BMRB Entry 36114

Name: NMR structure of YAP1-2 WW1 domain with LATS1 PPxY motif complex
Published: 2019-08-21

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PDB ID: 5ydx
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR36114
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: NMR structure of YAP1-2 WW1 domain with LATS1 PPxY motif complex PubMed: 29487715

Deposition date: 2017-09-15 Original release date: 2019-08-21

Authors: Fan, J.; Sivaraman, J.

Citation: Verma, Apoorva; Jing-Song, Fan; Finch-Edmondson, Megan; Velazquez-Campoy, Adrian; Balasegaran, Shanker; Sudol, Marius; Sivaraman, Jayaraman. "Biophysical studies and NMR structure of YAP2 WW domain - LATS1 PPxY motif complexes reveal the basis of their interaction" Oncotarget 9, 8068-8080 (2018).

Assembly members:
entity_1, polymer, 59 residues, 6578.255 Da.

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source: Production method: recombinant technology Host organism: Cloning vector pGEM3_Zf

Entity Sequences (FASTA):
entity_1: SFEIPDDVPLPAGWEMAKTS SGQRYFLNHIDQTTTWQDPR KAMGGGGNYQGPPPPYPKH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	170
15N chemical shifts	56
1H chemical shifts	356

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 59 residues - 6578.255 Da.

1

SER

PHE

GLU

ILE

PRO

ASP

VAL

PRO

LEU

2

PRO

ALA

GLY

TRP

GLU

MET

ALA

LYS

THR

SER

3

SER

GLY

GLN

ARG

TYR

PHE

LEU

ASN

HIS

ILE

4

ASP

GLN

THR

TRP

GLN

ASP

PRO

ARG

5

LYS

ALA

MET

GLY

ASN

TYR

GLN

6

GLY

PRO

TYR

PRO

LYS

HIS

Samples:

sample_1: WW domain with PPxY motif, [U-100% 13C; U-100% 15N], 1.0 ± 0.1 mM; H2O 90%; D2O, [U-2H], 10%

sample_2: WW domain with PPxY motif 1 ± 0.1 mM; D2O, [U-2H], 100%

sample_conditions_1: ionic strength: 100 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 100 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_2
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - data analysis

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

NMR spectrometers:

Bruker Avance 800 MHz

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