BMRB Entry 30937

Name: Solution NMR structure of PDLIM7 PDZ bound to SNX17 peptide
Published: 2022-08-26

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PDB ID: 7rm8
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30937
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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:

Solution NMR structure of PDLIM7 PDZ bound to SNX17 peptide

Deposition date:

2021-07-26

Original release date:

2022-08-26

Authors:

Healy, M.; Collins, B.; Mobli, M.

Citation:

Citation: Healy, Michael; Sacharz, Joanna; McNally, Kerrie; McConville, Calum; Tillu, Vikas; Hall, Ryan; Chilton, Molly; Cullen, Peter; Mobli, Mehdi; Ghai, Rajesh; Stroud, David; Collins, Brett. "Proteomic identification and structural basis for the interaction between sorting nexin SNX17 and PDLIM family proteins" Structure 30, 1590-1602 (2022).
PubMed: 36302387

Assembly members:

Assembly members:
entity_1, polymer, 112 residues, 11317.567 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 BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPMDSFKVVLEGPAPWGFRL QGGKDFNVPLSISRLTPGGK AAQAGVAVGDWVLSIDGENA GSLTHIEAQNKIRACGERLS LGLSRAGASAGASAGASAHG NFAFEGIGDEDL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	430
15N chemical shifts	118
1H chemical shifts	696

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 112 residues - 11317.567 Da.

1

GLY

PRO

MET

ASP

SER

PHE

LYS

VAL

LEU

2

GLU

GLY

PRO

ALA

PRO

TRP

GLY

PHE

ARG

LEU

3

GLN

GLY

LYS

ASP

PHE

ASN

VAL

PRO

LEU

4

SER

ILE

SER

ARG

LEU

THR

PRO

GLY

LYS

5

ALA

GLN

ALA

GLY

VAL

ALA

VAL

GLY

ASP

6

TRP

VAL

LEU

SER

ILE

ASP

GLY

GLU

ASN

ALA

7

GLY

SER

LEU

THR

HIS

ILE

GLU

ALA

GLN

ASN

8

LYS

ILE

ARG

ALA

CYS

GLY

GLU

ARG

LEU

SER

9

LEU

GLY

LEU

SER

ARG

ALA

GLY

ALA

SER

ALA

10

GLY

ALA

SER

ALA

GLY

ALA

SER

ALA

HIS

GLY

11

ASN

PHE

ALA

PHE

GLU

GLY

ILE

GLY

ASP

GLU

12

ASP

LEU

Samples:

sample_1: PDLIM7_SNX17_Fusion, [U-13C; U-15N], 1 mM; NaCl 75 mM; Bis-Tris 20 mM; DTT 4 mM

sample_conditions_1: ionic strength: 75 mM; pH: 5.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	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 HNCO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1

Software:

CcpNmr Analysis v3, CCPN - chemical shift assignment, peak picking, refinement

CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - structure calculation

NMR spectrometers:

Bruker AVANCE 900 MHz

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