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- SASDGT5: MvaT (high salt data set) (MvaT(mutant)) -

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Open data


ID or keywords:

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Basic information

Entry
Database: SASBDB / ID: SASDGT5
SampleMvaT (high salt data set)
  • MvaT(mutant) (protein), Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function / homologyMvaT, DNA-binding domain / negative regulation of single-species biofilm formation on inanimate substrate / negative regulation of secondary metabolite biosynthetic process / DNA-binding transcription activator activity / protein-DNA complex / transcription cis-regulatory region binding / positive regulation of DNA-templated transcription / MvaT
Function and homology information
Biological speciesPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (bacteria)
Contact author
  • Yann Sterckx (University of Antwerp)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Models

Model #3792
Type: atomic / P-value: 0.000012
Model #3793
Type: atomic / P-value: 0.000012

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Sample

SampleName: MvaT (high salt data set) / Specimen concentration: 9.5 mg/ml
BufferName: 20 mM Bis-Tris 300 mM KCl / pH: 6
Entity #1888Type: protein / Description: MvaT(mutant) / Formula weight: 14.107 / Num. of mol.: 2
Source: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
References: UniProt: Q9HW86
Sequence:
MSLINEYRAT EEAIKELQER LKSLEQDDKL CKELEDEEKL RTLDGTYQKS LRDVISLLDP DAKIGKSTRT AKAPAGKRAR KVKQYKNPHT GEVIETKGGN HKTLKEWKAK WGPEAVESWA TLLG

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Experimental information

BeamInstrument name: ESRF BioSAXS beamline BM29 / City: Grenoble / 国: France / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.099 Å / Dist. spec. to detc.: 2.81 mm
DetectorName: d / Type: PILATUS 1 M, DECTRIS / Pixsize x: 0.99 mm
Scan
Title: MvaT (high salt data set) / Measurement date: May 11, 2018 / Storage temperature: 20 °C / Cell temperature: 20 °C / Exposure time: 1 sec. / Number of frames: 3000 / Unit: 1/A /
MinMax
Q0.0082 0.4003
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 428 /
MinMax
Q0.00816413 0.208675
P(R) point1 428
R0 158.4
Result
Type of curve: sec
Comments: The protein employed in the SAS experiment contains three point mutations: K31C, F36D, and M44D. K31C was introduced to introduce a paramagnetic label, while F36D and M44D were introduced ...Comments: The protein employed in the SAS experiment contains three point mutations: K31C, F36D, and M44D. K31C was introduced to introduce a paramagnetic label, while F36D and M44D were introduced to abolish higher-order oligomerisation of the protein.
ExperimentalPorod
MW26.45 kDa29.35 kDa
Volume-49.91 nm3

P(R)P(R) errorGuinierGuinier error
Forward scattering, I074.89 0.08 74.46 0.09
Radius of gyration, Rg3.99 nm0.01 3.83 nm0.1

MinMax
D-15.84
Guinier point1 43

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