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 25192

Title: Haddock model of Bacillus subtilis L,D-transpeptidase in complex with a peptidoglycan hexamuropeptide   PubMed: 25429710

Authors: Schanda, Paul; Triboulet, Sebastien; Laguri, Cedric; Bougault, Catherine; Ayala, Isabel; Callon, Morgane; Arthur, Michel; Simorre, Jean-Pierre

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).

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

Entity Sequences (FASTA):
entity_1: GRKLLTYQVKQGDTLNSIAA DFRISTAALLQANPSLQAGL TAGQSIVIPGLPDPYTIPYH IAVSIGAKTLTLSLNNRVMK TYPIAVGKILTQTPTGEFYI INRQRNPGGPFGAYWLSLSK QHYGIHGTNNPASIGKAVSK GCIRMHNKDVIELASIVPNG TRVTINRGS
entity_2: XXXXXXXXXXXX
entity_3: AXXX

Data typeCount
13C chemical shifts192
15N chemical shifts192
1H chemical shifts192

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22
3entity_3_13
4entity_3_23
5entity_3_33
6entity_3_43
7entity_3_53

Entities:

Entity 1, entity_1 169 residues - 18132.004 Da.

1   GLYARGLYSLEULEUTHRTYRGLNVALLYS
2   GLNGLYASPTHRLEUASNSERILEALAALA
3   ASPPHEARGILESERTHRALAALALEULEU
4   GLNALAASNPROSERLEUGLNALAGLYLEU
5   THRALAGLYGLNSERILEVALILEPROGLY
6   LEUPROASPPROTYRTHRILEPROTYRHIS
7   ILEALAVALSERILEGLYALALYSTHRLEU
8   THRLEUSERLEUASNASNARGVALMETLYS
9   THRTYRPROILEALAVALGLYLYSILELEU
10   THRGLNTHRPROTHRGLYGLUPHETYRILE
11   ILEASNARGGLNARGASNPROGLYGLYPRO
12   PHEGLYALATYRTRPLEUSERLEUSERLYS
13   GLNHISTYRGLYILEHISGLYTHRASNASN
14   PROALASERILEGLYLYSALAVALSERLYS
15   GLYCYSILEARGMETHISASNLYSASPVAL
16   ILEGLULEUALASERILEVALPROASNGLY
17   THRARGVALTHRILEASNARGGLYSER

Entity 2, entity_2 12 residues - Formula weight is not available

1   NAGAMUNAGAMUNAGAMUNAGAMUNAGAMU
2   NAGAMU

Entity 3, entity_3_1 4 residues - Formula weight is not available

1   ALAFGAAPIDAL

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:

NameSampleSample stateSample conditions
13C-13C DARRsample_1solidsample_conditions_1
hCANHsample_1solidsample_conditions_1
hNHsample_1solidsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1

Software:

Haddock v2.1, Alexandre Bonvin - refinement, structure solution

NMR spectrometers:

  • Agilent vnmrs 600 MHz
  • Bruker Avance III 1000 MHz

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