[English] 日本語
Yorodumi- PDB-2rqs: 3D structure of Pin from the psychrophilic archeon Cenarcheaum sy... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2rqs | ||||||
---|---|---|---|---|---|---|---|
Title | 3D structure of Pin from the psychrophilic archeon Cenarcheaum symbiosum (CsPin) | ||||||
Components | Parvulin-like peptidyl-prolyl isomerase | ||||||
Keywords | ISOMERASE / cis/trans isomerisation / Cenarcheaum symbiosum / low temperature / NIMA-kinase / parvulin / Pin1 / cell cycle | ||||||
Function / homology | Function and homology information peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / rRNA processing / DNA binding Similarity search - Function | ||||||
Biological species | Cenarchaeum symbiosum (archaea) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | Pin (protein interacting with NIMA-kinase) catalyzes the cis/trans isomerisation of Xaa-Pro peptide ...Pin (protein interacting with NIMA-kinase) catalyzes the cis/trans isomerisation of Xaa-Pro peptide bonds of target proteins. | ||||||
Authors | Zhukov, I. / Jaremko, L. / Jaremko, M. / Mueller, J.W. / Bayer, P. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2011 Title: Structure and Dynamics of the First Archaeal Parvulin Reveal a New Functionally Important Loop in Parvulin-type Prolyl Isomerases Authors: Jaremko, L. / Jaremko, M. / Elfaki, I. / Mueller, J.W. / Ejchart, A. / Bayer, P. / Zhukov, I. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2rqs.cif.gz | 580.1 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2rqs.ent.gz | 486.5 KB | Display | PDB format |
PDBx/mmJSON format | 2rqs.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2rqs_validation.pdf.gz | 343.4 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 2rqs_full_validation.pdf.gz | 498.2 KB | Display | |
Data in XML | 2rqs_validation.xml.gz | 42.3 KB | Display | |
Data in CIF | 2rqs_validation.cif.gz | 67.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rq/2rqs ftp://data.pdbj.org/pub/pdb/validation_reports/rq/2rqs | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 10516.255 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Cenarchaeum symbiosum (archaea) / Gene: pinA / Production host: Escherichia coli (E. coli) / References: UniProt: O74049, peptidylprolyl isomerase |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR Details: Pin (protein interacting with NIMA-kinase) catalyzes the cis/trans isomerisation of Xaa-Pro peptide bonds of target proteins. | ||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details | Contents: 0.6mM [U-100% 13C; U-100% 15N] CsPin, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O |
---|---|
Sample | Conc.: 0.6 mM / Component: CsPin / Isotopic labeling: [U-100% 13C; U-100% 15N] |
Sample conditions | Ionic strength: 0.1 / pH: 7.5 / Pressure: ambient / Temperature: 289 K |
-NMR measurement
NMR spectrometer | Type: Varian Uniform NMR System / Manufacturer: Varian / Model: Uniform NMR System / Field strength: 800 MHz |
---|
-Processing
NMR software |
| ||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||
NMR constraints | NOE constraints total: 1585 / Hydrogen bond constraints total count: 76 | ||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 / Representative conformer: 1 |