Myosin Light Chain Kinase, Green Fluorescent Protein, Calmodulin Chimera

(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-329   ILE-330  4.9 5.3 -5.1 15.4 117.8 111.8 -10.9
 ILE-330   THR-331  1.4 2.0 -16.9 -26.6 42.7 56.4 51.5
 THR-331   THR-332  3.7 4.8 -1.7 29.0 66.5 90.4 20.5
 THR-332   LYS-333  4.2 6.8 4.9 -24.3 69.2 21.9 -18.5
 LYS-333   GLN-334  7.5 8.2 0.1 -7.2 49.6 54.7 -0.8
 GLN-334   LEU-335  5.4 4.8 -15.2 -21.9 76.9 75.2 36.5

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
 ILE-355   ASN-356  4.0 3.7 2.3 26.5 30.4 20.8 36.9
 ASN-356   GLU-357  3.4 3.6 13.3 -8.9 62.1 68.7 0.8
 GLU-357   VAL-358  4.9 5.0 32.2 -58.8 109.8 99.6 7.3
 GLY-364   THR-365  5.8 5.7 39.8 -47.4 132.9 156.5 4.0
 THR-365   ILE-366  4.4 3.9 17.4 22.3 68.9 81.3 16.9

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