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. 2020 Jun 25;11(47):12854–12870. doi: 10.1039/d0sc01651a

Fig. 7. (A) Ring pattern of Pcn 2.8. (B) Depiction of the minimum energy structure of Pcn 2.8. Residues involved in thioether linkages are marked. (C) Surface view of the minimum energy structure of Pcn 2.8 with Tyr14 and Trp15 shown as spheres to explain the lack of proteolytic degradation by chymotrypsin in the buried inter-lanthionine ring region and the proteolytic degradation by chymotrypsin in ring B. Elastase cleaves after Gly17,49 which is indeed solvent exposed. (D) Depiction of the 10 minimum energy structures of Pcn 2.8. Residues involved in thioether linkages are marked. For the ensemble of the 20 minimum energy structures, see Fig. S28..

Fig. 7