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Figure 2
Average energies (kcal mol−1) of the twenty dihedral-angle types in the 46 high-resolution protein structures based on (a) the currently used restraint parameters, and (b) the proposed new parameters. The dihedral energy based on the old parameters is clearly dominated by the peptide ω angle, implying that it is too tightly restrained. Note that the backbone conformational angles φ and ψ are not restrained (force constant = 0) in the old parameter set. The contribution to the dihedral energy by the various dihedral-angle types is more evenly distributed when the proposed new dihedral-angle restraint set is used.

Journal logoJOURNAL OF
APPLIED
CRYSTALLOGRAPHY
ISSN: 1600-5767
Volume 36| Part 1| February 2003| Pages 34-42
https://doi.org/10.1107/S0021889802018265
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