BMRB Entry 7350
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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/BMR7350
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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.; Dejong, 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, 54 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: MEMGQLKNKIENKKKELIQL
VARHGLDHDKVLLFSRDLDK
LINKFMNVKDKVHK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 257 |
| 15N chemical shifts | 59 |
| 1H chemical shifts | 433 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CONSERVED_DOMAIN_PROTEIN | 1 |
Entities:
Entity 1, CONSERVED_DOMAIN_PROTEIN 54 residues - Formula weight is not available
| 1 | MET | GLU | MET | GLY | GLN | LEU | LYS | ASN | LYS | ILE | ||||
| 2 | GLU | ASN | LYS | LYS | LYS | GLU | LEU | ILE | GLN | LEU | ||||
| 3 | VAL | ALA | ARG | HIS | GLY | LEU | ASP | HIS | ASP | LYS | ||||
| 4 | VAL | LEU | LEU | PHE | SER | ARG | ASP | LEU | ASP | LYS | ||||
| 5 | LEU | ILE | ASN | LYS | PHE | MET | ASN | VAL | LYS | ASP | ||||
| 6 | LYS | VAL | HIS | LYS |
Samples:
sample: CONSERVED_DOMAIN_PROTEIN mM; D2O 10%; H2O 90%
sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1.0 ATM; temperature: 298.0 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 |
| 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 | BAL17403 GAE97096 |
| EMBL | CCW06493 |
| GB | AAP25588 AAT30765 AAT53854 AAT63164 AAU18752 |
| REF | NP_844102 WP_000291689 WP_000425177 WP_000515272 WP_000515273 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
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SPARKY: Backbone
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