BMRB Entry 18757
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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/BMR18757
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Title: High resolution NMR structure of the theta-defensin HTD-2 (retrocyclin 2) PubMed: 23148585
Deposition date: 2012-10-02 Original release date: 2012-11-27
Authors: Conibear, Anne; Rosengren, K. Johan; Harvey, Peta; Craik, David
Citation: Conibear, Anne; Rosengren, K. Johan; Harvey, Peta; Craik, David. "Structural Characterization of the Cyclic Cystine Ladder Motif of -Defensins." Biochemistry 51, 9718-9726 (2012).
Assembly members:
HTD-2, polymer, 18 residues, 2046.613 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
HTD-2: GICRCICGRRICRCICGR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 49 |
| 15N chemical shifts | 10 |
| 1H chemical shifts | 117 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | theta-defensin HTD-2 (retrocyclin 2) | 1 |
Entities:
Entity 1, theta-defensin HTD-2 (retrocyclin 2) 18 residues - 2046.613 Da.
This is a head-to-tail cyclic peptide with a peptide bond between Arg18 and Gly1.
| 1 | GLY | ILE | CYS | ARG | CYS | ILE | CYS | GLY | ARG | ARG | ||||
| 2 | ILE | CYS | ARG | CYS | ILE | CYS | GLY | ARG |
Samples:
sample_1: HTD-2 1.0 mM; H2O 90%; D2O 10%
sample_2: HTD-2 1.0 mM; D2O 100%
sample_conditions_1: pH: 5.0; 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_2 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H ECOSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment, data analysis, peak picking
TOPSPIN v2.1, Bruker Biospin - collection, processing
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
CNS v2.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 600 MHz
- Bruker Avance 900 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts