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Yorodumi- PDB-2dj2: The solution structure of the second thioredoxin domain of mouse ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2dj2 | ||||||
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Title | The solution structure of the second thioredoxin domain of mouse Protein disulfide-isomerase A4 | ||||||
Components | Protein disulfide-isomerase A4 | ||||||
Keywords | ISOMERASE / Protein ERp-72 / ERp72 / Cai / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information positive regulation of protein folding / protein disulfide-isomerase / endoplasmic reticulum chaperone complex / blood coagulation, fibrin clot formation / protein disulfide isomerase activity / smooth endoplasmic reticulum / protein-disulfide reductase activity / chaperone-mediated protein folding / response to endoplasmic reticulum stress / platelet aggregation ...positive regulation of protein folding / protein disulfide-isomerase / endoplasmic reticulum chaperone complex / blood coagulation, fibrin clot formation / protein disulfide isomerase activity / smooth endoplasmic reticulum / protein-disulfide reductase activity / chaperone-mediated protein folding / response to endoplasmic reticulum stress / platelet aggregation / melanosome / integrin binding / protein folding / endoplasmic reticulum lumen / cell surface / endoplasmic reticulum / extracellular space Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Tochio, N. / Koshiba, S. / Inoue, M. / Kigawa, T. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: The solution structure of the second thioredoxin domain of mouse Protein disulfide-isomerase A4 Authors: Tochio, N. / 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 | 2dj2.cif.gz | 710.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2dj2.ent.gz | 595.4 KB | Display | PDB format |
PDBx/mmJSON format | 2dj2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dj/2dj2 ftp://data.pdbj.org/pub/pdb/validation_reports/dj/2dj2 | 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: 13152.770 Da / Num. of mol.: 1 / Fragment: 2nd thioredoxin domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Description: Cell-free protein synthesis / Gene: Pdia4, Cai, Erp72 / Plasmid: P050425-14 / Production host: Cell free synthesis / References: UniProt: P08003, protein disulfide-isomerase |
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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: 1.2mM Thioredoxin domain U-15N,13C; 20mM d-Tris HCl; 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 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
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 900 MHz |
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-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: target function,structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 20 |