SASDFG3

Filamin A Ig-like domains 4-6, H743P mutant (FLNa4-6 H743P) at 4 mg/ml

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

Three-domain fragment of human Filamin A Ig-like domains 4-6 with H743P mutation (FLNa4-6 H743P) . 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.

▼

1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Filamin A Ig-like domains 4-6, H743P mutant (FLNa4-6 H743P) at 4 mg/ml

Concentration	— – 4.0	Buffer / pH	20 mM Tris, 100 mM NaCl, 1 mM DTT / 8.0
Experimental temperature	20.0	Facility / beamline	ESRF / BM29
Wavelength	0.1 nm	Exposure	1.0 s × 10

Molecular Components

Component	Type / organism	UniProt and Construct	Oligomeric State	Molecular weight
Filamin A Ig-like domains 4-6, H743P mutation View sequence MSCGNQKVRAWGPGLEGGVVGKSADFVVEAIGDDVGTLGFSVEGPSQAKIECDDKGDGSCDVRYWPQEAGEYAVHVLCNSEDIRLSPFMADIRDAPQDFHPDRVKARGPGLEKTGVAVNKPAEFTVDAKHGGKAPLRVQVQDNEGCPVEALVKDNGNGTYSCSYVPRKPVKPTAMVSWGGVSIPNSPFRVNVGAGSHPNKVKVYGPGVAKTGLKAHEPTYFTVDCAEAGQGDVSIGIKCAPGVVGPAEADIDFDIIRNDNDTFTVKYTPRGAGSYTIMVLFADQATPTSPIRVKVEPS	proteinHomo sapiens	P21333574–869	monomerMolecule count 1	31.48 kDa

Experimental Curves

Curve	Points / columns	q range	Uncertainty quality	Negative-intensity points	Source file
1	1043[3]	0.03646643–4.941696 1/nm	Has uncertainty columnMissing 0	1	sasbdb/entries/g3/sasdfg3/source/SASDFG3.dat

▼

2. Measurements Reported by SASBDB Reported Results

Metric	Method	Value	Uncertainty	Unit
dmax	P(r)	16.0	—	nm
i0	Guinier	32.13	0.05	arbitrary
i0	P(r)	32.15	0.03	arbitrary
mw	Experimental	31.3	—	kDa
mw	Porod	44.0	—	kDa
porod_volume	Porod	70.0	—	nm³
rg	Guinier	4.29	0.1	nm
rg	P(r)	4.41	0.01	nm

These values are reported by SASBDB; SAXSdb did not recalculate them from the experimental curve.

▼

3. Source Fits and Models Source Fits & Models

This entry has no source fit record.

▶

4. Source File Index Source Files

Category	Path	Download status	Size
curve	sasbdb/entries/g3/sasdfg3/source/SASDFG3.dat	downloaded	57935
full_entry_zip	sasbdb/entries/g3/sasdfg3/source/SASDFG3.zip	downloaded	26025
pddf	sasbdb/entries/g3/sasdfg3/source/SASDFG3.out	downloaded	31308
sascif	sasbdb/entries/g3/sasdfg3/source/SASDFG3.sascif	downloaded	85591
summary	sasbdb/entries/g3/sasdfg3/source/summary.json	downloaded	9140

▶

5. Experiment Description and Publication Experiment & Publication

▼

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 name	20 mM Tris, 100 mM NaCl, 1 mM DTT	Buffer concentration	—
pH	8.0	Additives	—
Buffer description	—
Purity measurement method	—	Extinction coefficient	—
Absorbance	—	Scattering contrast	—
Specific volume / dry volume	— / —	Mixture / deuteration	— / —

Acquisition Conditions and Instrument

Measurement date	2017-02-10	Storage / measurement temperature	— / 20.0
Exposure time	1.0	Frames	10
Wavelength	0.1	Sample-to-detector distance	2.9
Source	X-ray synchrotron	Detector	Pilatus 1M
Facility / beamline	ESRF / BM29 · Grenoble, France
q range	0.036 – 4.942	Sample volume / flow rate	— / —

