BMRB Entry 15564

Name: GFT NMR based resonance assignment of membrane proteins: application to subunit c of E. coli F1F0 ATP synthase in LPPG micelles
Published: 2007-12-27

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15564

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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:

GFT NMR based resonance assignment of membrane proteins: application to subunit c of E. coli F1F0 ATP synthase in LPPG micelles

Deposition date:

2007-11-26

Original release date:

2007-12-27

Authors:

Zhang, Qi; Atreya, Hanudatta; Kamen, Doug; Girvin, Mark; Szypersk, Thomas

Citation:

Citation: Zhang, Qi; Atreya, Hanudatta; Kamen, Douglas; Girvin, Mark; Szyperski, Thomas. "GFT projection NMR based resonance assignment of membrane proteins: application to subunit C of E. coli F(1)F (0) ATP synthase in LPPG micelles" J. Biomol. NMR 40, 157-163 (2008).
PubMed: 18273680

Assembly members:

Assembly members:
subunit_c_of_E._coli_F1F0_ATP_synthas, 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: pEt 17b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
subunit_c_of_E._coli_F1F0_ATP_synthas: MENLNMDLLYMAAAVMMGLA AIGAAIGIGILGGKFLEGAA RQPDLIPLLRTQFFIVMGLV NAIPMIAVGLGLYVMFAVA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	261
15N chemical shifts	80
1H chemical shifts	575

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	subunit c	1

Entities:

Entity 1, subunit c 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

ASN

ALA

ILE

PRO

MET

ILE

ALA

VAL

GLY

LEU

8

GLY

LEU

TYR

VAL

MET

PHE

ALA

VAL

ALA

Samples:

sample_1: subunit c of E. coli F1F0 ATP synthas, [U-99% 13C; U-99% 15N], 0.9 mM; K-PO_4 50 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 320 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
(3,2)D HNNCO	sample_1	isotropic	sample_conditions_1
(4,2)D HACA(CO)NHN	sample_1	isotropic	sample_conditions_1
L-(4,3)D HNNCabCa	sample_1	isotropic	sample_conditions_1
L-(4,3)D HNN(CO)CabCa	sample_1	isotropic	sample_conditions_1
(4,3)D HCCH	sample_1	isotropic	sample_conditions_1
3D 15N,13Calip,13Caro-resolved [1H,1H]-NOESY	sample_1	isotropic	sample_conditions_1
(5,3)D HN{N,CO}{CabCa}}	sample_1	isotropic	sample_conditions_1
(5,3)D {CabCa}{CON}HN	sample_1	isotropic	sample_conditions_1

Software:

XEASY, Bartels et al. - chemical shift assignment

VNMR, Varian - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMR spectrometers:

Varian INOVA 750 MHz

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