BMRB Entry 19857
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR19857
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Title: NMR Studies of the Phosphorylation of the Mengovirus Leader Protein Reveal Stabilization of Intermolecular Domain Interactions
Deposition date: 2014-03-15 Original release date: 2014-10-07
Authors: Bacot-Davis, Valjean; Porter, Frederick; Palmenberg, Ann
Citation: Bacot-Davis, Valjean; Ciomperlik, J.; Basta, H.; Cornilescu, Claudia; Palmenberg, Ann. "Solution Structures of Mengovirus Leader Protein, its Phosphorylated Derivatives, and in Complex with Nuclear Transport Protein, RanGTPase" Proc. Nat. Acad. Sci, U.S.A. ., .-. (2014).
Assembly members:
entity_1, polymer, 71 residues, 8422.059 Da.
ZINC ION, non-polymer, 65.409 Da.
Natural source: Common Name: encephalomyocarditisvirus Taxonomy ID: 12107 Superkingdom: Viruses Kingdom: not available Genus/species: Cardiovirus Mengovirus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: GSTAMATTMEQEICAHSMTF
EECPKCSALQYRNGFYLLKY
DEEWXPEELLXDGEDDVFDP
DLDMEVVFETQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 159 |
| 15N chemical shifts | 69 |
| 1H chemical shifts | 209 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | ZINC ION | 2 |
Entities:
Entity 1, entity_1 71 residues - 8422.059 Da.
| 1 | GLY | SER | THR | ALA | MET | ALA | THR | THR | MET | GLU | ||||
| 2 | GLN | GLU | ILE | CYS | ALA | HIS | SER | MET | THR | PHE | ||||
| 3 | GLU | GLU | CYS | PRO | LYS | CYS | SER | ALA | LEU | GLN | ||||
| 4 | TYR | ARG | ASN | GLY | PHE | TYR | LEU | LEU | LYS | TYR | ||||
| 5 | ASP | GLU | GLU | TRP | PTR | PRO | GLU | GLU | LEU | LEU | ||||
| 6 | TPO | ASP | GLY | GLU | ASP | ASP | VAL | PHE | ASP | PRO | ||||
| 7 | ASP | LEU | ASP | MET | GLU | VAL | VAL | PHE | GLU | THR | ||||
| 8 | GLN |
Entity 2, ZINC ION - Zn - 65.409 Da.
| 1 | ZN |
Samples:
sample_1: L MENGO 2P, [U-100% 13C; U-100% 15N], 0.5 mM; HEPES 20 mM; potassium chloride 100 mM; magnesium chloride 2 mM; DTT 2 mM; sodium azide 0.04%; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 102 mM; pH: 7.4; pressure: ambient atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 31-P | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
SPARTA+, Shen and Bax - geometry optimization
SPARKY, Goddard - chemical shift assignment
CARA, Kurt W. Thrich, Swiss Federal Institute of Technology ETH - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts