Supplementary Figure 4: SSNMR internal validation of structural restraints and dihedral angles for the α-syn fibril structure.
From: Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein
(a) The backbone trace is shown in grey, and black lines represent unambiguous distance restraints. Blue lines correspond to the shortest observed distance among the possible ambiguous assignments. The resulting structure is the lowest energy conformer consistent with all of the data. (b-c) Ramachandran probability maps of accepted dihedral angle regions (Lovell, S.C. et al. Structure validation by Cα geometry: φ,ψ and Cβ deviation. Proteins 50, 437–450 (2003).) and plotted in Chimera (Pettersen, E.F. et al. UCSF Chimera—a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605–1612 (2004).) for residues 41–100. The only residue not in the accepted range is E57, which is part of an unstructured loop and lacks NMR restraints in the simulated annealing calculations. All glycine residues are within the accepted Ramachandran space.
