BMRB Entry 16926
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16926
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Title: NMR Structure of Escherichia coli BamE, a Lipoprotein Component of the beta-Barrel Assembly Machinery Complex PubMed: 21207987
Deposition date: 2010-05-13 Original release date: 2011-01-06
Authors: Kim, Kelly; Okon, Mark; Escobar, Eric; Kang, Hyun-Seo; McIntosh, Lawrence; Paetzel, Mark
Citation: Kim, Kelly; Kang, Hyun-Seo; Okon, Mark; Escobar-Cabrera, Eric; McIntosh, Lawrence; Paetzel, Mark. "Structural Characterization of Escherichia coli BamE, a Lipoprotein Component of the -Barrel Assembly Machinery Complex." Biochemistry 50, 1081-1090 (2011).
Assembly members:
E._coli_lipoprotein, polymer, 97 residues, 8072.073 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a
Entity Sequences (FASTA):
E._coli_lipoprotein: GSHMSTLERVVYRPDINQGN
YLTANDVSKIRVGMTQQQVA
YALGTPLMSDPFGTNTWFYV
FRQQPGHEGVTQQTLTLTFN
SSGVLTNIDNKPALSGN
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 236 |
| 15N chemical shifts | 92 |
| 1H chemical shifts | 544 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | E. coli lipoprotein | 1 |
Entities:
Entity 1, E. coli lipoprotein 97 residues - 8072.073 Da.
First four residues (GSHM) are remainder of thrombin-cleaved 6-His tag. This structure represents the full length mature BamE protein without its lipidated cysteine (Cys20).
| 1 | GLY | SER | HIS | MET | SER | THR | LEU | GLU | ARG | VAL | ||||
| 2 | VAL | TYR | ARG | PRO | ASP | ILE | ASN | GLN | GLY | ASN | ||||
| 3 | TYR | LEU | THR | ALA | ASN | ASP | VAL | SER | LYS | ILE | ||||
| 4 | ARG | VAL | GLY | MET | THR | GLN | GLN | GLN | VAL | ALA | ||||
| 5 | TYR | ALA | LEU | GLY | THR | PRO | LEU | MET | SER | ASP | ||||
| 6 | PRO | PHE | GLY | THR | ASN | THR | TRP | PHE | TYR | VAL | ||||
| 7 | PHE | ARG | GLN | GLN | PRO | GLY | HIS | GLU | GLY | VAL | ||||
| 8 | THR | GLN | GLN | THR | LEU | THR | LEU | THR | PHE | ASN | ||||
| 9 | SER | SER | GLY | VAL | LEU | THR | ASN | ILE | ASP | ASN | ||||
| 10 | LYS | PRO | ALA | LEU | SER | GLY | ASN |
Samples:
sample_1: E. coli protein, [U-100% 13C; U-100% 15N], 0.5 mM; D2O 15%; H2O 85%; Na2HPO4/NaH2PO4 20 mM
Phosphate_Buffer: ionic strength: 0.02 M; pH: 6.6; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | Phosphate_Buffer |
| 3D CBCA(CO)NH | sample_1 | isotropic | Phosphate_Buffer |
| 3D 1H-15N NOESY | sample_1 | isotropic | Phosphate_Buffer |
| 3D HNCO | sample_1 | isotropic | Phosphate_Buffer |
| 3D HNCACB | sample_1 | isotropic | Phosphate_Buffer |
| 3D HN(CO)CA | sample_1 | isotropic | Phosphate_Buffer |
| 3D 1H-13C NOESY | sample_1 | isotropic | Phosphate_Buffer |
| 2D 1H-1H COSY | sample_1 | isotropic | Phosphate_Buffer |
Software:
SPARKY v3.113, Goddard - chemical shift assignment, peak picking
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Varian Unity 500 MHz
Related Database Links:
| BMRB | 16424 |
| PDB | |
| DBJ | BAA16502 BAB36902 BAG78424 BAI26856 BAI31942 |
| EMBL | CAH23267 CAP77059 CAQ32986 CAQ88015 CAQ99565 |
| GB | AAA79787 AAC75666 AAG57727 AAN44171 AAN81589 |
| REF | NP_311506 NP_417107 NP_708464 WP_001203434 WP_001203436 |
| SP | P0A937 P0A938 P0A939 Q32CX2 |
| AlphaFold | P0A937 P0A938 P0A939 Q32CX2 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts