Differing conformational and subpocket preferences of the inhibitors in the crystal structures of the TbPTR1 complexes. We determined the crystal structures of five TbPTR1-NADP(H)-inhibitor complexes with compounds 1a, 2b, 2c, 2d, and 2e to resolutions ranging from 1.58 Å to 1.85 Å (Fig. ; Tabs S8 and S9, SI). In all complexes, the crystal asymmetric unit includes a whole TbPTR1 tetramer, whose structure is highly similar to the previously reported models . The 2-aminobenzothiazole moiety of all compounds adopted exactly the same binding mode in the current crystal structures, as was observed in the previously published structures and in most docking results in this work (Fig. ). More details of the general characteristics of the structures is presented in SI.