BMRB Entry 18792
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18792
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Title: Solution structure of BCL-xL determined with selective isotope labelling of I,L,V sidechains PubMed: 23340338
Deposition date: 2012-10-19 Original release date: 2013-01-22
Authors: Viacava Follis, Ariele; Royappa, Grace; Kriwacki, Richard
Citation: Follis, Ariele Viacava; Chipuk, Jerry; Fisher, John; Yun, Mi-Kyung; Grace, Christy; Nourse, Amanda; Baran, Katherine; Ou, Li; Min, Lie; White, Stephen; Green, Douglas; Kriwacki, Richard. "PUMA binding induces partial unfolding within BCL-xL to disrupt p53 binding and promote apoptosis." Nat. Chem. Biol. 9, 163-168 (2013).
Assembly members:
BCL-xL_apo, polymer, 181 residues, 20252.496 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
Entity Sequences (FASTA):
BCL-xL_apo: MSMAMSQSNRELVVDFLSYK
LSQKGYSWSQFSDVEENRTE
APEGTESEAVKQALREAGDE
FELRYRRAFSDLTSQLHITP
GTAYQSFEQVVNELFRDGVN
WGRIVAFFSFGGALCVESVD
KEMQVLVSRIAAWMATYLND
HLEPWIQENGGWDTFVELYG
NNAAAESRKGQERLEHHHHH
H
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 536 |
| 15N chemical shifts | 171 |
| 1H chemical shifts | 343 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | BCL-xL_apo | 1 |
Entities:
Entity 1, BCL-xL_apo 181 residues - 20252.496 Da.
Wild-type Human protein with truncation of 22 C terminal residues and disordered loop between alpha helices 1 and 2
| 1 | MET | SER | MET | ALA | MET | SER | GLN | SER | ASN | ARG | ||||
| 2 | GLU | LEU | VAL | VAL | ASP | PHE | LEU | SER | TYR | LYS | ||||
| 3 | LEU | SER | GLN | LYS | GLY | TYR | SER | TRP | SER | GLN | ||||
| 4 | PHE | SER | ASP | VAL | GLU | GLU | ASN | ARG | THR | GLU | ||||
| 5 | ALA | PRO | GLU | GLY | THR | GLU | SER | GLU | ALA | VAL | ||||
| 6 | LYS | GLN | ALA | LEU | ARG | GLU | ALA | GLY | ASP | GLU | ||||
| 7 | PHE | GLU | LEU | ARG | TYR | ARG | ARG | ALA | PHE | SER | ||||
| 8 | ASP | LEU | THR | SER | GLN | LEU | HIS | ILE | THR | PRO | ||||
| 9 | GLY | THR | ALA | TYR | GLN | SER | PHE | GLU | GLN | VAL | ||||
| 10 | VAL | ASN | GLU | LEU | PHE | ARG | ASP | GLY | VAL | ASN | ||||
| 11 | TRP | GLY | ARG | ILE | VAL | ALA | PHE | PHE | SER | PHE | ||||
| 12 | GLY | GLY | ALA | LEU | CYS | VAL | GLU | SER | VAL | ASP | ||||
| 13 | LYS | GLU | MET | GLN | VAL | LEU | VAL | SER | ARG | ILE | ||||
| 14 | ALA | ALA | TRP | MET | ALA | THR | TYR | LEU | ASN | ASP | ||||
| 15 | HIS | LEU | GLU | PRO | TRP | ILE | GLN | GLU | ASN | GLY | ||||
| 16 | GLY | TRP | ASP | THR | PHE | VAL | GLU | LEU | TYR | GLY | ||||
| 17 | ASN | ASN | ALA | ALA | ALA | GLU | SER | ARG | LYS | GLY | ||||
| 18 | GLN | GLU | ARG | LEU | GLU | HIS | HIS | HIS | HIS | HIS | ||||
| 19 | HIS |
Samples:
sample_1: BCL-xL_apo, [U-100% 13C; U-100% 15N; U-95% 2H; Ile,Leu,Val C1H3], 0.9 mM; sodium phosphate 10 mM; sodium chloride 40 mM; NaN3 0.1%; H2O 92%; D2O 8%
sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 273 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 HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection, processing
CARA, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, peak picking, structure solution
AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts