BMRB Entry 25942
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25942
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Title: Full-length WT SOD1 in DPC MICELLE PubMed: 27378311
Deposition date: 2016-01-06 Original release date: 2016-12-08
Authors: Lim, Liangzhong; Song, Jianxing
Citation: Lim, Liangzhong; Song, Jianxing. "SALS-linked WT-SOD1 adopts a highly similar helical conformation as FALS-causing L126Z-SOD1 in a membrane environment" Biochim. Biophys. Acta 1858, 2223-2230 (2016).
Assembly members:
entity, polymer, 161 residues, 15827.688 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: MGHHHHHHATKAVCVLKGDG
PVQGIINFEQKESNGPVKVW
GSIKGLTEGLHGFHVHEFGD
NTAGCTSAGPHFNPLSRKHG
GPKDEERHVGDLGNVTADKD
GVADVSIEDSVISLSGDHCI
IGRTLVVHEKADDLGKGGNE
ESTKTGNAGSRLACGVIGIA
Q
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 279 |
| 15N chemical shifts | 158 |
| 1H chemical shifts | 721 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 161 residues - 15827.688 Da.
Residue 1-8 are the non-native affinity 6xHis-tag of full-length SOD1
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | ALA | THR | ||||
| 2 | LYS | ALA | VAL | CYS | VAL | LEU | LYS | GLY | ASP | GLY | ||||
| 3 | PRO | VAL | GLN | GLY | ILE | ILE | ASN | PHE | GLU | GLN | ||||
| 4 | LYS | GLU | SER | ASN | GLY | PRO | VAL | LYS | VAL | TRP | ||||
| 5 | GLY | SER | ILE | LYS | GLY | LEU | THR | GLU | GLY | LEU | ||||
| 6 | HIS | GLY | PHE | HIS | VAL | HIS | GLU | PHE | GLY | ASP | ||||
| 7 | ASN | THR | ALA | GLY | CYS | THR | SER | ALA | GLY | PRO | ||||
| 8 | HIS | PHE | ASN | PRO | LEU | SER | ARG | LYS | HIS | GLY | ||||
| 9 | GLY | PRO | LYS | ASP | GLU | GLU | ARG | HIS | VAL | GLY | ||||
| 10 | ASP | LEU | GLY | ASN | VAL | THR | ALA | ASP | LYS | ASP | ||||
| 11 | GLY | VAL | ALA | ASP | VAL | SER | ILE | GLU | ASP | SER | ||||
| 12 | VAL | ILE | SER | LEU | SER | GLY | ASP | HIS | CYS | ILE | ||||
| 13 | ILE | GLY | ARG | THR | LEU | VAL | VAL | HIS | GLU | LYS | ||||
| 14 | ALA | ASP | ASP | LEU | GLY | LYS | GLY | GLY | ASN | GLU | ||||
| 15 | GLU | SER | THR | LYS | THR | GLY | ASN | ALA | GLY | SER | ||||
| 16 | ARG | LEU | ALA | CYS | GLY | VAL | ILE | GLY | ILE | ALA | ||||
| 17 | GLN |
Samples:
sample_1: DPC 20 mM; entity, [U-13C; U-15N], 0.4 mM
sample_conditions_1: ionic strength: 0 M; pH: 4; pressure: 1 atm; temperature: 313 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
Gromacs v4.5.3, David van der Spoel, and Erik Lindahl - refinement
Cyana v2, Guntert, Mumenthaler and Wuthrich - structure solution
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