BMRB Entry 34469
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34469
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Watzel, Jonas; Hacker, Carolin; Duchardt-Ferner, Elke; Bode, Helge; Woehnert, Jens. "A New Docking Domain Type in the Peptide-Antimicrobial-Xenorhabdus Peptide Producing Nonribosomal Peptide Synthetase from Xenorhabdus bovienii" ACS Chem. Biol. 15, 982-989 (2020).
PubMed: 32167274
Assembly members:
entity_1, polymer, 93 residues, 9841.622 Da.
Natural source: Common Name: Xenorhabdus bovienii SS-2004 Taxonomy ID: 406818 Superkingdom: Bacteria Kingdom: not available Genus/species: Xenorhabdus bovienii
Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)
Entity Sequences (FASTA):
entity_1: MNINEQTLDKLRQAVLQKKI
KERIQNSLSTEKYGSGSGSG
SGSGSGSGSGSGSGSGSGYQ
IETFFAQDIESVQKELENLS
EEELLAMLNGDQQ
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 292 |
| 15N chemical shifts | 78 |
| 1H chemical shifts | 502 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 93 residues - 9841.622 Da.
| 1 | MET | ASN | ILE | ASN | GLU | GLN | THR | LEU | ASP | LYS | ||||
| 2 | LEU | ARG | GLN | ALA | VAL | LEU | GLN | LYS | LYS | ILE | ||||
| 3 | LYS | GLU | ARG | ILE | GLN | ASN | SER | LEU | SER | THR | ||||
| 4 | GLU | LYS | TYR | GLY | SER | GLY | SER | GLY | SER | GLY | ||||
| 5 | SER | GLY | SER | GLY | SER | GLY | SER | GLY | SER | GLY | ||||
| 6 | SER | GLY | SER | GLY | SER | GLY | SER | GLY | TYR | GLN | ||||
| 7 | ILE | GLU | THR | PHE | PHE | ALA | GLN | ASP | ILE | GLU | ||||
| 8 | SER | VAL | GLN | LYS | GLU | LEU | GLU | ASN | LEU | SER | ||||
| 9 | GLU | GLU | GLU | LEU | LEU | ALA | MET | LEU | ASN | GLY | ||||
| 10 | ASP | GLN | GLN |
Samples:
sample_1: PaxC NDD 12.5xGS Y-PaxB CDD, [U-99% 13C; U-99% 15N], 370 uM
sample_2: PaxC NDD 12.5xGS Y-PaxB CDD, [U-99% 13C; U-99% 15N], 1620 uM
sample_3: PaxC NDD 12.5xGS Y-PaxB CDD, [U-99% 15N], 730 uM
sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC, 3D b-tr-HNCACB, 3D b-tr-HNCO, 3D HC(C)H-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC, 3D (H)CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC, 3D HBHA(CO)NH, 3D HN(CA)CO, 3D H(CCO)NH | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC, 3D 1H-15N NOESY | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic, 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic, 3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_1 |
Software:
CYANA v3.97, Guentert, Peter - refinement
CARA v1.8.4.2, Keller, Rochus and Wuethrich, Kurt - chemical shift assignment
TopSpin v3.5, Bruker Biospin - collection
CcpNmr Analysis v2.4.2, CCPN - data analysis
UNIO v10, Herrmann, Thorsten, Guentert, Peter and Wuethrich, Kurt - peak picking
CYANA, Guentert, Peter, Mumenthaler, Christian and Wuethrich, Kurt - structure calculation
NMR spectrometers:
- Bruker AVANCE 599 MHz
- Bruker AVANCE 700 MHz
- Bruker AVANCE 600 MHz
- Bruker AVANCE 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks