BMRB Entry 19002
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19002
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Title: Solution structure of the Core Domain (11-85) of the Murine Norovirus VPg protein. PubMed: 23487472
Deposition date: 2013-02-05 Original release date: 2013-03-21
Authors: Leen, Eoin; Kwok, Rex; Birtley, James; Prater, Sean; Simpson, Pete; Matthews, Steve; Marchant, Jan; Curry, Stephen
Citation: Leen, Eoin; Kwok, K. Y Rex; Birtley, James; Simpson, Peter; Subba-Reddy, Chennareddy; Chaudhry, Yasmin; Sosnovtsev, Stanislav; Green, Kim; Prater, Sean; Tong, Michael; Young, Joanna; Chung, Liliane; Marchant, Jan; Roberts, Lisa; Kao, C. Cheng; Matthews, Stephen; Goodfellow, Ian; Curry, Stephen. "Structures of the Compact Helical Core Domains of Feline Calicivirus and Murine Norovirus VPg Proteins." J. Virol. 87, 5318-5330 (2013).
Assembly members:
MNV_VPg, polymer, 75 residues, 8876.859 Da.
Natural source: Common Name: Murine norovirus Taxonomy ID: 357231 Superkingdom: Viruses Kingdom: not available Genus/species: Murine Norovirus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
MNV_VPg: GRPGVFRTRGLTDEEYDEFK
KRRESRGGKYSIDDYLADRE
REEELLERDEEEAIFGDGFG
LKATRRSRKAERAKL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 330 |
| 15N chemical shifts | 75 |
| 1H chemical shifts | 507 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | MNV_VPg | 1 |
Entities:
Entity 1, MNV_VPg 75 residues - 8876.859 Da.
| 1 | GLY | ARG | PRO | GLY | VAL | PHE | ARG | THR | ARG | GLY | ||||
| 2 | LEU | THR | ASP | GLU | GLU | TYR | ASP | GLU | PHE | LYS | ||||
| 3 | LYS | ARG | ARG | GLU | SER | ARG | GLY | GLY | LYS | TYR | ||||
| 4 | SER | ILE | ASP | ASP | TYR | LEU | ALA | ASP | ARG | GLU | ||||
| 5 | ARG | GLU | GLU | GLU | LEU | LEU | GLU | ARG | ASP | GLU | ||||
| 6 | GLU | GLU | ALA | ILE | PHE | GLY | ASP | GLY | PHE | GLY | ||||
| 7 | LEU | LYS | ALA | THR | ARG | ARG | SER | ARG | LYS | ALA | ||||
| 8 | GLU | ARG | ALA | LYS | LEU |
Samples:
sample_1: MNV VPg 11-85, [U-98% 13C; U-98% 15N], 590 uM; sodium phosphate 50 mM; Sodium chloride 300 mM; DTT 1 mM; H2O 90%; D2O 10%
sample_2: MNV VPg 11-85, [U-98% 13C; U-98% 15N], 710 uM; sodium chloride 360 mM; sodium azide 0.1 w/v; DTT 1 mM; sodium phosphate pH 6.5 60 mM; D2O 100%
sample_conditions_1: ionic strength: 300 mM; pH: 6.5; pressure: 1 atm; temperature: 303 K
sample_conditions_2: ionic strength: 360 mM; pH: 6.5; pressure: 1 Pa; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D H(C)CH-TOCSY | sample_2 | isotropic | sample_conditions_2 |
| 2D 1H-13C HSQC aliphatic | sample_2 | isotropic | sample_conditions_2 |
| 3D (H)CCH-TOCSY | sample_2 | isotropic | sample_conditions_2 |
| 2D 1H-13C HSQC aromatic | sample_2 | isotropic | sample_conditions_2 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CC)(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)C(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D (HB)CB(CGCD)HD | sample_2 | isotropic | sample_conditions_2 |
| 3D (HB)CB(CGCDCE)HE | sample_2 | isotropic | sample_conditions_2 |
| 3D HBHA(CBCACO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_2 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
ARIA, Linge, O, . - structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis
MARS, Zweckstetter et al., 2004 - chemical shift assignment
NMR spectrometers:
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts