Lysine Acetyltransferase

(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  PRO-160   VAL-161  3.7 3.6 -0.3 -10.2 18.4 11.9 7.6  VAL-161   LEU-162  3.4 3.9 5.5 -22.1 89.1 108.3 -1.3  LEU-162   PRO-163  0.5 0.9 -5.2 2.7 35.7 14.5 5.2  PRO-163   GLY-164  2.9 1.1 -161.2 -167.5 31.9 56.4 -19.3  GLY-164   ASP-165  1.7 2.6 1.4 0.9 97.4 90.3 1.6  ASP-165   ARG-166  2.1 4.9 -166.8 8.5 60.5 34.9 152.2  ARG-166   GLU-167  4.9 5.0 -29.7 7.0 123.9 53.0 -1.3  GLU-167   ARG-168  7.2 5.3 -25.6 7.2 103.2 109.0 -20.5  ARG-168   THR-169  6.6 8.2 5.0 25.8 132.0 100.7 1.7  THR-169   VAL-170  8.3 10.0 -42.1 45.6 67.7 14.9 -3.9 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

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-201   VAL-202  6.8 6.0 130.7 -35.3 156.5 124.7 339.7  VAL-202   ASP-203  7.8 8.1 169.1 -8.5 139.2 131.3 -151.7  ASP-203   TYR-204  9.5 9.8 -130.4 173.4 58.9 19.5 -59.5  TYR-204   VAL-205  8.4 8.5 -12.5 -9.4 57.6 46.6 14.3 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