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Open data
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Basic information
Entry | Database: PDB / ID: 4w8z | ||||||
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Title | Crystal structure of Cmr1 from Pyrococcus furiosus (apo form) | ||||||
![]() | CRISPR system Cmr subunit Cmr1-1 | ||||||
![]() | RNA BINDING PROTEIN / Cmr1 / apo form / CMR complex / CRISPR | ||||||
Function / homology | : / Cmr1-like, C-terminal / CRISPR-associated protein TM1795 / CRISPR type III-associated protein / RAMP superfamily / defense response to virus / RNA binding / cytoplasm / CRISPR system Cmr subunit Cmr1-1![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Benda, C. / Ebert, J. / Baumgaertner, M. / Conti, E. | ||||||
![]() | ![]() Title: Structural Model of a CRISPR RNA-Silencing Complex Reveals the RNA-Target Cleavage Activity in Cmr4. Authors: Benda, C. / Ebert, J. / Scheltema, R.A. / Schiller, H.B. / Baumgartner, M. / Bonneau, F. / Mann, M. / Conti, E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 145.9 KB | Display | ![]() |
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PDB format | ![]() | 115.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 423.2 KB | Display | ![]() |
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Full document | ![]() | 425.4 KB | Display | |
Data in XML | ![]() | 13.3 KB | Display | |
Data in CIF | ![]() | 17.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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
#1: Protein | Mass: 39782.711 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() References: UniProt: Q8U1S5 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.94 Å3/Da / Density % sol: 68.77 % |
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Crystal grow | Temperature: 293.15 K / Method: vapor diffusion, hanging drop Details: 100 mM bicine/Trizma base pH 6.0, 10% PEG 8000, 20% ethylene glycol, 20 mM each of sodium DL- alanine, sodium L-gutamate, gylcine, DL-lysine HCl, DL-serine and either 3% DMSO or 3% D-sorbitol |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Dec 13, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.037 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→50 Å / Num. obs: 33393 / % possible obs: 99.8 % / Redundancy: 19.4 % / Net I/σ(I): 18.2 |
Reflection shell | Resolution: 2.701→2.798 Å / Redundancy: 17.6 % / Mean I/σ(I) obs: 1.3 / % possible all: 97.88 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.7→45.589 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Origin x: 13.9224 Å / Origin y: 49.6218 Å / Origin z: 16.5057 Å
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Refinement TLS group | Selection details: all |