Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15732
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Citation: Yao, Wenming; Peng, Yu; Chen, Qun; Lin, Donghai. "1H, 13C, 15N backbone and side-chain resonance assignments of the Bright/ARID domain from the human histone demethylase JARID1B" Biomol. NMR Assignments 3, 85-87 (2009).
PubMed: 19636953
Assembly members:
bright_domain, polymer, 119 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 Vector: pet-22b
Entity Sequences (FASTA):
bright_domain: MRLNELEAQTRVKLNFLDQI
AKYWELQGSTLKIPHVERKI
LDLFQLNKLVAEEGGFAVVC
KDRKWTKIATKMGFAPGKAV
GSHIRGHYERILNPYNLFLS
GDSLRCLQKPNLEHHHHHH
Data type | Count |
13C chemical shifts | 270 |
15N chemical shifts | 92 |
1H chemical shifts | 544 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | jarid1B-bright | 1 |
Entity 1, jarid1B-bright 119 residues - Formula weight is not available
1 | MET | ARG | LEU | ASN | GLU | LEU | GLU | ALA | GLN | THR | ||||
2 | ARG | VAL | LYS | LEU | ASN | PHE | LEU | ASP | GLN | ILE | ||||
3 | ALA | LYS | TYR | TRP | GLU | LEU | GLN | GLY | SER | THR | ||||
4 | LEU | LYS | ILE | PRO | HIS | VAL | GLU | ARG | LYS | ILE | ||||
5 | LEU | ASP | LEU | PHE | GLN | LEU | ASN | LYS | LEU | VAL | ||||
6 | ALA | GLU | GLU | GLY | GLY | PHE | ALA | VAL | VAL | CYS | ||||
7 | LYS | ASP | ARG | LYS | TRP | THR | LYS | ILE | ALA | THR | ||||
8 | LYS | MET | GLY | PHE | ALA | PRO | GLY | LYS | ALA | VAL | ||||
9 | GLY | SER | HIS | ILE | ARG | GLY | HIS | TYR | GLU | ARG | ||||
10 | ILE | LEU | ASN | PRO | TYR | ASN | LEU | PHE | LEU | SER | ||||
11 | GLY | ASP | SER | LEU | ARG | CYS | LEU | GLN | LYS | PRO | ||||
12 | ASN | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
sample_1: bright domain, [U-95% 15N], 1 mM; NaH2PO4 20 mM; NaCl 150 mM; DTT 1 mM
sample_conditions_1: ionic strength: 0.15 M; pH: 6; pressure: 1 atm; temperature: 298 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | 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 HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D HNHA | sample_1 | isotropic | sample_conditions_1 |
SPARKY, Goddard - chemical shift assignment
BMRB | 11388 |
PDB | |
DBJ | BAC30898 BAD90482 BAE37363 |
EMBL | CAB43532 CAB63108 |
GB | AAD16061 AAH48180 AAH57318 AAI56050 AAI57032 |
REF | NP_001100647 NP_001300971 NP_006609 NP_690855 XP_002717636 |
SP | Q80Y84 Q9UGL1 |
TPG | DAA21261 |
AlphaFold | Q80Y84 Q9UGL1 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks