BMRB Entry 34990

Name: Solution structure of the Homer1 EVH1 domain
Published: 2025-12-03

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PDB ID: 9qux
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34990
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:

Solution structure of the Homer1 EVH1 domain

Deposition date:

2025-04-11

Original release date:

2025-12-03

Authors:

Czajlik, A.; Maruzs, B.; Fanni, F.; Batta, G.; Gaspari, Z.; Peterfia, B.

Citation:

Citation: Kalman, Z.; Czajlik, A.; Maruzs, B.; Farkas, F.; Pap, I.; Homonnay, C.; Klumpler, T.; Batta, G.; Gaspari, Z.; Peterfia, B.. "Structural Modeling and Dynamics of the Full-Length Homer1 Multimer" Proteins ., .-. (2025).
PubMed: 41267651

Assembly members:

Assembly members:
entity_1, polymer, 121 residues, 13757.411 Da.

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMGEQPIFSTRAHVFQID PNTKKNWVPTSKHAVTVSYF YDSTRNVYRIISLDGSKAII NSTITPNMTFTKTSQKFGQW ADSRANTVYGLGFSSEHHLS KFAEKFQEFKEAARLAKEKS Q

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	525
15N chemical shifts	127
1H chemical shifts	794

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 121 residues - 13757.411 Da.

1

GLY

SER

HIS

MET

GLY

GLU

GLN

PRO

ILE

PHE

2

SER

THR

ARG

ALA

HIS

VAL

PHE

GLN

ILE

ASP

3

PRO

ASN

THR

LYS

ASN

TRP

VAL

PRO

THR

4

SER

LYS

HIS

ALA

VAL

THR

VAL

SER

TYR

PHE

5

TYR

ASP

SER

THR

ARG

ASN

VAL

TYR

ARG

ILE

6

ILE

SER

LEU

ASP

GLY

SER

LYS

ALA

ILE

7

ASN

SER

THR

ILE

THR

PRO

ASN

MET

THR

PHE

8

THR

LYS

THR

SER

GLN

LYS

PHE

GLY

GLN

TRP

9

ALA

ASP

SER

ARG

ALA

ASN

THR

VAL

TYR

GLY

10

LEU

GLY

PHE

SER

GLU

HIS

LEU

SER

11

LYS

PHE

ALA

GLU

LYS

PHE

GLN

GLU

PHE

LYS

12

GLU

ALA

ARG

LEU

ALA

LYS

GLU

LYS

SER

13

GLN

Samples:

sample_1: Homer1 EVH1, [U-13C; U-15N], 180 uM; Sodium phosphate buffer 50 mM; sodium chloride 20 mM; NaN3 0.02%

sample_conditions_1: ionic strength: 215 mM; pH: 7.36; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
2D HBCBCGCDHD	sample_1	isotropic	sample_conditions_1
3D HCAN	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

CcpNmr Analysis v2.5.2, CCPN - peak picking

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure calculation

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

Bruker AVANCE NEO 700 MHz

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