Capsid Protein P24

(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
 MET-144   TYR-145  5.0 5.3 -30.2 13.9 79.1 80.9 1.8
 TYR-145   SER-146  3.2 3.2 13.9 16.1 31.2 42.3 11.2
 SER-146   PRO-147  3.7 3.8 -22.3 -13.7 114.0 100.5 -6.0
 PRO-147   THR-148  1.9 3.1 -167.9 -62.0 136.9 155.0 72.9
 THR-148   SER-149  1.4 3.2 37.5 5.2 23.0 47.9 23.0
 SER-149   ILE-150  0.3 1.0 17.9 11.4 54.4 46.0 10.5
 ILE-150   LEU-151  3.1 3.3 -3.2 -5.4 142.8 136.4 -3.2

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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