Myotonin-Protein Kinase

(All numbering and residues are taken from first PDB file)

Bending Residue Dihedral Analysis

Residue i Residue i+1 Distance of hinge axis to residue i in conformer 1 (A) Distance of hinge axis to residue i in conformer 2 (A) Change in psi (i) (deg) Change in phi (i+1) (deg) Angle of psi(i) axis to hinge axis conformer 1 (deg) Angle of psi(i) axis to hinge axis conformer 2 (deg) Percentage Progress  SER-27   ARG-28  6.3 6.1 -0.1 2.9 59.5 53.3 7.3  ARG-28   GLU-29  4.7 5.0 1.7 -3.3 70.8 77.7 -60.1  GLU-29   MET-30  1.2 1.4 11.7 5.2 33.3 38.9 139.9  MET-30   GLU-31  2.8 3.0 7.1 -8.7 100.3 104.6 15.3 Graph shows rotational transition at bending residues and can be used to identify hinge bending residues. Probably only informative for interdomain rotations greater than 20 degrees