BMRB Entry 5813

Title:
The solution structure of the whole N-terminal domain of the ATPase CopA from Bacillus Subtilis. Implications for the function
Deposition date:
2003-05-31
Original release date:
2004-01-21
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.. "Structural basis for the function of the N terminal domain of the ATPase CopA from Bacillus subtilis"  J. Biol. Chem. 278, 50506-50513 (2003).
PubMed: 14514665

Assembly members:

Assembly members:
copper-transporting ATPase CopA, polymer, 151 residues, 16380.7 Da.

Natural source:

Natural source:   Common Name: Bacillus subtilis   Taxonomy ID: 224308   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus subtilis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: PET21a

Data sets:
Data typeCount
13C chemical shifts552
15N chemical shifts156
1H chemical shifts947

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CopA1

Entities:

Entity 1, CopA 151 residues - 16380.7 Da.

1   METLEUSERGLUGLNLYSGLUILEALAMET
2   GLNVALSERGLYMETTHRCYSALAALACYS
3   ALAALAARGILEGLULYSGLYLEULYSARG
4   METPROGLYVALTHRASPALAASNVALASN
5   LEUALATHRGLUTHRVALASNVALILETYR
6   ASPPROALAGLUTHRGLYTHRALAALAILE
7   GLNGLULYSILEGLULYSLEUGLYTYRHIS
8   VALVALTHRGLULYSALAGLUPHEASPILE
9   GLUGLYMETTHRCYSALAALACYSALAASN
10   ARGILEGLULYSARGLEUASNLYSILEGLU
11   GLYVALALAASNALAPROVALASNPHEALA
12   LEUGLUTHRVALTHRVALGLUTYRASNPRO
13   LYSGLUALASERVALSERASPLEULYSGLU
14   ALAVALASPLYSLEUGLYTYRLYSLEULYS
15   LEULYSGLYGLUGLNASPSERILEGLUGLY
16   ARG

Samples:

sample_1: copper-transporting ATPase CopA, [U-95% 13C; U-90% 15N], 1.5 mM; phosphate 20 mM; H2O 90%; D2O 10%; DTT 2.0 mM

sample_cond_1: ionic strength: 22 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D NOESYnot availablenot availablenot available
2D TOCSYnot availablenot availablenot available
3D 13C-separated NOESYnot availablenot availablenot available
3D 15N-separated NOESYnot availablenot availablenot available
HNHAnot availablenot availablenot available
HNHBnot availablenot availablenot available
CC(CO)NHnot availablenot availablenot available
(H)CCH-TOCSYnot availablenot availablenot available
CBCANHnot availablenot availablenot available
CBCA(CO)NHnot availablenot availablenot available

Software:

xwinnmr v2.6 - processing

DYANA v1.5 - structure solution

XEASY v1.3 - structure solution

AMBER v5.0 - refinement

NMR spectrometers:

  • Bruker AVANCE 800 MHz
  • Bruker AVANCE 700 MHz
  • Bruker AVANCE 500 MHz

Related Database Links:

PDB

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