I am trying to model a protein which has 70% sequence similarity to the
template sequence. However, there are ~20 residues in the target/query
sequence which is not present in the template.
Now, from Secondary Structure Prediction algorithms, this region seems
to be partly helical. But the model generated by Modeller (9v3) gives a
random-coil or loop for these residues. Is it not possible to feed the
secondary structure info. into the program to improve the structural
quality of this extra region?