+Open data
-Basic information
Entry | Database: PDB / ID: 5jfz | ||||||
---|---|---|---|---|---|---|---|
Title | E. coli EcFicT in complex with EcFicA mutant E28G | ||||||
Components |
| ||||||
Keywords | TRANSFERASE / FIC domain / fic-1 / Class I Fic protein | ||||||
Function / homology | Function and homology information protein adenylyltransferase / regulation of cell division / nucleotidyltransferase activity / ATP binding Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) Escherichia coli K-12 (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.4 Å | ||||||
Authors | Stanger, F.V. / Schirmer, T. | ||||||
Citation | Journal: Plos One / Year: 2016 Title: Crystal Structure of the Escherichia coli Fic Toxin-Like Protein in Complex with Its Cognate Antitoxin. Authors: Stanger, F.V. / Harms, A. / Dehio, C. / Schirmer, T. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 5jfz.cif.gz | 149.2 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb5jfz.ent.gz | 116 KB | Display | PDB format |
PDBx/mmJSON format | 5jfz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jf/5jfz ftp://data.pdbj.org/pub/pdb/validation_reports/jf/5jfz | HTTPS FTP |
---|
-Related structure data
Related structure data | 5jffC 5fjjS S: Starting model for refinement C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
2 |
| ||||||||
3 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 25627.748 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Gene: fic, b3361, JW3324 / Plasmid: pRSFDuet1 / Production host: Escherichia coli BL21(DE3) (bacteria) References: UniProt: P20605, Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases #2: Protein | Mass: 7936.075 Da / Num. of mol.: 3 / Mutation: E28G Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli K-12 (bacteria) / Gene: yhfG, b3362, JW3325 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P0ADX5 #3: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 50.9 % / Mosaicity: 0.25 ° |
---|---|
Crystal grow | Temperature: 293.15 K / Method: vapor diffusion, sitting drop / pH: 6 Details: 19% PEG 1500 (w/v), 0.1 M MMT (malic acid, MES, Tris) buffer pH 6.0 |
-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1 Å | ||||||||||||||||||||||||||||||
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Oct 31, 2012 | ||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||
Reflection | Resolution: 2.4→80.41 Å / Num. obs: 30850 / % possible obs: 98.6 % / Redundancy: 6.2 % / CC1/2: 0.992 / Rmerge(I) obs: 0.176 / Rpim(I) all: 0.076 / Rrim(I) all: 0.193 / Net I/σ(I): 7.2 / Num. measured all: 192193 | ||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1 / Rejects: _
|
-Phasing
Phasing | Method: molecular replacement | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Phasing MR | Model details: Phaser MODE: MR_AUTO
|
-Processing
Software |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 5fjj Resolution: 2.4→80.41 Å / Cor.coef. Fo:Fc: 0.921 / Cor.coef. Fo:Fc free: 0.886 / SU B: 10.147 / SU ML: 0.234 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.484 / ESU R Free: 0.292 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 104.93 Å2 / Biso mean: 32.801 Å2 / Biso min: 12.84 Å2
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.4→80.41 Å
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.398→2.46 Å / Total num. of bins used: 20
|