1H, 13C and 15N resonance assignments of the Onconase FL-G zymogen

Abstract

Onconase® FL-G zymogen is a 120 residue protein produced by circular permutation of the native Onconase® sequence. In this construction, the wild type N- and C-termini are linked by a 16 residue segment and new N- and C-termini are generated at wild type positions R73 and S72. This novel segment linking the native N- and C-termini is designed to obstruct Onconase's® active site and encloses a cleavage site for the HIV-1 protease. As a first step towards the resolution of its 3D structure and the study of its structure-function relationships, we report here the nearly complete NMR 1H, 13C and 15N resonance chemical shift assignments at pH 5.2 and 35 C (BMRB deposit no 17973). The results presented here clearly show that the structure of the wild type Onconase ® is conserved in the FL-G zymogen