SASDFD3

Filamin A Ig-like domains 4-6 (FLNa4-6)

Data type: SASBDB experimental data Status: Published Curve type: Merged Last updated: 2019-12-06T13:07:15.624532+01:00

Wild type three-domain fragment of human Filamin A Ig-like domains 4-6 (FLNa4-6). There are two extra amino acids, Met and Ser, in the very N-terminus of the polypeptide that have resulted from TEV-cleavage of the GST fusion tag during the protein purification.

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Filamin A Ig-like domains 4-6 (FLNa4-6)

Concentration2.0 – 4.0 Buffer / pH20 mM Tris, 100 mM NaCl, 1 mM DTT / 8.0
Experimental temperature20.0 Facility / beamlineESRF / BM29
Wavelength0.1 nmExposure— s × —

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Filamin A Ig-like domains 4-6
View sequence
MSCGNQKVRAWGPGLEGGVVGKSADFVVEAIGDDVGTLGFSVEGPSQAKIECDDKGDGSCDVRYWPQEAGEYAVHVLCNSEDIRLSPFMADIRDAPQDFHPDRVKARGPGLEKTGVAVNKPAEFTVDAKHGGKAPLRVQVQDNEGCPVEALVKDNGNGTYSCSYVPRKPVKHTAMVSWGGVSIPNSPFRVNVGAGSHPNKVKVYGPGVAKTGLKAHEPTYFTVDCAEAGQGDVSIGIKCAPGVVGPAEADIDFDIIRNDNDTFTVKYTPRGAGSYTIMVLFADQATPTSPIRVKVEPS
proteinHomo sapiensP21333574–869monomerMolecule count 131.52 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1650[3]0.07412654–3.129303 1/nmHas uncertainty columnMissing 00sasbdb/entries/d3/sasdfd3/source/SASDFD3.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)9.5—nm
i0Guinier23.720.03arbitrary
i0P(r)23.910.03arbitrary
mwExperimental23.4—kDa
mwPorod25.0—kDa
porod_volumePorod41.0—nm³
rgGuinier2.730.03nm
rgP(r)2.820.005nm

