BMRB Entry 17256
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17256
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Title: Solution structure of Ste5PM24 in the presence of SDS micelle PubMed: 20933496
Deposition date: 2010-10-15 Original release date: 2011-03-30
Authors: Bhunia, A.; Bhattacharjya, S.
Citation: Saravanan, Rathi; Bhattacharjya, Surajit. "Oligomeric structure of a cathelicidin antimicrobial peptide in dodecylphosphocholine micelle determined by NMR spectroscopy." Biochim. Biophys. Acta 1808, 369-381 (2011).
Assembly members:
PROTEIN_STE5, polymer, 24 residues, 2897.501 Da.
Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
PROTEIN_STE5: PLSRGKKWTEKLARFQRSSA
KKKR
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 110 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PROTEIN STE5 | 1 |
Entities:
Entity 1, PROTEIN STE5 24 residues - 2897.501 Da.
| 1 | PRO | LEU | SER | ARG | GLY | LYS | LYS | TRP | THR | GLU | ||||
| 2 | LYS | LEU | ALA | ARG | PHE | GLN | ARG | SER | SER | ALA | ||||
| 3 | LYS | LYS | LYS | ARG |
Samples:
sample_1: PROTEIN STE5 0.5 mM; H2O 90%; D2O 10%; SDS 200 mM
sample_conditions_1: pH: 4.5; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- BRUKER DRX 600 MHz