+Open data
-Basic information
Entry | Database: PDB / ID: 1ofu | ||||||
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Title | Crystal structure of SulA:FtsZ from Pseudomonas aeruginosa | ||||||
Components |
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Keywords | BACTERIAL CELL DIVISION INHIBITOR / FTSZ / SULA PROTEIN | ||||||
Function / homology | Function and homology information chloroplast fission / negative regulation of cell division / FtsZ-dependent cytokinesis / division septum assembly / cell division site / SOS response / protein polymerization / cell division / GTPase activity / GTP binding / cytoplasm Similarity search - Function | ||||||
Biological species | PSEUDOMONAS AERUGINOSA (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å | ||||||
Authors | Cordell, S.C. / Robinson, E.J.H. / Lowe, J. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2003 Title: Crystal Structure of the SOS Cell Division Inhibitor Sula and in Complex with Ftsz Authors: Cordell, S.C. / Robinson, E.J.H. / Lowe, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ofu.cif.gz | 175.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ofu.ent.gz | 140.2 KB | Display | PDB format |
PDBx/mmJSON format | 1ofu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ofu_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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Full document | 1ofu_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | 1ofu_validation.xml.gz | 38.9 KB | Display | |
Data in CIF | 1ofu_validation.cif.gz | 54.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/of/1ofu ftp://data.pdbj.org/pub/pdb/validation_reports/of/1ofu | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 33146.961 Da / Num. of mol.: 2 / Fragment: RESIDUES 1-320 Source method: isolated from a genetically manipulated source Details: LAST 75 RESIDUES REMOVED FROM C-TERMINUS / Source: (gene. exp.) PSEUDOMONAS AERUGINOSA (bacteria) / Plasmid: PHIS17 / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P47204 #2: Protein | Mass: 13023.056 Da / Num. of mol.: 2 / Fragment: RESIDUES 43-161 Source method: isolated from a genetically manipulated source Details: FIRST 42 RESIDUES REMOVED FROM N-TERMINUS / Source: (gene. exp.) PSEUDOMONAS AERUGINOSA (bacteria) / Plasmid: PHIS17 / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q9HZJ8 #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.74 Å3/Da / Density % sol: 55.04 % | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 5.6 / Details: pH 5.60 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 19 ℃ / pH: 7.5 / Method: vapor diffusion, sitting drop | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.9393 |
Detector | Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9393 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→50 Å / Num. obs: 60044 / % possible obs: 99.7 % / Redundancy: 3.7 % / Biso Wilson estimate: 34.8 Å2 / Rmerge(I) obs: 0.096 / Net I/σ(I): 11.4 |
Reflection shell | Resolution: 2.1→2.21 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.334 / Mean I/σ(I) obs: 3.7 / % possible all: 99.7 |
Reflection | *PLUS Highest resolution: 2.1 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.096 |
Reflection shell | *PLUS % possible obs: 99.7 % / Rmerge(I) obs: 0.334 / Mean I/σ(I) obs: 3.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: MAD MODEL FROM C2 CRYSTAL FORM Resolution: 2.1→50 Å / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 43.7 Å2
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Refinement step | Cycle: LAST / Resolution: 2.1→50 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: RESTRAINTS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.1→2.11 Å / Total num. of bins used: 50
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Refinement | *PLUS Rfactor Rfree: 0.255 / Rfactor Rwork: 0.216 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | *PLUS Rfactor Rfree: 0.405 / Rfactor Rwork: 0.354 |