BMRB Entry 17544

Title:
Structure of the second domain of human Nedd4L in complex with a doubly phosphorylated human Smad3 derived peptide.   PubMed: 21685363
Deposition date:
2011-03-22
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).

Assembly members:

Assembly members:
second domain of human Nedd4L, polymer, 35 residues, 4184.715 Da.
doubly phosphorylated human Smad3, polymer, 12 residues, 1341.284 Da.

Natural source:

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETM11

Experimental source:

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETM11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
second domain of human Nedd4L: GLPSGWEERKDAKGRTYYVN HNNRTTTWTRPIMQL
doubly phosphorylated human Smad3: EXPPPGYLSEDG

Data sets:
Data typeCount
13C chemical shifts98
15N chemical shifts33
1H chemical shifts313

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Nedd4L1
2Smad32

Entities:

Entity 1, Nedd4L 35 residues - 4184.715 Da.

1   GLYLEUPROSERGLYTRPGLUGLUARGLYS
2   ASPALALYSGLYARGTHRTYRTYRVALASN
3   HISASNASNARGTHRTHRTHRTRPTHRARG
4   PROILEMETGLNLEU

Entity 2, Smad3 12 residues - 1341.284 Da.

1   GLUTPOPROPROPROGLYTYRLEUSERGLU
2   ASPGLY

Samples:

H: Nedd4L 1 mM; SMAD3 3 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 2 mM; H2O 90%; D2O 10%

15N: Nedd4L, [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: Nedd4L, [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 18501
PDB

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