BMRB Entry 16012
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16012
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
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Title: Solution NMR structure of BNIP3 transmembrane peptide dimer in detergent micelles PubMed: 19415897
Deposition date: 2008-10-30 Original release date: 2009-05-20
Authors: Sulistijo, Endah; MacKenzie, Kevin
Citation: Sulistijo, Endah; MacKenzie, Kevin. "The structural basis for dimerization of the BNIP3 transmembrane domain" Biochemistry 48, 5106-5120 (2009).
Assembly members:
Bcl2/Adenovirus_E1B_19_kDa_protein-interacting_protein_3, polymer, 35 residues, 3790.626 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: pET3A
Entity Sequences (FASTA):
Bcl2/Adenovirus_E1B_19_kDa_protein-interacting_protein_3: GGIFSAEFLKVFLPSLLLSH
LLAIGLGIYIGRRLT
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 178 |
| 15N chemical shifts | 39 |
| 1H chemical shifts | 284 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Bcl2/Adenovirus E1B 19 kDa protein-interacting protein 3_1 | 1 |
| 2 | Bcl2/Adenovirus E1B 19 kDa protein-interacting protein 3_2 | 1 |
Entities:
Entity 1, Bcl2/Adenovirus E1B 19 kDa protein-interacting protein 3_1 35 residues - 3790.626 Da.
| 1 | GLY | GLY | ILE | PHE | SER | ALA | GLU | PHE | LEU | LYS | ||||
| 2 | VAL | PHE | LEU | PRO | SER | LEU | LEU | LEU | SER | HIS | ||||
| 3 | LEU | LEU | ALA | ILE | GLY | LEU | GLY | ILE | TYR | ILE | ||||
| 4 | GLY | ARG | ARG | LEU | THR |
Samples:
sample_1: Bcl2/Adenovirus E1B 19 kDa protein-interacting protein 3, [U-100% 13C; U-100% 15N], 0.4 mM; Bcl2/Adenovirus E1B 19 kDa protein-interacting protein 3 0.6 mM; phosphate buffer 10 mM
sample_conditions_1: pH: 5.1; temperature: 313 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D CN-NOESY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 15N-edited NOESY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C-edited NOESY-HSQC optimized for aromatic carbon | sample_1 | isotropic | sample_conditions_1 |
| half-filtered 3D CN-NOESY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D spin-echo difference CT HSQC | sample_1 | isotropic | sample_conditions_1 |
| HNHA | sample_1 | isotropic | sample_conditions_1 |
| HNCA | sample_1 | isotropic | sample_conditions_1 |
| CBCACONNH | sample_1 | isotropic | sample_conditions_1 |
| HNCO | sample_1 | isotropic | sample_conditions_1 |
| H(C)CH-COSY | sample_1 | isotropic | sample_conditions_1 |
| (H)CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| HBCBCGCDHD | sample_1 | isotropic | sample_conditions_1 |
| HBCBCGCDCEHE | sample_1 | isotropic | sample_conditions_1 |
Software:
ARIA v1.2, Linge, O'Donoghue and Nilges - refinement, structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis, processing
SPARKY, Goddard - chemical shift assignment, peak picking
VNMR, Varian - collection
NMR spectrometers:
- Varian INOVA 800 MHz
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAB29214 BAC36072 BAD96346 BAE31356 BAG58159 |
| EMBL | CAX36485 |
| GB | AAC00022 AAC16738 AAD02922 AAF98317 AAH21989 |
| REF | NP_001015859 NP_001069834 NP_001083178 NP_004043 NP_033890 |
| SP | O55003 Q12983 Q32KN2 |
| AlphaFold | O55003 Q12983 Q32KN2 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts