BMRB Entry 16247

Title:
NMR solution structure of the b30-82 domain of subunit b of Escherichia coli F1FO ATP synthase
Deposition date:
2009-04-08
Original release date:
2009-10-16
Authors:
Priya, Ragunathan; Biukovic, Goran; Gayen, Shovanlal; Vivekanandan, Subramanian; Gruber, Gerhard
Citation:

Citation: Priya, Ragunathan; Biukovic, Goran; Gayen, Shovanlal; Vivekanandan, Subramanian; Gruber, Gerhard. "Solution structure, determined by nuclear magnetic resonance, of the b30-82 domain of subunit b of Escherichia coli F1Fo ATP synthase."  J. Bacteriol. 191, 7538-7544 (2009).
PubMed: 19820091

Assembly members:

Assembly members:
subunit_b_30-82, polymer, 53 residues, 5785.686 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET9d1-His3 vector

Entity Sequences (FASTA):

Entity Sequences (FASTA):
subunit_b_30-82: MAAIEKRQKEIADGLASAER AHKDLDLAKASATDQLKKAK AEAQVIIEQANKR

Data sets:
Data typeCount
13C chemical shifts210
15N chemical shifts51
1H chemical shifts326

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1subunit b 30-821

Entities:

Entity 1, subunit b 30-82 53 residues - 5785.686 Da.

1   METALAALAILEGLULYSARGGLNLYSGLU
2   ILEALAASPGLYLEUALASERALAGLUARG
3   ALAHISLYSASPLEUASPLEUALALYSALA
4   SERALATHRASPGLNLEULYSLYSALALYS
5   ALAGLUALAGLNVALILEILEGLUGLNALA
6   ASNLYSARG

Samples:

sample_1: subunit b 30-82, [U-99% 13C; U-99% 15N], 1 mM; H2O 90%; D2O 10%; NaH2PO4 25 mM; Na2HPO4 25 mM; NaN3 0.1%

sample_conditions_1: ionic strength: 0 mM; pH: 6.8; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, P.GUNTERT ET AL. - refinement

SPARKY, Goddard - chemical shift assignment

TOPSPIN v1.3, Bruker Biospin - processing

Molmol, Koradi, Billeter and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAB38101 BAE77552 BAG79550 BAI28000 BAI33123
EMBL CAA23516 CAA23523 CAA25778 CAD03126 CAP78194
GB AAA24733 AAA24741 AAA62088 AAA83871 AAC76759
PIR AB0954
REF NP_312705 NP_418192 NP_458074 NP_462768 NP_709549
SP A7ZTU8 A8A6J9 A8ACP2 A9MJR5 A9MXB0
AlphaFold A9MXB0 A9MJR5 A7ZTU8 A8A6J9 A8ACP2

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