BMRB Entry 18340
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PDB ID: 2lr1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18340
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: Ma, Junhe; Edlich, Frank; Bermejo, Guillermo; Norris, Kristi; Youle, Richard; Tjandra, Nico. "Structural mechanism of Bax inhibition by cytomegalovirus protein vMIA." Proc. Natl. Acad. Sci. U.S.A. 109, 20901-20906 (2012).
PubMed: 23213219
Assembly members:
entity_1, polymer, 192 residues, 21204.494 Da.
entity_2, polymer, 21 residues, 2732.313 Da.
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: pET28
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 38 |
| 15N chemical shifts | 11 |
| 1H chemical shifts | 124 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Bax | 1 |
| 2 | vMIA | 2 |
Entities:
Entity 1, Bax 192 residues - 21204.494 Da.
| 1 | MET | ASP | GLY | SER | GLY | GLU | GLN | PRO | ARG | GLY | ||||
| 2 | GLY | GLY | PRO | THR | SER | SER | GLU | GLN | ILE | MET | ||||
| 3 | LYS | THR | GLY | ALA | LEU | LEU | LEU | GLN | GLY | PHE | ||||
| 4 | ILE | GLN | ASP | ARG | ALA | GLY | ARG | MET | GLY | GLY | ||||
| 5 | GLU | ALA | PRO | GLU | LEU | ALA | LEU | ASP | PRO | VAL | ||||
| 6 | PRO | GLN | ASP | ALA | SER | THR | LYS | LYS | LEU | SER | ||||
| 7 | GLU | CYS | LEU | LYS | ARG | ILE | GLY | ASP | GLU | LEU | ||||
| 8 | ASP | SER | ASN | MET | GLU | LEU | GLN | ARG | MET | ILE | ||||
| 9 | ALA | ALA | VAL | ASP | THR | ASP | SER | PRO | ARG | GLU | ||||
| 10 | VAL | PHE | PHE | ARG | VAL | ALA | ALA | ASP | MET | PHE | ||||
| 11 | SER | ASP | GLY | ASN | PHE | ASN | TRP | GLY | ARG | VAL | ||||
| 12 | VAL | ALA | LEU | PHE | TYR | PHE | ALA | SER | LYS | LEU | ||||
| 13 | VAL | LEU | LYS | ALA | LEU | CYS | THR | LYS | VAL | PRO | ||||
| 14 | GLU | LEU | ILE | ARG | THR | ILE | MET | GLY | TRP | THR | ||||
| 15 | LEU | ASP | PHE | LEU | ARG | GLU | ARG | LEU | LEU | GLY | ||||
| 16 | TRP | ILE | GLN | ASP | GLN | GLY | GLY | TRP | ASP | GLY | ||||
| 17 | LEU | LEU | SER | TYR | PHE | GLY | THR | PRO | THR | TRP | ||||
| 18 | GLN | THR | VAL | THR | ILE | PHE | VAL | ALA | GLY | VAL | ||||
| 19 | LEU | THR | ALA | SER | LEU | THR | ILE | TRP | LYS | LYS | ||||
| 20 | MET | GLY |
Entity 2, vMIA 21 residues - 2732.313 Da.
| 1 | CYS | GLU | ALA | LEU | LYS | LYS | ALA | LEU | ARG | ARG | ||||
| 2 | HIS | ARG | PHE | LEU | TRP | GLN | ARG | ARG | GLN | ARG | ||||
| 3 | ALA |
Related Database Links:
| BMRB | 4632 |
| PDB | 1F16 2K7W 2LR1 4BD2 4BD6 4BD7 4BD8 4ZIE 4ZIF 4ZIG 4ZIH 4ZII |
| DBJ | BAC53619 BAF83765 BAI46883 |
| EMBL | CAD10744 CCF78739 CAA35396 |
| GB | AAA03619 AAA03620 AAC48806 AAD22706 AAF82094 AAK01675 AAK01676 AAK01677 AAK01678 AAK01679 |
| REF | NP_001003011 NP_001247945 NP_001278357 NP_001278358 NP_001278360 YP_081496 |
| SP | O02703 Q07812 P16778 Q6SW94 |
| TPG | DAA19512 DAA00142 |
| AlphaFold | O02703 Q07812 P16778 Q6SW94 |
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