Interleukin-10-Like 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
 CYS-114   GLY-116  6.1 6.4 20.5 11.6 83.0 81.4 88.5
 GLY-116   ASP-117  6.6 6.9 -97.8 81.0 80.5 61.9 65.9
 ASP-117   LYS-118  5.1 5.5 -39.6 43.7 38.8 38.6 -26.3
 LYS-118   SER-119  7.5 7.2 -2.7 -15.5 104.9 101.4 -41.0
 SER-119   VAL-120  10.7 10.5 -0.4 1.6 102.4 101.6 -18.7

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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