BMRB Entry 18200
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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/BMR18200
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Title: Resonance assignments for C-terminal DNA-binding domain of RstA protein from Klebsiella pneumonia PubMed: 22481468
Deposition date: 2012-01-17 Original release date: 2012-05-08
Authors: Chen, Sheng-Chia; Fang, Pei-Ju; Cheng, Ya-Hsin; Chang, Chi-Fon; Yu, Tsunai; Huang, Tai-huang
Citation: Chen, Sheng-Chia; Chang, Chi-Fon; Fan, Pei-Ju; Cheng, Ya-Hsin; Yu, Tsunai; Huang, Tai-Huang. "(1)H, (13)C and (15)N resonance assignments of the C-terminal DNA-binding domain of RstA protein from Klebsiella pneumoniae." Biomol. NMR Assignments 7, 85-88 (2013).
Assembly members:
RstA_C, polymer, 119 residues, Formula weight is not available
Natural source: Common Name: Klebsiella pneumonia Taxonomy ID: 573 Superkingdom: Bacteria Kingdom: not available Genus/species: Klebsiella pneumonia
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
RstA_C: MHHHHHHAMGTLTPHKTISF
GSLTIDPVNRQVLLGGENVA
LSTADFDLLWELATHAGQIM
DRDALLKNLRGVTYDGMDRS
VDVAISRLRKKLLDNATEPY
RIKTVRNKGYLFAPHAWDN
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 389 |
| 15N chemical shifts | 103 |
| 1H chemical shifts | 681 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RstA_C | 1 |
Entities:
Entity 1, RstA_C 119 residues - Formula weight is not available
| 1 | MET | HIS | HIS | HIS | HIS | HIS | HIS | ALA | MET | GLY | ||||
| 2 | THR | LEU | THR | PRO | HIS | LYS | THR | ILE | SER | PHE | ||||
| 3 | GLY | SER | LEU | THR | ILE | ASP | PRO | VAL | ASN | ARG | ||||
| 4 | GLN | VAL | LEU | LEU | GLY | GLY | GLU | ASN | VAL | ALA | ||||
| 5 | LEU | SER | THR | ALA | ASP | PHE | ASP | LEU | LEU | TRP | ||||
| 6 | GLU | LEU | ALA | THR | HIS | ALA | GLY | GLN | ILE | MET | ||||
| 7 | ASP | ARG | ASP | ALA | LEU | LEU | LYS | ASN | LEU | ARG | ||||
| 8 | GLY | VAL | THR | TYR | ASP | GLY | MET | ASP | ARG | SER | ||||
| 9 | VAL | ASP | VAL | ALA | ILE | SER | ARG | LEU | ARG | LYS | ||||
| 10 | LYS | LEU | LEU | ASP | ASN | ALA | THR | GLU | PRO | TYR | ||||
| 11 | ARG | ILE | LYS | THR | VAL | ARG | ASN | LYS | GLY | TYR | ||||
| 12 | LEU | PHE | ALA | PRO | HIS | ALA | TRP | ASP | ASN |
Samples:
sample_1: RstA_C, [U-13C; U-15N], 0.1-1.0 mM
sample_conditions_1: ionic strength: 50 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA, Keller and Wuthrich - chemical shift assignment
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAH63203 BAS35643 |
| EMBL | CCI77052 CCM80542 CCM87616 CCM95853 CCN29569 |
| GB | ABR76952 ACI11717 ADC58723 AEJ97988 AEW61123 |
| REF | WP_002903377 WP_008805070 WP_017898700 WP_020313713 WP_021440054 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts