BMRB Entry 27640

Name: Chemical Shifts of KCNE1TVG in LMPG micelles
Published: 2018-10-12

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27640

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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:

Chemical Shifts of KCNE1TVG in LMPG micelles

Deposition date:

2018-10-08

Original release date:

2018-10-12

Authors:

Law, Cheryl; Sanders, Charles

Citation:

Citation: Law, Cheryl; Sanders, Charles. "NMR resonance assignments and secondary structure of a mutant form of the human KCNE1 channel accessory protein that exhibits KCNE3-like function." Biomol. NMR Assignments 13, 143-147 (2019).
PubMed: 30603955

Assembly members:

Assembly members:
KCNE1TVG, polymer, 136 residues, 15434.45 Da.

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: pET16b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
KCNE1TVG: HHHHHHGMILSNTTAVTPFL TKLWQETVQQGGNMSGLARR SPRSGDGKLEALYVLMVLGF FGFTVGGIMLSYIRSKKLEH SNDPFNVYIESDAWQEKDKA YVQARVLESYRSSYVVENHL AIEQPNTHLPETKPSP

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2

Data type	Count
13C chemical shifts	300
15N chemical shifts	111
1H chemical shifts	118

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	LMPG detergent	1

Entities:

Entity 1, LMPG detergent 136 residues - 15434.45 Da.

Residues 1-7 represent a non native affinity tag

1

HIS

GLY

MET

ILE

LEU

2

SER

ASN

THR

ALA

VAL

THR

PRO

PHE

LEU

3

THR

LYS

LEU

TRP

GLN

GLU

THR

VAL

GLN

4

GLY

ASN

MET

SER

GLY

LEU

ALA

ARG

5

SER

PRO

ARG

SER

GLY

ASP

GLY

LYS

LEU

GLU

6

ALA

LEU

TYR

VAL

LEU

MET

VAL

LEU

GLY

PHE

7

PHE

GLY

PHE

THR

VAL

GLY

ILE

MET

LEU

8

SER

TYR

ILE

ARG

SER

LYS

LEU

GLU

HIS

9

SER

ASN

ASP

PRO

PHE

ASN

VAL

TYR

ILE

GLU

10

SER

ASP

ALA

TRP

GLN

GLU

LYS

ASP

LYS

ALA

11

TYR

VAL

GLN

ALA

ARG

VAL

LEU

GLU

SER

TYR

12

ARG

SER

TYR

VAL

GLU

ASN

HIS

LEU

13

ALA

ILE

GLU

GLN

PRO

ASN

THR

HIS

LEU

PRO

14

GLU

THR

LYS

PRO

SER

PRO

Samples:

sample_1: KCNE1TVG, [U-100% 13C; U-100% 15N], 1 mM; D2O, [U-99% 15N], 10%; imidazole 50 mM; potassium chloride 50 mM; EDTA 2 mM; LMPG detergent 8 % w/v

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 313 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 HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

SPARKY vnmrfam-sparky, Goddard - data analysis

NMR spectrometers:

Bruker Avance 900 MHz

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