BMRB Entry 52671

Name: 1H/13C/15N assignment of the ligand binding domain of Ephrin A2 receptor
Published: 2024-12-23

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52671

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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/13C/15N assignment of the ligand binding domain of Ephrin A2 receptor

Deposition date:

2024-11-01

Original release date:

2024-12-23

Authors:

Mineev, Konstantin; Gande, Santosh; Linhard, Verena; Khashkhashi Moghaddam, Sattar; Schwalbe, Harald

Citation:

Citation: Mineev, Konstantin; Gande, Santosh; Linhard, Verena; Khashkhashi Moghaddam, Sattar; Schwalbe, Harald. "NMR resonance assignment of a ligand-binding domain of ephrin receptor A2" Biomol. NMR Assignments ., .-. (2024).
PubMed: 39695021

Assembly members:

Assembly members:
entity_1, polymer, 186 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: pMALTEV

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMAQGKEVVLLDFAAAGGE LGWLTHPYGKGWDLMQNIMN DMPIYMYSVCNVMSGDQDNW LRTNWVYRGEAERIFIELKF TVRDCNSFPGGASSCKETFN LYYAESDLDYGTNFQKRLFT KIDTIAPDEITVSSDFEARH VKLNVEERSVGPLTRKGFYL AFQDIGACVALLSVRVYYKK APELLQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	814
15N chemical shifts	184
1H chemical shifts	1261

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	EphA2_LBD	1

Entities:

Entity 1, EphA2_LBD 186 residues - Formula weight is not available

GAM is a remaining part of the expression tag, due to the TEV cleavage and cloning.

1

GLY

ALA

MET

ALA

GLN

GLY

LYS

GLU

VAL

2

LEU

ASP

PHE

ALA

GLY

GLU

3

LEU

GLY

TRP

LEU

THR

HIS

PRO

TYR

GLY

LYS

4

GLY

TRP

ASP

LEU

MET

GLN

ASN

ILE

MET

ASN

5

ASP

MET

PRO

ILE

TYR

MET

TYR

SER

VAL

CYS

6

ASN

VAL

MET

SER

GLY

ASP

GLN

ASP

ASN

TRP

7

LEU

ARG

THR

ASN

TRP

VAL

TYR

ARG

GLY

GLU

8

ALA

GLU

ARG

ILE

PHE

ILE

GLU

LEU

LYS

PHE

9

THR

VAL

ARG

ASP

CYS

ASN

SER

PHE

PRO

GLY

10

GLY

ALA

SER

CYS

LYS

GLU

THR

PHE

ASN

11

LEU

TYR

ALA

GLU

SER

ASP

LEU

ASP

TYR

12

GLY

THR

ASN

PHE

GLN

LYS

ARG

LEU

PHE

THR

13

LYS

ILE

ASP

THR

ILE

ALA

PRO

ASP

GLU

ILE

14

THR

VAL

SER

ASP

PHE

GLU

ALA

ARG

HIS

15

VAL

LYS

LEU

ASN

VAL

GLU

ARG

SER

VAL

16

GLY

PRO

LEU

THR

ARG

LYS

GLY

PHE

TYR

LEU

17

ALA

PHE

GLN

ASP

ILE

GLY

ALA

CYS

VAL

ALA

18

LEU

SER

VAL

ARG

VAL

TYR

LYS

19

ALA

PRO

GLU

LEU

GLN

Samples:

sample_1: EphA2_LBD, [U-100% 13C; U-100% 15N], 500 uM; sodium phosphate 25 mM; sodium azide 0.03%

sample_conditions_1: ionic strength: 25 mM; pH: 6.7; pressure: 1 atm; temperature: 303 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 HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D 15N-separated NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
2D (HB)CB(CGCD)HD	sample_1	isotropic	sample_conditions_1

Software:

CARA v1.9.2 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE NEO 600 MHz