BMRB Entry 25622

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25622

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Title:
Backbone 1H, 13C, and 15N chemical shift assignments for the thioredoxin-like fold of the single mutant D91R of dimeric KaiB 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:
FTBN94YYD91RF_fs, polymer, 110 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FTBN94YYD91RF_fs: DYKDDDDKMAPLRKTAVLKL YVAGNTPNSVRALKTLNNIL EKEFKGVYALKVIDVLKNPQ LAEEDKILATPTLAKVLPPP VRRIIGDLSNREKVLIGLRL LADYKDDDDK

Data sets:
Data typeCount
13C chemical shifts244
15N chemical shifts77
1H chemical shifts77

Additional metadata:

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

Assembly:

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

Entities:

Entity 1, KaiB D91R mutant, chain 1 110 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   ARGGLULYSVALLEUILEGLYLEUARGLEU
11   LEUALAASPTYRLYSASPASPASPASPLYS

Samples:

sample_1: FTBN94YYD91RF_fs, [U-99% 13C; U-98% 15N], 1819 uM; Tris 20 mM; NaCl 100 mM; DSS 10 uM; NaNa3 0.02%; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.1 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 HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks