BMRB Entry 19216
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19216
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Title: Structural and Functional Analysis of Transmembrane Segment IV of the Salt Tolerance Protein Sod2 PubMed: 23836910
Deposition date: 2013-05-02 Original release date: 2013-06-04
Authors: Ullah, Asad; Kemp, Grant; Lee, Brian; Alves, Claudia; Young, Howard; Sykes, Brian; Fliegel, Larry
Citation: Ullah, Asad; Kemp, Grant; Lee, Brian; Alves, Claudia; Young, Howard; Sykes, Brian; Fliegel, Larry. "Structural and Functional Analysis of Transmembrane Segment IV of the Salt Tolerance Protein Sod2." J. Biol. Chem. 288, 24609-24624 (2013).
Assembly members:
sod2_TM_IV, polymer, 38 residues, 3073.673 Da.
Natural source: Common Name: Fission yeast Taxonomy ID: 4896 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Schizosaccharomyces pombe
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pMal-c2x
Entity Sequences (FASTA):
sod2_TM_IV: GSKKKLFPQINFLGSLLIAG
CITSTDPVLSALIVGKKK
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 35 |
| 1H chemical shifts | 176 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | sod2_TM_IV | 1 |
Entities:
Entity 1, sod2_TM_IV 38 residues - 3073.673 Da.
| 1 | GLY | SER | LYS | LYS | LYS | LEU | PHE | PRO | GLN | ILE | ||||
| 2 | ASN | PHE | LEU | GLY | SER | LEU | LEU | ILE | ALA | GLY | ||||
| 3 | CYS | ILE | THR | SER | THR | ASP | PRO | VAL | LEU | SER | ||||
| 4 | ALA | LEU | ILE | VAL | GLY | LYS | LYS | LYS |
Samples:
sample_1: sod2_TM_IV, [U-99% 15N], 0.2 – 0.7 mM; CDCl3 50 v/v; 2-propanol 50 v/v
sample_conditions_1: pressure: 1 atm; temperature: 303.15 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
Software:
VNMRJ, Varian - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRViewJ, Johnson, One Moon Scientific - data analysis, peak picking
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution
NMR spectrometers:
- Varian INOVA 500 MHz
Related Database Links:
| PDB |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
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