Protein (Aspartate Carbamoyltransferase)

(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-140   ASP-141  4.1 4.1 7.4 -4.5 86.4 89.3 -27.7
 ASP-141   LEU-142  3.3 3.2 9.3 -2.4 31.0 32.3 31.7
 LEU-142   PHE-143  2.6 2.1 -11.5 10.1 91.2 85.1 12.6
 PHE-143   THR-144  1.7 2.0 -10.3 1.7 62.3 57.3 -6.8

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
 ALA-289   GLY-290  2.3 2.3 -24.1 14.7 80.3 77.8 32.9
 GLY-290   ASN-291  5.3 5.1 7.9 -10.9 159.4 159.1 8.2
 ASN-291   GLY-292  5.0 5.0 11.9 -7.4 99.5 102.7 -3.8

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