Nicotinamide Phosphoribosyltransferase
(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-241
VAL-242
11.2
11.2
-4.5
7.3
103.2
102.0
4.1
VAL-242
PRO-243
7.7
7.7
0.0
5.9
149.5
152.3
52.3
PRO-243
ALA-244
5.8
5.9
2.1
-19.1
99.9
96.9
4.4
ALA-244
ALA-245
5.5
5.3
4.5
21.4
29.7
25.3
211.3
ALA-245
GLU-246
5.1
5.4
37.6
-21.3
92.9
87.5
-88.6
GLU-246
HIS-247
8.7
8.8
-9.4
2.6
131.2
124.0
-115.0
HIS-247
SER-248
10.9
10.7
14.3
-7.8
18.1
23.3
85.2
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
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
LEU-308
ILE-309
2.6
2.8
7.4
-11.2
69.8
63.1
8.3
ILE-309
ILE-310
3.6
3.8
-8.4
21.1
56.1
51.6
-53.8
ILE-310
ARG-311
7.1
7.2
9.6
-19.1
85.0
88.3
-79.9
ARG-311
PRO-312
9.7
9.5
-17.9
-12.2
79.3
69.0
-23.2
PRO-312
ASP-313
13.2
13.2
-2.3
-87.7
44.0
71.4
520.7
ASP-313
SER-314
16.3
15.3
-154.0
-74.9
104.0
74.1
125.3
SER-314
GLY-315
19.0
18.8
-6.3
-31.6
122.2
133.3
-207.7
GLY-315
ASN-316
22.2
21.6
-21.3
-6.9
151.9
145.3
-230.9
ASN-316
PRO-317
22.8
22.7
-2.2
11.9
107.4
114.6
35.8
ASP-319
THR-320
20.9
21.2
-0.5
-1.5
56.0
58.8
-2.7
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