Fig. 2. (A) Pcn 2.10 ring pattern determined in this work. (B) Representation of the minimum energy structure of the Pcn 2.10 ensemble. Former Cys and Ser/Thr amino acids making up the (Me)Lan rings and dehydroamino acids are highlighted. (C) Superimposition of a five-structure ensemble showing the molecular surface and burial of the hydrophobic side chain of Leu8, colored in green. The N- and C- terminal residues are marked. (D) Superimposition of a three-structure ensemble showing the alignment of the upfield shifted δ protons of Leu15 over the aromatic side chain of Trp14. Trp14 is almost fully solvent inaccessible. (E) Superimposition of the ensemble of the 10 minimum energy structures of prochlorosin 2.10 with the residues involved in thioethers annotated. For a superimposition of the ensemble of the 20 minimum energy structures of Pcn 2.10, see Fig. S6.†.