1H, 13C and 15N resonance assignments for the active conformation of the small G protein RalB in complex with its effector RLIP76

We report here the ¹H, ¹⁵N and ¹³C resonance assignments for the small G protein RalB bound to the GTP analogue, GMPPNP and complexed with the Ral binding domain of its downstream effector RLIP76. The BMRB accession code is 15525.     

1H, 13C and 15N resonance assignments for Binder of Arl2, BART

We report ¹H, ¹³C and ¹⁵N resonance assignments for Binder of Arl Two (BART), an effector of the small G protein Arl2. The BMRB accession code is 15914.     

Resonance assignments for the RLIP76 Ral binding domain in its free form and in complex with the small G protein RalB

We report ¹H and ¹⁵N resonance assignments for the free Ral binding domain of RLIP76 (393–446) and the ¹H, ¹⁵N and ¹³C resonance assignments for the RLIP76 Ral binding domain in complex with the active conformation of RalB. The BMRB accession code for free RLIP76 is 15524 and in complex with RalB is 15525.     

1H, 13C and 15N resonance assignments of domain 1 of receptor associated protein

The 39 kDa receptor associated protein (RAP) is a modular protein consisting of multiple domains. There has been no x-ray crystal structure of RAP available and the full-length protein does not behave well in a NMR tube. To elucidate the 3D structure of the RAP, we undertook structure determination of individual domains of the RAP. As the first step, here we report the nearly complete assignments of the ¹H, ¹³C and ¹⁵N chemical shift signals of domain 1 of the RAP.     

1H, 13C, and 15N resonance assignments of murine amelogenin, an enamel biomineralization protein

Amelogenin is the predominant matrix protein in developing dental enamel. Making extensive use of residue-specific ¹⁵N-labeled amino acids samples, the majority of the main and side chain resonances for murine amelogenin were assigned in 2% aqueous acetic acid at pH 3.0.     

Backbone and sidechain 1H, 13C and 15N resonance assignments of the RGS domain from human RGS14

We have assigned ¹H, ¹⁵N and ¹³C resonances of the RGS domain from the human RGS14 protein, a multi-domain member of the RGS (Regulators of G-protein signalling) family of proteins, important in the down-regulation of specific G-protein signalling pathways.     

1H, 15N,and 13C backbone resonance assignments for the yersinia protein tyrosine phosphatase YopH

YopH is a protein tyrosine phosphatase that functions as a required virulence factor in Yersinia. Here we report the backbone resonance assignments for a point mutant of the C-terminal catalytic domain of YopH.