Cyclopropane-Fatty-Acyl-Phospholipid Synthase 1

(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  THR-170   GLY-171  7.5 7.3 -13.6 -14.6 60.4 63.9 34.6  GLY-171   LEU-172  4.9 4.0 -12.2 -10.9 44.4 57.9 37.0  LEU-172   HIS-173  5.9 3.9 24.3 -7.4 75.7 62.5 15.2 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

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  ILE-199   PHE-200  7.3 8.2 12.4 -1.9 76.0 110.4 5.1  PHE-200   PRO-201  5.9 5.1 -36.9 16.9 101.6 67.1 313.7  PRO-201   GLY-202  4.9 2.6 154.4 -12.9 146.3 93.1 -151.9  GLY-202   GLY-203  3.9 1.5 -45.0 89.1 52.2 147.3 27.2  GLY-203   ARG-204  0.2 2.7 -14.0 -77.9 124.3 130.6 -107.4  ARG-204   LEU-205  3.5 3.8 10.6 12.2 69.7 42.4 18.4  LEU-205   PRO-206  5.0 4.9 -20.5 -5.8 109.4 111.0 -17.4 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