BMRB Entry 34589
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34589
MolProbity Validation Chart
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NMR-STAR v3 text file.
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Title: Solution structure of the chloroplast outer envelope channel OEP21 PubMed: 37156968
Deposition date: 2021-01-07 Original release date: 2022-01-16
Authors: Hagn, F.; Haeusler, E.
Citation: Gunsel, Umut; Klopfer, Kai; Hausler, Elisabeth; Hitzenberger, Manuel; Bolter, Bettina; Sperl, Laura; Zacharias, Martin; Soll, Jurgen; Hagn, Franz. "Structural basis of metabolite transport by the chloroplast outer envelope channel OEP21" Nat. Struct. Mol. Biol. 30, 761-769 (2023).
Assembly members:
entity_1, polymer, 189 residues, 22098.742 Da.
Natural source: Common Name: Garden pea Taxonomy ID: 3888 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Pisum sativum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: METSLRYGGDSKALKIHAKE
KLRIDTNTFFQVRGGLDTKT
GQPSSGSALIRHFYPNFSAT
LGVGVRYDKQDSVGVRYAKN
DKLRYTVLAKKTFPVTNDGL
VNFKIKGGCDVDQDFKEWKS
RGGAEFSWNVFNFQKDQDVR
LRIGYEAFEQVPYLQIRENN
WTFNADYKGRWNVRYDLLEH
HHHHHHHHH
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 459 |
| 15N chemical shifts | 151 |
| 1H chemical shifts | 370 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 189 residues - 22098.742 Da.
| 1 | MET | GLU | THR | SER | LEU | ARG | TYR | GLY | GLY | ASP | ||||
| 2 | SER | LYS | ALA | LEU | LYS | ILE | HIS | ALA | LYS | GLU | ||||
| 3 | LYS | LEU | ARG | ILE | ASP | THR | ASN | THR | PHE | PHE | ||||
| 4 | GLN | VAL | ARG | GLY | GLY | LEU | ASP | THR | LYS | THR | ||||
| 5 | GLY | GLN | PRO | SER | SER | GLY | SER | ALA | LEU | ILE | ||||
| 6 | ARG | HIS | PHE | TYR | PRO | ASN | PHE | SER | ALA | THR | ||||
| 7 | LEU | GLY | VAL | GLY | VAL | ARG | TYR | ASP | LYS | GLN | ||||
| 8 | ASP | SER | VAL | GLY | VAL | ARG | TYR | ALA | LYS | ASN | ||||
| 9 | ASP | LYS | LEU | ARG | TYR | THR | VAL | LEU | ALA | LYS | ||||
| 10 | LYS | THR | PHE | PRO | VAL | THR | ASN | ASP | GLY | LEU | ||||
| 11 | VAL | ASN | PHE | LYS | ILE | LYS | GLY | GLY | CYS | ASP | ||||
| 12 | VAL | ASP | GLN | ASP | PHE | LYS | GLU | TRP | LYS | SER | ||||
| 13 | ARG | GLY | GLY | ALA | GLU | PHE | SER | TRP | ASN | VAL | ||||
| 14 | PHE | ASN | PHE | GLN | LYS | ASP | GLN | ASP | VAL | ARG | ||||
| 15 | LEU | ARG | ILE | GLY | TYR | GLU | ALA | PHE | GLU | GLN | ||||
| 16 | VAL | PRO | TYR | LEU | GLN | ILE | ARG | GLU | ASN | ASN | ||||
| 17 | TRP | THR | PHE | ASN | ALA | ASP | TYR | LYS | GLY | ARG | ||||
| 18 | TRP | ASN | VAL | ARG | TYR | ASP | LEU | LEU | GLU | HIS | ||||
| 19 | HIS | HIS | HIS | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: OEP21, [U-13C; U-15N; U-2H], 0.4 ± 0.05 mM; LDAO, [U-100% 2H], 300 ± 50 mM; sodium phosphate 20 ± 2 mM; sodium chloride 50 ± 5 mM; DTT 5 ± 0.5 mM; EDTA 0.5 ± 0.05 mM
sample_2: OEP21, [ U-15N; U-2H],ILVAFY, 0.4 ± 0.05 mM; LDAO, [U-100% 2H], 300 ± 50 mM; sodium phosphate 20 ± 2 mM; sodium chloride 50 ± 5 mM; DTT 5 ± 0.5 mM; EDTA 0.5 ± 0.05 mM
sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N TROSY HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 3D 13C-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HMQC | sample_2 | isotropic | sample_conditions_1 |
| 3D 13C-15N NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N TROSY HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
TopSpin, Bruker Biospin - collection, processing
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
hmsIST, Wagner Lab, Harvard Medical School - processing
NMRFAM-SPARKY, Univ of Wisconsin - chemical shift assignment, peak picking
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation
NMR spectrometers:
- Bruker AVANCE III HD 900 MHz
- Bruker AVANCE III HD 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts