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  12.7 12.9 5.4 3.6 72.0 67.6 3.6  ILE-430   LYS-431  9.0 9.2 -12.6 -6.8 175.8 177.7 -10.9  LYS-431   ASP-432  8.1 8.9 177.8 -80.3 76.0 65.6 22.0  ASP-432   ARG-433  5.6 5.3 78.6 -66.3 69.9 135.6 0.6  ARG-433   LEU-434  3.0 2.3 134.7 41.6 34.5 77.7 -65.2  LEU-434   LYS-435  1.4 4.6 23.1 -3.8 38.6 80.4 12.1  LYS-435   ASP-436  4.4 4.3 140.9 47.7 79.2 32.9 109.6  ASP-436   LEU-437  6.2 4.9 133.5 -62.1 98.2 97.2 19.0  LEU-437   ILE-438  6.0 5.6 26.2 -10.2 55.5 60.4 7.3  ILE-438   LYS-439  7.0 7.1 17.6 -27.2 127.6 133.4 2.7 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