BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17543

Title: Structure of the second domain of human Smurf1 in complex with a human Smad1 derived peptide containing a PY motif   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: 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:
human Smurf1, polymer, 35 residues, 4032.543 Da.
human Smad1 derived peptide, polymer, 13 residues, 1408.524 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: Escherichia coli   Vector: pETM11

Entity Sequences (FASTA):
human Smurf1: LGPLPPGWEVRSTVSGRIYF VDHNNRTTQFTDPRL
human Smad1 derived peptide: DTPPPAYLPPEDP

Data sets:
Data typeCount
13C chemical shifts44
15N chemical shifts17
1H chemical shifts296

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1human Smurf11
2human Smad1 derived peptide2

Entities:

Entity 1, human Smurf1 35 residues - 4032.543 Da.

1   LEUGLYPROLEUPROPROGLYTRPGLUVAL
2   ARGSERTHRVALSERGLYARGILETYRPHE
3   VALASPHISASNASNARGTHRTHRGLNPHE
4   THRASPPROARGLEU

Entity 2, human Smad1 derived peptide 13 residues - 1408.524 Da.

1   ASPTHRPROPROPROALATYRLEUPROPRO
2   GLUASPPRO

Samples:

H: Smurf1 1 mM; Smad1 3 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 2 mM; H2O 90%; D2O 10%

15N: Smurf1, [U-100% 15N], 1 mM; Smad1 3 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 2 mM; H2O 90%; D2O 10%

15N13C: Smurf1, [U-100% 13C; U-100% 15N], 1 mM; Smad1 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 18500
PDB
DBJ BAB13451 BAB29770 BAE32623 BAG11347
GB AAC62434 AAF08298 AAH29097 AAI36805 AAI44415
REF NP_001033716 NP_001103068 NP_001186776 NP_001244560 NP_065162
SP Q9CUN6 Q9HCE7
TPG DAA15146
AlphaFold Q9UFT8 Q9HCE7 Q9CUN6

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