BMRB Entry 53371

Name: hDVL2 PDZ domain (265-361)
Published: 2025-09-26

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53371

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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:

hDVL2 PDZ domain (265-361)

Deposition date:

2025-09-23

Original release date:

2025-09-26

Authors:

Rutherford, Trevor; Bienz, Mariann; Gammons, Melissa

Citation:

Citation: Gammons, Melissa; Rutherford, Trevor; Steinhart, Zachary; Angers, Stephane; Bienz, Mariann. "Essential role of the Dishevelled DEP domain in a Wnt-dependent human cell-based complementation assay" J. Cell Sci. 129, 3892-3902 (2016).
PubMed: 27744318

Assembly members:

Assembly members:
entity_1, polymer, 102 residues, 10905 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: recombinant technology Host organism: Escherichia coli Vector: pETM-11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SGRGSIITVTLNMEKYNFLG ISIVGQSNERGDGGIYIGSI MKGGAVAADGRIEPGDMLLQ VNDMNFENMSNDDAVRVLRD IVHKPGPIVLTVAKCWDPSP QA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	279
15N chemical shifts	93
1H chemical shifts	93

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PDZ	1

Entities:

Entity 1, PDZ 102 residues - 10905 Da.

1

SER

GLY

ARG

GLY

SER

ILE

THR

VAL

THR

2

LEU

ASN

MET

GLU

LYS

TYR

ASN

PHE

LEU

GLY

3

ILE

SER

ILE

VAL

GLY

GLN

SER

ASN

GLU

ARG

4

GLY

ASP

GLY

ILE

TYR

ILE

GLY

SER

ILE

5

MET

LYS

GLY

ALA

VAL

ALA

ASP

GLY

6

ARG

ILE

GLU

PRO

GLY

ASP

MET

LEU

GLN

7

VAL

ASN

ASP

MET

ASN

PHE

GLU

ASN

MET

SER

8

ASN

ASP

ALA

VAL

ARG

VAL

LEU

ARG

ASP

9

ILE

VAL

HIS

LYS

PRO

GLY

PRO

ILE

VAL

LEU

10

THR

VAL

ALA

LYS

CYS

TRP

ASP

PRO

SER

PRO

11

GLN

ALA

Samples:

sample_1: PDZ, [U-100% 13C; U-100% 15N], 500 uM; H2O 95%; D2O, [U-100% 2H], 5%; sodium chloride 150 mM; sodium phosphate 25 mM

sample_conditions_1: ionic strength: 210 mM; pH: 6.7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCANH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.6.5 - collection, processing

NMRFAM-SPARKY v1.3 - chemical shift assignment

MARS v1.1 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 600 MHz