SASDB72

Death associated protein kinase (Basic Loop mutant)

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2023-06-21T07:56:39.492710+02:00

Characterisation of mutation of basic loop residues (R47E, R50E, R53E, R54E) on dimer formation of hDAPK2

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Death associated protein kinase (Basic Loop mutant)

Concentration— – 2.0 mg/mlBuffer / pH50 mM HEPES 250 mM NaCl 5mM CaCl2 0.25 mM TCEP 5% (v/v) glycerol / 7.5
Experimental temperature10.0 Facility / beamlinePETRA III / EMBL P12
Wavelength0.12 nmExposure0.05 s × 20

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Death associated protein kinase (Basic Loop mutant)
View sequence
GPMSEPFKQQKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKEQSEASEEGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITSVSYDFDEEFFSHTSELAKDFIRKLLVKETRKRLTIQEALRHPWITPVDNQQAMVRRESVVNLENFRKQYVRRRWKLSFSIVSLCNHLTR
proteinHomo sapiens——–—otherMolecule count —37.3 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
11682[3]0.027543–4.45043 1/nmHas uncertainty columnMissing 0261sasbdb/entries/72/sasdb72/source/SASDB72.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)7.5—nm
estimated_volumeReported45000.0—nm³
i0Guinier623.0——
i0P(r)617.0——
mwExperimental32.0—kDa
mwPorod46.0—kDa
porod_volumePorod78.0—nm³
rgGuinier2.4—nm
rgP(r)2.3—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 name50 mM HEPES 250 mM NaCl 5mM CaCl2 0.25 mM TCEP 5% (v/v) glycerolBuffer concentration50.0 mM
pH7.5Additives250 mM NaCl, 5mM CaCl2, 0.25 mM TCEP, 5% [v/v] glycerol
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / 45000Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2013-12-18Storage / measurement temperature10.0 / 10.0
Exposure time0.05Frames20
Wavelength0.12Sample-to-detector distance3.1
SourceX-ray synchrotronDetectorPilatus 2M
Facility / beamlinePETRA III / EMBL P12 · DESY; Hamburg, Germany
q range0.028 – 4.45Sample 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:169 field values
Field pathRaw value
codeSASDB72
statusPublished
type_of_curveSingle concentration
angular_unit1/nm
project.titleDeath-Associated Protein Kinase Activity Is Regulated by Coupled Calcium/Calmodulin Binding to Two Distinct Sites.
project.publication.titleDeath-Associated Protein Kinase Activity Is Regulated by Coupled Calcium/Calmodulin Binding to Two Distinct Sites.
project.publication.author_listSimon B, Huart AS, Temmerman K, Vahokoski J, Mertens HD, Komadina D, Hoffmann JE, Yumerefendi H, Svergun DI, Kursula P, Schultz C, McCarthy AA, Hart DJ, Wilmanns M
project.publication.journalStructure
project.publication.doi10.1016/j.str.2016.03.020
project.publication.pmid27133022
project.publication.published_date2016 Jun 7
project.statusreleased
project.submitted_date2015-09-24
project.released_date2015-09-24
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experiment.instrument.detector.namePilatus 2M
experiment.instrument.detector.resolutionnull
experiment.instrument.namePETRA III
experiment.instrument.cityDESY; Hamburg
experiment.instrument.countryGermany
experiment.instrument.beamline_nameEMBL P12
experiment.instrument.beam_geometrynull
experiment.instrument.type_of_sourceX-ray synchrotron
experiment.instrument.point_sourcenull
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experiment.instrument.beam_profile_alnull
experiment.sample.molecule[0].long_nameDeath associated protein kinase (Basic Loop mutant)
experiment.sample.molecule[0].short_namehDAPK2 BL mutant
experiment.sample.molecule[0].sequenceGPMSEPFKQQKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKEQSEASEEGVS REEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSGGELFDFLAQKESLSEEEAT SFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEIEDGVEFKNI FGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITSVSYDFD EEFFSHTSELAKDFIRKLLVKETRKRLTIQEALRHPWITPVDNQQAMVRRESVVNLENFR KQYVRRRWKLSFSIVSLCNHLTR
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codenull
experiment.sample.molecule[0].uniprot_range_firstnull
experiment.sample.molecule[0].uniprot_range_lastnull
experiment.sample.molecule[0].oligomerizationother
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequencenull
experiment.sample.molecule[0].mw37.3
experiment.sample.molecule[0].total_mw37.3
experiment.sample.molecule[0].number_molecules0
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.name50 mM HEPES 250 mM NaCl 5mM CaCl2 0.25 mM TCEP 5% (v/v) glycerol
experiment.sample.buffer.concentration_unitmM
experiment.sample.buffer.commentnull
experiment.sample.buffer.additive250 mM NaCl, 5mM CaCl2, 0.25 mM TCEP, 5% [v/v] glycerol
experiment.sample.buffer.concentration50.0
experiment.sample.buffer.pkanull
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experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameDeath associated protein kinase (Basic Loop mutant)
experiment.sample.ext_coefficientnull
experiment.sample.contrastnull
experiment.sample.specific_volnull
experiment.sample.dry_vol45000
experiment.sample.absorbptionnull
experiment.sample.deuterationnull
experiment.sample.mixturenull
experiment.contributor[0].affiliation[0].short_nameEMBL-Hamburg
experiment.contributor[0].affiliation[0].addressNotkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany
experiment.contributor[0].affiliation[0].full_nameEuropean Molecular Biology Laboratory (EMBL) - Hamburg outstation
experiment.contributor[0].affiliation[0].webpagehttp://www.embl-hamburg.de/index.php
experiment.contributor[0].contributor_nameHaydyn
experiment.contributor[0].contributor_surnameMertens
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitmg/ml
experiment.date2013-12-18
experiment.storage_temperature10.0
experiment.cell_temperature10.0
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pddf_softwareATSAS GNOM
pddf_software_versionGNOM
i0_calibration_standardnull
descriptionCharacterisation of mutation of basic loop residues (R47E, R50E, R53E, R54E) on dimer formation of hDAPK2
experiment_descriptionnull
tags[]
intensity_unitnull
experimental_mw32.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw46.0
porod_mw_errornull
pddf_i0617.0
pddf_i0_errornull
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pddf_dmax_errornull
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porod_volume_errornull
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estimated_volume_errornull
guinier_point_first48
guinier_point_last189
pddf_point_first48
pddf_point_last1274
i0_calibration_standard_datanull
intensities_log_log_plotSASDB72_datloglog_img.png
symmetrynull
last_modified2023-06-21T07:56:39.492710+02:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDB72
statussuccess
started_at2026-08-11T13:31:51.324340+00:00
finished_at2026-08-11T13:32:01.217923+00:00
source_last_modified2023-06-21T07:56:39.492710+02:00
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View the complete summary.json source
{
  "code": "SASDB72",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/nm",
  "project": {
    "title": "Death-Associated Protein Kinase Activity Is Regulated by Coupled Calcium/Calmodulin Binding to Two Distinct Sites.",
    "publication": {
      "title": "Death-Associated Protein Kinase Activity Is Regulated by Coupled Calcium/Calmodulin Binding to Two Distinct Sites.",
      "author_list": "Simon B, Huart AS, Temmerman K, Vahokoski J, Mertens HD, Komadina D, Hoffmann JE, Yumerefendi H, Svergun DI, Kursula P, Schultz C, McCarthy AA, Hart DJ, Wilmanns M",
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      "doi": "10.1016/j.str.2016.03.020",
      "pmid": "27133022",
      "published_date": "2016 Jun 7"
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    "released_date": "2015-09-24"
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