFAAEDLPAVIAAINARGYGLTFGLHSRIDARVETVAETIRAGNIYVNRNQIGAVVGSQPFGGEGLSGTGPKAGGPLYLNRFYAPEPVVAVGGWTEAATPILPEARETQLDEIFLPGPTGELNRLTRHQRGPILCLGPGAEAASAQAAAVVALGGQAVQASGAVSPKALETLTPLAGVLWWGAAEMGRAYAQALAVRPGPLVPLITAKPDLAHVAHERHLCVDTTAAGGNAALLAG
proteinEscherchia coli, Rhodobacter capsulatus——–—dimerMolecule count 2125.528 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1503[3]0.01125–0.316495 1/AHas uncertainty columnMissing 00sasbdb/entries/27/sasdb27/source/SASDB27.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)18.31.0Å
i0Guinier3011.4411.0—
i0P(r)3033.05.5—
mwExperimental251.0—kDa
porod_volumePorod308.0—ų
rgGuinier5.20.02Å
rgP(r)5.410.008Å

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, 200 mM NaCl, 0.5 mM Tris(3-hydroxypropyl)phosphineBuffer concentration—
pH7.5Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2012-10-16Storage / measurement temperature4.0 / 20.0
Exposure time0.5Frames2
Wavelength0.1Sample-to-detector distance1.5
SourceX-ray synchrotronDetectorMAR 165 CCD
Facility / beamlineAdvanced Light Source (ALS) / 12.3.1 (SIBYLS) · Berkeley, CA, USA
q range0.112 – 3.165Sample 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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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
codeSASDB27
statusPublished
type_of_curveSingle concentration
angular_unit1/A
project.titleEngineering a trifunctional proline utilization A chimaera by fusing a DNA-binding domain to a bifunctional PutA.
project.publication.titleEngineering a trifunctional proline utilization A chimaera by fusing a DNA-binding domain to a bifunctional PutA.
project.publication.author_listArentson BW, Hayes EL, Zhu W, Singh H, Tanner JJ, Becker DF
project.publication.journalBiosci Rep
project.publication.doi10.1042/BSR20160435
project.publication.pmid27742866
project.publication.published_date2016 Dec
project.statusreleased
project.submitted_date2016-10-10
project.released_date2016-10-16
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDB27.out
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experiment.instrument.detector.typenull
experiment.instrument.detector.nameMAR 165 CCD
experiment.instrument.detector.resolutionnull
experiment.instrument.nameAdvanced Light Source (ALS)
experiment.instrument.cityBerkeley, CA
experiment.instrument.countryUSA
experiment.instrument.beamline_name12.3.1 (SIBYLS)
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_nameProline utilization A
experiment.sample.molecule[0].short_namePutA
experiment.sample.molecule[0].sequenceMGSSHHHHHHSSGLVPRGSH MGTTTMGVKLDDATRERIKSAATRIDRTPHWLIKQAIFSY LEQLENSDTLPEH MTDLSALGPKAKFAPEAEVLQALVAQAALPQPQLDRIAARGADLVAR IRAEAKPSLMEHFLAQYGLSTREGVALMCLAEAMLRVPDTATIDALIEDKIAPSDWGKHL GTAASSLVNASTWALMLTGKVLDDGAGGIAGTLRGAMRRLGEPVIRAAVGQAMREMGRQF VLGETIEKALERAEKREAEGYTFSYDMLGEAALTAADAERYRLAYAQAITAIGKAATRGS IAANPGISIKLSALHPRYEVAQEARVMAELVPVVRDLARAAARAGIALHIDAEEQDRLAL SLRVMAAVIADPETAGWEGFGAVVQAYGKRAGAAIDALAAMARAAGRRINIRLVKGAYWD AEMKRAQVEGHPGFPLFTSKTGTDVAYICLAAKLFGLNDCIYPQFATHNAHTVAAVLEMA AGRPFEFQRLHGMGARLHDIVLRETGGRCRIYAPVGAHRDLLAYLVRRLLENGANSSFVN QIVNESVPPAEVAACPFAALPTARAPRGLLAPADLFGAGRVNAQGFDLSDPEVLARIEAA