Fusion Glycoprotein F0

(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-177   ASN-178  7.4 8.2 -119.4 15.3 29.1 45.4 56.7  ASN-178   LYS-179  4.8 6.4 -131.3 -129.5 96.0 104.2 16.3  LYS-179   ASN-180  5.9 4.3 -109.6 -129.9 156.9 123.4 75.6  ASN-180   LYS-181  8.1 3.5 -50.0 32.5 149.1 57.6 -9.7  LYS-181   CYS-182  5.5 4.8 -139.2 28.3 120.3 61.1 9.7  CYS-182   ASP-183  6.9 1.6 -28.0 19.2 150.3 125.2 -5.3  ASP-183   ILE-184  4.7 2.0 -99.3 27.5 79.2 100.0 -17.6  ILE-184   PRO-185  3.7 5.0 155.0 3.9 37.9 135.5 16.8  PRO-185   ASP-186  4.6 6.1 -27.3 25.7 97.2 89.4 4.6  ASP-186   LEU-187  8.1 6.2 -152.6 14.8 122.9 130.8 -59.9 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