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Open data
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Basic information
| Entry | Database: PDB / ID: 5fo3 | ||||||
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| 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 informationdivision septum assembly / FtsZ-dependent cytokinesis / cell division site / regulation of cell division / identical protein binding / cytoplasm Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| 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: 2015Title: 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. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 5fo3.cif.gz | 149.1 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb5fo3.ent.gz | 121.1 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 | 439.2 KB | Display | wwPDB validaton report |
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| Full document | 5fo3_full_validation.pdf.gz | 448.2 KB | Display | |
| Data in XML | 5fo3_validation.xml.gz | 16.4 KB | Display | |
| Data in CIF | 5fo3_validation.cif.gz | 20.6 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 |
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Links
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Assembly
| Deposited unit | ![]()
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| Unit cell |
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| Noncrystallographic symmetry (NCS) | NCS oper:
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Components
| #1: Protein | Mass: 21080.717 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Has protein modification | Y | |
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-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION |
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Sample preparation
| Crystal | Density Matthews: 2.68 Å3/Da / Density % sol: 56.6 % / Description: NONE |
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-Data collection
| Diffraction | Mean temperature: 100 K |
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| 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 |
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Processing
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| Refinement | Method to determine structure: SADStarting 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.
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| 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
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| Refinement step | Cycle: LAST / Resolution: 2.9→50.01 Å
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| Refine LS restraints |
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