BMRB Entry 34194
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34194
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Title: Solution Structure of Rhabdopeptide NRPS Docking Domain Kj12B-NDD PubMed: 30341296
Deposition date: 2017-11-06 Original release date: 2018-10-24
Authors: Hacker, C.; Cai, X.; Kegler, C.; Zhao, L.; Weickhmann, A.; Bode, H.; Woehnert, J.
Citation: Hacker, C.; Cai, X.; Kegler, C.; Zhao, L.; Weickhmann, A.; Bode, H.; Woehnert, J.. "Structure-based redesign of docking domain interactions modulates the product spectrum of a rhabdopeptide-synthesizing NRPS" Nat. Commun. 9, 4366-4366 (2018).
Assembly members:
entity_1, polymer, 62 residues, 7245.112 Da.
Natural source: Common Name: Xenorhabdus stockiae Taxonomy ID: 351614 Superkingdom: Bacteria Kingdom: not available Genus/species: Xenorhabdus stockiae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)
Entity Sequences (FASTA):
entity_1: MKNAAKIVNEALNQGITLFV
SDNKLKYKTNRDSIPSELLE
EWKQHKQELIDFLTQLESEE
ES
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 288 |
| 15N chemical shifts | 70 |
| 1H chemical shifts | 465 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 62 residues - 7245.112 Da.
| 1 | MET | LYS | ASN | ALA | ALA | LYS | ILE | VAL | ASN | GLU | ||||
| 2 | ALA | LEU | ASN | GLN | GLY | ILE | THR | LEU | PHE | VAL | ||||
| 3 | SER | ASP | ASN | LYS | LEU | LYS | TYR | LYS | THR | ASN | ||||
| 4 | ARG | ASP | SER | ILE | PRO | SER | GLU | LEU | LEU | GLU | ||||
| 5 | GLU | TRP | LYS | GLN | HIS | LYS | GLN | GLU | LEU | ILE | ||||
| 6 | ASP | PHE | LEU | THR | GLN | LEU | GLU | SER | GLU | GLU | ||||
| 7 | GLU | SER |
Samples:
sample_1: Kj12BCDD, [U-13C; U-15N], 1 mM; sodium phosphate buffer 50 mM; sodium chloride 100 mM
sample_2: Kj12BCDD, [U-15N], 200 uM; sodium phosphate buffer 50 mM; sodium chloride 100 mM
sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 bar; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY-HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
OpalP v3.97, Guenthert - refinement
CARA v3.97, Keller and Wuthrich - chemical shift assignment
Analysis, CCPN - data analysis
TOPSPIN, Bruker Biospin - processing
CANDID, Herrmann, Guntert and Wuthrich - peak picking
CYANA v3.97, Guentert Peter - structure calculation
NMR spectrometers:
- Bruker Avance 599 MHz
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts