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Yorodumi- PDB-2eyu: The Crystal Structure of the C-terminal Domain of Aquifex aeolicu... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2eyu | ||||||
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Title | The Crystal Structure of the C-terminal Domain of Aquifex aeolicus PilT | ||||||
Components | twitching motility protein PilT | ||||||
Keywords | PROTEIN TRANSPORT / Pilus Retraction Motor / C-terminal Domain PilT | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Aquifex aeolicus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / AB INITIO / Resolution: 1.87 Å | ||||||
Authors | Satyshur, K.A. / Worzalla, G.A. / Meyer, L.S. / Heiniger, E.K. / Aukema, K.G. / Forest, K.T. | ||||||
Citation | Journal: Structure / Year: 2007 Title: Crystal structures of the pilus retraction motor PilT suggest large domain movements and subunit cooperation drive motility. Authors: Satyshur, K.A. / Worzalla, G.A. / Meyer, L.S. / Heiniger, E.K. / Aukema, K.G. / Misic, A.M. / Forest, K.T. #1: Journal: Acta Crystallogr.,Sect.D / Year: 2004 Title: The pilus-retraction protein PilT: ultrastructure of the biological assembly Authors: Forest, K.T. / Satyshur, K.A. / Worzalla, G.A. / Hansen, J.K. / Herdendorf, T.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2eyu.cif.gz | 105.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2eyu.ent.gz | 86.3 KB | Display | PDB format |
PDBx/mmJSON format | 2eyu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2eyu_validation.pdf.gz | 455.9 KB | Display | wwPDB validaton report |
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Full document | 2eyu_full_validation.pdf.gz | 489.3 KB | Display | |
Data in XML | 2eyu_validation.xml.gz | 22.7 KB | Display | |
Data in CIF | 2eyu_validation.cif.gz | 30.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ey/2eyu ftp://data.pdbj.org/pub/pdb/validation_reports/ey/2eyu | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 29873.084 Da / Num. of mol.: 2 / Fragment: PilT C-terminal Domain / Mutation: Glu294Gly Source method: isolated from a genetically manipulated source Source: (gene. exp.) Aquifex aeolicus (bacteria) / Plasmid: pET-23a / Production host: Escherichia coli (E. coli) / References: GenBank: 15606134, UniProt: O66950*PLUS #2: Chemical | ChemComp-SO4 / | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.17 Å3/Da / Density % sol: 47.59 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 10 mg/ml protein 0.1 M Mes 10% Dioxane 1.6 M ammonium sulfate , pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 32-ID / Wavelength: 0.97934 Å |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Dec 11, 2004 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97934 Å / Relative weight: 1 |
Reflection | Resolution: 1.86→40 Å / Num. all: 45173 / Num. obs: 44351 / % possible obs: 96.8 % / Observed criterion σ(F): 4 / Observed criterion σ(I): 2 / Redundancy: 12 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 49.9 |
Reflection shell | Resolution: 1.86→1.94 Å / Redundancy: 6.9 % / Rmerge(I) obs: 0.197 / Mean I/σ(I) obs: 7.8 / % possible all: 83.9 |
-Processing
Software |
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Refinement | Method to determine structure: AB INITIO / Resolution: 1.87→20 Å / Num. parameters: 15692 / Num. restraintsaints: 16007 / Cross valid method: FREE R / σ(F): 4 / Stereochemistry target values: ENGH AND HUBER Details: Crystal is twinned, with BASF refined to 0.535 in ShelX h,-k,-l
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Displacement parameters | Biso mean: 35.3 Å2 | |||||||||||||||||||||||||||||||||
Refine analyze | Num. disordered residues: 0 / Occupancy sum hydrogen: 0 / Occupancy sum non hydrogen: 3922 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.87→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.87→1.871 Å /
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