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
 PHE-329   PRO-330  7.5 10.4 4.9 -4.2 41.3 44.0 7.9
 PRO-330   ASN-331  8.5 11.8 22.3 33.5 93.5 79.3 9.2
 ASN-331   ILE-332  9.6 12.1 63.6 35.5 36.3 64.8 91.9
 ILE-332   THR-333  7.5 9.0 -115.6 40.1 72.1 157.0 -46.4
 THR-333   ASN-334  8.2 9.8 169.4 141.0 52.9 60.5 -39.6
 ASN-334   LEU-335  6.6 7.2 -76.8 6.2 60.4 69.2 59.6
 LEU-335   CYS-336  6.5 6.1 10.3 -2.0 52.2 38.5 11.1
 CYS-336   PRO-337  5.3 5.2 10.2 1.0 70.7 78.7 12.5

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
 CYS-525   GLY-526  1.8 2.5 -3.8 4.2 112.3 111.5 -21.3
 GLY-526   PRO-527  1.4 1.7 -13.1 7.6 103.0 102.5 -6.3
 PRO-527   LYS-528  4.1 3.3 89.5 6.0 29.1 22.6 138.7
 LYS-528   LYS-529  3.6 4.4 -10.2 -10.3 80.6 105.2 -5.1
 LYS-529   SER-530  7.1 7.3 -12.8 -10.2 108.8 125.8 -19.3
 SER-530   THR-531  8.7 9.9 -5.4 10.9 134.2 136.5 6.5
 THR-531   ASN-532  11.3 11.9 0.1 2.1 107.6 94.8 2.3
 ASN-532   LEU-533  14.9 15.6 -0.3 -4.9 109.4 113.0 -0.1

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