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- PDB-6svh: Protein allostery of the WW domain at atomic resolution: FFpSPR b... -
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Basic information
Entry | Database: PDB / ID: 6svh | ||||||
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Title | Protein allostery of the WW domain at atomic resolution: FFpSPR bound structure | ||||||
![]() | Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 | ||||||
![]() | PEPTIDE BINDING PROTEIN / STRUCTURE FROM CYANA 3.98.12 | ||||||
Function / homology | ![]() cis-trans isomerase activity / phosphothreonine residue binding / negative regulation of cell motility / ubiquitin ligase activator activity / regulation of protein localization to nucleus / GTPase activating protein binding / postsynaptic cytosol / mitogen-activated protein kinase kinase binding / regulation of mitotic nuclear division / negative regulation of SMAD protein signal transduction ...cis-trans isomerase activity / phosphothreonine residue binding / negative regulation of cell motility / ubiquitin ligase activator activity / regulation of protein localization to nucleus / GTPase activating protein binding / postsynaptic cytosol / mitogen-activated protein kinase kinase binding / regulation of mitotic nuclear division / negative regulation of SMAD protein signal transduction / PI5P Regulates TP53 Acetylation / negative regulation of amyloid-beta formation / cytoskeletal motor activity / phosphoserine residue binding / RHO GTPases Activate NADPH Oxidases / protein peptidyl-prolyl isomerization / positive regulation of protein dephosphorylation / ciliary basal body / positive regulation of GTPase activity / regulation of cytokinesis / negative regulation of protein binding / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / Negative regulators of DDX58/IFIH1 signaling / phosphoprotein binding / synapse organization / negative regulation of transforming growth factor beta receptor signaling pathway / regulation of protein phosphorylation / regulation of protein stability / tau protein binding / neuron differentiation / negative regulation of protein catabolic process / negative regulation of ERK1 and ERK2 cascade / ISG15 antiviral mechanism / beta-catenin binding / positive regulation of canonical Wnt signaling pathway / positive regulation of protein binding / midbody / regulation of gene expression / Regulation of TP53 Activity through Phosphorylation / protein stabilization / response to hypoxia / nuclear speck / positive regulation of protein phosphorylation / cell cycle / glutamatergic synapse / positive regulation of transcription by RNA polymerase II / nucleoplasm / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
![]() | Strotz, D. / Orts, J. / Friedmann, M. / Guntert, P. / Vogeli, B. / Riek, R. | ||||||
![]() | ![]() Title: Protein Allostery at Atomic Resolution. Authors: Strotz, D. / Orts, J. / Kadavath, H. / Friedmann, M. / Ghosh, D. / Olsson, S. / Chi, C.N. / Pokharna, A. / Guntert, P. / Vogeli, B. / Riek, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 418.3 KB | Display | ![]() |
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PDB format | ![]() | 364.1 KB | Display | ![]() |
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-Validation report
Summary document | ![]() | 469.3 KB | Display | ![]() |
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Full document | ![]() | 3.7 MB | Display | |
Data in XML | ![]() | 356.6 KB | Display | |
Data in CIF | ![]() | 347.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6svcC ![]() 6sveC C: citing same article ( |
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Similar structure data | |
Other databases |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein/peptide | Mass: 4105.579 Da / Num. of mol.: 1 / Mutation: S18N, W34F Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Sample state: isotropic / Type: NOESY |
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Sample preparation
Details | Type: solution Contents: 1.2 mM [U-100% 13C; U-100% 15N] Pin1 WW domain, 12 mM FFpSPR, 97% H2O/3% D2O Details: Pin1 WW domain FFpSPR bound / Label: 15N/13C sample / Solvent system: 97% H2O/3% D2O | ||||||||||||
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Sample |
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Sample conditions | Details: 10 mM K2PO4, 100 mM NaCl, 0.02 % NaN3 / Ionic strength: 0.15 M / Label: FFpSPR WW domain / pH: 6.0 / Pressure: AMBIENT bar / Temperature: 277.15 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE III / Manufacturer: Bruker / Model: AVANCE III / Field strength: 700 MHz |
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Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 20 |