BMRB Entry 19962
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19962
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Lim, Liangzhong; Lee, Xiaowen; Song, Jianxing. "Mechanism for transforming cytosolic SOD1 into integral membrane proteins of organelles by ALS-causing mutations" Biochim. Biophys. Acta 1848, 1-7 (2015).
Assembly members:
L126Z-sod1, polymer, 125 residues, 13153.691 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 Vector: pET28a
Entity Sequences (FASTA):
L126Z-sod1: ATKAVCVLKGDGPVQGIINF
EQKESNGPVKVWGSIKGLTE
GLHGFHVHEFGDNTAGCTSA
GPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIE
DSVISLSGDHCIIGRTLVVH
EKADD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 230 |
| 15N chemical shifts | 117 |
| 1H chemical shifts | 252 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Truncated L126Z-sod1 | 1 |
Entities:
Entity 1, Truncated L126Z-sod1 125 residues - 13153.691 Da.
| 1 | ALA | THR | LYS | ALA | VAL | CYS | 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 | CYS | ILE | ILE | GLY | ARG | THR | LEU | VAL | VAL | HIS | ||||
| 13 | GLU | LYS | ALA | ASP | ASP |
Samples:
sample_1: L126Z-sod1, [U-100% 13C; U-100% 15N], 400 uM; dodecylphosphocholine (DPC) 20 mM; H2O 90%; D2O, [U-100% 2H], 10%
sample_conditions_1: pH: 4; pressure: 1 atm; temperature: 313 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 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 |
Software:
Cyana v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Bruker Avance 800 MHz
Related Database Links:
| BMRB | 18509 18708 26570 |
| 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 |
| AlphaFold | P00441 P60052 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks