BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 18911

Title: NMR STRUCTURE OF THE CATALYTIC DOMAIN FROM E. FAECIUM L,D- TRANSPEPTIDASE ACYLATED BY ERTAPENEM   PubMed: 23574509

Authors: Lecoq, L.; Triboulet, S.; Dubee, V.; Bougault, C.; Hugonnet, J.; Arthur, M.; Simorre, Jean-Pierre; Simorre, M.

Citation: Lecoq, Lauriane; Dubee, Vincent; Triboulet, Sebastien; Bougault, Catherine; Hugonnet, Jean-Emmanuel; Arthur, Michel; Simorre, Jean-Pierre. "Structure of Enterococcus faeciuml,d-transpeptidase acylated by ertapenem provides insight into the inactivation mechanism."  ACS Chem. Biol. 8, 1140-1146 (2013).

Assembly members:
ERFK-YBIS-YCFS-YNHG, polymer, 129 residues, 14549.0884 Da.
entity_1RG, non-polymer, 477.531 Da.

Natural source:   Common Name: Enterococcus faecium   Taxonomy ID: 1352   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Enterococcus faecium

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
ERFK-YBIS-YCFS-YNHG: GHMEDTYIEVDLENQHMWYY KDGKVALETDIVSGKPTTPT PAGVFYVWNKEEDATLKGTN DDGTPYESPVNYWMPIDWTG VGIHDSDWQPEYGGDLWKTR GSHGCINTPPSVMKELFGMV EKGTPVLVF

Data sets:
Data typeCount
13C chemical shifts555
15N chemical shifts130
1H chemical shifts871

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ERFK-YBIS-YCFS-YNHG1
2ligand 1RG2

Entities:

Entity 1, ERFK-YBIS-YCFS-YNHG 129 residues - 14549.0884 Da.

1   GLYHISMETGLUASPTHRTYRILEGLUVAL
2   ASPLEUGLUASNGLNHISMETTRPTYRTYR
3   LYSASPGLYLYSVALALALEUGLUTHRASP
4   ILEVALSERGLYLYSPROTHRTHRPROTHR
5   PROALAGLYVALPHETYRVALTRPASNLYS
6   GLUGLUASPALATHRLEULYSGLYTHRASN
7   ASPASPGLYTHRPROTYRGLUSERPROVAL
8   ASNTYRTRPMETPROILEASPTRPTHRGLY
9   VALGLYILEHISASPSERASPTRPGLNPRO
10   GLUTYRGLYGLYASPLEUTRPLYSTHRARG
11   GLYSERHISGLYCYSILEASNTHRPROPRO
12   SERVALMETLYSGLULEUPHEGLYMETVAL
13   GLULYSGLYTHRPROVALLEUVALPHE

Entity 2, ligand 1RG - C22 H27 N3 O7 S - 477.531 Da.

1   1RG

Samples:

sample_1: ERFK-YBIS-YCFS-YNHG, [U-13C; U-15N], 0.9 mM; NaCl 300 mM

sample_2: ERFK-YBIS-YCFS-YNHG, [U-13C; U-15N], 0.9 mM; NaCl 300 mM

sample_conditions_1: ionic strength: 300.000 mM; pH: 6.400; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

NameSampleSample stateSample conditions
1H-15N-HSQCsample_1solutionsample_conditions_1
1H-13C-HSQC centered on aliphaticssample_1solutionsample_conditions_1
1H-15N-HMQC detecting 2Jsample_1solutionsample_conditions_1
3J couplings in histidines imidazole ringsample_1solutionsample_conditions_1
HSQC detecting 1J coupling in histidines imidazole ringsample_1solutionsample_conditions_1
HNCACBsample_1solutionsample_conditions_1
HNCOsample_1solutionsample_conditions_1
3D-15N-NOESY-HSQCsample_1solutionsample_conditions_1
3D-13C-NOESY-HSQC centered on aliphaticssample_1solutionsample_conditions_1
1H-13C-HSQC centered on aromaticssample_2solutionsample_conditions_1
3D-13C-NOESY-HSQC centered on aromaticssample_2solutionsample_conditions_1
13C-15N-filtered NOESYsample_2solutionsample_conditions_1

Software:

CNS1.2 vany, BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,READ,RICE,SIMONSON,WARREN - chemical shift assignment

ANALYSIS vany, CCPN - chemical shift assignment

TALOS vany, Cornilescu, Delaglio and Bax - data analysis

UNIO v10, UNIO - data analysis

NMR spectrometers:

  • Varian Direct Drive 600 MHz
  • Varian Direct Drive 800 MHz
  • Bruker Avance 950 MHz

Related Database Links:

UNP Q3Y185_ENTFC
BMRB 18900
PDB
GB AFC64689 AFK60179 AGE31159 AGS76645 AII39985
REF WP_002287397 WP_002290929 WP_002296050 WP_002298179 WP_002307701