+Open data
-Basic information
Entry | Database: PDB / ID: 1jce | ||||||
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Title | MREB FROM THERMOTOGA MARITIMA | ||||||
Components | ROD SHAPE-DETERMINING PROTEIN MREB | ||||||
Keywords | STRUCTURAL PROTEIN / rod-shape determining / MreB / Mbl / actin / hsp-70 / ftsz | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Thermotoga maritima (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.1 Å | ||||||
Authors | van den Ent, F. / Amos, L.A. / Lowe, J. | ||||||
Citation | Journal: Nature / Year: 2001 Title: Prokaryotic origin of the actin cytoskeleton. Authors: van den Ent, F. / 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 | 1jce.cif.gz | 75.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1jce.ent.gz | 60.1 KB | Display | PDB format |
PDBx/mmJSON format | 1jce.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1jce_validation.pdf.gz | 427.5 KB | Display | wwPDB validaton report |
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Full document | 1jce_full_validation.pdf.gz | 431.9 KB | Display | |
Data in XML | 1jce_validation.xml.gz | 16.6 KB | Display | |
Data in CIF | 1jce_validation.cif.gz | 24.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jc/1jce ftp://data.pdbj.org/pub/pdb/validation_reports/jc/1jce | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | Crystal symmetry generates one-dimensional filaments. These filaments are similar to one of the strands of F-actin (protofilament) |
-Components
#1: Protein | Mass: 37174.738 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermotoga maritima (bacteria) / Gene: TM0588 / Plasmid: PHIS17 / Production host: Escherichia coli (E. coli) / Strain (production host): C41 / References: UniProt: Q9WZ57 |
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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: 2.81 Å3/Da / Density % sol: 56.24 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 19 ℃ / 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: 0.9780, 0.9802, 0.9394 | ||||||||||||
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: May 8, 2001 | ||||||||||||
Radiation | Monochromator: double / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||
Radiation wavelength |
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Reflection | Resolution: 2.1→50 Å / Num. all: 24183 / Num. obs: 22453 / % possible obs: 93.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 1.8 % / Biso Wilson estimate: 23.8 Å2 / Rmerge(I) obs: 0.063 / Net I/σ(I): 11.7 | ||||||||||||
Reflection shell | Resolution: 2.1→2.21 Å / Redundancy: 1.7 % / Rmerge(I) obs: 0.239 / % possible all: 67.5 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 2.1→50 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: CNS 1.0, protein_rep.param
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Displacement parameters | Biso mean: 28.6 Å2 | |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→50 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.1 Å / Lowest resolution: 50 Å / σ(F): 0 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 28.6 Å2 |