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  8.5 8.3 -4.0 1.4 75.4 75.0 45.1  LEU-174   LYS-175  5.5 5.3 -3.6 -5.7 76.1 73.7 -0.9  LYS-175   TYR-176  8.2 8.2 12.0 -15.6 33.6 39.7 -26.6  TYR-176   SER-177  8.8 9.4 16.0 5.3 62.8 52.4 78.5  SER-177   LYS-178  5.3 6.0 15.7 2.2 118.0 110.3 -29.0  LYS-178   ASN-179  4.1 6.1 2.2 -23.6 64.1 47.6 -85.4  ASN-179   ILE-180  7.1 8.3 49.5 -48.4 36.9 38.9 1.2  ILE-180   LEU-181  5.2 5.2 5.2 -22.7 103.7 108.0 45.7  LEU-181   ASP-182  2.9 2.8 0.6 -12.5 119.9 124.5 41.9  ASP-182   ARG-183  5.9 5.6 7.9 -7.9 61.4 66.4 4.0 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