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   MET-280  9.2 7.8 -25.3 17.9 147.7 165.7 -17.9  MET-280   ASN-281  11.6 9.4 -70.3 7.0 77.4 93.3 10.0  ASN-281   LEU-282  14.6 9.6 23.1 73.9 96.7 32.6 66.9  LEU-282   PRO-283  17.3 12.7 -13.7 1.9 9.2 104.3 19.9  PRO-283   ASP-284  19.1 13.9 7.8 9.9 109.5 92.8 -20.2  ASP-284   SER-285  18.7 17.7 -40.1 23.5 89.5 138.6 -10.1  SER-285   ALA-286  22.5 18.4 17.7 0.6 35.2 90.0 13.9  ALA-286   PHE-287  22.6 18.0 -8.5 -4.7 87.9 57.4 27.7  PHE-287   THR-288  20.5 20.8 7.6 36.2 124.3 66.2 -41.8  THR-288   ARG-289  22.6 24.5 20.6 8.9 74.1 139.6 -58.9  ARG-289   ILE-290  21.8 27.1 2.2 60.3 85.8 92.3 -11.7  ILE-290   VAL-291  24.4 30.1 -164.6 59.9 77.9 127.9 241.1  VAL-291   GLU-292  25.4 32.6 -129.9 31.5 99.5 157.3 -168.0  GLU-292   ALA-293  28.4 30.3 -119.3 12.3 94.9 96.5 -5.6  ALA-293   PRO-294  29.3 29.9 7.3 -6.3 85.2 91.5 12.0 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