Eiav Capsid Protein P26

(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  ILE-145   GLY-146  4.7 5.0 -174.1 -157.2 95.5 100.0 -6.4  GLY-146   LYS-147  2.3 1.5 7.8 -45.2 119.6 137.3 22.8  LYS-147   PRO-148  1.0 1.8 -76.9 -6.6 33.6 43.9 70.6  PRO-148   LYS-149  2.5 1.7 -44.1 19.3 36.8 25.0 32.4  LYS-149   ALA-150  1.0 1.2 157.7 -131.5 144.6 123.9 -27.3 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