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. Author manuscript; available in PMC: 2015 Jun 1.
Published in final edited form as: J Magn Reson. 2014 Apr 2;243:54–64. doi: 10.1016/j.jmr.2014.03.011

Figure 3. Recognition of native protein fold.

Figure 3

(A, B, G, H) Rosetta (black) and EEFx (red) energy landscapes of GB1 (A, B) and BAF (G, H). RMSD values are computed for CA atoms relative to the decoy with lowest energy (blue circles). (C, D, I, J) Cartoon representations of the decoys of GB1 (C, D) and BAF (I, J) with lowest Rosetta energy (gray) or lowest EEFx energy (red) and superimposed experimental PDB structures (cyan). RMSDs represent structural accuracy, computed for CA atoms relative to the experimental PDB structures. (E, F, K, L) Ribbon representations of the 10 decoys of GB1 (E, F) and BAF (K, L) with lowest Rosetta energy (gray) or lowest EEFx energy (red). RMSDs represent precision of the structural ensembles, evaluated as average pairwise values for CA atoms.