SASDFV4

Conformation of R11-15 human dystrophin fragment in interaction with anionic phospholipid bicelles (SANS)

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2022-08-15T14:51:04.900446+02:00

Data were collected at two sample detector positions: 1) 1.4 m for 5 min using a neutron wavelength of 0.6 nm and; 2) 8 m for 20 min using a neutron wavelength of 0.6 nm. Both datasets were recorded on the same sample at 5.6 mg/mL, measured at 22 °C.

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Conformation of R11-15 human dystrophin fragment in interaction with anionic phospholipid bicelles (SANS)

Concentration— – 5.6 Buffer / pH20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% v/v D2O / 7.1
Experimental temperature22.0 Facility / beamlineInstitut Laue-Langevin (ILL) / D22
Wavelength0.6 nmExposure1200.0 s × —

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Dystrophin (R11-15 human dystrophin fragment)
View sequence
GSFQKPANFEQRLQESKMILDEVKMHLPALETKSVEQEVVQSQLNHCVNLYKSLSEVKSEVEMVIKTGRQIVQKKQTENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMNVLTEWLAATDMELTKRSAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSITEVGEALKTVLGKKETLVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHMETFDQNVDHITKWIIQADTLLDESEKKKPQQKEDVLKRLKAELNDIRPKVDSTRDQAANLMANHGDHCRKLVEPQISELNHRFAAISHRIKTGKASIPLKELEQFNSDIQKLLEPLEAEIQQGVNLKEEDFNKDMNEDNEGTVKELLQRGDNLQQRITDERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPRDERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVEPTQIQLSKRWREIESKFAQFRRLNFAQ
proteinHomo sapiensP115321461–1973monomerMolecule count 160.065 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1181[3]0.006499–0.6143 1/AHas uncertainty columnMissing 029sasbdb/entries/v4/sasdfv4/source/SASDFV4.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)29.6—Å
i0Guinier0.2750.011/cm
i0P(r)0.2601—1/cm
mwExperimental53.0—kDa
porod_volumePorod231.0—ų
rgGuinier8.10.3Å
rgP(r)7.7—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

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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-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% v/v D2OBuffer concentration—
pH7.1Additives—
Buffer descriptionpD 7.5 (pH 7.1)
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2016-11-01Storage / measurement temperature— / 22.0
Exposure time1200.0Frames—
Wavelength0.6Sample-to-detector distance8.0
Sourceneutron sourceDetectorReuter-Stokes 3He
Facility / beamlineInstitut Laue-Langevin (ILL) / D22 · Grenoble, France
q range0.065 – 6.143Sample 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 (4 items)
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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:156 field values
Field pathRaw value
codeSASDFV4
statusPublished
type_of_curveSingle concentration
angular_unit1/A
project.titleHow the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids.
project.publication.titleHow the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids.
project.publication.author_listMias-Lucquin D, Dos Santos Morais R, Chéron A, Lagarrigue M, Winder SJ, Chenuel T, Pérez J, Appavou MS, Martel A, Alviset G, Le Rumeur E, Combet S, Hubert JF, Delalande O
project.publication.journalJ Struct Biol
project.publication.doi10.1016/j.jsb.2019.107411
project.publication.pmid31689503
project.publication.published_date2019 Nov 2
project.statusreleased
project.submitted_date2019-03-30
project.released_date2019-11-14
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDFV4.out
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDFV4.dat
intensities_log_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDFV4_dat_img.png
intensities_kratky_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDFV4_kratky_img.png
pddf_plothttps://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDFV4_pofr_img.png
intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDFV4_guinier_img.png
sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDFV4.sascif
experiment.instrument.detector.type128 linear sensitive multidetector
experiment.instrument.detector.nameReuter-Stokes 3He
experiment.instrument.detector.resolution0.8
experiment.instrument.nameInstitut Laue-Langevin (ILL)
experiment.instrument.cityGrenoble
experiment.instrument.countryFrance
experiment.instrument.beamline_nameD22
experiment.instrument.beam_geometrynull
experiment.instrument.type_of_sourceneutron source
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_nameDystrophin (R11-15 human dystrophin fragment)
experiment.sample.molecule[0].short_nameDystrophin 1461-1973
experiment.sample.molecule[0].sequenceGSFQKPANFEQRLQESKMILDEVKMHLPALETKSVEQEVVQSQLNHCVNLYKSLSEVKSEVEMVIKTGRQIVQKKQTENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMNVLTEWLAATDMELTKRSAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSITEVGEALKTVLGKKETLVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHMETFDQNVDHITKWIIQADTLLDESEKKKPQQKEDVLKRLKAELNDIRPKVDSTRDQAANLMANHGDHCRKLVEPQISELNHRFAAISHRIKTGKASIPLKELEQFNSDIQKLLEPLEAEIQQGVNLKEEDFNKDMNEDNEGTVKELLQRGDNLQQRITDERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPRDERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVEPTQIQLSKRWREIESKFAQFRRLNFAQ
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeP11532
experiment.sample.molecule[0].uniprot_range_first1461
experiment.sample.molecule[0].uniprot_range_last1973
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMLWWEEVEDCYEREDVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQ KLPKEKGSTRVHALNNVNKALRVLQNNNVDLVNIGSTDIVDGNHKLTLGLIWNIILHWQV KNVMKNIMAGLQQTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDL FDWNSVVCQQSATQRLEHAFNIARYQLGIEKLLDPEDVDTTYPDKKSILMYITSLFQVLP QQVSIEAIQEVEMLPRPPKVTKEEHFQLHHQMHYSQQITVSLAQGYERTSSPKPRFKSYA YTQAAYVTTSDPTRSPFPSQHLEAPEDKSFGSSLMESEVNLDRYQTALEEVLSWLLSAED TLQAQGEISNDVEVVKDQFHTHEGYMMDLTAHQGRVGNILQLGSKLIGTGKLSEDEETEV QEQMNLLNSRWECLRVASMEKQSNLHRVLMDLQNQKLKELNDWLTKTEERTRKMEEEPLG PDLEDLKRQVQQHKVLQEDLEQEQVRVNSLTHMVVVVDESSGDHATAALEEQLKVLGDRW ANICRWTEDRWVLLQDILLKWQRLTEEQCLFSAWLSEKEDAVNKIHTTGFKDQNEMLSSL