Serum Albumin

(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  ALA-194   LYS-195  14.4 14.6 10.6 -7.3 12.4 7.7 0.6  LYS-195   GLN-196  12.5 12.8 10.4 -1.7 72.5 69.0 11.1  GLN-196   ARG-197  12.2 12.8 -6.5 -13.4 89.5 95.8 -8.8  ARG-197   LEU-198  15.9 16.5 4.5 5.4 30.5 42.2 21.3  LEU-198   LYS-199  16.7 17.0 -0.1 2.8 134.4 153.6 23.9  LYS-199   CYS-200  14.9 15.4 -7.2 4.4 80.3 100.0 -15.4  CYS-200   ALA-201  17.4 18.1 -10.1 2.9 103.8 96.4 -5.9  ALA-201   SER-202  20.3 21.0 0.8 -2.2 7.3 30.0 -19.4  SER-202   LEU-203  19.6 20.2 0.4 12.0 70.8 40.3 50.3  LEU-203   GLN-204  19.6 19.8 -3.0 20.1 77.3 88.7 -4.3  GLN-204   LYS-205  22.7 23.3 -26.4 36.3 105.6 110.5 23.8 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