BMRB Entry 30211
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30211
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Ocellatin-LB1
Deposition date: 2016-12-17 Original release date: 2017-12-08
Authors: Gusmao, K.; Santos, D.; de Lima, M.; Pilo-Veloso, D.; Resende, J.
Citation: Gusmao, K.; Santos, D.; Verly, R.; de Lima, M.; Pilo-Veloso, D.; Resende, J.. "NMR structures in different membrane environments of three ocellatin peptides isolated from Leptodactylus labyrinthicus" . ., .-..
Assembly members:
entity_1, polymer, 23 residues, 2195.648 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):
entity_1: GVVDILKGAAKDIAGHLASK
VMX
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 68 |
| 15N chemical shifts | 20 |
| 1H chemical shifts | 145 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 23 residues - 2195.648 Da.
| 1 | GLY | VAL | VAL | ASP | ILE | LEU | LYS | GLY | ALA | ALA | ||||
| 2 | LYS | ASP | ILE | ALA | GLY | HIS | LEU | ALA | SER | LYS | ||||
| 3 | VAL | MET | NH2 |
Samples:
sample_1: DSS 1 mM; H2O 40%; Ocellatin-LB1 2.0 mM; TFE, d2, 60%; potassium phosphate 20 mM
sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 293.15 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H TOCSY | sample_1 | not available | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | not available | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | not available | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | not available | sample_conditions_1 |
Software:
Molmol, Koradi, Billeter and Wuthrich - data analysis
NMRPipe, Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. - processing
NMRView, Johnson BA, Blevins RA. - chemical shift assignment
Procheck 3.5.4, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Thornton - data analysis
X-PLOR_NIH 2.17.0, SCHWIETERS, KUSZEWSKI, TJANDRA AND CLORE - refinement, structure calculation
xwinnmr, Bruker Biospin - collection
NMR spectrometers:
- Bruker AvanceIII 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts