Conserved Protein (Mth177)

(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  ARG-71   SER-72  8.0 7.9 15.3 -17.8 74.5 83.0 23.1  SER-72   LEU-73  5.4 5.2 17.9 -35.9 119.5 120.6 21.5  LEU-73   GLU-74  2.2 2.9 132.1 -31.8 66.6 55.7 62.4  GLU-74   ALA-75  0.7 3.0 18.4 52.8 82.9 119.2 -66.7  ALA-75   GLU-76  4.4 6.5 -15.5 26.1 130.6 89.3 4.7 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