Extended Data Fig. 4: Rosetta energy minimization of hIAPP fibril structure and rIAPP homology model.
From: Cryo-EM structure and inhibitor design of human IAPP (amylin) fibrils
a, Structure superimposition between (grey) hIAPP fibril structure determined here and (blue) hIAPP fibril structure (upper panels) or rIAPP homology model (lower panels) optimized by Rosetta energy minimization. Calculation was done either allowing only side chain movements (left panels) or allowing both side chain and main chain movements (middle and right panels). Notice that during Rosetta energy minimization, we did not apply non-crystallographic symmetry so that the 5 layers in each model were not forced to be identical. b, Steric clashes of the rIAPP homology model after side chain Rosetta energy minimization were probed with COOT and displayed as red dots. Notice that most of the steric clashes are found near S28P and S29P.
