Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6449
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Citation: Lu, Jianyun; Cistola, David; Li, Ellen. "Analysis of ligand binding and protein dynamics of human retinoid x receptor
alpha ligand-binding domain by nuclear magnetic resonance" Biochemistry 45, 1629-1639 (2006).
PubMed: 16460010
Assembly members:
RXRalpha ligand-binding domain, polymer, 240 residues, Formula weight is not available
REA, non-polymer, 300.435 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
RXRalpha ligand-binding domain: TSSANEDMPVERILEAELAV
EPKTETYVEANMGLNPSSPN
DPVTNICQAADKQLFTLVEW
AKRIPHFSELPLDDQVILLR
AGWNELLIASFSHRSIAVKD
GILLATGLHVHRNSAHSAGV
GAIFDRVLTELVSKMRDMQM
DKTELGCLRAIVLFNPDSKG
LSNPAEVEALREKVYASLEA
YCKHKYPEQPGRFAKLLLRL
PALRSIGLKCLEHLFFFKLI
GDTPIDTFLMEMLEAPHQMT
Data type | Count |
1H chemical shifts | 137 |
13C chemical shifts | 366 |
15N chemical shifts | 137 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | retinoid X receptor alpha ligand-binding domain, chain 1 | 1 |
2 | retinoid X receptor alpha ligand-binding domain, chain 2 | 1 |
3 | 9-cis retinoic acid | 2 |
Entity 1, retinoid X receptor alpha ligand-binding domain, chain 1 240 residues - Formula weight is not available
1 | THR | SER | SER | ALA | ASN | GLU | ASP | MET | PRO | VAL | |
2 | GLU | ARG | ILE | LEU | GLU | ALA | GLU | LEU | ALA | VAL | |
3 | GLU | PRO | LYS | THR | GLU | THR | TYR | VAL | GLU | ALA | |
4 | ASN | MET | GLY | LEU | ASN | PRO | SER | SER | PRO | ASN | |
5 | ASP | PRO | VAL | THR | ASN | ILE | CYS | GLN | ALA | ALA | |
6 | ASP | LYS | GLN | LEU | PHE | THR | LEU | VAL | GLU | TRP | |
7 | ALA | LYS | ARG | ILE | PRO | HIS | PHE | SER | GLU | LEU | |
8 | PRO | LEU | ASP | ASP | GLN | VAL | ILE | LEU | LEU | ARG | |
9 | ALA | GLY | TRP | ASN | GLU | LEU | LEU | ILE | ALA | SER | |
10 | PHE | SER | HIS | ARG | SER | ILE | ALA | VAL | LYS | ASP | |
11 | GLY | ILE | LEU | LEU | ALA | THR | GLY | LEU | HIS | VAL | |
12 | HIS | ARG | ASN | SER | ALA | HIS | SER | ALA | GLY | VAL | |
13 | GLY | ALA | ILE | PHE | ASP | ARG | VAL | LEU | THR | GLU | |
14 | LEU | VAL | SER | LYS | MET | ARG | ASP | MET | GLN | MET | |
15 | ASP | LYS | THR | GLU | LEU | GLY | CYS | LEU | ARG | ALA | |
16 | ILE | VAL | LEU | PHE | ASN | PRO | ASP | SER | LYS | GLY | |
17 | LEU | SER | ASN | PRO | ALA | GLU | VAL | GLU | ALA | LEU | |
18 | ARG | GLU | LYS | VAL | TYR | ALA | SER | LEU | GLU | ALA | |
19 | TYR | CYS | LYS | HIS | LYS | TYR | PRO | GLU | GLN | PRO | |
20 | GLY | ARG | PHE | ALA | LYS | LEU | LEU | LEU | ARG | LEU | |
21 | PRO | ALA | LEU | ARG | SER | ILE | GLY | LEU | LYS | CYS | |
22 | LEU | GLU | HIS | LEU | PHE | PHE | PHE | LYS | LEU | ILE | |
23 | GLY | ASP | THR | PRO | ILE | ASP | THR | PHE | LEU | MET | |
24 | GLU | MET | LEU | GLU | ALA | PRO | HIS | GLN | MET | THR |
Entity 2, 9-cis retinoic acid - C20 H28 O2 - 300.435 Da.
1 | REA |
sample_1: RXRalpha ligand-binding domain, [U-2H; U-13C; U-15N], 1.0 mM; RETINOIC ACID 1.0 mM
conditions_1: pH: 7.4; temperature: 298 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
4D TROSY-HNCOCA | sample_1 | not available | conditions_1 |
4D TROSY-HNCOi-1CAi | sample_1 | not available | conditions_1 |
4D TROSY-HNCACO | sample_1 | not available | conditions_1 |
4D 15N,15N-NOESY | sample_1 | not available | conditions_1 |
3D TROSY-HNCO | sample_1 | not available | conditions_1 |
3D TROSY-HN(CA)CO | sample_1 | not available | conditions_1 |
3D TROSY-HNCACB | sample_1 | not available | conditions_1 |
3D TROSY HN(CO)CACB | sample_1 | not available | conditions_1 |
No software information available
BMRB | 6429 |
PDB | |
DBJ | BAE26004 BAE73032 BAG54745 BAG72733 BAH02296 |
EMBL | CAA36982 CAA46962 CAL25727 CAL25728 CAL36079 |
GB | AAA40080 AAA42093 AAB36777 AAB36778 AAC95154 |
PRF | 1609194A |
REF | NP_001277410 NP_001277411 NP_001278849 NP_001278850 NP_001291272 |
SP | P19793 P28700 Q05343 |
TPG | DAA24096 |
AlphaFold | P19793 P28700 Q05343 |
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