BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 15162

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR15162

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Title: Backbone Chemical Shift Assignments of Cholera Toxin Enzymatic Domain (1-167)   PubMed: 18272180

Deposition date: 2007-03-06 Original release date: 2007-06-20

Authors: Ampapathi, Ravi; Lou, In Hye; Creath, Andrea; Blanke, Steven; Legge, Glen

Citation: Ampapathi, Ravi; Creath, Andrea; Lou, Dianne; Craft, John; Blanke, Steven; Legge, Glen. "Order-disorder-order transitions mediate the activation of cholera toxin"  J. Mol. Biol. 377, 748-60 (2008).

Assembly members:
CTA1-T2, polymer, 167 residues, 18891.8 Da.

Natural source:   Common Name: Vibrio comma   Taxonomy ID: 666   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Vibrio cholerae

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

Entity Sequences (FASTA):
CTA1-T2: NDDKLYRADSRPPDEIKQSG GLMPRGQSDYFDRGTQMNIN LYDHARGTQTGFVRHDDGYV STSISLRSAHLVGQTILSGH STYYIYVIATAPNMFNVNDV LGAYSPHPDEQDVSALGGIP YSQIVGWYRVHFGVLDEQLH RNRGYRDRYYSNLDIAPAAD GYGLAGF

Data sets:
Data typeCount
13C chemical shifts390
15N chemical shifts131
1H chemical shifts131

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CTA1-T21

Entities:

Entity 1, CTA1-T2 167 residues - 18891.8 Da.

This is a truncated version(1-167) of Full length CTA1 (1-192), which increases the stability of the construct in solution.

1   ASNASPASPLYSLEUTYRARGALAASPSER
2   ARGPROPROASPGLUILELYSGLNSERGLY
3   GLYLEUMETPROARGGLYGLNSERASPTYR
4   PHEASPARGGLYTHRGLNMETASNILEASN
5   LEUTYRASPHISALAARGGLYTHRGLNTHR
6   GLYPHEVALARGHISASPASPGLYTYRVAL
7   SERTHRSERILESERLEUARGSERALAHIS
8   LEUVALGLYGLNTHRILELEUSERGLYHIS
9   SERTHRTYRTYRILETYRVALILEALATHR
10   ALAPROASNMETPHEASNVALASNASPVAL
11   LEUGLYALATYRSERPROHISPROASPGLU
12   GLNASPVALSERALALEUGLYGLYILEPRO
13   TYRSERGLNILEVALGLYTRPTYRARGVAL
14   HISPHEGLYVALLEUASPGLUGLNLEUHIS
15   ARGASNARGGLYTYRARGASPARGTYRTYR
16   SERASNLEUASPILEALAPROALAALAASP
17   GLYTYRGLYLEUALAGLYPHE

Samples:

sample_1: CTA1-T2 0.2 mM; TRIS, [U-99% 2H], 20 mM; sodium chloride 200 mM; D2O, [U-99% 2H], 6 % v/v; sodium azide 0.05 % w/v; EDTA 1 mM

sample_conditions_1: pH: 7.2; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

SPARKY v3.110, Goddard - data analysis, peak picking

NMRPipe vScript Version 2002.044.17.08, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw vScript Version 2002.044.17.08, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

GB VC1457 AAA27514 AAD51359 AAF94614 AAL09681 AAL60525
SWS 301555
PDB
DBJ BAA06288 BAA06290 BAG06738 BAG66065 BAI50777
EMBL CAA24995 CAA41590 CAA41592 CAE11218 CRZ40571
PRF 1001196A
REF NP_231100 WP_001881225 WP_001888508 WP_001911232 WP_005514365
SP P01555

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