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. Author manuscript; available in PMC: 2016 Feb 25.
Published in final edited form as: J Chem Theory Comput. 2007 Nov;3(6):2083–2097. doi: 10.1021/ct7001336

Table 3.

Shown is a comparison of the performance of the SFA and RPA in determining the perfect self-energy (kcal/mole) for a series of five folded proteins. Optimization of a single HCT scale factor for each method removes systematic error as shown by the mean signed percent differences. However, the mean RPA unsigned percent difference of 0.5 is smaller than that of the SFA.

Self-Energy Signed % Difference Unsigned % Difference



PMPB SFA RPA SFA RPA SFA RPA
CRN −8141 −8191 −8196 −0.6 −0.7 0.6 0.7
ENH −11919 −11852 −11878 0.6 0.3 0.6 0.3
FSV −6254 −6341 −6287 −1.4 −0.5 1.4 0.5
PGB −11794 −11743 −11803 0.4 −0.1 0.4 0.1
VII −7206 −7132 −7133 1.0 1.0 1.0 1.0

Mean 0.0 0.0 0.8 0.5