BMRB Entry 25912
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25912
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Title: Backbone 1H, 13C, and 15N Chemical Shift of bacterial IscA protein PubMed: 26887894
Deposition date: 2015-12-01 Original release date: 2016-01-19
Authors: Pastore, Annalisa; Popovic, Matija; Kelly, Geoff
Citation: Popovic, Matija; Kelly, Geoff; Pastore, Annalisa. "Chemical shift assignment of the difficult protein IscA" Biomol. NMR Assign. 10, 227-231 (2016).
Assembly members:
IscA, polymer, 107 residues, Formula weight is not available
Natural source: Common Name: enterobacteria Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: Eubacteria Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET30
Entity Sequences (FASTA):
IscA: MSITLSDSAAARVNTFLANR
GKGFGLRLGVRTSGCSGMAY
VLEFVDEPTPEDIVFEDKGV
KVVVDGKSLQFLDGTQLDFV
KEGLNEGFKFTNPNVKDECG
CGESFHV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 270 |
| 15N chemical shifts | 91 |
| 1H chemical shifts | 166 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | IscA, 1 | 1 |
| 2 | IscA, 2 | 1 |
Entities:
Entity 1, IscA, 1 107 residues - Formula weight is not available
| 1 | MET | SER | ILE | THR | LEU | SER | ASP | SER | ALA | ALA | ||||
| 2 | ALA | ARG | VAL | ASN | THR | PHE | LEU | ALA | ASN | ARG | ||||
| 3 | GLY | LYS | GLY | PHE | GLY | LEU | ARG | LEU | GLY | VAL | ||||
| 4 | ARG | THR | SER | GLY | CYS | SER | GLY | MET | ALA | TYR | ||||
| 5 | VAL | LEU | GLU | PHE | VAL | ASP | GLU | PRO | THR | PRO | ||||
| 6 | GLU | ASP | ILE | VAL | PHE | GLU | ASP | LYS | GLY | VAL | ||||
| 7 | LYS | VAL | VAL | VAL | ASP | GLY | LYS | SER | LEU | GLN | ||||
| 8 | PHE | LEU | ASP | GLY | THR | GLN | LEU | ASP | PHE | VAL | ||||
| 9 | LYS | GLU | GLY | LEU | ASN | GLU | GLY | PHE | LYS | PHE | ||||
| 10 | THR | ASN | PRO | ASN | VAL | LYS | ASP | GLU | CYS | GLY | ||||
| 11 | CYS | GLY | GLU | SER | PHE | HIS | VAL |
Samples:
sample_1: IscA, [U-99% 13C; U-99% 15N], 50 – 400 uM; Tris-HCl 20 mM; NaCl 150 mM; TCEP 5 mM; H2O 93%; D2O 7%
sample_conditions_1: ionic strength: 0.150 M; pH: 7.5; 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 CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts