Arginine Repressor/activator 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
 PRO-72   LEU-73  5.9 6.1 -19.8 10.2 43.6 45.1 57.3
 LEU-73   SER-74  3.3 3.3 -14.3 10.2 32.4 35.0 33.4
 SER-74   LYS-75  6.2 6.3 7.0 -5.9 123.3 128.4 -1.7
 LYS-75   LEU-76  7.5 7.4 -10.3 8.3 62.9 58.2 17.7
 LEU-76   LYS-77  4.4 4.4 -4.0 7.1 30.5 36.8 -15.8

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
 MET-110   ASP-111  6.5 6.7 1.1 2.5 165.9 159.1 -22.0
 ASP-111   ASN-112  8.4 8.9 11.3 -33.2 127.0 134.8 93.6
 ASN-112   LEU-113  6.6 6.6 9.2 27.3 99.7 88.6 6.3
 LEU-113   ASP-114  3.2 3.2 3.3 21.7 136.2 147.5 -133.3
 ASP-114   TRP-115  5.4 3.8 -6.4 -34.8 89.5 99.5 -43.3

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