Significant reduction in errors associated with nonbonded contacts in protein crystal structures: automated all-atom refinement with PrimeX.
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Structure of theArabidopsis thalianaTOP2 oligopeptidaseFitmunk: improving protein structures by accurate, automatic modeling of side-chain conformations.Evaluation of predictions in the CASP10 model refinement category.Prediction of Long Loops with Embedded Secondary Structure using the Protein Local Optimization Program.Molstack - interactive visualization tool for presentation, interpretation, and validation of macromolecules and electron density maps.OPTIMIZATION BIAS IN ENERGY-BASED STRUCTURE PREDICTION.Automating crystallographic structure solution and refinement of protein-ligand complexes.Protein-ligand cocrystal structures: we can do better.Validation of ligands in macromolecular structures determined by X-ray crystallography.
P2860
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P2860
Significant reduction in errors associated with nonbonded contacts in protein crystal structures: automated all-atom refinement with PrimeX.
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name
Significant reduction in error ...... l-atom refinement with PrimeX.
@en
type
label
Significant reduction in error ...... l-atom refinement with PrimeX.
@en
prefLabel
Significant reduction in error ...... l-atom refinement with PrimeX.
@en
P2093
P2860
P1476
Significant reduction in error ...... l-atom refinement with PrimeX.
@en
P2093
Jeffrey A Bell
Kenneth L Ho
Ramy Farid
P2860
P304
P356
10.1107/S0907444912017453
P577
2012-07-17T00:00:00Z