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- PDB-7oqj: Ternary complex of 14-3-3 sigma, Amot-p130 phosphopeptide, and WQ162 -
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Open data
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Basic information
Entry | Database: PDB / ID: 7oqj | ||||||
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Title | Ternary complex of 14-3-3 sigma, Amot-p130 phosphopeptide, and WQ162 | ||||||
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Function / homology | ![]() establishment of cell polarity involved in ameboidal cell migration / cell migration involved in gastrulation / positive regulation of embryonic development / Regulation of CDH11 function / blood vessel endothelial cell migration / establishment of epithelial cell polarity / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Centorrino, F. / Ottmann, C. | ||||||
Funding support | European Union, 1items
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![]() | ![]() Title: A crystallography-based study of fragment extensions into the 14-3-3 binding groove Authors: Centorrino, F. / Wu, Q. / Cossar, P. / Brunsveld, L. / Ottmann, C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 132.5 KB | Display | ![]() |
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PDB format | ![]() | 84 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 7opwC ![]() 7oq7C ![]() 7oq8C ![]() 7oq9C ![]() 7oqaC ![]() 7oqgC ![]() 7oqsC ![]() 7oquC ![]() 7oqwC ![]() 7or3C ![]() 7or5C ![]() 7or7C ![]() 7or8C ![]() 7orgC ![]() 7orhC ![]() 7orsC ![]() 7ortC ![]() 4jc3S S: Starting model for refinement C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 28226.518 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() | ||||||
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#2: Protein/peptide | Mass: 1626.817 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() ![]() | ||||||
#3: Chemical | #4: Chemical | ChemComp-CL / | ![]() #5: Water | ChemComp-HOH / | ![]() Has ligand of interest | Y | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.38 Å3/Da / Density % sol: 48.29 % |
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Crystal grow![]() | Temperature: 277.15 K / Method: vapor diffusion, hanging drop Details: 0.095 M Hepes pH 7.5, 26% PEG 400, 0.19 M CaCl2, and 5% Glycerol |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Feb 5, 2021 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.4→61.94 Å / Num. obs: 56362 / % possible obs: 100 % / Redundancy: 12.7 % / Biso Wilson estimate: 12.3 Å2 / CC1/2: 0.996 / Rpim(I) all: 0.067 / Net I/σ(I): 10 |
Reflection shell | Resolution: 1.4→1.42 Å / Redundancy: 12.9 % / Mean I/σ(I) obs: 1.4 / Num. unique obs: 2758 / CC1/2: 0.714 / Rpim(I) all: 1.019 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: 4JC3 Resolution: 1.4→55.37 Å / SU ML: 0.1581 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 21.2471 / Stereochemistry target values: GeoStd + Monomer Library
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 20.38 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.4→55.37 Å
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Refine LS restraints |
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LS refinement shell |
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