BMRB Entry 16349

Name: SOLUTION STRUCTURE OF C-terminal Domain of Tyrosine-protein kinase ABL2 FROM HOMO SAPIENS, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET HR5537A
Published: 2009-08-10

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PDB ID: 2kk1
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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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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

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:

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).
PubMed: 20077570

Assembly members:

Assembly members:
Tyrosine-protein kinase ABL2, polymer, 135 residues, 14557.594 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: pET 14-15C

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	547
15N chemical shifts	145
1H chemical shifts	918

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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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

SER

HIS

2

MET

ALA

ASN

GLY

ALA

GLY

THR

LYS

VAL

3

ALA

LEU

ARG

LYS

THR

LYS

GLN

ALA

GLU

4

LYS

ILE

SER

ALA

ASP

LYS

ILE

SER

LYS

GLU

5

ALA

LEU

GLU

CYS

ALA

ASP

LEU

SER

6

SER

ALA

LEU

THR

GLU

PRO

VAL

PRO

ASN

SER

7

GLN

LEU

VAL

ASP

THR

GLY

HIS

GLN

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

ALA

12

GLY

VAL

PRO

GLY

THR

ASN

PRO

VAL

LEU

ASN

13

ASN

LEU

SER

CYS

VAL

GLN

GLU

ILE

SER

14

ASP

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

PDB	2KK1
EMBL	CAD98092
GB	AAA35553 AAH65912 AAY16984 ACK76601 ACK76602
REF	NP_001129472 NP_001161708 NP_001161709 NP_001161710 NP_001161711
SP	P42684
AlphaFold	P42684