[English] 日本語
Yorodumi- PDB-2pv2: Crystallographic Structure of SurA first peptidyl-prolyl isomeras... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2pv2 | ||||||
---|---|---|---|---|---|---|---|
Title | Crystallographic Structure of SurA first peptidyl-prolyl isomerase domain complexed with peptide NFTLKFWDIFRK | ||||||
Components |
| ||||||
Keywords | ISOMERASE / Survival protein A / Peptidyl-prolyl cis-trans isomerase domain | ||||||
Function / homology | Function and homology information maintenance of stationary phase / maintenance of unfolded protein / Gram-negative-bacterium-type cell outer membrane assembly / chaperone-mediated protein folding / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / peptide binding / unfolded protein binding / protein folding / outer membrane-bounded periplasmic space / protein stabilization Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.3 Å | ||||||
Authors | Xu, X. / McKay, D.B. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2007 Title: The Periplasmic Bacterial Molecular Chaperone SurA Adapts its Structure to Bind Peptides in Different Conformations to Assert a Sequence Preference for Aromatic Residues. Authors: Xu, X. / Wang, S. / Hu, Y.X. / McKay, D.B. #1: Journal: Structure / Year: 2002 Title: Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins Authors: Bitto, E. / McKay, D.B. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2pv2.cif.gz | 100.3 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2pv2.ent.gz | 77.2 KB | Display | PDB format |
PDBx/mmJSON format | 2pv2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2pv2_validation.pdf.gz | 462.3 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 2pv2_full_validation.pdf.gz | 468.4 KB | Display | |
Data in XML | 2pv2_validation.xml.gz | 22.2 KB | Display | |
Data in CIF | 2pv2_validation.cif.gz | 32.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pv/2pv2 ftp://data.pdbj.org/pub/pdb/validation_reports/pv/2pv2 | HTTPS FTP |
-Related structure data
Related structure data | 2pv1C 2pv3C 1m5yS S: Starting model for refinement C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
2 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 10977.320 Da / Num. of mol.: 4 / Fragment: PPIC 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K-12 EMG2 / Gene: surA / Plasmid: pTYB1 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P0ABZ6, peptidylprolyl isomerase #2: Protein/peptide | Mass: 1617.910 Da / Num. of mol.: 2 / Source method: obtained synthetically #3: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.09 Å3/Da / Density % sol: 41.08 % |
---|---|
Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8 Details: 24% ployethylene glycol 8000, 0.1 M imdidazole, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL11-1 / Wavelength: 1 Å |
Detector | Type: MARMOSAIC 325 mm CCD / Detector: CCD / Date: Dec 20, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.3→50 Å / Num. obs: 93257 / % possible obs: 96.2 % / Redundancy: 2.5 % / Rsym value: 0.045 / Χ2: 3.377 / Net I/σ(I): 26.5 |
Reflection shell | Resolution: 1.3→1.35 Å / Redundancy: 2.2 % / Num. unique all: 8714 / Rsym value: 0.25 / Χ2: 2.093 / % possible all: 90.2 |
-Processing
Software |
| ||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1M5Y Resolution: 1.3→28.2 Å / Cross valid method: THROUGHOUT / σ(F): 0
| ||||||||||||||||||||||||||||
Solvent computation | Bsol: 48.339 Å2 | ||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 17.97 Å2
| ||||||||||||||||||||||||||||
Refine analyze |
| ||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.3→28.2 Å
| ||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||
LS refinement shell | Resolution: 1.3→1.38 Å / Rfactor Rfree error: 0.008
| ||||||||||||||||||||||||||||
Xplor file |
|