BMRB Entry 34503

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

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PDB ID: 6yet
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34503
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, 106 residues, 12336.062 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_EH12

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GGGNNQPPWPKMKPSDVQKY TKVFMEVDSDKDGKITGEQA RNLFLSWRLPREVLKHVWEL SDQDNDTMLSLREFCISLYL MERYREGRPLPTALPSSIMF DETLLS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	386
15N chemical shifts	110
1H chemical shifts	772

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_1 106 residues - 12336.062 Da.

1

GLY

ASN

GLN

PRO

TRP

PRO

2

LYS

MET

LYS

PRO

SER

ASP

VAL

GLN

LYS

TYR

3

THR

LYS

VAL

PHE

MET

GLU

VAL

ASP

SER

ASP

4

LYS

ASP

GLY

LYS

ILE

THR

GLY

GLU

GLN

ALA

5

ARG

ASN

LEU

PHE

LEU

SER

TRP

ARG

LEU

PRO

6

ARG

GLU

VAL

LEU

LYS

HIS

VAL

TRP

GLU

LEU

7

SER

ASP

GLN

ASP

ASN

ASP

THR

MET

LEU

SER

8

LEU

ARG

GLU

PHE

CYS

ILE

SER

LEU

TYR

LEU

9

MET

GLU

ARG

TYR

ARG

GLU

GLY

ARG

PRO

LEU

10

PRO

THR

ALA

LEU

PRO

SER

ILE

MET

PHE

11

ASP

GLU

THR

LEU

SER

Entity 2, unit_2 - Ca - 40.078 Da.

1

CA

Samples:

sample_1: EH12, [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