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 19419

Title: 1H, 13C, and 15N Chemical Shift Assignments of C-ala domain from Bizionia argentinensis   PubMed: 24258519

Deposition date: 2013-08-09 Original release date: 2014-02-13

Authors: Smal, Clara; Zanzoni, Serena; D'Onofrio, Mariapina; Assfalg, Michael; Cicero, Daniel; Molinari, Henriette

Citation: Smal, Clara; Zanzoni, Serena; D'Onofrio, Mariapina; Molinari, Henriette; Cicero, Daniel; Assfalg, Michael. "(1)H, (15)N and (13)C chemical shift assignments of the C-Ala domain of the alanyl-tRNA synthetase of the psychrophilic bacterium Bizionia argentinensis sp. nov."  Biomol NMR Assign 8, 415-418 (2014).

Assembly members:
C-ala_domain, polymer, 122 residues, Formula weight is not available

Natural source:   Common Name: Bizionia argentinensis   Taxonomy ID: 456455   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bizionia argentinensis

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

Entity Sequences (FASTA):
C-ala_domain: MKAKNLKGELKNEITEINGI HFLAKKVDLDAGGIKDLCFE LGSQYDNLFLLFGAENDGKA LLSCYVSKELVERKGLNAGQ IVRELGKFIQGGGGGQPFFA TAGGKNPAGIAEALEAAKKY LV

Data sets:
Data typeCount
13C chemical shifts530
15N chemical shifts130
1H chemical shifts860

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C-Ala domain1

Entities:

Entity 1, C-Ala domain 122 residues - Formula weight is not available

1   METLYSALALYSASNLEULYSGLYGLULEU
2   LYSASNGLUILETHRGLUILEASNGLYILE
3   HISPHELEUALALYSLYSVALASPLEUASP
4   ALAGLYGLYILELYSASPLEUCYSPHEGLU
5   LEUGLYSERGLNTYRASPASNLEUPHELEU
6   LEUPHEGLYALAGLUASNASPGLYLYSALA
7   LEULEUSERCYSTYRVALSERLYSGLULEU
8   VALGLUARGLYSGLYLEUASNALAGLYGLN
9   ILEVALARGGLULEUGLYLYSPHEILEGLN
10   GLYGLYGLYGLYGLYGLNPROPHEPHEALA
11   THRALAGLYGLYLYSASNPROALAGLYILE
12   ALAGLUALALEUGLUALAALALYSLYSTYR
13   LEUVAL

Samples:

sample_1: C-ala domain, [U-98% 13C; U-98% 15N], 0.5 mM; sodium phosphate 100 mM

sample_2: C-ala domain, [U-98% 13C; U-98% 15N], 0.5 mM; sodium phosphate 100 mM

sample_3: C-ala domain, [U-99% 15N], 0.5 mM; sodium phosphate 100 mM

sample_4: C-ala domain 0.5 mM; sodium phosphate 100 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_4isotropicsample_conditions_1
2D 1H-1H TOCSYsample_4isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - data analysis

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

GB EGV44671
REF WP_008634899

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts