BMRB Entry 11000

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR11000

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Title:
C-Terminal Domain of Epsilon Subunit of F1F0-ATP Synthase from The Thermophilic Bacillus PS3 WITH ATP
Deposition date:
2007-04-19
Original release date:
2008-02-20
Authors:
Yagi, Hiromasa; Akutsu, Hideo
Citation:

Citation: Yagi, Hiromasa; Kajiwara, Nobumoto; Tanaka, Hideaki; Tsukihara, Tomitake; Kato-Yamada, Yasuyuki; Yoshida, Masasuke; Akutsu, Hideo. "Structures of the thermophilic F1-ATPase epsilon subunit suggesting ATP-regulated arm motion of its C-terminal domain in F1."  Proc. Natl. Acad. Sci. U. S. A. 104, 11233-11238 (2007).
PubMed: 17581881

Assembly members:

Assembly members:
ATP_Synthase_Epsilon_Chain, polymer, 46 residues, 5382.318 Da.

Natural source:

Natural source:   Common Name: thermophilic bacterium PS-3   Taxonomy ID: 2334   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus PS3

Experimental source:

Experimental source:   Production method: recombinant technology   Vector: PET32A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ATP_Synthase_Epsilon_Chain: IDVLRAKAAKERAERRLQSQ QDDIDFKRAELALKRAMNRL SVAEMK

Data sets:
Data typeCount
13C chemical shifts90
15N chemical shifts44
1H chemical shifts44

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1ATP Synthase Epsilon Subunit1

Entities:

Entity 1, ATP Synthase Epsilon Subunit 46 residues - 5382.318 Da.

1   ILEASPVALLEUARGALALYSALAALALYS
2   GLUARGALAGLUARGARGLEUGLNSERGLN
3   GLNASPASPILEASPPHELYSARGALAGLU
4   LEUALALEULYSARGALAMETASNARGLEU
5   SERVALALAGLUMETLYS

Samples:

sample_1: TF1 epsilon subunit, [U-13C; U-15N], 0.5 mM; K phosphate buffer 50 mM; H20 90%; D20, [U-2H], 10%

sample_2: TF1 Epsilon Subunit, [U-15N], 0.5 mM; Phosphate Buffer K 50 mM; H20 90%; D20, [U-2H], 10%

sample_conditions_1: ionic strength: 10 mM; pH: 6.8; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D HACACBsample_1isotropicsample_conditions_1
3D HA(CO)CACBsample_1isotropicsample_conditions_1
3D HAHBCONHsample_1isotropicsample_conditions_1
3D HCCONHsample_1isotropicsample_conditions_1
3D 15N edited NOESYsample_2isotropicsample_conditions_1
3D 13C edited NOESYsample_2isotropicsample_conditions_1

Software:

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

xwinnmr v3.5, Bruker Biospin - collection

SPARKY v3.110, Goddard - peak picking

CYANA v1.0.6, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

PDB
DBJ BAA96810 BAD77642 BAS29592 GAD12924 GAJ57182
GB ACX79962 ADI28255 ADU95790 AEV21070 AGE23942
REF WP_011232824 WP_015376059 WP_033010830 WP_044732826 WP_053414172
SP Q5KUJ4
AlphaFold Q5KUJ4

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