BMRB Entry 5529
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR5529
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Title: The structure of G16A MNEI monellin supports a new model of interaction of sweet proteins with the T1R2-T1R3 receptor PubMed: 12706725
Deposition date: 2002-09-13 Original release date: 2003-07-07
Authors: Spadaccini, R.; Trabucco, F.; Saviano, G.; Picone, D.; Crescenzi, O.; Tancredi, T.; Temussi, P.
Citation: Spadaccini, R.; Trabucco, F.; Saviano, G.; Picone, D.; Crescenzi, O.; Tancredi, T.; Temussi, P.. "The Mechanism of Interaction of Sweet Proteins with the T1R2-T1R3 Receptor: Evidence from the Solution Structure of G16A-MNEI" J. Mol. Biol. 328, 683-692 (2003).
Assembly members:
monellin, polymer, 97 residues, Formula weight is not available
Natural source: Common Name: serendipity berry Taxonomy ID: 3457 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Dioscoreophyllum cumminsii
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
monellin: MGEWEIIDIGPFTQNLAKFA
VDEENKIGQYGRLTFNKVIR
PCMKKTIYENEGFREIKGYE
YQLYVYASDKLFRADISEDY
KTRGRKLLRFNGPVPPP
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 104 |
| 1H chemical shifts | 587 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Monellin chains B and A | 1 |
Entities:
Entity 1, Monellin chains B and A 97 residues - Formula weight is not available
| 1 | MET | GLY | GLU | TRP | GLU | ILE | ILE | ASP | ILE | GLY | ||||
| 2 | PRO | PHE | THR | GLN | ASN | LEU | ALA | LYS | PHE | ALA | ||||
| 3 | VAL | ASP | GLU | GLU | ASN | LYS | ILE | GLY | GLN | TYR | ||||
| 4 | GLY | ARG | LEU | THR | PHE | ASN | LYS | VAL | ILE | ARG | ||||
| 5 | PRO | CYS | MET | LYS | LYS | THR | ILE | TYR | GLU | ASN | ||||
| 6 | GLU | GLY | PHE | ARG | GLU | ILE | LYS | GLY | TYR | GLU | ||||
| 7 | TYR | GLN | LEU | TYR | VAL | TYR | ALA | SER | ASP | LYS | ||||
| 8 | LEU | PHE | ARG | ALA | ASP | ILE | SER | GLU | ASP | TYR | ||||
| 9 | LYS | THR | ARG | GLY | ARG | LYS | LEU | LEU | ARG | PHE | ||||
| 10 | ASN | GLY | PRO | VAL | PRO | PRO | PRO |
Samples:
sample_1: monellin 2 mM; pottasium phosphate buffer 18.5 mM; H2O 90%; D2O 10%
sample_2: monellin, [U-15N], 2 mM; pottasium phosphate buffer 18.5 mM; H2O 90%; D2O 10%
sample_cond_1: ionic strength: 18.5 mM; pH: 2.9; pressure: 1 atm; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D NOESY | not available | not available | sample_cond_1 |
| 3D 15N-separated TOCSY | not available | not available | sample_cond_1 |
| 3D 15N-separated NOESY | not available | not available | sample_cond_1 |
| HNHA | not available | not available | sample_cond_1 |
| HNHB | not available | not available | sample_cond_1 |
| HSQC | not available | not available | sample_cond_1 |
Software:
NMRPipe v1.7 - processing
NMRView v4.0.3 - data analysis
DYANA v1.5 - structure solution
NMR spectrometers:
- Bruker DRX 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts