BMRB Entry 19799

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:

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:

Assembly members:
lysm, polymer, 58 residues, 5440.227 Da.

Natural source:

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   Vector: pML520

Experimental source:

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   Vector: pML520

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts230
15N chemical shifts59
1H chemical shifts363

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1lysm1

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   METGLYTHRASNTHRTYRTYRTHRVALLYS
2   SERGLYASPTHRLEUASNLYSILEALAALA
3   GLNTYRGLYVALSERVALALAASNLEUARG
4   SERTRPASNGLYILESERGLYASPLEUILE
5   PHEVALGLYGLNLYSLEUILEVALLYSLYS
6   GLYSERHISHISHISHISHISHIS

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N/13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D H(N)COsample_1isotropicsample_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 HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks