+Open data
-Basic information
Entry | Database: PDB / ID: 1e4g | ||||||
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Title | FtsA (ATP-bound form) from Thermotoga maritima | ||||||
Components | CELL DIVISION PROTEIN FTSA | ||||||
Keywords | BACTERIAL CELL DIVISION / ACTIN FAMILY | ||||||
Function / homology | Function and homology information FtsZ-dependent cytokinesis / cell division site / cytoplasmic side of plasma membrane / cell division / ATP binding / identical protein binding Similarity search - Function | ||||||
Biological species | THERMOTOGA MARITIMA (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.6 Å | ||||||
Authors | van den Ent, F. / Lowe, J. | ||||||
Citation | Journal: Embo J. / Year: 2000 Title: Crystal Structure of the Cell Division Protein Ftsa from Thermotoga Maritima Authors: van den Ent, F. / Lowe, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1e4g.cif.gz | 85.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1e4g.ent.gz | 68.8 KB | Display | PDB format |
PDBx/mmJSON format | 1e4g.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/e4/1e4g ftp://data.pdbj.org/pub/pdb/validation_reports/e4/1e4g | 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: 47404.000 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) THERMOTOGA MARITIMA (bacteria) / Gene: FTSA / Plasmid: PHIS17 / Production host: ESCHERICHIA COLI BL21(DE3) (bacteria) / Variant (production host): C41 / References: UniProt: Q9WZU0 |
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#2: Chemical | ChemComp-ATP / |
#3: Chemical | ChemComp-MG / |
#4: 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: 2.05 Å3/Da / Density % sol: 42 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 5.5 Details: 200 MM AMMONIUM ACETATE, 100 MM NA ACETATE PH 5.5, 15% PEG | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 18 ℃ / 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, 0.9787, 0.9791 | ||||||||||||
Detector | Date: Feb 15, 2000 | ||||||||||||
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||
Radiation wavelength |
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Reflection | Resolution: 2.6→30 Å / Num. obs: 11678 / % possible obs: 97.9 % / Redundancy: 6.2 % / Biso Wilson estimate: 55.8 Å2 / Rmerge(I) obs: 0.066 / Net I/σ(I): 18.1 | ||||||||||||
Reflection shell | Resolution: 2.6→2.74 Å / Redundancy: 5.8 % / Rmerge(I) obs: 0.235 / Mean I/σ(I) obs: 5.9 / % possible all: 98.1 | ||||||||||||
Reflection shell | *PLUS % possible obs: 98.1 % |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 2.6→30 Å / Data cutoff high absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: A POSTERIORI / σ(F): 0
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Solvent computation | Solvent model: FLAT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 43.27 Å2
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Refinement step | Cycle: LAST / Resolution: 2.6→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.6→2.68 Å / Total num. of bins used: 11
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