Gamma-Glutamyltranspeptidase

(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  ASN-457   LYS-458  20.4 19.9 11.6 -18.4 108.5 107.7 -107.7  LYS-458   ARG-459  19.4 18.9 1.0 -0.5 158.4 159.7 84.8  ARG-459   PRO-460  17.1 16.8 3.7 -8.0 120.8 115.0 114.5  PRO-460   LEU-461  19.0 18.8 10.8 -4.2 110.2 112.9 -6.9  LEU-461   SER-462  17.9 17.6 12.3 -22.3 161.4 160.9 180.7  SER-462   SER-463  15.6 15.6 -23.7 35.0 69.7 72.8 -141.6  SER-465   PRO-466  9.7 9.5 4.7 5.5 108.8 113.9 43.8  PRO-466   THR-467  6.0 5.9 7.7 -8.1 66.1 66.9 30.9 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