Electron Transfer Flavoprotein Alpha-Subunit, Mitochondrial Precursor

(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  GLN-202   LYS-203  23.8 24.7 -9.1 29.9 67.3 63.9 -11.1  LYS-203   LEU-204  20.3 21.4 -14.7 29.2 132.2 127.8 9.8  LEU-204   THR-205  17.2 18.5 42.6 -150.4 99.1 100.6 4.3  ARG-209   PRO-210  6.4 7.1 70.9 -22.1 72.5 59.9 27.3  PRO-210   GLU-211  9.4 9.7 -16.1 16.0 95.2 128.5 10.2  GLU-211   LEU-212  11.3 11.7 -28.8 24.4 158.4 154.6 -4.4  LEU-212   THR-213  10.0 10.0 -6.2 10.9 146.3 141.2 2.7  THR-213   GLY-214  12.5 12.8 17.0 -37.8 80.7 85.0 -1.0  GLY-214   ALA-215  13.8 13.2 25.2 -9.0 82.3 95.9 0.4  ALA-215   LYS-216  10.6 9.8 -26.5 30.2 148.9 142.7 1.7 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