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 16470

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for ShcA PTB Domain   PubMed: 20075861

Deposition date: 2009-08-27 Original release date: 2010-01-28

Authors: Smith, Matthew; Ikura, Mitsu

Citation: Smith, Matthew; Hardy, W. Rod; Li, Guang-Yao; Goudreault, Marilyn; Hersch, Steven; Metalnikov, Pavel; Starostine, Andrei; Pawson, Tony; Ikura, Mitsuhiko. "The PTB domain of ShcA couples receptor activation to the cytoskeletal regulator IQGAP1."  EMBO J. 29, 884-896 (2010).

Assembly members:
PTP-PEST_peptide, polymer, 14 residues, 1665.7 Da.
ShcA_PTB_domain, polymer, 191 residues, 20969 Da.

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

Experimental source:   Production method: recombinant technology' 'Escherichia coli

Entity Sequences (FASTA):
PTP-PEST_peptide: PLSFTNPLHSDDWH
ShcA_PTB_domain: GQLGGEEWTRHGSFVNKPTR GWLHPNDKVMGPGVSYLVRY MGCVEVLQSMRALDFNTRTQ VTREAISLVCEAVPGAKGAT RRRKPCSRPLSSILGRSNLK FAGMPITLTVSTSSLNLMAA DCKQIIANHHMQSISFASGG DPDTAEYVAYVAKDPVNQRA CHILECPEGLAQDVISTIGQ AFELRFKQYLR

Data sets:
Data typeCount
13C chemical shifts264
15N chemical shifts153
1H chemical shifts153

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1peptide ligand1
2binding domain2

Entities:

Entity 1, peptide ligand 14 residues - 1665.7 Da.

1   PROLEUSERPHETHRASNPROLEUHISSER
2   ASPASPTRPHIS

Entity 2, binding domain 191 residues - 20969 Da.

1   GLYGLNLEUGLYGLYGLUGLUTRPTHRARG
2   HISGLYSERPHEVALASNLYSPROTHRARG
3   GLYTRPLEUHISPROASNASPLYSVALMET
4   GLYPROGLYVALSERTYRLEUVALARGTYR
5   METGLYCYSVALGLUVALLEUGLNSERMET
6   ARGALALEUASPPHEASNTHRARGTHRGLN
7   VALTHRARGGLUALAILESERLEUVALCYS
8   GLUALAVALPROGLYALALYSGLYALATHR
9   ARGARGARGLYSPROCYSSERARGPROLEU
10   SERSERILELEUGLYARGSERASNLEULYS
11   PHEALAGLYMETPROILETHRLEUTHRVAL
12   SERTHRSERSERLEUASNLEUMETALAALA
13   ASPCYSLYSGLNILEILEALAASNHISHIS
14   METGLNSERILESERPHEALASERGLYGLY
15   ASPPROASPTHRALAGLUTYRVALALATYR
16   VALALALYSASPPROVALASNGLNARGALA
17   CYSHISILELEUGLUCYSPROGLUGLYLEU
18   ALAGLNASPVALILESERTHRILEGLYGLN
19   ALAPHEGLULEUARGPHELYSGLNTYRLEU
20   ARG

Samples:

sample_1: ShcA PTB domain' '[U-13C; U-15N]; .; .; .; .

sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

SWS P35831
BMRB 17080 5566
PDB
DBJ BAA74950 BAC33706 BAD92086 BAE33083 BAF84832
EMBL CAA48251 CAA70977 CAH92143
GB AAA91777 AAB49972 AAC52146 AAH14158 AAH33925
REF NP_001068773 NP_001106802 NP_001123512 NP_001123513 NP_001126253
SP P29353 P98083 Q0IIE2 Q5M824 Q5R7W7
TPG DAA31779 DAA31780

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