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Yorodumi- PDB-1wir: Solution structure of the C2H2 zinc finger domain of the protein ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1wir | ||||||
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Title | Solution structure of the C2H2 zinc finger domain of the protein arginine N-methyltransferase 3 from Mus musculus | ||||||
Components | Protein arginine N-methyltransferase 3 | ||||||
Keywords | TRANSFERASE / C2H2 zinc finger domain / protein arginine N-methyltransferase 3 / PRMT3 / Structural Genomics / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information peptidyl-arginine methylation, to asymmetrical-dimethyl arginine / Protein methylation / modified amino acid binding / peptidyl-arginine methylation / RMTs methylate histone arginines / protein-arginine omega-N asymmetric methyltransferase activity / protein methylation / protein-arginine N-methyltransferase activity / dendritic spine morphogenesis / negative regulation of protein ubiquitination ...peptidyl-arginine methylation, to asymmetrical-dimethyl arginine / Protein methylation / modified amino acid binding / peptidyl-arginine methylation / RMTs methylate histone arginines / protein-arginine omega-N asymmetric methyltransferase activity / protein methylation / protein-arginine N-methyltransferase activity / dendritic spine morphogenesis / negative regulation of protein ubiquitination / Transferases; Transferring one-carbon groups; Methyltransferases / methyltransferase activity / ribosome binding / metal ion binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Miyamoto, K. / Tomizawa, T. / Koshiba, S. / Inoue, M. / Kigawa, T. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution structure of the C2H2 zinc finger domain of the protein arginine N-methyltransferase 3 from Mus musculus Authors: Miyamoto, K. / Tomizawa, T. / Koshiba, S. / Inoue, M. / Kigawa, T. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1wir.cif.gz | 733.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1wir.ent.gz | 613.3 KB | Display | PDB format |
PDBx/mmJSON format | 1wir.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wi/1wir ftp://data.pdbj.org/pub/pdb/validation_reports/wi/1wir | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 13787.360 Da / Num. of mol.: 1 / Fragment: C2H2 zinc finger domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Description: Cell-free protein synthesis / Gene: RIKEN cDNA 2410018A17 / Plasmid: P040126-40 / References: UniProt: Q922H1 |
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#2: Chemical | ChemComp-ZN / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1.14mM C2H2 zinc finger domain U-13C,15N; 20mM d-Tris-HCl(pH7.0); 100mM NaCl; 1mM d-DTT;0.02% NaN3;0.1mM ZnCl2; 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 120mM / pH: 7.0 / Pressure: ambient / Temperature: 296 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations, structures with the lowest energy, target function Conformers calculated total number: 100 / Conformers submitted total number: 20 |