BMRB Entry 19251
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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/BMR19251
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Title: Structure, function, and tethering of DNA-binding domains in 54 transcriptional activators PubMed: 23818155
Deposition date: 2013-05-19 Original release date: 2013-08-26
Authors: HONG, EUNMI; Wemmer, David E
Citation: Vidangos, Natasha; Maris, Ann; Young, Anisa; Hong, Eunmi; Pelton, Jeffrey; Batchelor, Joseph; Wemmer, David. "Structure, function, and tethering of DNA-binding domains in (54) transcriptional activators." Biopolymers 99, 1082-1096 (2013).
Assembly members:
entity, polymer, 70 residues, 8334.906 Da.
Natural source: Common Name: aquificales Taxonomy ID: 63363 Superkingdom: Bacteria Kingdom: not available Genus/species: Aquifex aeolicus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: TSSELPELLRKRERKTGDLP
KFIEETEKKRIIEALEKTGY
VKSRAAKLLGYTLRQLDYRI
KKYGIELKKF
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 187 |
| 15N chemical shifts | 58 |
| 1H chemical shifts | 413 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Nlh2 | 1 |
Entities:
Entity 1, Nlh2 70 residues - 8334.906 Da.
| 1 | THR | SER | SER | GLU | LEU | PRO | GLU | LEU | LEU | ARG | |
| 2 | LYS | ARG | GLU | ARG | LYS | THR | GLY | ASP | LEU | PRO | |
| 3 | LYS | PHE | ILE | GLU | GLU | THR | GLU | LYS | LYS | ARG | |
| 4 | ILE | ILE | GLU | ALA | LEU | GLU | LYS | THR | GLY | TYR | |
| 5 | VAL | LYS | SER | ARG | ALA | ALA | LYS | LEU | LEU | GLY | |
| 6 | TYR | THR | LEU | ARG | GLN | LEU | ASP | TYR | ARG | ILE | |
| 7 | LYS | LYS | TYR | GLY | ILE | GLU | LEU | LYS | LYS | PHE |
Samples:
sample_1: Nlh2, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate, [U-100% 15N], 1 mM; H2O 95%; D2O 5%
sample_2: Nlh2, [U-100% 13C; U-100% 15N], 1 mM; D2O 100%
sample_conditions_1: ionic strength: 100 mM; pH: 7; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C 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 HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment, data analysis, peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
Molmol, Koradi, Billeter and Wuthrich - refinement
TALOS, Cornilescu, Delaglio and Bax - chemical shift calculation
NMR spectrometers:
- Bruker DRX 800 MHz
- Bruker DRX 900 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts