BMRB Entry 26570
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26570
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Backbone and sidechain 1H, 13C and 15N chemical shifts for human superoxide dismutase (hSOD1) lacking bound metal and the intrasubunit disulfide bond PubMed: 26099300
Deposition date: 2015-05-04 Original release date: 2015-06-08
Authors: Kay, Lewis; Sekhar, Ashok; Rumfeldt, Jessica; Broom, Helen; Doyle, Colleen; Meiering, Elizabeth
Citation: Sekhar, Ashok; Rumfeldt, Jessica; Broom, Helen; Doyle, Colleen; Meiering, Elizabeth; Kay, Lewis. "Thermal Fluctuations of Immature SOD1 Lead to Separate Folding and Misfolding Pathways" ELife 4, e07296-e07296 (2015).
Assembly members:
SOD1, polymer, 153 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
SOD1: ATKAVAVLKGDGPVQGIINF
EQKESNGPVKVWGSIKGLTE
GLHGFHVHEFGDNTAGCTSA
GPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIE
DSVISLSGDHSIIGRTLVVH
EKADDLGKGGNEESTKTGNA
GSRLACGVIGIAQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 546 |
| 15N chemical shifts | 136 |
| 1H chemical shifts | 829 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SOD1 monomer | 1 |
Entities:
Entity 1, SOD1 monomer 153 residues - Formula weight is not available
| 1 | ALA | THR | LYS | ALA | VAL | ALA | VAL | LEU | LYS | GLY | ||||
| 2 | ASP | GLY | PRO | VAL | GLN | GLY | ILE | ILE | ASN | PHE | ||||
| 3 | GLU | GLN | LYS | GLU | SER | ASN | GLY | PRO | VAL | LYS | ||||
| 4 | VAL | TRP | GLY | SER | ILE | LYS | GLY | LEU | THR | GLU | ||||
| 5 | GLY | LEU | HIS | GLY | PHE | HIS | VAL | HIS | GLU | PHE | ||||
| 6 | GLY | ASP | ASN | THR | ALA | GLY | CYS | THR | SER | ALA | ||||
| 7 | GLY | PRO | HIS | PHE | ASN | PRO | LEU | SER | ARG | LYS | ||||
| 8 | HIS | GLY | GLY | PRO | LYS | ASP | GLU | GLU | ARG | HIS | ||||
| 9 | VAL | GLY | ASP | LEU | GLY | ASN | VAL | THR | ALA | ASP | ||||
| 10 | LYS | ASP | GLY | VAL | ALA | ASP | VAL | SER | ILE | GLU | ||||
| 11 | ASP | SER | VAL | ILE | SER | LEU | SER | GLY | ASP | HIS | ||||
| 12 | SER | ILE | ILE | GLY | ARG | THR | LEU | VAL | VAL | HIS | ||||
| 13 | GLU | LYS | ALA | ASP | ASP | LEU | GLY | LYS | GLY | GLY | ||||
| 14 | ASN | GLU | GLU | SER | THR | LYS | THR | GLY | ASN | ALA | ||||
| 15 | GLY | SER | ARG | LEU | ALA | CYS | GLY | VAL | ILE | GLY | ||||
| 16 | ILE | ALA | GLN |
Samples:
sample_1: SOD1, [U-99% 13C; U-99% 15N], 1.5 mM; HEPES 20 mM; NaN3 1 mM; TCEP 1 mM
sample_conditions_1: ionic strength: 0.02 M; pH: 7.4; pressure: 1 atm; temperature: 298 K
Experiments:
| 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 HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Varian INOVA 800 MHz
- Varian INOVA 600 MHz
Related Database Links:
| BMRB | 15711 15712 15713 15714 18509 18708 18968 19962 4202 |
| PDB | |
| DBJ | BAA14373 BAC20345 BAG35052 BAG73767 |
| EMBL | CAA26182 CAG29351 CAG46542 |
| GB | AAA72747 AAA80237 AAB05661 AAB05662 AAB27818 |
| REF | NP_000445 NP_001009025 XP_003813274 XP_004062735 XP_004062736 |
| SP | P00441 P60052 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts