BMRB Entry 17529

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR17529
MolProbity Validation Chart

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Title:
Third WW domain of human Nedd4L in complex with doubly phosphorylated human smad3 derived peptide.
Deposition date:
2011-03-16
Original release date:
2011-06-23
Authors:
Macias, Maria; Aragon, Eric; Goerner, Nina; Zaromytidou, Alexia-Ileana; Xi, Qiaoran; Escobedo, Albert; Massague, Joan
Citation:

Citation: Aragon, Eric; Goerner, Nina; Zaromytidou, Alexia-Ileana; Xi, Qiaoran; Escobedo, Albert; Massague, Joan; Macias, Maria. "A Smad action turnover switch operated by WW domain readers of a phosphoserine code."  Genes Dev. 25, 1275-1288 (2011).
PubMed: 21685363

Assembly members:

Assembly members:
NEDD4LWW3, polymer, 44 residues, 4822.491 Da.
SMAD3, polymer, 10 residues, 1112.977 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   Vector: petM11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NEDD4LWW3: GAMEQSFLPPGWEMRIAPNG RPFFYDHNTKTTTWEDPRLK FPVH
SMAD3: AGXPNLXPNP

Data sets:
Data typeCount
13C chemical shifts61
15N chemical shifts22
1H chemical shifts276

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1NEDD4LWW31
2SMAD32

Entities:

Entity 1, NEDD4LWW3 44 residues - 4822.491 Da.

1   GLYALAMETGLUGLNSERPHELEUPROPRO
2   GLYTRPGLUMETARGILEALAPROASNGLY
3   ARGPROPHEPHETYRASPHISASNTHRLYS
4   THRTHRTHRTRPGLUASPPROARGLEULYS
5   PHEPROVALHIS

Entity 2, SMAD3 10 residues - 1112.977 Da.

1   ALAGLYSEPPROASNLEUSEPPROASNPRO

Samples:

H: NEDD4LWW3 1 mM; SMAD3 3 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 2 mM; H2O 90%; D2O 10%

15N: NEDD4LWW3, [U-100% 15N], 1 mM; SMAD3 3 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 2 mM; H2O 90%; D2O 10%

15N13C: NEDD4LWW3, [U-100% 13C; U-100% 15N], 1 mM; SMAD3 3 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 2 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.420 M; pH: 7; pressure: 1 atm; temperature: 285 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYHisotropicsample_conditions_1
2D 1H-1H TOCSYHisotropicsample_conditions_1
3D CBCA(CO)NH15N13Cisotropicsample_conditions_1
3D HNCACB15N13Cisotropicsample_conditions_1
2D 1H-15N HSQC15Nisotropicsample_conditions_1

Software:

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

XEASY, Bartels et al. - chemical shift assignment

TOPSPIN, Bruker Biospin - collection

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

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

BMRB 25000
PDB
GB EPY82706
AlphaFold Q9GKR4

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