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 25623

Title: Backbone 1H, 13C, and 15N chemical shift assignments for the double mutant G89A,D91R of dimeric KaiB from the Thermosynechococcus elongatus BP-1 cyanobacterial species   PubMed: 26113641

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: 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).

Assembly members:
FTeKaiBN94YYGD, polymer, 102 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
FTeKaiBN94YYGD: DYKDDDDKMAPLRKTAVLKL YVAGNTPNSVRALKTLNNIL EKEFKGVYALKVIDVLKNPQ LAEEDKILATPTLAKVLPPP VRRIIGDLSNREKVLIALRL LA

Data sets:
Data typeCount
13C chemical shifts271
15N chemical shifts85
1H chemical shifts85

Additional metadata:

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

Assembly:

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

Entities:

Entity 1, KaiB G89A D91R mutant, chain 1 102 residues - Formula weight is not available

1   ASPTYRLYSASPASPASPASPLYSMETALA
2   PROLEUARGLYSTHRALAVALLEULYSLEU
3   TYRVALALAGLYASNTHRPROASNSERVAL
4   ARGALALEULYSTHRLEUASNASNILELEU
5   GLULYSGLUPHELYSGLYVALTYRALALEU
6   LYSVALILEASPVALLEULYSASNPROGLN
7   LEUALAGLUGLUASPLYSILELEUALATHR
8   PROTHRLEUALALYSVALLEUPROPROPRO
9   VALARGARGILEILEGLYASPLEUSERASN
10   ARGGLULYSVALLEUILEALALEUARGLEU
11   LEUALA

Samples:

sample_1: FTeKaiBN94YYGD, [U-99% 13C; U-98% 15N], 800 uM; Tris 20 mM; NaCl 50 mM; DSS 10 uM; NaNa3 0.02%; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.05 M; pH: 7.0; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D 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 simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts