BMRB Entry 16923

Click here to enlarge.

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/BMR16923
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Solution Structure of Smurf2 WW2 and WW3 bound to Smad7 PY peptide Smad7 PY motif containing peptide
Deposition date:
2010-05-11
Original release date:
2010-10-14
Authors:
Chong, Andrew; Lin, Hong; Wrana, Jeff; Forman-Kay, Julie
Citation:

Citation: Chong, P. Andrew; Lin, Hong; Wrana, Jeffrey; Forman-Kay, Julie. "Coupling of tandem Smad ubiquitination regulatory factor (Smurf) WW domains modulates target specificity."  Proc. Natl. Acad. Sci. U.S.A. 107, 18404-18409 (2010).
PubMed: 20937913

Assembly members:

Assembly members:
WW23, polymer, 90 residues, 10114.108 Da.
S7PY, polymer, 20 residues, 2190.426 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: PGEX6P1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
WW23: GPLGGSPPDLPEGYEQRTTQ QGQVYFLHTQTGVSTWHDPR VPRDLSNINCEELGPLPPGW EIRNTATGRVYFVDHNNRTT QFTDPRLSAN
S7PY: GPLGSELESPPPPYSRYPMD

Data sets:
Data typeCount
13C chemical shifts369
15N chemical shifts128
1H chemical shifts720

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 90 residues - 10114.108 Da.

1   GLYPROLEUGLYGLYSERPROPROASPLEU
2   PROGLUGLYTYRGLUGLNARGTHRTHRGLN
3   GLNGLYGLNVALTYRPHELEUHISTHRGLN
4   THRGLYVALSERTHRTRPHISASPPROARG
5   VALPROARGASPLEUSERASNILEASNCYS
6   GLUGLULEUGLYPROLEUPROPROGLYTRP
7   GLUILEARGASNTHRALATHRGLYARGVAL
8   TYRPHEVALASPHISASNASNARGTHRTHR
9   GLNPHETHRASPPROARGLEUSERALAASN

Entity 2, entity_2 20 residues - 2190.426 Da.

1   GLYPROLEUGLYSERGLULEUGLUSERPRO
2   PROPROPROTYRSERARGTYRPROMETASP

Samples:

sample_1: WW23, [U-100% 13C; U-100% 15N], 1.2 mM; S7PY, [U-100% 13C; U-100% 15N], 1.2 mM; NaCl 20 mM; NaPi 40 mM; EDTA 1 mM; NaAzide 0.05%; Benzamidine 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 235 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D NC-NOESY (N and C simultaneous)sample_1isotropicsample_conditions_1
HACANsample_1isotropicsample_conditions_1
3D CCC-TOCSY-NNHsample_1isotropicsample_conditions_1
HBCBCGCDHD_AROsample_1isotropicsample_conditions_1
HBCBCGCDCDHE_AROsample_1isotropicsample_conditions_1

Software:

CNS v1.1, AT Brunger et al. - structure solution

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 500 MHz

Related Database Links:

PDB
EMBL CDQ73841
GB EAW94194 ELW67486 ERE69223 ETE71876 KFQ44520
REF XP_004946261 XP_005056211 XP_005738172 XP_006534001 XP_006912359

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