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
 ASN-328   ILE-329  10.2 12.0 132.0 -4.8 58.0 64.3 107.1
 ILE-329   THR-330  7.1 8.9 -5.8 -0.6 55.7 156.6 -4.0
 THR-330   ASN-331  7.4 8.7 134.8 143.0 52.7 64.8 -78.3
 ASN-331   LEU-332  6.2 6.3 -60.0 -1.8 66.5 62.8 49.6

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  0.5 1.0 -11.4 11.7 112.1 120.1 -6.4
 PRO-524   LYS-525  3.1 3.8 37.3 31.4 30.3 24.6 114.5
 LYS-525   LYS-526  4.1 3.8 149.4 -81.8 94.5 40.2 38.1
 LYS-526   SER-527  7.8 6.8 44.8 -81.0 82.7 107.1 8.8
 SER-527   THR-528  10.1 10.6 -11.9 -15.0 129.1 148.5 -32.0
 THR-528   ASN-529  12.9 13.1 -10.6 1.8 78.8 83.3 1.2

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