Unsolved

Hi,

I want to model circular permutation together with domain insertion for my protein. Can anybody tell how can I do this using rosetta 3.2 ??

Thanks in advance

Dear Rosetta users,

I have created the missing domain of an X-ray structure by homology modeling and I would like to refine only this part. Is there an easy way to define a residue range in Rosetta and restrict relaxation to these residues rather than writing my own constraints file that includes only atoms from the experimentally derived part? If not what kind of constraints should I impose to the experimentally derived part of my protein (distance, dihedral, etc.)?

thanks in advance,
Thomas

Hey, I was testing the enzyme design application with the files (1a91_CHGW_d1_mod.pdb, D2N_aX.params, D2N_ax_confs.pdb, Est_CHba_d2n.cst and flags) provided in one of the test folders.

Here is my command line:
/usr/local/rosetta3.2/rosetta_source/bin/enzyme_design.linuxgccrelease -database /usr/local/rosetta3.2/rosetta_database/ -overwrite @flags > enzyme_design.log

The run stopped a few seconds after it started. Here is the short log file:

core.init: Mini-Rosetta version exported from unknown

Friends,
I have installed rosetta 3.2.1. I want to predict the structure of a loop. The two terminal residues of the loop are cysteins. So i would like to tell the AbinitioRelax.linuxgccrelease script to consider the disulfide bond between the residues during structure prediction. Is there any option that i use with the AbinitionRelax script do achieve this ?

Thanks