Tyrosine-Protein Kinase Fyn

(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  LYS-25   PHE-26  11.0 10.7 17.5 3.9 61.9 56.7 188.3  PHE-26   GLN-27  7.9 7.9 -14.2 32.6 141.0 156.8 68.5  GLN-27   ILE-28  7.2 7.3 -16.5 13.0 98.8 96.6 12.3  ILE-28   LEU-29  5.7 5.9 -2.0 1.2 161.4 143.2 5.5  LEU-29   ASN-30  3.4 2.8 -7.9 -2.7 108.6 110.5 -34.8 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