Eiav Capsid Protein P26

(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
 ILE-145   GLY-146  5.0 4.7 174.1 157.2 100.0 95.5 -6.4
 GLY-146   LYS-147  1.5 2.3 -7.8 45.2 137.3 119.6 22.8
 LYS-147   PRO-148  1.8 1.0 76.9 6.6 43.9 33.6 70.6
 PRO-148   LYS-149  1.7 2.5 44.1 -19.3 25.0 36.8 32.4
 LYS-149   ALA-150  1.2 1.0 -157.7 131.5 123.9 144.6 -27.3

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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