BMRB Entry 15834
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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/BMR15834
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Title: Solution NMR structure of FeoA protein from Chlorobium tepidum. Northeast Structural Genomics Consortium target CtR121
Deposition date: 2008-06-27 Original release date: 2008-07-24
Authors: Eletsky, Alexander; Sathyamoorthy, Bharathwaj; Mills, Jeffrey; Zeri, Ana; Zhao, Li; Hamilton, Keith; Foote, Erica; Xiao, Rong; Nair, Rajesh; Baran, Michael; Swapna, G.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Szyperski, Thomas
Citation: Eletsky, Alexander; Sathyamoorthy, Bharathwaj; Mills, Jeffrey; Zeri, Ana; Zhao, Li; Hamilton, Keith; Foote, Erica; Xiao, Rong; Nair, Rajesh; Baran, Michael; Swapna, G.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR structure of FeoA protein from Chlorobium tepidum. Northeast Structural Genomics Consortium target CtR121" Proteins: Struct. Funct. Genet. ., .-..
Assembly members:
FeoA_protein, polymer, 105 residues, 11872.900 Da.
Natural source: Common Name: Chlorobium tepidum Taxonomy ID: 1097 Superkingdom: Bacteria Kingdom: not available Genus/species: Chlorobium tepidum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
FeoA_protein: MKLSELKAGDRAEVTSVAAE
PAVRRRLMDLGLVRGAKLKV
LRFAPLGDPIEVNCNGMLLT
MRRNEAEGITVHILAGDEGH
PHGWPGFRRRHRFGKRALEH
HHHHH
- assigned_chemical_shifts
- coupling_constants
| Data type | Count |
| 13C chemical shifts | 416 |
| 15N chemical shifts | 104 |
| 1H chemical shifts | 682 |
| coupling constants | 68 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | FeoA_protein | 1 |
Entities:
Entity 1, FeoA_protein 105 residues - 11872.900 Da.
8-residue C-terminal tag LEHHHHHH
| 1 | MET | LYS | LEU | SER | GLU | LEU | LYS | ALA | GLY | ASP | ||||
| 2 | ARG | ALA | GLU | VAL | THR | SER | VAL | ALA | ALA | GLU | ||||
| 3 | PRO | ALA | VAL | ARG | ARG | ARG | LEU | MET | ASP | LEU | ||||
| 4 | GLY | LEU | VAL | ARG | GLY | ALA | LYS | LEU | LYS | VAL | ||||
| 5 | LEU | ARG | PHE | ALA | PRO | LEU | GLY | ASP | PRO | ILE | ||||
| 6 | GLU | VAL | ASN | CYS | ASN | GLY | MET | LEU | LEU | THR | ||||
| 7 | MET | ARG | ARG | ASN | GLU | ALA | GLU | GLY | ILE | THR | ||||
| 8 | VAL | HIS | ILE | LEU | ALA | GLY | ASP | GLU | GLY | HIS | ||||
| 9 | PRO | HIS | GLY | TRP | PRO | GLY | PHE | ARG | ARG | ARG | ||||
| 10 | HIS | ARG | PHE | GLY | LYS | ARG | ALA | LEU | GLU | HIS | ||||
| 11 | HIS | HIS | HIS | HIS | HIS |
Samples:
NC: FeoA protein, [U-100% 13C; U-100% 15N], 1.26 mM; sodium azide 0.02%; DTT 100 mM; calcium chloride 5 mM; sodium chloride 100 mM; MES 20 mM; DSS 50 uM; H2O 90%; D2O, [U-100% 2H], 10%
NC5: FeoA protein, [U-5% 13C; U-100% 15N], 1.26 mM; sodium azide 0.02%; DTT 100 mM; calcium chloride 5 mM; sodium chloride 100 mM; MES 20 mM; DSS 50 uM; H2O 90%; D2O, [U-100% 2H], 10%
sample_conditions_1: ionic strength: 115 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | NC | isotropic | sample_conditions_1 |
| 3D HNCO | NC | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | NC | isotropic | sample_conditions_1 |
| 3D HNCACB | NC | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | NC | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | NC | isotropic | sample_conditions_1 |
| (4,3)D GFT HCCH-COSY ali | NC | isotropic | sample_conditions_1 |
| (4,3)D GFT L-HCCH-COSY aro | NC | isotropic | sample_conditions_1 |
| 3D HNHA | NC | isotropic | sample_conditions_1 |
| 3D HNCO (hbond) | NC | isotropic | sample_conditions_1 |
| 3D 1H-15N,13Cali,13Caro NOESY | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C CT-HSQC 28ms | NC5 | isotropic | sample_conditions_1 |
Software:
VNMRJ v2.1B, Varian - collection
PROSA v6.0.2, Guntert - processing
CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
XEASY v1.3.13, Bartels et al. - data analysis
AutoAssign v1.15.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
CSI v2.0, Wishat and Sykes - data analysis
TALOS v2003.027.13.05, Cornilescu, Delaglio and Bax - data analysis
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - structure solution
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
PSVS v1.3, Bhattacharya and Montelione - validation
NMR spectrometers:
- Varian INOVA 750 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts