BMRB Entry 27396
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27396
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Title: NMR assignments of Rous sarcoma virus matrix protein (M domain)
Deposition date: 2018-02-06 Original release date: 2018-10-15
Authors: Vlach, Jiri; Saad, Jamil; Eastep, Gunnar; Ghanam, Ruba
Citation: Vlach, Jiri; Saad, Jamil; Eastep, Gunnar; Ghanam, Ruba. "ASV MA interaction with phospholipids" J. Mol. Biol. ., .-..
Assembly members:
sRSV_MA, polymer, 87 residues, 9201.7769 Da.
Natural source: Common Name: Rous sarcoma virus Taxonomy ID: 11886 Superkingdom: Viruses Kingdom: not available Genus/species: Alpharetrovirus Rous sarcoma virus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
sRSV_MA: SEAVIKVISSACKTYCGKTS
PSKKEIGAMLSLLQKEGLLM
SPSDLYSPGSWDPITAALSQ
RAMILGKSGELKTWGLVLGA
LKAAREE
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 390 |
| 15N chemical shifts | 89 |
| 1H chemical shifts | 622 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | sRSV MA | 1 |
Entities:
Entity 1, sRSV MA 87 residues - 9201.7769 Da.
| 1 | SER | GLU | ALA | VAL | ILE | LYS | VAL | ILE | SER | SER | ||||
| 2 | ALA | CYS | LYS | THR | TYR | CYS | GLY | LYS | THR | SER | ||||
| 3 | PRO | SER | LYS | LYS | GLU | ILE | GLY | ALA | MET | LEU | ||||
| 4 | SER | LEU | LEU | GLN | LYS | GLU | GLY | LEU | LEU | MET | ||||
| 5 | SER | PRO | SER | ASP | LEU | TYR | SER | PRO | GLY | SER | ||||
| 6 | TRP | ASP | PRO | ILE | THR | ALA | ALA | LEU | SER | GLN | ||||
| 7 | ARG | ALA | MET | ILE | LEU | GLY | LYS | SER | GLY | GLU | ||||
| 8 | LEU | LYS | THR | TRP | GLY | LEU | VAL | LEU | GLY | ALA | ||||
| 9 | LEU | LYS | ALA | ALA | ARG | GLU | GLU |
Samples:
13C15N: sRSV MA, [U-95% 13C; U-90% 15N], .5 mM; sodium phosphate 50 mM; sodium chloride 50 mM; TCEP 2 mM
15N: sRSV MA, [U-95% 13C; U-90% 15N], .5 mM; sodium phosphate 50 mM; sodium chloride 50 mM; TCEP 2 mM
13C15ND2O: sRSV MA, [U-95% 13C; U-90% 15N], .5 mM; sodium phosphate 50 mM; potassium chloride 50 mM; TCEP 2 mM
sample_conditions_1: ionic strength: 0.100 M; pH: 6.000; pressure: 1.000 atm; temperature: 305 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | 13C15N | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | 13C15N | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC/HMQC | 15N | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC/HMQC | 13C15N | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | 13C15N | isotropic | sample_conditions_1 |
| 3D HNCA | 13C15N | isotropic | sample_conditions_1 |
| 3D HNCACB | 13C15N | isotropic | sample_conditions_1 |
| HNcoCACB (H[N[co[{CA|ca[C]}]]]) | 13C15N | isotropic | sample_conditions_1 |
| 3D HNCO | 13C15N | isotropic | sample_conditions_1 |
| hCCH (hC_CH.relayed) | 13C15N | isotropic | sample_conditions_1 |
| hCCH-aro (hC_CH.relayed) | 13C15N | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | 13C15ND2O | isotropic | sample_conditions_1 |
Software:
CcpNmr_Analysis v2.4, CCPN - spectral analysis
nmrDraw vany, Frank Delaglio - Spectrum analysis, Spectrum display
nmrPipe vany, Frank Delaglio - Spectrum processing
NMR spectrometers:
- Bruker DMX 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts