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
 ARG-325   PHE-326  6.8 4.5 37.2 -25.9 45.7 37.7 10.8
 PHE-326   PRO-327  4.4 3.3 2.6 7.0 33.7 40.4 46.3
 PRO-327   ASN-328  4.8 4.6 -7.0 33.0 93.9 103.3 11.9

Downloading Image

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


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
 GLY-523   PRO-524  4.9 7.1 -15.8 10.4 96.5 124.4 -8.7
 PRO-524   LYS-525  4.9 4.9 22.2 64.3 30.5 12.8 147.4
 LYS-525   LYS-526  2.8 3.4 -2.8 43.8 75.8 121.4 13.1
 LYS-526   SER-527  4.9 4.0 14.2 -45.2 65.8 84.7 -1.7
 SER-527   THR-528  6.2 4.4 -41.1 28.6 123.6 140.5 -7.3

Downloading Image

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