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  6.8 6.9 169.8 167.3 73.3 68.8 -14.9
 GLY-146   LYS-147  6.8 6.8 -26.5 70.2 109.7 93.9 9.1
 LYS-147   PRO-148  3.5 3.6 73.0 17.6 30.4 20.5 157.7
 PRO-148   LYS-149  3.7 3.4 -120.1 33.3 124.1 118.9 -73.0
 LYS-149   ALA-150  0.5 0.6 -86.0 123.2 158.2 138.8 51.2
 ALA-150   GLN-151  1.0 1.1 -76.9 20.5 98.0 110.4 -43.8

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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