Nopaline-Binding Periplasmic 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
 TYR-112   LEU-113  9.9 10.0 -4.3 -2.7 147.0 152.1 -13.1
 LEU-113   LEU-114  7.1 7.4 -13.5 44.6 68.5 76.5 -9.1
 LEU-114   THR-115  4.5 4.8 23.3 36.6 37.4 52.0 93.6
 THR-115   PRO-116  1.9 1.3 -61.8 10.3 71.3 111.0 37.5
 PRO-116   MET-117  3.8 3.6 -29.2 -4.5 115.5 116.0 -18.6
 MET-117   THR-118  5.6 5.5 3.1 4.0 52.5 54.4 6.4

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
 LEU-234   PHE-235  8.1 8.2 1.5 -11.2 126.0 126.9 17.2
 PHE-235   GLY-236  5.5 5.4 21.7 9.7 63.0 66.3 19.6
 GLY-236   LYS-237  2.6 2.7 -35.5 67.1 54.0 84.4 -14.7
 LYS-237   GLY-238  1.2 2.1 -136.9 26.9 76.5 40.6 110.4
 GLY-238   VAL-239  3.1 2.6 24.6 12.8 96.6 78.6 -29.4
 VAL-239   GLY-240  5.7 5.7 10.0 0.4 58.1 55.7 -0.4
 GLY-240   VAL-241  8.6 8.4 -2.2 1.8 92.3 93.3 -0.9

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