+Open data
-Basic information
Entry | Database: PDB / ID: 2k8i | ||||||
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Title | Solution structure of E.Coli SlyD | ||||||
Components | Peptidyl-prolyl cis-trans isomeraseProlyl isomerase | ||||||
Keywords | ISOMERASE / PPIase / chaperone / Rotamase | ||||||
Function / homology | Function and homology information protein maturation by protein folding / cobalt ion binding / nickel cation binding / protein maturation / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / unfolded protein binding / response to heat / protein refolding / protein stabilization ...protein maturation by protein folding / cobalt ion binding / nickel cation binding / protein maturation / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / unfolded protein binding / response to heat / protein refolding / protein stabilization / copper ion binding / zinc ion binding / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / molecular dynamics | ||||||
Authors | Weininger, U. / Balbach, J. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2009 Title: NMR solution structure of SlyD from Escherichia coli: spatial separation of prolyl isomerase and chaperone function. Authors: Weininger, U. / Haupt, C. / Schweimer, K. / Graubner, W. / Kovermann, M. / Bruser, T. / Scholz, C. / Schaarschmidt, P. / Zoldak, G. / Schmid, F.X. / Balbach, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2k8i.cif.gz | 506.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2k8i.ent.gz | 422.9 KB | Display | PDB format |
PDBx/mmJSON format | 2k8i.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/k8/2k8i ftp://data.pdbj.org/pub/pdb/validation_reports/k8/2k8i | 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: 18848.682 Da / Num. of mol.: 1 / Fragment: residues 1-171 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Genus: slyD / Gene: slyD, Ecok1_33310, APECO1_3105 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 References: UniProt: A1AGN5, UniProt: P0A9K9*PLUS, peptidylprolyl 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 mM [U-13C; U-15N] protein, 90% H2O/10% D2O / Solvent system: 90% H2O/10% D2O |
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Sample | Conc.: 1 mM / Component: protein / Isotopic labeling: [U-13C; U-15N] |
Sample conditions | Ionic strength: 0.1 / pH: 7.4 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software | Name: CNS / Classification: refinement |
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Refinement | Method: molecular dynamics / Software ordinal: 1 |
NMR representative | Selection criteria: lowest energy |
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 10 / Representative conformer: 1 |