Protein Disulfide-Isomerase

(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  LYS-131   ARG-132  22.1 21.8 38.3 -58.9 115.5 109.3 124.6  ARG-132   THR-133  23.5 23.2 17.6 14.6 101.9 126.1 -97.4  THR-133   GLY-134  20.5 20.3 7.9 5.3 33.9 46.2 84.1  GLY-134   PRO-135  19.1 19.1 -45.9 17.1 119.1 96.8 -124.5  PRO-135   ALA-136  21.3 21.7 13.8 2.8 89.4 61.6 47.4  ALA-136   ALA-137  25.0 25.1 8.9 22.8 25.3 18.8 285.9  ALA-137   THR-138  25.3 25.3 -31.1 3.7 121.8 127.9 -150.0  THR-138   THR-139  22.9 23.2 -8.7 0.7 137.8 132.5 -38.0 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