RDVTLPDAAPIVAGPVSGTLRPVRNPATGAVVAQVTEADAATVALALDAAQVWSAPAATR AAVLCRAADLYEENFGPIFAALAQEAGKTLGDAVSELREAVDFLRYYAAEGAADTRPPRG AVVAISPWNFPLAIFTGQVAAALMAGNAVLAKPAEQTPIIAALAVRLLHQAGVPETALQL LPGDGPTVGAALTRDPRVAGVVFTGSTETAQIIARAMAAHLAPGTPLIAETGGLNAMVVD STALPEQAVRDVVASAFRSAGQRCSALRCLYVQDDIAPHLIGMLKGAMEELVSGDPARLS TDVGPVIDAEAKAGIETYLAANKARILHRSTAPEGGHFVAPALLQVGGIADLEREIFGPV LHLATFAAEDLPAVIAAINARGYGLTFGLHSRIDARVETVAETIRAGNIYVNRNQIGAVV GSQPFGGEGLSGTGPKAGGPLYLNRFYAPEPVVAVGGWTEAATPILPEARETQLDEIFLP GPTGELNRLTRHQRGPILCLGPGAEAASAQAAAVVALGGQAVQASGAVSPKALETLTPLA GVLWWGAAEMGRAYAQALAVRPGPLVPLITAKPDLAHVAHERHLCVDTTAAGGNAALLAG
experiment.sample.molecule[0].organismEscherchia coli, Rhodobacter capsulatus
experiment.sample.molecule[0].uniprot_codenull
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_sequencenull
experiment.sample.molecule[0].mw125.528
experiment.sample.molecule[0].total_mw251.056
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.name50 mM Tris, 200 mM NaCl, 0.5 mM Tris(3-hydroxypropyl)phosphine
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.nameChimeric EcRHH-RcPutA: The E.coli Proline utilization A RHH domain fused to R.capsulatus PutA
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_nameMizzou
experiment.contributor[0].affiliation[0].addressColumbia, MO, USA
experiment.contributor[0].affiliation[0].full_nameUniversity of Missouri-Columbia
experiment.contributor[0].affiliation[0].webpagehttp://missouri.edu/
experiment.contributor[0].contributor_nameJohn
experiment.contributor[0].contributor_surnameTanner
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2012-10-16
experiment.storage_temperature4.0
experiment.cell_temperature20.0
experiment.exposure_time0.5
experiment.number_of_frames2
experiment.wavelength0.1
experiment.sample_detector_distance1.5
experiment.concentration_minnull
experiment.concentration_max6.0
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.112
experiment.s_max3.165
experiment.total_exposure_timenull
experiment.seccolumnnull
fits[]
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_versionGNOM
i0_calibration_standardnull
descriptionnull
experiment_descriptionSynchrotron SAXS data from solutions of a chimeric EcRHH-RcPutA protein fusion in 50 mM Tris, 200 mM NaCl, 0.5 mM Tris(3-hydroxypropyl)phosphine, pH 7.5 were collected on the 12.3.1 (SIBYLS) camera on the storage ring Advanced Light Source (ALS) (Berkeley, CA, USA) using a MAR 165 CCD detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4π sin θ/λ and 2θ is the scattering angle). A solute concentrations of 6 mg/ml was measured at 20°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. The merged SAXS curve displayed in this entry was obtained by merging the low-s region (points 2-140, s=0.1125 — 0.9517 nm-1) from an image collected with an exposure time of 0.5 s with the higher-s region (points 19-505, s=0.2159 — 3.1710 nm-1) of a profile collected with exposure time of 2.0 s. The errors in PDDF Rg and I0 were estimated by running GNOM via primus/qt (r4556) assuming Dmax in the range of 173-193 and using all points of the scattering curve (1-503).
