BMRB Entry 25619
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25619
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Title: Backbone 1H, 13C, and 15N chemical shift assignments for N-SasA, the N-terminal domain of SasA, in complex with the CI domain of KaiC 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:
FTeSasA16107P16AF, polymer, 108 residues, Formula weight is not available
FTeCI17247R41AK173AF, polymer, 247 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):
FTeSasA16107P16AF: DYKDDDDKALSLLLFVANRP
GDEEETAAIQAHIQQLPSNF
SFELKVVPIGEQPYLLEEYK
LVATPALIKVRPEPRQTLAG
RKLLQKVDYWWPRWQREVAL
DYKDDDDK
FTeCI17247R41AK173AF: DYKDDDDKAEVKKIPTMIEG
FDDISHGGLPQGATTLVSGT
SGTGKTLFAVQFLYNGITIF
NEPGIFVTFEESPQDIIKNA
LSFGWNLQSLIDQGKLFILD
ASPDPDGQEVAGDFDLSALI
ERIQYAIRKYKATRVSIDSV
TAVFQQYDAASVVRREIFRL
AFRLAQLGVTTIMTTERVDE
YGPVARFGVEEFVSDNVVIL
RNVLEGERRRRTVEILKLRG
TTHMKGEYPFTINNGINIFD
YKDDDDK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 235 |
| 15N chemical shifts | 69 |
| 1H chemical shifts | 69 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | N-SasA | 1 |
| 2 | CI | 2 |
Entities:
Entity 1, N-SasA 108 residues - Formula weight is not available
| 1 | ASP | TYR | LYS | ASP | ASP | ASP | ASP | LYS | ALA | LEU | ||||
| 2 | SER | LEU | LEU | LEU | PHE | VAL | ALA | ASN | ARG | PRO | ||||
| 3 | GLY | ASP | GLU | GLU | GLU | THR | ALA | ALA | ILE | GLN | ||||
| 4 | ALA | HIS | ILE | GLN | GLN | LEU | PRO | SER | ASN | PHE | ||||
| 5 | SER | PHE | GLU | LEU | LYS | VAL | VAL | PRO | ILE | GLY | ||||
| 6 | GLU | GLN | PRO | TYR | LEU | LEU | GLU | GLU | TYR | LYS | ||||
| 7 | LEU | VAL | ALA | THR | PRO | ALA | LEU | ILE | LYS | VAL | ||||
| 8 | ARG | PRO | GLU | PRO | ARG | GLN | THR | LEU | ALA | GLY | ||||
| 9 | ARG | LYS | LEU | LEU | GLN | LYS | VAL | ASP | TYR | TRP | ||||
| 10 | TRP | PRO | ARG | TRP | GLN | ARG | GLU | VAL | ALA | LEU | ||||
| 11 | ASP | TYR | LYS | ASP | ASP | ASP | ASP | LYS |
Entity 2, CI 247 residues - Formula weight is not available
| 1 | ASP | TYR | LYS | ASP | ASP | ASP | ASP | LYS | ALA | GLU | ||||
| 2 | VAL | LYS | LYS | ILE | PRO | THR | MET | ILE | GLU | GLY | ||||
| 3 | PHE | ASP | ASP | ILE | SER | HIS | GLY | GLY | LEU | PRO | ||||
| 4 | GLN | GLY | ALA | THR | THR | LEU | VAL | SER | GLY | THR | ||||
| 5 | SER | GLY | THR | GLY | LYS | THR | LEU | PHE | ALA | VAL | ||||
| 6 | GLN | PHE | LEU | TYR | ASN | GLY | ILE | THR | ILE | PHE | ||||
| 7 | ASN | GLU | PRO | GLY | ILE | PHE | VAL | THR | PHE | GLU | ||||
| 8 | GLU | SER | PRO | GLN | ASP | ILE | ILE | LYS | ASN | ALA | ||||
| 9 | LEU | SER | PHE | GLY | TRP | ASN | LEU | GLN | SER | LEU | ||||
| 10 | ILE | ASP | GLN | GLY | LYS | LEU | PHE | ILE | LEU | ASP | ||||
| 11 | ALA | SER | PRO | ASP | PRO | ASP | GLY | GLN | GLU | VAL | ||||
| 12 | ALA | GLY | ASP | PHE | ASP | LEU | SER | ALA | LEU | ILE | ||||
| 13 | GLU | ARG | ILE | GLN | TYR | ALA | ILE | ARG | LYS | TYR | ||||
| 14 | LYS | ALA | THR | ARG | VAL | SER | ILE | ASP | SER | VAL | ||||
| 15 | THR | ALA | VAL | PHE | GLN | GLN | TYR | ASP | ALA | ALA | ||||
| 16 | SER | VAL | VAL | ARG | ARG | GLU | ILE | PHE | ARG | LEU | ||||
| 17 | ALA | PHE | ARG | LEU | ALA | GLN | LEU | GLY | VAL | THR | ||||
| 18 | THR | ILE | MET | THR | THR | GLU | ARG | VAL | ASP | GLU | ||||
| 19 | TYR | GLY | PRO | VAL | ALA | ARG | PHE | GLY | VAL | GLU | ||||
| 20 | GLU | PHE | VAL | SER | ASP | ASN | VAL | VAL | ILE | LEU | ||||
| 21 | ARG | ASN | VAL | LEU | GLU | GLY | GLU | ARG | ARG | ARG | ||||
| 22 | ARG | THR | VAL | GLU | ILE | LEU | LYS | LEU | ARG | GLY | ||||
| 23 | THR | THR | HIS | MET | LYS | GLY | GLU | TYR | PRO | PHE | ||||
| 24 | THR | ILE | ASN | ASN | GLY | ILE | ASN | ILE | PHE | ASP | ||||
| 25 | TYR | LYS | ASP | ASP | ASP | ASP | LYS |
Samples:
sample_1: N-SasA, [U-13C; U-15N; U-2H], 570 uM; CI 600 uM; Protease Inhibitor Cocktail 570 uM; Tris 20 mM; NaCl 50 mM; MgCl2 1 mM; ADP 1 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 TROSY | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY 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