SASDVX6

Monomeric Adhesion-associated domain in MUC4 and Other Proteins (AMOP-domain) of Isthmin-1, I455E, F458E douple mutant

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2025-04-27T20:19:00.615493+02:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Monomeric Adhesion-associated domain in MUC4 and Other Proteins (AMOP-domain) of Isthmin-1, I455E, F458E douple mutant

Concentration— – 3.0 Buffer / pH20 mM HEPES 100 mM NaCl / 7.5
Experimental temperature4.0 Facility / beamlinePennsylvania State University / Rigaku BioSAXS-2000
Wavelength0.1542 nmExposure600.0 s × 9

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
L-AMOP-IFEE
View sequence
GHHHHHHHHIEGRGIEDTFRTAATEVSLLAGSEEFNATKLFEVDTDSCERWMSCKSEFLKKYMHKVMNDLPSCPCSYPTEVAYSTADIFDRIKRKDFRWKDASGPKEKLEIYKPTARYCIRSMLSLESTTLAAQHCCYGDNMQLITRGKGAGTPNLISTEFSAELHYKVDVLPWIICKGDWSRYNEARPPNNGQKCTESPSDEDYEKQEQEAREY
proteinHomo sapiensB1AKI9263–464monomerMolecule count 124.776 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1607[3]0.00862952945–0.506676658 1/AHas uncertainty columnMissing 07sasbdb/entries/x6/sasdvx6/source/SASDVX6.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)8.8—Å
i0Guinier0.130989—1/cm
i0P(r)0.1322—1/cm
mwExperimental29.8—kDa
mwPorod29.8—kDa
porod_volumePorod46874.0—ų
rgGuinier2.3680.015Å
rgP(r)2.45—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 name20 mM HEPES 100 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 date2023-06-21Storage / measurement temperature4.0 / 4.0
Exposure time600.0Frames9
Wavelength0.1542Sample-to-detector distance0.491
SourceX-ray in houseDetectorRigaku HyPix-3000
Facility / beamlinePennsylvania State University / Rigaku BioSAXS-2000 · University Park, PA, USA
q range0.086 – 5.067Sample 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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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:134 field values
Field pathRaw value
codeSASDVX6
statusPublished
type_of_curveSingle concentration
angular_unit1/A
project.titleCrystal structure of Isthmin-1 and reassessment of its functional role in pre-adipocyte signaling.
project.publication.titleCrystal structure of Isthmin-1 and reassessment of its functional role in pre-adipocyte signaling.
project.publication.author_listLi T, Stayrook SE, Li W, Wang Y, Li H, Zhang J, Liu Y, Klein DE
project.publication.journalNat Commun
project.publication.doi10.1038/s41467-025-58828-w
project.publication.pmid40234450
project.publication.published_date2025 Apr 15
project.statusreleased
project.submitted_date2024-09-06
project.released_date2025-02-20
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sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDVX6.sascif
experiment.instrument.detector.typeHybrid Photon Counting (HPC) X-ray detector
experiment.instrument.detector.nameRigaku HyPix-3000
experiment.instrument.detector.resolution100.0
experiment.instrument.namePennsylvania State University
experiment.instrument.cityUniversity Park, PA
experiment.instrument.countryUSA
experiment.instrument.beamline_nameRigaku BioSAXS-2000
experiment.instrument.beam_geometrynull
experiment.instrument.type_of_sourceX-ray in house
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_nameL-AMOP-IFEE
experiment.sample.molecule[0].short_namenull
experiment.sample.molecule[0].sequenceGHHHHHHHHIEGRGIEDTFRTAATEVSLLAGSEEFNATKLFEVDTDSCERWMSCKSEFLKKYMHKVMNDLPSCPCSYPTEVAYSTADIFDRIKRKDFRWKDASGPKEKLEIYKPTARYCIRSMLSLESTTLAAQHCCYGDNMQLITRGKGAGTPNLISTEFSAELHYKVDVLPWIICKGDWSRYNEARPPNNGQKCTESPSDEDYEKQEQEAREY
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeB1AKI9
experiment.sample.molecule[0].uniprot_range_first263
experiment.sample.molecule[0].uniprot_range_last464
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMVRLAAELLLLLGLLLLTLHITVLRGSGAADGPDAAAGNASQAQLQNNLNVGSDTTSETS FSLSKEAPREHLDHQAAHQPFPRPRFRQETGHPSLQRDFPRSFLLDLPNFPDLSKADING QNPNIQVTIEVVDGPDSEADKDQHPENKPSWSVPSPDWRAWWQRSLSLARANSGDQDYKY DSTSDDSNFLNPPRGWDHTAPGHRTFETKDQPEYDSTDGEGDWSLWSVCSVTCGNGNQKR TRSCGYACTATESRTCDRPNCPGIEDTFRTAATEVSLLAGSEEFNATKLFEVDTDSCERW MSCKSEFLKKYMHKVMNDLPSCPCSYPTEVAYSTADIFDRIKRKDFRWKDASGPKEKLEI YKPTARYCIRSMLSLESTTLAAQHCCYGDNMQLITRGKGAGTPNLISTEFSAELHYKVDV LPWIICKGDWSRYNEARPPNNGQKCTESPSDEDYIKQFQEAREY
experiment.sample.molecule[0].mw24.776
experiment.sample.molecule[0].total_mw24.776
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_descriptionMonomeric Adhesion-associated domain in MUC4 and Other Proteins (AMOP-domain) of Isthmin-1, with a N-terminal 8x-HisTag. Point mutations are introduced into the C-terminal end of the construct E458F and E455I.
experiment.sample.buffer.name20 mM HEPES 100 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.nameMonomeric Adhesion-associated domain in MUC4 and Other Proteins (AMOP-domain) of Isthmin-1, I455E, F458E douple mutant
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 Haven, CT, USA
experiment.contributor[0].affiliation[0].full_nameYale University
experiment.contributor[0].affiliation[0].webpagehttps://www.yale.edu/
experiment.contributor[0].contributor_nameTongqing
experiment.contributor[0].contributor_surnameLi
experiment.contributor[0].orcidhttps://orcid.org/0000-0002-5272-4380
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2023-06-21
experiment.storage_temperature4.0
experiment.cell_temperature4.0
experiment.exposure_time600.0
experiment.number_of_frames9
experiment.wavelength0.1542
experiment.sample_detector_distance0.491
experiment.concentration_minnull
experiment.concentration_max3.0
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.086
experiment.s_max5.067
experiment.total_exposure_timenull
experiment.seccolumnnull
fits[]
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionnull
experiment_descriptionnull
tags[]
intensity_unit1/cm
experimental_mw29.8
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw29.8
porod_mw_errornull
pddf_i00.1322
pddf_i0_errornull
guinier_i00.130989
guinier_i0_errornull
pddf_rg2.45
pddf_rg_errornull
guinier_rg2.368
guinier_rg_error0.015
pddf_dmax8.8
pddf_dmax_errornull
porod_volume46874.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first2
guinier_point_last57
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDVX6_datloglog_img.png
symmetrynull
last_modified2025-04-27T20:19:00.615493+02:00
bragg_peak[]
manifest.json:34 field values
Field pathRaw value
codeSASDVX6
statussuccess
started_at2026-08-11T15:18:22.936346+00:00
finished_at2026-08-11T15:18:30.623471+00:00
source_last_modified2025-04-27T20:19:00.615493+02:00
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View the complete summary.json source
{
  "code": "SASDVX6",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "project": {
    "title": "Crystal structure of Isthmin-1 and reassessment of its functional role in pre-adipocyte signaling.",
    "publication": {
      "title": "Crystal structure of Isthmin-1 and reassessment of its functional role in pre-adipocyte signaling.",
      "author_list": "Li T, Stayrook SE, Li W, Wang Y, Li H, Zhang J, Liu Y, Klein DE",
      "journal": "Nat Commun",
      "doi": "10.1038/s41467-025-58828-w",
      "pmid": "40234450",
      "published_date": "2025 Apr 15"
    },
    "status": "released",
    "submitted_date": "2024-09-06",
    "released_date": "2025-02-20"
  },
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      "country": "USA",
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          "short_name": null,
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          "organism": "Homo sapiens",
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          "uniprot_range_first": 263,
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          "oligomerization": "monomer",
          "molecular_type": "protein",
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      "ext_coefficient": null,
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View the complete manifest.json source
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