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Open data
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Basic information
Entry | Database: PDB / ID: 2xvo | ||||||
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Title | SSO1725, a protein involved in the CRISPR/Cas pathway | ||||||
![]() | SSO1725 | ||||||
![]() | STRUCTURAL GENOMICS | ||||||
Function / homology | Jelly Rolls - #1670 / defense response to virus / Jelly Rolls / Sandwich / Mainly Beta / BETA-MERCAPTOETHANOL / Putative CRISPR system CMR subunit Cmr7 2![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Reeks, J. / Liu, H. / Naismith, J. / White, M. / McMahon, S. | ||||||
![]() | ![]() Title: Structure and Mechanism of the Cmr Complex for Crispr-Mediated Antiviral Immunity. Authors: Zhang, J. / Rouillon, C. / Kerou, M. / Reeks, J. / Brugger, K. / Graham, S. / Reimann, J. / Cannone, G. / Liu, H. / Albers, S. / Naismith, J.H. / Spagnolo, L. / White, M.F. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 297.2 KB | Display | ![]() |
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PDB format | ![]() | 254.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 471 KB | Display | ![]() |
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Full document | ![]() | 475.2 KB | Display | |
Data in XML | ![]() | 27.7 KB | Display | |
Data in CIF | ![]() | 38.2 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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Unit cell |
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Components
#1: Protein | Mass: 21563.377 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Details: MERCAPTHOETHANOL ADDUCT / Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | Sequence details | N-TERMINAL GA COMES FROM TAG. THE S2G MUTATION IS OWING TO THE CLONING STRATEGY USED. | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.28 Å3/Da / Density % sol: 45 % / Description: NONE |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97 Å / Relative weight: 1 |
Reflection | Resolution: 2.08→47.48 Å / Num. obs: 46758 / % possible obs: 97.8 % / Observed criterion σ(I): 0 / Redundancy: 4.7 % / Rmerge(I) obs: 0.04 / Net I/σ(I): 19.2 |
Reflection shell | Resolution: 2.08→2.13 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.57 / Mean I/σ(I) obs: 2.2 / % possible all: 86.1 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: NONE Resolution: 2.08→47.48 Å / Cor.coef. Fo:Fc: 0.958 / Cor.coef. Fo:Fc free: 0.946 / SU B: 10.609 / SU ML: 0.138 / Cross valid method: THROUGHOUT / ESU R: 0.228 / ESU R Free: 0.179 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT. REFMAC NCSR-LOCAL WAS USED FOR NCS RESTRAINTS. BME ADDUCTS ON CYS96 IN A, B, AND C. NOT OBSERVED IN D.
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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: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 48.91 Å2
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Refinement step | Cycle: LAST / Resolution: 2.08→47.48 Å
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Refine LS restraints |
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