+Open data
-Basic information
Entry | Database: PDB / ID: 4oh4 | ||||||
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Title | Crystal structure of BRI1 in complex with BKI1 | ||||||
Components |
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Keywords | TRANSFERASE/SIGNALING PROTEIN / kinase domain / transferase / ATP binding / Phosphorylation / Membrane / TRANSFERASE-SIGNALING PROTEIN complex | ||||||
Function / homology | Function and homology information negative regulation of brassinosteroid biosynthetic process / detection of brassinosteroid stimulus / brassinosteroid homeostasis / anther wall tapetum cell differentiation / pollen exine formation / seedling development / skotomorphogenesis / positive regulation of flower development / brassinosteroid mediated signaling pathway / leaf development ...negative regulation of brassinosteroid biosynthetic process / detection of brassinosteroid stimulus / brassinosteroid homeostasis / anther wall tapetum cell differentiation / pollen exine formation / seedling development / skotomorphogenesis / positive regulation of flower development / brassinosteroid mediated signaling pathway / leaf development / microtubule bundle formation / response to UV-B / protein kinase inhibitor activity / steroid binding / transmembrane receptor protein tyrosine kinase activity / lipid metabolic process / receptor protein-tyrosine kinase / endosome membrane / non-specific serine/threonine protein kinase / endosome / protein kinase activity / protein heterodimerization activity / phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / protein homodimerization activity / protein-containing complex / ATP binding / identical protein binding / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Arabidopsis thaliana (thale cress) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.25 Å | ||||||
Authors | Wang, J. / Wang, J. / Wu, J.W. / Wang, Z.X. | ||||||
Citation | Journal: Cell Res. / Year: 2014 Title: Structural insights into the negative regulation of BRI1 signaling by BRI1-interacting protein BKI1. Authors: Wang, J. / Jiang, J. / Wang, J. / Chen, L. / Fan, S.L. / Wu, J.W. / Wang, X. / Wang, Z.X. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4oh4.cif.gz | 273.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4oh4.ent.gz | 221.4 KB | Display | PDB format |
PDBx/mmJSON format | 4oh4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/oh/4oh4 ftp://data.pdbj.org/pub/pdb/validation_reports/oh/4oh4 | HTTPS FTP |
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-Related structure data
Related structure data | 4q5jC 2qkwS 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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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 37555.660 Da / Num. of mol.: 2 / Fragment: kinase domain, UNP residues 863-1172 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: At4g39400, BRI1, F23K16.30 / Plasmid: pET-Duet / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) References: UniProt: O22476, receptor protein-tyrosine kinase, non-specific serine/threonine protein kinase #2: Protein/peptide | Mass: 2281.564 Da / Num. of mol.: 2 / Fragment: C-terminal peptide, UNP residues 306-325 / Source method: obtained synthetically Details: This sequence occurs naturally in Arabidopsis thaliana. Source: (synth.) Arabidopsis thaliana (thale cress) / References: UniProt: Q9FMZ0 #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.38 Å3/Da / Density % sol: 48.41 % |
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Crystal grow | Temperature: 294 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 20% PEG 3350, 0.2M Lithium Citrate, 0.1M Hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 0.9793 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Dec 3, 2011 |
Radiation | Monochromator: double crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9793 Å / Relative weight: 1 |
Reflection | Resolution: 2.25→50 Å / Num. all: 35679 / Num. obs: 35446 / % possible obs: 99.5 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 7.3 % / Biso Wilson estimate: 45.77 Å2 / Rmerge(I) obs: 0.066 / Net I/σ(I): 25.4 |
Reflection shell | Resolution: 2.25→2.33 Å / Redundancy: 6.9 % / Rmerge(I) obs: 0.479 / Mean I/σ(I) obs: 2.9 / Num. unique all: 3525 / % possible all: 98.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2QKW Resolution: 2.25→37.839 Å / SU ML: 0.32 / σ(F): 1.34 / Phase error: 32.05 / 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 / Bsol: 36.228 Å2 / ksol: 0.306 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.25→37.839 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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