BMRB Entry 7349

Click here to enlarge.

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
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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.; De Jong, 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, 57 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: MNVTKLNDRIEAKKKELIYL VEKYGFTHHKVISFSQELDR LLNLLIELKTKKKRYSL

Data sets:
Data typeCount
13C chemical shifts279
15N chemical shifts59
1H chemical shifts443

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1CONSERVED_DOMAIN_PROTEIN1

Entities:

Entity 1, CONSERVED_DOMAIN_PROTEIN 57 residues - Formula weight is not available

1   METASNVALTHRLYSLEUASNASPARGILE
2   GLUALALYSLYSLYSGLULEUILETYRLEU
3   VALGLULYSTYRGLYPHETHRHISHISLYS
4   VALILESERPHESERGLNGLULEUASPARG
5   LEULEUASNLEULEUILEGLULEULYSTHR
6   LYSLYSLYSARGTYRSERLEU

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:

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
CCCONHsampleisotropicsample_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 GAF00519
GB AAP28843 AAT34304 AAT57102 AAT62951 AAU15604
REF NP_847357 WP_001103330 WP_001103331 WP_009879807 WP_011199052

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks