BMRB Entry 34504

Name: Second EH domain of AtEH1/Pan1
Published: 2021-03-26

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PDB ID: 6yeu
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34504
MolProbity Validation Chart

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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:

Second EH domain of AtEH1/Pan1

Deposition date:

2020-03-25

Original release date:

2021-03-26

Authors:

Yperman, K.; Papageorgiou, A.; Evangelidis, T.; Van Damme, D.; Tripsianes, K.

Citation:

Citation: Yperman, Klaas; Papageorgiou, Anna; Merceron, Romain; De Munck, Steven; Bloch, Yehudi; Eeckhout, Dominique; Jiang, Qihang; Tack, Pieter; Grigoryan, Rosa; Evangelidis, Thomas; Van Leene, Jelle; Vincze, Laszlo; Vandenabeele, Peter; Vanhaecke, Frank; Potocky, Martin; De Jaeger, Geert; Savvides, Savvas; Tripsianes, Konstantinos; Pleskot, Roman; Van Damme, Daniel. "Distinct EH domains of the endocytic TPLATE complex confer lipid and protein binding" Nat. Commun. 12, 3050-3050 (2021).
PubMed: 34031427

Assembly members:

Assembly members:
entity_1, polymer, 109 residues, 11736.118 Da.
entity_CA, non-polymer, 40.078 Da.

Natural source:

Natural source: Common Name: Thale cress Taxonomy ID: 3702 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Arabidopsis thaliana

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21 Vector: pET22b_EH11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GGMAGQNPNMDQFEAYFKRA DLDGDGRISGAEAVGFFQGS GLSKQVLAQIWSLSDRSHSG FLDRQNFYNSLRLVTVAQSK RDLTPEIVNAALNTPAAAKI PPPKINLSA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	362
15N chemical shifts	118
1H chemical shifts	747

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1
2	unit_2	2

Entities:

Entity 1, unit_1 109 residues - 11736.118 Da.

1

GLY

MET

ALA

GLY

GLN

ASN

PRO

ASN

MET

2

ASP

GLN

PHE

GLU

ALA

TYR

PHE

LYS

ARG

ALA

3

ASP

LEU

ASP

GLY

ASP

GLY

ARG

ILE

SER

GLY

4

ALA

GLU

ALA

VAL

GLY

PHE

GLN

GLY

SER

5

GLY

LEU

SER

LYS

GLN

VAL

LEU

ALA

GLN

ILE

6

TRP

SER

LEU

SER

ASP

ARG

SER

HIS

SER

GLY

7

PHE

LEU

ASP

ARG

GLN

ASN

PHE

TYR

ASN

SER

8

LEU

ARG

LEU

VAL

THR

VAL

ALA

GLN

SER

LYS

9

ARG

ASP

LEU

THR

PRO

GLU

ILE

VAL

ASN

ALA

10

ALA

LEU

ASN

THR

PRO

ALA

LYS

ILE

11

PRO

LYS

ILE

ASN

LEU

SER

ALA

Entity 2, unit_2 - Ca - 40.078 Da.

1

CA

Samples:

sample_1: EH11, [U-99% 13C; U-99% 15N], 1 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
4D HC(CC TOCSY(CO))NH	sample_1	isotropic	sample_conditions_1
4D 13C,15N edited HMQC-NOESY-HSQC	sample_1	isotropic	sample_conditions_1
4D 13C,13C edited HMQC-NOESY-HSQC	sample_1	isotropic	sample_conditions_1
3D 13C edited NOESY-HSQC	sample_1	isotropic	sample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

4D-CHAINS, Evangelidis and Tripsianes - chemical shift assignment

Sparky, Goddard - peak picking

NMR spectrometers:

Bruker AVANCE III 850 MHz

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