+Open data
-Basic information
Entry | Database: PDB / ID: 2xj4 | ||||||
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Title | Structure of the bacterial cell division regulator protein MipZ | ||||||
Components | MIPZ | ||||||
Keywords | REPLICATION / CELL DIVISION / ATPASE / WACA | ||||||
Function / homology | Function and homology information ATPase MipZ / ATPase MipZ / : / P-loop containing nucleotide triphosphate hydrolases / Rossmann fold / P-loop containing nucleoside triphosphate hydrolase / 3-Layer(aba) Sandwich / Alpha Beta Similarity search - Domain/homology | ||||||
Biological species | CAULOBACTER CRESCENTUS (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.6 Å | ||||||
Authors | Michie, K.A. / Lowe, J. | ||||||
Citation | Journal: Mol.Cell / Year: 2012 Title: Localized Dimerization and Nucleoid Binding Drive Gradient Formation by the Bacterial Cell Division Inhibitor Mipz. Authors: Kiekebusch, D. / Michie, K.A. / Essen, L.O. / Lowe, J. / Thanbichler, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2xj4.cif.gz | 132 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2xj4.ent.gz | 104.4 KB | Display | PDB format |
PDBx/mmJSON format | 2xj4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2xj4_validation.pdf.gz | 435.2 KB | Display | wwPDB validaton report |
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Full document | 2xj4_full_validation.pdf.gz | 444.3 KB | Display | |
Data in XML | 2xj4_validation.xml.gz | 17.2 KB | Display | |
Data in CIF | 2xj4_validation.cif.gz | 25.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xj/2xj4 ftp://data.pdbj.org/pub/pdb/validation_reports/xj/2xj4 | 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 on special symmetry positions |
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-Components
#1: Protein | Mass: 31763.359 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) CAULOBACTER CRESCENTUS (bacteria) / Strain: CB15N / Description: PCR OF GENOMIC DNA SUPPLIED BY ATCC (19089D) / Plasmid: PHIS17 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / Variant (production host): AI / References: UniProt: B8GY04, UniProt: A0A0H3CA70*PLUS |
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#2: 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: 2.5 Å3/Da / Density % sol: 50.7 % / Description: NONE |
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Crystal grow | pH: 6.5 / Details: 0.1 M MES/NAOH PH6.5, 30% V/V PEG400 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.9747 |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Jun 16, 2007 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9747 Å / Relative weight: 1 |
Reflection | Resolution: 1.5→20.69 Å / Num. obs: 40200 / % possible obs: 99.6 % / Observed criterion σ(I): 0 / Redundancy: 5.4 % / Biso Wilson estimate: 18.813 Å2 / Rmerge(I) obs: 0.09 / Net I/σ(I): 11.6 |
Reflection shell | Resolution: 1.6→1.69 Å / Redundancy: 5.5 % / Rmerge(I) obs: 0.29 / Mean I/σ(I) obs: 5.1 / % possible all: 100 |
-Processing
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Refinement | Method to determine structure: SAD Starting model: NONE Resolution: 1.6→61.31 Å / Cor.coef. Fo:Fc: 0.976 / Cor.coef. Fo:Fc free: 0.962 / SU B: 2.612 / SU ML: 0.042 / Cross valid method: THROUGHOUT / ESU R: 0.08 / ESU R Free: 0.072 / 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: 23.685 Å2
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Refinement step | Cycle: LAST / Resolution: 1.6→61.31 Å
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Refine LS restraints |
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