BMRB Entry 18906
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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/BMR18906
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Title: 1H, 13C and 15N resonance assignments of an N-terminal domain of CHD4 PubMed: 23417793
Deposition date: 2012-12-17 Original release date: 2013-02-20
Authors: Silva, Ana; Mackay, Joel
Citation: Silva, Ana; Kwan, Ann; Mackay, Joel. "1H, 13C and 15N resonance assignments of an N-terminal domain of CHD4" Biomol. NMR Assignments ., .-..
Assembly members:
CHD4, polymer, 86 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
CHD4: GPLGSSKEPKSSAQLLEDWG
MEDIDHVFSEEDYRTLTNYK
AFSQFVRPLIAAKNPKIAVS
KMMMVLGAKWREFSTNNPFK
GSSGAS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 306 |
| 15N chemical shifts | 74 |
| 1H chemical shifts | 550 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CHD4 | 1 |
Entities:
Entity 1, CHD4 86 residues - Formula weight is not available
| 1 | GLY | PRO | LEU | GLY | SER | SER | LYS | GLU | PRO | LYS | ||||
| 2 | SER | SER | ALA | GLN | LEU | LEU | GLU | ASP | TRP | GLY | ||||
| 3 | MET | GLU | ASP | ILE | ASP | HIS | VAL | PHE | SER | GLU | ||||
| 4 | GLU | ASP | TYR | ARG | THR | LEU | THR | ASN | TYR | LYS | ||||
| 5 | ALA | PHE | SER | GLN | PHE | VAL | ARG | PRO | LEU | ILE | ||||
| 6 | ALA | ALA | LYS | ASN | PRO | LYS | ILE | ALA | VAL | SER | ||||
| 7 | LYS | MET | MET | MET | VAL | LEU | GLY | ALA | LYS | TRP | ||||
| 8 | ARG | GLU | PHE | SER | THR | ASN | ASN | PRO | PHE | LYS | ||||
| 9 | GLY | SER | SER | GLY | ALA | SER |
Samples:
sample_1: CHD4, [U-100% 13C; U-100% 15N], 350 uM; sodium phosphate 20 mM; sodium chloride 150 mM; D2O 5%; DSS 0.2 mM
sample_conditions_1: ionic strength: 230 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection, processing
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| DBJ | BAD90499 BAE26488 BAG54725 |
| EMBL | CAA60384 |
| GB | AAH14964 AAH25962 AAH38596 AAH58578 AAI51804 |
| REF | NP_001193430 NP_001264 NP_001284482 NP_666091 XP_001063352 |
| SP | Q14839 Q6PDQ2 |
| TPG | DAA29256 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts