Nickel-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
 LEU-1242   SER-1243  9.7 9.4 -7.4 1.6 37.0 37.0 59.1
 SER-1243   GLN-1244  10.1 9.5 -11.3 0.1 88.5 92.9 -13.5
 GLN-1244   PRO-1245  9.6 8.3 -11.0 -3.6 73.5 65.2 10.7
 PRO-1245   ILE-1246  6.2 4.7 2.7 4.9 149.2 167.8 -42.1
 ILE-1246   GLU-1247  4.3 3.6 -5.4 -2.4 68.8 63.3 18.2
 GLU-1247   THR-1248  0.9 0.3 20.2 12.7 55.2 49.5 104.7
 THR-1248   VAL-1249  3.7 3.8 1.9 -13.9 76.1 72.8 -24.2

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


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
 SER-1468   TYR-1469  5.7 5.3 -2.2 10.7 138.9 140.0 25.5
 TYR-1469   ILE-1470  3.7 3.1 3.5 -30.3 117.1 117.7 46.8
 ILE-1470   SER-1471  1.3 0.7 20.0 -4.8 73.0 67.6 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