Tyrosine-Protein Kinase Syk

(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-369   LEU-370  3.6 3.9 -1.2 -5.5 38.6 43.5 159.4
 LEU-370   THR-371  0.6 0.6 0.7 -2.1 86.9 87.1 -62.2
 THR-371   LEU-372  4.0 3.8 2.0 3.7 131.9 129.2 -83.2
 LEU-372   GLU-373  6.0 6.0 -10.7 -10.3 70.5 69.0 -25.9
 GLU-373   ASP-374  8.9 8.5 23.2 -12.2 73.7 89.2 38.0
 ASP-374   LYS-375  12.4 12.1 30.7 -9.0 135.1 143.9 -350.3
 LYS-375   GLU-376  13.3 11.2 -39.9 20.2 85.9 98.4 -113.9
 GLU-376   LEU-377  12.8 12.5 -31.0 5.2 14.4 23.0 495.4

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
 VAL-399   ALA-400  2.2 2.5 2.5 3.6 83.5 87.4 45.5
 ALA-400   VAL-401  5.4 5.8 1.0 3.5 145.1 146.2 -32.9
 VAL-401   LYS-402  7.3 7.5 1.7 2.4 93.2 93.5 -58.2

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