BMRB Entry 16167

Name: NMR data for FXYD4 in micelles
Published: 2009-03-12

Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16167

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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:

NMR data for FXYD4 in micelles

Deposition date:

2009-02-11

Original release date:

2009-03-12

Authors:

Marassi, Francesca; Franzin, Carla; Teriete, Peter

Citation:

Citation: Franzin, Carla; Teriete, Peter; Marassi, Francesca. "Structural similarity of a membrane protein in micelles and membranes." J. Am. Chem. Soc. 129, 8078-8079 (2007).
PubMed: 17567018

Assembly members:

Assembly members:
FXYD4, polymer, 67 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FXYD4: NGPVDKGSPFYYDWESLQLG GLIFGGLLCIAGIALALSGK CKCRRNHTPSSLPEKVTPLI TPGSAST

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	123
15N chemical shifts	60
1H chemical shifts	136

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FXYD4 subunit	1

Entities:

Entity 1, FXYD4 subunit 67 residues - Formula weight is not available

1

ASN

GLY

PRO

VAL

ASP

LYS

GLY

SER

PRO

PHE

2

TYR

ASP

TRP

GLU

SER

LEU

GLN

LEU

GLY

3

GLY

LEU

ILE

PHE

GLY

LEU

CYS

ILE

4

ALA

GLY

ILE

ALA

LEU

ALA

LEU

SER

GLY

LYS

5

CYS

LYS

CYS

ARG

ASN

HIS

THR

PRO

SER

6

SER

LEU

PRO

GLU

LYS

VAL

THR

PRO

LEU

ILE

7

THR

PRO

GLY

SER

ALA

SER

THR

Samples:

sample_1: FXYD4, [U-100% 13C; U-100% 15N], 0.75 mM; FXYD4, [U-100% 15N], 0.75 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 20 mM; pH: 5; pressure: 1 atm; temperature: 313 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
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

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

SPARKY, Goddard - data analysis

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 500 MHz