1H, 13C and 15N resonance assignments for the small G protein RalB in its active conformation

We report 1H, 13C and 15N resonance assignments for the small G protein RalB in its active conformation. Backbone amide dynamics parameters for a majority of residues have also been obtained. The BMRB accession code is 15230 [corrected]

Saved in:
Bibliographic Details
Published in:Biomolecular NMR assignments 2007-07, Vol.1 (1), p.147-149
Main Authors: Prasannan, Sunil, Fenwick, R Bryn, Campbell, Louise J, Evetts, Katrina A, Nietlispach, Daniel, Owen, Darerca, Mott, Helen R
Format: Article
Language:English
Subjects:
Humans
Molecular biology
Molecular Structure
Mutagenesis, Site-Directed
NMR
Nuclear magnetic resonance
Nuclear Magnetic Resonance, Biomolecular
Peptide Fragments - chemistry
Peptide Fragments - genetics
Protein Conformation
Protein Structure, Tertiary
Proteins
ral GTP-Binding Proteins - chemistry
ral GTP-Binding Proteins - genetics
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:We report 1H, 13C and 15N resonance assignments for the small G protein RalB in its active conformation. Backbone amide dynamics parameters for a majority of residues have also been obtained. The BMRB accession code is 15230 [corrected]
ISSN:1874-2718
1874-270X
DOI:10.1007/s12104-007-9040-1