Long Chain Fatty Acid-Coa Ligase

(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  GLU-429   ILE-430  12.6 12.8 14.6 -5.8 72.2 74.2 2.0  ILE-430   LYS-431  8.9 9.1 -13.3 -10.5 175.4 178.9 -12.6  LYS-431   ASP-432  8.0 8.7 -172.9 -87.6 103.7 113.7 22.5  ASP-432   ARG-433  5.5 5.1 77.2 -72.3 69.8 135.5 2.2  ARG-433   LEU-434  2.9 2.2 136.6 40.7 34.9 75.9 -64.7  LEU-434   LYS-435  1.2 4.7 23.0 4.5 38.4 82.0 15.9  LYS-435   ASP-436  4.3 4.4 146.7 36.0 78.8 28.6 105.4  ASP-436   LEU-437  6.1 5.2 121.5 -61.6 98.0 91.3 18.3  LEU-437   ILE-438  5.9 5.9 25.3 -0.2 55.6 64.8 10.4  ILE-438   LYS-439  7.0 7.1 14.9 -18.8 127.5 135.9 1.6 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