Zinc-Alpha-2-Glycoprotein

(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  TYR-173   LEU-174  8.9 8.6 -4.4 3.0 74.3 74.6 55.1  LEU-174   LYS-175  5.9 5.6 -3.2 -3.6 74.9 74.0 4.2  LYS-175   TYR-176  8.7 8.5 9.6 -13.6 34.9 39.3 -34.4  TYR-176   SER-177  9.3 9.7 14.5 6.7 63.1 54.1 83.7  SER-177   LYS-178  5.7 6.4 13.1 5.0 118.4 110.6 -22.0  LYS-178   ASN-179  4.4 6.4 -1.1 -16.3 114.7 135.6 -53.1  ASN-179   ILE-180  7.3 8.7 49.4 -56.0 36.5 37.7 -42.5  ILE-180   LEU-181  5.5 5.6 6.1 -24.7 103.2 104.6 54.8  LEU-181   ASP-182  2.8 2.8 4.2 -11.4 120.7 126.1 27.3  ASP-182   ARG-183  5.7 5.6 10.2 -10.1 62.5 66.2 14.0 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