BMRB Entry 34481
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34481
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: Solution NMR structure of the S0_2.126 designed protein PubMed: 32409444
Deposition date: 2020-01-23 Original release date: 2020-04-13
Authors: Abriata, L.
Citation: Sesterhenn, Fabian; Yang, Che; Bonet, Jaume; Cramer, Johannes; Wen, Xiaolin; Wang, Yimeng; Chiang, Chi-I; Abriata, Luciano; Kucharska, Iga; Castoro, Giacomo; Vollers, Sabrina; Galloux, Marie; Dheilly, Elie; Rosset, Stephane; Corthesy, Patricia; Georgeon, Sandrine; Villard, Melanie; Richard, Charles-Adrien; Descamps, Delphyne; Delgado, Teresa; Oricchio, Elisa; Rameix-Welti, Marie-Anne; Mas, Vicente; Ervin, Sean; Eleouet, Jean-Francois; Riffault, Sabine; Bates, John; Julien, Jean-Philippe; Li, Yuxing; Jardetzky, Theodore; Krey, Thomas; Correia, Bruno. "De novo protein design enables precise induction of RSV neutralizing antibodies" Science 368, .-. (2020).
Assembly members:
entity_1, polymer, 71 residues, 8209.471 Da.
Natural source: Common Name: not available Taxonomy ID: 32630 Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: ASPCDKQKNYIDKQLLPIVN
KAGCSRPEEVEERIRRALKK
MGDTSCFDEILKGLKEIKCG
GSWLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 207 |
| 15N chemical shifts | 61 |
| 1H chemical shifts | 313 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 71 residues - 8209.471 Da.
| 1 | ALA | SER | PRO | CYS | ASP | LYS | GLN | LYS | ASN | TYR | ||||
| 2 | ILE | ASP | LYS | GLN | LEU | LEU | PRO | ILE | VAL | ASN | ||||
| 3 | LYS | ALA | GLY | CYS | SER | ARG | PRO | GLU | GLU | VAL | ||||
| 4 | GLU | GLU | ARG | ILE | ARG | ARG | ALA | LEU | LYS | LYS | ||||
| 5 | MET | GLY | ASP | THR | SER | CYS | PHE | ASP | GLU | ILE | ||||
| 6 | LEU | LYS | GLY | LEU | LYS | GLU | ILE | LYS | CYS | GLY | ||||
| 7 | GLY | SER | TRP | LEU | GLU | HIS | HIS | HIS | HIS | HIS | ||||
| 8 | HIS |
Samples:
sample_1: protein 3hb_126543, natural anundance, 500 uM; sodium phosphate, natural anundance, 20 mM
sample_2: protein 3hb_126543, [U-99% 15N], 500 uM; sodium phosphate, natural anundance, 20 mM
sample_3: protein 3hb_126543, [U-99% 13C; U-99% 15N], 400 uM; sodium phosphate, natural anundance, 20 mM
sample_4: protein 3hb_126543, natural anundance, 500 uM; sodium phosphate, natural anundance, 20 mM
sample_conditions_1: ionic strength: 20 mM; pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_3 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_3 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_3 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_3 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_4 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_4 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
Software:
CARA, Keller and Wuthrich - chemical shift assignment
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
UNIO, T. Herrmann - structure calculation
TopSpin, Bruker Biospin - collection
NMR spectrometers:
- Bruker AVANCE II 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts