BMRB Entry 18856
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18856
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Title: HADDOCK structure of GtYybT PAS Homodimer PubMed: 23504327
Deposition date: 2012-11-25 Original release date: 2013-03-25
Authors: Liang, Zhao-xun; Pervushin, Konstantin; Tan, Edward; Rao, Feng; Pasunooti, Swathi; Soehano, Ishin; Lescar, Julien
Citation: Tan, Edward; Rao, Feng; Pasunooti, Swathi; Pham, Thi Huong; Soehano, Ishin; Turner, Mark; Liew, Chong Wai; Lescar, Julien; Pervushin, Konstantin; Liang, Zhao-Xun. "Solution structure of the PAS domain of a thermophilic YybT protein homolog reveals a potential ligand-binding site." J. Biol. Chem. 288, 11949-11959 (2013).
Assembly members:
PAS_domain_of_DHH_subfamily_1_protein, polymer, 113 residues, 13209.449 Da.
Natural source: Common Name: Geobacillus thermodenitrificans Taxonomy ID: 33940 Superkingdom: Bacteria Kingdom: not available Genus/species: Geobacillus thermodenitrificans
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
PAS_domain_of_DHH_subfamily_1_protein: RGSHMRSLHKELQQYISNLS
YRVKKVSEEALMQMPIGILL
LDEEDKIEWSNRFLAACFKE
QTLIGRSLAELSEPLAAFVK
KGKTDEEIIELNGKQLKVIV
HRHERLLYFFDVT
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 498 |
| 15N chemical shifts | 122 |
| 1H chemical shifts | 865 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PAS domain of DHH subfamily 1 protein_1 | 1 |
| 2 | PAS domain of DHH subfamily 1 protein_2 | 1 |
Entities:
Entity 1, PAS domain of DHH subfamily 1 protein_1 113 residues - 13209.449 Da.
| 1 | ARG | GLY | SER | HIS | MET | ARG | SER | LEU | HIS | LYS | ||||
| 2 | GLU | LEU | GLN | GLN | TYR | ILE | SER | ASN | LEU | SER | ||||
| 3 | TYR | ARG | VAL | LYS | LYS | VAL | SER | GLU | GLU | ALA | ||||
| 4 | LEU | MET | GLN | MET | PRO | ILE | GLY | ILE | LEU | LEU | ||||
| 5 | LEU | ASP | GLU | GLU | ASP | LYS | ILE | GLU | TRP | SER | ||||
| 6 | ASN | ARG | PHE | LEU | ALA | ALA | CYS | PHE | LYS | GLU | ||||
| 7 | GLN | THR | LEU | ILE | GLY | ARG | SER | LEU | ALA | GLU | ||||
| 8 | LEU | SER | GLU | PRO | LEU | ALA | ALA | PHE | VAL | LYS | ||||
| 9 | LYS | GLY | LYS | THR | ASP | GLU | GLU | ILE | ILE | GLU | ||||
| 10 | LEU | ASN | GLY | LYS | GLN | LEU | LYS | VAL | ILE | VAL | ||||
| 11 | HIS | ARG | HIS | GLU | ARG | LEU | LEU | TYR | PHE | PHE | ||||
| 12 | ASP | VAL | THR |
Samples:
sample: PAS domain of DHH subfamily 1 protein, [U-99% 13C; U-99% 15N], 0.7 mM; phosphate buffer 50 mM; NaCl 200 mM
sample_conditions_1: ionic strength: 250 mM; pH: 6.2; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D_15N_TROSY-HSQC | sample | isotropic | sample_conditions_1 |
| 2D_13C_HMQC | sample | isotropic | sample_conditions_1 |
| 3D_HNCA | sample | isotropic | sample_conditions_1 |
| 3D_HN(CO)CA | sample | isotropic | sample_conditions_1 |
| 3D_HNCO | sample | isotropic | sample_conditions_1 |
| 3D_HN(CA)CO | sample | isotropic | sample_conditions_1 |
| 3D_CBCA(CO)NH | sample | isotropic | sample_conditions_1 |
| 3D_HN(CA)CB | sample | isotropic | sample_conditions_1 |
| 3D_15N-separated_NOESY | sample | isotropic | sample_conditions_1 |
| 3D_13C-separated_NOESY | sample | isotropic | sample_conditions_1 |
Software:
CNS, Brunger A. T. et.al. - refinement
NMR spectrometers:
- Bruker AVANCE II 600, 700 MHz
Related Database Links:
| PDB | |
| GB | ABO68756 EDY05509 KQB91469 |
| REF | WP_008880810 WP_011888454 WP_029761080 |
Download simulated HSQC data in one of the following formats:
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