BMRB Entry 27198

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

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27198

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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 PDZ3 domain

Deposition date:

2017-08-02

Original release date:

2018-02-15

Authors:

Susanne, Bruekner; Fabian, Renschler; Silke, Wiesner

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, 108 residues, Formula weight is not available

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Par3_PDZ3_domain: NSWHSREELTLHIPVHDTEK AGLGVSVKGKTCSDGDLGIF VKNVIHGGAASRDGRLRMND QLLSVNGVSLRGQNNAEAME TLRRAMVNTPGKHPGTITLL VGRKILRS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	268
15N chemical shifts	89
1H chemical shifts	89

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

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

Entities:

Entity 1, Par3 PDZ3 domain 108 residues - Formula weight is not available

Residues 667-685 of the natural sequence were deleted from the domain

1

ASN

SER

TRP

HIS

SER

ARG

GLU

LEU

THR

2

LEU

HIS

ILE

PRO

VAL

HIS

ASP

THR

GLU

LYS

3

ALA

GLY

LEU

GLY

VAL

SER

VAL

LYS

GLY

LYS

4

THR

CYS

SER

ASP

GLY

ASP

LEU

GLY

ILE

PHE

5

VAL

LYS

ASN

VAL

ILE

HIS

GLY

ALA

6

SER

ARG

ASP

GLY

ARG

LEU

ARG

MET

ASN

ASP

7

GLN

LEU

SER

VAL

ASN

GLY

VAL

SER

LEU

8

ARG

GLY

GLN

ASN

ALA

GLU

ALA

MET

GLU

9

THR

LEU

ARG

ALA

MET

VAL

ASN

THR

PRO

10

GLY

LYS

HIS

PRO

GLY

THR

ILE

THR

LEU

11

VAL

GLY

ARG

LYS

ILE

LEU

ARG

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: 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
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

XEASY, Bartels et al. - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

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