Conserved Hypothetical Protein Mth1747

(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  ALA-157   ILE-158  8.0 8.0 7.0 -7.5 75.2 73.4 2.4  ILE-158   LYS-159  4.5 4.5 0.6 -2.4 64.7 62.3 0.7  LYS-159   MET-160  7.0 7.2 5.0 -1.2 17.3 23.8 13.7  MET-160   LEU-161  8.3 8.4 -0.4 -1.2 128.1 131.2 8.5  LEU-161   ARG-162  4.8 5.0 0.2 -0.8 75.3 73.1 -14.5  ARG-162   SER-163  4.5 4.6 -6.3 2.9 132.6 133.2 -18.3  SER-163   SER-164  7.8 8.0 7.8 -2.3 22.8 27.7 47.5  SER-164   TYR-165  6.4 6.7 -2.8 4.6 120.5 125.8 9.6  TYR-165   THR-166  3.7 4.0 1.8 0.4 71.7 69.0 20.3 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