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- PDB-2xs5: Crystal structure of the RRM domain of mouse Deleted in azoosperm... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2xs5 | ||||||
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Title | Crystal structure of the RRM domain of mouse Deleted in azoospermia- like in complex with Mvh RNA, UGUUC | ||||||
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![]() | RNA BINDING PROTEIN/RNA / RNA BINDING PROTEIN-RNA COMPLEX / TRANSLATION REGULATION | ||||||
Function / homology | ![]() female meiosis II / translation activator activity / positive regulation of meiotic nuclear division / oocyte maturation / 3'-UTR-mediated mRNA stabilization / germ cell development / positive regulation of translational initiation / mRNA 3'-UTR binding / spermatogenesis / ribosome ...female meiosis II / translation activator activity / positive regulation of meiotic nuclear division / oocyte maturation / 3'-UTR-mediated mRNA stabilization / germ cell development / positive regulation of translational initiation / mRNA 3'-UTR binding / spermatogenesis / ribosome / protein-containing complex / identical protein binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Jenkins, H.T. / Edwards, T.A. | ||||||
![]() | ![]() Title: Kinked Beta-Strands Mediate High-Affinity Recognition of Mrna Targets by the Germ-Cell Regulator Dazl Authors: Jenkins, H.T. / Edwards, T.A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 101.6 KB | Display | ![]() |
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PDB format | ![]() | 77.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 452.4 KB | Display | ![]() |
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Full document | ![]() | 452.5 KB | Display | |
Data in XML | ![]() | 11.9 KB | Display | |
Data in CIF | ![]() | 17.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2xs2SC ![]() 2xs7C ![]() 2xsfC S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.9987, -0.05053, -0.000232), Vector: |
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Components
#1: Protein | Mass: 9797.299 Da / Num. of mol.: 2 / Fragment: RESIDUES 32-117 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: RNA chain | Mass: 1523.928 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) ![]() ![]() #3: Chemical | ChemComp-PEG / | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.76 Å3/Da / Density % sol: 55 % / Description: NONE |
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Crystal grow | Details: 0.1 M MAGNESIUM ACETATE, 18% (W/V) PEG 3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: May 15, 2010 Details: KIRKPATRICK BAEZ BIMORPH MIRROR PAIR FOR HORIZONTAL AND VERTICAL FOCUSSING |
Radiation | Monochromator: DOUBLE CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→27.07 Å / Num. obs: 29634 / % possible obs: 98.7 % / Observed criterion σ(I): 6 / Redundancy: 4.9 % / Biso Wilson estimate: 16.6 Å2 / Rmerge(I) obs: 0.09 / Net I/σ(I): 11.2 |
Reflection shell | Resolution: 1.6→1.69 Å / Redundancy: 4.9 % / Rmerge(I) obs: 0.76 / Mean I/σ(I) obs: 2.1 / % possible all: 98 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2XS2 Resolution: 1.6→27.07 Å / Cor.coef. Fo:Fc: 0.963 / Cor.coef. Fo:Fc free: 0.954 / SU B: 4.234 / SU ML: 0.066 / Cross valid method: THROUGHOUT / ESU R: 0.09 / ESU R Free: 0.092 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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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: 19.648 Å2
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Refinement step | Cycle: LAST / Resolution: 1.6→27.07 Å
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Refine LS restraints |
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