BMRB Entry 27812

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for the intrinsically disordered NHE1 distal tail phosphorylated at six sites by ERK2
Published: 2019-04-03

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27812

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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:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for the intrinsically disordered NHE1 distal tail phosphorylated at six sites by ERK2

Deposition date:

2019-03-01

Original release date:

2019-04-03

Authors:

Hendus-Altenburger, Ruth; Kragelund, Birthe

Citation:

Citation: Hendus-Altenburger, Ruth; Pedraz-Cuesta, Elena; Olesen, Christina; Papaleo, Elena; Schnell, Jeff; Hoppner, Jonathan; Robinson, Carol; Pedersen, Stine; Kragelund, Birthe. "The human Na(+)/H(+) exchanger 1 is a membrane scaffold protein for extracellular signal-regulated kinase 2" BMC Biol. 14, .-. (2016).
PubMed: 27083547

Assembly members:

Assembly members:
NHE1, polymer, 137 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NHE1: MINNYLTVPAHKLDXPTMSR ARIGSDPLAYEPKEDLPVIT IDPAXPQXPESVDLVNEELK GKVLGLSRDPAKVAEEDEDD DGGIMMRSKETSXPGTDDVF XPAPSDXPSSQRIQRCLSDP GPHPEPGEGEPFFPKGQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	386
15N chemical shifts	114
1H chemical shifts	114

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NHE1	1

Entities:

Entity 1, NHE1 137 residues - Formula weight is not available

Met + human NHE1 I680-Q815

1

MET

ILE

ASN

TYR

LEU

THR

VAL

PRO

ALA

2

HIS

LYS

LEU

ASP

SEP

PRO

THR

MET

SER

ARG

3

ALA

ARG

ILE

GLY

SER

ASP

PRO

LEU

ALA

TYR

4

GLU

PRO

LYS

GLU

ASP

LEU

PRO

VAL

ILE

THR

5

ILE

ASP

PRO

ALA

SEP

PRO

GLN

SEP

PRO

GLU

6

SER

VAL

ASP

LEU

VAL

ASN

GLU

LEU

LYS

7

GLY

LYS

VAL

LEU

GLY

LEU

SER

ARG

ASP

PRO

8

ALA

LYS

VAL

ALA

GLU

ASP

GLU

ASP

9

ASP

GLY

ILE

MET

ARG

SER

LYS

GLU

10

THR

SER

SEP

PRO

GLY

THR

ASP

VAL

PHE

11

TPO

PRO

ALA

PRO

SER

ASP

SEP

PRO

SER

12

GLN

ARG

ILE

GLN

ARG

CYS

LEU

SER

ASP

PRO

13

GLY

PRO

HIS

PRO

GLU

PRO

GLY

GLU

GLY

GLU

14

PRO

PHE

PRO

LYS

GLY

GLN

Samples:

sample_1: NHE1, [U-13C; U-15N], 400 uM; PBS 150 mM; DTT 10 mM; DSS 500 uM; D2O, [U-99% 2H], 10%

sample_conditions_1: ionic strength: 150 mM; pH: 7.2; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, CCPN - chemical shift assignment, data analysis, peak picking, processing

NMR spectrometers:

Varian INOVA 750 MHz
Varian INOVA 800 MHz

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