BMRB Entry 25462
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25462
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Title: Backbone Chemical Shift Assignments for the Monomeric [R238A] Mutant of Non-Structural Protein 1 Effector Domain from Influenza B Virus PubMed: 27545620
Deposition date: 2015-02-02 Original release date: 2015-03-02
Authors: Hamilton, Keith; Aramini, James; Ma, Li-Chung; Krug, Robert; Montelione, Gaetano
Citation: Ma, Li-Chung; Guan, Rongjin; Hamilton, Keith; Aramini, James; Mao, Lei; Wang, Shanshan; Krug, Robert; Montelione, Gaetano. "A Second RNA-Binding Site in the NS1 Protein of Influenza B Virus." Structure 24, 1562-1572 (2016).
Assembly members:
[R238A] NS1B ED, polymer, 141 residues, Formula weight is not available
Natural source: Common Name: Influenza B virus Taxonomy ID: 11520 Superkingdom: Viruses Kingdom: not available Genus/species: Influenzavirus B Influenza B virus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
[R238A] NS1B ED: HPIEVVLRDMNNKDARQKIK
DEVNTQKEGKFRLTIKRDIR
NVLSLRVLVNGTFLKHPNGD
KSLSTLHRLNAYDQNGGLVA
KLVATDDLTVEDEKDGHAIL
NSLFERFDEGHSKPIRAAET
AVGVLSQFGQEHRLSPEEGD
N
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 408 |
| 15N chemical shifts | 136 |
| 1H chemical shifts | 136 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | [R238A] NS1B ED | 1 |
Entities:
Entity 1, [R238A] NS1B ED 141 residues - Formula weight is not available
| 1 | HIS | PRO | ILE | GLU | VAL | VAL | LEU | ARG | ASP | MET | ||||
| 2 | ASN | ASN | LYS | ASP | ALA | ARG | GLN | LYS | ILE | LYS | ||||
| 3 | ASP | GLU | VAL | ASN | THR | GLN | LYS | GLU | GLY | LYS | ||||
| 4 | PHE | ARG | LEU | THR | ILE | LYS | ARG | ASP | ILE | ARG | ||||
| 5 | ASN | VAL | LEU | SER | LEU | ARG | VAL | LEU | VAL | ASN | ||||
| 6 | GLY | THR | PHE | LEU | LYS | HIS | PRO | ASN | GLY | ASP | ||||
| 7 | LYS | SER | LEU | SER | THR | LEU | HIS | ARG | LEU | ASN | ||||
| 8 | ALA | TYR | ASP | GLN | ASN | GLY | GLY | LEU | VAL | ALA | ||||
| 9 | LYS | LEU | VAL | ALA | THR | ASP | ASP | LEU | THR | VAL | ||||
| 10 | GLU | ASP | GLU | LYS | ASP | GLY | HIS | ALA | ILE | LEU | ||||
| 11 | ASN | SER | LEU | PHE | GLU | ARG | PHE | ASP | GLU | GLY | ||||
| 12 | HIS | SER | LYS | PRO | ILE | ARG | ALA | ALA | GLU | THR | ||||
| 13 | ALA | VAL | GLY | VAL | LEU | SER | GLN | PHE | GLY | GLN | ||||
| 14 | GLU | HIS | ARG | LEU | SER | PRO | GLU | GLU | GLY | ASP | ||||
| 15 | ASN |
Samples:
sample_1: [R238A] NS1B ED, [U-100% 13C; U-100% 15N], 300 uM; ammonium acetate 25 mM; sodium chloride 450 mM; calcium chloride 5 mM; arginine 50 mM; sodium azide 0.02%; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.45 M; pH: 5.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | 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 HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - data collection
NMRPipe v2.1, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data processing
PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
AutoAssign v2.4.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
AVS v2.4.0, Moseley and Montelione - chemical shift validation
SPARKY v3, Goddard - data analysis
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