BMRB Entry 17821
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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/BMR17821
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Title: Human C30S/C59S-Cox17 mutant PubMed: 21816817
Deposition date: 2011-08-01 Original release date: 2011-09-13
Authors: Bertini, Ivano; Ciofi-Baffoni, Simone; Gallo, Angelo
Citation: Banci, Lucia; Bertini, Ivano; Cefaro, Chiara; Ciofi-Baffoni, Simone; Gallo, Angelo. "Functional role of two interhelical disulfide bonds in human Cox17 protein from a structural perspective." J. Biol. Chem. 286, 34382-34390 (2011).
Assembly members:
Human C30S/C59S-Cox17 mutant, polymer, 67 residues, 7288.475 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
Entity Sequences (FASTA):
Human C30S/C59S-Cox17 mutant: GSFTMPGLVDSNPAPPESQE
KKPLKPCCASPETKKARDAC
IIEKGEEHCGHLIEAHKESM
RALGFKI
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 244 |
| 15N chemical shifts | 54 |
| 1H chemical shifts | 221 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Human C30S/C59S-Cox17 mutant | 1 |
Entities:
Entity 1, Human C30S/C59S-Cox17 mutant 67 residues - 7288.475 Da.
GSFT residues are present as cloning artifacts
| 1 | GLY | SER | PHE | THR | MET | PRO | GLY | LEU | VAL | ASP | ||||
| 2 | SER | ASN | PRO | ALA | PRO | PRO | GLU | SER | GLN | GLU | ||||
| 3 | LYS | LYS | PRO | LEU | LYS | PRO | CYS | CYS | ALA | SER | ||||
| 4 | PRO | GLU | THR | LYS | LYS | ALA | ARG | ASP | ALA | CYS | ||||
| 5 | ILE | ILE | GLU | LYS | GLY | GLU | GLU | HIS | CYS | GLY | ||||
| 6 | HIS | LEU | ILE | GLU | ALA | HIS | LYS | GLU | SER | MET | ||||
| 7 | ARG | ALA | LEU | GLY | PHE | LYS | ILE |
Samples:
sample_1: C30S/C59S-Cox17_mutant, [U-100% 15N], 0.5 mM; sodium phosphate 50 mM; EDTA 0.5 mM; DTT 1 mM; D2O 10%; H2O 90%
sample_2: C30S/C59S-Cox17_mutant, [U-99% 13C; U-99% 15N], 1 mM; sodium phosphate 50 mM; EDTA 0.5 mM; DTT 1 mM; D2O 10%; H2O 90%
sample_conditions_1: ionic strength: 50 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - collection, data analysis, processing
CARA v2.1, Keller and Wuthrich - chemical shift assignment
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
PECAN, Eghbalnia, Wang, Bahrami, Assadi, and Markley - data analysis
AMBER v11.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement
NMR spectrometers:
- Bruker Avance 900 MHz
- Bruker Avance 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts