+Open data
-Basic information
Entry | Database: PDB / ID: 2vam | ||||||
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Title | FtsZ B. subtilis | ||||||
Components | CELL DIVISION PROTEIN FTSZ | ||||||
Keywords | CELL CYCLE / BACTERIAL CELL DIVISION PROTEIN / TUBULIN HOMOLOG / NUCLEOTIDE-BINDING / GTPASE / SEPTATION / CYTOPLASM / GTP-BINDING / CELL DIVISION / POLYMERIZATION | ||||||
Function / homology | Function and homology information chloroplast fission / cell septum / FtsZ-dependent cytokinesis / division septum assembly / cell division site / protein polymerization / cell division / GTPase activity / GTP binding / identical protein binding / cytoplasm Similarity search - Function | ||||||
Biological species | BACILLUS SUBTILIS (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å | ||||||
Authors | Oliva, M.A. / Lowe, J. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2007 Title: Structural Insights Into the Conformational Variability of Ftsz Authors: Oliva, M.A. / Trambaiolo, D. / Lowe, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2vam.cif.gz | 69.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2vam.ent.gz | 50.9 KB | Display | PDB format |
PDBx/mmJSON format | 2vam.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2vam_validation.pdf.gz | 427.3 KB | Display | wwPDB validaton report |
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Data in XML | 2vam_validation.xml.gz | 13.4 KB | Display | |
Data in CIF | 2vam_validation.cif.gz | 18.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/va/2vam ftp://data.pdbj.org/pub/pdb/validation_reports/va/2vam | HTTPS FTP |
-Related structure data
Related structure data | 2r6rC 2vapC 2vawC 1fszS S: Starting model for refinement C: citing same article (ref.) |
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Similar 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: 40395.660 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) BACILLUS SUBTILIS (bacteria) / Plasmid: PHIS17 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 AI (DE3) / References: UniProt: P17865 |
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#2: Chemical | ChemComp-SO4 / |
#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: 2.4 Å3/Da / Density % sol: 49.1 % / Description: NONE |
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Crystal grow | pH: 9 Details: 0.1M TRIS-HCL, PH9.0, 18.857% PEG 3000, 0.24M LI2SO4 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.9393 |
Detector | Type: ADSC CCD / Detector: CCD / Date: Mar 28, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9393 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→7.91 Å / Num. obs: 13740 / % possible obs: 99.9 % / Observed criterion σ(I): 0 / Redundancy: 7.1 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 16.9 |
Reflection shell | Resolution: 2.5→2.64 Å / Redundancy: 7.2 % / Rmerge(I) obs: 0.35 / Mean I/σ(I) obs: 4.9 / % possible all: 99.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1FSZ Resolution: 2.5→75.81 Å / Cor.coef. Fo:Fc: 0.934 / Cor.coef. Fo:Fc free: 0.894 / SU B: 9.163 / SU ML: 0.208 / Cross valid method: THROUGHOUT / ESU R: 0.407 / ESU R Free: 0.287 / 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: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 40.2 Å2
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Refinement step | Cycle: LAST / Resolution: 2.5→75.81 Å
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Refine LS restraints |
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