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Good baseline settings for side chain packing

Category: 
Structure prediction

Hi,

I'm trying to compare another method to Rosetta's side chain packing. My first pass is just using default options for the PackMover, and the results I'm getting out of Rosetta are pretty bad by comparison. Are there good rule of thumb settings for establishing a baseline over a set of proteins?

I am setting up a PackMover in C++ code, as opposed to running the command line fixbb application. Looking through the fixbb code I see the following options, some of which aren't mentioned in the documentation:

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ddg_monomer: what is the meaning of "total score" and "score"?

Category: 
Structure prediction

Dear friends,
After using a PDB of -740 REU to run ddg_monomer, I use score_jd2.linuxgccrelease to score the silent output. In the score file (attached), the first two elements are "total_score" and "score". The scale of "total_score" is close to the talaris2013, i.e. -700 to -730; the scale of "score" is -1000, much lower than -700.

Can I ask
1) What is the difference of "total score" and "score"?

2) Why cannot we just use one score?

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ddg_monomer: if MPI executable is reproducible and efficient?

Category: 
Structure prediction

Dear friends,
It is my first time using an MPI executable to run the ddg_monomer. I tested it to mutate the first residue from D to A with different cores, which is compared to a serial job. The following is the results:

Core number, time, ddg prediction
1 (serial), 32 hours, -0.362
2, 25.433 hours, -1.722
4, 29.766 hours, 0.055
8, 24.68 hours, 0.239
24, 25.13 hours, -3.080

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Does relax.linuxgccrelease fully relax the structure compared to ddg_monomer.linuxgccrelease?

Category: 
Structure prediction

Dear friends,
I was using relax.linuxgccrelease to relax my protein (442 residues) with 100 outputs:

~/Cheng/rosetta_2014.30.57114_bundle/main/source/bin/relax.linuxgccrelease -database ~/Cheng/rosetta_2014.30.57114_bundle/main/database -s /home/lanselibai/Cheng/relax/input/C226S_raw.pdb -out:show_accessed_options -nstruct 100 -relax:quick &> /home/lanselibai/Cheng/relax/output/record.log &

Then I score it using score_jd2.linuxgccrelease:

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Robetta fragments and silent.out-file

Category: 
Fragment Generation

Hello,
I have a question about the robetta fragment-file. what does the numbers mean?!

1ofd A 1068 S L -163.692 159.068 168.636 -0.177 4.773 84.262 3 0.000 P 1 F 1
1ofd A 1069 P L -59.041 138.502 179.354 -0.177 4.773 84.262 3 0.000 P 1 F 1
1ofd A 1070 L L -65.398 -35.892 176.967 -0.177 4.773 84.262 3 0.000 P 1 F 1
Are the first free values angles?!

I have the same understanding problems with the silent.out file.

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How to automatically position new peptides into the binding site of a enzime, in order to run peptide-protein docking approaches

Category: 
Docking

Hello,
I would like to know how to automatically position new peptides into the binding site of a enzime, in order to run peptide-protein docking approaches?
In my case, I know the binding site and I have the crystallographic structure of a reference peptide located at the binding site, but I need to generate several (thousands) of other new linear peptide structures at this same binding site, in order to run the docking calculations using the rosetta3 protocols.

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Docking with constraint

Category: 
Docking

Hi everyone,
I am trying to dock a domain into a dimer protein. The domain is lowest score structure that was generated by abinition relax. Because they are continous amino acid sequence, so i use atompair constraint betwen c terminal of first monomer with n terminal of predicted domain. I also constraint its c terminal with n terminal of the second mononer.

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