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  LEU-174   LYS-175  9.7 10.0 -3.0 1.4 115.4 113.1 -17.0  LYS-175   TYR-176  12.4 12.6 19.4 -21.6 118.6 116.8 23.7  TYR-176   SER-177  12.2 11.7 -9.7 0.3 83.0 86.9 24.4  SER-177   LYS-178  8.5 7.9 -33.1 20.4 144.6 142.1 -57.3  LYS-178   ASN-179  7.9 6.5 -3.6 17.3 83.9 95.2 7.5  ASN-179   ILE-180  8.9 6.8 -75.0 81.9 46.4 53.1 -47.2  ILE-180   LEU-181  5.9 5.2 5.1 12.9 71.4 74.2 50.4  LEU-181   ASP-182  2.8 1.9 -8.0 15.0 161.6 152.5 45.4  ASP-182   ARG-183  3.3 2.2 -22.7 28.5 102.6 98.4 -3.3  ARG-183   GLN-184  5.8 5.3 -8.5 3.3 115.4 114.7 -5.2 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