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 30091

Title: NMR structure of foldswitch-stablized KaiB from Thermosynechococcus elongatus

Deposition date: 2016-05-15 Original release date: 2017-03-23

Authors: Tseng, Roger; Wang, Andy

Citation: Tseng, Roger; Wang, Andy. "NMR structure of foldswitch-stablized KaiB from Thermosynechococcus elongatus"  . ., .-..

Assembly members:
Circadian clock protein KaiB, polymer, 106 residues, 11779.870 Da.

Natural source:   Common Name: cyanobacteria   Taxonomy ID: 197221   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Thermosynechococcus elongatus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Entity Sequences (FASTA):
Circadian clock protein KaiB: MAPLRKTAVLKLYVAGNTPN SVRALKTLANILEKEFKGVY ALKVIDVLKNPQLAEEDKIL ATPTLAKVLPPPVRRIIGDL SNREKVLIALRLLAEEIGDY KDDDDK

Data sets:
Data typeCount
13C chemical shifts466
15N chemical shifts97
1H chemical shifts761

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 106 residues - 11779.870 Da.

1   METALAPROLEUARGLYSTHRALAVALLEU
2   LYSLEUTYRVALALAGLYASNTHRPROASN
3   SERVALARGALALEULYSTHRLEUALAASN
4   ILELEUGLULYSGLUPHELYSGLYVALTYR
5   ALALEULYSVALILEASPVALLEULYSASN
6   PROGLNLEUALAGLUGLUASPLYSILELEU
7   ALATHRPROTHRLEUALALYSVALLEUPRO
8   PROPROVALARGARGILEILEGLYASPLEU
9   SERASNARGGLULYSVALLEUILEALALEU
10   ARGLEULEUALAGLUGLUILEGLYASPTYR
11   LYSASPASPASPASPLYS

Samples:

sample_1: KaiB mutant in foldswitched state, [U-99% 13C; U-99% 15N], 800 uM; H2O 95%; D2O 5%

sample_2: KaiB mutant in foldswitched state, [U-99% 13C; U-99% 15N], 800 uM; H2O 0.04%; D2O 99.96%

sample_3: KaiB mutant in foldswitched state, [U-99% 13C; U-99% 15N], 300 uM; H2O 90%; D2O 10%

sample_4: KaiB mutant in foldswitched state, [U-99% 13C; U-99% 15N], 356 uM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.100 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HCANsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D HCA(CO)Nsample_2isotropicsample_conditions_1
3D IPAP-HNCO(CA)sample_3isotropicsample_conditions_1
3D IPAP-HNCO(CA)sample_4anisotropicsample_conditions_1
3D IPAP-HNCOsample_4anisotropicsample_conditions_1
3D IPAP-HNCOsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

MARS, robust automatic backbone assignment of proteins Journal of Biomolecular NMR, 2004, Volume 30, Number 1, Page 11 Young-Sang Jung, Markus Zweckstetter - chemical shift assignment

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

X-PLOR NIH v2.39, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

XIPP, Garrett DS, Powers R, Gronenborn AM, Clore GM. J Magn Reson. 2011 Dec;213(2):357-63. doi: 10.1016/j.jmr.2011.09.007. A common sense approach to peak picking in two-, three-, and four-dimensional spectra using automatic computer analysis of contour diagrams http://spin.niddk.nih.gov/dgarrett/Xipp/xipp.html - peak picking

NMR spectrometers:

  • Bruker AvanceIII 600 MHz

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