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 16999

Title: Solution structure of protein CV0426 from Chromobacterium violaceum. NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET CVT2.

Deposition date: 2010-06-11 Original release date: 2010-07-07

Authors: Lemak, Alexander; Yee, Adelinda; Lee, Hsiau-Wei; Semesi, Anthony; Prestegard, James; Montelione, Gaetano; Arrowsmith, Cheryl

Citation: Lemak, Alexander; Yee, Adelinda; Lee, Hsiau-Wei; Semesi, Anthony; Prestegard, James; Montelione, Gaetano; Arrowsmith, Cheryl. "Solution structure of protein CV0426 from Chromobacterium violaceum."  Not known ., .-..

Assembly members:
cv0426, polymer, 102 residues, 13259.014 Da.

Natural source:   Common Name: Chromobacterium 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):
cv0426: QGMLLHSVETPRGEILNVSE QEARDVFGASEQAIADARKA TILQTLRIERDERLRACDWT QVQDVVLTADQKATWAKYRQ ALRDLPETVTDLSQIVWPQL PV

Data typeCount
13C chemical shifts381
15N chemical shifts94
1H chemical shifts642

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1cv04261

Entities:

Entity 1, cv0426 102 residues - 13259.014 Da.

1   GLNGLYMETLEULEUHISSERVALGLUTHR
2   PROARGGLYGLUILELEUASNVALSERGLU
3   GLNGLUALAARGASPVALPHEGLYALASER
4   GLUGLNALAILEALAASPALAARGLYSALA
5   THRILELEUGLNTHRLEUARGILEGLUARG
6   ASPGLUARGLEUARGALACYSASPTRPTHR
7   GLNVALGLNASPVALVALLEUTHRALAASP
8   GLNLYSALATHRTRPALALYSTYRARGGLN
9   ALALEUARGASPLEUPROGLUTHRVALTHR
10   ASPLEUSERGLNILEVALTRPPROGLNLEU
11   PROVAL

Samples:

sample_1: cv0426, [U-13C; U-15N], 0.5 mM; MOPS 10 mM; sodium chloride 450 mM; ZnSO4 10 uM; DTT 10 mM; NaN3 0.01%; benzamidine 10 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 450 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C_arom NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQC (IPAP)sample_1anisotropicsample_conditions_1

Software:

SPARKY, Goddard - peak picking

FMC, Lemak, Steren, Llinas, Arrowsmith - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

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

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
GB AAQ58104
REF WP_011133981 WP_052942315

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