Major Envelope Protein E

(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
 ALA-263   LEU-264  3.9 3.4 -6.1 -5.6 9.0 11.6 32.3
 LEU-264   THR-265  3.4 3.5 55.8 -42.5 121.1 112.2 -32.0
 THR-265   GLY-266  7.0 6.8 -3.9 -12.3 36.6 12.9 38.4

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
 LEU-283   LYS-284  1.6 1.7 2.0 12.9 23.5 27.5 34.9
 LYS-284   CYS-285  1.4 2.6 12.7 -13.9 46.6 47.7 9.8
 CYS-285   ARG-286  2.5 2.5 7.5 -2.3 25.5 27.8 -27.9

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