Original SASBDB Plots

Downloadable Files

Category	File	Status	Size	Checksum	Download and View
curve	sasbdb/entries/g3/sasdfg3/source/SASDFG3.dat	downloaded	57935	bc903c502259903e9dbe2415bd0bf803ec1b04406586a68201f2bb376ab59a4f	DownloadView source fileSource site
full_entry_zip	sasbdb/entries/g3/sasdfg3/source/SASDFG3.zip	downloaded	26025	54247576f2694cdeb527290b84f9ee02963a88d3e34c162d5e929e2fe232a7fe	DownloadView source fileSource site
pddf	sasbdb/entries/g3/sasdfg3/source/SASDFG3.out	downloaded	31308	079112c86eb0614d5b56aa4b18c5c085684c72a66bbb3bab46b88d6c9bde40d2	DownloadView source fileSource site
sascif	sasbdb/entries/g3/sasdfg3/source/SASDFG3.sascif	downloaded	85591	0d1645732edcd67bbba70647daacdfeda601c810fa7e3f708135b0374252da06	DownloadView source fileSource site
summary	sasbdb/entries/g3/sasdfg3/source/summary.json	downloaded	9140	c7155412fba9dbbdaf21f0316411d2597b91c06735e855f6d091f1a891a551dd	DownloadView source fileSource site

curve：source record

{
  "path": "/data/saxsdb/sasbdb/entries/g3/sasdfg3/source/SASDFG3.dat",
  "role": "curve",
  "sha256": "bc903c502259903e9dbe2415bd0bf803ec1b04406586a68201f2bb376ab59a4f",
  "size": 57935,
  "status": "downloaded",
  "url": "https://www.sasbdb.org/media/intensities_files/SASDFG3.dat"
}

full_entry_zip：source record and ZIP contents (2 items)

{
  "path": "/data/saxsdb/sasbdb/entries/g3/sasdfg3/source/SASDFG3.zip",
  "role": "full_entry_zip",
  "sha256": "54247576f2694cdeb527290b84f9ee02963a88d3e34c162d5e929e2fe232a7fe",
  "size": 26025,
  "status": "downloaded",
  "url": "https://www.sasbdb.org/media/zip_directories/SASDFG3.zip",
  "zip_member_count": 2,
  "zip_members": [
    {
      "crc32": "008e3851",
      "name": "SASDFG3/experimental_data/SASDFG3.dat",
      "size": 57935
    },
    {
      "crc32": "113bf8a7",
      "name": "SASDFG3/pddf/SASDFG3.out",
      "size": 31308
    }
  ],
  "zip_validation": "central_directory_readable"
}

pddf：source record

{
  "path": "/data/saxsdb/sasbdb/entries/g3/sasdfg3/source/SASDFG3.out",
  "role": "pddf",
  "sha256": "079112c86eb0614d5b56aa4b18c5c085684c72a66bbb3bab46b88d6c9bde40d2",
  "size": 31308,
  "status": "downloaded",
  "url": "https://www.sasbdb.org/media/p_of_R_files/SASDFG3.out"
}

sascif：source record

{
  "path": "/data/saxsdb/sasbdb/entries/g3/sasdfg3/source/SASDFG3.sascif",
  "role": "sascif",
  "sha256": "0d1645732edcd67bbba70647daacdfeda601c810fa7e3f708135b0374252da06",
  "size": 85591,
  "status": "downloaded",
  "url": "https://www.sasbdb.org/media/sascif/sascif_files/SASDFG3.sascif"
}

summary：source record

{
  "path": "/data/saxsdb/sasbdb/entries/g3/sasdfg3/source/summary.json",
  "sha256": "c7155412fba9dbbdaf21f0316411d2597b91c06735e855f6d091f1a891a551dd",
  "size": 9140,
  "status": "downloaded",
  "url": "https://www.sasbdb.org/rest-api/entry/summary/SASDFG3/"
}

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 path	Raw value
code	SASDFG3
status	Published
type_of_curve	Single concentration
angular_unit	1/nm
project.title	Critical Structural Defects Explain Filamin A Mutations Causing Mitral Valve Dysplasia.
project.publication.title	Critical Structural Defects Explain Filamin A Mutations Causing Mitral Valve Dysplasia.
project.publication.author_list	Haataja TJK, Capoulade R, Lecointe S, Hellman M, Merot J, Permi P, Pentikäinen U
project.publication.journal	Biophys J
project.publication.doi	10.1016/j.bpj.2019.08.032
project.publication.pmid	31542223
project.publication.published_date	2019 Oct 15
project.status	released
project.submitted_date	2019-02-26
project.released_date	2019-09-16
pddf_data	https://www.sasbdb.org/media/p_of_R_files/SASDFG3.out
intensities_data	https://www.sasbdb.org/media/intensities_files/SASDFG3.dat
intensities_log_plot	https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDFG3_dat_img.png
intensities_kratky_plot	https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDFG3_kratky_img.png
pddf_plot	https://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDFG3_pofr_img.png
intensities_guinier_plot	https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDFG3_guinier_img.png
sascif_data	https://www.sasbdb.org/media/sascif/sascif_files/SASDFG3.sascif
experiment.instrument.detector.type	Dectris
experiment.instrument.detector.name	Pilatus 1M
experiment.instrument.detector.resolution	172.0
experiment.instrument.name	ESRF
experiment.instrument.city	Grenoble
experiment.instrument.country	France
experiment.instrument.beamline_name	BM29
experiment.instrument.beam_geometry
experiment.instrument.type_of_source	X-ray synchrotron
experiment.instrument.point_source	null
experiment.instrument.line_collimation	null
experiment.instrument.sample_path_length	null
experiment.instrument.line_collimation_slitlength	null
experiment.instrument.line_collimation_integrationwidth	null
experiment.instrument.xray_energy	null
experiment.instrument.beam_profile_ah	null
experiment.instrument.beam_profile_al	null
experiment.sample.molecule[0].long_name	Filamin A Ig-like domains 4-6, H743P mutation
experiment.sample.molecule[0].short_name	FLNa4-6 H743P
experiment.sample.molecule[0].sequence	MSCGNQKVRAWGPGLEGGVVGKSADFVVEAIGDDVGTLGFSVEGPSQAKIECDDKGDGSCDVRYWPQEAGEYAVHVLCNSEDIRLSPFMADIRDAPQDFHPDRVKARGPGLEKTGVAVNKPAEFTVDAKHGGKAPLRVQVQDNEGCPVEALVKDNGNGTYSCSYVPRKPVKPTAMVSWGGVSIPNSPFRVNVGAGSHPNKVKVYGPGVAKTGLKAHEPTYFTVDCAEAGQGDVSIGIKCAPGVVGPAEADIDFDIIRNDNDTFTVKYTPRGAGSYTIMVLFADQATPTSPIRVKVEPS
experiment.sample.molecule[0].organism	Homo sapiens
experiment.sample.molecule[0].uniprot_code	P21333
experiment.sample.molecule[0].uniprot_range_first	574
experiment.sample.molecule[0].uniprot_range_last	869
experiment.sample.molecule[0].oligomerization	monomer
experiment.sample.molecule[0].molecular_type	protein
experiment.sample.molecule[0].uniprot_sequence	MSSSHSRAGQSAAGAAPGGGVDTRDAEMPATEKDLAEDAPWKKIQQNTFTRWCNEHLKCV 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].mw	31.48
experiment.sample.molecule[0].total_mw	31.48
experiment.sample.molecule[0].number_molecules	1
experiment.sample.molecule[0].complex_state	False
experiment.sample.molecule[0].deuteration	null
experiment.sample.molecule[0].molecule_source	biological
experiment.sample.molecule[0].molecule_description	null
experiment.sample.buffer.name	20 mM Tris, 100 mM NaCl, 1 mM DTT
experiment.sample.buffer.concentration_unit	null
experiment.sample.buffer.comment	null
experiment.sample.buffer.additive	null
experiment.sample.buffer.concentration	null
experiment.sample.buffer.pka	null
experiment.sample.buffer.ph	8.0
experiment.sample.buffer.deuteration	null
experiment.sample.purity_method	null
experiment.sample.name	Filamin A Ig-like domains 4-6, H743P mutant (FLNa4-6 H743P) at 4 mg/ml
experiment.sample.ext_coefficient	null
experiment.sample.contrast	null
experiment.sample.specific_vol	null
experiment.sample.dry_vol	null
experiment.sample.absorbption	null
experiment.sample.deuteration	null
experiment.sample.mixture	null
experiment.contributor[0].affiliation[0].short_name	null
experiment.contributor[0].affiliation[0].address	Jyväskylän, Finland
experiment.contributor[0].affiliation[0].full_name	University of Jyväskylä
experiment.contributor[0].affiliation[0].webpage	https://www.jyu.fi
experiment.contributor[0].contributor_name	Tatu
experiment.contributor[0].contributor_surname	Haataja
experiment.contributor[0].orcid	null
experiment.concentration_method	null
experiment.concentration_unit	null
experiment.date	2017-02-10
experiment.storage_temperature	null
experiment.cell_temperature	20.0
experiment.exposure_time	1.0
experiment.number_of_frames	10
experiment.wavelength	0.1
experiment.sample_detector_distance	2.9
experiment.concentration_min	null
experiment.concentration_max	4.0
experiment.sample_volume	null
experiment.flow_rate	null
experiment.s_min	0.036
experiment.s_max	4.942
experiment.total_exposure_time	null
experiment.seccolumn	null
fits	[]
estimated_volume_method	null
pddf_software	ATSAS GNOM
pddf_software_version	4.6
i0_calibration_standard	null
description	Three-domain fragment of human Filamin A Ig-like domains 4-6 with H743P mutation (FLNa4-6 H743P) . 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_description	Synchrotron SAXS data from solutions of Filamin A Ig-like domains 4-6 (H743P mutant) 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). One solute concentration of 4.00 mg/ml was measured at 20°C. 10 successive 1 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_unit	arbitrary
experimental_mw	31.3
experimental_mw_error	null
guinier_i0_mw	null
guinier_i0_mw_error	null
porod_mw	44.0
porod_mw_error	null
pddf_i0	32.15
pddf_i0_error	0.03
guinier_i0	32.13
guinier_i0_error	0.05
pddf_rg	4.41
pddf_rg_error	0.01
guinier_rg	4.29
guinier_rg_error	0.1
pddf_dmax	16.0
pddf_dmax_error	null
porod_volume	70.0
porod_volume_error	null
estimated_volume	null
estimated_volume_error	null
guinier_point_first	11
guinier_point_last	44
pddf_point_first	null
pddf_point_last	null
i0_calibration_standard_data	null
intensities_log_log_plot	SASDFG3_datloglog_img.png
symmetry	null
last_modified	2019-12-06T13:07:15.624532+01:00
bragg_peak	[]

