Tt1252 Protein

(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
 ALA-43   ARG-44  9.5 9.6 16.8 -2.5 56.5 46.9 103.7
 ARG-44   ALA-45  6.8 7.0 14.1 -17.6 122.8 119.7 -1.3
 ALA-45   ARG-46  4.5 5.2 8.7 -9.7 107.6 109.4 -86.4
 ARG-46   GLU-47  7.9 8.7 3.0 3.9 46.2 44.1 64.8
 GLU-47   ASN-48  9.1 9.8 3.0 -6.8 77.4 80.6 1.6
 ASN-48   LYS-49  7.1 7.7 6.0 -0.4 133.7 139.4 -49.2
 LYS-49   GLU-50  8.5 9.1 -34.8 20.5 71.5 76.5 143.8

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
 HIS-90   PRO-91  1.7 2.0 3.8 -7.5 117.8 117.8 3.5
 PRO-91   GLU-92  2.0 1.6 0.0 -2.4 6.3 6.7 38.5
 GLU-92   VAL-93  1.4 1.2 6.3 -8.1 108.8 112.7 7.3

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