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 15551

Title: Backbone 1H and 15N Chemical Shift Assignments for Dok1 PTB domain   PubMed: 18156175

Deposition date: 2007-11-09 Original release date: 2008-01-09

Authors: Oxley, Camilla; Vakonakis, Ioannis; Wegener, Kate; Campbell, Iain

Citation: Oxley, Camilla; Anthis, Nicholas; Lowe, Edward; Vakonakis, Ioannis; Campbell, Iain; Wegener, Kate. "An integrin phosphorylation switch: the effect of beta3 integrin tail phosphorylation on DOK1 and talin binding."  J. Biol. Chem. 283, 5420-5426 (2008).

Assembly members:
Dok1, polymer, 108 residues, 12087.7 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   Vector: pGEX 6P2

Entity Sequences (FASTA):
Dok1: GPLGSQFWVTVQRTEAAERC GLHGSYVLRVEAERLTLLTV GAQSQILEPLLSWWYTLLRR YGRDKVMFSFEAGRRCPSGP GTFTFQTAQGNDIFQAVETA IHRQKAQG

Data sets:
Data typeCount
15N chemical shifts113
1H chemical shifts119

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Dok11

Entities:

Entity 1, Dok1 108 residues - 12087.7 Da.

1   GLYPROLEUGLYSERGLNPHETRPVALTHR
2   VALGLNARGTHRGLUALAALAGLUARGCYS
3   GLYLEUHISGLYSERTYRVALLEUARGVAL
4   GLUALAGLUARGLEUTHRLEULEUTHRVAL
5   GLYALAGLNSERGLNILELEUGLUPROLEU
6   LEUSERTRPTRPTYRTHRLEULEUARGARG
7   TYRGLYARGASPLYSVALMETPHESERPHE
8   GLUALAGLYARGARGCYSPROSERGLYPRO
9   GLYTHRPHETHRPHEGLNTHRALAGLNGLY
10   ASNASPILEPHEGLNALAVALGLUTHRALA
11   ILEHISARGGLNLYSALAGLNGLY

Samples:

sample_1: Dok1 (pH 6.1), [U-100% 13C; U-100% 15N], 1 mM; PBS 50 mM; NaCl 100 mM; DTT 10 mM; D2O 5%; Azide 10%

sample_conditions_1: ionic strength: 100 mM; pH: 6.1; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Home build Home build 600 MHz

Related Database Links:

BMRB 19672
PDB
DBJ BAD96603 BAG51595 BAG58893 BAJ17765
GB AAB88182 AAC51127 AAI14441 AAX93224 AIC48651
REF NP_001184189 NP_001372 XP_001111248 XP_001161802 XP_002757635
SP Q99704
AlphaFold Q99704

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