title: 1H, 13C and 15N resonance assignments for the small G protein RalB in its active conformation.
abstract: 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]
authors.affiliation: Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB21GA, UK.
authors.forename: Sunil
authors.initials: S
authors.lastname: Prasannan
authors.forename: R Bryn
authors.initials: RB
authors.lastname: Fenwick
authors.forename: Louise J
authors.initials: LJ
authors.lastname: Campbell
authors.forename: Katrina A
authors.initials: KA
authors.lastname: Evetts
authors.forename: Daniel
authors.initials: D
authors.lastname: Nietlispach
authors.forename: Darerca
authors.initials: D
authors.lastname: Owen
authors.forename: Helen R
authors.initials: HR
authors.lastname: Mott
mesh_terms: D006801:Humans; D015394:Molecular Structure; D016297:Mutagenesis, Site-Directed; D019906:Nuclear Magnetic Resonance, Biomolecular; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D020725:ral GTP-Binding Proteins / Q000737:chemistry* / Q000235:genetics
chemical_list: D010446:Peptide Fragments; C483163:Ralb protein, human; D011994:Recombinant Proteins; D020725:ral GTP-Binding Proteins