Monoclonal Antibody 2D12.5, Lambda Light Chain

(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-107   VAL-108  16.2 16.3 -1.4 -8.9 143.5 140.7 -31.7
 VAL-108   LEU-109  17.1 17.5 0.5 1.8 41.6 38.6 -29.2
 LEU-109   GLY-110  16.9 16.4 13.8 6.7 28.4 48.7 63.3
 GLY-110   GLN-111  15.6 15.5 5.3 0.0 85.2 100.3 17.2
 GLN-111   PRO-112  12.7 12.9 21.5 -12.3 56.2 42.2 2.2
 PRO-112   LYS-113  9.9 10.6 -32.6 -13.8 63.2 73.5 75.4
 LYS-113   SER-114  6.6 7.0 0.6 -0.8 82.8 72.5 38.4
 SER-114   SER-115  4.0 4.0 15.2 -18.7 106.1 106.6 -24.1

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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