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- PDB-1fc3: THE CRYSTAL STRUCTURE OF TRANS-ACTIVATION DOMAIN OF THE SPORULATI... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1fc3 | ||||||
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Title | THE CRYSTAL STRUCTURE OF TRANS-ACTIVATION DOMAIN OF THE SPORULATION RESPONSE REGULATOR, SPO0A | ||||||
![]() | SPO0A | ||||||
![]() | SIGNALING PROTEIN / RESPONSE REGULATOR | ||||||
Function / homology | ![]() detection of stimulus / regulation of sporulation resulting in formation of a cellular spore / phosphorelay response regulator activity / sporulation resulting in formation of a cellular spore / DNA-binding transcription factor activity / calcium ion binding / DNA binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Lewis, R.J. / Krzywda, S. / Wilkinson, A.J. | ||||||
![]() | ![]() Title: The trans-activation domain of the sporulation response regulator Spo0A revealed by X-ray crystallography. Authors: Lewis, R.J. / Krzywda, S. / Brannigan, J.A. / Turkenburg, J.P. / Muchova, K. / Dodson, E.J. / Barak, I. / Wilkinson, A.J. #1: ![]() Title: Domain-Swapping in the Sporulation Response Regulator Spo0A Authors: Lewis, R.J. / Muchova, K. / Brannigan, J.A. / Barak, I. / Leonard, G. / Wilkinson, A.J. #2: ![]() Title: Phosphorylated Aspartate in the Structure of a Response Regulator Protein Authors: Lewis, R.J. / Brannigan, J.A. / Muchova, K. / Barak, I. / Wilkinson, A.J. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 83.1 KB | Display | ![]() |
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PDB format | ![]() | 63.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 441 KB | Display | ![]() |
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Full document | ![]() | 452.5 KB | Display | |
Data in XML | ![]() | 19.4 KB | Display | |
Data in CIF | ![]() | 27.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 13374.438 Da / Num. of mol.: 3 / Fragment: C-TERMINAL DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Plasmid: PET / Species (production host): Escherichia coli / Production host: ![]() ![]() #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.63 Å3/Da / Density % sol: 52.91 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 Details: 0.1 M HEPES pH 7.5, 20% w/v PEG 10K, 0.1 M MALTOSE, 10 mM BME | ||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS Density % sol: 53.4 % | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 289 K / Method: vapor diffusion, hanging drop / Details: Muchova, K., (1999) Acta Crystallogr., D55, 671. | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Dec 10, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 2→20 Å / Num. obs: 27976 / % possible obs: 87.6 % / Redundancy: 7.27 % / Biso Wilson estimate: 29.38 Å2 / Rsym value: 0.06 / Net I/σ(I): 19.41 |
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 1.31 % / Mean I/σ(I) obs: 3.23 / Rsym value: 0.313 / % possible all: 55.6 |
Reflection | *PLUS Redundancy: 3.6 % / Rmerge(I) obs: 0.06 |
Reflection shell | *PLUS % possible obs: 55.6 % / Rmerge(I) obs: 0.313 |
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Processing
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Refinement | Method to determine structure: ![]()
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Displacement parameters | Biso mean: 31.3 Å2
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Refinement step | Cycle: LAST / Resolution: 2→20 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2 Å / Lowest resolution: 20 Å / σ(F): 0 / % reflection Rfree: 5 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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