+Open data
-Basic information
Entry | Database: PDB / ID: 5fo3 | ||||||
---|---|---|---|---|---|---|---|
Title | ZapC cell division regulator from E. coli | ||||||
Components | CELL DIVISION PROTEIN ZAPC | ||||||
Keywords | CELL CYCLE / FTSZ / BACTERIAL CELL DIVISION / Z-RING ASSOCIATED PROTEIN C | ||||||
Function / homology | Function and homology information : / FtsZ-dependent cytokinesis / division septum assembly / cell division site / regulation of cell division / identical protein binding / cytoplasm Similarity search - Function | ||||||
Biological species | ESCHERICHIA COLI (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.9 Å | ||||||
Authors | Ortiz, C. / Kureisaite-Ciziene, D. / Schmitz, F. / Vicente, M. / Lowe, J. | ||||||
Citation | Journal: FEBS Lett. / Year: 2015 Title: Crystal Structure of the Z-Ring Associated Cell Division Protein Zapc from Escherichia Coli. Authors: Ortiz, C. / Kureisaite-Ciziene, D. / Schmitz, F. / Mclaughlin, S.H. / Vicente, M. / Lowe, J. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 5fo3.cif.gz | 145 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb5fo3.ent.gz | 123.8 KB | Display | PDB format |
PDBx/mmJSON format | 5fo3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5fo3_validation.pdf.gz | 437.9 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 5fo3_full_validation.pdf.gz | 447.3 KB | Display | |
Data in XML | 5fo3_validation.xml.gz | 14.9 KB | Display | |
Data in CIF | 5fo3_validation.cif.gz | 19.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fo/5fo3 ftp://data.pdbj.org/pub/pdb/validation_reports/fo/5fo3 | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-Links
-Assembly
Deposited unit |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||||||
Unit cell |
| ||||||||||||
Noncrystallographic symmetry (NCS) | NCS oper:
|
-Components
#1: Protein | Mass: 21080.717 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P75862 |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
---|
-Sample preparation
Crystal | Density Matthews: 2.68 Å3/Da / Density % sol: 56.6 % / Description: NONE |
---|
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I24 / Wavelength: 0.97858 |
Detector | Type: DECTRIS PILATUS / Detector: PIXEL / Date: Apr 12, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97858 Å / Relative weight: 1 |
Reflection | Resolution: 2.9→50 Å / Num. obs: 10807 / % possible obs: 100 % / Observed criterion σ(I): 0 / Redundancy: 41.8 % / Rmerge(I) obs: 0.3 / Net I/σ(I): 17 |
Reflection shell | Resolution: 2.9→3.06 Å / Redundancy: 40.7 % / Rmerge(I) obs: 1.5 / Mean I/σ(I) obs: 3.9 / % possible all: 100 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: SAD Starting model: NONE Resolution: 2.9→50.01 Å / Cor.coef. Fo:Fc: 0.912 / Cor.coef. Fo:Fc free: 0.893 / SU B: 33.423 / SU ML: 0.256 / Cross valid method: THROUGHOUT / ESU R Free: 0.377 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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 mean: 50.974 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.9→50.01 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|