Igm-Kappa Cold Agglutinin (Heavy 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  SER-84   VAL-85  12.9 13.0 9.3 -6.0 85.4 90.9 543.6  VAL-85   THR-86  11.6 11.4 15.4 -0.7 111.7 114.4 -375.2  THR-86   ALA-87  8.1 7.8 -8.1 5.5 86.6 85.5 -115.0  ALA-87   ALA-88  7.8 7.5 -0.7 -0.6 151.5 148.5 -119.8  ALA-88   ASP-89  7.9 7.8 2.3 4.3 77.3 74.0 81.6  ASP-89   THR-90  11.4 11.1 -1.2 -6.3 60.5 64.3 76.1 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

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-115   VAL-116  20.5 20.4 4.4 6.6 113.9 115.0 70.3  VAL-116   THR-117  17.8 17.7 -1.8 9.4 81.9 73.9 14.3  THR-117   VAL-118  14.7 14.7 -4.2 2.1 76.2 78.8 247.2 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