BMRB Entry 15634
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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/BMR15634
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Title: Solution Structure of Putative Ferrous Iron Transport Protein C (FeoC) of Klebsiella pneumoniae PubMed: 22580893
Deposition date: 2008-01-23 Original release date: 2012-07-19
Authors: Hung, Kuo-Wei; Lin, Yi-Chao; Chen, Jia-Hui; Huang, Tai-Huang
Citation: Hung, Kuo-Wei; Juan, Tzu-hsuan; Hsu, Yen-lan; Huang, Tai-Huang. "NMR structure note: the ferrous iron transport protein C (FeoC) from Klebsiella pneumoniae" J. Biomol. NMR 53, 161-165 (2012).
Assembly members:
FeoC, polymer, 87 residues, Formula weight is not available
Natural source: Common Name: Klebsiella pneumoniae Taxonomy ID: 573 Superkingdom: Bacteria Kingdom: not available Genus/species: Klebsiella pneumoniae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
FeoC: MASLMEVRDMLALQGRMEAK
QLSARLQTPQPLIDAMLERM
EAMGKVVRISETSEGCLSGS
CKSCPEGKAACRQEWWALRL
EHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 322 |
| 15N chemical shifts | 77 |
| 1H chemical shifts | 518 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | FeoC_monomer | 1 |
Entities:
Entity 1, FeoC_monomer 87 residues - Formula weight is not available
| 1 | MET | ALA | SER | LEU | MET | GLU | VAL | ARG | ASP | MET | ||||
| 2 | LEU | ALA | LEU | GLN | GLY | ARG | MET | GLU | ALA | LYS | ||||
| 3 | GLN | LEU | SER | ALA | ARG | LEU | GLN | THR | PRO | GLN | ||||
| 4 | PRO | LEU | ILE | ASP | ALA | MET | LEU | GLU | ARG | MET | ||||
| 5 | GLU | ALA | MET | GLY | LYS | VAL | VAL | ARG | ILE | SER | ||||
| 6 | GLU | THR | SER | GLU | GLY | CYS | LEU | SER | GLY | SER | ||||
| 7 | CYS | LYS | SER | CYS | PRO | GLU | GLY | LYS | ALA | ALA | ||||
| 8 | CYS | ARG | GLN | GLU | TRP | TRP | ALA | LEU | ARG | LEU | ||||
| 9 | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: FeoC, [U-13C; U-15N], 0.7 mM; TRIS 20 mM; NaCl 50 mM; DTT 10 mM
sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 288 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS v1.2, Linge, O, . - refinement
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 600 MHz
Related Database Links:
Download simulated HSQC data in one of the following formats:
CSV: Backbone
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SPARKY: Backbone
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