BMRB Entry 30738
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30738
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Title: Solution NMR structure of the myristoylated 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 myristoylated feline immunodeficiency virus matrix protein" . ., .-..
Assembly members:
entity_1, polymer, 125 residues, 13922.065 Da.
entity_MYR, non-polymer, 228.371 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: XGNGQGRDWKMAIKRCSNVA
VGVGGKSKKFGEGNFRWAIR
MANVSTGREPGDIPETLDQL
RLVICDLQERREKFGSSKEI
DMAIVTLKVFAVAGLLNMTV
STAAAAENMYSQMGLDTRPH
HHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 449 |
| 15N chemical shifts | 114 |
| 1H chemical shifts | 602 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 125 residues - 13922.065 Da.
| 1 | MYR | GLY | ASN | GLY | GLN | GLY | ARG | ASP | TRP | LYS | ||||
| 2 | MET | ALA | ILE | LYS | ARG | CYS | SER | ASN | VAL | ALA | ||||
| 3 | VAL | GLY | VAL | GLY | GLY | LYS | SER | LYS | LYS | PHE | ||||
| 4 | GLY | GLU | GLY | ASN | PHE | ARG | TRP | ALA | ILE | ARG | ||||
| 5 | MET | ALA | ASN | VAL | SER | THR | GLY | ARG | GLU | PRO | ||||
| 6 | GLY | ASP | ILE | PRO | GLU | THR | LEU | ASP | GLN | LEU | ||||
| 7 | ARG | LEU | VAL | ILE | CYS | ASP | LEU | GLN | GLU | ARG | ||||
| 8 | ARG | GLU | LYS | PHE | GLY | SER | SER | LYS | GLU | ILE | ||||
| 9 | ASP | MET | ALA | ILE | VAL | THR | LEU | LYS | VAL | PHE | ||||
| 10 | ALA | VAL | ALA | GLY | LEU | LEU | ASN | MET | THR | VAL | ||||
| 11 | SER | THR | ALA | ALA | ALA | ALA | GLU | ASN | MET | TYR | ||||
| 12 | SER | GLN | MET | GLY | LEU | ASP | THR | ARG | PRO | HIS | ||||
| 13 | HIS | HIS | HIS | HIS | HIS |
Entity 2, entity_2 - C14 H28 O2 - 228.371 Da.
| 1 | MYR |
Samples:
sample_1: sodium phosphate 50 mM; DTT 10 mM; sodium chloride 5 mM; glucose 4 g/L; ammonium chloride, [U-99% 15N], 1 g/L; Feline Immunodeficiency Virus Myristoylated Matrix Protein, [U-15N], 300 uM
sample_2: sodium phosphate 50 mM; DTT, [U-98% 2H], 10 mM; sodium chloride 5 mM; glucose, [U-99% 13C], 4 g/L; ammonium chloride 1 g/L; Feline Immunodeficiency Virus Myristoylated Matrix Protein, [U-13C], 300 uM
sample_3: sodium phosphate 50 mM; DTT, [U-98% 2H], 10 mM; sodium chloride 5 mM; glucose, [U-99% 13C], 4 g/L; ammonium chloride 1 g/L; Feline Immunodeficiency Virus Myristoylated Matrix Protein, [U-13C], 300 uM; Myristoyl coenzyme A 50 mg/L
sample_4: 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; Feline Immunodeficiency Virus Myristoylated Matrix Protein, [U-13C; U-15N], 300 uM
sample_5: sodium phosphate 50 mM; DTT, [U-98% 2H], 10 mM; sodium chloride 5 mM; glucose 4 g/L; ammonium chloride 1 g/L; Feline Immunodeficiency Virus Myristoylated Matrix Protein 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
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H NOESY | sample_5 | isotropic | sample_conditions_2 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_4 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_4 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_4 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_4 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HMQC | sample_3 | isotropic | sample_conditions_2 |
| 2D 1H-13C HMQC | sample_2 | isotropic | sample_conditions_2 |
| 4D HMQC-NOESY-HMQC | sample_2 | isotropic | sample_conditions_2 |
| 4D HSQC-NOESY-HMQC | sample_4 | isotropic | sample_conditions_1 |
Software:
NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking
NMRFx, Johnson, One Moon Scientific - processing
CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation
TopSpin, Bruker Biospin - collection
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker DMX 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts