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Yorodumi- PDB-4n1j: Crystal structures of NLRP14 pyrin domain reveal a conformational... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4n1j | ||||||
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Title | Crystal structures of NLRP14 pyrin domain reveal a conformational switch mechanism, regulating its molecular interactions | ||||||
Components | NACHT, LRR and PYD domains-containing protein 14 | ||||||
Keywords | SIGNALING PROTEIN / death domain fold / pyrin domain / NOD-like receptor / protein binding / spermatogenesis / innate immunity | ||||||
Function / homology | Function and homology information regulation of inflammatory response / spermatogenesis / cell differentiation / ATP binding / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.6 Å | ||||||
Authors | Eibl, C. / Hessenberger, M. / Wenger, J. / Brandstetter, H. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 2014 Title: Structures of the NLRP14 pyrin domain reveal a conformational switch mechanism regulating its molecular interactions. Authors: Eibl, C. / Hessenberger, M. / Wenger, J. / Brandstetter, H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4n1j.cif.gz | 84.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4n1j.ent.gz | 70.4 KB | Display | PDB format |
PDBx/mmJSON format | 4n1j.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4n1j_validation.pdf.gz | 461.8 KB | Display | wwPDB validaton report |
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Full document | 4n1j_full_validation.pdf.gz | 468.6 KB | Display | |
Data in XML | 4n1j_validation.xml.gz | 15.2 KB | Display | |
Data in CIF | 4n1j_validation.cif.gz | 20.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/n1/4n1j ftp://data.pdbj.org/pub/pdb/validation_reports/n1/4n1j | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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3 |
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Unit cell |
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-Components
#1: Protein | Mass: 12452.578 Da / Num. of mol.: 4 / Fragment: UNP residues 1-100 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: NLRP14, NALP14, NOD5 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 Star (DE3) / References: UniProt: Q86W24 #2: Chemical | #3: 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: 2.51 Å3/Da / Density % sol: 50.98 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 0.1 M HEPES pH 7.5, 2.6 M Ammonium sulfate and 2% PEG400, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: BESSY / Beamline: 14.1 / Wavelength: 0.97973, 0.97626, 1.00801, 0.97985 | |||||||||||||||
Detector | Type: RAYONIX MX-225 / Detector: CCD / Date: Oct 4, 2011 / Details: mirrors | |||||||||||||||
Radiation | Monochromator: Double Crystal Monochromator / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||
Radiation wavelength |
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Reflection | Resolution: 2.36→44.79 Å / Num. obs: 19457 / % possible obs: 95.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 7.2 % | |||||||||||||||
Reflection shell | Resolution: 2.36→2.49 Å / % possible all: 99.9 |
-Processing
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Refinement | Method to determine structure: MAD / Resolution: 2.6→44.79 Å / SU ML: 0.4 / σ(F): 1.33 / Phase error: 29.02 / 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: 2.6→44.79 Å
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Refine LS restraints |
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LS refinement shell |
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