Apolipoprotein A-II

(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-31   PRO-32  11.1 10.8 -16.7 -14.5 102.9 112.2 -2.6  PRO-32   GLU-33  8.9 8.4 115.3 -30.8 25.4 19.9 68.6  GLU-33   LEU-34  8.5 8.3 -85.6 66.9 92.0 111.7 -3.8  LEU-34   GLN-35  7.3 4.8 71.0 -19.4 160.5 133.6 -37.3  LYS-39   SER-40  5.9 4.8 31.0 -4.5 108.1 86.5 -2.4 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