manifest.json：36 field values

Field path	Raw value
code	SASDFG3
status	success
started_at	2026-08-11T13:59:47.070614+00:00
finished_at	2026-08-11T13:59:54.902556+00:00
source_last_modified	2019-12-06T13:07:15.624532+01:00
files[0].status	downloaded
files[0].url	https://www.sasbdb.org/rest-api/entry/summary/SASDFG3/
files[0].path	/data/saxsdb/sasbdb/entries/g3/sasdfg3/source/summary.json
files[0].size	9140
files[0].sha256	c7155412fba9dbbdaf21f0316411d2597b91c06735e855f6d091f1a891a551dd
files[1].status	downloaded
files[1].url	https://www.sasbdb.org/media/intensities_files/SASDFG3.dat
files[1].path	/data/saxsdb/sasbdb/entries/g3/sasdfg3/source/SASDFG3.dat
files[1].size	57935
files[1].sha256	bc903c502259903e9dbe2415bd0bf803ec1b04406586a68201f2bb376ab59a4f
files[1].role	curve
files[2].status	downloaded
files[2].url	https://www.sasbdb.org/media/p_of_R_files/SASDFG3.out
files[2].path	/data/saxsdb/sasbdb/entries/g3/sasdfg3/source/SASDFG3.out
files[2].size	31308
files[2].sha256	079112c86eb0614d5b56aa4b18c5c085684c72a66bbb3bab46b88d6c9bde40d2
files[2].role	pddf
files[3].status	downloaded
files[3].url	https://www.sasbdb.org/media/sascif/sascif_files/SASDFG3.sascif
files[3].path	/data/saxsdb/sasbdb/entries/g3/sasdfg3/source/SASDFG3.sascif
files[3].size	85591
files[3].sha256	0d1645732edcd67bbba70647daacdfeda601c810fa7e3f708135b0374252da06
files[3].role	sascif
files[4].status	downloaded
files[4].url	https://www.sasbdb.org/media/zip_directories/SASDFG3.zip
files[4].path	/data/saxsdb/sasbdb/entries/g3/sasdfg3/source/SASDFG3.zip
files[4].size	26025
files[4].sha256	54247576f2694cdeb527290b84f9ee02963a88d3e34c162d5e929e2fe232a7fe
files[4].role	full_entry_zip
files[4].zip_member_count	2
files[4].zip_validation	central_directory_readable

View the complete summary.json source

{
  "code": "SASDFG3",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/nm",
  "project": {
    "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"
    },
    "status": "released",
    "submitted_date": "2019-02-26",
    "released_date": "2019-09-16"
  },
  "pddf_data": "https://www.sasbdb.org/media/p_of_R_files/SASDFG3.out",
  "intensities_data": "https://www.sasbdb.org/media/intensities_files/SASDFG3.dat",
  "intensities_log_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDFG3_dat_img.png",
  "intensities_kratky_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDFG3_kratky_img.png",
  "pddf_plot": "https://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDFG3_pofr_img.png",
  "intensities_guinier_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDFG3_guinier_img.png",
  "sascif_data": "https://www.sasbdb.org/media/sascif/sascif_files/SASDFG3.sascif",
  "experiment": {
    "instrument": {
      "detector": {
        "type": "Dectris",
        "name": "Pilatus 1M",
        "resolution": 172.0
      },
      "name": "ESRF",
      "city": "Grenoble",
      "country": "France",
      "beamline_name": "BM29",
      "beam_geometry": "",
      "type_of_source": "X-ray synchrotron",
      "point_source": null,
      "line_collimation": null,
      "sample_path_length": null,
      "line_collimation_slitlength": null,
      "line_collimation_integrationwidth": null,
      "xray_energy": null,
      "beam_profile_ah": null,
      "beam_profile_al": null
    },
    "sample": {
      "molecule": [
        {
          "long_name": "Filamin A Ig-like domains 4-6, H743P mutation",
          "short_name": "FLNa4-6 H743P",
          "sequence": "MSCGNQKVRAWGPGLEGGVVGKSADFVVEAIGDDVGTLGFSVEGPSQAKIECDDKGDGSCDVRYWPQEAGEYAVHVLCNSEDIRLSPFMADIRDAPQDFHPDRVKARGPGLEKTGVAVNKPAEFTVDAKHGGKAPLRVQVQDNEGCPVEALVKDNGNGTYSCSYVPRKPVKPTAMVSWGGVSIPNSPFRVNVGAGSHPNKVKVYGPGVAKTGLKAHEPTYFTVDCAEAGQGDVSIGIKCAPGVVGPAEADIDFDIIRNDNDTFTVKYTPRGAGSYTIMVLFADQATPTSPIRVKVEPS",
          "organism": "Homo sapiens",
          "uniprot_code": "P21333",
          "uniprot_range_first": 574,
          "uniprot_range_last": 869,
          "oligomerization": "monomer",
          "molecular_type": "protein",
          "uniprot_sequence": "MSSSHSRAGQSAAGAAPGGGVDTRDAEMPATEKDLAEDAPWKKIQQNTFTRWCNEHLKCV\nSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENVSVALEFLDRESIK\nLVSIDSKAIVDGNLKLILGLIWTLILHYSISMPMWDEEEDEEAKKQTPKQRLLGWIQNKL\nPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQADDWLGIPQ\nVITPEEIVDPNVDEHSVMTYLSQFPKAKLKPGAPLRPKLNPKKARAYGPGIEPTGNMVKK\nRAEFTVETRSAGQGEVLVYVEDPAGHQEEAKVTANNDKNRTFSVWYVPEVTGTHKVTVLF\nAGQHIAKSPFEVYVDKSQGDASKVTAQGPGLEPSGNIANKTTYFEIFTAGAGTGEVEVVI\nQDPMGQKGTVEPQLEARGDSTYRCSYQPTMEGVHTVHVTFAGVPIPRSPYTVTVGQACNP\nSACRAVGRGLQPKGVRVKETADFKVYTKGAGSGELKVTVKGPKGEERVKQKDLGDGVYGF\nEYYPMVPGTYIVTITWGGQNIGRSPFEVKVGTECGNQKVRAWGPGLEGGVVGKSADFVVE\nAIGDDVGTLGFSVEGPSQAKIECDDKGDGSCDVRYWPQEAGEYAVHVLCNSEDIRLSPFM\nADIRDAPQDFHPDRVKARGPGLEKTGVAVNKPAEFTVDAKHGGKAPLRVQVQDNEGCPVE\nALVKDNGNGTYSCSYVPRKPVKHTAMVSWGGVSIPNSPFRVNVGAGSHPNKVKVYGPGVA\nKTGLKAHEPTYFTVDCAEAGQGDVSIGIKCAPGVVGPAEADIDFDIIRNDNDTFTVKYTP\nRGAGSYTIMVLFADQATPTSPIRVKVEPSHDASKVKAEGPGLSRTGVELGKPTHFTVNAK\nAAGKGKLDVQFSGLTKGDAVRDVDIIDHHDNTYTVKYTPVQQGPVGVNVTYGGDPIPKSP\nFSVAVSPSLDLSKIKVSGLGEKVDVGKDQEFTVKSKGAGGQGKVASKIVGPSGAAVPCKV\nEPGLGADNSVVRFLPREEGPYEVEVTYDGVPVPGSPFPLEAVAPTKPSKVKAFGPGLQGG\nSAGSPARFTIDTKGAGTGGLGLTVEGPCEAQLECLDNGDGTCSVSYVPTEPGDYNINILF\nADTHIPGSPFKAHVVPCFDASKVKCSGPGLERATAGEVGQFQVDCSSAGSAELTIEICSE\nAGLPAEVYIQDHGDGTHTITYIPLCPGAYTVTIKYGGQPVPNFPSKLQVEPAVDTSGVQC\nYGPGIEGQGVFREATTEFSVDARALTQTGGPHVKARVANPSGNLTETYVQDRGDGMYKVE\nYTPYEEGLHSVDVTYDGSPVPSSPFQVPVTEGCDPSRVRVHGPGIQSGTTNKPNKFTVET\nRGAGTGGLGLAVEGPSEAKMSCMDNKDGSCSVEYIPYEAGTYSLNVTYGGHQVPGSPFKV\nPVHDVTDASKVKCSGPGLSPGMVRANLPQSFQVDTSKAGVAPLQVKVQGPKGLVEPVDVV\nDNADGTQTVNYVPSREGPYSISVLYGDEEVPRSPFKVKVLPTHDASKVKASGPGLNTTGV\nPASLPVEFTIDAKDAGEGLLAVQITDPEGKPKKTHIQDNHDGTYTVAYVPDVTGRYTILI\nKYGGDEIPFSPYRVRAVPTGDASKCTVTVSIGGHGLGAGIGPTIQIGEETVITVDTKAAG\nKGKVTCTVCTPDGSEVDVDVVENEDGTFDIFYTAPQPGKYVICVRFGGEHVPNSPFQVTA\nLAGDQPSVQPPLRSQQLAPQYTYAQGGQQTWAPERPLVGVNGLDVTSLRPFDLVIPFTIK\nKGEITGEVRMPSGKVAQPTITDNKDGTVTVRYAPSEAGLHEMDIRYDNMHIPGSPLQFYV\nDYVNCGHVTAYGPGLTHGVVNKPATFTVNTKDAGEGGLSLAIEGPSKAEISCTDNQDGTC\nSVSYLPVLPGDYSILVKYNEQHVPGSPFTARVTGDDSMRMSHLKVGSAADIPINISETDL\nSLLTATVVPPSGREEPCLLKRLRNGHVGISFVPKETGEHLVHVKKNGQHVASSPIPVVIS\nQSEIGDASRVRVSGQGLHEGHTFEPAEFIIDTRDAGYGGLSLSIEGPSKVDINTEDLEDG\nTCRVTYCPTEPGNYIINIKFADQHVPGSPFSVKVTGEGRVKESITRRRRAPSVANVGSHC\nDLSLKIPEISIQDMTAQVTSPSGKTHEAEIVEGENHTYCIRFVPAEMGTHTVSVKYKGQH\nVPGSPFQFTVGPLGEGGAHKVRAGGPGLERAEAGVPAEFSIWTREAGAGGLAIAVEGPSK\nAEISFEDRKDGSCGVAYVVQEPGDYEVSVKFNEEHIPDSPFVVPVASPSGDARRLTVSSL\nQESGLKVNQPASFAVSLNGAKGAIDAKVHSPSGALEECYVTEIDQDKYAVRFIPRENGVY\nLIDVKFNGTHIPGSPFKIRVGEPGHGGDPGLVSAYGAGLEGGVTGNPAEFVVNTSNAGAG\nALSVTIDGPSKVKMDCQECPEGYRVTYTPMAPGSYLISIKYGGPYHIGGSPFKAKVTGPR\nLVSNHSLHETSSVFVDSLTKATCAPQHGAPGPGPADASKVVAKGLGLSKAYVGQKSSFTV\nDCSKAGNNMLLVGVHGPRTPCEEILVKHVGSRLYSVSYLLKDKGEYTLVVKWGDEHIPGS\nPYRVVVP",
          "mw": 31.48,
          "total_mw": 31.48,
          "number_molecules": 1,
          "complex_state": false,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": null
        }
      ],
      "buffer": {
        "name": "20 mM Tris, 100 mM NaCl, 1 mM DTT",
        "concentration_unit": null,
        "comment": null,
        "additive": null,
        "concentration": null,
