BMRB Entry 19521
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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/BMR19521
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Title: Solution structure of BCL-xL containing the alpha1-alpha2 disordered loop determined with selective isotope labelling of I,L,V sidechains
Deposition date: 2013-09-25 Original release date: 2014-04-28
Authors: Viacava Follis, Ariele; Grace, Christy; Kriwacki, Richard
Citation: Kriwacki, 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, 23670.139 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
Entity Sequences (FASTA):
BCL-xL: GHSMSQSNRELVVDFLSYKL
SQKGYSWSQFSDVEENRTEA
PEGTESEMETPSAINGNPSW
HLADSPAVNGATGHSSSLDA
REVIPMAAVKQALREAGDEF
ELRYRRAFSDLTSQLHITPG
TAYQSFEQVVNELFRDGVNW
GRIVAFFSFGGALCVESVDK
EMQVLVSRIAAWMATYLNDH
LEPWIQENGGWDTFVELYGN
NAAAESRKGQER
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 642 |
| 15N chemical shifts | 209 |
| 1H chemical shifts | 1041 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | BCL-xL | 1 |
Entities:
Entity 1, BCL-xL 212 residues - 23670.139 Da.
The three N terminal residues constitute the leftover of a cleaved 6xHis Tag. The construct bears a deletion of the C terminal 22 residues of the wild type protein for solubility purposes
| 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 |
Samples:
sample_1: BCL-xL, [U- 98% 13C; U- 98% 15N; U- 98% 2H; U- I,LV CH3 1H], 0.6 mM; sodium phosphate 10 mM; sodium chloride 40 mM; DTT 5 mM; NaN3 0.01%; H2O 93%; D2O 7%
sample_conditions_1: ionic strength: 0.05 M; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | 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 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - collection, processing
CARA, Keller, R.L.J. - chemical shift assignment, data analysis
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Related Database Links:
| GB | CAA80661 AAA51039 AAA82173 AAA82174 AAB17352 AAB17353 |
| BMRB | 19520 19522 |
| PDB | |
| 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 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts