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 18500

Title: Smurf1 WW2 domain in complex with a Smad7 derived peptide.   PubMed: 22921829

Deposition date: 2012-06-04 Original release date: 2012-11-19

Authors: Macias, Maria; Aragon, Eric; Goerner, Nina; Xi, Qiaoran; Lopes, Tiago; Gao, Sheng; Massague, Joan

Citation: Aragon, Eric; Goerner, Nina; Xi, Qiaoran; Gomes, Tiago; Gao, Sheng; Massague, Joan; Macias, Maria. "Structural Basis for the Versatile Interactions of Smad7 with Regulator WW Domains in TGF-beta Pathways"  Structure 20, 1726-1736 (2012).

Assembly members:
SMURF1WW2, polymer, 35 residues, 4057.533 Da.
SMAD7, polymer, 15 residues, 1778.969 Da.

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

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

Entity Sequences (FASTA):
SMURF1WW2: GPLPPGWEVRSTVSGRIYFV DHNNRTTQFTDPRLH
SMAD7: ELESPPPPYSRYPMD

Data sets:
Data typeCount
1H chemical shifts281

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Smurf1 WW2 domain1
2Smad7 derived peptide2

Entities:

Entity 1, Smurf1 WW2 domain 35 residues - 4057.533 Da.

1   GLYPROLEUPROPROGLYTRPGLUVALARG
2   SERTHRVALSERGLYARGILETYRPHEVAL
3   ASPHISASNASNARGTHRTHRGLNPHETHR
4   ASPPROARGLEUHIS

Entity 2, Smad7 derived peptide 15 residues - 1778.969 Da.

1   GLULEUGLUSERPROPROPROPROTYRSER
2   ARGTYRPROMETASP

Samples:

Homonuclear: SMURF1WW2 1 mM; SMAD7 2 mM; TRIS, [U-100% 2H], 20 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

15N13C: SMURF1WW2, [U-100% 13C; U-100% 15N], 1 mM; SMAD7 3 mM; TRIS, [U-100% 2H], 20 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.2; pressure: 1 atm; temperature: 285 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15N13Cisotropicsample_conditions_1
2D 1H-1H TOCSYHomonuclearisotropicsample_conditions_1
2D 1H-1H NOESYHomonuclearisotropicsample_conditions_1
3D CBCA(CO)NH15N13Cisotropicsample_conditions_1
3D HNCACB15N13Cisotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

CNSSOLVE, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 17543 16923 18501 18502
PDB
DBJ BAB13451 BAB29770 BAE32623 BAG11347 BAG11040
EMBL CAF92291 CAA04182 CAA04183 CAG12446 CDQ87305 CDQ93148
GB AAC62434 AAF08298 AAH29097 AAI36805 AAI44415 AAB81246 AAB81353 AAB81354 AAC25062 AAD41130
REF NP_001033716 NP_001103068 NP_001186776 NP_001244560 NP_065162 NP_001036125 NP_001153135 NP_001177750 NP_001231104 NP_001268265
SP Q9CUN6 Q9HCE7 O15105 O35253 O88406
TPG DAA15146 DAA15864