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  7.2 9.4 23.6 -15.5 172.0 150.8 -20.3
 ILE-280   ASP-281  8.6 11.8 69.1 -6.1 98.4 80.7 -1.6
 ASP-281   ILE-282  9.3 14.8 -19.7 -79.6 25.9 91.5 91.0
 ILE-282   PRO-283  11.9 17.6 12.7 -1.9 110.7 15.1 17.1
 PRO-283   GLU-284  13.1 19.6 -6.0 -7.4 86.5 108.7 -13.3
 GLU-284   ALA-285  16.9 19.4 33.3 -18.8 143.0 95.3 -14.6
 ALA-285   ALA-286  17.2 23.1 -18.7 -0.9 91.2 33.1 12.7
 ALA-286   PHE-287  16.7 22.8 6.2 5.7 62.7 86.0 23.1
 PHE-287   THR-288  19.7 20.6 -5.4 -31.0 59.2 120.8 -34.0
 THR-288   ARG-289  23.4 22.6 -24.1 -11.3 137.0 76.6 -70.8
 ARG-289   VAL-290  26.4 21.6 -1.4 -60.0 93.5 82.3 -19.6
 VAL-290   VAL-291  29.0 24.0 168.9 -62.7 127.3 74.6 239.1
 VAL-291   ASP-292  31.8 25.0 130.6 -37.4 159.2 102.8 -167.4
 ASP-292   ALA-293  29.6 27.8 113.6 -12.4 97.5 91.2 5.6
 ALA-293   PRO-294  29.2 28.6 -7.6 4.4 89.1 82.1 16.0

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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