Spike Glycoprotein

(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  PRO-589   CYS-590  57.3 57.1 5.1 24.4 37.0 30.0 875.9  CYS-590   SER-591  54.9 55.0 -35.2 -110.0 74.5 95.2 -92.9  SER-591   PHE-592  51.1 52.7 67.5 -36.5 108.7 119.4 -1154.5  PHE-592   GLY-593  51.8 49.8 21.5 68.4 56.9 89.0 1053.7  GLY-593   GLY-594  49.4 47.5 26.8 27.7 100.5 89.5 -236.4  GLY-594   VAL-595  45.7 44.0 -16.9 20.8 146.3 155.7 80.7 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