Envelope 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
 LEU-264   THR-265  3.3 3.3 -26.7 17.8 123.4 124.5 -53.4
 THR-265   GLY-266  6.6 6.8 6.7 -7.2 34.6 38.1 1.0
 GLY-266   ALA-267  6.4 6.8 18.8 -27.7 53.6 51.3 -29.7

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
 LYS-284   CYS-285  3.1 3.2 -18.5 17.7 52.2 48.7 4.8
 CYS-285   ARG-286  4.2 4.4 -12.2 7.4 25.3 24.7 14.9
 ARG-286   LEU-287  4.6 4.9 -18.8 11.6 52.5 52.6 10.0

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