+Open data
-Basic information
Entry | Database: PDB / ID: 2wac | ||||||
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Title | Extended Tudor domain of Drosophila Melanogaster Tudor-SN (p100) | ||||||
Components | CG7008-PA | ||||||
Keywords | SPLICING / UNKNOWN FUNCTION / TUDOR / BETA-BARREL / NUCLEASE DOMAIN / TUDOR-SN / P100 / SND1 / METHYLATED ARGININE / SDMA | ||||||
Function / homology | Function and homology information : / nuclease activity / regulatory ncRNA-mediated gene silencing / RNA catabolic process / RISC complex / micrococcal nuclease / spermatogenesis / endonuclease activity / RNA binding / nucleus ...: / nuclease activity / regulatory ncRNA-mediated gene silencing / RNA catabolic process / RISC complex / micrococcal nuclease / spermatogenesis / endonuclease activity / RNA binding / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | DROSOPHILA MELANOGASTER (fruit fly) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.1 Å | ||||||
Authors | Friberg, A. / Corsini, L. / Sattler, M. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2009 Title: Structure and Ligand Binding of the Extended Tudor Domain of D. Melanogaster Tudor-Sn Authors: Friberg, A. / Corsini, L. / Mourao, A. / Sattler, M. | ||||||
History |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 5-STRANDED BARREL THIS IS REPRESENTED BY A 6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2wac.cif.gz | 101.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2wac.ent.gz | 78.3 KB | Display | PDB format |
PDBx/mmJSON format | 2wac.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wa/2wac ftp://data.pdbj.org/pub/pdb/validation_reports/wa/2wac | HTTPS FTP |
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-Related structure data
Related structure data | 2hqeS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 24233.254 Da / Num. of mol.: 2 / Fragment: TSN DOMAIN, TUDOR AND SN5, RESIDUES 700-916 Source method: isolated from a genetically manipulated source Source: (gene. exp.) DROSOPHILA MELANOGASTER (fruit fly) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / References: UniProt: Q9W0S7 #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 51 % / Description: NONE |
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Crystal grow | pH: 6.8 / Details: 20% PEG 3350, 100 MM BIS-TRIS PH 5.5, 200 MM NACL |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Wavelength: 1.54179 |
Detector | Date: Jun 2, 2007 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54179 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→19.64 Å / Num. obs: 28296 / % possible obs: 98.7 % / Observed criterion σ(I): 3 / Redundancy: 3.63 % / Rmerge(I) obs: 0.04 / Net I/σ(I): 24.4 |
Reflection shell | Resolution: 2.1→2.22 Å / Redundancy: 3.51 % / Rmerge(I) obs: 0.15 / Mean I/σ(I) obs: 10.2 / % possible all: 97.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2HQE Resolution: 2.1→19.64 Å / Cor.coef. Fo:Fc: 0.925 / Cor.coef. Fo:Fc free: 0.893 / SU B: 11.159 / SU ML: 0.165 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.266 / ESU R Free: 0.212 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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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: 25.08 Å2
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Refinement step | Cycle: LAST / Resolution: 2.1→19.64 Å
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Refine LS restraints |
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