BMRB Entry 19143
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19143
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Title: Solution structure of the Escherichia coli apo ferric enterobactin binding protein
Deposition date: 2013-04-05 Original release date: 2014-04-28
Authors: Chu, Byron; Otten, Renee; Krewulak, Karla; Mulder, Frans; Vogel, Hans
Citation: Chu, Byron; Otten, Renee; Krewulak, Karla; Mulder, Frans; Vogel, Hans. "The structure, binding properties, and dynamics of the 34 kDa bacterial siderophore binding protein FepB in solution." Not known ., .-..
Assembly members:
FepB, polymer, 315 residues, 31590.873 Da.
Natural source: Common Name: Eenterobacteria Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 860 |
| 15N chemical shifts | 268 |
| 1H chemical shifts | 268 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | FepB | 1 |
Entities:
Entity 1, FepB 315 residues - 31590.873 Da.
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | HIS | HIS | SER | GLY | HIS | ILE | ASP | ASP | ASP | ASP | ||||
| 3 | LYS | HIS | MET | ALA | ASP | TRP | PRO | ARG | GLN | ILE | ||||
| 4 | THR | ASP | SER | ARG | GLY | THR | HIS | THR | LEU | GLU | ||||
| 5 | SER | GLN | PRO | GLN | ARG | ILE | VAL | SER | THR | SER | ||||
| 6 | VAL | THR | LEU | THR | GLY | SER | LEU | LEU | ALA | ILE | ||||
| 7 | ASP | ALA | PRO | VAL | ILE | ALA | SER | GLY | ALA | THR | ||||
| 8 | THR | PRO | ASN | ASN | ARG | VAL | ALA | ASP | ASP | GLN | ||||
| 9 | GLY | PHE | LEU | ARG | GLN | TRP | SER | LYS | VAL | ALA | ||||
| 10 | LYS | GLU | ARG | LYS | LEU | GLN | ARG | LEU | TYR | ILE | ||||
| 11 | GLY | GLU | PRO | SER | ALA | GLU | ALA | VAL | ALA | ALA | ||||
| 12 | GLN | MET | PRO | ASP | LEU | ILE | LEU | ILE | SER | ALA | ||||
| 13 | THR | GLY | GLY | ASP | SER | ALA | LEU | ALA | LEU | TYR | ||||
| 14 | ASP | GLN | LEU | SER | THR | ILE | ALA | PRO | THR | LEU | ||||
| 15 | ILE | ILE | ASN | TYR | ASP | ASP | LYS | SER | TRP | GLN | ||||
| 16 | SER | LEU | LEU | THR | GLN | LEU | GLY | GLU | ILE | THR | ||||
| 17 | GLY | HIS | GLU | LYS | GLN | ALA | ALA | GLU | ARG | ILE | ||||
| 18 | ALA | GLN | PHE | ASP | LYS | GLN | LEU | ALA | ALA | ALA | ||||
| 19 | LYS | GLU | GLN | ILE | LYS | LEU | PRO | PRO | GLN | PRO | ||||
| 20 | VAL | THR | ALA | ILE | VAL | TYR | THR | ALA | ALA | ALA | ||||
| 21 | HIS | SER | ALA | ASN | LEU | TRP | THR | PRO | GLU | SER | ||||
| 22 | ALA | GLN | GLY | GLN | MET | LEU | GLU | GLN | LEU | GLY | ||||
| 23 | PHE | THR | LEU | ALA | LYS | LEU | PRO | ALA | GLY | LEU | ||||
| 24 | ASN | ALA | SER | GLN | SER | GLN | GLY | LYS | ARG | HIS | ||||
| 25 | ASP | ILE | ILE | GLN | LEU | GLY | GLY | GLU | ASN | LEU | ||||
| 26 | ALA | ALA | GLY | LEU | ASN | GLY | GLU | SER | LEU | PHE | ||||
| 27 | LEU | PHE | ALA | GLY | ASP | GLN | LYS | ASP | ALA | ASP | ||||
| 28 | ALA | ILE | TYR | ALA | ASN | PRO | LEU | LEU | ALA | HIS | ||||
| 29 | LEU | PRO | ALA | VAL | GLN | ASN | LYS | GLN | VAL | TYR | ||||
| 30 | ALA | LEU | GLY | THR | GLU | THR | PHE | ARG | LEU | ASP | ||||
| 31 | TYR | TYR | SER | ALA | MET | GLN | VAL | LEU | ASP | ARG | ||||
| 32 | LEU | LYS | ALA | LEU | PHE |
Samples:
sample_1: FepB mM; H2O 93%; D2O 7%
sample_2: FepB mM; H2O 93%; D2O 7%
sample_3: FepB mM; H2O 93%; D2O 7%
sample_conditions: ionic strength: 0 M; pH: 6.4; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions |
| 3D HNCACB | sample_3 | isotropic | sample_conditions |
| 3D CBCA(CO)NH | sample_3 | isotropic | sample_conditions |
| 3D HNCO | sample_3 | isotropic | sample_conditions |
| 3D HN(CO)CA | sample_3 | isotropic | sample_conditions |
| 3D HNCA | sample_3 | isotropic | sample_conditions |
| 2D 1H-15N HSQC | sample_3 | isotropic | sample_conditions |
Software:
No software information available
NMR spectrometers:
- Bruker Avance 700 MHz
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAB34054 BAE76347 BAG76183 BAI23996 BAI29464 |
| EMBL | CAP75093 CAQ31065 CAQ89998 CAQ97446 CAR01973 |
| GB | AAA83853 AAB40791 AAC73693 AAG54927 AAN42155 |
| REF | NP_308658 NP_415124 NP_706448 WP_000948435 WP_001234290 |
| SP | P0AEL6 P0AEL7 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts