E1 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
 SER-279   ILE-280  7.5 9.5 24.3 -16.4 170.6 150.1 -20.0
 ILE-280   ASP-281  8.9 11.9 69.7 -7.5 97.0 79.2 0.5
 ASP-281   ILE-282  9.4 14.9 -19.5 -79.8 26.4 92.2 88.2
 ILE-282   PRO-283  12.1 17.6 12.4 -1.9 109.5 13.7 17.9
 PRO-283   GLU-284  13.3 19.7 -5.8 -7.7 87.3 108.4 -14.0
 GLU-284   ALA-285  17.1 19.4 34.4 -20.3 143.0 93.9 -14.6
 ALA-285   ALA-286  17.5 23.1 -18.7 -0.2 90.4 32.9 12.4
 ALA-286   PHE-287  17.0 22.9 6.3 4.8 62.2 86.6 24.1
 PHE-287   THR-288  20.0 20.8 -4.5 -31.1 60.3 121.3 -35.4
 THR-288   ARG-289  23.7 22.8 -24.1 -11.1 137.9 75.7 -70.9
 ARG-289   VAL-290  26.7 21.9 -2.2 -59.5 93.3 82.8 -19.8
 VAL-290   VAL-291  29.3 24.3 168.6 -62.7 126.4 75.6 244.8
 VAL-291   ASP-292  32.1 25.3 131.2 -38.1 160.5 102.2 -167.5
 ASP-292   ALA-293  29.9 28.1 113.8 -12.5 98.6 92.5 0.9
 ALA-293   PRO-294  29.5 29.0 -8.5 4.3 89.3 82.5 16.5

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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