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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25793
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
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Citation: Jureka, Alexander; Kleinpeter, Alexander; Cornilescu, Gabriel; Cornilescu, Claudia; Schwieters, Charles; Petit, Chad. "Structural Basis for a Novel Interaction between the NS1 Protein Derived from the 1918 Influenza Virus and RIG-I" Structure 23, 2001-2010 (2015).
PubMed: 26365801
Assembly members:
Influenza_NS1_RNA_Binding_Domain, polymer, 73 residues, 16801.115 Da.
Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-SUMO
Entity Sequences (FASTA):
Influenza_NS1_RNA_Binding_Domain: MDSNTVSSFQVDCFLWHVRK
RFADQELGDAPFLDRLRRDQ
KSLRGRGSTLGLDIETATRA
GKQIVERILKEES
Data type | Count |
13C chemical shifts | 311 |
15N chemical shifts | 71 |
1H chemical shifts | 458 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | entity | 1 |
Entity 1, entity 73 residues - 16801.115 Da.
1 | MET | ASP | SER | ASN | THR | VAL | SER | SER | PHE | GLN | ||||
2 | VAL | ASP | CYS | PHE | LEU | TRP | HIS | VAL | ARG | LYS | ||||
3 | ARG | PHE | ALA | ASP | GLN | GLU | LEU | GLY | ASP | ALA | ||||
4 | PRO | PHE | LEU | ASP | ARG | LEU | ARG | ARG | ASP | GLN | ||||
5 | LYS | SER | LEU | ARG | GLY | ARG | GLY | SER | THR | LEU | ||||
6 | GLY | LEU | ASP | ILE | GLU | THR | ALA | THR | ARG | ALA | ||||
7 | GLY | LYS | GLN | ILE | VAL | GLU | ARG | ILE | LEU | LYS | ||||
8 | GLU | GLU | SER |
sample_1: Influenza NS1 RNA Binding Domain, [U-13C; U-15N], 1.0 mM; Ammonium Acetate pH 6.0 300 mM; EDTA 2.2 mM; sodium azide 0.1%; H2O 95%; D2O 5%
sample_2: Influenza NS1 RNA Binding Domain, [U-15N], 1 mM; Ammonium Acetate pH 6.0 300 mM; EDTA 2.0 mM; sodium azide 0.1%; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 300 mM; pH: 6; pressure: 1 atm; temperature: 273 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | 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 HNHA | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-COSY | 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 |
3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - chemical shift assignment
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement
TALOS, Cornilescu, Delaglio and Bax - refinement
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks