BMRB Entry 15695
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15695
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Title: Solution NMR structure of the chromobox protein homolog 4
Deposition date: 2008-03-27 Original release date: 2008-03-28
Authors: Kaustov, Lilia; Lemak, Alexander; Quyang, Hui; Fares, Christophe; Gutmanas, Alexandras; Ravichandran, Mani; Loppnau, Peter; Bountra, Chas; Weigelt, Johan; Edwards, Aled; Min, Jinrong; Arrowsmith, Cheryl
Citation: Kaustov, Lilia; Lemak, Alexander; Quyang, Hui; Fares, Christophe; Gutmanas, Alexandras; Ravichandran, Mani; Loppnau, Peter; Bountra, Chas; Weigelt, Johan; Edwards, Aled; Min, Jinrong; Arrowsmith, Cheryl. "Solution NMR structure of the chromobox protein homolog 4" . ., .-..
Assembly members:
cbx4, polymer, 60 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):
cbx4: GSEHVFAVESIEKKRIRKGR
VEYLVKWRGWSPKYNTWEPE
ENILDPRLLIAFQNRERQEQ
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 262 |
| 15N chemical shifts | 56 |
| 1H chemical shifts | 429 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | cbx4 | 1 |
Entities:
Entity 1, cbx4 60 residues - Formula weight is not available
| 1 | GLY | SER | GLU | HIS | VAL | PHE | ALA | VAL | GLU | SER | |
| 2 | ILE | GLU | LYS | LYS | ARG | ILE | ARG | LYS | GLY | ARG | |
| 3 | VAL | GLU | TYR | LEU | VAL | LYS | TRP | ARG | GLY | TRP | |
| 4 | SER | PRO | LYS | TYR | ASN | THR | TRP | GLU | PRO | GLU | |
| 5 | GLU | ASN | ILE | LEU | ASP | PRO | ARG | LEU | LEU | ILE | |
| 6 | ALA | PHE | GLN | ASN | ARG | GLU | ARG | GLN | GLU | GLN |
Samples:
sample_1: phosphate 0.5 mM; phosphate 10 mM; sodium chloride 300 mM; DTT 2 mM
sample_conditions_1: ionic strength: 300 mM; pH: 7.4; 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-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY | 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 |
| 3D aromat 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - peak picking
ABACUS, Grishaev - chemical shift assignment
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 500 MHz
Related Database Links:
| PDB | |
| DBJ | BAA33402 BAG73014 |
| GB | AAB80718 AAB96874 AAH14967 AAH45162 AAI17802 |
| REF | NP_003646 NP_031651 NP_989973 XP_001081757 XP_001149752 |
| SP | O00257 O55187 |
| TPG | DAA18114 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts