BMRB Entry 16349
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16349
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Title: SOLUTION STRUCTURE OF C-terminal Domain of Tyrosine-protein kinase ABL2 FROM HOMO SAPIENS, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET HR5537A PubMed: 20077570
Deposition date: 2009-06-14 Original release date: 2009-08-10
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
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 547 |
| 15N chemical shifts | 145 |
| 1H chemical shifts | 918 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Tyrosine-protein kinase ABL2 | 1 |
Entities:
Entity 1, Tyrosine-protein kinase ABL2 135 residues - 14557.594 Da.
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | SER | HIS | ||||
| 2 | MET | ALA | ASN | GLY | ALA | ALA | GLY | THR | LYS | VAL | ||||
| 3 | ALA | LEU | ARG | LYS | THR | LYS | GLN | ALA | ALA | GLU | ||||
| 4 | LYS | ILE | SER | ALA | ASP | LYS | ILE | SER | LYS | GLU | ||||
| 5 | ALA | LEU | LEU | GLU | CYS | ALA | ASP | LEU | LEU | SER | ||||
| 6 | SER | ALA | LEU | THR | GLU | PRO | VAL | PRO | ASN | SER | ||||
| 7 | GLN | LEU | VAL | ASP | THR | GLY | HIS | GLN | LEU | LEU | ||||
| 8 | ASP | TYR | CYS | SER | GLY | TYR | VAL | ASP | CYS | ILE | ||||
| 9 | PRO | GLN | THR | ARG | ASN | LYS | PHE | ALA | PHE | ARG | ||||
| 10 | GLU | ALA | VAL | SER | LYS | LEU | GLU | LEU | SER | LEU | ||||
| 11 | GLN | GLU | LEU | GLN | VAL | SER | SER | ALA | ALA | ALA | ||||
| 12 | GLY | VAL | PRO | GLY | THR | ASN | PRO | VAL | LEU | ASN | ||||
| 13 | ASN | LEU | LEU | SER | CYS | VAL | GLN | GLU | ILE | SER | ||||
| 14 | ASP | VAL | VAL | GLN | ARG |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_3 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C-15N simutaneous NOESY | sample_1 | isotropic | sample_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 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts