BMRB Entry 19045
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19045
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: The NMR structure of the BID-BAK complex PubMed: 23604079
Deposition date: 2013-02-19 Original release date: 2013-04-15
Authors: Grace, Christy; Kriwacki, Richard; Green, Douglas
Citation: Moldoveanu, Tudor; Grace, Christy; Llambi, Fabien; Nourse, Amanda; Fitzgerald, Patrick; Gehring, Kalle; Kriwacki, Richard; Green, Douglas. "BID-induced structural changes in BAK promote apoptosis." Nat. Struct. Mol. Biol. 20, 589-597 (2013).
Assembly members:
human_cBAK, polymer, 169 residues, 18950.404 Da.
human_BID_BH3_SAHB, polymer, 23 residues, 2278.613 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):
human_cBAK: ALPSASEEQVAQDTEEVFRS
YVFYRHQQEQEAEGVAAPAD
PEMVTLPLQPSSTMGQVGRQ
LAIIGDDINRRYDSEFQTML
QHLQPTAENAYEYFTKIATS
LFESGINWGRVVALLGFGYR
LALHVYQHGLTGFLGQVTRF
VVDFMLHHCIARWIAQRGGW
VAALNLGNG
human_BID_BH3_SAHB: EDIIRNIARHLAXVGDXXDR
SIX
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 556 |
| 15N chemical shifts | 176 |
| 1H chemical shifts | 1363 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | human_cBAK | 1 |
| 2 | human_BID_BH3_SAHB | 2 |
Entities:
Entity 1, human_cBAK 169 residues - 18950.404 Da.
| 1 | ALA | LEU | PRO | SER | ALA | SER | GLU | GLU | GLN | VAL | ||||
| 2 | ALA | GLN | ASP | THR | GLU | GLU | VAL | PHE | ARG | SER | ||||
| 3 | TYR | VAL | PHE | TYR | ARG | HIS | GLN | GLN | GLU | GLN | ||||
| 4 | GLU | ALA | GLU | GLY | VAL | ALA | ALA | PRO | ALA | ASP | ||||
| 5 | PRO | GLU | MET | VAL | THR | LEU | PRO | LEU | GLN | PRO | ||||
| 6 | SER | SER | THR | MET | GLY | GLN | VAL | GLY | ARG | GLN | ||||
| 7 | LEU | ALA | ILE | ILE | GLY | ASP | ASP | ILE | ASN | ARG | ||||
| 8 | ARG | TYR | ASP | SER | GLU | PHE | GLN | THR | MET | LEU | ||||
| 9 | GLN | HIS | LEU | GLN | PRO | THR | ALA | GLU | ASN | ALA | ||||
| 10 | TYR | GLU | TYR | PHE | THR | LYS | ILE | ALA | THR | SER | ||||
| 11 | LEU | PHE | GLU | SER | GLY | ILE | ASN | TRP | GLY | ARG | ||||
| 12 | VAL | VAL | ALA | LEU | LEU | GLY | PHE | GLY | TYR | ARG | ||||
| 13 | LEU | ALA | LEU | HIS | VAL | TYR | GLN | HIS | GLY | LEU | ||||
| 14 | THR | GLY | PHE | LEU | GLY | GLN | VAL | THR | ARG | PHE | ||||
| 15 | VAL | VAL | ASP | PHE | MET | LEU | HIS | HIS | CYS | ILE | ||||
| 16 | ALA | ARG | TRP | ILE | ALA | GLN | ARG | GLY | GLY | TRP | ||||
| 17 | VAL | ALA | ALA | LEU | ASN | LEU | GLY | ASN | GLY |
Entity 2, human_BID_BH3_SAHB 23 residues - 2278.613 Da.
| 1 | GLU | ASP | ILE | ILE | ARG | ASN | ILE | ALA | ARG | HIS | ||||
| 2 | LEU | ALA | MK8 | VAL | GLY | ASP | MK8 | NLE | ASP | ARG | ||||
| 3 | SER | ILE | NH2 |
Samples:
SAHB-BAK: human cBAK, [U-98% 13C; U-98% 15N], 0.5 mM; human BID BH3 SAHB 0.5 mM; Phosphate buffer 20 mM
sample_conditions_1: ionic strength: 0.02 M; pH: 6.8; pressure: 1 atm; temperature: 300 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | SAHB-BAK | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | SAHB-BAK | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | SAHB-BAK | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | SAHB-BAK | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | SAHB-BAK | isotropic | sample_conditions_1 |
| 2D 1H-1H COSY | SAHB-BAK | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | SAHB-BAK | isotropic | sample_conditions_1 |
| 3D HNCA | SAHB-BAK | isotropic | sample_conditions_1 |
| 3D HNCACB | SAHB-BAK | isotropic | sample_conditions_1 |
| 3D HBHA(CBCACO)NH | SAHB-BAK | isotropic | sample_conditions_1 |
| 3D 1H HCCH-TOCSY | SAHB-BAK | isotropic | sample_conditions_1 |
| 3D 13C-detected HCC-TOCSY | SAHB-BAK | isotropic | sample_conditions_1 |
| 2D 1H-15N TROSY | SAHB-BAK | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | SAHB-BAK | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | SAHB-BAK | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | SAHB-BAK | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | SAHB-BAK | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | SAHB-BAK | isotropic | sample_conditions_1 |
| 2D 13C-1H TROSY | SAHB-BAK | isotropic | sample_conditions_1 |
| 3D 13C/15N half-filtered 15N-edited NOESY | SAHB-BAK | isotropic | sample_conditions_1 |
| 3D 13C/15N half-filtered 13C-edited NOESY | SAHB-BAK | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin, Guntert, Mumenthaler and Wuthrich, Keller and Wuthrich - chemical shift assignment, processing, structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| GB | AAA74466 AAA74466 AAA93066 AAH04431 AAO74828 AAX32376 CAG30275 |
| PDB | |
| DBJ | BAA13606 BAF84782 BAG52419 BAG57025 BAG64474 |
| EMBL | CAA58997 CAG33700 CAI46254 |
| PRF | 2110382A 2110383A 2110384A |
| REF | NP_001179 NP_001253660 XP_003808607 XP_003897507 XP_003897509 |
| SP | Q16611 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts