Phosphoglucosamine Mutase

(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-368   PHE-369  4.3 4.3 -11.7 -17.0 126.5 128.0 -35.6  PHE-369   PRO-370  2.1 1.2 4.1 16.4 83.6 101.4 14.9  PRO-370   GLN-371  2.0 2.7 -3.2 -39.9 42.1 25.8 154.6  GLN-371   LEU-372  4.2 4.5 -20.1 22.4 96.4 89.9 -46.8 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

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  LEU-408   VAL-409  10.0 10.1 -7.1 10.6 103.5 100.0 12.8  VAL-409   ARG-410  12.4 12.7 -2.7 16.9 176.2 178.1 42.2  ARG-410   PRO-411  12.3 12.6 8.7 36.7 70.4 67.4 51.9  PRO-411   SER-412  13.0 13.5 -39.6 59.7 134.2 99.3 64.8  SER-412   GLY-413  11.6 11.6 89.9 -125.5 42.6 25.5 -95.0  GLY-413   THR-414  13.0 11.2 -20.9 -62.3 85.3 114.3 -21.5  THR-414   GLU-415  13.0 12.8 63.8 -24.6 113.2 118.4 -145.0  GLU-415   PRO-416  15.7 15.4 11.3 -3.0 92.5 97.4 -7.4  PRO-416   LEU-417  17.1 18.4 55.2 -48.2 140.3 164.0 46.8  LEU-417   ILE-418  16.7 16.8 -1.5 -2.9 73.9 88.1 45.1 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