Lysr-Type Regulatory Protein

(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  THR-82   ALA-83  12.0 11.2 -25.3 9.4 96.9 97.2 3.8  ALA-83   LEU-84  9.2 9.3 -12.9 -33.7 93.9 129.5 -1.5  LEU-84   THR-85  7.8 7.5 -11.4 -2.0 46.6 66.0 7.5  THR-85   THR-86  5.9 7.4 18.2 -5.0 66.7 138.8 2.0  THR-86   ARG-87  3.0 4.7 -31.8 -43.5 55.4 35.2 41.0  ARG-87   ASP-88  4.3 5.6 -164.8 -11.4 43.3 62.1 134.4  ASP-88   SER-89  2.1 6.4 140.2 19.4 141.3 133.1 -74.1  SER-89   PHE-90  2.0 4.2 7.9 21.4 126.4 154.0 -20.8  PHE-90   ASP-91  3.9 4.6 -5.9 -5.2 39.1 54.0 3.6  ASP-91   PRO-92  5.5 5.5 5.7 3.1 141.9 150.0 -4.3  PRO-92   PHE-93  5.5 5.4 2.0 4.6 121.4 117.5 -4.6 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