BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16247

Title: NMR solution structure of the b30-82 domain of subunit b of Escherichia coli F1FO ATP synthase   PubMed: 19820091

Deposition date: 2009-04-08 Original release date: 2009-10-16

Authors: Priya, Ragunathan; Biukovic, Goran; Gayen, Shovanlal; Vivekanandan, Subramanian; Gruber, Gerhard

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).

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

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

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

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

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts