N-Ethylmaleimide Sensitive Fusion Protein (Nsf)
(All numbering and residues are taken from first PDB file)
Bending Residue Dihedral Analysis
Residue
iResidue
i+1Distance of hinge axis to residue i in
(A) Distance of hinge axis to residue i in
(A) Change in
(deg) Change in
(deg) Angle of psi(i) axis to hinge axis
(deg) Angle of psi(i) axis to hinge axis
(deg) Percentage Progress
SER-84
PHE-85
8.8
9.0
-2.5
14.9
37.4
40.8
-173.6
PHE-85
ASP-86
10.4
10.2
36.8
48.3
81.2
86.0
53.3
ASP-86
LYS-87
14.1
13.8
72.7
74.7
113.8
159.0
2116.0
LYS-87
ALA-88
15.7
14.5
-152.2
-32.3
8.6
54.2
-2065.4
ALA-88
LYS-89
16.7
17.6
23.1
-65.0
119.7
118.7
223.6
LYS-89
GLN-90
15.3
15.8
3.1
-30.3
91.5
108.8
126.5
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