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
 VAL-314   ARG-315  3.7 4.0 0.3 -1.4 42.2 42.1 -2.1
 ARG-315   PHE-316  4.5 5.2 54.7 -43.2 31.0 31.7 25.8
 PHE-316   PRO-317  3.6 4.6 13.1 6.0 51.9 52.1 15.3
 PRO-317   ASN-318  5.5 6.6 14.2 5.7 72.4 80.7 20.9
 CYS-323   PRO-324  9.1 8.6 -29.4 6.7 143.0 137.3 -24.2
 PRO-324   PHE-325  10.4 10.1 79.8 -61.0 101.8 105.2 6.0

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
 VAL-510   CYS-511  3.2 4.3 -2.6 10.7 168.5 166.0 21.0
 CYS-511   GLY-512  4.3 4.8 -24.2 13.3 96.8 113.1 -0.2
 THR-517   ASP-518  9.2 9.2 -37.8 -33.4 94.3 88.8 -19.1
 ASP-518   LEU-519  10.8 10.6 17.1 16.5 59.2 33.2 38.2
 LEU-519   ILE-520  10.1 10.6 5.0 -8.1 23.1 21.7 -16.3
 ILE-520   LYS-521  10.4 10.6 23.4 -24.2 73.0 70.8 2.0
 LYS-521   ASN-522  12.1 12.0 7.2 -1.7 8.7 6.1 8.2
 ASN-522   GLN-523  12.4 12.2 7.4 1.7 51.8 54.2 7.8

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