BMRB Entry 17600

Name: Solution structure of the isolated Par-6 PDZ domain
Published: 2011-12-01

Click here to enlarge.

PDB ID: 2lc7
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17600
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Solution structure of the isolated Par-6 PDZ domain

Deposition date:

2011-04-25

Original release date:

2011-12-01

Authors:

Volkman, B.; Whitney, D.; Peterson, F.

Citation:

Citation: Whitney, Dustin; Peterson, Francis; Volkman, Brian. "A Conformational Switch in the CRIB-PDZ Module of Par-6" Structure 19, 1711-1722 (2011).
PubMed: 22078569

Assembly members:

Assembly members:
Par-6, polymer, 102 residues, 10926.561 Da.

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: pBH4

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Par-6: GSETHRRVRLLKHGSDKPLG FYIRDGTSVRVTASGLEKQP GIFISRLVPGGLAESTGLLA VNDEVIEVNGIEVAGKTLDQ VTDMMVANSSNLIITVKPAN QR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	427
15N chemical shifts	103
1H chemical shifts	682

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Par-6	1

Entities:

Entity 1, Par-6 102 residues - 10926.561 Da.

The N-terminal GS dipeptide is a cloning artifact.

1

GLY

SER

GLU

THR

HIS

ARG

VAL

ARG

LEU

2

LEU

LYS

HIS

GLY

SER

ASP

LYS

PRO

LEU

GLY

3

PHE

TYR

ILE

ARG

ASP

GLY

THR

SER

VAL

ARG

4

VAL

THR

ALA

SER

GLY

LEU

GLU

LYS

GLN

PRO

5

GLY

ILE

PHE

ILE

SER

ARG

LEU

VAL

PRO

GLY

6

GLY

LEU

ALA

GLU

SER

THR

GLY

LEU

ALA

7

VAL

ASN

ASP

GLU

VAL

ILE

GLU

VAL

ASN

GLY

8

ILE

GLU

VAL

ALA

GLY

LYS

THR

LEU

ASP

GLN

9

VAL

THR

ASP

MET

VAL

ALA

ASN

SER

10

ASN

LEU

ILE

THR

VAL

LYS

PRO

ALA

ASN

11

GLN

ARG

Samples:

sample: Par-6, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 20 mM; potassium chloride 50 mM

sample_conditions_1: ionic strength: 53 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D_15N-separated_NOESY	sample	isotropic	sample_conditions_1
3D_13C-separated_NOESY	sample	isotropic	sample_conditions_1
3D_13C-separated_NOESY (AROMATIC)	sample	isotropic	sample_conditions_1

Software:

X-PLOR NIH v2.9.3, SCHWIETERS,C.D.,KUSZEWSKI,J.J.,TJANDRA,N.,CLORE,G.M. - refinement

TOPSPIN v2.1, Bruker - collection

NMRPipe v2007, Delagio,F. et al. - processing

XEASY v1.3, Eccles, C., Guntert, P., Billeter, M., Wuthrich, K. - data analysis

GARANT v2.1, C. Bartels - data analysis

CYANA v2.1, Guntert, P. - structural calculation

NMR spectrometers:

Bruker Avance II 600 MHz

BMRB	17599
PDB	1RY4 1RZX 1X8S 2LC6 2LC7
GB	AAD15927 AAF48757 AAL28917 AAN09592 ACL90845
REF	NP_573238 NP_728094 XP_001355305 XP_001963708 XP_001977590