BMRB Entry 18333

Title:
Solution structure of phosphorylated CRKL
Deposition date:
2012-03-16
Original release date:
2012-08-29
Authors:
Jankowski, Wojciech; Saleh, Tamjeed; Kalodimos, Charalampos
Citation:

Citation: Jankowski, Wojciech; Saleh, Tamjeed; Pai, Ming-Tao; Sriram, Ganapathy; Birge, Raymond; Kalodimos, Charalampos. "Domain organization differences explain Bcr-Abl's preference for CrkL over CrkII"  Nat. Chem. Biol. 8, 590-596 (2012).
PubMed: 22581121

Assembly members:

Assembly members:
entity, polymer, 303 residues, 33897.184 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: pET42A

Data sets:
Data typeCount
13C chemical shifts701
15N chemical shifts235
1H chemical shifts1015

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1phosphorylated CRKL1

Entities:

Entity 1, phosphorylated CRKL 303 residues - 33897.184 Da.

1   METSERSERALAARGPHEASPSERSERASP
2   ARGSERALATRPTYRMETGLYPROVALSER
3   ARGGLNGLUALAGLNTHRARGLEUGLNGLY
4   GLNARGHISGLYMETPHELEUVALARGASP
5   SERSERTHRCYSPROGLYASPTYRVALLEU
6   SERVALSERGLUASNSERARGVALSERHIS
7   TYRILEILEASNSERLEUPROASNARGARG
8   PHELYSILEGLYASPGLNGLUPHEASPHIS
9   LEUPROALALEULEUGLUPHETYRLYSILE
10   HISTYRLEUASPTHRTHRTHRLEUILEGLU
11   PROALAPROARGTYRPROSERPROPROMET
12   GLYSERVALSERALAPROASNLEUPROTHR
13   ALAGLUASPASNLEUGLUTYRVALARGTHR
14   LEUTYRASPPHEPROGLYASNASPALAGLU
15   ASPLEUPROPHELYSLYSGLYGLUILELEU
16   VALILEILEGLULYSPROGLUGLUGLNTRP
17   TRPSERALAARGASNLYSASPGLYARGVAL
18   GLYMETILEPROVALPROTYRVALGLULYS
19   LEUVALARGSERSERPROHISGLYLYSHIS
20   GLYASNARGASNSERASNSERTYRGLYILE
21   PROGLUPROALAHISALAPTRALAGLNPRO
22   GLNTHRTHRTHRPROLEUPROALAVALSER
23   GLYSERPROGLYALAALAILETHRPROLEU
24   PROSERTHRGLNASNGLYPROVALPHEALA
25   LYSALAILEGLNLYSARGVALPROCYSALA
26   TYRASPLYSTHRALALEUALALEUGLUVAL
27   GLYASPILEVALLYSVALTHRARGMETASN
28   ILEASNGLYGLNTRPGLUGLYGLUVALASN
29   GLYARGLYSGLYLEUPHEPROPHETHRHIS
30   VALLYSILEPHEASPPROGLNASNPROASP
31   GLUASNGLU

Samples:

sample_1: potassium phosphate0.3 – 0.8 mM; potassium chloride0.3 – 0.8 mM; beta-mercaptoethanol0.3 – 0.8 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.15 M; pH: 6.8; pressure: 1 atm; temperature: 305 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz

Related Database Links:

BMRB 18321
PDB
DBJ BAF85598 BAG72855
EMBL CAA42199 CAG30309 CAK54415 CAK54714
GB AAH43500 EAX02932 EAX02933 EAX02934 EFB28378
REF NP_001244412 NP_005198 XP_002743611 XP_002834682 XP_002926331
SP P46109
AlphaFold P46109

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