BMRB Entry 25756

Title:
Backbone Assignment of the Tyrosine Kinase Src Catalytic Domain
Deposition date:
2015-08-14
Original release date:
2016-07-01
Authors:
Morando, Maria; D'Amelio, Nicola; Lovera, Silvia; Lelli, Moreno; Lopez, Blanca; Campos-Olivas, Ramon; Saladino, Giorgio; Gervasio, Francesco
Citation:

Citation: Morando, Maria; Saladino, Giorgio; D'Amelio, Nicola; Pucheta-Martinez, Encarna; Lovera, Silvia; Lelli, Moreno; Lopez-Mendez, Blanca; Marenchino, Marco; Campos-Olivas, Ramon; Gervasio, Francesco. "Conformational Selection and Induced Fit Mechanisms in the Binding of an Anticancer Drug to the c-Src Kinase"  Sci. Rep. 6, 24439-24439 (2016).
PubMed: 27087366

Assembly members:

Assembly members:
Src_catalytic_domain, polymer, 286 residues, 32689.6 Da.

Natural source:

Natural source:   Common Name: chicken   Taxonomy ID: 9031   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Gallus Gallus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: modified pET28

Data sets:
Data typeCount
13C chemical shifts540
15N chemical shifts179
1H chemical shifts179

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Src catalytic domain1

Entities:

Entity 1, Src catalytic domain 286 residues - 32689.6 Da.

1   GLYHISMETGLNTHRGLNGLYLEUALALYS
2   ASPALATRPGLUILEPROARGGLUSERLEU
3   ARGLEUGLUVALLYSLEUGLYGLNGLYCYS
4   PHEGLYGLUVALTRPMETGLYTHRTRPASN
5   GLYTHRTHRARGVALALAILELYSTHRLEU
6   LYSPROGLYTHRMETSERPROGLUALAPHE
7   LEUGLNGLUALAGLNVALMETLYSLYSLEU
8   ARGHISGLULYSLEUVALGLNLEUTYRALA
9   VALVALSERGLUGLUPROILETYRILEVAL
10   THRGLUTYRMETSERLYSGLYSERLEULEU
11   ASPPHELEULYSGLYGLUMETGLYLYSTYR
12   LEUARGLEUPROGLNLEUVALASPMETALA
13   ALAGLNILEALASERGLYMETALATYRVAL
14   GLUARGMETASNTYRVALHISARGASPLEU
15   ARGALAALAASNILELEUVALGLYGLUASN
16   LEUVALCYSLYSVALALAASPPHEGLYLEU
17   ALAARGLEUILEGLUASPASNGLUTYRTHR
18   ALAARGGLNGLYALALYSPHEPROILELYS
19   TRPTHRALAPROGLUALAALALEUTYRGLY
20   ARGPHETHRILELYSSERASPVALTRPSER
21   PHEGLYILELEULEUTHRGLULEUTHRTHR
22   LYSGLYARGVALPROTYRPROGLYMETVAL
23   ASNARGGLUVALLEUASPGLNVALGLUARG
24   GLYTYRARGMETPROCYSPROPROGLUCYS
25   PROGLUSERLEUHISASPLEUMETCYSGLN
26   CYSTRPARGLYSASPPROGLUGLUARGPRO
27   THRPHEGLUTYRLEUGLNALAPHELEUGLU
28   ASPTYRPHETHRSERTHRGLUPROGLNTYR
29   GLNPROGLYGLUASNLEU

Samples:

sample_1: Src catalytic domain, [U-99% 13C; U-99% 15N; U>70% 2H], 0.4 mM; magnesium chloride 1 mM; sodium chloride 500 mM; sodium azide 0.03%; TCEP 1 mM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 0.541 M; pH: 6.4; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - aid in the analysis of NMR spectra for assignment

xwinnmr, Bruker Biospin - spectra processing

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 1000 MHz
  • Bruker Avance 600 MHz

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