BMRB Entry 51439
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51439
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Title: 1H, 13C,15N assignment of human CISD3 mitochondrial protein PubMed: 36502664
Deposition date: 2022-05-13 Original release date: 2022-12-12
Authors: Silva, Jose; Grifagni, Deborah; Cantini, Francesca; Piccioli, Mario; Banci, Lucia
Citation: Grifagni, Deborah; Silva, Jose; Cantini, Francesca; Piccioli, Mario; Banci, Lucia. "Relaxation-based NMR assignment: Spotlights on ligand binding sites in human CISD3" J. Inorg. Biochem. 239, 112089-112089 (2022).
Assembly members:
entity_1, polymer, 93 residues, 10360.14 Da.
entity_FES, non-polymer, 175.820 Da.
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 Vector: PET28a(+)
Entity Sequences (FASTA):
entity_1: MGARSVVALKTPIKVELVAG
KTYRWCVCGRSKKQPFCDGS
HFFQRTGLSPLKFKAQETRM
VALCTCKATQRPPYCDGTHR
SERVQKAEVGSPL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 166 |
| 15N chemical shifts | 60 |
| 1H chemical shifts | 59 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CISD3 | 1 |
| 2 | Fe2-S2, 1 | 2 |
| 3 | Fe2-S2, 2 | 2 |
Entities:
Entity 1, CISD3 93 residues - 10360.14 Da.
Construct of CISD3
| 1 | MET | GLY | ALA | ARG | SER | VAL | VAL | ALA | LEU | LYS | ||||
| 2 | THR | PRO | ILE | LYS | VAL | GLU | LEU | VAL | ALA | GLY | ||||
| 3 | LYS | THR | TYR | ARG | TRP | CYS | VAL | CYS | GLY | ARG | ||||
| 4 | SER | LYS | LYS | GLN | PRO | PHE | CYS | ASP | GLY | SER | ||||
| 5 | HIS | PHE | PHE | GLN | ARG | THR | GLY | LEU | SER | PRO | ||||
| 6 | LEU | LYS | PHE | LYS | ALA | GLN | GLU | THR | ARG | MET | ||||
| 7 | VAL | ALA | LEU | CYS | THR | CYS | LYS | ALA | THR | GLN | ||||
| 8 | ARG | PRO | PRO | TYR | CYS | ASP | GLY | THR | HIS | ARG | ||||
| 9 | SER | GLU | ARG | VAL | GLN | LYS | ALA | GLU | VAL | GLY | ||||
| 10 | SER | PRO | LEU |
Entity 2, Fe2-S2, 1 - Fe2 S2 - 175.820 Da.
| 1 | FES |
Samples:
sample_1: CISD3, [U-99% 13C; U-99% 15N], 0.5 mM; sodium phosphate 50 mM
sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC ANTIPHASE | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC ANTIPHASE INVERSION RECOVERY | sample_1 | isotropic | sample_conditions_1 |
| 2D 13C-detected CACO | sample_1 | isotropic | sample_conditions_1 |
| 2D 13C-detected CON | sample_1 | isotropic | sample_conditions_1 |
| 2D 13C-detected CON PARAMAGNETIC | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA v1.9 - chemical shift assignment
TOPSPIN v3.6 - collection
NMR spectrometers:
- Bruker AVANCE NEO 700 MHz
- Bruker AVANCE NEO 500 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts