BMRB Entry 5769

Title:
Solution structure of apo-CopAS46V from Bacillus subtilis
Deposition date:
2003-04-11
Original release date:
2003-09-08
Authors:
Banci, L.; Bertini, I.; Ciofi-Baffoni, S.; Gonnelli, L.; Su, X.
Citation:

Citation: Banci, L.; Bertini, I.; Ciofi-Baffoni, S.; Gonnelli, L.; Su, X.. "A Core Mutation Affecting the Folding Properties of a Soluble Domain of the ATPase Protein CopA from Bacillus subtilis "  J. Mol. Biol. 331, 473-484 (2003).
PubMed: 12888353

Assembly members:

Assembly members:
CPx-type ATPase CopA, polymer, 76 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Bacillus subtilis   Taxonomy ID: 1423   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Bacillus subtilis

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Data sets:
Data typeCount
1H chemical shifts463
15N chemical shifts77

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CopA1

Entities:

Entity 1, CopA 76 residues - Formula weight is not available

1   METLEUSERGLUGLNLYSGLUILEALAMET
2   GLNVALSERGLYMETTHRCYSALAALACYS
3   ALAALAARGILEGLULYSGLYLEULYSARG
4   METPROGLYVALTHRASPALAASNVALASN
5   LEUALATHRGLUTHRVALASNVALILETYR
6   ASPPROALAGLUTHRGLYTHRALAALAILE
7   GLNGLULYSILEGLULYSLEUGLYTYRHIS
8   VALVALILEGLUGLYARG

Samples:

sample_1: CPx-type ATPase CopA, [U-15N], 1.2 mM; phosphate 20 mM; DTT 2 mM; H2O 90%; D2O 10%

sample_cond_1: pH: 7.0; temperature: 298 K; ionic strength: 20 mM; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
2D NOESYnot availablenot availablenot available
2D TOCSYnot availablenot availablenot available
3D 15N-separated NOESYnot availablenot availablenot available
HNHAnot availablenot availablenot available
HNHBnot availablenot availablenot available

Software:

XWINNMR v2.6 - processing

Xeasy v1.3 - structure solution

DYANA v1.5 - structure solution

AMBER v5.0 - refinement

NMR spectrometers:

  • Bruker AVANCE 600 MHz

Related Database Links:

BMRB 5768
PDB

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