BMRB Entry 25277
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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/BMR25277
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Title: Solution structure of the lantibiotic self-resistance lipoprotein MlbQ from Microbispora ATCC PTA-5024 PubMed: 25923468
Deposition date: 2014-10-09 Original release date: 2015-07-13
Authors: Pozzi, Roberta; Schwartz, Paul; Linke, Dirk; Kulik, Andreas; Nega, Mulugeta; Wohlleben, Wolfgang; Stegmann, Evi; Coles, Murray
Citation: Pozzi, Roberta; Coles, Murray; Schwartz, Paul; Linke, Dirk; Kulik, Andreas; Nega, Mulugeta; Wohlleben, Wolfgang; Stegmann, Evi. "Distinct mechanisms contribute to immunity in the lantibiotic NAI-107 producer strain Microbispora ATCC PTA-5024" Environ. Microbiol. 18, 118-132 (2016).
Assembly members:
MlbQ, polymer, 147 residues, 15456.215 Da.
Natural source: Common Name: high GC Gram+ Taxonomy ID: 316330 Superkingdom: Bacteria Kingdom: not available Genus/species: Microbispora ATCC PTA-5024
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
MlbQ: HHHHHHSSGLVPRGSGMKET
AAAKFERQHMDSPDLGTDDD
DKTGGGRADPAHRSPVPLPS
PTSNKQDISEANLAYLWPLT
VDHGTIECLPSDNAVFVAPD
GTTYALNDRAEKAGHPPITP
IRAKGSGGGYISLGALLSTT
LNLCGKG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 347 |
| 15N chemical shifts | 82 |
| 1H chemical shifts | 573 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | MlbQ | 1 |
Entities:
Entity 1, MlbQ 147 residues - 15456.215 Da.
Residues -5-36 represent a non-native cloning/affinity tag
| 1 | HIS | HIS | HIS | HIS | HIS | HIS | SER | SER | GLY | LEU | ||||
| 2 | VAL | PRO | ARG | GLY | SER | GLY | MET | LYS | GLU | THR | ||||
| 3 | ALA | ALA | ALA | LYS | PHE | GLU | ARG | GLN | HIS | MET | ||||
| 4 | ASP | SER | PRO | ASP | LEU | GLY | THR | ASP | ASP | ASP | ||||
| 5 | ASP | LYS | THR | GLY | GLY | GLY | ARG | ALA | ASP | PRO | ||||
| 6 | ALA | HIS | ARG | SER | PRO | VAL | PRO | LEU | PRO | SER | ||||
| 7 | PRO | THR | SER | ASN | LYS | GLN | ASP | ILE | SER | GLU | ||||
| 8 | ALA | ASN | LEU | ALA | TYR | LEU | TRP | PRO | LEU | THR | ||||
| 9 | VAL | ASP | HIS | GLY | THR | ILE | GLU | CYS | LEU | PRO | ||||
| 10 | SER | ASP | ASN | ALA | VAL | PHE | VAL | ALA | PRO | ASP | ||||
| 11 | GLY | THR | THR | TYR | ALA | LEU | ASN | ASP | ARG | ALA | ||||
| 12 | GLU | LYS | ALA | GLY | HIS | PRO | PRO | ILE | THR | PRO | ||||
| 13 | ILE | ARG | ALA | LYS | GLY | SER | GLY | GLY | GLY | TYR | ||||
| 14 | ILE | SER | LEU | GLY | ALA | LEU | LEU | SER | THR | THR | ||||
| 15 | LEU | ASN | LEU | CYS | GLY | LYS | GLY |
Samples:
15N-labelled: MlbQ, [U-100% 15N], 0.5 mM; TRIS 20 mM; sodium chloride 250 mM; H2O 90%; D2O 10%
13C-15N-labelled: MlbQ, [U-100% 13C; U-100% 15N], 0.5 mM; TRIS 20 mM; sodium chloride 250 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.240 M; pH: 8.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | 13C-15N-labelled | isotropic | sample_conditions_1 |
| 3D C(CO)NH | 13C-15N-labelled | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | 13C-15N-labelled | isotropic | sample_conditions_1 |
| 3D CCH NOESY | 13C-15N-labelled | isotropic | sample_conditions_1 |
| 3D CNH NOESY | 13C-15N-labelled | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | 15N-labelled | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | 13C-15N-labelled | isotropic | sample_conditions_1 |
| 3D HNHA | 15N-labelled | isotropic | sample_conditions_1 |
| 3D HNHB | 15N-labelled | isotropic | sample_conditions_1 |
| 3D 3JHBHA(CO)NH | 13C-15N-labelled | isotropic | sample_conditions_1 |
| 3D NNH NOESY | 15N-labelled | isotropic | sample_conditions_1 |
| 3D HN(CA)NNH | 13C-15N-labelled | isotropic | sample_conditions_1 |
| 3D HNCA | 13C-15N-labelled | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection, processing
SPARKY, Goddard - chemical shift assignment, data analysis
X-PLOR_NIH v2.9.4, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution
NMR-SPIRIT v1.1, In house - refinement
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts