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-33   ASN-34  4.9 5.0 0.6 4.0 93.8 90.5 42.9  ASN-34   ASP-35  5.2 5.5 1.1 0.1 163.3 159.1 -8.7  ASP-35   LEU-36  5.5 6.1 -13.7 13.4 44.6 44.2 -5.4  LEU-36   GLN-37  2.7 3.1 -3.9 -2.3 81.9 84.5 -30.6 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

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  8.3 8.6 3.1 -0.7 76.0 74.6 39.1  LEU-174   LYS-175  5.3 5.6 5.9 -0.3 75.0 74.4 -7.9  LYS-175   TYR-176  8.1 8.3 16.7 -17.2 144.9 143.5 0.8  TYR-176   SER-177  9.5 9.0 -9.4 -7.3 53.7 62.3 82.3  SER-177   LYS-178  6.1 5.4 -24.0 6.4 111.4 119.1 -50.3  LYS-178   ASN-179  6.2 4.1 -0.2 13.8 48.7 66.6 -43.3  ASN-179   ILE-180  8.5 7.0 -57.0 64.6 38.0 34.6 -33.5  ILE-180   LEU-181  5.4 5.3 -1.4 17.6 106.4 102.3 51.1  LEU-181   ASP-182  2.8 2.8 -9.7 22.3 128.1 120.8 50.9  ASP-182   ARG-183  5.7 5.7 -17.2 15.3 68.7 63.4 -0.8 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