SASDBV3

Dystrophin central domain repeats 16 to 21 (Δ2146-2305; Becker muscular dystrophy variant)

Data type: SASBDB experimental data Status: Published Curve type: Merged Last updated: 2019-12-06T13:07:15.624532+01:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Dystrophin central domain repeats 16 to 21 (Δ2146-2305; Becker muscular dystrophy variant)

Concentration— – 5.0 mg/mlBuffer / pH20 mM Tris 150 mM NaCl 1 mM EDTA 2% glycerol 5% acetonitrile / 7.5
Experimental temperature— Facility / beamlineSOLEIL / SWING
Wavelength0.1 nmExposure1.5 s × 21

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Dystrophin central domain repeats 16 to 21 (Δ2146-2305; Becker muscular dystrophy variant, deletion of exons 45-47)
View sequence
GSLEISYVPSTYLTEITHVSQALLEVEQLLNAPDLCAKDFEDLFKQEESLKNIKDSLQQSSGRIDIIHSKKTAALQSATPVERVKLQEALSQLDFQWEKVNKMYKDRQGRFDRSVEKWRRFHYDIKIFNQWLTEAEQFLRKTQIPENWEHAKYKWYLKVSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQPNQEGPFDVQETEIAVQAKQPDVEEILSKGQHLYKEKPATQPVKRKLEDLSSEWKAVNRLLQELRAKQPDLAPGLTTIGASPTQTVTLVTQPVVTKETAISKLEMPSSLMLEVPALADFNRAWTELTDWLSLLDQVIKSQRVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNKTSNQEARTIITDRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALKLLRDYSADDTRKVHMITENINASWRSIHKRVSEREAALEETHRLLQQF
proteinHomo sapiensP115321991–2694monomerMolecule count 163.894 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1973[3]0.0621535–5.99563 1/nmHas uncertainty columnMissing 00sasbdb/entries/v3/sasdbv3/source/SASDBV3.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)21.0—nm
i0Guinier0.00010462——
i0P(r)0.0001——
mwExperimental210.0—kDa
porod_volumePorod184.0—nm³
rgGuinier6.01—nm
rgP(r)6.01—nm

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 150 mM NaCl 1 mM EDTA 2% glycerol 5% acetonitrileBuffer concentration20.0 mM
pH7.5Additives150 mM NaCl, 1 mM EDTA, 2% glycerol, 5% acetonitrile
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2014-02-05Storage / measurement temperature15.0 / —
Exposure time1.5Frames21
Wavelength0.1Sample-to-detector distance1.82
SourceX-ray synchrotronDetectorAVIEX PCCD170170
Facility / beamlineSOLEIL / SWING · Saint-Aubin, France
q range0.062 – 5.996Sample 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

CategoryFileStatusSizeChecksumDownload and View
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full_entry_zipsasbdb/entries/v3/sasdbv3/source/SASDBV3.zipdownloaded14001919d14542c51cc7a50bd10f158bd65ae205d4b9105b0e1d106b449ddf2d70321aDownloadView source fileSource site
pddfsasbdb/entries/v3/sasdbv3/source/SASDBV3.outdownloaded4214322d557113dc0cf116f9762a8f8d98992f95778dc59111fda3bd5a6e367d3653aDownloadView source fileSource site
sascifsasbdb/entries/v3/sasdbv3/source/SASDBV3.sascifdownloaded1936699a6608c416ebe84e43e84b0fe87a0027957b7e81f1434828f5cd79f03688fe0dDownloadView source fileSource site
summarysasbdb/entries/v3/sasdbv3/source/summary.jsondownloaded12517e1d343d0c8564512d22c9adac9cfca644a21a83fbb962c6f3f668f41f8c3d865DownloadView source fileSource site
curve:source record
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full_entry_zip:source record and ZIP contents (8 items)
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pddf:source record
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sascif: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:156 field values
Field pathRaw value
codeSASDBV3
statusPublished
type_of_curveMerged
angular_unit1/nm
project.titleDystrophin's central domain forms a complex filament that becomes disorganized by in-frame deletions.
project.publication.titleDystrophin's central domain forms a complex filament that becomes disorganized by in-frame deletions.
project.publication.author_listDelalande O, Molza AE, Dos Santos Morais R, Chéron A, Pollet É, Raguenes-Nicol C, Tascon C, Giudice E, Guilbaud M, Nicolas A, Bondon A, Leturcq F, Férey N, Baaden M, Perez J, Roblin P, Piétri-Rouxel F, Hubert JF, Czjzek M, Le Rumeur E
project.publication.journalJ Biol Chem
project.publication.doi10.1074/jbc.M117.809798
project.publication.pmid29535188
project.publication.published_date2018 May 4
project.statusreleased
project.submitted_date2016-01-20
project.released_date2018-04-21
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDBV3.out
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDBV3.dat
intensities_log_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDBV3_dat_img.png
intensities_kratky_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDBV3_kratky_img.png
pddf_plothttps://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDBV3_pofr_img.png
intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDBV3_guinier_img.png
sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDBV3.sascif
experiment.instrument.detector.typeCCD
experiment.instrument.detector.nameAVIEX PCCD170170
experiment.instrument.detector.resolutionnull
experiment.instrument.nameSOLEIL
experiment.instrument.citySaint-Aubin
experiment.instrument.countryFrance
experiment.instrument.beamline_nameSWING
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_nameDystrophin central domain repeats 16 to 21 (Δ2146-2305; Becker muscular dystrophy variant, deletion of exons 45-47)
experiment.sample.molecule[0].short_nameDystrophin1991-2694Δ
experiment.sample.molecule[0].sequenceGSleisyvpsty lteithvsqa lleveqllna pdlcakdfed lfkqeeslkn ikdslqqssg ridiihskkt aalqsatpve rvklqealsq ldfqwekvnk mykdrqgrfd rs vekwrrfh ydikifnqwl teaeqflrkt qipenwehak ykwylk vsralp ekqgeieaqi kdlgql ekkl edleeqlnhl llwlspirnq leiynqpnqe gpfdvqetei avqakqpdve eilskgqhly kekpatqpvk rkledlssew kavnrllqel rakqpdlapg lttigasptq tvtlvtqpvv tketaiskle mpsslmle vp aladfnrawt eltdwlslld qviksqrvmv gdledinemi ikqkatmqdl eqrrpqleel itaaqnlknk tsnqeartii tdrieriqnq wdevqehlqn rrqqlnemlk dstqwleake eaeqvlgqar akleswkegp ytvdaiqkki tetkqlakdl rqwqtnvdva ndlalkllrd ysaddtrkvh miteninasw rsihkrvser eaaleethrl lqqf
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeP11532
experiment.sample.molecule[0].uniprot_range_first1991
experiment.sample.molecule[0].uniprot_range_last2694
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].mw63.894
experiment.sample.molecule[0].total_mw63.894
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 150 mM NaCl 1 mM EDTA 2% glycerol 5% acetonitrile
experiment.sample.buffer.concentration_unitmM
experiment.sample.buffer.commentnull
experiment.sample.buffer.additive150 mM NaCl, 1 mM EDTA, 2% glycerol, 5% acetonitrile
experiment.sample.buffer.concentration20.0
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph7.5
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameDystrophin central domain repeats 16 to 21 (Δ2146-2305; Becker muscular dystrophy variant)
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].addressInstitut Génétique et Développement de Rennes, France
experiment.contributor[0].affiliation[0].full_nameUniversité de Rennes 1
experiment.contributor[0].affiliation[0].webpage
