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NMR assignment of the domain 513–651 from the SARS-CoV nonstructural protein nsp3
Sequence-specific NMR assignments of an internal domain of the protein nsp3, nsp3(513–651), which is a part of the SARS coronavirus (SARS-CoV) replicase polyprotein, have been determined, using triple-resonance NMR experiments with the uniformly [(13)C,(15)N]-labeled protein. The complete assignment...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Netherlands
2007
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7090708/ https://www.ncbi.nlm.nih.gov/pubmed/19636862 http://dx.doi.org/10.1007/s12104-007-9052-x |
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author | Chatterjee, Amarnath Johnson, Margaret A. Serrano, Pedro Pedrini, Bill Wüthrich, Kurt |
author_facet | Chatterjee, Amarnath Johnson, Margaret A. Serrano, Pedro Pedrini, Bill Wüthrich, Kurt |
author_sort | Chatterjee, Amarnath |
collection | PubMed |
description | Sequence-specific NMR assignments of an internal domain of the protein nsp3, nsp3(513–651), which is a part of the SARS coronavirus (SARS-CoV) replicase polyprotein, have been determined, using triple-resonance NMR experiments with the uniformly [(13)C,(15)N]-labeled protein. The complete assignments (>99%) provide the basis for the ongoing three-dimensional structure determination. |
format | Online Article Text |
id | pubmed-7090708 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2007 |
publisher | Springer Netherlands |
record_format | MEDLINE/PubMed |
spelling | pubmed-70907082020-03-24 NMR assignment of the domain 513–651 from the SARS-CoV nonstructural protein nsp3 Chatterjee, Amarnath Johnson, Margaret A. Serrano, Pedro Pedrini, Bill Wüthrich, Kurt Biomol NMR Assign Article Sequence-specific NMR assignments of an internal domain of the protein nsp3, nsp3(513–651), which is a part of the SARS coronavirus (SARS-CoV) replicase polyprotein, have been determined, using triple-resonance NMR experiments with the uniformly [(13)C,(15)N]-labeled protein. The complete assignments (>99%) provide the basis for the ongoing three-dimensional structure determination. Springer Netherlands 2007-10-30 2007 /pmc/articles/PMC7090708/ /pubmed/19636862 http://dx.doi.org/10.1007/s12104-007-9052-x Text en © Springer Science+Business Media B.V. 2007 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic. |
spellingShingle | Article Chatterjee, Amarnath Johnson, Margaret A. Serrano, Pedro Pedrini, Bill Wüthrich, Kurt NMR assignment of the domain 513–651 from the SARS-CoV nonstructural protein nsp3 |
title | NMR assignment of the domain 513–651 from the SARS-CoV nonstructural protein nsp3 |
title_full | NMR assignment of the domain 513–651 from the SARS-CoV nonstructural protein nsp3 |
title_fullStr | NMR assignment of the domain 513–651 from the SARS-CoV nonstructural protein nsp3 |
title_full_unstemmed | NMR assignment of the domain 513–651 from the SARS-CoV nonstructural protein nsp3 |
title_short | NMR assignment of the domain 513–651 from the SARS-CoV nonstructural protein nsp3 |
title_sort | nmr assignment of the domain 513–651 from the sars-cov nonstructural protein nsp3 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7090708/ https://www.ncbi.nlm.nih.gov/pubmed/19636862 http://dx.doi.org/10.1007/s12104-007-9052-x |
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