BMRB Entry 50594
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50594
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: NMR resonance assignments for a docking domain pair with an attached thiolation domain from the PAX peptide-producing NRPS from Xenorhabdus cabanillasii PubMed: 33675014
Deposition date: 2020-11-25 Original release date: 2021-06-02
Authors: Watzel, Jonas; Sarawi, Sepas; Duchardt-Ferner, Elke; Bode, Helge; Woehnert, Jens
Citation: Watzel, Jonas; Sarawi, Sepas; Duchardt-Ferner, Elke; Bode, Helge; Woehnert, Jens. "NMR resonance assignments for a docking domain pair with an attached thiolation domain from the PAX peptide-producing NRPS from Xenorhabdus cabanillasii." Biomol. NMR Assign. 15, 229-234 (2021).
Assembly members:
entity_1, polymer, 104 residues, Formula weight is not available
Natural source: Common Name: Xenorhabdus cabanillasii Taxonomy ID: 351673 Superkingdom: Bacteria Kingdom: not available Genus/species: Xenorhabdus cabanillasii
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-11a
Entity Sequences (FASTA):
entity_1: DHSSVITQEYAAPQGEIEEQ
LADIWQTILKIDRIGRYDNF
FELGGHSLLVLQLQSRINEI
FDVDISIQQLFAHPSICQLE
ECIINAQLLQFDADSLQDIY
KSME
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 300 |
| 15N chemical shifts | 99 |
| 1H chemical shifts | 376 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PaxA T1-Cdd | 1 |
Entities:
Entity 1, PaxA T1-Cdd 104 residues - Formula weight is not available
| 1 | ASP | HIS | SER | SER | VAL | ILE | THR | GLN | GLU | TYR | ||||
| 2 | ALA | ALA | PRO | GLN | GLY | GLU | ILE | GLU | GLU | GLN | ||||
| 3 | LEU | ALA | ASP | ILE | TRP | GLN | THR | ILE | LEU | LYS | ||||
| 4 | ILE | ASP | ARG | ILE | GLY | ARG | TYR | ASP | ASN | PHE | ||||
| 5 | PHE | GLU | LEU | GLY | GLY | HIS | SER | LEU | LEU | VAL | ||||
| 6 | LEU | GLN | LEU | GLN | SER | ARG | ILE | ASN | GLU | ILE | ||||
| 7 | PHE | ASP | VAL | ASP | ILE | SER | ILE | GLN | GLN | LEU | ||||
| 8 | PHE | ALA | HIS | PRO | SER | ILE | CYS | GLN | LEU | GLU | ||||
| 9 | GLU | CYS | ILE | ILE | ASN | ALA | GLN | LEU | LEU | GLN | ||||
| 10 | PHE | ASP | ALA | ASP | SER | LEU | GLN | ASP | ILE | TYR | ||||
| 11 | LYS | SER | MET | GLU |
Samples:
sample_1: PaxA T1-Cdd, [U-13C; U-15N], 300 uM; sodium phosphate 50 mM; sodium chloride 100 mM; D2O, [U-2H], 10%; DSS 100 uM; beta-mercaptoethanol 2 mM
sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA v1.8.4 - chemical shift assignment, peak picking
TOPSPIN v3.6.2 - data analysis
NMR spectrometers:
- Bruker Avance II 600 MHz
- Bruker AVANCE III HD 800 MHz
Related Database Links:
| NCBI | PHM77429.1 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts