Fig. 6

DynaMut results depiction of molecular flexibility analysis and interatomic interactions of regulatory domain of PKC γ. a. Variant C52S is shown. Hydrogen bonds are present at 3.1A-3.6A. b. Variant C114Y is shown. Hydrogen bonds are present between 2.8A and 3.5A (Angstrom) while hydrophobic interactions are displayed between 2.9A and 4.5A. The aromatic interactions are observed between 2.7A and 3.9A. c. Variant D115Y is represented. Hydrogen bonds are present between 2.7A to 3.2A. Hydrophobic interactions are observed at 3.9A and 4.5A. d. Variant G128R is shown. Hydrogen bonds are present between 2.4A and 3.7A. Hydrophobic interactions are displayed between 3.9A and 4.5A. e. Variant C131Y is shown. Hydrogen bonds are present between 2.8A and 3.7A. Hydrophobic interactions and aromatic interactions are observed at 3.0A-4.5A and 3.4A-3.9A respectively. f. Variant V138M is shown. Hydrogen bonds are present between 2.8A and 2.9A distance. Hydrophobic interactions are observed between 3.5A and 4.5A. g. Variant C150R is shown. Hydrogen bonds are present between 2.8A and 3.9A. Hydrophobic interactions are observed at 3.4A, 4.3A and 4.4A. h. Variant G159R is shown. Hydrogen bonds are present at 2.5A–3.0A. Hydrophobic interactions are observed between 3.8A and 4.5A. The region where mutation is present is highlighted inside the red box that depicts the rigidification of the structure and decrease of molecular flexibility in the represented structures