BMRB Entry 25625

Title:
Backbone 1H, 13C, and 15N chemical shift assignments for the double mutant G89A,D91R of KaiB in complex with the CI domain of KaiC from the Thermosynechococcus elongatus BP-1 cyanobacterial species
Deposition date:
2015-05-16
Original release date:
2015-07-14
Authors:
Chang, Yonggang; Cohen, Susan; Phong, Connie; Myers, William; Kim, Yong-Ick; Tseng, Roger; Lin, Jenny; Zhang, Li; Boyd, Joseph; Lee, Yvonne; Kang, Shannon; Lee, David; Li, Sheng; Britt, R.; Rust, Michael; Golden, Susan; LiWang, Andy
Citation:

Citation: Chang, Yonggang; Cohen, Susan; Phong, Connie; Myers, William; Kim, Yong-Ick; Tseng, Roger; Lin, Jenny; Zhang, Li; Boyd, Joseph; Lee, Yvonne; Kang, Shannon; Lee, David; Li, Sheng; Britt, R.; Rust, Michael; Golden, Susan; LiWang, Andy. "A Protein Fold Switch Joins the Circadian Oscillator to Clock Output in Cyanobacteria"  Science 349, 324-328 (2015).
PubMed: 26113641

Assembly members:

Assembly members:
FTeKaiBGDF, polymer, 124 residues, Formula weight is not available
FTeCI17247R41AK173AF, polymer, 247 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: cyanobacteria   Taxonomy ID: 146786   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Thermosynechococcus elongatus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-28b

Data sets:
Data typeCount
13C chemical shifts155
15N chemical shifts49
1H chemical shifts49

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1KaiB G89A D91R mutant, chian 11
2KaiB G89A D91R mutant, chain 21
3CI2

Entities:

Entity 1, KaiB G89A D91R mutant, chian 1 124 residues - Formula weight is not available

1   ASPTYRLYSASPASPASPASPLYSMETALA
2   PROLEUARGLYSTHRTYRVALLEULYSLEU
3   TYRVALALAGLYASNTHRPROASNSERVAL
4   ARGALALEULYSTHRLEUASNASNILELEU
5   GLULYSGLUPHELYSGLYVALTYRALALEU
6   LYSVALILEASPVALLEULYSASNPROGLN
7   LEUALAGLUGLUASPLYSILELEUALATHR
8   PROTHRLEUALALYSVALLEUPROPROPRO
9   VALARGARGILEILEGLYASPLEUSERASN
10   ARGGLULYSVALLEUILEALALEUARGLEU
11   LEUTYRGLUGLUILEGLYASPGLNALAGLU
12   ASPASPLEUGLYLEUGLUASPTYRLYSASP
13   ASPASPASPLYS

Entity 2, CI 247 residues - Formula weight is not available

1   ASPTYRLYSASPASPASPASPLYSALAGLU
2   VALLYSLYSILEPROTHRMETILEGLUGLY
3   PHEASPASPILESERHISGLYGLYLEUPRO
4   GLNGLYALATHRTHRLEUVALSERGLYTHR
5   SERGLYTHRGLYLYSTHRLEUPHEALAVAL
6   GLNPHELEUTYRASNGLYILETHRILEPHE
7   ASNGLUPROGLYILEPHEVALTHRPHEGLU
8   GLUSERPROGLNASPILEILELYSASNALA
9   LEUSERPHEGLYTRPASNLEUGLNSERLEU
10   ILEASPGLNGLYLYSLEUPHEILELEUASP
11   ALASERPROASPPROASPGLYGLNGLUVAL
12   ALAGLYASPPHEASPLEUSERALALEUILE
13   GLUARGILEGLNTYRALAILEARGLYSTYR
14   LYSALATHRARGVALSERILEASPSERVAL
15   THRALAVALPHEGLNGLNTYRASPALAALA
16   SERVALVALARGARGGLUILEPHEARGLEU
17   ALAPHEARGLEUALAGLNLEUGLYVALTHR
18   THRILEMETTHRTHRGLUARGVALASPGLU
19   TYRGLYPROVALALAARGPHEGLYVALGLU
20   GLUPHEVALSERASPASNVALVALILELEU
21   ARGASNVALLEUGLUGLYGLUARGARGARG
22   ARGTHRVALGLUILELEULYSLEUARGGLY
23   THRTHRHISMETLYSGLYGLUTYRPROPHE
24   THRILEASNASNGLYILEASNILEPHEASP
25   TYRLYSASPASPASPASPLYS

Samples:

sample_1: KaiB G89A D91R mutant, [U-13C; U-15N; U-2H], 650 uM; CI 650 uM; Tris 25 mM; NaCl 64 mM; MgCl2 0.8 mM; ADP 0.8 mM; DSS 10 uM; Protease Inhibitor Cocktail 650 uM; NaNa3 0.02%; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.064 M; pH: 7.0; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D TROSY HNCACBsample_1isotropicsample_conditions_1
3D TROSY HN(CO)CACBsample_1isotropicsample_conditions_1
3D TROSY HNCAsample_1isotropicsample_conditions_1
3D TROSY HN(CO)CAsample_1isotropicsample_conditions_1
3D TROSY HN(CA)COsample_1isotropicsample_conditions_1
3D TROSY HNCOsample_1isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - data analysis

Mars, Young-Sang Jung and Markus Zweckstetter - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks