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The 3-D structure of a protein in space. It can refer to secondary structures, such as alpha helices or beta sheets, or the 3-D coordinates of the atoms making up a protein.

1 vote

Delete chains from a protein

You can also do this with pdb-tools: pdb_selchain -A prot.pdb > prot_A.pdb
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1 vote

DMPfold error while running protein structure prediction

The comment by Devon Ryan is correct - looks like your blastpgp command is not working properly. For a protein of that length it's more likely to be a problem with the BLAST executable running on your …
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1 vote

Dmpfold error "No such file or directory: 'best_qdope.pdb'" when running "run_dmpfold.sh"?

The target variable, which is set to the first part of the sequence file name, should be sequence according to your given command line. However the error message thinks it is c600m2-tail-before-lysin- …
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3 votes
Accepted

DMPfold: is it suitable to get 5000 models to compare with rosetta

DMPfold tends to produce low-variability models - it produces a small number of distinct conformations, and either the right one is in there or it isn't. This arises from the way the models are genera …
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1 vote
Accepted

DMPfold: Understand the run of DMPfold "run_dmpfold.sh"?

From the docs: The final model is final_1.pdb and other structures may or may not be generated as final_2.pdb to final_5.pdb if they are significantly different. Many other files are generated tot …
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0 votes
Accepted

DMPfold: number of models produced using "10 500" feature in "run_dmpfold.sh"?

The sequence_n.pdb files are temporary and are combined into an ensemble.i.pdb file after each iteration i. That file has many structures in. After the run is complete there will be a final_1.pdb file …
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1 vote
Accepted

Can DMPfold and I-Tasser work well for de novo structure prediction of 1135 amino acid long ...

For DMPfold you might like to look at Figure 5B of the paper, which implies that performance starts to drop off after ~600 residues. Only proteins up to 500 residues were used in the training set, for …
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1 vote

Rosetta ab initio run gives 0.00 RMSD for generated 2000 models? (run still in progress)

RMSD is a measure of similarity between two structures. The relevant RMSD in protein structure prediction is between a model and the native structure. If you don't have a native structure you cannot h …
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2 votes
Accepted

What does final generated models with TM-score of DMPfold signify in "sequence.ema.txt" file?

This is described briefly in the paper. The four quantities are inputs to the estimator of model accuracy: nres is the sequence length. neff is an effective sequence count, or how deep the alignment …
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2 votes

PDB codes for misfolded proteins?

Searching "misfolded" on the RCSB PDB turns up 64 hits. Most of these won't be relevant, but there are some interesting entries on tumor associated EGFR and misolded RNA. In order to experimentally o …
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0 votes

How can we find the distance between all residues in a PDB file?

Distance between C-alphas can also be found using the BioStructures.jl package in Julia: using BioStructures struc = read("1AKE.pdb", PDB) calphas = collectatoms(struc['A'], calphaselector) dm = Dist …
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2 votes

How do you calculate the top L/5 score?

A contact map predictor will usually output the probability of a contact for every residue pair in a protein, often ommitting very close pairs (e.g. less than 6 residue separation). To calculate the L …
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5 votes

How to quickly and robustly convert between mmCIF and PDB?

Converting a PDB file to some version of an mmCIF file is always possible provided the PDB file doesn't have any "problems". However grouping identical molecules into the same entity is non-trivial so …
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4 votes

How does sequence alignment help with protein folding prediction?

Protein sequences from the same family form a sequence alignment. Some positions in the alignment will be conserved, i.e. the same in all sequences. These are often associated with function, e.g. a ca …
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2 votes

What is the best way to start with Structural bioinformatics with zero prior experience?

As others have said, there is no short cut and you will need to spend some time with a good book. I would say there are 3 broad areas of understanding you have to have as a structural bioinformaticia …
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