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. Author manuscript; available in PMC: 2018 Aug 2.
Published in final edited form as: J Am Chem Soc. 2017 Jul 24;139(30):10403–10409. doi: 10.1021/jacs.7b04830

Figure 4.

Figure 4

Conformer 2 of benenodin-1 ΔC5 is partially unthreaded. A: Cartoon representation of the benenodin-1 ΔC5 conformer 2 structure showing NOEs between the ring residues (grey) and the new steric lock residues (Ala-16 and Lys-17, turquoise). B: 20 lowest energy structures of benenodin-1 ΔC5 conformer 2 with the same coloring as part A and showing the sidechains of Glu-14, Gln-15, Ala-16, and Lys-17. C: Comparison of the lowest energy structures of conformer 1 (left) and conformer 2 (right) of benenodin-1 ΔC5.