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 16349

Title: SOLUTION STRUCTURE OF C-terminal Domain of Tyrosine-protein kinase ABL2 FROM HOMO SAPIENS, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET HR5537A   PubMed: 20077570

Authors: Liu, Gaohua; Wang, Dongyang; Nwosu, Chioma; Owens, Leah; Xiao, Rong; Liu, Jinfeng; Baran, Micheal; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano

Citation: Liu, Gaohua; Huang, Yuanpeng; Xiao, Rong; Wang, Dongyan; Acton, Thomas; Montelione, Gaetano. "NMR structure of F-actin-binding domain of Arg/Abl2 from Homo sapiens."  Proteins 78, 1326-1330 (2010).

Assembly members:
Tyrosine-protein kinase ABL2, polymer, 135 residues, 14557.594 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

Entity Sequences (FASTA):
Tyrosine-protein kinase ABL2: MGHHHHHHSHMANGAAGTKV ALRKTKQAAEKISADKISKE ALLECADLLSSALTEPVPNS QLVDTGHQLLDYCSGYVDCI PQTRNKFAFREAVSKLELSL QELQVSSAAAGVPGTNPVLN NLLSCVQEISDVVQR

Data sets:
Data typeCount
13C chemical shifts547
15N chemical shifts145
1H chemical shifts918

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Tyrosine-protein kinase ABL21

Entities:

Entity 1, Tyrosine-protein kinase ABL2 135 residues - 14557.594 Da.

1   METGLYHISHISHISHISHISHISSERHIS
2   METALAASNGLYALAALAGLYTHRLYSVAL
3   ALALEUARGLYSTHRLYSGLNALAALAGLU
4   LYSILESERALAASPLYSILESERLYSGLU
5   ALALEULEUGLUCYSALAASPLEULEUSER
6   SERALALEUTHRGLUPROVALPROASNSER
7   GLNLEUVALASPTHRGLYHISGLNLEULEU
8   ASPTYRCYSSERGLYTYRVALASPCYSILE
9   PROGLNTHRARGASNLYSPHEALAPHEARG
10   GLUALAVALSERLYSLEUGLULEUSERLEU
11   GLNGLULEUGLNVALSERSERALAALAALA
12   GLYVALPROGLYTHRASNPROVALLEUASN
13   ASNLEULEUSERCYSVALGLNGLUILESER
14   ASPVALVALGLNARG

Samples:

sample_1: entity, [U-100% 15N], 1.2 mM; NACL 200 mM

sample_2: entity, [U-100% 13C; U-100% 15N], 1.2 mM; NACL 200 mM

sample_3: entity, [U-10% 13C; U-100% 15N], 1.2 mM; NACL 200 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 4.5; pressure: 1.0 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C-15N simutaneous NOESYsample_1isotropicsample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinement, structure solution

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis, refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, data analysis

XEASY v1.3, Bartels et al. - chemical shift assignment, data analysis, peak picking

NMRPipe v1.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMRJ v1.3, Varian - collection

TOPSPIN v1.3, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
EMBL CAD98092
GB AAA35553 AAH65912 AAY16984 ACK76601 ACK76602
REF NP_001129472 NP_001161708 NP_001161709 NP_001161710 NP_001161711
SP P42684