BMRB Entry 17080

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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/BMR17080
MolProbity Validation Chart

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Title:
Shc-PTB:biphosphorylated integrin beta3 cytoplasmic tail complex (1:1)
Deposition date:
2010-07-27
Original release date:
2010-09-02
Authors:
Deshmukh, Lalit; Gorbatyuk, Vitaliy; Vinogradova, Olga
Citation:

Citation: Deshmukh, Lalit; Gorbatyuk, Vitaliy; Vinogradova, Olga. "Integrin {beta}3 phosphorylation dictates its complex with the Shc phosphotyrosine-binding (PTB) domain."  J. Biol. Chem. 285, 34875-34884 (2010).
PubMed: 20739287

Assembly members:

Assembly members:
Shc-PTB, polymer, 211 residues, 20996.234 Da.
Integrin_beta3, polymer, 27 residues, 3284.411 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: Pet15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Shc-PTB: GSSHHHHHHSSGLVPRGSHM GQLGGEEWTRHGSFVNKPTR GWLHPNDKVMGPGVSYLVRY MGCVEVLQSMRALDFNTRTQ VTREAISLVCEAVPGAKGAT RRRKPCSRPLSSILGRSNLK FAGMPITLTVSTSSLNLMAA DCKQIIANHHMQSISFASGG DPDTAEYVAYVAKDPVNQRA CHILECPEGLAQDVISTIGQ AFELRFKQYLR
Integrin_beta3: RAKWDTANNPLXKEATSTFT NITXRGT

Data sets:
Data typeCount
13C chemical shifts720
15N chemical shifts181
1H chemical shifts1322
heteronuclear NOE values154
T1 relaxation values154
T2 relaxation values154

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Shc PTB domain1
2Integrin beta32

Entities:

Entity 1, Shc PTB domain 211 residues - 20996.234 Da.

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

Entity 2, Integrin beta3 27 residues - 3284.411 Da.

1   ARGALALYSTRPASPTHRALAASNASNPRO
2   LEUPTRLYSGLUALATHRSERTHRPHETHR
3   ASNILETHRPTRARGGLYTHR

Samples:

sample_1: Shc-PTB, [U-99% 13C; U-99% 15N], 0.4 mM; Integrin_beta3 0.8 mM; DTT 5 mM; sodium chloride 50 mM; sodium phosphate 50 mM; DSS 1 mM; H2O 93%; D2O 7%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N edited NOESYsample_1isotropicsample_conditions_1
3D 1H-13C edited NOESYsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D 1H-13C aromatic NOESYsample_1isotropicsample_conditions_1
2D 13C,15N FilteredTOCSYsample_1isotropicsample_conditions_1
2D 13C,15N Filtered NOESYsample_1isotropicsample_conditions_1
3D F1 13C,15N Filtered, F2 13C edited NOESY-HSQCsample_1isotropicsample_conditions_1
2D 1H-15N Het NOEsample_1isotropicsample_conditions_1
2D 1H-15N T1-HSQCsample_1isotropicsample_conditions_1
2D 1H-15N T2-HSQCsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

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

VNMRJ, Varian - collection

CCPN-Analysis v2.1.3, (CCPN-Analysis)-Vranken,Boucher, Stevens, Fogh, Pajon,Llinas,Ulrich,Markley,Ionides,Laue - data analysis, peak picking

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAA74950 BAC33706 BAE33083 BAF84832 BAF98733
EMBL CAA48251 CAA70977 CAH92143
GB AAA91777 AAB49972 AAC52146 AAH14158 AAH36172
REF NP_001068773 NP_001106802 NP_001123512 NP_001123513 NP_001126253
SP P29353 P98083 Q0IIE2 Q5M824 Q5R7W7
TPG DAA31779 DAA31780
BMRB 17931
AlphaFold P29353 P98083 Q0IIE2 Q5M824 Q5R7W7

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