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
MolProbity Validation Chart

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Title:
NMR SOLUTION STRUCTURE OF A PROTEIN ASPARTIC ACID PHOSPHATE PHOSPHATASE FROM BACILLUS ANTHRACIS
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:

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).
PubMed: 17001075

Assembly members:

Assembly members:
CONSERVED_DOMAIN_PROTEIN, polymer, 54 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: BACILLUS ANTHRACIS   Taxonomy ID: 1392   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus anthracis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: ESCHERICHIA COLI   Vector: PET28A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CONSERVED_DOMAIN_PROTEIN: MEMGQLKNKIENKKKELIQL VARHGLDHDKVLLFSRDLDK LINKFMNVKDKVHK

Data sets:
Data typeCount
13C chemical shifts257
15N chemical shifts59
1H chemical shifts433

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1CONSERVED_DOMAIN_PROTEIN1

Entities:

Entity 1, CONSERVED_DOMAIN_PROTEIN 54 residues - Formula weight is not available

1   METGLUMETGLYGLNLEULYSASNLYSILE
2   GLUASNLYSLYSLYSGLULEUILEGLNLEU
3   VALALAARGHISGLYLEUASPHISASPLYS
4   VALLEULEUPHESERARGASPLEUASPLYS
5   LEUILEASNLYSPHEMETASNVALLYSASP
6   LYSVALHISLYS

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:

NameSampleSample stateSample conditions
HNCOsampleisotropicsample_conditions_1
HNCACOsampleisotropicsample_conditions_1
HNCACBsampleisotropicsample_conditions_1
CBCACONHsampleisotropicsample_conditions_1
HNCAsampleisotropicsample_conditions_1
HBHACONHsampleisotropicsample_conditions_1
HNCAHAsampleisotropicsample_conditions_1
CCH-COSYsampleisotropicsample_conditions_1
HCCH-TOCSYsampleisotropicsample_conditions_1
HNH-NOESYsampleisotropicsample_conditions_1
HCH-NOESYsampleisotropicsample_conditions_1
CNH- NOESYsampleisotropicsample_conditions_1
HH-NOESYsampleisotropicsample_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 HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks