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Open data
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Basic information
Entry | Database: PDB / ID: 2kap | ||||||
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Title | Solution structure of DLC1-SAM | ||||||
![]() | Rho GTPase-activating protein 7 | ||||||
![]() | SIGNALING PROTEIN / Solution Structure / SAM domain / DLC-1 / Cytoplasm / GTPase activation / Phosphoprotein / Polymorphism | ||||||
Function / homology | ![]() hindbrain morphogenesis / negative regulation of focal adhesion assembly / regulation of Rho protein signal transduction / focal adhesion assembly / regulation of small GTPase mediated signal transduction / negative regulation of stress fiber assembly / negative regulation of Rho protein signal transduction / cortical actin cytoskeleton / RHOB GTPase cycle / RHOC GTPase cycle ...hindbrain morphogenesis / negative regulation of focal adhesion assembly / regulation of Rho protein signal transduction / focal adhesion assembly / regulation of small GTPase mediated signal transduction / negative regulation of stress fiber assembly / negative regulation of Rho protein signal transduction / cortical actin cytoskeleton / RHOB GTPase cycle / RHOC GTPase cycle / RHOQ GTPase cycle / positive regulation of execution phase of apoptosis / CDC42 GTPase cycle / RHOA GTPase cycle / heart morphogenesis / positive regulation of protein dephosphorylation / forebrain development / RAC1 GTPase cycle / SH2 domain binding / negative regulation of cell migration / GTPase activator activity / neural tube closure / caveola / regulation of actin cytoskeleton organization / ruffle membrane / activation of cysteine-type endopeptidase activity involved in apoptotic process / regulation of cell shape / actin cytoskeleton organization / membrane raft / negative regulation of cell population proliferation / intracellular membrane-bounded organelle / focal adhesion / lipid binding / apoptotic process / endoplasmic reticulum / signal transduction / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / molecular dynamics | ||||||
![]() | Yang, S. / Yang, D. | ||||||
![]() | ![]() Title: Characterization of DLC1-SAM equilibrium unfolding at the amino acid residue level Authors: Yang, S. / Noble, C.G. / Yang, D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 197.9 KB | Display | ![]() |
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PDB format | ![]() | 162.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 350.8 KB | Display | ![]() |
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Full document | ![]() | 402.8 KB | Display | |
Data in XML | ![]() | 9.9 KB | Display | |
Data in CIF | ![]() | 16.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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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 | Mass: 7102.202 Da / Num. of mol.: 1 Fragment: sterile alpha motif (SAM) domain, UNP residues 17-76 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 |
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Sample preparation
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Sample |
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Sample conditions | pH: 6.8 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 500 MHz |
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Processing
NMR software |
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Refinement | Method: molecular dynamics / Software ordinal: 1 | |||||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 10 / Representative conformer: 1 |