        "pka": null,
        "ph": 8.0,
        "deuteration": null
      },
      "purity_method": null,
      "name": "Filamin A Ig-like domains 4-6, H743P mutant (FLNa4-6 H743P) at 4 mg/ml",
      "ext_coefficient": null,
      "contrast": null,
      "specific_vol": null,
      "dry_vol": null,
      "absorbption": null,
      "deuteration": null,
      "mixture": null
    },
    "contributor": [
      {
        "affiliation": [
          {
            "short_name": null,
            "address": "Jyväskylän, Finland",
            "full_name": "University of Jyväskylä",
            "webpage": "https://www.jyu.fi"
          }
        ],
        "contributor_name": "Tatu",
        "contributor_surname": "Haataja",
        "orcid": null
      }
    ],
    "concentration_method": null,
    "concentration_unit": null,
    "date": "2017-02-10",
    "storage_temperature": null,
    "cell_temperature": 20.0,
    "exposure_time": 1.0,
    "number_of_frames": 10,
    "wavelength": 0.1,
    "sample_detector_distance": 2.9,
    "concentration_min": null,
    "concentration_max": 4.0,
    "sample_volume": null,
    "flow_rate": null,
    "s_min": 0.036,
    "s_max": 4.942,
    "total_exposure_time": null,
    "seccolumn": null
  },
  "fits": [],
  "estimated_volume_method": null,
  "pddf_software": "ATSAS GNOM",
  "pddf_software_version": "4.6",
  "i0_calibration_standard": null,
  "description": "Three-domain fragment of human Filamin A Ig-like domains 4-6 with H743P mutation (FLNa4-6 H743P) . 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_description": "Synchrotron SAXS data from solutions of Filamin A Ig-like domains 4-6 (H743P mutant) 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). One solute concentration of 4.00 mg/ml was measured at 20°C. 10 successive 1 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_unit": "arbitrary",
  "experimental_mw": 31.3,
  "experimental_mw_error": null,
  "guinier_i0_mw": null,
  "guinier_i0_mw_error": null,
  "porod_mw": 44.0,
  "porod_mw_error": null,
  "pddf_i0": 32.15,
  "pddf_i0_error": 0.03,
  "guinier_i0": 32.13,
  "guinier_i0_error": 0.05,
  "pddf_rg": 4.41,
  "pddf_rg_error": 0.01,
  "guinier_rg": 4.29,
  "guinier_rg_error": 0.1,
  "pddf_dmax": 16.0,
  "pddf_dmax_error": null,
  "porod_volume": 70.0,
  "porod_volume_error": null,
  "estimated_volume": null,
  "estimated_volume_error": null,
  "guinier_point_first": 11,
  "guinier_point_last": 44,
  "pddf_point_first": null,
  "pddf_point_last": null,
  "i0_calibration_standard_data": null,
  "intensities_log_log_plot": "SASDFG3_datloglog_img.png",
  "symmetry": null,
  "last_modified": "2019-12-06T13:07:15.624532+01:00",
  "bragg_peak": []
}

