BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 27176

Title: 1H, 13C, and 15N Chemical Shift Assignments for truncated forms of the coronavirus nsp1 protein and its solubility domain GB1   PubMed: 28750053

Deposition date: 2017-07-13 Original release date: 2017-08-10

Authors: Vazquez, Leonardo; Almeida, Marcius

Citation: Vazquez, Leonardo; Lima, Luis; Almeida, Marcius. "Comprehensive structural analysis of designed incomplete polypeptide chains of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus"  PLoS ONE 12, e0182132-e0182132 (2017).

Assembly members:
nsp1(13-25), polymer, 99 residues, Formula weight is not available

Natural source:   Common Name: SARS coronavirus   Taxonomy ID: 227859   Superkingdom: Viruses   Kingdom: not available   Genus/species: SARS coronavirus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-25(+)

Entity Sequences (FASTA):
nsp1(13-25): MGHVQLSLPVLQVRDHGRAP IKVESQEHKLVPRGSFQYKL ILNGKTLKGETTTEAVDAAT AEKVFKQYANDNGVDGEWTY DDATKTFTVTESGHHHHHH

Data sets:
Data typeCount
13C chemical shifts247
15N chemical shifts86
1H chemical shifts201

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Coronavirus nsp1 truncated proteins; nsp1(13-25)1

Entities:

Entity 1, Coronavirus nsp1 truncated proteins; nsp1(13-25) 99 residues - Formula weight is not available

1   METGLYHISVALGLNLEUSERLEUPROVAL
2   LEUGLNVALARGASPHISGLYARGALAPRO
3   ILELYSVALGLUSERGLNGLUHISLYSLEU
4   VALPROARGGLYSERPHEGLNTYRLYSLEU
5   ILELEUASNGLYLYSTHRLEULYSGLYGLU
6   THRTHRTHRGLUALAVALASPALAALATHR
7   ALAGLULYSVALPHELYSGLNTYRALAASN
8   ASPASNGLYVALASPGLYGLUTRPTHRTYR
9   ASPASPALATHRLYSTHRPHETHRVALTHR
10   GLUSERGLYHISHISHISHISHISHIS

Samples:

All_samples: potassium phosphate 2 mM; sodium chloride 250 mM; DTT 1 mM; sodium azide 3 mM; nsp1(13-25), [U-13C; U-15N], 2 mM

Condition_of_all_samples: ionic strength: 250 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCAll_samplesisotropicCondition_of_all_samples
2D 1H-13C HSQC aliphaticAll_samplesisotropicCondition_of_all_samples
2D 1H-13C HSQC aromaticAll_samplesisotropicCondition_of_all_samples
3D CBCA(CO)NHAll_samplesisotropicCondition_of_all_samples
3D HNCACBAll_samplesisotropicCondition_of_all_samples
3D HNCOAll_samplesisotropicCondition_of_all_samples
3D HNCAAll_samplesisotropicCondition_of_all_samples
3D HBHA(CO)NHAll_samplesisotropicCondition_of_all_samples

Software:

XEASY, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

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