BMRB Entry 34213

Name: NMR structure of EphA2-Sam stapled peptides (S13ST)
Published: 2018-07-26

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PDB ID: 6f7m
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34213
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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:

NMR structure of EphA2-Sam stapled peptides (S13ST)

Deposition date:

2017-12-11

Original release date:

2018-07-26

Authors:

Mercurio, F.; Leone, M.

Citation:

Citation: Mercurio, F.; Pirone, L.; Di Natale, C.; Marasco, D.; Pedone, E.; Leone, M.. "Sam domain-based stapled peptides: Structural analysis and interaction studies with the Sam domains from the EphA2 receptor and the lipid phosphatase Ship2" Bioorg. Chem. 80, 602-610 (2018).
PubMed: 30036816

Assembly members:

Assembly members:
entity_1, polymer, 27 residues, 2905.534 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: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: XKRIGVRLPGHQKRXAYSXL GLKDQVX

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
1H chemical shifts	200

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 27 residues - 2905.534 Da.

1

ACE

LYS

ARG

ILE

GLY

VAL

ARG

LEU

PRO

GLY

2

HIS

GLN

LYS

ARG

MK8

ALA

TYR

SER

MK8

LEU

3

GLY

LEU

LYS

ASP

GLN

VAL

NH2

Samples:

sample_1: S13ST 650 uM

sample_conditions_1: pH: 7.1; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D DQF-COSY	sample_1	isotropic	sample_conditions_1

Software:

VNMRJ, Varian - processing

XEASY, Bartels et al. - chemical shift assignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement

Chimera v1.10.1, Pettersen et al. - geometry optimization

NMR spectrometers:

Varian INOVA 600 MHz