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- PDB-7rzz: Crystal structure of FBF-2 in complex with LST-1 site A peptide a... -
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Open data
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Basic information
Entry | Database: PDB / ID: 7rzz | ||||||
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Title | Crystal structure of FBF-2 in complex with LST-1 site A peptide and compact FBE RNA | ||||||
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![]() | RNA BINDING PROTEIN / Pumilio RNA-binding proteins | ||||||
Function / homology | ![]() sex differentiation / P granule / post-transcriptional regulation of gene expression / G-protein alpha-subunit binding / mRNA 3'-UTR binding / regulation of gene expression / cell differentiation / negative regulation of translation / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Qiu, C. / Hall, T.M.T. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Bipartite interaction sites differentially modulate RNA-binding affinity of a protein complex essential for germline stem cell self-renewal. Authors: Qiu, C. / Wine, R.N. / Campbell, Z.T. / Hall, T.M.T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 228.5 KB | Display | ![]() |
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PDB format | ![]() | 149.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 447.6 KB | Display | ![]() |
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Full document | ![]() | 449.6 KB | Display | |
Data in XML | ![]() | 16.7 KB | Display | |
Data in CIF | ![]() | 23.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7s02C ![]() 3k5qS S: Starting model for refinement C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 47019.055 Da / Num. of mol.: 1 / Fragment: UNP residues 164-575 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: RNA chain | Mass: 2872.750 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() ![]() |
#3: Protein/peptide | Mass: 3979.517 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.59 Å3/Da / Density % sol: 52.47 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / Details: 30% (v/v) PEG 400, 0.1 M CHES, pH 9.5 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jun 29, 2019 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.39→35.7 Å / Num. obs: 26102 / % possible obs: 99.5 % / Redundancy: 5.1 % / Biso Wilson estimate: 42.65 Å2 / Rpim(I) all: 0.031 / Net I/σ(I): 14.5 |
Reflection shell | Resolution: 2.39→2.48 Å / Num. unique obs: 2118 / Rpim(I) all: 0.186 / % possible all: 99.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3k5q Resolution: 2.39→35.7 Å / SU ML: 0.2743 / Cross valid method: FREE R-VALUE / σ(F): 1.39 / Phase error: 22.4784 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 50.93 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.39→35.7 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group | Refine-ID: X-RAY DIFFRACTION
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