BMRB Entry 6570

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6570
MolProbity Validation Chart

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Title:
NMR Assignments of the F-actin binding domain of human Bcr-Abl/c-Abl
Deposition date:
2005-03-24
Original release date:
2005-10-24
Authors:
Wiesner, Silke; Hantschel, Oliver; Mackereth, Cameron; Superti-Furga, Giulio; Sattler, Michael
Citation:

Citation: Wiesner, Silke; Hantschel, Oliver; Mackereth, Cameron; Superti-Furga, Giulio; Sattler, Michael. "NMR Assignment Reveals an alpha-Helical Fold for the F-Actin Binding Domain of Human Bcr-Abl/c-Abl"  J. Biomol. NMR 32, 335-335 (2005).
PubMed: 16211486

Assembly members:

Assembly members:
F-actin binding domain of cellular Abelson tyrosine kinase, polymer, 130 residues, 10251 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: pETM30 (modified pET24d)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
F-actin binding domain of cellular Abelson tyrosine kinase: GAMASTRVSLRKTRQPPERI ASGAITKGVVLDSTEALCLA ISRNSEQMASHSAVLEAGKN LYSFCVSYVDSIQQMRNKFA FREAINKLENNLRELQICPA TAGSGPAATQDFSKLLSSVK EISDIVQRLE

Data sets:
Data typeCount
1H chemical shifts763
13C chemical shifts499
15N chemical shifts137

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1c-Abl, FABD1

Entities:

Entity 1, c-Abl, FABD 130 residues - 10251 Da.

1   GLYALAMETALASERTHRARGVALSERLEU
2   ARGLYSTHRARGGLNPROPROGLUARGILE
3   ALASERGLYALAILETHRLYSGLYVALVAL
4   LEUASPSERTHRGLUALALEUCYSLEUALA
5   ILESERARGASNSERGLUGLNMETALASER
6   HISSERALAVALLEUGLUALAGLYLYSASN
7   LEUTYRSERPHECYSVALSERTYRVALASP
8   SERILEGLNGLNMETARGASNLYSPHEALA
9   PHEARGGLUALAILEASNLYSLEUGLUASN
10   ASNLEUARGGLULEUGLNILECYSPROALA
11   THRALAGLYSERGLYPROALAALATHRGLN
12   ASPPHESERLYSLEULEUSERSERVALLYS
13   GLUILESERASPILEVALGLNARGLEUGLU

Samples:

15N-labeled_sample: F-actin binding domain of cellular Abelson tyrosine kinase, [U-100% 15N], 1.0 mM

15N-13C-labeled_sample: F-actin binding domain of cellular Abelson tyrosine kinase, [U-100% 13C; U-100% 15N], 1.0 mM

ExpCondition: pH: 6.3; temperature: 295 K

Experiments:

NameSampleSample stateSample conditions
HN-HSQCnot availablenot availablenot available
HNCAnot availablenot availablenot available
CBCANHnot availablenot availablenot available
CBCA(CO)NHnot availablenot availablenot available
HNHA-Jnot availablenot availablenot available
HNCOnot availablenot availablenot available
CBCACO(N)Hnot availablenot availablenot available
HN-HSQC-NOESY-(H)C-HMQCnot availablenot availablenot available
HC-HSQCnot availablenot availablenot available
H(CCO)NHnot availablenot availablenot available
(H)C(CO)NHnot availablenot availablenot available
HC(C)H-TOCSYnot availablenot availablenot available
13C-HMQC-NOESYnot availablenot availablenot available
15N-HSQC-NOESYnot availablenot availablenot available

Software:

XEASY - assignment

NMRPipe-NMRDraw - data processing

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker DRX 600 MHz
  • Bruker DRX 900 MHz

Related Database Links:

PDB
DBJ BAD92693 BAD92879 BAG10808 BAG58052
EMBL CAA34438
GB AAB60393 AAB60394 AAI07070 AAI07071 AAI17452
REF NP_005148 NP_009297 XP_001118598 XP_001166213 XP_003276793
SP P00519
AlphaFold P00519

Download HSQC peak lists in one of the following formats:
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