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  5.2 5.3 -1.9 2.3 29.1 30.3 0.2  ILE-430   LYS-431  7.3 7.5 -11.4 -10.6 44.3 36.2 29.0  LYS-431   ASP-432  6.4 6.6 73.9 14.8 131.9 137.5 -142.5  ASP-432   ARG-433  9.2 7.4 66.7 -42.9 142.1 82.4 -13.7  ARG-433   LEU-434  8.2 9.8 127.3 106.1 154.9 128.5 264.2  LEU-434   LYS-435  10.0 9.6 6.9 -1.1 97.7 177.3 -12.5  LYS-435   ASP-436  10.8 10.6 -46.5 78.6 101.5 67.3 12.1  ASP-436   LEU-437  7.5 8.9 42.8 3.2 106.1 83.7 -6.0  LEU-437   ILE-438  4.6 5.5 18.5 -3.9 166.8 148.6 -25.2  ILE-438   LYS-439  2.8 2.8 -9.0 -3.3 92.0 94.7 -2.2  LYS-439   SER-440  4.7 4.6 0.6 -0.3 139.8 140.6 0.3 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