Mannan-Binding Lectin Serine Protease 2

(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  CYS-430   GLU-431  6.6 6.5 -2.2 9.4 140.5 141.6 56.9  GLU-431   PRO-432  3.9 4.0 1.1 -2.7 107.7 105.1 24.0  PRO-432   VAL-433  0.4 0.5 1.6 -6.1 92.5 92.7 -3.3 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