Outer Surface Protein A

(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-157   LYS-158  44.4 44.1 8.1 -5.7 137.5 124.5 -16.7  LYS-158   LYS-159  47.3 47.2 -23.4 25.7 72.1 64.4 -53.0  LYS-159   ILE-160  47.7 47.1 -6.8 5.6 43.3 50.0 20.7  ILE-160   THR-161  50.8 50.4 5.0 -11.9 113.3 122.9 -15.0  ARG-185   ALA-186  52.9 53.4 6.9 -19.8 158.8 164.8 81.4  ALA-186   ASP-187  53.7 54.3 17.4 -0.4 92.9 96.4 -116.4  ASP-187   LYS-188  53.3 54.2 12.4 -24.7 66.9 73.0 -71.8  LYS-188   SER-189  49.8 50.5 5.4 -4.2 11.3 18.0 -24.9  SER-189   SER-190  51.1 51.2 23.9 -14.6 64.9 62.4 107.1 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