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 18832

Title: Solution structure of the SH3 domain of DOCK180   PubMed: 23239367

Deposition date: 2012-11-08 Original release date: 2012-08-12

Authors: Liu, Xiangrong; Wen, Wenyu

Citation: Liu, Xiangrong; Li, Fengjuan; Pan, Zhu; Wang, Wenning; Wen, Wenyu. "Solution structure of the SH3 domain of DOCK180."  Proteins 81, 906-910 (2013).

Assembly members:
entity, polymer, 74 residues, 8659.928 Da.

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

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

Entity Sequences (FASTA):
entity: MTRWVPTKREEKYGVAFYNY DARGADELSLQIGDTVHILE TYEGWYRGYTLRKKSKKGIF PASYIHLKEAIVEG

Data sets:
Data typeCount
13C chemical shifts212
15N chemical shifts61
1H chemical shifts498

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SH3 domain of DOCK1801

Entities:

Entity 1, SH3 domain of DOCK180 74 residues - 8659.928 Da.

1   METTHRARGTRPVALPROTHRLYSARGGLU
2   GLULYSTYRGLYVALALAPHETYRASNTYR
3   ASPALAARGGLYALAASPGLULEUSERLEU
4   GLNILEGLYASPTHRVALHISILELEUGLU
5   THRTYRGLUGLYTRPTYRARGGLYTYRTHR
6   LEUARGLYSLYSSERLYSLYSGLYILEPHE
7   PROALASERTYRILEHISLEULYSGLUALA
8   ILEVALGLUGLY

Samples:

SH3-1: SH3, [U-100% 15N], 0.4 mM; PBS 50 mM; DTT 1 mM; EDTA 1 mM; H2O 90%; D2O 10%

SH3-2: SH3, [U-100% 13C; U-100% 15N], 0.4 mM; PBS 50 mM; DTT 1 mM; EDTA 1 mM; H2O 90%; D2O 10%

SH3-3: SH3, [U-100% 13C; U-100% 15N], 0.4 mM; PBS 50 mM; DTT, [U-100% 2H], 1 mM; EDTA 1 mM; D2O 100%

SH3-4: SH3 0.4 mM; PBS 50 mM; DTT, [U-100% 2H], 1 mM; EDTA 1 mM; D2O 100%

sample_condition: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCSH3-1isotropicsample_condition
3D 1H-15N NOESYSH3-1isotropicsample_condition
2D 1H-15N HSQCSH3-2isotropicsample_condition
3D CBCA(CO)NHSH3-2isotropicsample_condition
3D HNCACBSH3-2isotropicsample_condition
3D HNCOSH3-2isotropicsample_condition
2D 1H-13C HSQCSH3-3isotropicsample_condition
3D 1H-13C NOESYSH3-3isotropicsample_condition
2D 1H-1H NOESYSH3-4anisotropicsample_condition
2D 1H-1H TOCSYSH3-4anisotropicsample_condition

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

SPARKY, Goddard - peak picking

PIPP, Garrett - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian VNMRS 600 MHz

Related Database Links:

BMRB 18327
PDB
DBJ BAA09454 BAC38645 BAE24599
GB AAI46858 EDL17793 EDL17794 EDL17796 EDL17797
REF NP_001028592 NP_001137330 NP_001277152 NP_001371 XP_001089124
SP Q14185 Q8BUR4
TPG DAA14676

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