Biotin Carboxylase

(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
 VAL-128   PRO-129  10.1 10.6 3.5 -7.5 112.8 108.8 -8.1
 PRO-129   CYS-130  7.5 7.9 -9.4 10.4 66.0 65.9 24.3
 CYS-130   VAL-131  4.8 5.3 3.2 -10.6 117.3 122.3 0.9
 VAL-131   PRO-132  1.8 2.7 27.3 -15.6 48.6 44.0 23.0
 PRO-132   GLY-133  1.5 1.2 -28.5 17.8 81.3 82.7 14.3

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


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-203   LEU-204  3.9 4.6 4.7 6.6 63.1 60.9 3.4
 LEU-204   GLU-205  0.5 1.5 33.8 -0.5 17.0 8.6 66.4
 GLU-205   ASN-206  1.5 1.4 -12.9 8.2 126.9 125.6 -0.5
 ASN-206   PRO-207  2.1 2.0 -3.1 -11.0 60.8 58.6 22.7

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