(1)H, (13)C, and (15)N NMR assignments of StnII-R29Q, a defective lipid binding mutant of the sea anemone actinoporin Sticholysin II.

Several studies have been made to characterize the molecular properties and activity of Sticholysin II (StnII), a 175 amino acid protein secreted by the sea anemone Stichodactyla helianthus. In particular, the biochemical characterization of different mutants of this protein have been shown to be essential for the rational understanding of its activity. Here we report the nearly complete NMR (15)N, (13)C and (1)H chemical shift assignments, at pH 4.0 and 25 degrees C, of a less hemolytic and defective lipid binding mutant of StnII, the R29Q variant (BMRB no 16362).