Fusion Glycoprotein F0

(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-172   SER-173  8.1 9.4 -8.6 32.9 53.8 62.0 -10.9
 SER-173   THR-174  4.7 8.4 -13.5 77.4 108.6 80.7 3.1
 THR-174   ASN-175  2.6 4.6 135.1 54.6 52.8 149.7 10.3
 ASN-175   LYS-176  4.8 5.1 -44.6 82.2 162.6 39.2 -37.4
 LYS-176   ALA-177  2.6 6.4 -152.9 86.4 95.6 80.2 -14.6
 ALA-177   VAL-178  2.2 4.7 167.3 17.3 18.7 120.0 101.6
 VAL-178   VAL-179  3.8 1.1 -150.5 43.9 83.5 18.4 -109.9
 VAL-179   SER-180  7.2 2.9 -176.4 28.8 154.7 58.3 67.9
 SER-180   LEU-181  9.6 4.8 -162.4 19.1 99.3 83.6 57.6
 LEU-181   SER-182  11.4 4.3 164.0 -4.8 62.2 132.0 -88.1
 SER-182   ASN-183  14.9 1.8 -27.0 32.6 175.4 19.1 -0.4
 ASN-183   GLY-184  13.8 2.6 -39.0 -170.3 105.9 77.7 4.6
 GLY-184   VAL-185  11.6 6.0 -34.4 18.7 84.0 74.8 -3.0
 VAL-185   SER-186  8.1 6.3 -150.9 16.9 15.2 26.9 89.9
 SER-186   VAL-187  6.3 4.2 -163.5 39.9 82.3 40.7 -138.1
 VAL-187   LEU-188  4.5 6.2 -178.8 23.7 28.0 89.4 67.5
 LEU-188   THR-189  2.5 9.3 -178.0 67.2 66.4 64.6 39.6
 THR-189   PHE-190  5.2 9.1 173.2 72.2 139.2 172.8 -160.8

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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