BMRB Entry 30396
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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/BMR30396
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Title: The clavanin peptide in the presence of TFE (2,2,2-trifluoroethanol), presented a amphipathic alpha-helices from Phe-2 to Val-22 residues PubMed: 27292548
Deposition date: 2018-01-11 Original release date: 2018-02-02
Authors: Alves, E.; Liao, L.
Citation: Silva, O.; Alves, E.; de la Fuente-Nunez, C.; Ribeiro, S.; Mandal, S.; Gaspar, D.; Veiga, A.; Castanho, M.; Andrade, C.; Nascimento, J.; Fensterseifer, I.; Porto, W.; Correa, J.; Hancock, R.; Korpole, S.; Oliveira, A.; Liao, L.; Franco, O.. "Structural Studies of a Lipid-Binding Peptide from Tunicate Hemocytes with Anti-Biofilm Activity." Sci. Rep. 6, 27128-27128 (2016).
Assembly members:
entity_1, polymer, 24 residues, 2670.120 Da.
Natural source: Common Name: Sea squirt Taxonomy ID: 7725 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Styela clava
Experimental source: Production method: recombinant technology Host organism: Styela clava
Entity Sequences (FASTA):
entity_1: VFQFLGKIIHHVGNFVHGFS
HVFX
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 15N chemical shifts | 24 |
| 1H chemical shifts | 140 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 24 residues - 2670.120 Da.
| 1 | VAL | PHE | GLN | PHE | LEU | GLY | LYS | ILE | ILE | HIS | ||||
| 2 | HIS | VAL | GLY | ASN | PHE | VAL | HIS | GLY | PHE | SER | ||||
| 3 | HIS | VAL | PHE | NH2 |
Samples:
sample_1: TFE, [U-99% 2H], 35%; D2O, [U-99% 2H], 10%; H2O 55%; Clavanin A 2 mM
sample_conditions_1: pH: 4.3; pressure: 1 atm; temperature: 298 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 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HMQC | sample_1 | isotropic | sample_conditions_1 |
Software:
X-PLOR, Brunger - refinement, structure calculation
NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
NMR spectrometers:
- 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