BMRB Entry 50432

Name: ETV6 PNT Domain with an A93D PNT domain complexed to an unlabelled V112E PNT domain
Published: 2021-01-25

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50432

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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:

ETV6 PNT Domain with an A93D PNT domain complexed to an unlabelled V112E PNT domain

Deposition date:

2020-08-11

Original release date:

2021-01-25

Authors:

Gerak, Chloe; Okon, Mark; McIntosh, Lawrence

Citation:

Citation: Gerak, Chloe; Cho, Sophia; Kolesnikov, Maxim; Okon, Mark; Sessions, Richard; Murphy, Michael; Roberge, Michel; McIntosh, Lawrence. "Biophysical characterization of the ETV6 PNT domain polymerization interfaces" J. Biol. Chem. 296, 100284-100284 (2021).
PubMed: 33450226

Assembly members:

Assembly members:
entity_1, polymer, 83 residues, Formula weight is not available
entity_2, polymer, 83 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: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MEEDSIRLPAHLRLQPIYWS RDDVAQWLKWAENEFSLRPI DSNTFEMNGKDLLLLTKEDF RYRSPHSGDVLYELLQHILK QRK
entity_2: MEEDSIRLPAHLRLQPIYWS RDDVAQWLKWAENEFSLRPI DSNTFEMNGKALLLLTKEDF RYRSPHSGDELYELLQHILK QRK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	74
1H chemical shifts	74

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ETV6 PNT Domain A93D Complexed	1
2	Unlabelled ETV6 PNT domain V112E	2

Entities:

Entity 1, ETV6 PNT Domain A93D Complexed 83 residues - Formula weight is not available

1

MET

GLU

ASP

SER

ILE

ARG

LEU

PRO

ALA

2

HIS

LEU

ARG

LEU

GLN

PRO

ILE

TYR

TRP

SER

3

ARG

ASP

VAL

ALA

GLN

TRP

LEU

LYS

TRP

4

ALA

GLU

ASN

GLU

PHE

SER

LEU

ARG

PRO

ILE

5

ASP

SER

ASN

THR

PHE

GLU

MET

ASN

GLY

LYS

6

ASP

LEU

THR

LYS

GLU

ASP

PHE

7

ARG

TYR

ARG

SER

PRO

HIS

SER

GLY

ASP

VAL

8

LEU

TYR

GLU

LEU

GLN

HIS

ILE

LEU

LYS

9

GLN

ARG

LYS

Entity 2, Unlabelled ETV6 PNT domain V112E 83 residues - Formula weight is not available

1

MET

GLU

ASP

SER

ILE

ARG

LEU

PRO

ALA

2

HIS

LEU

ARG

LEU

GLN

PRO

ILE

TYR

TRP

SER

3

ARG

ASP

VAL

ALA

GLN

TRP

LEU

LYS

TRP

4

ALA

GLU

ASN

GLU

PHE

SER

LEU

ARG

PRO

ILE

5

ASP

SER

ASN

THR

PHE

GLU

MET

ASN

GLY

LYS

6

ALA

LEU

THR

LYS

GLU

ASP

PHE

7

ARG

TYR

ARG

SER

PRO

HIS

SER

GLY

ASP

GLU

8

LEU

TYR

GLU

LEU

GLN

HIS

ILE

LEU

LYS

9

GLN

ARG

LYS

Samples:

sample_1: MOPS 20 mM; NaCl 50 mM; EDTA 0.5 mM; ETV6 PNT Domain A93D, [U-99% 13C; U-99% 15N], 150 uM; Unlabelled ETV6 PNT domain V112E 150 uM

sample_conditions_1: ionic strength: 70 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

NMRFAM-SPARKY - chemical shift assignment, peak picking

TOPSPIN - collection

NMRPipe - processing

PINE - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 600 MHz

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