Interleukin-10

(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-112   PRO-113  6.3 7.2 2.7 2.5 93.3 98.7 -0.2
 PRO-113   CYS-114  3.7 5.2 -35.7 46.6 41.9 33.4 -4.5
 CYS-114   GLU-115  1.5 2.6 -172.1 3.8 29.2 27.9 85.6
 LYS-117   SER-118  9.8 8.3 -43.3 35.6 120.3 121.1 -5.8
 SER-118   LYS-119  12.0 10.8 -2.3 -0.8 65.3 61.1 200.6

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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