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Open data
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Basic information
Entry | Database: PDB / ID: 2xes | ||||||
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Title | Human PatL1 C-terminal domain (loop variant) | ||||||
![]() | PROTEIN PAT1 HOMOLOG 1 | ||||||
![]() | RNA BINDING PROTEIN / MRNA DECAPPING / P-BODIES | ||||||
Function / homology | ![]() poly(G) binding / mRNA decay by 5' to 3' exoribonuclease / deadenylation-dependent decapping of nuclear-transcribed mRNA / P-body assembly / poly(U) RNA binding / P-body / PML body / cytoplasmic ribonucleoprotein granule / nuclear speck / RNA binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Tritschler, F. / Weichenrieder, O. | ||||||
![]() | ![]() Title: The C-Terminal Alpha-Alpha Superhelix of Pat is Required for Mrna Decapping in Metazoa. Authors: Braun, J.E. / Tritschler, F. / Haas, G. / Igreja, C. / Truffault, V. / Weichenrieder, O. / Izaurralde, E. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR PROVIDED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 114.2 KB | Display | ![]() |
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PDB format | ![]() | 94.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 449.3 KB | Display | ![]() |
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Full document | ![]() | 457 KB | Display | |
Data in XML | ![]() | 25 KB | Display | |
Data in CIF | ![]() | 37.4 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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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 28807.371 Da / Num. of mol.: 2 / Fragment: C-TERMINAL DOMAIN, RESIDUES 517-767 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | ChemComp-SCN / #3: Chemical | #4: Water | ChemComp-HOH / | Compound details | ENGINEERED | Sequence details | THE FIRST 5 AMINO ACIDS GPQDP RESULT FROM THE 5' CLONING SITE. RESIDUES 664-673 (QSAATPALSN) HAVE ...THE FIRST 5 AMINO ACIDS GPQDP RESULT FROM THE 5' CLONING SITE. RESIDUES 664-673 (QSAATPALSN | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 48 % / Description: NONE |
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Crystal grow | pH: 7 / Details: 12% PEG3350, 0.2 M KSCN, pH 7 |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||
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Diffraction source | Source: ![]() ![]() ![]() | |||||||||
Detector | Type: MARRESEARCH / Detector: CCD / Date: Feb 13, 2009 / Details: MIRRORS | |||||||||
Radiation | Monochromator: SI(111) / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||
Radiation wavelength |
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Reflection | Resolution: 2.1→67 Å / Num. obs: 32014 / % possible obs: 99.3 % / Observed criterion σ(I): 0 / Redundancy: 4 % / Biso Wilson estimate: 26.11 Å2 / Rsym value: 0.1 / Net I/σ(I): 9.1 | |||||||||
Reflection shell | Resolution: 2.1→2.15 Å / Redundancy: 4 % / Mean I/σ(I) obs: 2.2 / Rsym value: 0.66 / % possible all: 99.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: NONE Resolution: 2.1→67.02 Å / SU ML: 0.27 / σ(F): 2.01 / Phase error: 21.66 / Stereochemistry target values: ML Details: RESIDUES 512-516 AND 703-710 AND 767 OF CHAIN A ARE DISORDERED. RESIDUES 512-516 AND 704- -708 OF CHAIN B ARE DISORDERED.
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 40.652 Å2 / ksol: 0.321 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 33.6 Å2
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Refinement step | Cycle: LAST / Resolution: 2.1→67.02 Å
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Refine LS restraints |
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LS refinement shell |
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