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  12.9 13.0 8.7 0.6 72.4 74.0 2.3  ILE-430   LYS-431  9.1 9.3 -15.2 -10.1 176.0 178.3 -13.9  LYS-431   ASP-432  8.3 8.9 -171.1 -87.7 103.9 114.6 23.1  ASP-432   ARG-433  5.8 5.3 79.6 -71.9 70.4 136.0 1.8  ARG-433   LEU-434  3.1 2.3 136.8 42.6 34.8 76.2 -63.6  LEU-434   LYS-435  1.5 4.5 33.0 -11.2 38.1 79.3 12.6  LYS-435   ASP-436  4.5 4.0 137.0 55.4 79.2 30.0 111.5  ASP-436   LEU-437  6.3 5.0 119.7 -60.0 98.7 96.1 15.1  LEU-437   ILE-438  6.1 5.7 18.6 0.0 56.0 63.3 7.9  ILE-438   LYS-439  7.1 7.1 16.7 -25.9 128.2 134.8 2.5 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