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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 2.

Figure 2

NMR structure of benenodin-1 ΔC5. A: Cartoon of the structure with grey residues representing the ring of the peptide, lime green residues in the loop, and blue residues in the tail. The steric lock residues Glu-14 and Gln-15 are shown in red. Arrows show NOEs observed between ring residues and steric lock residues. B: The lowest energy conformer of benenodin-1 showing the backbone of the peptide and the sidechains of the steric lock residues. Coloring is the same as in the cartoon in part A. C: As in part B, but showing the 20 lowest energy structures.