View the complete manifest.json source

{
  "code": "SASDFG3",
  "status": "success",
  "started_at": "2026-08-11T13:59:47.070614+00:00",
  "finished_at": "2026-08-11T13:59:54.902556+00:00",
  "source_last_modified": "2019-12-06T13:07:15.624532+01:00",
  "files": [
    {
      "status": "downloaded",
      "url": "https://www.sasbdb.org/rest-api/entry/summary/SASDFG3/",
      "path": "/data/saxsdb/sasbdb/entries/g3/sasdfg3/source/summary.json",
      "size": 9140,
      "sha256": "c7155412fba9dbbdaf21f0316411d2597b91c06735e855f6d091f1a891a551dd"
    },
    {
      "status": "downloaded",
      "url": "https://www.sasbdb.org/media/intensities_files/SASDFG3.dat",
      "path": "/data/saxsdb/sasbdb/entries/g3/sasdfg3/source/SASDFG3.dat",
      "size": 57935,
      "sha256": "bc903c502259903e9dbe2415bd0bf803ec1b04406586a68201f2bb376ab59a4f",
      "role": "curve"
    },
    {
      "status": "downloaded",
      "url": "https://www.sasbdb.org/media/p_of_R_files/SASDFG3.out",
      "path": "/data/saxsdb/sasbdb/entries/g3/sasdfg3/source/SASDFG3.out",
      "size": 31308,
      "sha256": "079112c86eb0614d5b56aa4b18c5c085684c72a66bbb3bab46b88d6c9bde40d2",
      "role": "pddf"
    },
    {
      "status": "downloaded",
      "url": "https://www.sasbdb.org/media/sascif/sascif_files/SASDFG3.sascif",
      "path": "/data/saxsdb/sasbdb/entries/g3/sasdfg3/source/SASDFG3.sascif",
      "size": 85591,
      "sha256": "0d1645732edcd67bbba70647daacdfeda601c810fa7e3f708135b0374252da06",
      "role": "sascif"
    },
    {
      "status": "downloaded",
      "url": "https://www.sasbdb.org/media/zip_directories/SASDFG3.zip",
      "path": "/data/saxsdb/sasbdb/entries/g3/sasdfg3/source/SASDFG3.zip",
      "size": 26025,
      "sha256": "54247576f2694cdeb527290b84f9ee02963a88d3e34c162d5e929e2fe232a7fe",
      "role": "full_entry_zip",
      "zip_member_count": 2,
      "zip_validation": "central_directory_readable"
    }
  ]
}

Title	Critical Structural Defects Explain Filamin A Mutations Causing Mitral Valve Dysplasia.
Authors	Haataja TJK, Capoulade R, Lecointe S, Hellman M, Merot J, Permi P, Pentikäinen U
DOI / PMID	10.1016/j.bpj.2019.08.032 / 31542223