BMRB Entry 25706
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25706
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Title: 1H, 13C, and 15N Chemical Shift Assignments of PKS domains PubMed: 26982529
Deposition date: 2015-07-14 Original release date: 2016-03-21
Authors: Dorival, Gonathan; Annaval, Thibault; Risser, Fanny; Collin, Sabrina; Roblin, Pierre; Jacob, Christophe; Gruez, Arnaud; Chagot, Benjamin; Weissman, Kira
Citation: Dorival, Gonathan; Annaval, Thibault; Risser, Fanny; Collin, Sabrina; Roblin, Pierre; Jacob, Christophe; Gruez, Arnaud; Chagot, Benjamin; Weissman, Kira. "Characterization of Intersubunit Communication in the Virginiamycin trans-Acyl Transferase Polyketide Synthase" J. Am. Chem. Soc. 138, 4155-4167 (2016).
Assembly members:
entity, polymer, 84 residues, 8455.489 Da.
Natural source: Common Name: high GC Gram+ Taxonomy ID: 1961 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptomyces virginiae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: GPGSYTGAGEPSQADLDALL
SAVRDNRLSIEQAVTLLTPR
RGGGSGGGSMDAKEILTRFK
DGGLDRAAAQALLAGRTPAA
APRP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 321 |
| 15N chemical shifts | 80 |
| 1H chemical shifts | 518 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 84 residues - 8455.489 Da.
Residues 1-5 represent a non-native affinity tag. Residues 6-41 is from VirA protein. Residues 42-49 is an non-native fusion linker. Residues 50-88 is from VirFG protein.
| 1 | GLY | PRO | GLY | SER | TYR | THR | GLY | ALA | GLY | GLU | ||||
| 2 | PRO | SER | GLN | ALA | ASP | LEU | ASP | ALA | LEU | LEU | ||||
| 3 | SER | ALA | VAL | ARG | ASP | ASN | ARG | LEU | SER | ILE | ||||
| 4 | GLU | GLN | ALA | VAL | THR | LEU | LEU | THR | PRO | ARG | ||||
| 5 | ARG | GLY | GLY | GLY | SER | GLY | GLY | GLY | SER | MET | ||||
| 6 | ASP | ALA | LYS | GLU | ILE | LEU | THR | ARG | PHE | LYS | ||||
| 7 | ASP | GLY | GLY | LEU | ASP | ARG | ALA | ALA | ALA | GLN | ||||
| 8 | ALA | LEU | LEU | ALA | GLY | ARG | THR | PRO | ALA | ALA | ||||
| 9 | ALA | PRO | ARG | PRO |
Samples:
sample_1: entity, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 100 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.0, Bruker Biospin - collection
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
SPARKY v3.115, Goddard - chemical shift assignment
AMBER v14, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement
ProcheckNMR, Laskowski and MacArthur - data analysis
TALOS v+, Cornilescu, Delaglio and Bax - structure solution
NMR spectrometers:
- 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