BMRB Entry 50188
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50188
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Title: Structures of the free and bound forms of the intrinsically disordered plant viral genome-linked protein PubMed: 33269926
Deposition date: 2020-02-02 Original release date: 2021-08-12
Authors: Dixit, Karuna; Karanth, Megha; Nair, Smita; Kumari, Khushboo; Chakraborti, Kalyan; Savitri, H.; Sarma, Siddhartha
Citation: Dixit, Karuna; Karanth, Megha; Nair, Smita; Kumari, Khushboo; Chakraborti, Kalyan; Savitri, H.; Sarma, Siddhartha. "Aromatic Interactions Drive the Coupled Folding and Binding of the Intrinsically Disordered Sesbania mosaic Virus VPg Protein" Biochemistry 59, 4663-4680 (2020).
Assembly members:
entity_1, polymer, 296 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pRSET
Entity Sequences (FASTA):
entity_1: MRGSHHHHHHGMASSLKLNV
GDASNESAVLGSFYSPVKAG
DEPASLVAIKSGPTTIGFGC
RTKIDGEDCLLTAHHVWCNS
MRPTGLAKAGKQVSVEDWEI
SMSSSDKMLDFAIVRVPTHV
WSKLGVKSTPLVCPSSKDVI
TCYGGSSSDCLMSGVGSSST
SEFTWKLTHTCPTAAGWAGT
PLYSSRGVVGMHVGFEEIGK
LNRGVNMFYVANYLLRSNET
LPPELSIIEIPFDDVETRSY
EFIEVEIKGRGKAKLGKREF
AWIPESGKYWADEDEDELPP
PPKLVGGKLVWENAQE
- RDCs
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 461 |
| 15N chemical shifts | 217 |
| 1H chemical shifts | 322 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ProVPg | 1 |
Entities:
Entity 1, ProVPg 296 residues - Formula weight is not available
Karuna Dixit, N. Megha Karanth, Smita Nair, Khushboo Kumari, Kalyan S. Chakraborti, H.S. Savithri, and Siddhartha P Sarma.
| 1 | MET | ARG | GLY | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | GLY | MET | ALA | SER | SER | LEU | LYS | LEU | ASN | VAL | ||||
| 3 | GLY | ASP | ALA | SER | ASN | GLU | SER | ALA | VAL | LEU | ||||
| 4 | GLY | SER | PHE | TYR | SER | PRO | VAL | LYS | ALA | GLY | ||||
| 5 | ASP | GLU | PRO | ALA | SER | LEU | VAL | ALA | ILE | LYS | ||||
| 6 | SER | GLY | PRO | THR | THR | ILE | GLY | PHE | GLY | CYS | ||||
| 7 | ARG | THR | LYS | ILE | ASP | GLY | GLU | ASP | CYS | LEU | ||||
| 8 | LEU | THR | ALA | HIS | HIS | VAL | TRP | CYS | ASN | SER | ||||
| 9 | MET | ARG | PRO | THR | GLY | LEU | ALA | LYS | ALA | GLY | ||||
| 10 | LYS | GLN | VAL | SER | VAL | GLU | ASP | TRP | GLU | ILE | ||||
| 11 | SER | MET | SER | SER | SER | ASP | LYS | MET | LEU | ASP | ||||
| 12 | PHE | ALA | ILE | VAL | ARG | VAL | PRO | THR | HIS | VAL | ||||
| 13 | TRP | SER | LYS | LEU | GLY | VAL | LYS | SER | THR | PRO | ||||
| 14 | LEU | VAL | CYS | PRO | SER | SER | LYS | ASP | VAL | ILE | ||||
| 15 | THR | CYS | TYR | GLY | GLY | SER | SER | SER | ASP | CYS | ||||
| 16 | LEU | MET | SER | GLY | VAL | GLY | SER | SER | SER | THR | ||||
| 17 | SER | GLU | PHE | THR | TRP | LYS | LEU | THR | HIS | THR | ||||
| 18 | CYS | PRO | THR | ALA | ALA | GLY | TRP | ALA | GLY | THR | ||||
| 19 | PRO | LEU | TYR | SER | SER | ARG | GLY | VAL | VAL | GLY | ||||
| 20 | MET | HIS | VAL | GLY | PHE | GLU | GLU | ILE | GLY | LYS | ||||
| 21 | LEU | ASN | ARG | GLY | VAL | ASN | MET | PHE | TYR | VAL | ||||
| 22 | ALA | ASN | TYR | LEU | LEU | ARG | SER | ASN | GLU | THR | ||||
| 23 | LEU | PRO | PRO | GLU | LEU | SER | ILE | ILE | GLU | ILE | ||||
| 24 | PRO | PHE | ASP | ASP | VAL | GLU | THR | ARG | SER | TYR | ||||
| 25 | GLU | PHE | ILE | GLU | VAL | GLU | ILE | LYS | GLY | ARG | ||||
| 26 | GLY | LYS | ALA | LYS | LEU | GLY | LYS | ARG | GLU | PHE | ||||
| 27 | ALA | TRP | ILE | PRO | GLU | SER | GLY | LYS | TYR | TRP | ||||
| 28 | ALA | ASP | GLU | ASP | GLU | ASP | GLU | LEU | PRO | PRO | ||||
| 29 | PRO | PRO | LYS | LEU | VAL | GLY | GLY | LYS | LEU | VAL | ||||
| 30 | TRP | GLU | ASN | ALA | GLN | GLU |
Samples:
sample_1: entity_1, [U-100% 13C; U-100% 15N; U-80% 2H], 0.3 ± 0.02 mM; potassium phosphate buffer 20 mM; NaCl 50 mM; EDTA 1 mM; sodium azide 0.01%
sample_conditions_1: ionic strength: 0.065 M; pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
Analysis, CCPN - data analysis
CcpNMR, CCPN - data analysis
NMR spectrometers:
- Agilent AMX 600 MHz
- Bruker AMX 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts