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. Author manuscript; available in PMC: 2016 Oct 13.
Published in final edited form as: J Chem Theory Comput. 2015 Sep 17;11(10):4770–4779. doi: 10.1021/acs.jctc.5b00662

Figure 3.

Figure 3

RMSD distributions from native in protein G folding simulations with different force fields and number of restraints. The percentages refer to the RMSD populations below 2.5Å sampled in the last 50 ns of a 60 ns restrained folding trajectory. We use a stringent value of 2.5Å as a cutoff since the use of restraints already favor a native like topology; notice that in all cases most conformations are within 4Å from the experimental structure.

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