33 Kda Early Protein

(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-119   SER-120  10.0 10.0 -0.2 -7.6 52.1 56.7 26.4
 SER-120   VAL-121  7.9 7.8 12.6 -7.0 80.5 82.1 17.6
 VAL-121   VAL-122  4.1 4.1 0.5 0.0 143.4 143.4 -5.6
 VAL-122   LYS-123  1.9 1.8 14.2 -11.5 81.5 81.3 23.9

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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