Pyruvate Kinase Isozymes M1/m2

(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  THR-113   LYS-114  7.6 7.6 -2.4 0.9 55.7 57.3 -3.4  LYS-114   GLY-115  6.6 6.7 -2.9 -8.2 76.4 75.8 3.5  GLY-115   PRO-116  2.8 3.0 17.0 -0.1 87.2 98.5 -7.1  PRO-116   GLU-117  3.4 3.5 -64.4 26.7 30.8 38.5 120.8  GLU-117   ILE-118  6.3 6.0 -11.3 9.6 98.4 100.1 -14.0 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  ASP-216   LEU-217  10.3 9.9 5.4 -11.5 130.4 133.5 12.9  LEU-217   PRO-218  7.3 7.1 5.9 -2.0 119.7 108.2 -7.8  PRO-218   ALA-219  5.4 4.8 1.4 -15.2 61.6 59.3 -7.2  ALA-219   VAL-220  4.2 3.2 2.9 -0.4 103.2 121.4 8.6  VAL-220   SER-221  1.5 1.5 -21.5 -6.3 61.1 50.6 62.5  SER-221   GLU-222  2.3 2.1 7.0 -11.4 152.1 146.7 8.9  GLU-222   LYS-223  3.9 3.2 2.5 -0.8 85.1 78.4 -8.5  LYS-223   ASP-224  6.3 6.0 1.3 -6.8 80.3 68.3 7.4  ASP-224   ILE-225  4.7 4.6 11.6 -9.9 145.3 138.4 -8.0  ILE-225   GLN-226  4.3 4.2 4.5 -5.0 113.2 114.0 0.3 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