Autor: |
Vuister GW; Department of Biochemistry, School of Biological Sciences, University of Leicester, Henry Wellcome Building, Lancaster Road, Leicester, LE1 9HN, UK, gv29@le.ac.uk., Fogh RH, Hendrickx PM, Doreleijers JF, Gutmanas A |
Jazyk: |
angličtina |
Zdroj: |
Journal of biomolecular NMR [J Biomol NMR] 2014 Apr; Vol. 58 (4), pp. 259-85. Date of Electronic Publication: 2013 Jul 23. |
DOI: |
10.1007/s10858-013-9750-x |
Abstrakt: |
Biomolecular structures at atomic resolution present a valuable resource for the understanding of biology. NMR spectroscopy accounts for 11% of all structures in the PDB repository. In response to serious problems with the accuracy of some of the NMR-derived structures and in order to facilitate proper analysis of the experimental models, a number of program suites are available. We discuss nine of these tools in this review: PROCHECK-NMR, PSVS, GLM-RMSD, CING, Molprobity, Vivaldi, ResProx, NMR constraints analyzer and QMEAN. We evaluate these programs for their ability to assess the structural quality, restraints and their violations, chemical shifts, peaks and the handling of multi-model NMR ensembles. We document both the input required by the programs and output they generate. To discuss their relative merits we have applied the tools to two representative examples from the PDB: a small, globular monomeric protein (Staphylococcal nuclease from S. aureus, PDB entry 2kq3) and a small, symmetric homodimeric protein (a region of human myosin-X, PDB entry 2lw9). |
Databáze: |
MEDLINE |
Externí odkaz: |
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