BMRB Entry 25623
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25623
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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
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 271 |
15N chemical shifts | 85 |
1H chemical shifts | 85 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | KaiB G89A D91R mutant, chain 1 | 1 |
2 | KaiB G89A D91R mutant, chain 2 | 1 |
Entities:
Entity 1, KaiB G89A D91R mutant, chain 1 102 residues - Formula weight is not available
1 | ASP | TYR | LYS | ASP | ASP | ASP | ASP | LYS | MET | ALA | ||||
2 | PRO | LEU | ARG | LYS | THR | ALA | VAL | LEU | LYS | LEU | ||||
3 | TYR | VAL | ALA | GLY | ASN | THR | PRO | ASN | SER | VAL | ||||
4 | ARG | ALA | LEU | LYS | THR | LEU | ASN | ASN | ILE | LEU | ||||
5 | GLU | LYS | GLU | PHE | LYS | GLY | VAL | TYR | ALA | LEU | ||||
6 | LYS | VAL | ILE | ASP | VAL | LEU | LYS | ASN | PRO | GLN | ||||
7 | LEU | ALA | GLU | GLU | ASP | LYS | ILE | LEU | ALA | THR | ||||
8 | PRO | THR | LEU | ALA | LYS | VAL | LEU | PRO | PRO | PRO | ||||
9 | VAL | ARG | ARG | ILE | ILE | GLY | ASP | LEU | SER | ASN | ||||
10 | ARG | GLU | LYS | VAL | LEU | ILE | ALA | LEU | ARG | LEU | ||||
11 | LEU | ALA |
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:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_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