|Entry||Database: PDB / ID: 2juc|
|Title||URN1 FF domain yeast|
|Components||Pre-mRNA-splicing factor URN1|
|Keywords||UNKNOWN FUNCTION / FF / helical bundle / solution / mRNA processing / mRNA splicing / Nucleus / Spliceosome|
|Function / homology|
Function and homology information
prespliceosome / U2-type prespliceosome / U1 snRNP / mRNA splicing, via spliceosome / RNA binding / nucleus
Similarity search - Function
FF domain / FF domain / FF domain profile. / FF domain / FF domain superfamily / Contains two conserved F residues / WW domain / WW/rsp5/WWP domain signature. / WW domain superfamily / Domain with 2 conserved Trp (W) residues ...FF domain / FF domain / FF domain profile. / FF domain / FF domain superfamily / Contains two conserved F residues / WW domain / WW/rsp5/WWP domain signature. / WW domain superfamily / Domain with 2 conserved Trp (W) residues / WW/rsp5/WWP domain profile. / WW domain / Arc Repressor Mutant, subunit A / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Pre-mRNA-splicing factor URN1
Similarity search - Component
|Biological species||Saccharomyces cerevisiae (baker's yeast)|
|Method||SOLUTION NMR / torsion angle dynamics|
|Model details||URN1 FF domain yeast|
|Authors||Bonet, R. / Ramirez-Espain, X. / Macias, M.J.|
|Citation||Journal: Proteins / Year: 2008|
Title: Solution structure of the yeast URN1 splicing factor FF domain: Comparative analysis of charge distributions in FF domain structures-FFs and SURPs, two domains with a similar fold.
Authors: Bonet, R. / Ramirez-Espain, X. / Macias, M.J.
|Structure viewer||Molecule: |
Downloads & links
A: Pre-mRNA-splicing factor URN1
|#1: Protein|| |
Mass: 7183.930 Da / Num. of mol.: 1 / Fragment: FF domain (residues 212-266)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (baker's yeast)
Gene: URN1 / Plasmid: petm30 / Production host: Escherichia coli (E. coli) / References: UniProt: Q06525
|Experiment||Method: SOLUTION NMR / Details: URN1 FF domain yeast|
|Sample conditions||pH: 5.8 / Pressure: ambient / Temperature: 285 K|
|Refinement||Method: torsion angle dynamics / Software ordinal: 1|
|NMR representative||Selection criteria: lowest energy|
|NMR ensemble||Conformer selection criteria: structures with the lowest energy|
Conformers calculated total number: 60 / Conformers submitted total number: 15
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