tags[]
intensity_unitnull
experimental_mw251.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mwnull
porod_mw_errornull
pddf_i03033.0
pddf_i0_error5.5
guinier_i03011.44
guinier_i0_error11.0
pddf_rg5.41
pddf_rg_error0.008
guinier_rg5.2
guinier_rg_error0.02
pddf_dmax18.3
pddf_dmax_error1.0
porod_volume308.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first1
guinier_point_last23
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDB27_datloglog_img.png
symmetrynull
last_modified2026-05-18T10:07:55.648439+02:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDB27
statussuccess
started_at2026-08-11T15:20:00.476624+00:00
finished_at2026-08-11T15:20:08.500214+00:00
source_last_modified2026-05-18T10:07:55.648439+02:00
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View the complete summary.json source
{
  "code": "SASDB27",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "project": {
    "title": "Engineering a trifunctional proline utilization A chimaera by fusing a DNA-binding domain to a bifunctional PutA.",
    "publication": {
      "title": "Engineering a trifunctional proline utilization A chimaera by fusing a DNA-binding domain to a bifunctional PutA.",
      "author_list": "Arentson BW, Hayes EL, Zhu W, Singh H, Tanner JJ, Becker DF",
      "journal": "Biosci Rep",
      "doi": "10.1042/BSR20160435",
      "pmid": "27742866",
      "published_date": "2016 Dec"
    },
    "status": "released",
    "submitted_date": "2016-10-10",
    "released_date": "2016-10-16"
  },
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      "point_source": null,
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    "sample": {
      "molecule": [
        {
          "long_name": "Proline utilization A",
          "short_name": "PutA",
          "sequence": "MGSSHHHHHHSSGLVPRGSH\r\nMGTTTMGVKLDDATRERIKSAATRIDRTPHWLIKQAIFSY\r\nLEQLENSDTLPEH\r\nMTDLSALGPKAKFAPEAEVLQALVAQAALPQPQLDRIAARGADLVAR\r\nIRAEAKPSLMEHFLAQYGLSTREGVALMCLAEAMLRVPDTATIDALIEDKIAPSDWGKHL\r\nGTAASSLVNASTWALMLTGKVLDDGAGGIAGTLRGAMRRLGEPVIRAAVGQAMREMGRQF\r\nVLGETIEKALERAEKREAEGYTFSYDMLGEAALTAADAERYRLAYAQAITAIGKAATRGS\r\nIAANPGISIKLSALHPRYEVAQEARVMAELVPVVRDLARAAARAGIALHIDAEEQDRLAL\r\nSLRVMAAVIADPETAGWEGFGAVVQAYGKRAGAAIDALAAMARAAGRRINIRLVKGAYWD\r\nAEMKRAQVEGHPGFPLFTSKTGTDVAYICLAAKLFGLNDCIYPQFATHNAHTVAAVLEMA\r\nAGRPFEFQRLHGMGARLHDIVLRETGGRCRIYAPVGAHRDLLAYLVRRLLENGANSSFVN\r\nQIVNESVPPAEVAACPFAALPTARAPRGLLAPADLFGAGRVNAQGFDLSDPEVLARIEAA\r\nRDVTLPDAAPIVAGPVSGTLRPVRNPATGAVVAQVTEADAATVALALDAAQVWSAPAATR\r\nAAVLCRAADLYEENFGPIFAALAQEAGKTLGDAVSELREAVDFLRYYAAEGAADTRPPRG\r\nAVVAISPWNFPLAIFTGQVAAALMAGNAVLAKPAEQTPIIAALAVRLLHQAGVPETALQL\r\nLPGDGPTVGAALTRDPRVAGVVFTGSTETAQIIARAMAAHLAPGTPLIAETGGLNAMVVD\r\nSTALPEQAVRDVVASAFRSAGQRCSALRCLYVQDDIAPHLIGMLKGAMEELVSGDPARLS\r\nTDVGPVIDAEAKAGIETYLAANKARILHRSTAPEGGHFVAPALLQVGGIADLEREIFGPV\r\nLHLATFAAEDLPAVIAAINARGYGLTFGLHSRIDARVETVAETIRAGNIYVNRNQIGAVV\r\nGSQPFGGEGLSGTGPKAGGPLYLNRFYAPEPVVAVGGWTEAATPILPEARETQLDEIFLP\r\nGPTGELNRLTRHQRGPILCLGPGAEAASAQAAAVVALGGQAVQASGAVSPKALETLTPLA\r\nGVLWWGAAEMGRAYAQALAVRPGPLVPLITAKPDLAHVAHERHLCVDTTAAGGNAALLAG",
          "organism": "Escherchia coli, Rhodobacter capsulatus",
          "uniprot_code": null,
          "uniprot_range_first": null,
          "uniprot_range_last": null,
          "oligomerization": "dimer",
          "molecular_type": "protein",
          "uniprot_sequence": null,
          "mw": 125.528,
          "total_mw": 251.056,
          "number_molecules": 2,
          "complex_state": false,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": null
        }
      ],
      "buffer": {
