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. Author manuscript; available in PMC: 2017 Apr 5.
Published in final edited form as: J Am Chem Soc. 2016 May 10;138(22):7143–7150. doi: 10.1021/jacs.6b03422

Figure 9.

Figure 9

Models of ReAsH in complex with previously reported bipartite motifs within CRABP I and the associated values of Ω and Ω’: (A) CRABP I St1-10; (B) CRABP I St1-2; and (C) CRABP I St1’-10. The FlAsH complex of variant St1’-10, which was stable to the highest concentration of EDT,16 possessed a Cys4 arrangement closest to the ideal, with Ω and Ω’ values of 20.17 and -75.17. In each case, the minimized structure of the indicated protein variant bound to ReAsH is shown in teal and aligned with the native structure shown in green.