Lambda III Bence Jones Protein Cle

(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
 THR-105   VAL-106  5.9 5.4 -0.6 -13.2 9.2 13.4 9.1
 VAL-106   LEU-106A  5.5 5.4 -5.4 -29.1 79.4 65.0 9.4
 LEU-106A   GLY-107  2.8 2.8 -5.1 -116.6 91.7 55.3 44.2
 GLY-107   GLN-108  1.1 1.8 46.9 77.7 82.1 67.8 30.4
 GLN-108   PRO-109  4.4 4.7 -17.4 -8.1 78.4 79.2 1.7
 PRO-109   LYS-110  7.1 7.4 -19.6 25.0 142.7 143.9 0.3

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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