QKLAVLKADLEKKKQSMGKLYSLKQDLLSTLKNKSVTQKTEAWLDNFARCWDNLVQKLEK STAQISQAVTTTQPSLTQTTVMETVTTVTTREQILVKHAQEELPPPPPQKKRQITVDSEI RKRLDVDITELHSWITRSEAVLQSPEFAIFRKEGNFSDLKEKVNAIEREKAEKFRKLQDA SRSAQALVEQMVNEGVNADSIKQASEQLNSRWIEFCQLLSERLNWLEYQNNIIAFYNQLQ QLEQMTTTAENWLKIQPTTPSEPTAIKSQLKICKDEVNRLSDLQPQIERLKIQSIALKEK GQGPMFLDADFVAFTNHFKQVFSDVQAREKELQTIFDTLPPMRYQETMSAIRTWVQQSET KLSIPQLSVTDYEIMEQRLGELQALQSSLQEQQSGLYYLSTTVKEMSKKAPSEISRKYQS EFEEIEGRWKKLSSQLVEHCQKLEEQMNKLRKIQNHIQTLKKWMAEVDVFLKEEWPALGD SEILKKQLKQCRLLVSDIQTIQPSLNSVNEGGQKIKNEAEPEFASRLETELKELNTQWDH MCQQVYARKEALKGGLEKTVSLQKDLSEMHEWMTQAEEEYLERDFEYKTPDELQKAVEEM KRAKEEAQQKEAKVKLLTESVNSVIAQAPPVAQEALKKELETLTTNYQWLCTRLNGKCKT LEEVWACWHELLSYLEKANKWLNEVEFKLKTTENIPGGAEEISEVLDSLENLMRHSEDNP NQIRILAQTLTDGGVMDELINEELETFNSRWRELHEEAVRRQKLLEQSIQSAQETEKSLH LIQESLTFIDKQLAAYIADKVDAAQMPQEAQKIQSDLTSHEISLEEMKKHNQGKEAAQRV LSQIDVAQKKLQDVSMKFRLFQKPANFEQRLQESKMILDEVKMHLPALETKSVEQEVVQS QLNHCVNLYKSLSEVKSEVEMVIKTGRQIVQKKQTENPKELDERVTALKLHYNELGAKVT ERKQQLEKCLKLSRKMRKEMNVLTEWLAATDMELTKRSAVEGMPSNLDSEVAWGKATQKE IEKQKVHLKSITEVGEALKTVLGKKETLVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKH METFDQNVDHITKWIIQADTLLDESEKKKPQQKEDVLKRLKAELNDIRPKVDSTRDQAAN LMANRGDHCRKLVEPQISELNHRFAAISHRIKTGKASIPLKELEQFNSDIQKLLEPLEAE IQQGVNLKEEDFNKDMNEDNEGTVKELLQRGDNLQQRITDERKREEIKIKQQLLQTKHNA LKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPRDERKIKEIDRELQ KKKEELNAVRRQAEGLSEDGAAMAVEPTQIQLSKRWREIESKFAQFRRLNFAQIHTVREE TMMVMTEDMPLEISYVPSTYLTEITHVSQALLEVEQLLNAPDLCAKDFEDLFKQEESLKN IKDSLQQSSGRIDIIHSKKTAALQSATPVERVKLQEALSQLDFQWEKVNKMYKDRQGRFD RSVEKWRRFHYDIKIFNQWLTEAEQFLRKTQIPENWEHAKYKWYLKELQDGIGQRQTVVR TLNATGEEIIQQSSKTDASILQEKLGSLNLRWQEVCKQLSDRKKRLEEQKNILSEFQRDL NEFVLWLEEADNIASIPLEPGKEQQLKEKLEQVKLLVEELPLRQGILKQLNETGGPVLVS APISPEEQDKLENKLKQTNLQWIKVSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHL LLWLSPIRNQLEIYNQPNQEGPFDVKETEIAVQAKQPDVEEILSKGQHLYKEKPATQPVK RKLEDLSSEWKAVNRLLQELRAKQPDLAPGLTTIGASPTQTVTLVTQPVVTKETAISKLE MPSSLMLEVPALADFNRAWTELTDWLSLLDQVIKSQRVMVGDLEDINEMIIKQKATMQDL EQRRPQLEELITAAQNLKNKTSNQEARTIITDRIERIQNQWDEVQEHLQNRRQQLNEMLK DSTQWLEAKEEAEQVLGQARAKLESWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVA NDLALKLLRDYSADDTRKVHMITENINASWRSIHKRVSEREAALEETHRLLQQFPLDLEK FLAWLTEAETTANVLQDATRKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQ KILRSLEGSDDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHLSLQELLVW LQLKDDELSRQAPIGGDFPAVQKQNDVHRAFKRELKTKEPVIMSTLETVRIFLTEQPLEG LEKLYQEPRELPPEERAQNVTRLLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLQELQ EATDELDLKLRQAEVIKGSWQPVGDLLIDSLQDHLEKVKALRGEIAPLKENVSHVNDLAR QLTTLGIQLSPYNLSTLEDLNTRWKLLQVAVEDRVRQLHEAHRDFGPASQHFLSTSVQGP WERAISPNKVPYYINHETQTTCWDHPKMTELYQSLADLNNVRFSAYRTAMKLRRLQKALC LDLLSLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLN WLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHD SIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDWMRLEPQSMVWLPVLHR VAAAETAKHQAKCNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVEYC TPTTSGEDVRDFAKVLKNKFRTKRYFAKHPRMGYLPVQTVLEGDNMETPVTLINFWPVDS APASSPQLSHDDTHSRIEHYASRLAEMENSNGSYLNDSISPNESIDDEHLLIQHYCQSLN QDSPLSQPRSPAQILISLESEERGELERILADLEEENRNLQAEYDRLKQQHEHKGLSPLP SPPEMMPTSPQSPRDAELIAEAKLLRQHKGRLEARMQILEDHNKQLESQLHRLRQLLEQP QAEAKVNGTTVSSPSTSLQRSDSSQPMLLRVVGSQTSDSMGEEDLLSPPQDTSTGLEEVM EQLNNSFPSSRGRNTPGKPMREDTM
experiment.sample.molecule[0].mw60.065
experiment.sample.molecule[0].total_mw60.065
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-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% v/v D2O
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentpD 7.5 (pH 7.1)
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph7.1
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameConformation of R11-15 human dystrophin fragment in interaction with anionic phospholipid bicelles (SANS)
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].addressFrance
experiment.contributor[0].affiliation[0].full_nameUniversity of Lorraine
experiment.contributor[0].affiliation[0].webpagehttp://welcome.univ-lorraine.fr/
experiment.contributor[0].contributor_nameRaphael
experiment.contributor[0].contributor_surnameDos Santos Morais
experiment.contributor[0].orcid
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2016-11-01
experiment.storage_temperaturenull
experiment.cell_temperature22.0
experiment.exposure_time1200.0
experiment.number_of_framesnull
experiment.wavelength0.6
experiment.sample_detector_distance8.0
experiment.concentration_minnull
experiment.concentration_max5.6
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.065
experiment.s_max6.143
experiment.total_exposure_timenull
experiment.seccolumnnull
fits[0].models[0].model_plothttps://www.sasbdb.org/media/pdb_file/images/SASDFV4_fit1_model1_img.png
fits[0].models[0].softwareDAMMIF
fits[0].models[0].pdb_link[]
fits[0].models[0].model_titlenull
fits[0].models[0].type_of_modeldummy
fits[0].models[0].software_versionnull
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fits[0].models[0].model_mw50.0
fits[0].models[0].bead_radius2.1
fits[0].models[0].lognull
fits[0].models[0].symmetrynull
fits[0].models[0].commentnull
fits[0].models[0].user427
fits[0].fit_unit1/A
fits[0].fit_plothttps://www.sasbdb.org/media/fitting_files/scattering_plots/R11-15-3_2_fixed_fit_img.png
fits[0].softwareDAMMIF
fits[0].chi_square_value0.676
fits[0].p_value0.362668
fits[0].fit_residual_plotR11-15-3_2_fitresiduals_img.png
fits[0].fit_datahttps://www.sasbdb.org/media/fitting_files/SASDFV4_fit1.fir
fits[0].fit_lognull
fits[0].software_versionnull
fits[0].description
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version4.6
i0_calibration_standardnull
descriptionData were collected at two sample detector positions: 1) 1.4 m for 5 min using a neutron wavelength of 0.6 nm and; 2) 8 m for 20 min using a neutron wavelength of 0.6 nm. Both datasets were recorded on the same sample at 5.6 mg/mL, measured at 22 °C.
experiment_descriptionSANS data from solutions of the R11-15 human dystrophin fragment with anionic phospholipid bicelles in 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% v/v D2O, pH 7.1 were collected on the D22 beam line at the ILL (Grenoble, France) using a 3He multidetector 128 linear sensitive Reuter-Stokes detector at a wavelength of λ = 0.6 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 5.60 mg/ml was measured at 22°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
tags[0]sans
intensity_unit1/cm
experimental_mw53.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mwnull
porod_mw_errornull
pddf_i00.2601
pddf_i0_errornull
guinier_i00.275
guinier_i0_error0.01
pddf_rg7.7
pddf_rg_errornull
guinier_rg8.1
guinier_rg_error0.3
pddf_dmax29.6
pddf_dmax_errornull
porod_volume231.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first2
guinier_point_last8
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDFV4_datloglog_img.png
symmetrynull
last_modified2022-08-15T14:51:04.900446+02:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDFV4
statussuccess
started_at2026-08-11T16:43:08.425632+00:00
finished_at2026-08-11T16:43:16.183065+00:00
source_last_modified2022-08-15T14:51:04.900446+02:00
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View the complete summary.json source
{
  "code": "SASDFV4",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "project": {
    "title": "How the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids.",
    "publication": {
      "title": "How the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids.",
      "author_list": "Mias-Lucquin D, Dos Santos Morais R, Chéron A, Lagarrigue M, Winder SJ, Chenuel T, Pérez J, Appavou MS, Martel A, Alviset G, Le Rumeur E, Combet S, Hubert JF, Delalande O",
      "journal": "J Struct Biol",
      "doi": "10.1016/j.jsb.2019.107411",
      "pmid": "31689503",
      "published_date": "2019 Nov 2"
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    "submitted_date": "2019-03-30",
    "released_date": "2019-11-14"
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View the complete manifest.json source
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