4 - Central Institute of Brackishwater Aquaculture

Natlonal Workshop-cum-Training on Bldnfonnatics and Information Management in Aquaculture
favoured reglons
275 94.2%
Res~dues in addlt~onal allowed regens
I
I
I
I
------'
Resldues In disallowed reglons
1 1 0.3%
---- .........................................
...............................
I
Number of non-glyc~ne and non-prol~ne
res~dues 292 100.0%
AII kgree, Pro) 2
Number of glyclne res~dues (shown as
triangles) 30
Number of prol~ne res~dues
..............................................
...............................
Total number of res~dues
337
..............................................
...............................
M/c bond lengths: 99.5%
0.5% h~ghl~ghted
M/c bond angles: 93.2%
1 1 6.E0/0 h~ghl~ghted
Figure 6: Ramachandran plot of Holliday junction DNA helicase RuvB protein
generated by PROCHECK. The most favored regions are colored red, additional
allowed, generously allowed and disallowed regions are indicated as yellow, light
yellow and white fields, respectively.
Errat analyzes the statistics of non-bonded interactions between different atom
types and plots the value of the error function versus position of a residue
[Colovos and Yeates, 19931. Errat is showing an overall quality factor of 80.938.
Verify-3D determines the compatibility of an atomic model (3D) with its own
amino acid sequence (ID) by assigned & structural class based on its location
and environment (alpha, beta, loop, polar, nonpolar etc) and comparing the
results to good structures [Eisenberg et al., 19971. Verify-3D results show
92.90% of the residues had an averaged 3D-1D score larger than 0.2 and passed
the test.
3.3 Active Site Prediction and Docking Study: Active sites of the target
protein were predicted using the CASTp active site prediction tool. The feasible
active sites predicted by the tool are shown in Table 2.
I
I
wlthln l~m~ts
I Planar groups: 100.0% wlth~n llmlts
0.0% h~ghl~ghted
I