BMRB Entry 51885
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51885
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Hsu, Min-Feng; Sriramouju, Manoj; Lai, Chih-Hsuan; Chen, Yun-Ru; Huang, Jing-Siou; Ko, Tzu-Ping; Huang, Kai-Fa; Hsu, Shang-Te Danny. "Structure, dynamics and stability of the smallest and most complex 71 protein knot" J. Biol. Chem. 300, 105553-105553 (2023).
PubMed: 38072060
Assembly members:
entity_1, polymer, 89 residues, Formula weight is not available
Natural source: Common Name: Ureaplasma parvum serovar 3 Taxonomy ID: 38504 Superkingdom: Bacteria Kingdom: not available Genus/species: Ureaplasma parvum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a
Entity Sequences (FASTA):
entity_1: MYNYKEVKHMGYGKGYLAMF
KNKKVRFKVVNSFPDLKVQF
VTSFPDYKVKISNSSSFCEE
TIKIQVVTSFPDVKLQKVTS
FGDFEAYID
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 244 |
| 15N chemical shifts | 81 |
| 1H chemical shifts | 81 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Q9PR55 | 1 |
Entities:
Entity 1, Q9PR55 89 residues - Formula weight is not available
| 1 | MET | TYR | ASN | TYR | LYS | GLU | VAL | LYS | HIS | MET | ||||
| 2 | GLY | TYR | GLY | LYS | GLY | TYR | LEU | ALA | MET | PHE | ||||
| 3 | LYS | ASN | LYS | LYS | VAL | ARG | PHE | LYS | VAL | VAL | ||||
| 4 | ASN | SER | PHE | PRO | ASP | LEU | LYS | VAL | GLN | PHE | ||||
| 5 | VAL | THR | SER | PHE | PRO | ASP | TYR | LYS | VAL | LYS | ||||
| 6 | ILE | SER | ASN | SER | SER | SER | PHE | CYS | GLU | GLU | ||||
| 7 | THR | ILE | LYS | ILE | GLN | VAL | VAL | THR | SER | PHE | ||||
| 8 | PRO | ASP | VAL | LYS | LEU | GLN | LYS | VAL | THR | SER | ||||
| 9 | PHE | GLY | ASP | PHE | GLU | ALA | TYR | ILE | ASP |
Samples:
sample_1: Q9PR55, [U-13C; U-15N], 1.3 mM; phosphate buffer 50 mM
sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe - processing
NMRFAM-SPARKY - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE III 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks