BMRB Entry 18498

Title:
YAP WW2 in complex with a Smad7 derived peptide.
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:

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).
PubMed: 22921829

Assembly members:

Assembly members:
YAPWW2, polymer, 36 residues, 4191.631 Da.
SMAD7, polymer, 12 residues, 1407.580 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):
YAPWW2: GPLPDGWEQAMTQDGEIYYI NHKNKTTSWLDPRLDP
SMAD7: GSPPPPYSRYPMD

Data sets:
Data typeCount
1H chemical shifts279

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1YAP WW21
2Smad7 derived peptide2

Entities:

Entity 1, YAP WW2 36 residues - 4191.631 Da.

1   GLYPROLEUPROASPGLYTRPGLUGLNALA
2   METTHRGLNASPGLYGLUILETYRTYRILE
3   ASNHISLYSASNLYSTHRTHRSERTRPLEU
4   ASPPROARGLEUASPPRO

Entity 2, Smad7 derived peptide 12 residues - 1407.580 Da.

1   GLYSERPROPROPROPROTYRSERARGTYR
2   PROMETASP

Samples:

Homonuclear: YAPWW2 1 mM; SMAD7 2 mM; TRIS, [U-100% 2H], 20 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

15N13C: YAPWW2, [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 17538
PDB
DBJ BAG62143 BAH14487
EMBL CCI79621 CCI79622
GB EAW67013 ELW64947 EMP37969 ETE73276 KFP99983
REF NP_001181974 XP_002822438 XP_003253086 XP_004052073 XP_004283405
AlphaFold Q6DK23