BMRB Entry 18947
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18947
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NMR-STAR v3 text file.
XML gzip file.
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Citation: Zheng, Jianting; Fage, Christopher; Demeler, Borries; Hoffman, David; Keatinge-Clay, Adrian. "The missing linker: a dimerization motif located within polyketide synthase modules." ACS Chem. Biol. 8, 1263-1270 (2013).
PubMed: 23489133
Assembly members:
SpnDE1, polymer, 72 residues, 7800 Da.
Natural source: Common Name: High GC Gram+ Taxonomy ID: 60894 Superkingdom: Bacteria Kingdom: not available Genus/species: Saccharopolyspora spinosa
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28b
Entity Sequences (FASTA):
SpnDE1: GSHMALRESSAGDMGRRVEA
KFWGAVEHEDVESLARVLGI
VDDGAAVDSLRSALPVLAGW
QRTRTTESIMDQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 238 |
| 15N chemical shifts | 64 |
| 1H chemical shifts | 406 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SpnDE1 | 1 |
Entities:
Entity 1, SpnDE1 72 residues - 7800 Da.
Residues 1-3 are remnants of a thrombin-cleaved hexahistidine tag
| 1 | GLY | SER | HIS | MET | ALA | LEU | ARG | GLU | SER | SER | ||||
| 2 | ALA | GLY | ASP | MET | GLY | ARG | ARG | VAL | GLU | ALA | ||||
| 3 | LYS | PHE | TRP | GLY | ALA | VAL | GLU | HIS | GLU | ASP | ||||
| 4 | VAL | GLU | SER | LEU | ALA | ARG | VAL | LEU | GLY | ILE | ||||
| 5 | VAL | ASP | ASP | GLY | ALA | ALA | VAL | ASP | SER | LEU | ||||
| 6 | ARG | SER | ALA | LEU | PRO | VAL | LEU | ALA | GLY | TRP | ||||
| 7 | GLN | ARG | THR | ARG | THR | THR | GLU | SER | ILE | MET | ||||
| 8 | ASP | GLN |
Samples:
sample_1: SpnDE1, [U-15N], 7 mM; SpnDE1, [U-13C], 7 mM; sodium phosphate 100 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.100 M; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Varian INOVA 500 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks