摘要：YwlE (150 amino acids) fromBacillus subtilisis identified as a low molecular weight protein tyrosinephosphatase (LMW PTPase) and belongs to protein phosphatase super-family, which is involved in variouscellular process and plays important roles, such as signal transduction, proliferation and differentiation(Hunter, 1995; Mijakovic et al., 2003). We here report the nearly complete1H,13Cand15N resonanceassignments of YwlE. 2D and 3D heteronuclear NMR experiments were performed with uniformly15N-,13C-labeled YwlE. About 96%backbone and 90%side-chain1H,13C and15N resonance assignments areobtained with the exception of 10 residues, among which, residues T8, G9, T11, C12 and R13 are in theflexible P-loop region, whereas N31, H50, N63, H64 and G121 in other flexible loops. BMRB deposits withaccession number 6460.
