BMRB Entry 19799
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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/BMR19799
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Title: Solution structure of LysM the peptidoglycan binding domain of autolysin AtlA from Enterococcus faecalis
Deposition date: 2014-02-14 Original release date: 2014-06-12
Authors: Baxter, Nicola; Williamson, Michael
Citation: Mesnage, Stephane; Dellarole, Mariano; Baxter, Nicola; Rouget, Jean-Baptiste; Dimitrov, Jordan; Wang, Ning; Fujimoto, Yukari; Hounslow, Andrea; Lacroix-Desmazes, Sebastien; Fukase, Koichi; Foster, Simon; Williamson, Michael. "Molecular basis for bacterial peptidoglycan recognition by LysM domains" Nature Communications ., .-..
Assembly members:
lysm, polymer, 58 residues, 5440.227 Da.
Natural source: Common Name: firmicutes Taxonomy ID: 1351 Superkingdom: Bacteria Kingdom: not available Genus/species: Enterococcus faecalis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
lysm: MGTNTYYTVKSGDTLNKIAA
QYGVSVANLRSWNGISGDLI
FVGQKLIVKKGSHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 230 |
| 15N chemical shifts | 59 |
| 1H chemical shifts | 363 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | lysm | 1 |
Entities:
Entity 1, lysm 58 residues - 5440.227 Da.
residue S51 is a cloning artifact residues H52-H57 represent a non-native affinity tag
| 1 | MET | GLY | THR | ASN | THR | TYR | TYR | THR | VAL | LYS | ||||
| 2 | SER | GLY | ASP | THR | LEU | ASN | LYS | ILE | ALA | ALA | ||||
| 3 | GLN | TYR | GLY | VAL | SER | VAL | ALA | ASN | LEU | ARG | ||||
| 4 | SER | TRP | ASN | GLY | ILE | SER | GLY | ASP | LEU | ILE | ||||
| 5 | PHE | VAL | GLY | GLN | LYS | LEU | ILE | VAL | LYS | LYS | ||||
| 6 | GLY | SER | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: lysm, [U-100% 13C; U-100% 15N], 0.6 mM; potassium phosphate 40 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 40 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | 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 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N/13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D H(N)CO | sample_1 | isotropic | sample_conditions_1 |
Software:
Felix v2007, Accelrys Software Inc. - chemical shift assignment, peak picking, processing
CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution
TOPSPIN v1.3, Bruker Biospin - collection
NMR spectrometers:
- Bruker DRX 600 MHz
Related Database Links:
| UNP | P37710 |
| PDB | |
| EMBL | CBL32623 |
| GB | EEU16387 EEU84558 EFM65690 EFM72497 EFM76217 |
| REF | WP_002380112 WP_010775020 WP_033625932 WP_048951859 WP_049095956 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts