BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 15306

Title: Solution Structure of the C2 domain of human Smurf2   PubMed: 17719543

Authors: Wiesner, Silke; Ogunjimi, Abiodun; Wang, Hong-Rui; Rotin, Daniela; Sicheri, Frank; Wrana, Jeff; Forman-Kay, Julie

Citation: Wiesner, Silke; Ogunjimi, Abiodun; Wang, Hong-Rui; Rotin, Daniela; Sicheri, Frank; Wrana, Jeff; Forman-Kay, Julie. "Auto-inhibition of the HECT-type ubiquitin ligase Smurf2 through its C2 domain"  Cell 130, 651-662 (2007).

Assembly members:
C2 domain of Smurf2, polymer, 131 residues, 14707.108 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

Entity Sequences (FASTA):
C2 domain of Smurf2: GPVKLRLTVLCAKNLVKKDF FRLPDPFAKVVVDGSGQCHS TDTVKNTLDPKWNQHYDLYI GKSDSVTISVWNHKKIHKKQ GAGFLGCVRLLSNAINRLKD TGYQRLDLCKLGPNDNDTVR GQIVVSLQSRD

Data sets:
Data typeCount
13C chemical shifts433
15N chemical shifts138
1H chemical shifts864

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C2 domain of Smurf21

Entities:

Entity 1, C2 domain of Smurf2 131 residues - 14707.108 Da.

1   GLYPROVALLYSLEUARGLEUTHRVALLEU
2   CYSALALYSASNLEUVALLYSLYSASPPHE
3   PHEARGLEUPROASPPROPHEALALYSVAL
4   VALVALASPGLYSERGLYGLNCYSHISSER
5   THRASPTHRVALLYSASNTHRLEUASPPRO
6   LYSTRPASNGLNHISTYRASPLEUTYRILE
7   GLYLYSSERASPSERVALTHRILESERVAL
8   TRPASNHISLYSLYSILEHISLYSLYSGLN
9   GLYALAGLYPHELEUGLYCYSVALARGLEU
10   LEUSERASNALAILEASNARGLEULYSASP
11   THRGLYTYRGLNARGLEUASPLEUCYSLYS
12   LEUGLYPROASNASPASNASPTHRVALARG
13   GLYGLNILEVALVALSERLEUGLNSERARG
14   ASP

Samples:

sample_1: HEPES 20 mM; sodium chloride 200 mM; DTT 3 mM; sodium azide 0.03%

sample_2: hepes, [U-13C; U-15N], 20 mM; sodium chloride 200 mM; DTT 3 mM; sodium azide 0.03%

sample_conditions_1: ionic strength: 0.2 M; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

ARIA v1.2, Linge, O, . - structure solution

XEASY, Bartels et al. - chemical shift assignment

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

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 800 MHz

Related Database Links:

PDB
DBJ BAG11417
EMBL CDQ73842
GB AAG25641 AAG45422 AAG50421 AAG50422 AAH93876
REF NP_001082282 NP_001100531 NP_073576 NP_079757 XP_002186702
SP A2A5Z6 Q2TAS2 Q9HAU4
TPG DAA18293