BMRB Entry 16995
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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/BMR16995
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Title: Solution structure of a bolA protein (ECH_0303) from Ehrlichia chaffeensis, the causative agent of human monocytic ehrlichiosis. Seattle Structural Genomics Center for Infectious Disease (SSGCID) target EhchA.10365.a
Deposition date: 2010-06-10 Original release date: 2010-07-01
Authors: Garry, Buchko
Citation: Buchko, Garry; Hewitt, Stephen; Napuli, Alberto; Van Voorhis, Wesley; Myler, Peter. "Structural characterization of a BolA protein (ECH_0303) from Ehrlichia chaffeensis, the agent responsible for human monocytotropic ehrlichiosis." Not known ., .-..
Assembly members:
ECH_0303, polymer, 76 residues, Formula weight is not available
Natural source: Common Name: Ehrlichia chaffeensis Taxonomy ID: 945 Superkingdom: Bacteria Kingdom: not available Genus/species: Ehrlichia chaffeensis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
ECH_0303: PGSMTVTQSQLELLIRNAFP
EAEITVTSLVGDNNHYSIKV
ISSQFQGKSKLEQHRMIYKV
LDGLNIHAIQIQTGCK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 272 |
| 15N chemical shifts | 66 |
| 1H chemical shifts | 447 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ECH_0303 | 1 |
Entities:
Entity 1, ECH_0303 76 residues - Formula weight is not available
The first three residues, PGS-, are left over after removal of the N-terminal tag. The first native residue is M4.
| 1 | PRO | GLY | SER | MET | THR | VAL | THR | GLN | SER | GLN | ||||
| 2 | LEU | GLU | LEU | LEU | ILE | ARG | ASN | ALA | PHE | PRO | ||||
| 3 | GLU | ALA | GLU | ILE | THR | VAL | THR | SER | LEU | VAL | ||||
| 4 | GLY | ASP | ASN | ASN | HIS | TYR | SER | ILE | LYS | VAL | ||||
| 5 | ILE | SER | SER | GLN | PHE | GLN | GLY | LYS | SER | LYS | ||||
| 6 | LEU | GLU | GLN | HIS | ARG | MET | ILE | TYR | LYS | VAL | ||||
| 7 | LEU | ASP | GLY | LEU | ASN | ILE | HIS | ALA | ILE | GLN | ||||
| 8 | ILE | GLN | THR | GLY | CYS | LYS |
Samples:
sample_1: ECH_0303, [U-99% 13C; U-99% 15N], 1.5 ± 0.3 mM; sodium chloride 100 ± 2 mM; TRIS 20 ± 1 mM; DTT 1 ± 0.2 mM; H2O 90%; D2O 10%
sample_2: ECH_0303, [U-99% 13C; U-99% 15N], 1.0 ± 0.1 mM; sodium chloride 100 ± 2 mM; TRIS 20 ± 1 mM; DTT 1 ± 0.2 mM; D2O 100%
sample_conditions_1: ionic strength: 0.12 M; pH: 7.1; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(COCA)CB | 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 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
FELIX v2007, Accelrys Software Inc. - processing
SPARKY v3.115, Goddard - data analysis
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Varian INOVA 600 MHz
- 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