BMRB Entry 25192
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25192
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: Schanda, Paul; Triboulet, Sebastien; Laguri, Cedric; Bougault, Catherine; Ayala, Isabel; Callon, Morgane; Arthur, Michel; Simorre, Jean-Pierre. "Atomic model of a cell-wall cross-linking enzyme in complex with an intact bacterial peptidoglycan" J. Am. Chem. Soc. 136, 17852-17860 (2014).
PubMed: 25429710
Assembly members:
entity_1, polymer, 169 residues, 18132.004 Da.
entity_2, polymer, 12 residues, Formula weight is not available
entity_3, polymer, 4 residues, Formula weight is not available
Natural source: Common Name: Hay bacillus Taxonomy ID: 1423 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus subtilis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET2818
Entity Sequences (FASTA):
entity_1: GRKLLTYQVKQGDTLNSIAA
DFRISTAALLQANPSLQAGL
TAGQSIVIPGLPDPYTIPYH
IAVSIGAKTLTLSLNNRVMK
TYPIAVGKILTQTPTGEFYI
INRQRNPGGPFGAYWLSLSK
QHYGIHGTNNPASIGKAVSK
GCIRMHNKDVIELASIVPNG
TRVTINRGS
entity_2: XXXXXXXXXXXX
entity_3: AXXX
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 192 |
| 15N chemical shifts | 192 |
| 1H chemical shifts | 192 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
| 3 | entity_3_1 | 3 |
| 4 | entity_3_2 | 3 |
| 5 | entity_3_3 | 3 |
| 6 | entity_3_4 | 3 |
| 7 | entity_3_5 | 3 |
Entities:
Entity 1, entity_1 169 residues - 18132.004 Da.
| 1 | GLY | ARG | LYS | LEU | LEU | THR | TYR | GLN | VAL | LYS | ||||
| 2 | GLN | GLY | ASP | THR | LEU | ASN | SER | ILE | ALA | ALA | ||||
| 3 | ASP | PHE | ARG | ILE | SER | THR | ALA | ALA | LEU | LEU | ||||
| 4 | GLN | ALA | ASN | PRO | SER | LEU | GLN | ALA | GLY | LEU | ||||
| 5 | THR | ALA | GLY | GLN | SER | ILE | VAL | ILE | PRO | GLY | ||||
| 6 | LEU | PRO | ASP | PRO | TYR | THR | ILE | PRO | TYR | HIS | ||||
| 7 | ILE | ALA | VAL | SER | ILE | GLY | ALA | LYS | THR | LEU | ||||
| 8 | THR | LEU | SER | LEU | ASN | ASN | ARG | VAL | MET | LYS | ||||
| 9 | THR | TYR | PRO | ILE | ALA | VAL | GLY | LYS | ILE | LEU | ||||
| 10 | THR | GLN | THR | PRO | THR | GLY | GLU | PHE | TYR | ILE | ||||
| 11 | ILE | ASN | ARG | GLN | ARG | ASN | PRO | GLY | GLY | PRO | ||||
| 12 | PHE | GLY | ALA | TYR | TRP | LEU | SER | LEU | SER | LYS | ||||
| 13 | GLN | HIS | TYR | GLY | ILE | HIS | GLY | THR | ASN | ASN | ||||
| 14 | PRO | ALA | SER | ILE | GLY | LYS | ALA | VAL | SER | LYS | ||||
| 15 | GLY | CYS | ILE | ARG | MET | HIS | ASN | LYS | ASP | VAL | ||||
| 16 | ILE | GLU | LEU | ALA | SER | ILE | VAL | PRO | ASN | GLY | ||||
| 17 | THR | ARG | VAL | THR | ILE | ASN | ARG | GLY | SER |
Entity 2, entity_2 12 residues - Formula weight is not available
| 1 | NAG | AMU | NAG | AMU | NAG | AMU | NAG | AMU | NAG | AMU | ||||
| 2 | NAG | AMU |
Entity 3, entity_3_1 4 residues - Formula weight is not available
| 1 | ALA | FGA | API | DAL |
Samples:
sample_1: entity_1, [U-13C; U-15N; U-2H], 2.5 mg/ml; entity_2 3 mg/mL; HEPES 50 mM
sample_2: entity_1, [U-99% 13C; U-99% 15N], 376 uM; HEPES 50 mM
sample_conditions_1: ionic strength: 0.05 M; pH: 7.2; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 13C-13C DARR | sample_1 | solid | sample_conditions_1 |
| hCANH | sample_1 | solid | sample_conditions_1 |
| hNH | sample_1 | solid | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
Software:
Haddock v2.1, Alexandre Bonvin - refinement, structure solution
NMR spectrometers:
- Agilent vnmrs 600 MHz
- Bruker Avance III 1000 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks