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- PDB-1zw2: Vinculin Head (0-258) in Complex with the Talin Rod residues 2345-2369 -
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Open data
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Basic information
Entry | Database: PDB / ID: 1zw2 | ||||||
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Title | Vinculin Head (0-258) in Complex with the Talin Rod residues 2345-2369 | ||||||
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![]() | PROTEIN BINDING / TALIN / VINCULIN / COMPLEX | ||||||
Function / homology | ![]() muscle tendon junction / Platelet degranulation / Smooth Muscle Contraction / regulation of protein localization to adherens junction / podosome ring / outer dense plaque of desmosome / inner dense plaque of desmosome / terminal web / epithelial cell-cell adhesion / zonula adherens ...muscle tendon junction / Platelet degranulation / Smooth Muscle Contraction / regulation of protein localization to adherens junction / podosome ring / outer dense plaque of desmosome / inner dense plaque of desmosome / terminal web / epithelial cell-cell adhesion / zonula adherens / dystroglycan binding / muscle alpha-actinin binding / MAP2K and MAPK activation / alpha-catenin binding / vinculin binding / fascia adherens / cell-cell contact zone / apical junction assembly / adherens junction assembly / costamere / regulation of establishment of endothelial barrier / axon extension / protein localization to cell surface / lamellipodium assembly / regulation of focal adhesion assembly / alpha-actinin binding / brush border / skeletal muscle myofibril / stress fiber / ruffle / regulation of cell migration / Neutrophil degranulation / cell projection / morphogenesis of an epithelium / adherens junction / neuromuscular junction / structural constituent of cytoskeleton / sarcolemma / cell-cell adhesion / ruffle membrane / Z disc / beta-catenin binding / actin filament binding / cell-cell junction / actin cytoskeleton / integrin binding / scaffold protein binding / mitochondrial inner membrane / cytoskeleton / cell adhesion / cadherin binding / focal adhesion / ubiquitin protein ligase binding / structural molecule activity / cell surface / protein homodimerization activity / protein-containing complex / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Gingras, A.R. / Ziegler, W.H. / Barsukov, I.L. / Roberts, G.C. / Critchley, D.R. / Emsley, J. | ||||||
![]() | ![]() Title: Mapping and consensus sequence identification for multiple vinculin binding sites within the talin rod Authors: Gingras, A.R. / Ziegler, W.H. / Frank, R. / Barsukov, I.L. / Roberts, G.C. / Critchley, D.R. / Emsley, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 66.9 KB | Display | ![]() |
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PDB format | ![]() | 48.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1zvzC ![]() 1zw3C ![]() 1xwjS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 31195.908 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 2444.802 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: The peptide was chemically synthesized. The sequence of the peptide is naturally found in Gallus gallus (chicken). References: GenBank: 45383127, UniProt: P54939*PLUS |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 52.4 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7 Details: 100mM Tris, pH 7.0, 20% PEG 2000 MME, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Nov 29, 2004 / Details: TOROIDAL ZERODUR MIRROR |
Radiation | Monochromator: Diamond (111), Ge(220) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.931 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→20 Å / Num. all: 21165 / Num. obs: 21165 / Rmerge(I) obs: 0.065 / Net I/σ(I): 23.4 |
Reflection shell | Resolution: 2.1→2.17 Å / Rmerge(I) obs: 0.38 / Mean I/σ(I) obs: 2.49 / % possible all: 85.1 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1XWJ Resolution: 2.1→20 Å / Cor.coef. Fo:Fc: 0.941 / Cor.coef. Fo:Fc free: 0.922 / SU B: 8.305 / SU ML: 0.202 / Cross valid method: THROUGHOUT / ESU R: 0.277 / ESU R Free: 0.229 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 51.525 Å2
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Refinement step | Cycle: LAST / Resolution: 2.1→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.1→2.154 Å / Total num. of bins used: 20
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