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Stereoview of the 2Fo − Fc electron density of the terminal rhamnose I (Rha I) of the O-antigen fragment from S. typhi253Ty bound to the active site at 1.8 Å resolution contoured at 1σ. The discontinuity of the electron density between C2 and C3 is also observed for S. typhimurium and S. enteritidis receptor fragments. The main conformation adopted by Rha I corresponds to a twisted boat conformation with C1 in α-configuration as in the substrate.
