BMRB Entry 30503
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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/BMR30503
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NMR-STAR v3 text file.
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Title: MPER-TM Domain of HIV-1 envelope glycoprotein (Env) PubMed: 30185554
Deposition date: 2018-07-31 Original release date: 2018-08-31
Authors: Fu, Q.; Shaik, M.; Cai, Y.; Ghantous, F.; Piai, A.; Peng, H.; Rits-Volloch, S.; Liu, Z.; Harrison, S.; Seaman, M.; Chen, B.; Chou, J.
Citation: Fu, Q.; Shaik, M.; Cai, Y.; Ghantous, F.; Piai, A.; Peng, H.; Rits-Volloch, S.; Liu, Z.; Harrison, S.; Seaman, M.; Chen, B.; Chou, J.. "Structure of the membrane proximal external region of HIV-1 envelope glycoprotein" Proc. Natl. Acad. Sci. U.S.A. 115, E8892-E8899 (2018).
Assembly members:
entity_1, polymer, 51 residues, 6179.373 Da.
Natural source: Common Name: HIV-1 Taxonomy ID: 11676 Superkingdom: Viruses Kingdom: not available Genus/species: Lentivirus HIV-1
Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21 Vector: pMM - LR6
Entity Sequences (FASTA):
entity_1: LLELDKWASLWNWFDITNWL
WYIRIFIIIVGSLIGLRIVF
AVLSLVNRVRQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 88 |
| 15N chemical shifts | 49 |
| 1H chemical shifts | 49 |
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 |
Entities:
Entity 1, entity_1, 1 51 residues - 6179.373 Da.
| 1 | LEU | LEU | GLU | LEU | ASP | LYS | TRP | ALA | SER | LEU | ||||
| 2 | TRP | ASN | TRP | PHE | ASP | ILE | THR | ASN | TRP | LEU | ||||
| 3 | TRP | TYR | ILE | ARG | ILE | PHE | ILE | ILE | ILE | VAL | ||||
| 4 | GLY | SER | LEU | ILE | GLY | LEU | ARG | ILE | VAL | PHE | ||||
| 5 | ALA | VAL | LEU | SER | LEU | VAL | ASN | ARG | VAL | ARG | ||||
| 6 | GLN |
Samples:
sample_1: DMPC 50 mM; DHPC 100 mM; Envelope glycoprotein gp160, 15N, 2H,
sample_2: DMPC 50 mM; DHPC 100 mM; Envelope glycoprotein gp160, [U-13C; U-15N; U-2H],
sample_3: DMPC, [U-99% 2H], 50 mM; DHPC, [U-99% 2H], 100 mM; Envelope glycoprotein gp160, [U-100% 13C; U-100% 15N],
sample_4: DMPC, [U-99% 2H], 50 mM; DHPC, [U-99% 2H], 100 mM; Envelope glycoprotein gp160, 15N, 2H mixed with 13C(15%),
sample_5: DMPC, [U-99% 2H], 50 mM; DHPC, [U-99% 2H], 100 mM; Envelope glycoprotein gp160, 15N, 2H mixed with 13C,
sample_conditions_1: ionic strength: 20 mM; pH: 6.7; pressure: 1 atm; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N Trosy 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 HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY tr-HSQC | sample_3 | isotropic | sample_conditions_1 |
| 3D Jch Modulated 1H-15N NOESY | sample_5 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_4 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY tr-HSQC | sample_4 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_3 | isotropic | sample_conditions_1 |
Software:
XEASY, Bartels et al. - chemical shift assignment
X-PLOR NIH v2.48, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN, Bruker Biospin - collection
NMR spectrometers:
- Bruker AvanceII 800 MHz
- Bruker AvanceIII 900 MHz
- Bruker AvanceII 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts