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-330   ASN-331  8.0 9.0 -19.4 33.6 99.4 104.2 -7.8
 ASN-331   ILE-332  7.9 9.4 67.8 44.6 28.8 30.4 128.3
 ILE-332   THR-333  5.2 6.6 -10.0 50.4 78.6 160.8 34.8
 THR-333   ASN-334  5.4 6.5 -136.7 11.9 125.4 126.2 -101.2
 ASN-334   LEU-335  3.6 5.4 -21.3 30.8 63.4 63.6 4.8

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


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-526   PRO-527  3.0 3.9 11.2 -5.9 81.6 74.7 -13.7
 PRO-527   LYS-528  2.4 3.2 62.0 19.1 30.1 28.4 106.5
 LYS-528   LYS-529  1.6 1.8 -34.3 33.4 76.6 117.2 23.6
 LYS-529   SER-530  5.3 4.5 25.2 -72.8 65.9 71.7 -25.7
 SER-530   THR-531  7.7 7.4 -11.2 22.2 126.1 124.5 3.6

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