Aspartate Aminotransferase

(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
 VAL-8   GLN-9  24.9 25.2 -7.4 -1.9 110.5 105.1 -13.5
 GLN-9   ALA-10  25.0 25.3 2.4 11.5 112.4 120.9 -16.3
 ALA-10   MET-11  22.1 22.6 21.5 -7.2 67.9 64.7 -4.2
 MET-11   LYS-12  19.9 20.0 -7.4 20.6 149.2 118.5 5.2
 LYS-12   PRO-13  17.1 17.5 30.8 -12.8 61.4 16.9 48.9
 PRO-13   SER-14  17.2 16.7 -28.1 -31.3 98.7 94.8 -5.9
 SER-14   ALA-15  14.1 13.1 19.7 -6.5 52.2 56.7 28.9
 ALA-15   THR-16  11.2 10.9 13.6 1.0 52.3 39.9 42.4

Downloading Image

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-32   LEU-33  0.8 0.7 30.3 12.4 18.4 18.2 120.5
 LEU-33   VAL-34  0.7 0.6 -10.8 -0.9 115.5 108.1 -33.8
 VAL-34   ALA-35  3.2 3.3 -3.7 3.8 149.7 155.3 0.2

Downloading Image

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