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-46   LYS-47  4.2 1.7 -33.9 70.8 55.9 51.8 -11.3
 LYS-47   SER-48  6.2 2.9 140.1 1.7 141.1 83.2 -61.9
 SER-48   HIS-49  4.2 5.5 -177.8 -66.4 74.4 44.5 173.3
 HIS-49   LYS-50  7.2 6.2 142.3 -7.2 86.4 73.2 1.8
 LYS-50   ALA-51  9.6 9.5 -158.4 45.1 25.3 107.1 -196.8
 ALA-51   ILE-52  10.0 10.8 130.7 28.0 116.7 127.0 184.1
 ILE-52   GLN-53  10.6 10.8 -18.4 31.3 108.0 84.1 10.2

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


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-173   LYS-174  11.9 13.2 -140.1 -4.7 90.4 87.4 87.5
 LYS-174   GLY-175  9.7 11.4 129.8 9.5 147.6 21.7 -21.0
 GLY-175   LEU-176  8.2 11.6 -165.6 -1.3 66.9 108.2 -28.4
 LEU-176   CYS-177  5.9 9.6 -2.4 35.8 82.3 63.7 -14.3
 CYS-177   ASP-178  4.7 6.9 -39.1 -7.3 140.5 115.2 -14.7
 ASP-178   SER-179  5.7 7.2 9.3 45.6 71.4 27.3 23.1
 SER-179   ASN-180  2.5 5.5 168.2 -29.9 133.1 101.2 178.3
 ASN-180   LEU-181  4.3 2.2 -123.2 -50.0 68.0 50.7 -78.0

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