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-331   ILE-332  7.9 8.4 50.7 52.6 39.4 58.7 99.3
 ILE-332   THR-333  4.6 5.7 -27.4 12.5 77.2 149.8 -7.6
 THR-333   ASN-334  4.1 6.4 -34.2 -18.2 127.1 128.0 -44.2
 ASN-334   LEU-335  3.0 3.6 -19.3 -7.7 74.2 74.3 14.5
 LEU-335   CYS-336  4.2 5.0 29.3 16.1 37.3 48.1 45.7
 CYS-336   PRO-337  5.5 6.2 -1.2 6.6 76.5 115.4 -17.1

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  4.0 4.5 -12.6 4.5 95.9 109.3 -3.8
 PRO-527   LYS-528  2.6 2.0 149.6 -28.5 49.4 22.2 170.3
 LYS-528   LYS-529  0.3 0.6 -37.6 63.8 62.6 110.7 17.5
 LYS-529   SER-530  3.9 3.4 24.7 -91.3 42.1 72.0 -46.2
 SER-530   THR-531  7.0 6.2 -12.8 10.3 143.3 141.3 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