Cited by 5,502Protein Structure and DynamicsAdvanced NMR Techniques and ApplicationsEnzyme Structure and Function

AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR

Laskowski, RomanA., Rullmann, J.AntoonC., MacArthur, MalcolmW., Kaptein, Robert, Thornton, JanetM.·1996·Journal of Biomolecular NMR

Abstract

The AQUA and PROCHECK-NMR programs provide a means of validating the geometry and restraint violations of an ensemble of protein structures solved by solution NMR. The outputs include a detailed breakdown of the restraint violations, a number of plots in PostScript format and summary statistics. These various analyses indicate both the degree of agreement of the model structures with the experimental dat, and the quality of their geometrical properties. They are intended to be of use both to support ongoing NMR structure determination and in the validation of the final results.

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Crossref · 10.1007/bf00228148

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21 of 21 references verified0 citation errors · 0 not checkable

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  • The quality of Cn-AMP1 structures was evaluated by analyzing the Ramachandran diagram from PROCHECK-NMR.

    “Furthermore, the quality of Cn-AMP1 structures was evaluated by analyzing the Ramachandran diagram that is part of the PROCHECK-NMR software [18,25].”
  • The Ramachandran statistics among the top 20 lowest-energy structures are 98% for most favoured regions, 2% for additional allowed regions and 0% for disallowed regions.

    “On the basis of Procheck82 analysis of secondary structure elements, the Ramachandran statistics among the top 20 lowest-energy structures are 98% for most favoured regions, 2% for additional allowed regions and 0% for disallowed regions.”

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Authors
Laskowski, R., Rullmann, J. A., MacArthur, M., Kaptein, R., & Thornton, J.
Affiliations
Utrecht University (NL)
Venue
Journal of Biomolecular NMR
Published
1996-12
Volume
8
Issue
4
Pages
477-86
ISSN
  • 0925-2738 (ISSN-L)
  • 1573-5001
OpenAlex
W1975459052
Cited by
5,502
References
21
Citations by year
2026: 142 · 2025: 203 · 2024: 205 · 2023: 219 · 2022: 238 · 2021: 204 · 2020: 198 · 2019: 153 · 2018: 130 · 2017: 173 · 2016: 191 · 2015: 194 · 2014: 248 · 2013: 248 · 2012: 233
FWCI
21.02
Type
journal article
Language
en
Open access
closed
Locations
  • Journal of Biomolecular NMR (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Physical Sciences › Chemistry › Spectroscopy › Advanced NMR Techniques and Applications
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Keywords
Aqua, protein conformational ensembles
MeSH terms
Amino Acid Sequence, Bacterial Proteins, DNA-Binding Proteins, Evaluation Studies as Topic, Models, Molecular, Molecular Sequence Data, Magnetic Resonance Spectroscopy, Proteins, Quality Control, Software, Solutions, Reproducibility of Results, Molecular Structure, Protein Structure, Secondary

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