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Yorodumi- PDB-1wik: Solution Structure of the PICOT homology 2 domain of the mouse PK... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1wik | ||||||
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Title | Solution Structure of the PICOT homology 2 domain of the mouse PKC-interacting cousin of thioredoxin protein | ||||||
Components | Thioredoxin-like protein 2 | ||||||
Keywords | ELECTRON TRANSPORT / PICOT homology 2 domain / PICOT protein / thioredoxin like 2 / Structural Genomics / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information protein maturation by iron-sulfur cluster transfer / negative regulation of cardiac muscle hypertrophy / regulation of the force of heart contraction / [2Fe-2S] cluster assembly / iron-sulfur cluster binding / protein-disulfide reductase activity / protein kinase C binding / Z disc / cell cortex / intracellular iron ion homeostasis ...protein maturation by iron-sulfur cluster transfer / negative regulation of cardiac muscle hypertrophy / regulation of the force of heart contraction / [2Fe-2S] cluster assembly / iron-sulfur cluster binding / protein-disulfide reductase activity / protein kinase C binding / Z disc / cell cortex / intracellular iron ion homeostasis / dendrite / identical protein binding / metal ion binding / nucleus / cytosol 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 PICOT homology 2 domain of the mouse PKC-interacting cousin of thioredoxin protein 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 | 1wik.cif.gz | 642.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1wik.ent.gz | 557.9 KB | Display | PDB format |
PDBx/mmJSON format | 1wik.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wi/1wik ftp://data.pdbj.org/pub/pdb/validation_reports/wi/1wik | 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: 11840.396 Da / Num. of mol.: 1 / Fragment: PICOT homology 2 domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Description: Cell-free protein synthesis / Gene: RIKEN cDNA 2410003E11 / Plasmid: P030421-03 / References: UniProt: Q9CQM9 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 0.65mM PICOT homology 2 domain U-13C,15N; 20mM d-Tris-HCl(pH6.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10%D2O Solvent system: 90% H2O, 10% D20 |
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Sample conditions | Ionic strength: 120mM / pH: 6.0 / Pressure: ambient / Temperature: 298 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: 600 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 |