BMRB Entry 27203

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for Dm. Par3 PDZ2 domain
Published: 2018-02-15

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27203

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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 Dm. Par3 PDZ2 domain PubMed: 29440511

Deposition date: 2017-08-07 Original release date: 2018-02-15

Authors: Bruekner, Susanne; Renschler, Fabian; Wiesner, Silke

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).

Assembly members:
Par3_PDZ2_domain, polymer, 99 residues, Formula weight is not available

Natural source: Common Name: fruit fly Taxonomy ID: 7227 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Drosophila Melanogaster

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pETM-30

Entity Sequences (FASTA):
Par3_PDZ2_domain: GAMGKLGRKIEIMLKKGPNG LGFSVTTRDNPAGGHCPIYI KNILPRGAAIEDGRLKPGDR LLEVDGTPMTGKTQTDVVAI LRGMPAGATVRIVVSRQQE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	129
15N chemical shifts	61
1H chemical shifts	61

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Dm. Par3 PDZ2 domain	1

Entities:

Entity 1, Dm. Par3 PDZ2 domain 99 residues - Formula weight is not available

The N-terminal 4 residues (GAMG) result from the NcoI restriction site and are not part of the natural sequence.

1

GLY

ALA

MET

GLY

LYS

LEU

GLY

ARG

LYS

ILE

2

GLU

ILE

MET

LEU

LYS

GLY

PRO

ASN

GLY

3

LEU

GLY

PHE

SER

VAL

THR

ARG

ASP

ASN

4

PRO

ALA

GLY

HIS

CYS

PRO

ILE

TYR

ILE

5

LYS

ASN

ILE

LEU

PRO

ARG

GLY

ALA

ILE

6

GLU

ASP

GLY

ARG

LEU

LYS

PRO

GLY

ASP

ARG

7

LEU

GLU

VAL

ASP

GLY

THR

PRO

MET

THR

8

GLY

LYS

THR

GLN

THR

ASP

VAL

ALA

ILE

9

LEU

ARG

GLY

MET

PRO

ALA

GLY

ALA

THR

VAL

10

ARG

ILE

VAL

SER

ARG

GLN

GLU

Samples:

sample_1: Par3 PDZ2 domain, [U-99% 13C; U-99% 15N], 0.3 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: 293 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 shifts
SPARKY: Backbone or all simulated shifts