Open Access
Nucleic Acids Research, volume 43, issue W1, pages W370-W377
CSI 3.0: a web server for identifying secondary and super-secondary structure in proteins using NMR chemical shifts
1
Department of Computing Science University of Alberta Edmonton, AB, T6G 2E8, Canada
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2
Department of Computing Science, University of Alberta, Edmonton, AB T6G 2E8, Canada Department of Biological Sciences, University of Alberta, Edmonton, AB T6G 2E8, Canada
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Publication type: Journal Article
Publication date: 2015-05-15
Journal:
Nucleic Acids Research
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor: 14.9
ISSN: 03051048, 13624962
PubMed ID:
25979265
Genetics
Abstract
The Chemical Shift Index or CSI 3.0 (http://csi3.wishartlab.com) is a web server designed to accurately identify the location of secondary and super-secondary structures in protein chains using only nuclear magnetic resonance (NMR) backbone chemical shifts and their corresponding protein sequence data. Unlike earlier versions of CSI, which only identified three types of secondary structure (helix, β-strand and coil), CSI 3.0 now identifies total of 11 types of secondary and super-secondary structures, including helices, β-strands, coil regions, five common β-turns (type I, II, I′, II′ and VIII), β hairpins as well as interior and edge β-strands. CSI 3.0 accepts experimental NMR chemical shift data in multiple formats (NMR Star 2.1, NMR Star 3.1 and SHIFTY) and generates colorful CSI plots (bar graphs) and secondary/super-secondary structure assignments. The output can be readily used as constraints for structure determination and refinement or the images may be used for presentations and publications. CSI 3.0 uses a pipeline of several well-tested, previously published programs to identify the secondary and super-secondary structures in protein chains. Comparisons with secondary and super-secondary structure assignments made via standard coordinate analysis programs such as DSSP, STRIDE and VADAR on high-resolution protein structures solved by X-ray and NMR show >90% agreement between those made with CSI 3.0.
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- We do not take into account publications that without a DOI.
- Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
- Statistics recalculated weekly.
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Hafsa N., Arndt D., Wishart D. S. CSI 3.0: a web server for identifying secondary and super-secondary structure in proteins using NMR chemical shifts // Nucleic Acids Research. 2015. Vol. 43. No. W1. p. W370-W377.
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Hafsa N., Arndt D., Wishart D. S. CSI 3.0: a web server for identifying secondary and super-secondary structure in proteins using NMR chemical shifts // Nucleic Acids Research. 2015. Vol. 43. No. W1. p. W370-W377.
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TY - JOUR
DO - 10.1093/nar/gkv494
UR - https://doi.org/10.1093%2Fnar%2Fgkv494
TI - CSI 3.0: a web server for identifying secondary and super-secondary structure in proteins using NMR chemical shifts
T2 - Nucleic Acids Research
AU - Hafsa, Noor
AU - Arndt, David
AU - Wishart, David S
PY - 2015
DA - 2015/05/15 00:00:00
PB - Oxford University Press
SP - W370-W377
IS - W1
VL - 43
PMID - 25979265
SN - 0305-1048
SN - 1362-4962
ER -
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@article{2015_Hafsa,
author = {Noor Hafsa and David Arndt and David S Wishart},
title = {CSI 3.0: a web server for identifying secondary and super-secondary structure in proteins using NMR chemical shifts},
journal = {Nucleic Acids Research},
year = {2015},
volume = {43},
publisher = {Oxford University Press},
month = {may},
url = {https://doi.org/10.1093%2Fnar%2Fgkv494},
number = {W1},
pages = {W370--W377},
doi = {10.1093/nar/gkv494}
}
Cite this
MLA
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Hafsa, Noor, et al. “CSI 3.0: a web server for identifying secondary and super-secondary structure in proteins using NMR chemical shifts.” Nucleic Acids Research, vol. 43, no. W1, May. 2015, pp. W370-W377. https://doi.org/10.1093%2Fnar%2Fgkv494.