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  ARG-87   GLY-88  7.2 6.8 7.4 -5.6 121.9 124.5 0.1  GLY-88   ASP-89  5.1 4.7 -2.9 -17.6 40.2 39.6 10.4  ASP-89   VAL-90  2.5 2.6 176.2 57.5 79.5 75.6 25.4  VAL-90   GLY-91  1.2 1.6 169.3 -35.6 62.7 65.5 63.1  GLY-91   GLU-92  4.6 4.9 39.3 -4.3 129.8 123.0 -11.4 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