BMRB Entry 15442
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15442
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: Richter, Carsten; Nietlispach, Daniel; Broadhurst, Richard; Weissman, Kira. "Multienzyme docking in hybrid megasynthetases" Nat. Chem. Biol. 4, 75-81 (2008).
PubMed: 18066054
Assembly members:
TubCdd, polymer, 78 residues, 8132.495 Da.
Natural source: Common Name: Angiococcus disciformis Taxonomy ID: 38 Superkingdom: Bacteria Kingdom: not available Genus/species: Angiococcus disciformis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-6P-1
Entity Sequences (FASTA):
TubCdd: GPLGSSAGALLAHAASLGVR
LWVEGERLRFQAPPGVMTPE
LQSRLGGARHELIALLRQLQ
PSSQGGSLLAPVARNGRL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 308 |
| 15N chemical shifts | 75 |
| 1H chemical shifts | 515 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | TubCdd A | 1 |
| 2 | TubCdd B | 1 |
Entities:
Entity 1, TubCdd A 78 residues - 8132.495 Da.
The first four residues represent the remnant of the Precission protease cleavage sequence that separated the polypeptide from its N-terminal glutathoine-S-transferase fusion partner.
| 1 | GLY | PRO | LEU | GLY | SER | SER | ALA | GLY | ALA | LEU | ||||
| 2 | LEU | ALA | HIS | ALA | ALA | SER | LEU | GLY | VAL | ARG | ||||
| 3 | LEU | TRP | VAL | GLU | GLY | GLU | ARG | LEU | ARG | PHE | ||||
| 4 | GLN | ALA | PRO | PRO | GLY | VAL | MET | THR | PRO | GLU | ||||
| 5 | LEU | GLN | SER | ARG | LEU | GLY | GLY | ALA | ARG | HIS | ||||
| 6 | GLU | LEU | ILE | ALA | LEU | LEU | ARG | GLN | LEU | GLN | ||||
| 7 | PRO | SER | SER | GLN | GLY | GLY | SER | LEU | LEU | ALA | ||||
| 8 | PRO | VAL | ALA | ARG | ASN | GLY | ARG | LEU |
Samples:
sample_1: TubCdd, [U-100% 13C; U-100% 15N], 1 mM; TSP 20 uM; sodium azide 0.1%; sodium phosphate 50 mM; sodium chloride 100 mM; H2O 90%; D2O 10%
sample_2: TubCdd, [U-100% 13C; U-100% 15N], 0.5 mM; TubCdd 0.5 mM; TSP 20 uM; sodium azide 0.1%; sodium phosphate 50 mM; sodium chloride 100 mM; TubCdd 0.5 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.15 M; pH: 6; pressure: 1 atm; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C-separated 12C-selected NOESY | sample_2 | isotropic | sample_conditions_1 |
| 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 HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
ARIA v1.2, Linge, O'Donoghue and Nilges - structure solution
AZARA, Boucher - processing
ANALYSIS v1.0.15, Vranken, Boucher, Stevens, Fogh, Pajon, Llinas, Ulrich, Markley, Ionides and Laue - chemical shift assignment, data analysis, peak picking
NMR spectrometers:
- Bruker DRX 500 MHz
- Bruker DRX 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks