BMRB Entry 27776
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27776
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Title: ssNMR assignment of membrane embedded Rhomboid protease GlpG PubMed: 31603315
Deposition date: 2019-02-05 Original release date: 2020-02-28
Authors: Shi, Chaowei; Chevelkov, Veniamin; Bohg, Claudia; Lange, Sascha; Lange, Adam
Citation: Shi, Chaowei; Oster, Carl; Bohg, Claudia; Li, Longmei; Lange, Sascha; Chevelkov, Veniamin; Lange, Adam. "Structure and Dynamics of the Rhomboid Protease GlpG in Liposomes Studied by Solid-State NMR" J. Am. Chem. Soc. 141, 17314-17321 (2019).
Assembly members:
GlpG, polymer, 211 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15b
Entity Sequences (FASTA):
GlpG: MGSSHHHHHHSSGLVPRGSH
MAALRERAGPVTWVMMIACV
VVFIAMQILGDQEVMLWLAW
PFDPTLKFEFWRYFTHALMH
FSLMHILFNLLWWWYLGGAV
EKRLGSGKLIVITLISALLS
GYVQQKFSGPWFGGLSGVVY
ALMGYVWLRGERDPQSGIYL
QRGLIIFALIWIVAGWFDLF
GMSMANGAHIAGLAVGLAMA
FVDSLNARKRK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 279 |
| 15N chemical shifts | 90 |
| 1H chemical shifts | 90 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | GlpG | 1 |
Entities:
Entity 1, GlpG 211 residues - Formula weight is not available
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | ||||
| 3 | MET | ALA | ALA | LEU | ARG | GLU | ARG | ALA | GLY | PRO | ||||
| 4 | VAL | THR | TRP | VAL | MET | MET | ILE | ALA | CYS | VAL | ||||
| 5 | VAL | VAL | PHE | ILE | ALA | MET | GLN | ILE | LEU | GLY | ||||
| 6 | ASP | GLN | GLU | VAL | MET | LEU | TRP | LEU | ALA | TRP | ||||
| 7 | PRO | PHE | ASP | PRO | THR | LEU | LYS | PHE | GLU | PHE | ||||
| 8 | TRP | ARG | TYR | PHE | THR | HIS | ALA | LEU | MET | HIS | ||||
| 9 | PHE | SER | LEU | MET | HIS | ILE | LEU | PHE | ASN | LEU | ||||
| 10 | LEU | TRP | TRP | TRP | TYR | LEU | GLY | GLY | ALA | VAL | ||||
| 11 | GLU | LYS | ARG | LEU | GLY | SER | GLY | LYS | LEU | ILE | ||||
| 12 | VAL | ILE | THR | LEU | ILE | SER | ALA | LEU | LEU | SER | ||||
| 13 | GLY | TYR | VAL | GLN | GLN | LYS | PHE | SER | GLY | PRO | ||||
| 14 | TRP | PHE | GLY | GLY | LEU | SER | GLY | VAL | VAL | TYR | ||||
| 15 | ALA | LEU | MET | GLY | TYR | VAL | TRP | LEU | ARG | GLY | ||||
| 16 | GLU | ARG | ASP | PRO | GLN | SER | GLY | ILE | TYR | LEU | ||||
| 17 | GLN | ARG | GLY | LEU | ILE | ILE | PHE | ALA | LEU | ILE | ||||
| 18 | TRP | ILE | VAL | ALA | GLY | TRP | PHE | ASP | LEU | PHE | ||||
| 19 | GLY | MET | SER | MET | ALA | ASN | GLY | ALA | HIS | ILE | ||||
| 20 | ALA | GLY | LEU | ALA | VAL | GLY | LEU | ALA | MET | ALA | ||||
| 21 | PHE | VAL | ASP | SER | LEU | ASN | ALA | ARG | LYS | ARG | ||||
| 22 | LYS |
Samples:
sample_1: GlpG, [U-13C; U-15N; U-2H], 35 % w/w; E.coli total lipid extract 35 % w/w; TRIS 20 mM; sodium chloride 100 mM; H2O 30 % w/w; beta-mercaptoethanol 1 mM
sample_conditions_1: ionic strength: 0.12 M; pH: 8; pressure: 1 atm; temperature: 283 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D (H)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CaNH | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CoNH | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)Ca(Co)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CaCo(N)H | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)Cb(Ca)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CbCa(N)H | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)Co(Ca)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CoCa(N)H | sample_1 | isotropic | sample_conditions_1 |
| 3D H(N)(Co)(Ca)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)N(Co)(Ca)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment, data analysis
TOPSPIN, Bruker Biospin - collection, processing
NMR spectrometers:
- Bruker Avance HD 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts