BMRB Entry 11172

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR11172

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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 and 15N chemical shifts of the membrane-reconstituted subunit c-ring of E. coli H+-ATP synthase

Deposition date:

2010-05-14

Original release date:

2017-08-03

Authors:

Todokoro, Yasuto; Kobayashi, Masatoshi; Sato, Takeshi; Kawakami, Toru; Yumen, Ikuko; Aimoto, Saburo; Fujiwara, Toshimichi; Akutsu, Hideo

Citation:

Citation: Todokoro, Yasuto; Kobayashi, Masatoshi; Sato, Takeshi; Kawakami, Toru; Yumen, Ikuko; Aimoto, Saburo; Fujiwara, Toshimichi; Akutsu, Hideo. "Structural analysis of the membrane-reconstituted subunit c-ring of E. coli H+-ATP synthase by solid-state NMR" J. Biomol. NMR 48, 1-11 (2010).
PubMed: 20596883

Assembly members:

Assembly members:
FoF1 ATP synthase subunit c (EFoc), polymer, 79 residues, Formula weight is not available

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: pCP35

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FoF1 ATP synthase subunit c (EFoc): MENLNMDLLYMAAAVMMGLA AIGAAIGIGILGGKFLEGAA RQPDLIPLLRTQFFIVMGLV DAIPMIAVGLGLYVMFAVA

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	127
15N chemical shifts	35

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FoF1 ATP synthase subunit c (EFoc)	1

Entities:

Entity 1, FoF1 ATP synthase subunit c (EFoc) 79 residues - Formula weight is not available

1

MET

GLU

ASN

LEU

ASN

MET

ASP

LEU

TYR

2

MET

ALA

VAL

MET

GLY

LEU

ALA

3

ALA

ILE

GLY

ALA

ILE

GLY

ILE

GLY

ILE

4

LEU

GLY

LYS

PHE

LEU

GLU

GLY

ALA

5

ARG

GLN

PRO

ASP

LEU

ILE

PRO

LEU

ARG

6

THR

GLN

PHE

ILE

VAL

MET

GLY

LEU

VAL

7

ASP

ALA

ILE

PRO

MET

ILE

ALA

VAL

GLY

LEU

8

GLY

LEU

TYR

VAL

MET

PHE

ALA

VAL

ALA

Samples:

sample_1: EFoc-ring, [U-13C; U-15N], 6 mg; DMPC-d54, 2H-hydrocarbon chain, 21.3 mg; H2O10 – 50%; NaN3 1 mM; Tris-HCl 10 mM

sample_2: EFoc-ring, [3-13C]-Ala24, [4-13C]-Asp61, 6 mg; H2O 100%; DMPC-d54, 2H-hydrocarbon chain, 21.3 mg; NaN3 1 mM; Tris-HCl 10 mM

condition_233K: pH: 8.0; temperature: 233 K

condition_223K: pH: 8.0; temperature: 223 K

condition_193K: pH: 8.0; temperature: 193 K

Experiments:

Name	Sample	Sample state	Sample conditions
Intra-residue 2D 13C-13C DARR	sample_1	solid	condition_233K
Inter-residue 2D CACA	sample_1	solid	condition_233K
Intra-residue 2D NCACB	sample_1	solid	condition_233K
Inter-residue 2D N(CO)CACB	sample_1	solid	condition_233K
Inter-residue 3D N(CO)CA	sample_1	solid	condition_233K
Intra-residue 3D NCACO	sample_1	solid	condition_233K
2H-selective 1H-depolarization 13C-NMR(CODSHD)	sample_1	solid	condition_223K
13C rotational resonance	sample_2	solid	condition_193K

Software:

FELIX v2007, Felix NMR Inc., San Diego, CA - processing

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Varian Infinity-plus 600 MHz
Varian Infinity-plus 500 MHz