BMRB Entry 7349
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR7349
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Title: NMR SOLUTION STRUCTURE OF A PROTEIN ASPARTIC ACID PHOSPHATE PHOSPHATASE FROM BACILLUS ANTHRACIS PubMed: 17001075
Deposition date: 2006-12-01 Original release date: 2008-08-14
Authors: Grenha, R.; Rzechorzek, N.; Brannigan, J.; Ab, E.; Folkers, G.; De Jong, R.; Diercks, T.; Wilkinson, A.; Kaptein, R.; Wilson, K.
Citation: Grenha, Rosa; Rzechorzek, Neil; Brannigan, James; de Jong, Rob; AB, Eiso; Diercks, Tammo; Truffault, Vincent; Ladds, Joanne; Fogg, Mark; Bongiorni, Christina; Perego, Marta; Kaptein, Robert; Wilson, Keith; Folkers, Gert; Wilkinson, Anthony. "Structural characterization of Spo0E-like protein-aspartic acid phosphatases that regulate sporulation in bacilli." J. Biol. Chem. 281, 37993-38003 (2006).
Assembly members:
CONSERVED_DOMAIN_PROTEIN, polymer, 57 residues, Formula weight is not available
Natural source: Common Name: BACILLUS ANTHRACIS Taxonomy ID: 1392 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus anthracis
Experimental source: Production method: recombinant technology Host organism: ESCHERICHIA COLI
Entity Sequences (FASTA):
CONSERVED_DOMAIN_PROTEIN: MNVTKLNDRIEAKKKELIYL
VEKYGFTHHKVISFSQELDR
LLNLLIELKTKKKRYSL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 279 |
| 15N chemical shifts | 59 |
| 1H chemical shifts | 443 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CONSERVED_DOMAIN_PROTEIN | 1 |
Entities:
Entity 1, CONSERVED_DOMAIN_PROTEIN 57 residues - Formula weight is not available
| 1 | MET | ASN | VAL | THR | LYS | LEU | ASN | ASP | ARG | ILE | ||||
| 2 | GLU | ALA | LYS | LYS | LYS | GLU | LEU | ILE | TYR | LEU | ||||
| 3 | VAL | GLU | LYS | TYR | GLY | PHE | THR | HIS | HIS | LYS | ||||
| 4 | VAL | ILE | SER | PHE | SER | GLN | GLU | LEU | ASP | ARG | ||||
| 5 | LEU | LEU | ASN | LEU | LEU | ILE | GLU | LEU | LYS | THR | ||||
| 6 | LYS | LYS | LYS | ARG | TYR | SER | LEU |
Samples:
sample: CONSERVED_DOMAIN_PROTEIN mM; D2O 10%; H2O 90%
sample_conditions_1: ionic strength: 150 mM; pH: 6.0; pressure: 1.0 ATM; temperature: 278.0 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| HNCO | sample | isotropic | sample_conditions_1 |
| HNCACO | sample | isotropic | sample_conditions_1 |
| HNCACB | sample | isotropic | sample_conditions_1 |
| CBCACONH | sample | isotropic | sample_conditions_1 |
| HNCA | sample | isotropic | sample_conditions_1 |
| HBHACONH | sample | isotropic | sample_conditions_1 |
| HNCAHA | sample | isotropic | sample_conditions_1 |
| CCH-COSY | sample | isotropic | sample_conditions_1 |
| HCCH-TOCSY | sample | isotropic | sample_conditions_1 |
| CCCONH | sample | isotropic | sample_conditions_1 |
| HNH-NOESY | sample | isotropic | sample_conditions_1 |
| HCH-NOESY | sample | isotropic | sample_conditions_1 |
| CNH-NOESY | sample | isotropic | sample_conditions_1 |
| HH-NOESY | sample | isotropic | sample_conditions_1 |
Software:
CNS, BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,SIMONSON,WARREN - refinement
SPARKY - structure solution
CYANA2.1 - structure solution
NMR spectrometers:
- BRUKER OTHER 700 MHz
Related Database Links:
| PDB | |
| DBJ | GAF00519 |
| GB | AAP28843 AAT34304 AAT57102 AAT62951 AAU15604 |
| REF | NP_847357 WP_001103330 WP_001103331 WP_009879807 WP_011199052 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts