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Table 2 Structural features used in Prethermut

From: Predicting changes in protein thermostability brought about by single- or multi-site mutations

Feature Programa Feature Program
Total energy FoldX Stereochemical improper dihedral potential Modeller 9.7
Backbone H-bond FoldX Frequency_[0,2.1) b Modeller 9.7
Sidechain H-bond FoldX Frequency_[2.1,2.2) Modeller 9.7
Van der Waals forces FoldX Frequency_[2.2,2.3) Modeller 9.7
Electrostatic attractions FoldX Frequency_[2.3,2.4) Modeller 9.7
Solvation polar FoldX Frequency_[2.4,2.5) Modeller 9.7
Solvation hydrophobic FoldX Frequency_[2.5,2.6) Modeller 9.7
Van der Waals clashes FoldX Frequency_[2.6,2.7) Modeller 9.7
Entropy side chain FoldX Frequency_[2.7,2.8) Modeller 9.7
Entropy main chain FoldX Frequency_[2.8,2.9) Modeller 9.7
Torsional clash FoldX Frequency_[2.9,3.0) Modeller 9.7
Backbone clash FoldX Frequency_[3.0,3.1) Modeller 9.7
Helix dipole FoldX Frequency_[3.1,3.2) Modeller 9.7
Current energy Modeller 9.7 Frequency_[3.2,3.3) Modeller 9.7
Bond energy Modeller 9.7   
  1. aThe corresponding feature was calculated by the programs (FoldX [11, 28] and Modeller 9.7 [29]). bThe frequency of short non-covalent contacts with a distance of less than 2.1 Å.