experiment.contributor[0].contributor_nameElisabeth
experiment.contributor[0].contributor_surnameLe Rumeur
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitmg/ml
experiment.date2014-02-05
experiment.storage_temperature15.0
experiment.cell_temperaturenull
experiment.exposure_time1.5
experiment.number_of_frames21
experiment.wavelength0.1
experiment.sample_detector_distance1.82
experiment.concentration_minnull
experiment.concentration_max5.0
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.062
experiment.s_max5.996
experiment.total_exposure_timenull
experiment.seccolumnnull
fits[0].models[0].model_plothttps://www.sasbdb.org/media/pdb_file/images/SASDBV3_fit1_model1_img.png
fits[0].models[0].softwareGASBOR
fits[0].models[0].pdb_link[]
fits[0].models[0].model_titlenull
fits[0].models[0].type_of_modeldummy
fits[0].models[0].software_version
fits[0].models[0].model_datahttps://www.sasbdb.org/media/pdb_file/SASDBV3_fit1_model1.pdb
fits[0].models[0].model_mwnull
fits[0].models[0].bead_radius1.9
fits[0].models[0].lognull
fits[0].models[0].symmetry
fits[0].models[0].comment
fits[0].models[0].user97
fits[0].fit_unit1/A
fits[0].fit_plothttps://www.sasbdb.org/media/fitting_files/scattering_plots/SASDBV3_fit1_fit_img.png
fits[0].softwarenull
fits[0].chi_square_value2.34
fits[0].p_value0.0005
fits[0].fit_residual_plotSASDBV3_fit1_fitresiduals_img.png
fits[0].fit_datahttps://www.sasbdb.org/media/fitting_files/SASDBV3_fit1.fir
fits[0].fit_lognull
fits[0].software_versionnull
fits[0].descriptionnull
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_versionnull
i0_calibration_standardnull
descriptionnull
experiment_descriptionSynchrotron SAXS data were measured from solutions of Human Dystrophin central domain repeats 16 to 21 Becker muscular dystrophy variant (Δ2146-2305 deletion of exons 45-47) in 20 mM Tris 150 mM NaCl, 1 mM EDTA, 2% glycerol, 5% acetonitrile buffer using size exclusion chromatography (SEC-SAXS) on the SWING beam line (SOLEIL, Saint-Aubin, France). The sample load concentration was 5 mg/mL. The scattering data, I(s) vs s (s = 4π sin θ/λ, where 2θ is the scattering angle) were collected through the corresponding SEC protein elution peak (21 x 1.5 s frames) as well as from the SEC column running buffer. The buffer scattering contributions were subtracted from each sample frame, which were then scaled and averaged to produce the SAXS profile displayed in this entry. The corresponding UV SEC-SAXS trace can be found in the full entry zip archive. The SAXS acquisition was performed on the peak positioned at 11.49 minutes on the 280 nm UV trace where the SEC-SAXS frames produced consistent Rg and I(0). The experimental MW was estimated from exclusion chromatography to be 210 kDa for a Stokes radius of 6.3 nm. However, as the protein is elongated, the calculation of the MW from Stokes radius is a large overestimation. In addition to the the Gasbor model displayed above, an image of the protein viewed as a continuous volume representation is also included in the full entry zip archive following the protocol designed by John Stone et al. (VMD, MDFF package).
tags[]
intensity_unitnull
experimental_mw210.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mwnull
porod_mw_errornull
pddf_i00.0001
pddf_i0_errornull
guinier_i00.00010462
guinier_i0_errornull
pddf_rg6.01
pddf_rg_errornull
guinier_rg6.01
guinier_rg_errornull
pddf_dmax21.0
pddf_dmax_errornull
porod_volume184.0
porod_volume_errornull
estimated_volumenull
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guinier_point_first4
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manifest.json:36 field values
Field pathRaw value
codeSASDBV3
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View the complete summary.json source
{
  "code": "SASDBV3",
  "status": "Published",
  "type_of_curve": "Merged",
  "angular_unit": "1/nm",
  "project": {
    "title": "Dystrophin's central domain forms a complex filament that becomes disorganized by in-frame deletions.",
    "publication": {
      "title": "Dystrophin's central domain forms a complex filament that becomes disorganized by in-frame deletions.",
      "author_list": "Delalande O, Molza AE, Dos Santos Morais R, Chéron A, Pollet É, Raguenes-Nicol C, Tascon C, Giudice E, Guilbaud M, Nicolas A, Bondon A, Leturcq F, Férey N, Baaden M, Perez J, Roblin P, Piétri-Rouxel F, Hubert JF, Czjzek M, Le Rumeur E",
      "journal": "J Biol Chem",
      "doi": "10.1074/jbc.M117.809798",
      "pmid": "29535188",
      "published_date": "2018 May 4"
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View the complete manifest.json source
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