BMRB Entry 19522
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PDB ID: 2mej
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19522
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Viacava Follis, Ariele; Ou, Li; Llambi, Fabien; Green, Douglas; Kriwacki, Richard. "The DNA Binding Domain is a Promiscuous Interaction Hub that Mediates the Nuclear and Cytoplasmic Functions of p53" Nat. Struct. Biol. ., .-..
Assembly members:
BCL-xL, polymer, 212 residues, 16553.609 Da.
p53, polymer, 214 residues, 22016.141 Da.
ZINC ION, non-polymer, 65.409 Da.
Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28
Entity Sequences (FASTA):
BCL-xL: GHSMSQSNRELVVDFLSYKL
SQKGYSWSQFSDVEENRTEA
PEGTESEMETPSAINGNPSW
HLADSPAVNGATGHSSSLDA
REVIPMAAVKQALREAGDEF
ELRYRRAFSDLTSQLHITPG
TAYQSFEQVVNELFRDGVNW
GRIVAFFSFGGALCVESVDK
EMQVLVSRIAAWMATYLNDH
LEPWIQENGGWDTFVELYGN
NAAAESRKGQER
p53: GHSTYQGSYGFRLGFLHSGT
AKSVTCTYSPALNKMFCQLA
KTCPVQLWVDSTPPPGTRVR
AMAIYKQSQHMTEVVRRCPH
HERCSDSDGLAPPQHLIRVE
GNLRVEYLDDRNTFRHSVVV
PYEPPEVGSDCTTIHYNYMC
NSSCMGGMNRRPILTIITLE
DSSGNLLGRNSFEVRVCACP
GRDRRTEEENLRKKGEPHHE
LPPGSTKRALSNNT
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 646 |
| 15N chemical shifts | 209 |
| 1H chemical shifts | 399 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | BCL-xL | 1 |
| 2 | p53 | 2 |
| 3 | ZINC ION | 3 |
Entities:
Entity 1, BCL-xL 212 residues - 16553.609 Da.
The three N terminal residues constitute the leftover portion of a cleaved 6XHis affinity tag. The construct bears a deletion of the C terminal 22 aminoacids for solubility reasons
| 1 | GLY | HIS | SER | MET | SER | GLN | SER | ASN | ARG | GLU | ||||
| 2 | LEU | VAL | VAL | ASP | PHE | LEU | SER | TYR | LYS | LEU | ||||
| 3 | SER | GLN | LYS | GLY | TYR | SER | TRP | SER | GLN | PHE | ||||
| 4 | SER | ASP | VAL | GLU | GLU | ASN | ARG | THR | GLU | ALA | ||||
| 5 | PRO | GLU | GLY | THR | GLU | SER | GLU | MET | GLU | THR | ||||
| 6 | PRO | SER | ALA | ILE | ASN | GLY | ASN | PRO | SER | TRP | ||||
| 7 | HIS | LEU | ALA | ASP | SER | PRO | ALA | VAL | ASN | GLY | ||||
| 8 | ALA | THR | GLY | HIS | SER | SER | SER | LEU | ASP | ALA | ||||
| 9 | ARG | GLU | VAL | ILE | PRO | MET | ALA | ALA | VAL | LYS | ||||
| 10 | GLN | ALA | LEU | ARG | GLU | ALA | GLY | ASP | GLU | PHE | ||||
| 11 | GLU | LEU | ARG | TYR | ARG | ARG | ALA | PHE | SER | ASP | ||||
| 12 | LEU | THR | SER | GLN | LEU | HIS | ILE | THR | PRO | GLY | ||||
| 13 | THR | ALA | TYR | GLN | SER | PHE | GLU | GLN | VAL | VAL | ||||
| 14 | ASN | GLU | LEU | PHE | ARG | ASP | GLY | VAL | ASN | TRP | ||||
| 15 | GLY | ARG | ILE | VAL | ALA | PHE | PHE | SER | PHE | GLY | ||||
| 16 | GLY | ALA | LEU | CYS | VAL | GLU | SER | VAL | ASP | LYS | ||||
| 17 | GLU | MET | GLN | VAL | LEU | VAL | SER | ARG | ILE | ALA | ||||
| 18 | ALA | TRP | MET | ALA | THR | TYR | LEU | ASN | ASP | HIS | ||||
| 19 | LEU | GLU | PRO | TRP | ILE | GLN | GLU | ASN | GLY | GLY | ||||
| 20 | TRP | ASP | THR | PHE | VAL | GLU | LEU | TYR | GLY | ASN | ||||
| 21 | ASN | ALA | ALA | ALA | GLU | SER | ARG | LYS | GLY | GLN | ||||
| 22 | GLU | ARG |
Entity 2, p53 214 residues - 22016.141 Da.
| 1 | GLY | HIS | SER | THR | TYR | GLN | GLY | SER | TYR | GLY | ||||
| 2 | PHE | ARG | LEU | GLY | PHE | LEU | HIS | SER | GLY | THR | ||||
| 3 | ALA | LYS | SER | VAL | THR | CYS | THR | TYR | SER | PRO | ||||
| 4 | ALA | LEU | ASN | LYS | MET | PHE | CYS | GLN | LEU | ALA | ||||
| 5 | LYS | THR | CYS | PRO | VAL | GLN | LEU | TRP | VAL | ASP | ||||
| 6 | SER | THR | PRO | PRO | PRO | GLY | THR | ARG | VAL | ARG | ||||
| 7 | ALA | MET | ALA | ILE | TYR | LYS | GLN | SER | GLN | HIS | ||||
| 8 | MET | THR | GLU | VAL | VAL | ARG | ARG | CYS | PRO | HIS | ||||
| 9 | HIS | GLU | ARG | CYS | SER | ASP | SER | ASP | GLY | LEU | ||||
| 10 | ALA | PRO | PRO | GLN | HIS | LEU | ILE | ARG | VAL | GLU | ||||
| 11 | GLY | ASN | LEU | ARG | VAL | GLU | TYR | LEU | ASP | ASP | ||||
| 12 | ARG | ASN | THR | PHE | ARG | HIS | SER | VAL | VAL | VAL | ||||
| 13 | PRO | TYR | GLU | PRO | PRO | GLU | VAL | GLY | SER | ASP | ||||
| 14 | CYS | THR | THR | ILE | HIS | TYR | ASN | TYR | MET | CYS | ||||
| 15 | ASN | SER | SER | CYS | MET | GLY | GLY | MET | ASN | ARG | ||||
| 16 | ARG | PRO | ILE | LEU | THR | ILE | ILE | THR | LEU | GLU | ||||
| 17 | ASP | SER | SER | GLY | ASN | LEU | LEU | GLY | ARG | ASN | ||||
| 18 | SER | PHE | GLU | VAL | ARG | VAL | CYS | ALA | CYS | PRO | ||||
| 19 | GLY | ARG | ASP | ARG | ARG | THR | GLU | GLU | GLU | ASN | ||||
| 20 | LEU | ARG | LYS | LYS | GLY | GLU | PRO | HIS | HIS | GLU | ||||
| 21 | LEU | PRO | PRO | GLY | SER | THR | LYS | ARG | ALA | LEU | ||||
| 22 | SER | ASN | ASN | THR |
Entity 3, ZINC ION - Zn - 65.409 Da.
| 1 | ZN |
Related Database Links:
| GB | CAA80661 AAA51039 AAA82173 AAA82174 AAB17352 AAB17353 BAC16799 |
| BMRB | 19520 19521 |
| PDB | 1AF3 1BXL 1LXL 1MAZ 1PQ0 1PQ1 1R2D 1R2E 1R2G 1R2H 1R2I 2B48 2BZW 2ME8 2ME9 2MEJ 3CVA 3IHC 3IHD 3IHE 3IHF 3IIG 3IIH 3ILB 3ILC 4HNJ |
| DBJ | BAB71819 BAB85856 BAE27189 BAE42906 BAE73044 |
| EMBL | CAA04597 CAA57886 CAA58557 CAA80661 CAI56777 |
| REF | NP_001003072 NP_001009226 NP_001009228 NP_001028842 NP_001028844 |
| SP | O77737 P53563 Q07817 Q64373 |
| TPG | DAA23121 |
| AlphaFold | O77737 P53563 Q07817 Q64373 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks