+Open data
-Basic information
Entry | Database: PDB / ID: 5nwi | ||||||
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Title | 14-3-3c in complex with CPP | ||||||
Components |
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Keywords | SIGNALING PROTEIN / 14-3-3 / complex / fusicoccin / channel | ||||||
Function / homology | Function and homology information inward rectifier potassium channel activity / monoatomic ion channel complex / signal transduction / identical protein binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Nicotiana tabacum (common tobacco) Arabidopsis thaliana (thale cress) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.35 Å | ||||||
Authors | Saponaro, A. / Porro, A. / Chaves-Sanjuan, A. / Nardini, M. / Thiel, G. / Moroni, A. | ||||||
Citation | Journal: Plant Cell / Year: 2017 Title: Fusicoccin Activates KAT1 Channels by Stabilizing Their Interaction with 14-3-3 Proteins. Authors: Saponaro, A. / Porro, A. / Chaves-Sanjuan, A. / Nardini, M. / Rauh, O. / Thiel, G. / Moroni, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5nwi.cif.gz | 118.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5nwi.ent.gz | 91.7 KB | Display | PDB format |
PDBx/mmJSON format | 5nwi.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nw/5nwi ftp://data.pdbj.org/pub/pdb/validation_reports/nw/5nwi | HTTPS FTP |
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-Related structure data
Related structure data | 5nwjC 5nwkC 1o9dS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-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: 29554.143 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: Initial PG do not belongs to the natural protein sequence Source: (gene. exp.) Nicotiana tabacum (common tobacco) / Gene: 14-3-3 c-1, LOC107777576, Nt14-3-3omega2 / Production host: Escherichia coli BL21 (bacteria) / References: UniProt: Q5KTN5, UniProt: P93343*PLUS |
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#2: Protein/peptide | Mass: 696.600 Da / Num. of mol.: 1 / Fragment: UNP residues 673-677 / Source method: obtained synthetically / Source: (synth.) Arabidopsis thaliana (thale cress) / References: UniProt: Q39128 |
#3: Chemical | ChemComp-ACT / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.96 Å3/Da / Density % sol: 68.93 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop Details: 30% PEG 400, 0.2 M ammonium acetate pH 7.0, 0.1 M sodium citrate pH 4.4, 10mM DTT and 5% glycerol |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: MASSIF-3 / Wavelength: 0.9677 Å |
Detector | Type: DECTRIS EIGER X 4M / Detector: PIXEL / Date: Apr 2, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9677 Å / Relative weight: 1 |
Reflection | Resolution: 2.35→47.71 Å / Num. obs: 21014 / % possible obs: 100 % / Observed criterion σ(I): 5.1 / Redundancy: 39 % / Biso Wilson estimate: 32.28 Å2 / CC1/2: 0.971 / Rpim(I) all: 0.045 / Net I/σ(I): 15.2 |
Reflection shell | Resolution: 2.35→2.43 Å / Redundancy: 27.7 % / Mean I/σ(I) obs: 5.1 / Num. unique obs: 2044 / CC1/2: 0.706 / Rpim(I) all: 0.365 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1O9D Resolution: 2.35→45.043 Å / SU ML: 0.35 / Cross valid method: FREE R-VALUE / σ(F): 1.61 / Phase error: 23.21 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.35→45.043 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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