BMRB Entry 52972

Name: 1H/15N/13C chemical shift assignments of ephrin A1
Published: 2025-09-26

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52972

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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 chemical shift assignments of ephrin A1

Deposition date:

2025-03-17

Original release date:

2025-09-26

Authors:

Mineev, Konstantin; Gande, Santosh; Linhard, Verena; Schwalbe, Harald

Citation:

Citation: Mineev, Konstantin; Gande, Santosh; Wenzel, Annika; Linhard, Verena; Clark, Halle Andrews; Witt, Kerstin; Koster, Sabine; Segarra, Marta; McDowell, Melanie; Acker-Palmer, Amparo; Schwalbe, Harald. "Structural role of conformational heterogeneity and juxtamembrane regions in the Ephrin A1 interactions with the EphA2 receptor ligand-binding domain" J. Mol. Biol. ., .-. (2025).
PubMed: 40998111

Assembly members:

Assembly members:
entity_1, polymer, 158 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: pETTev

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MSHHHHHHHASENLYFQGAM AAADRHTVFWNSSNPKFRNE DYTIHVQLNDYVDIICPHYE DHSVADAAMEQYILYLVEHE EYQLCQPQSKDQVRWQCNRP SAKHGPEKLSEKFQRFTPFT LGKEFKEGHSYYYISKPIHQ HEDRCLRLKVTVSGKITH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	432
15N chemical shifts	110
1H chemical shifts	714

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	EFNA1s	1

Entities:

Entity 1, EFNA1s 158 residues - Formula weight is not available

1

MET

SER

HIS

ALA

2

SER

GLU

ASN

LEU

TYR

PHE

GLN

GLY

ALA

MET

3

ALA

ASP

ARG

HIS

THR

VAL

PHE

TRP

4

ASN

SER

ASN

PRO

LYS

PHE

ARG

ASN

GLU

5

ASP

TYR

THR

ILE

HIS

VAL

GLN

LEU

ASN

ASP

6

TYR

VAL

ASP

ILE

CYS

PRO

HIS

TYR

GLU

7

ASP

HIS

SER

VAL

ALA

ASP

ALA

MET

GLU

8

GLN

TYR

ILE

LEU

TYR

LEU

VAL

GLU

HIS

GLU

9

GLU

TYR

GLN

LEU

CYS

GLN

PRO

GLN

SER

LYS

10

ASP

GLN

VAL

ARG

TRP

GLN

CYS

ASN

ARG

PRO

11

SER

ALA

LYS

HIS

GLY

PRO

GLU

LYS

LEU

SER

12

GLU

LYS

PHE

GLN

ARG

PHE

THR

PRO

PHE

THR

13

LEU

GLY

LYS

GLU

PHE

LYS

GLU

GLY

HIS

SER

14

TYR

ILE

SER

LYS

PRO

ILE

HIS

GLN

15

HIS

GLU

ASP

ARG

CYS

LEU

ARG

LEU

LYS

VAL

16

THR

VAL

SER

GLY

LYS

ILE

THR

HIS

Samples:

sample_1: EFNA1s, [U-100% 13C; U-100% 15N], 0.5 ± 0.05 mM; sodium chloride 50 ± 1 mM; TRIS 20 ± 1 mM

sample_conditions_1: ionic strength: 70 mM; pH: 8.0; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
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 HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 15N-separated NOESY	sample_1	isotropic	sample_conditions_1
3D 13C-separated NOESY	sample_1	isotropic	sample_conditions_1

Software:

CARA v1.9 - chemical shift assignment

TOPSPIN v4.5 - collection

NMR spectrometers:

Bruker AVANCE NEO 600 MHz