BMRB Entry 27232

Name: 13C chemical shifts of solid-state NMR signals of subunit c-ring of TFoF1 ATP synthase
Published: 2017-08-28

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27232

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

13C chemical shifts of solid-state NMR signals of subunit c-ring of TFoF1 ATP synthase

Deposition date:

2017-08-24

Original release date:

2017-08-28

Authors:

Akutsu, Hideo; Kang, Sujin; Todokoro, Yasuto; Bak, Suyeon; Suzuki, Toshiharu; Yoshida, Masasuke; Fujiwara, Toshimichi

Citation:

Citation: Kang, Su-Jin; Todokoro, Yasuto; Bak, Suyeon; Suzuki, Toshiharu; Yoshida, Masasuke; Fujiwara, Toshimichi; Akutsu, Hideo. "Direct assignment of 13C solid-state NMR signals of TFoF1 ATP synthase subunit c-ring in lipid membranes and its implication for the ring structure" J. Biomol. NMR 70, 53-65 (2018).
PubMed: 29197977

Assembly members:

Assembly members:
FoF1_ATP_synthase_subunit_c, polymer, 72 residues, 7384 Da.

Natural source:

Natural source: Common Name: thermophilic Bacillus Taxonomy ID: 1386 Superkingdom: Bacteria Kingdom: not available Genus/species: thermophilic Bacillus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pTR19-ASDS-cHis2R

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FoF1_ATP_synthase_subunit_c: MHLGVLAAAIAVGLGALGAG IGNGLIVSRTIEGIARQPEL RPVLQTTMFIGVALVEALPI IGVVFSFIYLGR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	294

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ATP synthase subunit c	1

Entities:

Entity 1, ATP synthase subunit c 72 residues - 7384 Da.

1

MET

HIS

LEU

GLY

VAL

LEU

ALA

ILE

2

ALA

VAL

GLY

LEU

GLY

ALA

LEU

GLY

ALA

GLY

3

ILE

GLY

ASN

GLY

LEU

ILE

VAL

SER

ARG

THR

4

ILE

GLU

GLY

ILE

ALA

ARG

GLN

PRO

GLU

LEU

5

ARG

PRO

VAL

LEU

GLN

THR

MET

PHE

ILE

6

GLY

VAL

ALA

LEU

VAL

GLU

ALA

LEU

PRO

ILE

7

ILE

GLY

VAL

PHE

SER

PHE

ILE

TYR

LEU

8

GLY

ARG

Samples:

Rev1: FoF1 ATP synthase subunit c-ring, [U-13C], 3 mg

Rev2: FoF1 ATP synthase subunit c-ring, [U-13C], 3 mg

Rev3: FoF1 ATP synthase subunit c-ring, [U-13C], 3 mg

sample_condition_1: ionic strength: 10 mM; pH: 7.5; temperature: 248 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 13C homonuclear correlation experiments with the dipolar assisted rotational resonance (DARR)	Rev1	isotropic	sample_condition_1
2D 13C homonuclear correlation experiments with the dipolar assisted rotational resonance (DARR)	Rev2	isotropic	sample_condition_1
2D 13C homonuclear correlation experiments with the dipolar assisted rotational resonance (DARR)	Rev3	isotropic	sample_condition_1
2D Cai+1-(C Ca)i correlation spectra	Rev1	isotropic	sample_condition_1
2D Cai+1-(C Ca)i correlation spectra	Rev2	isotropic	sample_condition_1
2D Cai+1-(C Ca)i correlation spectra	Rev3	isotropic	sample_condition_1

Software:

SPARKY v3.114, Goddard & Kneller (SPARKY) - chemical shift assignment

Felix vFelix2007, Felix NMR Inc. - processing

NMR spectrometers:

Varian Infinity-plus 600 600 MHz
Varian Infinity-plus 700 700 MHz