BMRB Entry 27205

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for Hs. Par3 PDZ3 domain
Published: 2018-02-15

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27205

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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:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for Hs. Par3 PDZ3 domain

Deposition date:

2017-08-07

Original release date:

2018-02-15

Authors:

Wiesner, Silke

Citation:

Citation: Renschler, Fabian; Bruekner, Susanne; Salomon, Paulin; Mukherjee, Amrita; Kullmann, Lars; Schutz-Stoffregen, Mira; Henzler, Christine; Pawson, Tony; Krahn, Michael; Wiesner, Silke. "Structural basis for the interaction between the cell polarity proteins Par3 and Par6" Sci. Signal. 11, 9899-9899 (2018).
PubMed: 29440511

Assembly members:

Assembly members:
Par3_PDZ3_domain, polymer, 107 residues, Formula weight is not available

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-41

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Par3_PDZ3_domain: GAMGTREFLTFEVPLNDSGS AGLGVSVKGNRSKENHADLG IFVKSIINGGAASKDGRLRV NDQLIAVNGESLLGKTNQDA METLRRSMSTEGNKRGMIQL IVARRIS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	190
15N chemical shifts	93
1H chemical shifts	93

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Hs. Par3 PDZ3 domain	1

Entities:

Entity 1, Hs. Par3 PDZ3 domain 107 residues - Formula weight is not available

The N-terminal 4 residues (GAMG) are the result of the NcoI restriction site.

1

GLY

ALA

MET

GLY

THR

ARG

GLU

PHE

LEU

THR

2

PHE

GLU

VAL

PRO

LEU

ASN

ASP

SER

GLY

SER

3

ALA

GLY

LEU

GLY

VAL

SER

VAL

LYS

GLY

ASN

4

ARG

SER

LYS

GLU

ASN

HIS

ALA

ASP

LEU

GLY

5

ILE

PHE

VAL

LYS

SER

ILE

ASN

GLY

6

ALA

SER

LYS

ASP

GLY

ARG

LEU

ARG

VAL

7

ASN

ASP

GLN

LEU

ILE

ALA

VAL

ASN

GLY

GLU

8

SER

LEU

GLY

LYS

THR

ASN

GLN

ASP

ALA

9

MET

GLU

THR

LEU

ARG

SER

MET

SER

THR

10

GLU

GLY

ASN

LYS

ARG

GLY

MET

ILE

GLN

LEU

11

ILE

VAL

ALA

ARG

ILE

SER

Samples:

sample_1: Par3 PDZ3 domain, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 150 mM; DTT 1 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

XEASY, Bartels et al. - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz

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