BMRB Entry 16146
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16146
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Saline, Maria; Orekhov, Vladislav; Lindkvist-Petersson, Karin; Karlsson, B. Goran. "Backbone resonance assignment of Staphylococcal Enterotoxin H." Biomol. NMR Assignments 4, 1-4 (2010).
PubMed: 19888679
Assembly members:
SEH, polymer, 217 residues, 25143.2 Da.
Natural source: Common Name: Staphylococcus aureus Taxonomy ID: 1280 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus aureus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: PLR16
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 396 |
| 15N chemical shifts | 207 |
| 1H chemical shifts | 207 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SEH | 1 |
Entities:
Entity 1, SEH 217 residues - 25143.2 Da.
| 1 | GLU | ASP | LEU | HIS | ASP | LYS | SER | GLU | LEU | THR | ||||
| 2 | ASP | LEU | ALA | LEU | ALA | ASN | ALA | TYR | GLY | GLN | ||||
| 3 | TYR | ASN | HIS | PRO | PHE | ILE | LYS | GLU | ASN | ILE | ||||
| 4 | LYS | SER | ASP | GLU | ILE | SER | GLY | GLU | LYS | ASP | ||||
| 5 | LEU | ILE | PHE | ARG | ASN | GLN | GLY | ASP | SER | GLY | ||||
| 6 | ASN | ASP | LEU | ARG | VAL | LYS | PHE | ALA | THR | ALA | ||||
| 7 | ASP | LEU | ALA | GLN | LYS | PHE | LYS | ASN | LYS | ASN | ||||
| 8 | VAL | ASP | ILE | TYR | GLY | ALA | SER | PHE | TYR | TYR | ||||
| 9 | LYS | CYS | GLU | LYS | ILE | SER | GLU | ASN | ILE | SER | ||||
| 10 | GLU | CYS | LEU | TYR | GLY | GLY | THR | THR | LEU | ASN | ||||
| 11 | SER | GLU | LYS | LEU | ALA | GLN | GLU | ARG | VAL | ILE | ||||
| 12 | GLY | ALA | ASN | VAL | TRP | VAL | ASP | GLY | ILE | GLN | ||||
| 13 | LYS | GLU | THR | GLU | LEU | ILE | ARG | THR | ASN | LYS | ||||
| 14 | LYS | ASN | VAL | THR | LEU | GLN | GLU | LEU | ASP | ILE | ||||
| 15 | LYS | ILE | ARG | LYS | ILE | LEU | SER | ASP | LYS | TYR | ||||
| 16 | LYS | ILE | TYR | TYR | LYS | ASP | SER | GLU | ILE | SER | ||||
| 17 | LYS | GLY | LEU | ILE | GLU | PHE | ASP | MET | LYS | THR | ||||
| 18 | PRO | ARG | ASP | TYR | SER | PHE | ASP | ILE | TYR | ASP | ||||
| 19 | LEU | LYS | GLY | GLU | ASN | ASP | TYR | GLU | ILE | ASP | ||||
| 20 | LYS | ILE | TYR | GLU | ASP | ASN | LYS | THR | LEU | LYS | ||||
| 21 | SER | ASP | ASP | ILE | SER | HIS | ILE | ASP | VAL | ASN | ||||
| 22 | LEU | TYR | THR | LYS | LYS | LYS | VAL |
Samples:
sample_1: SEH, [U-100% 13C; U-100% 15N; 80% 2H], 0.8 mM; ammonium acetate 300 mM; sodium chloride 150 mM
sample_2: SEH, [U-100% 13C; U-100% 15N], 1.6 mM; TRIS 20 uM; sodium chloride 150 uM
sample_conditions_1: ionic strength: 150 mM; pH: 6.8; pressure: 1 atm; temperature: 313 K
sample_conditions_2: ionic strength: 150 mM; pH: 7.0; temperature: 313 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_2 |
| 3D 1H-15N TOCSY | sample_2 | isotropic | sample_conditions_2 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_2 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_2 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_2 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_2 |
Software:
CCPN, CCPN - chemical shift assignment
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Varian INOVA 900 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks