BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16008

Title: Solution structure of the SARS-unique domain-C from the nonstructural protein 3 (nsp3) of the severe acute respiratory syndrome coronavirus   PubMed: 19828617

Deposition date: 2008-10-28 Original release date: 2009-01-06

Authors: Johnson, Margaret; Mohanty, Biswaranjan; Pedrini, Bill; Serrano, Pedro; Chatterjee, Amarnath; Herrmann, Torsten; Joseph, Jeremiah; Saikatendu, Kumar; Buchmeier, Michael; Kuhn, Peter; Wuthrich, Kurt

Citation: Serrano, Pedro; Johnson, Margaret; Chatterjee, Amarnath; Neuman, Benjamin; Joseph, Jeremiah; Buchmeier, Michael; Kuhn, Peter; Wuthrich, Kurt. "Nuclear magnetic resonance structure of the nucleic acid-binding domain of severe acute respiratory syndrome coronavirus nonstructural protein 3."  J. Virol. 83, 12998-13008 (2009).

Assembly members:
SUD-C, polymer, 67 residues, Formula weight is not available

Natural source:   Common Name: not available   Taxonomy ID: 227984   Superkingdom: virus   Kingdom: not available   Genus/species: Coronavirus SARS coronavirus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-28b

Entity Sequences (FASTA):
SUD-C: GSEEHFVETVSLAGSYRDWS YSGQRTELGVEFLKRGDKIV YHTLESPVEFHLDGEVLSLD KLKSLLS

Data sets:
Data typeCount
13C chemical shifts291
15N chemical shifts66
1H chemical shifts466

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1SUD-C1

Entities:

Entity 1, SUD-C 67 residues - Formula weight is not available

1   GLYSERGLUGLUHISPHEVALGLUTHRVAL
2   SERLEUALAGLYSERTYRARGASPTRPSER
3   TYRSERGLYGLNARGTHRGLULEUGLYVAL
4   GLUPHELEULYSARGGLYASPLYSILEVAL
5   TYRHISTHRLEUGLUSERPROVALGLUPHE
6   HISLEUASPGLYGLUVALLEUSERLEUASP
7   LYSLEULYSSERLEULEUSER

Samples:

sample_1: SUD-C, [U-98% 13C; U-98% 15N], 1.2 mM; sodium chloride 20 mM; sodium phosphate 20 mM; sodium azide 2.8 mM

sample_conditions_1: ionic strength: 0.0628 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
5D APSY-CBCACONHsample_1isotropicsample_conditions_1
5D APSY-HACACONHsample_1isotropicsample_conditions_1
4D APSY-HACANHsample_1isotropicsample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - collection

MATCH, Volk, Herrmann and Wuthrich - chemical shift assignment

ASCAN, Fiorito, Herrmann, Damberger and Wuthrich - chemical shift assignment

CARA, Keller and Wuthrich - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 16613
PDB
DBJ BAC81346 BAC81347 BAC81360 BAC81361 BAC81374
GB AAP13439 AAP13442 AAP13566 AAP13575 AAP30028
REF NP_828849 NP_828850 NP_828862
SP P0C6U8 P0C6X7

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts