BMRB Entry 51122

Name: 1H, 15N, 13C backbone assignment of ApoE3 NTD at pH 3.5 and 20C
Published: 2021-11-28

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51122

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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:

1H, 15N, 13C backbone assignment of ApoE3 NTD at pH 3.5 and 20C

Deposition date:

2021-10-03

Original release date:

2021-11-28

Authors:

Pandit, Subhendu

Citation:

Citation: Pandit, Subhendu. "1H, 15N and 13C chemical shift assignments of the N-terminal domain of the two isoforms of the human apolipoprotein E" Biomol. NMR Assign. 16, 191-196 (2022).
PubMed: 35451799

Assembly members:

Assembly members:
entity_1, polymer, 167 residues, 18569.01 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: pET-32

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: KVEQAVETEPEPELRQQTEW QSGQRWELALGRFWDYLRWV QTLSEQVQEELLSSQVTQEL RALMDETMKELKAYKSELEE QLTPVAEETRARLSKELQAA QARLGADMEDVCGRLVQYRG EVQAMLGQSTEELRVRLASH LRKLRKRLLRDADDLQKRLA VYQAGAR

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	595
15N chemical shifts	151
1H chemical shifts	741

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ApoE3-NTD	1

Entities:

Entity 1, ApoE3-NTD 167 residues - 18569.01 Da.

1

LYS

VAL

GLU

GLN

ALA

VAL

GLU

THR

GLU

PRO

2

GLU

PRO

GLU

LEU

ARG

GLN

THR

GLU

TRP

3

GLN

SER

GLY

GLN

ARG

TRP

GLU

LEU

ALA

LEU

4

GLY

ARG

PHE

TRP

ASP

TYR

LEU

ARG

TRP

VAL

5

GLN

THR

LEU

SER

GLU

GLN

VAL

GLN

GLU

6

LEU

SER

GLN

VAL

THR

GLN

GLU

LEU

7

ARG

ALA

LEU

MET

ASP

GLU

THR

MET

LYS

GLU

8

LEU

LYS

ALA

TYR

LYS

SER

GLU

LEU

GLU

9

GLN

LEU

THR

PRO

VAL

ALA

GLU

THR

ARG

10

ALA

ARG

LEU

SER

LYS

GLU

LEU

GLN

ALA

11

GLN

ALA

ARG

LEU

GLY

ALA

ASP

MET

GLU

ASP

12

VAL

CYS

GLY

ARG

LEU

VAL

GLN

TYR

ARG

GLY

13

GLU

VAL

GLN

ALA

MET

LEU

GLY

GLN

SER

THR

14

GLU

LEU

ARG

VAL

ARG

LEU

ALA

SER

HIS

15

LEU

ARG

LYS

LEU

ARG

LYS

ARG

LEU

ARG

16

ASP

ALA

ASP

LEU

GLN

LYS

ARG

LEU

ALA

17

VAL

TYR

GLN

ALA

GLY

ALA

ARG

Samples:

sample_1: ApoE3-NTD, [U-99% 13C; U-99% 15N], 1 mM; sodium phosphate 50 mM; EDTA 1 mM; sodium azide 1 mM; DTT 5 mM

sample_conditions_1: pH: 3.5; pressure: 1 atm; temperature: 293 K

Experiments:

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

Software:

NMRFAM-SPARKY v1.413 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III HD 700 MHz

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