BMRB Entry 17241

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17241
MolProbity Validation Chart

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Title:
YAP WW2
Deposition date:
2010-10-07
Original release date:
2011-03-30
Authors:
Webb, Claire; Upadhyay, Abhishek; Furutani-Seiki, Makoto; Bagby, Stefan
Citation:

Citation: Webb, Claire; Upadhyay, Abhishek; Giuntini, Francesca; Eggleston, Ian; Furutani-Seiki, Makoto; Ishima, Rieko; Bagby, Stefan. "Structural Features and Ligand Binding Properties of Tandem WW Domains from YAP and TAZ, Nuclear Effectors of the Hippo Pathway."  Biochemistry 50, 3300-3309 (2011).
PubMed: 21417403

Assembly members:

Assembly members:
entity, polymer, 46 residues, 5130.625 Da.

Natural source:

Natural source:   Common Name: Japanese medaka   Taxonomy ID: 8090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Oryzias latipes

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pSV281

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GSPNSSPASGPLPEGWEQAI TPEGEIYYINHKNKTTSWLD PRLETR

Data sets:
Data typeCount
13C chemical shifts193
15N chemical shifts46
1H chemical shifts264

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1YAP1

Entities:

Entity 1, YAP 46 residues - 5130.625 Da.

The first 5 residues (residues 177-181) are remains of a non-native affinity tag.

1   GLYSERPROASNSERSERPROALASERGLY
2   PROLEUPROGLUGLYTRPGLUGLNALAILE
3   THRPROGLUGLYGLUILETYRTYRILEASN
4   HISLYSASNLYSTHRTHRSERTRPLEUASP
5   PROARGLEUGLUTHRARG

Samples:

sample_1: potassium phosphate 50 mM; sodium chloride 200 mM; EDTA 5 mM; YAP WW2 protein, [U-15N], 400 – 600 mM; H2O 93%; D2O 7%

sample_2: potassium phosphate 50 mM; sodium chloride 200 mM; EDTA 5 mM; YAP WW2 protein, [U-13C; U-15N], 400 – 600 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 0.2 M; pH: 5.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1

Software:

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

CCPN_Analysis, CCPN - chemical shift assignment, data analysis, peak picking

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

NMR spectrometers:

  • Varian Unity INOVA 600 MHz

Related Database Links:

PDB

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