SZYBKI 1.2.2

New features

  • Two new functions are added to the API:

    void SetResidueFlexibility(double dist); double GetResidueFlexibility() const;

    These allow the user to introduce and query for the flexibility of entire residues around the ligand.

Bug fixes

  • In the case when protein electrostatic model was set at OEProteinElectrostatics::NoElectrostatics and partial protein flexibility was allowed with the void SetSideChainsFlexibility(double) or void SetPolarHFlexibility(double) functions, Coulombic terms describing the interaction between the ligand and flexible protein atoms were included during optimization. This was inconsistent with the meaning of NoElectrostatics, therefore those Coulombic terms were eliminated in the current release
  • Using the function void SetSideChainsFlexibility(double) resulted occasionally in double counting of some residues. This bug was fixed.
  • Fixing atoms with a function bool FixAtoms(std::string) where the passed string is SMARTS pattern, was based on MMFF aromaticity types. Starting from the current release OE aromaticity model is used.