SASDG55

Deglycosylated latency associated peptide, LAP (TGFB-1)

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2020-02-28T18:01:03.158567+01:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Deglycosylated latency associated peptide, LAP (TGFB-1)

Concentration— – 1.4 Buffer / pHphosphate buffered saline 2% glycerol / 7.4
Experimental temperature10.0 Facility / beamlineAdvanced Light Source (ALS) / 12.3.1 (SIBYLS)
Wavelength0.127 nmExposure0.1 s × 100

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Latency associated peptide
View sequence
>SP|P01137|30-278LSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRDRVAGESAEPEPEPEADYYAKEVTRVLMVETHNEIYDKFKQSTHSIYMFFNTSELREAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSNNSWRYLSNRLLAPSDSPEWLSFDVTGVVRQWLSRGGEIEGFRLSAHCSCDSRDNTLQVDINGFTTGRRGDLATIHGMNRPFLLLMATPLERAQHLQSSRHRAHHHHHH
proteinHomo sapiensP0113730–277dimerMolecule count 229.228 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1450[3]0.01087–0.261142 1/AHas uncertainty columnMissing 00sasbdb/entries/55/sasdg55/source/SASDG55.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)13.0—Å
i0Guinier1.990.01arbitrary
i0P(r)1.987—arbitrary
mwExperimental59.1—kDa
mwGuinier I(0)47.05.0kDa
porod_volumePorod129.0—ų
rgGuinier3.510.11Å
rgP(r)3.55—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 namephosphate buffered saline 2% glycerolBuffer concentration—
pH7.4Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2019-04-20Storage / measurement temperature4.0 / 10.0
Exposure time0.1Frames100
Wavelength0.127Sample-to-detector distance2.0
SourceX-ray synchrotronDetectorPilatus3 X 2M
Facility / beamlineAdvanced Light Source (ALS) / 12.3.1 (SIBYLS) · Berkeley, CA, USA
q range0.109 – 2.611Sample 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 (2 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:134 field values
Field pathRaw value
codeSASDG55
statusPublished
type_of_curveSingle concentration
angular_unit1/A
project.titleStructural insights into conformational switching in latency-associated peptide between transforming growth factor β-1 bound and unbound states
project.publication.titleStructural insights into conformational switching in latency-associated peptide between transforming growth factor β-1 bound and unbound states
project.publication.author_listStachowski T, Snell M, Snell E
project.publication.journalIUCrJ
project.publication.doi10.1107/S205225251901707X
project.publication.pmidnull
project.publication.published_date2020 Feb 06
project.statusreleased
project.submitted_date2019-09-04
project.released_date2020-02-28
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experiment.instrument.detector.typenull
experiment.instrument.detector.namePilatus3 X 2M
experiment.instrument.detector.resolution172.0
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_nameLatency associated peptide
experiment.sample.molecule[0].short_nameLAP
experiment.sample.molecule[0].sequence>sp|P01137|30-278 LSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRDRVA GESAEPEPEPEADYYAKEVTRVLMVETHNEIYDKFKQSTHSIYMFFNTSELREAVPEPVL LSRAELRLLRLKLKVEQHVELYQKYSNNSWRYLSNRLLAPSDSPEWLSFDVTGVVRQWLS RGGEIEGFRLSAHCSCDSRDNTLQVDINGFTTGRRGDLATIHGMNRPFLLLMATPLERAQ HLQSSRHRAHHHHHH
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeP01137
experiment.sample.molecule[0].uniprot_range_first30
experiment.sample.molecule[0].uniprot_range_last277
experiment.sample.molecule[0].oligomerizationdimer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMPPSGLRLLLLLLPLLWLLVLTPGRPAAGLSTCKTIDMELVKRKRIEAIRGQILSKLRLA SPPSQGEVPPGPLPEAVLALYNSTRDRVAGESAEPEPEPEADYYAKEVTRVLMVETHNEI YDKFKQSTHSIYMFFNTSELREAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSNNSWR YLSNRLLAPSDSPEWLSFDVTGVVRQWLSRGGEIEGFRLSAHCSCDSRDNTLQVDINGFT TGRRGDLATIHGMNRPFLLLMATPLERAQHLQSSRHRRALDTNYCFSSTEKNCCVRQLYI DFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHNPGASAAPCCVPQA LEPLPIVYYVGRKPKVEQLSNMIVRSCKCS
experiment.sample.molecule[0].mw29.228
experiment.sample.molecule[0].total_mw58.456
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.namephosphate buffered saline 2% glycerol
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.nameDeglycosylated latency associated peptide, LAP (TGFB-1)
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].addressNew York, USA
experiment.contributor[0].affiliation[0].full_nameHauptman-Woodward Medical Research Institute
