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Open data
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Basic information
Entry | Database: PDB / ID: 2xsk | ||||||
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Title | E. coli curli protein CsgC - SeCys | ||||||
![]() | CSGC | ||||||
![]() | CHAPERONE | ||||||
Function / homology | Curli production protein CsgC / Thin aggregative fimbriae synthesis protein / Immunoglobulin-like - #2420 / periplasmic space / Immunoglobulin-like / Sandwich / Mainly Beta / ACETATE ION / Curli assembly protein![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Salgado, P.S. / Taylor, J.D. / Cota, E. / Matthews, S.J. | ||||||
![]() | ![]() Title: Extending the Usability of the Phasing Power of Diselenide Bonds: Secys Sad Phasing of Csgc Using a Non-Auxotrophic Strain. Authors: Salgado, P.S. / Taylor, J.D. / Cota, E. / Matthews, S.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 28 KB | Display | ![]() |
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PDB format | ![]() | 21.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 406.3 KB | Display | ![]() |
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Full document | ![]() | 406.4 KB | Display | |
Data in XML | ![]() | 3.9 KB | Display | |
Data in CIF | ![]() | 5.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 12400.276 Da / Num. of mol.: 1 / Fragment: RESIDUES 11-110 Source method: isolated from a genetically manipulated source Details: CYSTEINE 29 AND 31 SUBSTITUTED FOR SELENOCYSTEINE AND DISELENIDE BOND BETWEEN SECYS 29 AND SECYS31 Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.06 Å3/Da / Density % sol: 40.16 % / Description: SE SAD USING SELENOCYSTEINE |
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Crystal grow | pH: 4.6 / Details: pH 4.6 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Jul 17, 2009 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→32.2 Å / Num. obs: 11136 / % possible obs: 98.8 % / Observed criterion σ(I): 2.6 / Redundancy: 3 % / Rmerge(I) obs: 0.04 / Net I/σ(I): 16.8 |
Reflection shell | Resolution: 1.7→1.8 Å / Rmerge(I) obs: 0.41 / Mean I/σ(I) obs: 2.6 / % possible all: 98.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: NONE Resolution: 1.7→26.66 Å / Cor.coef. Fo:Fc: 0.946 / Cor.coef. Fo:Fc free: 0.923 / SU B: 3.274 / SU ML: 0.104 / Cross valid method: THROUGHOUT / ESU R: 0.132 / ESU R Free: 0.134 Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 1-2 AND 98-110 INCLUDING CTERM HISTAG ARE DISORDERED
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 28.851 Å2
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Refinement step | Cycle: LAST / Resolution: 1.7→26.66 Å
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Refine LS restraints |
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