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

Fit 1 · DAMMIF

χ²: 0.855CorMap p: 0.426529Unit: 1/A

Fit of one of the 20 DAMMIF-models created for FLNa4-6

ModelName / TypeSoftwareSymmetryModel MWPDB DeclarationSource file
1—dummyDAMFILT DAMFILT 5P128.031—Model Image
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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 Tris, 100 mM NaCl, 1 mM DTTBuffer concentration—
pH8.0Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2017-02-10Storage / measurement temperature— / 20.0
Exposure time—Frames—
Wavelength0.1Sample-to-detector distance2.9
SourceX-ray synchrotronDetectorPilatus 1M
Facility / beamlineESRF / BM29 · Grenoble, France
q range0.074 – 3.129Sample 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:182 field values
Field pathRaw value
codeSASDFD3
statusPublished
type_of_curveMerged
angular_unit1/nm
project.titleCritical Structural Defects Explain Filamin A Mutations Causing Mitral Valve Dysplasia.
project.publication.titleCritical Structural Defects Explain Filamin A Mutations Causing Mitral Valve Dysplasia.
project.publication.author_listHaataja TJK, Capoulade R, Lecointe S, Hellman M, Merot J, Permi P, Pentikäinen U
project.publication.journalBiophys J
project.publication.doi10.1016/j.bpj.2019.08.032
project.publication.pmid31542223
project.publication.published_date2019 Oct 15
project.statusreleased
project.submitted_date2019-02-26
project.released_date2019-09-16
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDFD3.out
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pddf_plothttps://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDFD3_pofr_img.png
intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDFD3_guinier_img.png
sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDFD3.sascif
experiment.instrument.detector.typeDectris
experiment.instrument.detector.namePilatus 1M
experiment.instrument.detector.resolution172.0
experiment.instrument.nameESRF
experiment.instrument.cityGrenoble
experiment.instrument.countryFrance
experiment.instrument.beamline_nameBM29
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_nameFilamin A Ig-like domains 4-6
experiment.sample.molecule[0].short_nameFLNa4-6
experiment.sample.molecule[0].sequenceMSCGNQKVRAWGPGLEGGVVGKSADFVVEAIGDDVGTLGFSVEGPSQAKIECDDKGDGSCDVRYWPQEAGEYAVHVLCNSEDIRLSPFMADIRDAPQDFHPDRVKARGPGLEKTGVAVNKPAEFTVDAKHGGKAPLRVQVQDNEGCPVEALVKDNGNGTYSCSYVPRKPVKHTAMVSWGGVSIPNSPFRVNVGAGSHPNKVKVYGPGVAKTGLKAHEPTYFTVDCAEAGQGDVSIGIKCAPGVVGPAEADIDFDIIRNDNDTFTVKYTPRGAGSYTIMVLFADQATPTSPIRVKVEPS
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeP21333
experiment.sample.molecule[0].uniprot_range_first574
experiment.sample.molecule[0].uniprot_range_last869
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMSSSHSRAGQSAAGAAPGGGVDTRDAEMPATEKDLAEDAPWKKIQQNTFTRWCNEHLKCV SKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENVSVALEFLDRESIK LVSIDSKAIVDGNLKLILGLIWTLILHYSISMPMWDEEEDEEAKKQTPKQRLLGWIQNKL PQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQADDWLGIPQ VITPEEIVDPNVDEHSVMTYLSQFPKAKLKPGAPLRPKLNPKKARAYGPGIEPTGNMVKK RAEFTVETRSAGQGEVLVYVEDPAGHQEEAKVTANNDKNRTFSVWYVPEVTGTHKVTVLF AGQHIAKSPFEVYVDKSQGDASKVTAQGPGLEPSGNIANKTTYFEIFTAGAGTGEVEVVI QDPMGQKGTVEPQLEARGDSTYRCSYQPTMEGVHTVHVTFAGVPIPRSPYTVTVGQACNP SACRAVGRGLQPKGVRVKETADFKVYTKGAGSGELKVTVKGPKGEERVKQKDLGDGVYGF EYYPMVPGTYIVTITWGGQNIGRSPFEVKVGTECGNQKVRAWGPGLEGGVVGKSADFVVE AIGDDVGTLGFSVEGPSQAKIECDDKGDGSCDVRYWPQEAGEYAVHVLCNSEDIRLSPFM ADIRDAPQDFHPDRVKARGPGLEKTGVAVNKPAEFTVDAKHGGKAPLRVQVQDNEGCPVE