BMRB Entry 50434

Name: Backbone assignments of AEG12
Published: 2021-06-30

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50434

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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 assignments of AEG12

Deposition date:

2020-08-12

Original release date:

2021-06-30

Authors:

Foo, Alexander; Mueller, Geoffrey

Citation:

Citation: Foo, Alexander; Thompson, Peter; Chen, Shih-Heng; Jadi, Ramesh; Lupo, Brianna; DeRose, Eugene; Arora, Simrat; Placentra, Victoria; Premkumar, Lakshmanane; Perera, Lalith; Pedersen, Lars; Martin, Negin; Mueller, Geoffrey. "The mosquito protein AEG12 displays both cytolytic and antiviral properties via a common lipid transfer mechanism." Proc. Natl. Acad. Sci. U. S. A. 118, e2019251118-e2019251118 (2021).
PubMed: 33688047

Assembly members:

Assembly members:
entity_1, polymer, 193 residues, Formula weight is not available

Natural source:

Natural source: Common Name: yellow fever mosquito Taxonomy ID: 7159 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Aedes aegypti

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSAAAPDSRALKDDFQEFVD LVPVDKLVNVALQYLVSDKE FKEFFGYLQGEEFSAVWDQF FALNEVKDVLNYLEAADLAV YDALNTVADFLGLHHVKPTV HTLRTGGLTGFFDETVALLP LDKFEALFEEKLKTSPEFKA FFEKLRNLDYQKFVDFHNNS KEVQGFLQKLRSYGLDVDGF FNLVAGFFGWGKF

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	425
15N chemical shifts	136
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	AEG12	1

Entities:

Entity 1, AEG12 193 residues - Formula weight is not available

1

GLY

SER

ALA

PRO

ASP

SER

ARG

ALA

2

LEU

LYS

ASP

PHE

GLN

GLU

PHE

VAL

ASP

3

LEU

VAL

PRO

VAL

ASP

LYS

LEU

VAL

ASN

VAL

4

ALA

LEU

GLN

TYR

LEU

VAL

SER

ASP

LYS

GLU

5

PHE

LYS

GLU

PHE

GLY

TYR

LEU

GLN

GLY

6

GLU

PHE

SER

ALA

VAL

TRP

ASP

GLN

PHE

7

PHE

ALA

LEU

ASN

GLU

VAL

LYS

ASP

VAL

LEU

8

ASN

TYR

LEU

GLU

ALA

ASP

LEU

ALA

VAL

9

TYR

ASP

ALA

LEU

ASN

THR

VAL

ALA

ASP

PHE

10

LEU

GLY

LEU

HIS

VAL

LYS

PRO

THR

VAL

11

HIS

THR

LEU

ARG

THR

GLY

LEU

THR

GLY

12

PHE

ASP

GLU

THR

VAL

ALA

LEU

PRO

13

LEU

ASP

LYS

PHE

GLU

ALA

LEU

PHE

GLU

14

LYS

LEU

LYS

THR

SER

PRO

GLU

PHE

LYS

ALA

15

PHE

GLU

LYS

LEU

ARG

ASN

LEU

ASP

TYR

16

GLN

LYS

PHE

VAL

ASP

PHE

HIS

ASN

SER

17

LYS

GLU

VAL

GLN

GLY

PHE

LEU

GLN

LYS

LEU

18

ARG

SER

TYR

GLY

LEU

ASP

VAL

ASP

GLY

PHE

19

PHE

ASN

LEU

VAL

ALA

GLY

PHE

GLY

TRP

20

GLY

LYS

PHE

Samples:

sample_1: AEG12 with ligands, [U-13C; U-15N; U-2H], 300 uM; palmitate, laureate, and stearate 2400 uM; D2O 10%; sodium chloride 123.3 mM; potassium chloride 2.41 mM; potassium phosphate 1.323 mM; sodium phosphate 3.86 mM; DSS 70 uM

sample_conditions_1: ionic strength: 162.7 mM; pH: 7.4; pressure: 1 atm; temperature: 298 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 HNCACO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

NMRViewJ - chemical shift assignment

VNMRj - collection

NMRPipe - processing

MddNMR - processing

NMR spectrometers:

Agilent DD2 600 MHz

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