BMRB Entry 30092
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30092
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Title: NMR structure of pseudo receiver domain of CikA from Thermosynechococcus elongatus
Deposition date: 2016-05-15 Original release date: 2017-03-23
Authors: Tseng, Roger; Wang, Andy
Citation: Tseng, Roger; Wang, Andy. "To be published" . ., .-..
Assembly members:
Two-component sensor histidine kinase, polymer, 117 residues, 12899.736 Da.
Natural source: Common Name: cyanobacteria Taxonomy ID: 197221 Superkingdom: Bacteria Kingdom: not available Genus/species: Thermosynechococcus elongatus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
Entity Sequences (FASTA):
Two-component sensor histidine kinase: EGRIVLVSEDEATSTLICSI
LTTAGYQVIWLVDGEVERLL
ALTPIAVLLAEPFSYGDVQE
LVDQLRQRCTPEQLKIFILG
SKGNYQGVDRYIPLPIHPES
FLQQVTMGLTSLATSAQ
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 488 |
| 15N chemical shifts | 110 |
| 1H chemical shifts | 799 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 117 residues - 12899.736 Da.
| 1 | GLU | GLY | ARG | ILE | VAL | LEU | VAL | SER | GLU | ASP | ||||
| 2 | GLU | ALA | THR | SER | THR | LEU | ILE | CYS | SER | ILE | ||||
| 3 | LEU | THR | THR | ALA | GLY | TYR | GLN | VAL | ILE | TRP | ||||
| 4 | LEU | VAL | ASP | GLY | GLU | VAL | GLU | ARG | LEU | LEU | ||||
| 5 | ALA | LEU | THR | PRO | ILE | ALA | VAL | LEU | LEU | ALA | ||||
| 6 | GLU | PRO | PHE | SER | TYR | GLY | ASP | VAL | GLN | GLU | ||||
| 7 | LEU | VAL | ASP | GLN | LEU | ARG | GLN | ARG | CYS | THR | ||||
| 8 | PRO | GLU | GLN | LEU | LYS | ILE | PHE | ILE | LEU | GLY | ||||
| 9 | SER | LYS | GLY | ASN | TYR | GLN | GLY | VAL | ASP | ARG | ||||
| 10 | TYR | ILE | PRO | LEU | PRO | ILE | HIS | PRO | GLU | SER | ||||
| 11 | PHE | LEU | GLN | GLN | VAL | THR | MET | GLY | LEU | THR | ||||
| 12 | SER | LEU | ALA | THR | SER | ALA | GLN |
Samples:
sample_1: pseudo receiver domain of CikA, [U-99% 13C; U-99% 15N], 1500 uM; H2O 95%; D2O 5%
sample_2: pseudo receiver domain of CikA, [U-99% 13C; U-99% 15N], 1500 uM; H2O 0.04%; D2O 99.96%
sample_3: pseudo receiver domain of CikA, [U-99% 13C; U-99% 15N], 300 uM; H2O 90%; D2O 10%
sample_4: pseudo receiver domain of CikA, [U-99% 13C; U-99% 15N], 450 uM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.1 mM; pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D IPAP-HNCO | sample_4 | anisotropic | sample_conditions_1 |
| 3D IPAP-HNCO | sample_3 | isotropic | sample_conditions_1 |
| 3D IPAP-HNCO(CA) | sample_4 | anisotropic | sample_conditions_1 |
| 3D IPAP-HNCO(CA) | sample_3 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
MARS, robust automatic backbone assignment of proteins Journal of Biomolecular NMR, 2004, Volume 30, Number 1, Page 11 Young-Sang Jung, Markus Zweckstetter - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
X-PLOR NIH v2.39, Schwieters, Kuszewski, Tjandra and Clore - structure calculation
XIPP, Garrett DS, Powers R, Gronenborn AM, Clore GM. J Magn Reson. 2011 Dec;213(2):357-63. doi: 10.1016/j.jmr.2011.09.007. A common sense approach to peak picking in two-, three-, and four-dimensional spectra using automatic computer analysis of contour diagrams http://spin.niddk.nih.gov/dgarrett/Xipp/xipp.html - peak picking
NMR spectrometers:
- Bruker AvanceIII 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts