Serine/threonine-Protein Kinase Mtor

(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  LEU-2209   ALA-2210  4.7 4.7 0.4 -1.5 43.6 44.3 -132.9  ALA-2210   ASN-2211  2.9 2.9 2.1 -1.2 60.2 60.4 25.7  ASN-2211   ASP-2212  6.6 6.7 -0.4 -0.6 126.5 127.0 -53.2  ASP-2212   PRO-2213  7.9 7.9 2.1 -1.2 37.1 39.3 213.3  PRO-2213   THR-2214  6.8 6.7 1.1 -1.2 82.3 82.5 -2.8  THR-2214   SER-2215  7.7 7.7 1.3 -1.5 129.1 129.6 -38.9  SER-2215   LEU-2216  6.2 6.1 0.5 -0.5 77.9 77.9 130.3 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

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-2220   SER-2221  5.9 5.9 -0.6 1.8 136.5 137.0 97.4  SER-2221   ILE-2222  4.6 4.6 0.1 0.0 36.4 36.5 1.8  ILE-2222   GLN-2223  5.6 5.6 -2.1 0.5 98.7 98.9 -106.3  GLN-2223   ARG-2224  7.6 7.6 0.5 -0.4 14.7 14.1 71.3 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