BMRB Entry 27246
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27246
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Title: Backbone assignments of engineered hairpin loop3 mutant of single chain monellin. PubMed: 30692525
Deposition date: 2017-09-08 Original release date: 2019-02-08
Authors: Surana, Parag; Nandwani, Neha; Udgaonkar, Jayant; Gosavi, Shachi; Das, Ranabir
Citation: Nandwani, Neha; Surana, Parag; Negi, Hitendra; Mascarenhas, Nahren; Udgaonkar, Jayant; Das, Ranabir; Gosavi, Shachi. "A five-residue motif for the design of domain swapping in proteins." Nat. Commun. 10, 452-452 (2019).
Assembly members:
single_chain_monellin, polymer, 100 residues, 11479 Da.
Natural source: Common Name: serendipity berry Taxonomy ID: 3457 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Dioscoreophyllum cumminsi
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET22b+
Entity Sequences (FASTA):
single_chain_monellin: MGEWEIIDIGPFTQNLGKFA
VDEENKIGQYGRLTFNKVIR
PCMKKTIYENEGFREIKGYE
YQLYVYASDKLFRADISEQV
VAGGRKLLRFNGPVPPPSTP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 263 |
| 15N chemical shifts | 89 |
| 1H chemical shifts | 89 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | single chain monellin | 1 |
Entities:
Entity 1, single chain monellin 100 residues - 11479 Da.
| 1 | MET | GLY | GLU | TRP | GLU | ILE | ILE | ASP | ILE | GLY | |
| 2 | PRO | PHE | THR | GLN | ASN | LEU | GLY | 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 | GLN | VAL | |
| 9 | VAL | ALA | GLY | GLY | ARG | LYS | LEU | LEU | ARG | PHE | |
| 10 | ASN | GLY | PRO | VAL | PRO | PRO | PRO | SER | THR | PRO |
Samples:
sample_1: single chain monellin, [U-13C; U-15N], 400 uM
sample_conditions_1: ionic strength: 10 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment, peak picking
TOPSPIN, Bruker Biospin - collection
NMR spectrometers:
- Bruker Avance 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts