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
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Title: NMR structure of the SARS Coronavirus E protein pentameric ion channel PubMed: 29474890
Deposition date: 2017-01-31 Original release date: 2017-06-05
Authors: Torres, J.; Surya, W.; Li, Y.
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).
Assembly members:
Envelope small membrane protein, polymer, 81 residues, 9003.540 Da.
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: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)
Entity Sequences (FASTA):
Envelope small membrane protein: MHHHHHHSSGVDLGTENLYF
QSMETGTLIVNSVLLFLAFV
VFLLVTLAILTALRLAAYAA
NIVNVSLVKPTVYVYSRVKN
L
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 274 |
| 15N chemical shifts | 65 |
| 1H chemical shifts | 472 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1, 1 | 1 |
| 2 | entity_1, 2 | 1 |
| 3 | entity_1, 3 | 1 |
| 4 | entity_1, 4 | 1 |
| 5 | entity_1, 5 | 1 |
Entities:
Entity 1, entity_1, 1 81 residues - 9003.540 Da.
| 1 | MET | HIS | HIS | HIS | HIS | HIS | HIS | SER | SER | GLY | ||||
| 2 | VAL | ASP | LEU | GLY | THR | GLU | ASN | LEU | TYR | PHE | ||||
| 3 | GLN | SER | MET | GLU | THR | GLY | THR | LEU | ILE | VAL | ||||
| 4 | ASN | SER | VAL | LEU | LEU | PHE | LEU | ALA | PHE | VAL | ||||
| 5 | VAL | PHE | LEU | LEU | VAL | THR | LEU | ALA | ILE | LEU | ||||
| 6 | THR | ALA | LEU | ARG | LEU | ALA | ALA | TYR | ALA | ALA | ||||
| 7 | ASN | ILE | VAL | ASN | VAL | SER | LEU | VAL | LYS | PRO | ||||
| 8 | THR | VAL | TYR | VAL | TYR | SER | ARG | VAL | LYS | ASN | ||||
| 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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_4 | isotropic | sample_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 simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts