Aminopeptidase T

(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  PHE-174   GLN-175  1.6 1.6 1.3 -1.0 116.1 115.7 1.8  GLN-175   ALA-176  4.6 4.6 0.9 -1.4 161.5 161.7 0.5  ALA-176   THR-177  4.0 4.0 0.9 -2.0 126.3 125.9 3.2  PRO-184   ILE-185  9.8 9.6 -35.2 64.2 21.2 29.2 -111.2  ILE-185   ALA-186  11.1 11.1 1.7 -2.0 122.5 122.2 -2.0  ALA-186   ALA-187  13.4 13.4 0.1 0.8 94.9 95.5 -1.3 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