BMRB Entry 15167
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15167
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Title: NMR Structure of E. Coli YehR Protein. Northeast Structural Genomics Target ER538.
Deposition date: 2007-03-08 Original release date: 2007-04-11
Authors: Ding, Keyang; Ramelot, Theresa; Cort, John; Chen, Chen; Jiang, Mei; Cunningham, Kellie; Ma, Li-Chung; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, Gurla; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Kennedy, Michael
Citation: Ding, Keyang; Ramelot, Theresa; Cort, John; Jiang, Mei; Xiao, Rong; Swapna, Gurla; Montelione, Gaetano; Kennedy, Michael. "NMR Structure of E. Coli YehR Protein" . ., .-..
Assembly members:
YehR, polymer, 139 residues, 15389.607 Da.
Natural source: Common Name: not available Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
YehR: MGDKEESKKFSANLNGTEIA
ITYVYKGDKVLKQSSETKIQ
FASIGATTKEDAAKTLEPLS
AKYKNIAGVEEKLTYTDTYA
QENVTIDMEKVDFKALQGIS
GINVSAEDAKKGITMAQMEL
VMKAAGFKEVKLEHHHHHH
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 611 |
| 15N chemical shifts | 147 |
| 1H chemical shifts | 974 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | YehR | 1 |
Entities:
Entity 1, YehR 139 residues - 15389.607 Da.
The C-terminal his-tag LEHHHHHH was included in calculation. The N-terminal 22 residues MKAFNKLFSLVVASVLVFSLAG was not included in the cloning.
| 1 | MET | GLY | ASP | LYS | GLU | GLU | SER | LYS | LYS | PHE | ||||
| 2 | SER | ALA | ASN | LEU | ASN | GLY | THR | GLU | ILE | ALA | ||||
| 3 | ILE | THR | TYR | VAL | TYR | LYS | GLY | ASP | LYS | VAL | ||||
| 4 | LEU | LYS | GLN | SER | SER | GLU | THR | LYS | ILE | GLN | ||||
| 5 | PHE | ALA | SER | ILE | GLY | ALA | THR | THR | LYS | GLU | ||||
| 6 | ASP | ALA | ALA | LYS | THR | LEU | GLU | PRO | LEU | SER | ||||
| 7 | ALA | LYS | TYR | LYS | ASN | ILE | ALA | GLY | VAL | GLU | ||||
| 8 | GLU | LYS | LEU | THR | TYR | THR | ASP | THR | TYR | ALA | ||||
| 9 | GLN | GLU | ASN | VAL | THR | ILE | ASP | MET | GLU | LYS | ||||
| 10 | VAL | ASP | PHE | LYS | ALA | LEU | GLN | GLY | ILE | SER | ||||
| 11 | GLY | ILE | ASN | VAL | SER | ALA | GLU | ASP | ALA | LYS | ||||
| 12 | LYS | GLY | ILE | THR | MET | ALA | GLN | MET | GLU | LEU | ||||
| 13 | VAL | MET | LYS | ALA | ALA | GLY | PHE | LYS | GLU | VAL | ||||
| 14 | LYS | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: protein, [U-100% 13C; U-100% 15N], 1 ± 0.2 mM; NH4OAc 20 ± 1 mM; NaCl 100 ± 5 mM; DTT 10 ± 1 mM; CaCl2 5 ± 1 mM; NaN3 0.02 ± 0.001 %; H2O 95 ± 0.001 %; D2O 5 ± 0.001 %
sample_2: protein, [U-5% 13C; U-100% 15N], 1 ± 0.2 mM; NH4OAc 20 ± 1 mM; NaCl 100 ± 5 mM; DTT 10 ± 1 mM; CaCl2 5 ± 1 mM; NaN3 0.02 ± 0.001 %; H2O 95 ± 0.001 %; D2O 5 ± 0.001 %
sample_3: protein, [U-100% 13C; U-100% 15N], 1 ± 0.2 mM; NH4OAc 20 ± 1 mM; NaCl 100 ± 5 mM; DTT 10 ± 1 mM; CaCl2 5 ± 1 mM; NaN3 0.02 ± 0.001 %; D2O 100 ± 0.001 %
sample_conditions_1: ionic strength: 100 mM; pH: 5.5; pressure: 1 atm; temperature: 283 K
sample_conditions_2: ionic strength: 100 mM; pH: 5.5; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_2 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_2 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_2 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_2 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_2 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_2 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_2 |
| 3D HNHA | sample_2 | isotropic | sample_conditions_2 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_2 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_2 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_2 |
| 2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_2 |
| 2D 1H-13C (Arom) HSQC | sample_1 | isotropic | sample_conditions_2 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N (NH2) HSQC | sample_1 | isotropic | sample_conditions_2 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C (Aliph) NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C (Arom) NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C (Aliph) NOESY | sample_3 | isotropic | sample_conditions_2 |
| 4D 1H-13C NOESY | sample_3 | isotropic | sample_conditions_2 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
X-PLOR NIH v2.15.0, Schwieters, Kuszewski, Tjandra and Clore - structure solution
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
SPARKY v3.1, Goddard - peak picking
NMRPipe vlinux9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
AutoStruct v2.1.1, Huang, Swapana, Rajan, Ke, Xia, Shukla, Inouye and Montelione - data analysis
NMR spectrometers:
- Varian INOVA 750 MHz
- Varian INOVA 600 MHz
- Varian INOVA 500 MHz
Related Database Links:
| PDB | |
| DBJ | BAB19552 BAB36357 BAE76599 BAG66588 BAG77915 |
| EMBL | CAP76626 CAQ32527 CAQ99044 CAR03550 CAR08661 |
| GB | AAA60486 AAC75184 AAG57191 AAN43719 AAN81109 |
| PRF | 2014253T |
| REF | NP_310961 NP_416627 NP_708012 WP_000293099 WP_000397950 |
| SP | P33354 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts