BMRB Entry 16685

Title:
NMR resonance assignment of the major extracytoplasmic domain of MreC from Bacillus subtilis
Deposition date:
2010-01-20
Original release date:
2010-07-27
Authors:
Kyburz, Annika; Raulinaitis, Vytautas; Koskela, Outi; Kontinen, Vesa; Permi, Perttu; Kilpelainen, Ilkka; Seppala-Lehto, Raili
Citation:

Citation: Kyburz, Annika; Raulinaitis, Vytautas; Koskela, Outi; Kontinen, Vesa; Permi, Perttu; Kilpelainen, Ilkka; Seppala, Raili. "1H, 13C and 15N resonance assignments of the major extracytoplasmic domain of the cell shape-determining protein MreC from Bacillus subtilis."  Biomol. NMR Assignments 4, 235-238 (2010).
PubMed: 20623345

Assembly members:

Assembly members:
MreC, polymer, 178 residues, 19225.8340 Da.

Natural source:

Natural source:   Common Name: Bacillus subtilis   Taxonomy ID: 1423   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Bacillus subtilis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-2T

Data sets:
Data typeCount
13C chemical shifts566
15N chemical shifts170
1H chemical shifts1165

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MreC1

Entities:

Entity 1, MreC 178 residues - 19225.8340 Da.

1   GLYSERGLYHISVALLYSSERILELYSASP
2   TYRLYSPROILELEUALATHRVALILEALA
3   ARGSERPROASPASNTRPALALYSGLNVAL
4   THRILEASNLYSGLYTHRGLNGLNASNVAL
5   ALALYSASPMETALAVALTHRASNGLULYS
6   GLYALALEUILEGLYLYSILELYSSERSER
7   GLYLEUASNASNPHETHRSERALAVALGLN
8   LEULEUSERASPTHRASPARGASNASNARG
9   VALALATHRLYSILESERGLYLYSLYSGLY
10   SERLYSGLYTYRGLYLEUILEGLUGLYTYR
11   ASPLYSGLULYSLYSARGLEULYSMETTHR
12   ILEILEGLUARGLYSASPLYSGLNASPVAL
13   LYSLYSGLYASPLEUILEGLUTHRSERGLY
14   THRGLYGLYVALPHEPROGLUGLYLEUTHR
15   ILEGLYGLUVALTHRASPILEGLUSERASP
16   SERTYRGLYLEUTHRLYSVALALATYRVAL
17   LYSPROALAALAASPLEUTHRASPLEUASN
18   ASNVALILEVALVALASNARGASP

Samples:

sample_1: MreC 104-279, [U-100% 13C; U-100% 15N], 0.54 mM; potassium phosphate 20 mM; sodium azide 2 mM; EDTA 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 20 mM; pH: 6.5; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D CC(CO)NHsample_1isotropicsample_conditions_1
3D H(CC)(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-13C-CT-HSQCsample_1isotropicsample_conditions_1
3D HCCH-COSY_aromaticssample_1isotropicsample_conditions_1

Software:

VNMRJ, Varian - collection, processing

SPARKY v3.113, Goddard - chemical shift assignments, data analysis, peak picking

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz

Related Database Links:

DBJ BAI86290 BAM53237 BAM58879 GAK80355
EMBL CAB14762 CCU59293 CEI58031 CEJ78453 CJR47029
GB AAA22398 AAA22606 ADM38751 ADV93593 AEP87648
PRF 2207195A
REF NP_390680 WP_003222609 WP_003237571 WP_009967915 WP_010335163
SP P84480 Q01466
AlphaFold Q01466 P84480

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks