Camp-Dependent Protein Kinase Type I-Alpha Regulatory Subunit

(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  ASP-225   ARG-226  12.0 12.7 -4.0 2.1 86.7 95.8 -0.3  ARG-226   ASP-227  8.3 9.9 18.6 -3.8 79.9 92.9 0.9  ASP-227   SER-228  8.5 8.5 -10.4 -8.3 42.2 28.7 7.4  SER-228   TYR-229  10.5 8.5 14.3 -7.5 137.2 117.3 -4.6  TYR-229   ARG-230  7.8 7.7 11.9 -8.2 78.4 75.1 0.6  ARG-230   ARG-231  5.2 4.4 6.8 8.4 91.3 115.4 -2.0  ARG-231   ILE-232  8.3 3.8 -27.2 -13.0 31.4 16.0 23.9  ILE-232   LEU-233  9.6 4.2 -10.1 -30.9 61.5 69.0 7.8  LEU-233   MET-234  6.5 4.6 12.5 16.5 66.3 62.4 14.8  MET-234   GLY-235  7.7 4.8 -5.0 9.6 76.2 71.0 0.8  GLY-235   SER-236  11.3 3.6 -4.9 -15.4 18.3 32.2 9.4  SER-236   THR-237  10.8 4.7 22.1 10.3 96.8 84.3 0.4 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