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
 GLY-127   VAL-128  10.2 10.4 -6.4 0.5 11.5 1.7 3.9
 VAL-128   PRO-129  10.0 10.2 -3.5 4.1 67.3 67.7 9.4
 PRO-129   CYS-130  7.5 7.5 0.5 -1.1 113.8 112.3 -0.3
 CYS-130   VAL-131  4.7 5.1 -8.7 -4.3 62.8 66.0 13.0
 VAL-131   PRO-132  1.6 2.3 17.6 4.6 48.5 48.8 28.5
 PRO-132   GLY-133  1.8 1.4 -41.2 32.1 81.5 82.9 19.0

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  4.0 4.7 -9.1 27.8 117.1 123.1 12.5
 LEU-204   GLU-205  0.7 1.4 41.2 -2.9 17.2 12.6 73.7
 GLU-205   ASN-206  1.7 1.8 -11.2 4.4 127.1 124.7 -0.3
 ASN-206   PRO-207  2.1 1.5 -6.4 6.4 61.0 66.1 9.7
 PRO-207   ARG-208  4.7 4.5 4.1 -9.4 63.2 59.4 -0.7

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