BMRB Entry 15790
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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/BMR15790
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Title: NMR STRUCTURE OF THE N-TERMINAL COILED COIL DOMAIN OF THE ANDES HANTAVIRUS NUCLEOCAPSID PROTEIN PubMed: 18687679
Deposition date: 2008-05-30 Original release date: 2008-07-29
Authors: Wang, Yu; Boudreaux, Daniel; Estrada, David; Egan, Chet; St. Jeor, Stephen; De Guzman, Roberto
Citation: Wang, Yu; Boudreaux, Daniel; Estrada, David; Egan, Chet; St. Jeor, Stephen; De Guzman, Roberto. "NMR STRUCTURE OF THE N-TERMINAL COILED COIL DOMAIN OF THE ANDES HANTAVIRUS NUCLEOCAPSID PROTEIN" J. Biol. Chem. 283, 28297-28304 (2008).
Assembly members:
ANDES HANTAVIRUS NUCLEOCAPSID PROTEIN, polymer, 107 residues, 12071.731 Da.
Natural source: Common Name: Andes Hantavirus Taxonomy ID: 46607 Superkingdom: Viruses Kingdom: not available Genus/species: Hantavirus Andes virus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
ANDES HANTAVIRUS NUCLEOCAPSID PROTEIN: MHHHHHHGKPIPNPLLGLDS
TENLYFQGIDPFTMSTLQEL
QENITAHEQQLVTARQKLKD
AEKAVEVDPDDVNKSTLQNR
RAAVSTLETKLGELKRQLAD
LVAAQKL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 416 |
| 15N chemical shifts | 96 |
| 1H chemical shifts | 670 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ANDES HANTAVIRUS NUCLEOCAPSID PROTEIN | 1 |
Entities:
Entity 1, ANDES HANTAVIRUS NUCLEOCAPSID PROTEIN 107 residues - 12071.731 Da.
| 1 | MET | HIS | HIS | HIS | HIS | HIS | HIS | GLY | LYS | PRO | ||||
| 2 | ILE | PRO | ASN | PRO | LEU | LEU | GLY | LEU | ASP | SER | ||||
| 3 | THR | GLU | ASN | LEU | TYR | PHE | GLN | GLY | ILE | ASP | ||||
| 4 | PRO | PHE | THR | MET | SER | THR | LEU | GLN | GLU | LEU | ||||
| 5 | GLN | GLU | ASN | ILE | THR | ALA | HIS | GLU | GLN | GLN | ||||
| 6 | LEU | VAL | THR | ALA | ARG | GLN | LYS | LEU | LYS | ASP | ||||
| 7 | ALA | GLU | LYS | ALA | VAL | GLU | VAL | ASP | PRO | ASP | ||||
| 8 | ASP | VAL | ASN | LYS | SER | THR | LEU | GLN | ASN | ARG | ||||
| 9 | ARG | ALA | ALA | VAL | SER | THR | LEU | GLU | THR | LYS | ||||
| 10 | LEU | GLY | GLU | LEU | LYS | ARG | GLN | LEU | ALA | ASP | ||||
| 11 | LEU | VAL | ALA | ALA | GLN | LYS | LEU |
Samples:
sample_1: entity, [U-100% 13C; U-100% 15N], 1.0 ± 0.1 mM; sodium phosphate 10 mM; sodium chloride 10 mM; H2O 90%; D2O 10%
sample_2: entity, [U-100% 13C; U-100% 15N], 1.0 ± 0.1 mM; sodium phosphate 10 mM; sodium chloride 10 mM; D2O 100%
sample_3: entity, [U-100% 15N], 1.0 ± 0.1 mM; sodium phosphate 10 mM; sodium chloride 10 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.028 M; pH: 6.9; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView v5.0.4, Johnson, One Moon Scientific - data analysis
CYANA v1.0, Guntert, Mumenthaler and Wuthrich - refinement, structure solution
AMBER v7, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement
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