ALVKDNGNGTYSCSYVPRKPVKHTAMVSWGGVSIPNSPFRVNVGAGSHPNKVKVYGPGVA KTGLKAHEPTYFTVDCAEAGQGDVSIGIKCAPGVVGPAEADIDFDIIRNDNDTFTVKYTP RGAGSYTIMVLFADQATPTSPIRVKVEPSHDASKVKAEGPGLSRTGVELGKPTHFTVNAK AAGKGKLDVQFSGLTKGDAVRDVDIIDHHDNTYTVKYTPVQQGPVGVNVTYGGDPIPKSP FSVAVSPSLDLSKIKVSGLGEKVDVGKDQEFTVKSKGAGGQGKVASKIVGPSGAAVPCKV EPGLGADNSVVRFLPREEGPYEVEVTYDGVPVPGSPFPLEAVAPTKPSKVKAFGPGLQGG SAGSPARFTIDTKGAGTGGLGLTVEGPCEAQLECLDNGDGTCSVSYVPTEPGDYNINILF ADTHIPGSPFKAHVVPCFDASKVKCSGPGLERATAGEVGQFQVDCSSAGSAELTIEICSE AGLPAEVYIQDHGDGTHTITYIPLCPGAYTVTIKYGGQPVPNFPSKLQVEPAVDTSGVQC YGPGIEGQGVFREATTEFSVDARALTQTGGPHVKARVANPSGNLTETYVQDRGDGMYKVE YTPYEEGLHSVDVTYDGSPVPSSPFQVPVTEGCDPSRVRVHGPGIQSGTTNKPNKFTVET RGAGTGGLGLAVEGPSEAKMSCMDNKDGSCSVEYIPYEAGTYSLNVTYGGHQVPGSPFKV PVHDVTDASKVKCSGPGLSPGMVRANLPQSFQVDTSKAGVAPLQVKVQGPKGLVEPVDVV DNADGTQTVNYVPSREGPYSISVLYGDEEVPRSPFKVKVLPTHDASKVKASGPGLNTTGV PASLPVEFTIDAKDAGEGLLAVQITDPEGKPKKTHIQDNHDGTYTVAYVPDVTGRYTILI KYGGDEIPFSPYRVRAVPTGDASKCTVTVSIGGHGLGAGIGPTIQIGEETVITVDTKAAG KGKVTCTVCTPDGSEVDVDVVENEDGTFDIFYTAPQPGKYVICVRFGGEHVPNSPFQVTA LAGDQPSVQPPLRSQQLAPQYTYAQGGQQTWAPERPLVGVNGLDVTSLRPFDLVIPFTIK KGEITGEVRMPSGKVAQPTITDNKDGTVTVRYAPSEAGLHEMDIRYDNMHIPGSPLQFYV DYVNCGHVTAYGPGLTHGVVNKPATFTVNTKDAGEGGLSLAIEGPSKAEISCTDNQDGTC SVSYLPVLPGDYSILVKYNEQHVPGSPFTARVTGDDSMRMSHLKVGSAADIPINISETDL SLLTATVVPPSGREEPCLLKRLRNGHVGISFVPKETGEHLVHVKKNGQHVASSPIPVVIS QSEIGDASRVRVSGQGLHEGHTFEPAEFIIDTRDAGYGGLSLSIEGPSKVDINTEDLEDG TCRVTYCPTEPGNYIINIKFADQHVPGSPFSVKVTGEGRVKESITRRRRAPSVANVGSHC DLSLKIPEISIQDMTAQVTSPSGKTHEAEIVEGENHTYCIRFVPAEMGTHTVSVKYKGQH VPGSPFQFTVGPLGEGGAHKVRAGGPGLERAEAGVPAEFSIWTREAGAGGLAIAVEGPSK AEISFEDRKDGSCGVAYVVQEPGDYEVSVKFNEEHIPDSPFVVPVASPSGDARRLTVSSL QESGLKVNQPASFAVSLNGAKGAIDAKVHSPSGALEECYVTEIDQDKYAVRFIPRENGVY LIDVKFNGTHIPGSPFKIRVGEPGHGGDPGLVSAYGAGLEGGVTGNPAEFVVNTSNAGAG ALSVTIDGPSKVKMDCQECPEGYRVTYTPMAPGSYLISIKYGGPYHIGGSPFKAKVTGPR LVSNHSLHETSSVFVDSLTKATCAPQHGAPGPGPADASKVVAKGLGLSKAYVGQKSSFTV DCSKAGNNMLLVGVHGPRTPCEEILVKHVGSRLYSVSYLLKDKGEYTLVVKWGDEHIPGS PYRVVVP
experiment.sample.molecule[0].mw31.52
experiment.sample.molecule[0].total_mw31.52
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.name20 mM Tris, 100 mM NaCl, 1 mM DTT
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph8.0
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameFilamin A Ig-like domains 4-6 (FLNa4-6)
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].addressJyväskylän, Finland
experiment.contributor[0].affiliation[0].full_nameUniversity of Jyväskylä
experiment.contributor[0].affiliation[0].webpagehttps://www.jyu.fi
experiment.contributor[0].contributor_nameTatu
experiment.contributor[0].contributor_surnameHaataja
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2017-02-10
experiment.storage_temperaturenull
experiment.cell_temperature20.0
experiment.exposure_timenull
experiment.number_of_framesnull
experiment.wavelength0.1
experiment.sample_detector_distance2.9
experiment.concentration_min2.0
experiment.concentration_max4.0
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.074
experiment.s_max3.129
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].models[0].pdb_link[]
fits[0].models[0].model_titlenull
fits[0].models[0].type_of_modeldummy
fits[0].models[0].software_versionDAMFILT 5
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fits[0].models[0].model_mw28.031
fits[0].models[0].bead_radius2.0
fits[0].models[0].lognull
fits[0].models[0].symmetryP1
fits[0].models[0].commentnull
fits[0].models[0].user251
fits[0].fit_unit1/A
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fits[0].softwareDAMMIF
fits[0].chi_square_value0.855
fits[0].p_value0.426529
fits[0].fit_residual_plot4-6_03p_1_fitresiduals_img.png
fits[0].fit_datahttps://www.sasbdb.org/media/fitting_files/SASDFD3_fit1.fir
fits[0].fit_lognull
fits[0].software_versionnull
fits[0].descriptionFit of one of the 20 DAMMIF-models created for FLNa4-6
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fits[1].models[0].softwareSASREF
fits[1].models[0].pdb_link[0].pdb_code4m9p
fits[1].models[0].pdb_link[0].ext_code4M9P
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fits[1].models[0].software_versionnull
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fits[1].models[0].model_mw31.28
fits[1].models[0].bead_radiusnull
fits[1].models[0].lognull
fits[1].models[0].symmetryP1
fits[1].models[0].commentRange 574-766 of 4m9p and homology model of FLNa6 used for generating the SASREF model
fits[1].models[0].user251
fits[1].fit_unit1/A
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fits[1].softwareSASREF
fits[1].chi_square_value0.92
fits[1].p_value9e-06
fits[1].fit_residual_plot2-4SAS5-1_fitresiduals_img.png
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fits[1].fit_lognull
fits[1].software_versionnull
fits[1].description
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version4.6
i0_calibration_standardnull
descriptionWild type three-domain fragment of human Filamin A Ig-like domains 4-6 (FLNa4-6). There are two extra amino acids, Met and Ser, in the very N-terminus of the polypeptide that have resulted from TEV-cleavage of the GST fusion tag during the protein purification.
experiment_descriptionSynchrotron SAXS data from solutions of Filamin A Ig-like domains 4-6 in 20 mM Tris, 100 mM NaCl, 1 mM DTT, pH 8 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.1 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 2 and 4 mg/ml were 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 low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.
tags[]
intensity_unitarbitrary
experimental_mw23.4
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw25.0
porod_mw_errornull
pddf_i023.91
pddf_i0_error0.03
guinier_i023.72
guinier_i0_error0.03
pddf_rg2.82
pddf_rg_error0.005
guinier_rg2.73
guinier_rg_error0.03
pddf_dmax9.5
pddf_dmax_errornull
porod_volume41.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first18
guinier_point_last80
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDFD3_datloglog_img.png
symmetrynull
last_modified2019-12-06T13:07:15.624532+01:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDFD3
statussuccess
started_at2026-08-11T13:57:53.584686+00:00
finished_at2026-08-11T13:58:02.052988+00:00
source_last_modified2019-12-06T13:07:15.624532+01:00
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View the complete summary.json source
{
  "code": "SASDFD3",
  "status": "Published",
  "type_of_curve": "Merged",
  "angular_unit": "1/nm",
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    "title": "Critical Structural Defects Explain Filamin A Mutations Causing Mitral Valve Dysplasia.",
    "publication": {
      "title": "Critical Structural Defects Explain Filamin A Mutations Causing Mitral Valve Dysplasia.",
      "author_list": "Haataja TJK, Capoulade R, Lecointe S, Hellman M, Merot J, Permi P, Pentikäinen U",
      "journal": "Biophys J",
      "doi": "10.1016/j.bpj.2019.08.032",
      "pmid": "31542223",
      "published_date": "2019 Oct 15"
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View the complete manifest.json source
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