        "name": "50 mM Tris, 200 mM NaCl, 0.5 mM Tris(3-hydroxypropyl)phosphine",
        "concentration_unit": null,
        "comment": null,
        "additive": null,
        "concentration": null,
        "pka": null,
        "ph": 7.5,
        "deuteration": null
      },
      "purity_method": null,
      "name": "Chimeric EcRHH-RcPutA: The E.coli Proline utilization A RHH domain fused to R.capsulatus PutA",
      "ext_coefficient": null,
      "contrast": null,
      "specific_vol": null,
      "dry_vol": null,
      "absorbption": null,
      "deuteration": null,
      "mixture": null
    },
    "contributor": [
      {
        "affiliation": [
          {
            "short_name": "Mizzou",
            "address": "Columbia, MO, USA",
            "full_name": "University of Missouri-Columbia",
            "webpage": "http://missouri.edu/"
          }
        ],
        "contributor_name": "John",
        "contributor_surname": "Tanner",
        "orcid": null
      }
    ],
    "concentration_method": null,
    "concentration_unit": null,
    "date": "2012-10-16",
    "storage_temperature": 4.0,
    "cell_temperature": 20.0,
    "exposure_time": 0.5,
    "number_of_frames": 2,
    "wavelength": 0.1,
    "sample_detector_distance": 1.5,
    "concentration_min": null,
    "concentration_max": 6.0,
    "sample_volume": null,
    "flow_rate": null,
    "s_min": 0.112,
    "s_max": 3.165,
    "total_exposure_time": null,
    "seccolumn": null
  },
  "fits": [],
  "estimated_volume_method": null,
  "pddf_software": "ATSAS GNOM",
  "pddf_software_version": "GNOM",
  "i0_calibration_standard": null,
  "description": null,
  "experiment_description": "Synchrotron SAXS data from solutions of a chimeric EcRHH-RcPutA protein fusion in 50 mM Tris, 200 mM NaCl, 0.5 mM Tris(3-hydroxypropyl)phosphine, pH 7.5 were collected on the 12.3.1 (SIBYLS) camera on the storage ring Advanced Light Source (ALS) (Berkeley, CA, USA) using a MAR 165 CCD detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4π sin θ/λ and  2θ is the scattering angle). A solute concentrations of 6 mg/ml was measured at 20°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. The merged SAXS curve displayed in this entry was obtained by merging the low-s region (points 2-140, s=0.1125 — 0.9517 nm-1) from an image collected with an exposure time of 0.5 s with the higher-s region (points 19-505, s=0.2159 — 3.1710 nm-1) of a profile collected with exposure time of 2.0 s. The errors in PDDF Rg and I0 were estimated by running GNOM via primus/qt (r4556) assuming Dmax in the range of 173-193 and using all points of the scattering curve (1-503).",
  "tags": [],
  "intensity_unit": null,
  "experimental_mw": 251.0,
  "experimental_mw_error": null,
  "guinier_i0_mw": null,
  "guinier_i0_mw_error": null,
  "porod_mw": null,
  "porod_mw_error": null,
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  "pddf_i0_error": 5.5,
  "guinier_i0": 3011.44,
  "guinier_i0_error": 11.0,
  "pddf_rg": 5.41,
  "pddf_rg_error": 0.008,
  "guinier_rg": 5.2,
  "guinier_rg_error": 0.02,
  "pddf_dmax": 18.3,
  "pddf_dmax_error": 1.0,
  "porod_volume": 308.0,
  "porod_volume_error": null,
  "estimated_volume": null,
  "estimated_volume_error": null,
  "guinier_point_first": 1,
  "guinier_point_last": 23,
  "pddf_point_first": null,
  "pddf_point_last": null,
  "i0_calibration_standard_data": null,
  "intensities_log_log_plot": "SASDB27_datloglog_img.png",
  "symmetry": null,
  "last_modified": "2026-05-18T10:07:55.648439+02:00",
  "bragg_peak": []
}
View the complete manifest.json source
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