BMRB Entry 30162
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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/BMR30162
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Title: Structure of the Ebola virus envelope protein MPER/TM domain and its interaction with the fusion loop explains their fusion activity PubMed: 28874543
Deposition date: 2016-08-28 Original release date: 2017-08-22
Authors: Lee, J.; Nyenhuis, D.; Nelson, E.; Cafiso, D.; White, J.; Tamm, L.
Citation: Lee, J.; Nyenhuis, D.; Nelson, E.; Cafiso, D.; White, J.; Tamm, L.. "Structure of the Ebola virus envelope protein MPER/TM domain and its interaction with the fusion loop explains their fusion activity" Proc. Natl. Acad. Sci. U. S. A. 114, E7987-E7996 (2017).
Assembly members:
entity_1, polymer, 47 residues, 5134.819 Da.
Natural source: Common Name: ZEBOV Taxonomy ID: 128951 Superkingdom: Viruses Kingdom: not available Genus/species: Ebolavirus ZEBOV
Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)
Entity Sequences (FASTA):
entity_1: GSDKTLPDQGDNDNWWTGWR
QWIPAGIGVTGVVIAVIALF
AIAKFVF
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 187 |
| 15N chemical shifts | 49 |
| 1H chemical shifts | 284 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 47 residues - 5134.819 Da.
| 1 | GLY | SER | ASP | LYS | THR | LEU | PRO | ASP | GLN | GLY | ||||
| 2 | ASP | ASN | ASP | ASN | TRP | TRP | THR | GLY | TRP | ARG | ||||
| 3 | GLN | TRP | ILE | PRO | ALA | GLY | ILE | GLY | VAL | THR | ||||
| 4 | GLY | VAL | VAL | ILE | ALA | VAL | ILE | ALA | LEU | PHE | ||||
| 5 | ALA | ILE | ALA | LYS | PHE | VAL | PHE |
Samples:
sample_1: EBOV_MPER/TM, [U-99% 15N], 500 uM; Pi 30 mM; NaCl 100 mM
sample_2: EBOV_MPER/TM, [U-99% 13C; U-99% 15N], 500 uM; Pi 30 mM; NaCl 100 mM
sample_conditions_1: ionic strength: 125 mM; pH: 5.5; pressure: 1 atm; temperature: 303 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 HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCANH | sample_2 | isotropic | sample_conditions_1 |
| HCCCONH | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - geometry optimization
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
ProcheckNMR, Laskowski and MacArthur - data analysis
SPARKY, Goddard - peak picking
TALOS, Cornilescu, Delaglio and Bax - chemical shift calculation
NMR spectrometers:
- Bruker AvanceIII 600 MHz
- Bruker AvanceIII 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts