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Yorodumi- PDB-1f47: THE BACTERIAL CELL-DIVISION PROTEIN ZIPA AND ITS INTERACTION WITH... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1f47 | ||||||
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Title | THE BACTERIAL CELL-DIVISION PROTEIN ZIPA AND ITS INTERACTION WITH AN FTSZ FRAGMENT REVEALED BY X-RAY CRYSTALLOGRAPHY | ||||||
Components |
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Keywords | CELL CYCLE / cell division zipa / CELL DIVISiON ftsz / SEPARATION / INNER MEMBRANE / TRANSMEMBRANE | ||||||
Function / homology | Function and homology information divisome complex / chloroplast fission / FtsZ-dependent cytokinesis / division septum assembly / cell division site / protein polymerization / cell division / GTPase activity / GTP binding / protein homodimerization activity ...divisome complex / chloroplast fission / FtsZ-dependent cytokinesis / division septum assembly / cell division site / protein polymerization / cell division / GTPase activity / GTP binding / protein homodimerization activity / identical protein binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.95 Å | ||||||
Authors | Mosyak, L. / Zhang, Y. / Glasfeld, E. / Stahl, M. / Somers, W.S. | ||||||
Citation | Journal: EMBO J. / Year: 2000 Title: The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography. Authors: Mosyak, L. / Zhang, Y. / Glasfeld, E. / Haney, S. / Stahl, M. / Seehra, J. / Somers, W.S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1f47.cif.gz | 47.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1f47.ent.gz | 33.8 KB | Display | PDB format |
PDBx/mmJSON format | 1f47.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/f4/1f47 ftp://data.pdbj.org/pub/pdb/validation_reports/f4/1f47 | HTTPS FTP |
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-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: 16134.484 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli) / References: UniProt: P77173 |
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#2: Protein/peptide | Mass: 2022.281 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli) / References: UniProt: P0A9A6 |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.07 Å3/Da / Density % sol: 40.57 % | ||||||||||||||||||||
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 9 Details: 30% PEG 6000, 100 mM Bicine, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 18K | ||||||||||||||||||||
Crystal grow | *PLUS pH: 6 | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 |
Detector | Type: RIGAKU RAXIS / Detector: IMAGE PLATE / Date: Dec 12, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.95→25 Å / Num. all: 10556 / Num. obs: 10556 / % possible obs: 95.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.92 % / Biso Wilson estimate: 30 Å2 / Rmerge(I) obs: 0.055 / Net I/σ(I): 26.9 |
Reflection shell | Resolution: 1.95→2.02 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.146 / % possible all: 88.6 |
Reflection | *PLUS |
Reflection shell | *PLUS % possible obs: 88.6 % / Mean I/σ(I) obs: 8.6 |
-Processing
Software |
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Refinement | Resolution: 1.95→25 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.95→25 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Classification: refinement | ||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 25 Å / σ(F): 0 / % reflection Rfree: 5 % | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS |