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. Author manuscript; available in PMC: 2014 Jul 2.
Published in final edited form as: Structure. 2013 May 30;21(7):1107–1117. doi: 10.1016/j.str.2013.04.022

Figure 3. Accurate models are produced for targets of varying size, complexity, and SSE content.

Figure 3

A – NCO versus amino acids. Each point represents the best model produced for a particular target. Single subunit predictions are circles and multimer predictions are squares. Both use the following coloring scheme based on RMSD100: RMSD100 < 6.0 Å (green), 6.0 Å ≤ RMSD100 < 8.0 Å (light green), 8.0 Å ≤ RMSD100 < 10.0 Å (yellow), 10.0 Å ≤ RMSD100 (red). Proteins with multiple chains in the protomer are excluded since the contact order is undefined. For multimers, the contact order reported is for the protomer while the amino acid count is the total for the complete multimer. B – Q3 versus SSE content. The plotted Q3 value is the average of the JUFO9D and SPOCTOPUS predictions. SSE content is the percentage of residues that are part of a helix or strand. C – RMSD100 of top 5% of best models versus amino acids. BCL::MP-Fold shown as black triangles and Rosetta-Membrane as circles. D – RMSD100 was computed for BCL::MP-Fold and Rosetta-Membrane to the SSEs of the native models. The value for the top 1% of models ± S.D. sampled is plotted for each method. The dashed line at 8 Å indicates the arbitrary cutoff for “native-like” quality.