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- PDB-6s2w: Structure of S. pombe Erh1, a protein important for meiotic mRNA ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6s2w | ||||||
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Title | Structure of S. pombe Erh1, a protein important for meiotic mRNA decay in mitosis and meiosis progression. | ||||||
![]() | Enhancer of rudimentary-like protein | ||||||
![]() | CELL CYCLE / Meiosis / mRNA degradation | ||||||
Function / homology | ![]() ascospore-type prospore nucleus / regulation of siRNA-independent facultative heterochromatin formation / nuclear exosome focus / nuclear-transcribed mRNA catabolic process, meiosis-specific transcripts / heterochromatin island / termination of RNA polymerase II transcription, poly(A)-coupled / rDNA heterochromatin / molecular function inhibitor activity / nucleoplasm / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Hazra, D. / Graille, M. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Formation of S. pombe Erh1 homodimer mediates gametogenic gene silencing and meiosis progression. Authors: Hazra, D. / Andric, V. / Palancade, B. / Rougemaille, M. / Graille, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 133.7 KB | Display | ![]() |
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PDB format | ![]() | 104.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 492.6 KB | Display | ![]() |
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Full document | ![]() | 496 KB | Display | |
Data in XML | ![]() | 12.5 KB | Display | |
Data in CIF | ![]() | 17.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1w9gS S: Starting model for refinement |
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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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Components
-Protein , 1 types, 3 molecules ABC
#1: Protein | Mass: 12630.225 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: Erh1 / Production host: ![]() ![]() |
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-Non-polymers , 5 types, 81 molecules ![](data/chem/img/EDO.gif)
![](data/chem/img/TRS.gif)
![](data/chem/img/ACY.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/TRS.gif)
![](data/chem/img/ACY.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-EDO / #3: Chemical | ChemComp-TRS / | #4: Chemical | ChemComp-ACY / | #5: Chemical | ChemComp-SO4 / | #6: Water | ChemComp-HOH / | |
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-Details
Has ligand of interest | N |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.37 Å3/Da / Density % sol: 48.04 % |
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Crystal grow | Temperature: 277.15 K / Method: vapor diffusion, hanging drop / Details: 0.3M Ammonium sulfate, 0.1M Sodium Acetate pH 3.8 |
-Data collection
Diffraction | Mean temperature: 93.15 K / Serial crystal experiment: N | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Apr 7, 2018 / Details: bimorph mirrors Kirkpatrick-Baez (KB) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 1.95→45.918 Å / Num. obs: 22390 / % possible obs: 99.6 % / Redundancy: 7.891 % / Biso Wilson estimate: 48.29 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.077 / Rrim(I) all: 0.083 / Χ2: 1.088 / Net I/σ(I): 14.26 / Num. measured all: 176672 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1W9G Resolution: 1.95→45.918 Å / Cor.coef. Fo:Fc: 0.944 / Cor.coef. Fo:Fc free: 0.917 / Rfactor Rfree error: 0 / SU R Cruickshank DPI: 0.17 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.17 / SU Rfree Blow DPI: 0.148 / SU Rfree Cruickshank DPI: 0.149
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Displacement parameters | Biso max: 172.97 Å2 / Biso mean: 61.25 Å2 / Biso min: 32.09 Å2
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Refine analyze | Luzzati coordinate error obs: 0.28 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 1.95→45.918 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.95→2.04 Å / Rfactor Rfree error: 0 / Total num. of bins used: 11
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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