BMRB Entry 7350
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PDB ID: 2bzb
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:
Related Database Links:
| PDB | 2BZB |
| DBJ | BAL17403 GAE97096 |
| EMBL | CCW06493 |
| GB | AAP25588 AAT30765 AAT53854 AAT63164 AAU18752 |
| REF | NP_844102 WP_000291689 WP_000425177 WP_000515272 WP_000515273 |
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