BMRB Entry 25768
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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/BMR25768
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Title: Solution NMR structure of Outer Membrane Protein G from Pseudomonas aeruginosa PubMed: 26655471
Deposition date: 2015-08-26 Original release date: 2015-12-28
Authors: Kucharska, Iga; Seelheim, Patrick; Edrington, Thomas; Liang, Binyong; Tamm, Lukas
Citation: Kucharska, Iga; Seelheim, Patrick; Edrington, Thomas; Liang, Binyong; Tamm, Lukas. "OprG Harnesses the Dynamics of its Extracellular Loops to Transport Small Amino Acids across the Outer Membrane of Pseudomonas aeruginosa" Structure 23, 2234-2245 (2015).
Assembly members:
entity, polymer, 215 residues, 22885.924 Da.
Natural source: Common Name: g-proteobacteria Taxonomy ID: 287 Superkingdom: Bacteria Kingdom: not available Genus/species: Pseudomonas aeruginosa
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: MHKAGDFIIRGGFATVDPDD
SSSDIKLDGAKQRGTKATVD
SDTQLGLTFTYMFADKWGVE
LVAATPFNHQVDVKGLGPGL
DGKLADIKQLPPTLLLQYYP
MGGTNSAFQPYGGLGVNYTT
FFDEDLASNRKAQGFSSMKL
QDSWGLAGELGFDYMLNEHA
LFNMAVWYMDIDTKASINGP
SALGVNKTKVDVDVDPWVYM
IGFGYKFLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 558 |
| 15N chemical shifts | 181 |
| 1H chemical shifts | 181 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 215 residues - 22885.924 Da.
| 1 | MET | HIS | LYS | ALA | GLY | ASP | PHE | ILE | ILE | ARG | ||||
| 2 | GLY | GLY | PHE | ALA | THR | VAL | ASP | PRO | ASP | ASP | ||||
| 3 | SER | SER | SER | ASP | ILE | LYS | LEU | ASP | GLY | ALA | ||||
| 4 | LYS | GLN | ARG | GLY | THR | LYS | ALA | THR | VAL | ASP | ||||
| 5 | SER | ASP | THR | GLN | LEU | GLY | LEU | THR | PHE | THR | ||||
| 6 | TYR | MET | PHE | ALA | ASP | LYS | TRP | GLY | VAL | GLU | ||||
| 7 | LEU | VAL | ALA | ALA | THR | PRO | PHE | ASN | HIS | GLN | ||||
| 8 | VAL | ASP | VAL | LYS | GLY | LEU | GLY | PRO | GLY | LEU | ||||
| 9 | ASP | GLY | LYS | LEU | ALA | ASP | ILE | LYS | GLN | LEU | ||||
| 10 | PRO | PRO | THR | LEU | LEU | LEU | GLN | TYR | TYR | PRO | ||||
| 11 | MET | GLY | GLY | THR | ASN | SER | ALA | PHE | GLN | PRO | ||||
| 12 | TYR | GLY | GLY | LEU | GLY | VAL | ASN | TYR | THR | THR | ||||
| 13 | PHE | PHE | ASP | GLU | ASP | LEU | ALA | SER | ASN | ARG | ||||
| 14 | LYS | ALA | GLN | GLY | PHE | SER | SER | MET | LYS | LEU | ||||
| 15 | GLN | ASP | SER | TRP | GLY | LEU | ALA | GLY | GLU | LEU | ||||
| 16 | GLY | PHE | ASP | TYR | MET | LEU | ASN | GLU | HIS | ALA | ||||
| 17 | LEU | PHE | ASN | MET | ALA | VAL | TRP | TYR | MET | ASP | ||||
| 18 | ILE | ASP | THR | LYS | ALA | SER | ILE | ASN | GLY | PRO | ||||
| 19 | SER | ALA | LEU | GLY | VAL | ASN | LYS | THR | LYS | VAL | ||||
| 20 | ASP | VAL | ASP | VAL | ASP | PRO | TRP | VAL | TYR | MET | ||||
| 21 | ILE | GLY | PHE | GLY | TYR | LYS | PHE | LEU | GLU | HIS | ||||
| 22 | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: entity, [U-13C; U-15N; U-2H], 1 mM; sodium phosphate 25 mM; potassium chloride 50 mM; sodium azide 0.05%; 1,2-dihexanoyl-sn-glycero-3-phosphocholine 0.9%; D2O 10%; H2O 90%
sample_2: entity, [U-13C; U-15N; U-2H], 1 mM; sodium phosphate 25 mM; potassium chloride 50 mM; sodium azide 0.05%; 1,2-dihexanoyl-sn-glycero-3-phosphocholine 0.9%; D2O 100%
sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H 15N TROSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA(CO) | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H 15N TROSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 15N 1H 1H NOESY TROSY | sample_1 | isotropic | sample_conditions_1 |
| 4D 15N 1H 15N HSQC NOESY HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
TALOS vTalos+, Yang Shen, Frank Delaglio, Gabriel Cornilescu, and Ad Bax - Prediction of Protein Backbone Torsion Angles from NMR Chemical Shifts
SPARKY, T. D. Goddard and D. G. Kneller - NMR assignments
CNS v1.2, Brunger, A.T et al - structure solution
Bruker_TopSpin v2.1.6, Bruker - collection
NMRPipe, F. Delaglio, S. Grzesiek, G. W. Vuister, G. Zhu, J. Pfeifer and A. Bax - processing
NMR spectrometers:
- Bruker Bruker Avance III 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts