BMRB Entry 30740
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30740
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Title: Solution NMR Structure of the G4L/Q5K/G6S (NOS) Unmyristoylated Feline Immunodeficiency Virus Matrix Protein
Deposition date: 2020-03-24 Original release date: 2020-07-20
Authors: Brown, J.; Summers, H.; Brown, L.; Marchant, J.; Canova, P.; O'Hern, C.; Abbott, S.; Nyaunu, C.; Maxwell, S.; Johnson, T.; Moser, M.; Ablan, S.; Carter, H.; Freed, E.; Summers, M.
Citation: Brown, J.; Summers, H.; Brown, L.; Marchant, J.; Canova, P.; O'Hern, C.; Abbott, S.; Nyaunu, C.; Maxwell, S.; Johnson, T.; Moser, M.; Ablan, S.; Carter, H.; Freed, E.; Summers, M.. "Solution NMR Structure of the G4L/Q5K/G6S (NOS) Unmyristoylated Feline Immunodeficiency Virus Matrix Protein" . ., .-..
Assembly members:
entity_1, polymer, 126 residues, 14075.185 Da.
Natural source: Common Name: FIV Taxonomy ID: 11673 Superkingdom: Viruses Kingdom: not available Genus/species: Lentivirus FIV
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: GNLKSRDWKMAIKRCSNVAV
GVGGKSKKFGEGNFRWAIRM
ANVSTGREPGDIPETLDQLR
LVICDLQERREKFGSSKEID
MAIVTLKVFAVAGLLNMTVS
TAAAAENMYSQMGLDTRPHH
HHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 442 |
| 15N chemical shifts | 126 |
| 1H chemical shifts | 342 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 126 residues - 14075.185 Da.
| 1 | GLY | ASN | LEU | LYS | SER | ARG | ASP | TRP | LYS | MET | ||||
| 2 | ALA | ILE | LYS | ARG | CYS | SER | ASN | VAL | ALA | VAL | ||||
| 3 | GLY | VAL | GLY | GLY | LYS | SER | LYS | LYS | PHE | GLY | ||||
| 4 | GLU | GLY | ASN | PHE | ARG | TRP | ALA | ILE | ARG | MET | ||||
| 5 | ALA | ASN | VAL | SER | THR | GLY | ARG | GLU | PRO | GLY | ||||
| 6 | ASP | ILE | PRO | GLU | THR | LEU | ASP | GLN | LEU | ARG | ||||
| 7 | LEU | VAL | ILE | CYS | ASP | LEU | GLN | GLU | ARG | ARG | ||||
| 8 | GLU | LYS | PHE | GLY | SER | SER | LYS | GLU | ILE | ASP | ||||
| 9 | MET | ALA | ILE | VAL | THR | LEU | LYS | VAL | PHE | ALA | ||||
| 10 | VAL | ALA | GLY | LEU | LEU | ASN | MET | THR | VAL | SER | ||||
| 11 | THR | ALA | ALA | ALA | ALA | GLU | ASN | MET | TYR | SER | ||||
| 12 | GLN | MET | GLY | LEU | ASP | THR | ARG | PRO | HIS | HIS | ||||
| 13 | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: sodium phosphate 50 mM; DTT 10 mM; sodium chloride 5 mM; glucose, [U-99% 13C], 4 g/L; ammonium chloride 1 g/L; Unmyristoylated G4L/Q5K/G6S (NOS) Feline Immunodeficiency Virus Matrix Protein, [U-13C], 300 uM
sample_2: sodium phosphate 50 mM; DTT 10 mM; sodium chloride 5 mM; Unmyristoylated G4L/Q5K/G6S (NOS) Feline Immunodeficiency Virus Matrix Protein 300 uM
sample_3: sodium phosphate 50 mM; DTT 10 mM; sodium chloride 5 mM; glucose, [U-99% 13C], 4 g/L; ammonium chloride, [U-99% 15N], 1 g/L; Unmyristoylated G4L/Q5K/G6S (NOS) Feline Immunodeficiency Virus Matrix Protein, [U-13C; U-15N], 300 uM
sample_4: sodium phosphate 50 mM; DTT 10 mM; sodium chloride 5 mM; glucose 4 g/L; ammonium chloride, [U-99% 15N], 1 g/L; Unmyristoylated G4L/Q5K/G6S (NOS) Feline Immunodeficiency Virus Matrix Protein, [U-15N], 300 uM
sample_conditions_1: ionic strength: 5 mM; pH: 8; pressure: 1 atm; temperature: 298 K
sample_conditions_2: ionic strength: 5 mM; pH: 8 pD; pressure: 1 atm; temperature: 298 K
sample_conditions_3: ionic strength: 5 mM; pH: 5; pressure: 1 atm; temperature: 298 K
sample_conditions_4: ionic strength: 5 mM; pH: 5 pD; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_2 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_4 |
| 2D 1H-15N HSQC | sample_4 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_4 | isotropic | sample_conditions_3 |
| 3D CBCA(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_3 | isotropic | sample_conditions_3 |
| 3D HNCACB | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_3 | isotropic | sample_conditions_3 |
| 3D HNCO | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_3 | isotropic | sample_conditions_3 |
| 3D HN(CA)CO | sample_3 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_3 | isotropic | sample_conditions_3 |
| 3D 1H-15N NOESY | sample_4 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_4 | isotropic | sample_conditions_3 |
| 4D HSQC-NOESY-HMQC | sample_3 | isotropic | sample_conditions_1 |
| 4D HMQC-NOESY-HMQC | sample_1 | isotropic | sample_conditions_2 |
| 2D 1H-13C HMQC | sample_2 | isotropic | sample_conditions_2 |
| 2D 1H-13C HMQC | sample_2 | isotropic | sample_conditions_4 |
Software:
TopSpin, Bruker Biospin - collection
NMRFx, Johnson, One Moon Scientific - processing
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation
NMR spectrometers:
- Bruker DMX 600 MHz
- Bruker DMX 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts