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 16545

Title: Solution NMR structure of protein CV0237 from Chromobacterium violaceum. Northeast Structural Genomics Consortium (NESG) target CvT1.

Deposition date: 2009-10-07 Original release date: 2010-11-10

Authors: Fares, Christophe; Lemak, Alexander; Yee, Adelinda; Garcia, Maite; Arrowsmith, Cheryl

Citation: Fares, Christophe; Lemak, Alexander; Yee, Adelinda; Garcia, Maite; Arrowsmith, Cheryl. "Solution structure of protein CV0237 from Chromobacterium violaceum"  The BMRB entry is the only known published source for the data..

Assembly members:
CV0237, polymer, 82 residues, 8624.769 Da.

Natural source:   Common Name: C. violaceum   Taxonomy ID: 536   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Chromobacterium violaceum

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

Entity Sequences (FASTA):
CV0237: QGHMDTSNHLLPGLFRQLGL EDEPAAIRAFIDSHPLPPRV PLPEAPFWTPAQAAFLRQAL ECDAEWSEAADGLAVLLQQG EA

Data sets:
Data typeCount
13C chemical shifts306
15N chemical shifts64
1H chemical shifts499

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CV02371

Entities:

Entity 1, CV0237 82 residues - 8624.769 Da.

1   GLNGLYHISMETASPTHRSERASNHISLEU
2   LEUPROGLYLEUPHEARGGLNLEUGLYLEU
3   GLUASPGLUPROALAALAILEARGALAPHE
4   ILEASPSERHISPROLEUPROPROARGVAL
5   PROLEUPROGLUALAPROPHETRPTHRPRO
6   ALAGLNALAALAPHELEUARGGLNALALEU
7   GLUCYSASPALAGLUTRPSERGLUALAALA
8   ASPGLYLEUALAVALLEULEUGLNGLNGLY
9   GLUALA

Samples:

sample_1: CV0237, [U-99% 13C; U-99% 15N], 0.4 – 0.7 mM; TRIS, [U-99% 2H], 10 mM; sodium chloride 300 mM; DTT, [U-99% 2H], 10 mM; sodium azide 0.01%; Zinc Sulfate 10 uM; Roche inhibitor cocktail 1 x; H20 90%; D20 10%

sample_conditions_1: ionic strength: 300 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NH (with NUS)sample_1isotropicsample_conditions_1
3D HBHA(CO)NH (with NUS)sample_1isotropicsample_conditions_1
3D HNCO (with NUS)sample_1isotropicsample_conditions_1
3D HNCA (with NUS)sample_1isotropicsample_conditions_1
3D 1H-15N NOESY (with NUS)sample_1isotropicsample_conditions_1
3D 1H-13C NOESY (aliph) (with NUS)sample_1isotropicsample_conditions_1
3D HCCH-TOCSY (HCH,aliph) (with NUS)sample_1isotropicsample_conditions_1
3D HCCH-TOCSY (CCH,aliph) (with NUS)sample_1isotropicsample_conditions_1
3D 1H-13C NOESY (arom) (with NUS)sample_1isotropicsample_conditions_1
3D HCCH-TOCSY (HCH.arom) (with NUS)sample_1isotropicsample_conditions_1
3D HCCH-TOCSY (CCH,arom) (with NUS)sample_1isotropicsample_conditions_1
2D HBCBCGCDHDsample_1isotropicsample_conditions_1
2D HBCBCGCDCEHEsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - peak picking

MDDNMR, Vlad Orekhov - processing (multidimensional decomposition)

ABACUS, Alexander Lemak - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - data analysis

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
GB AAQ57916 KJH68161
REF WP_011133792 WP_045050730

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