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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 15N, 13C and 1H chemical shift assignments, at pH 4.0 and 25°C, of a less hemolytic and defective lipid binding mutant of StnII, the R29Q variant (BMRB no 16362). [ABSTRACT FROM AUTHOR]

Sticholysin I is an actinoporin, a pore forming toxin, of 176 aminoacids produced by the sea anemone Stichodactyla heliantus. Isotopically labelled 13C/15N recombinant protein was produced in E. coli. Here we report the complete NMR 15N, 13C and 1H chemical shifts assignments of Stn I at pH 4.0 and 25°C (BMRB No. 15927). [ABSTRACT FROM AUTHOR]