BMRB Entry 36049

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36049
MolProbity Validation Chart

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Title:
NMR structure of the SARS Coronavirus E protein pentameric ion channel
Deposition date:
2017-01-31
Original release date:
2017-06-05
Authors:
Torres, J.; Surya, W.; Li, Y.
Citation:

Citation: Surya, W.; Li, Y.; Torres, J.. "Structure of the SARS coronavirus E protein pentameric ion channel in LMPG micelles"  Biochim. Biophys. Acta Biomembr. 1860, 1309-1317 (2018).
PubMed: 29474890

Assembly members:

Assembly members:
Envelope small membrane protein, polymer, 81 residues, 9003.540 Da.

Natural source:

Natural source:   Common Name: SARS-CoV   Taxonomy ID: 227859   Superkingdom: Viruses   Kingdom: not available   Genus/species: Betacoronavirus Severe acute respiratory syndrome-related coronavirus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: pNIC28-Bsa4

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Envelope small membrane protein: MHHHHHHSSGVDLGTENLYF QSMETGTLIVNSVLLFLAFV VFLLVTLAILTALRLAAYAA NIVNVSLVKPTVYVYSRVKN L

Data sets:
Data typeCount
13C chemical shifts274
15N chemical shifts65
1H chemical shifts472

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1, 11
2entity_1, 21
3entity_1, 31
4entity_1, 41
5entity_1, 51

Entities:

Entity 1, entity_1, 1 81 residues - 9003.540 Da.

1   METHISHISHISHISHISHISSERSERGLY
2   VALASPLEUGLYTHRGLUASNLEUTYRPHE
3   GLNSERMETGLUTHRGLYTHRLEUILEVAL
4   ASNSERVALLEULEUPHELEUALAPHEVAL
5   VALPHELEULEUVALTHRLEUALAILELEU
6   THRALALEUARGLEUALAALATYRALAALA
7   ASNILEVALASNVALSERLEUVALLYSPRO
8   THRVALTYRVALTYRSERARGVALLYSASN
9   LEU

Samples:

sample_1: Envelope small membrane protein, [U-99% 15N], 0.67 mM; LMPG 200 mM; sodium chloride 50 mM; sodium phosphate 20 mM; H2O 95%; D2O, [U-2H], 5%

sample_2: Envelope small membrane protein, [U-99% 13C; U-99% 15N], 0.67 mM; LMPG 200 mM; sodium chloride 50 mM; sodium phosphate 20 mM; H2O 95%; D2O, [U-2H], 5%

sample_3: Envelope small membrane protein, [U-99% 15N, U-99% 2H], 0.67 mM; LMPG 200 mM; sodium chloride 50 mM; sodium phosphate 20 mM; H2O 95%; D2O, [U-2H], 5%

sample_4: Envelope small membrane protein, [U-99% 13C], 0.33 mM; Envelope small membrane protein, [U-99% 15N, U-99% 2H], 0.33 mM; LMPG 200 mM; sodium chloride 50 mM; sodium phosphate 20 mM; H2O 95%; D2O, [U-2H], 5%

sample_conditions_1: ionic strength: 50 mM; pH: 5.5; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_4isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure calculation

HADDOCK v2.2, Bonvin - refinement

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AvanceII 700 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks