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  3.6 3.7 2.2 -7.5 14.5 13.7 -13.5
 VAL-108   LEU-109  2.1 2.0 -3.5 8.2 89.5 87.1 10.3
 LEU-109   GLY-110  5.2 4.9 -72.9 174.4 124.5 118.7 103.2
 GLY-110   GLN-111  6.8 5.5 -12.6 -88.4 61.7 90.6 111.2
 GLN-111   PRO-112  6.8 9.2 11.5 15.6 94.3 93.8 6.3
 PRO-112   LYS-113  10.5 11.9 30.7 12.8 156.1 154.2 -109.0
 LYS-113   SER-114  12.2 12.5 5.0 -7.0 111.8 115.8 2.0
 SER-114   SER-115  14.3 14.8 -7.2 17.4 34.0 31.5 -8.3

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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