Maltose-Binding Periplasmic Protein

(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  GLU-181   ASN-182  7.0 4.7 4.8 -120.5 79.3 42.6 -33.4  ASN-182   GLY-183  6.2 3.7 102.1 -139.3 84.7 108.9 -13.6  GLY-183   LYS-184  9.9 2.4 109.9 36.9 141.2 100.4 -44.4  LYS-184   TYR-185  11.1 5.7 25.8 -2.2 104.5 76.1 2.7 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