BMRB Entry 18358
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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/BMR18358
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Title: The solution structure of the dimeric Acanthaporin
Deposition date: 2012-03-28 Original release date: 2012-05-01
Authors: Michalek, Matthias; Soennichsen, Frank; Wechselberger, Rainer; Dingley, Andrew; Wienk, Hans; Simanski, Maren; Herbst, Rosa; Lorenzen, Inken; Marciano-Cabral, Francine; Gelhaus, Christoph; Groetzinger, Joachim; Leippe, Matthias
Citation: Michalek, Matthias; Soennichsen, Frank; Wechselberger, Rainer; Dingley, Andrew; Wienk, Hans; Simanski, Maren; Herbst, Rosa; Lorenzen, Inken; Marciano-Cabral, Francine; Gelhaus, Christoph; Groetzinger, Joachim; Leippe, Matthias. "The solution structure of the dimeric Acanthaporin" Not known ., .-..
Assembly members:
acanthaporin_dimer, polymer, 61 residues, 6001.235 Da.
Natural source: Common Name: Acanthamoeba culbertsoni Taxonomy ID: 43142 Superkingdom: Eukaryota Kingdom: not available Genus/species: Acanthamoeba culbertsoni
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
acanthaporin_dimer: AMGKCSVLKKVACAAAIAGA
VAACGGIDLPCVLAALKAAE
GCASCFCEDHCHGVCKDLHL
C
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 43 |
| 1H chemical shifts | 220 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | acanthaporin_dimer, chain 1 | 1 |
| 2 | acanthaporin_dimer, chain 2 | 1 |
Entities:
Entity 1, acanthaporin_dimer, chain 1 61 residues - 6001.235 Da.
| 1 | ALA | MET | GLY | LYS | CYS | SER | VAL | LEU | LYS | LYS | ||||
| 2 | VAL | ALA | CYS | ALA | ALA | ALA | ILE | ALA | GLY | ALA | ||||
| 3 | VAL | ALA | ALA | CYS | GLY | GLY | ILE | ASP | LEU | PRO | ||||
| 4 | CYS | VAL | LEU | ALA | ALA | LEU | LYS | ALA | ALA | GLU | ||||
| 5 | GLY | CYS | ALA | SER | CYS | PHE | CYS | GLU | ASP | HIS | ||||
| 6 | CYS | HIS | GLY | VAL | CYS | LYS | ASP | LEU | HIS | LEU | ||||
| 7 | CYS |
Samples:
sample_1: acanthaporin_dimer, [U-100% 15N], 0.7 mM; TRIS, [U-2H], 25 mM; sodium azide 0.001%; H2O 93%; D2O 7%
sample_2: acanthaporin_dimer, [U-100% 15N], 0.7 mM; TRIS, [U-2H], 25 mM; sodium azide 0.001%; H2O 93%; D2O 7%
sample_conditions_1: ionic strength: 0.025 M; pH: 8.0; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 750 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts