+Open data
-Basic information
Entry | Database: PDB / ID: 4v02 | ||||||
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Title | MinC:MinD cell division protein complex, Aquifex aeolicus | ||||||
Components |
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Keywords | CELL CYCLE / BACTERIAL CELL DIVISION / FTSZ / MIN SYSTEM | ||||||
Function / homology | Function and homology information regulation of cell septum assembly / negative regulation of cell division / division septum assembly / cell morphogenesis / cytoplasmic side of plasma membrane / ATP hydrolysis activity / ATP binding / cytosol Similarity search - Function | ||||||
Biological species | AQUIFEX AEOLICUS (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å | ||||||
Authors | Ghosal, D. / Lowe, J. | ||||||
Citation | Journal: Nat.Commun. / Year: 2014 Title: Mincd Cell Division Proteins Form Alternating Copolymeric Cytomotive Filaments. Authors: Ghosal, D. / Trambaiolo, D. / Amos, L.A. / Lowe, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4v02.cif.gz | 146.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4v02.ent.gz | 121.9 KB | Display | PDB format |
PDBx/mmJSON format | 4v02.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v0/4v02 ftp://data.pdbj.org/pub/pdb/validation_reports/v0/4v02 | 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: 28697.398 Da / Num. of mol.: 2 Fragment: C-TERMINAL AMPHIPATHIC HELIX REMOVED, UNP RESDIUES 1-250 Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) AQUIFEX AEOLICUS (bacteria) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: O67033 #2: Protein | Mass: 14075.339 Da / Num. of mol.: 2 / Fragment: C-TERMINAL DOMAIN, UNP RESIDUES 82-201 Source method: isolated from a genetically manipulated source Source: (gene. exp.) AQUIFEX AEOLICUS (bacteria) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: O67034 #3: Chemical | #4: Chemical | Sequence details | AMPHIPATHI | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 4.3 Å3/Da / Density % sol: 71 % / Description: NONE |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.9795 |
Detector | Type: ADSC CCD / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→50 Å / Num. obs: 42285 / % possible obs: 100 % / Observed criterion σ(I): 0 / Redundancy: 14.3 % / Biso Wilson estimate: 52.22 Å2 / Rmerge(I) obs: 0.1 / Net I/σ(I): 20.6 |
Reflection shell | Resolution: 2.7→2.85 Å / Redundancy: 12.9 % / Rmerge(I) obs: 0.63 / Mean I/σ(I) obs: 4.6 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.7→49.171 Å / SU ML: 0.33 / σ(F): 1.4 / Phase error: 23.16 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.7→49.171 Å
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Refine LS restraints |
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LS refinement shell |
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