Choline Kinase Alpha

(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  GLU-189   ARG-190  9.8 10.4 -10.7 6.4 75.7 71.4 -7.4  ARG-190   SER-191  9.2 9.9 11.9 -12.1 170.1 167.5 20.9  SER-191   LEU-192  8.5 9.2 -3.8 13.3 76.7 76.1 -14.3  LEU-192   GLY-193  5.4 6.4 -43.5 49.6 75.5 67.1 10.4  GLY-193   PRO-194  3.6 3.9 10.1 0.7 113.0 119.3 -22.3 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

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  ILE-209   PRO-210  6.2 5.9 -13.5 -3.8 25.3 26.4 80.4  PRO-210   SER-211  5.7 5.5 6.3 7.3 93.3 95.0 2.2  SER-211   ARG-212  2.3 1.9 -8.9 3.7 77.7 71.8 27.0 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