experiment.contributor[0].affiliation[0].webpagehttp://hwi.buffalo.edu/
experiment.contributor[0].contributor_nameTim
experiment.contributor[0].contributor_surnameStachowski
experiment.contributor[0].orcidhttps://orcid.org/0000-0002-6097-4857
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2019-04-20
experiment.storage_temperature4.0
experiment.cell_temperature10.0
experiment.exposure_time0.1
experiment.number_of_frames100
experiment.wavelength0.127
experiment.sample_detector_distance2.0
experiment.concentration_minnull
experiment.concentration_max1.4
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.109
experiment.s_max2.611
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 deglycosylated latency associated peptide (LAP) from the transforming growth factor beta-1 proprotein (TGFB-1) in phosphate buffered saline, 2% glycerol, pH 7.4 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS; Berkeley, CA, USA) using a Pilatus3 X 2M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.127 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.40 mg/ml was measured at 10°C. 100 successive 0.100 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
tags[]
intensity_unitarbitrary
experimental_mw59.1
experimental_mw_errornull
guinier_i0_mw47.0
guinier_i0_mw_error5.0
porod_mwnull
porod_mw_errornull
pddf_i01.987
pddf_i0_errornull
guinier_i01.99
guinier_i0_error0.01
pddf_rg3.55
pddf_rg_errornull
guinier_rg3.51
guinier_rg_error0.11
pddf_dmax13.0
pddf_dmax_errornull
porod_volume129.0
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_plotSASDG55_datloglog_img.png
symmetrynull
last_modified2020-02-28T18:01:03.158567+01:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDG55
statussuccess
started_at2026-08-11T14:38:48.872881+00:00
finished_at2026-08-11T14:38:56.807631+00:00
source_last_modified2020-02-28T18:01:03.158567+01:00
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View the complete summary.json source
{
  "code": "SASDG55",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "project": {
    "title": "Structural insights into conformational switching in latency-associated peptide between transforming growth factor β-1 bound and unbound states",
    "publication": {
      "title": "Structural insights into conformational switching in latency-associated peptide between transforming growth factor β-1 bound and unbound states",
      "author_list": "Stachowski T, Snell M, Snell E",
      "journal": "IUCrJ",
      "doi": "10.1107/S205225251901707X",
      "pmid": null,
      "published_date": "2020 Feb 06"
    },
    "status": "released",
    "submitted_date": "2019-09-04",
    "released_date": "2020-02-28"
  },
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          "long_name": "Latency associated peptide",
          "short_name": "LAP",
          "sequence": ">sp|P01137|30-278\r\nLSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRDRVA\r\nGESAEPEPEPEADYYAKEVTRVLMVETHNEIYDKFKQSTHSIYMFFNTSELREAVPEPVL\r\nLSRAELRLLRLKLKVEQHVELYQKYSNNSWRYLSNRLLAPSDSPEWLSFDVTGVVRQWLS\r\nRGGEIEGFRLSAHCSCDSRDNTLQVDINGFTTGRRGDLATIHGMNRPFLLLMATPLERAQ\r\nHLQSSRHRAHHHHHH",
          "organism": "Homo sapiens",
          "uniprot_code": "P01137",
          "uniprot_range_first": 30,
          "uniprot_range_last": 277,
          "oligomerization": "dimer",
          "molecular_type": "protein",
          "uniprot_sequence": "MPPSGLRLLLLLLPLLWLLVLTPGRPAAGLSTCKTIDMELVKRKRIEAIRGQILSKLRLA\nSPPSQGEVPPGPLPEAVLALYNSTRDRVAGESAEPEPEPEADYYAKEVTRVLMVETHNEI\nYDKFKQSTHSIYMFFNTSELREAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSNNSWR\nYLSNRLLAPSDSPEWLSFDVTGVVRQWLSRGGEIEGFRLSAHCSCDSRDNTLQVDINGFT\nTGRRGDLATIHGMNRPFLLLMATPLERAQHLQSSRHRRALDTNYCFSSTEKNCCVRQLYI\nDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHNPGASAAPCCVPQA\nLEPLPIVYYVGRKPKVEQLSNMIVRSCKCS",
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          "molecule_source": "biological",
          "molecule_description": null
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        "comment": null,
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        "pka": null,
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      "purity_method": null,
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  "tags": [],
  "intensity_unit": "arbitrary",
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View the complete manifest.json source
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