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Found 1 Document (1.643 seconds)

BMRB: 16349

2KK1

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

Authors

Liu, G., Wang, D., Nwosu, C., Owens, L., Xiao, R., Liu, J., Baran, M.C., Swapna, G., Acton, T.B., Rost, B., Montelione, G.T.

Assembly

Tyrosine-protein kinase ABL2

Entity

1. Tyrosine-protein kinase ABL2 (polymer, Thiol state: all free), 135 monomers, 14537.31 Da Detail

MGHHHHHHSH MANGAAGTKV ALRKTKQAAE KISADKISKE ALLECADLLS SALTEPVPNS QLVDTGHQLL DYCSGYVDCI PQTRNKFAFR EAVSKLELSL QELQVSSAAA GVPGTNPVLN NLLSCVQEIS DVVQR

Formula weight

14537.31 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

molecular dynamics, simulated annealing, distance geometry

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 99.3 %, Completeness: 93.5 %, Completeness (bb): 96.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	93.5 % (1401 of 1498)	93.1 % (719 of 772)	92.8 % (540 of 582)	98.6 % (142 of 144)
Backbone	96.5 % (772 of 800)	96.0 % (261 of 272)	96.2 % (383 of 398)	98.5 % (128 of 130)
Sidechain	91.3 % (754 of 826)	91.6 % (458 of 500)	90.4 % (282 of 312)	100.0 % (14 of 14)
Aromatic	45.6 % (31 of 68)	58.8 % (20 of 34)	32.4 % (11 of 34)
Methyl	97.6 % (162 of 166)	96.4 % (80 of 83)	98.8 % (82 of 83)

1. Tyrosine-protein kinase ABL2

MGHHHHHHSH MANGAAGTKV ALRKTKQAAE KISADKISKE ALLECADLLS SALTEPVPNS QLVDTGHQLL DYCSGYVDCI PQTRNKFAFR EAVSKLELSL QELQVSSAAA GVPGTNPVLN NLLSCVQEIS DVVQR

Show sample condition

Sample #1

Solvent system 95% H2O/5% D2O, Pressure 1.0 atm, Temperature 298 K, pH 4.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 15N]		1.2 mM
2	NACL	natural abundance		200 mM

Sample #2

Solvent system 100% D2O, Pressure 1.0 atm, Temperature 298 K, pH 4.5

#	Name	Isotope labeling	Type	Concentration
3	entity	[U-100% 13C; U-100% 15N]		1.2 mM
4	NACL	natural abundance		200 mM

Sample #3

Solvent system 95% H2O/5% D2O, Pressure 1.0 atm, Temperature 298 K, pH 4.5

#	Name	Isotope labeling	Type	Concentration
5	entity	[U-10% 13C; U-100% 15N]		1.2 mM
6	NACL	natural abundance		200 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: 0.05 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: 0.05 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: 0.03 ppm, Outliers: 1 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: 0.01 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2KK1, Strand ID: A Detail

Release date

2009-08-09

Citation

NMR structure of F-actin-binding domain of Arg/Abl2 from Homo sapiens
Liu, G., Huang, Y.J., Xiao, R., Wang, D., Acton, T.B., Montelione, G.T.
Proteins (2010), 78, 1326-1330, PubMed 20077570 , DOI 10.1002/prot.22656 , Abstract

Related entities 1. Tyrosine-protein kinase ABL2, : 1 : 16 entities Detail

Interaction partners 1. Tyrosine-protein kinase ABL2, : 31 interactors Detail

More details for 31 interactors identified by 17 citations

Experiments performed 12 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1.0 atm, Temperature 298 K, pH 4.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 15N]		1.2 mM
2	NACL	natural abundance		200 mM

2 2D 1H-13C HSQC aliphatic

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1.0 atm, Temperature 298 K, pH 4.5

#	Name	Isotope labeling	Type	Concentration
5	entity	[U-10% 13C; U-100% 15N]		1.2 mM
6	NACL	natural abundance		200 mM

3 2D 1H-13C HSQC aromatic

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1.0 atm, Temperature 298 K, pH 4.5

#	Name	Isotope labeling	Type	Concentration
5	entity	[U-10% 13C; U-100% 15N]		1.2 mM
6	NACL	natural abundance		200 mM

4 3D CBCA(CO)NH

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1.0 atm, Temperature 298 K, pH 4.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 15N]		1.2 mM
2	NACL	natural abundance		200 mM

5 3D HNCO

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1.0 atm, Temperature 298 K, pH 4.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 15N]		1.2 mM
2	NACL	natural abundance		200 mM

6 3D HNCACB

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1.0 atm, Temperature 298 K, pH 4.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 15N]		1.2 mM
2	NACL	natural abundance		200 mM

7 3D 1H-13C NOESY aliphatic

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1.0 atm, Temperature 298 K, pH 4.5

#	Name	Isotope labeling	Type	Concentration
3	entity	[U-100% 13C; U-100% 15N]		1.2 mM
4	NACL	natural abundance		200 mM

8 3D 1H-13C NOESY aromatic

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1.0 atm, Temperature 298 K, pH 4.5

#	Name	Isotope labeling	Type	Concentration
3	entity	[U-100% 13C; U-100% 15N]		1.2 mM
4	NACL	natural abundance		200 mM

9 3D HBHA(CO)NH

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1.0 atm, Temperature 298 K, pH 4.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 15N]		1.2 mM
2	NACL	natural abundance		200 mM

10 3D C(CO)NH

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1.0 atm, Temperature 298 K, pH 4.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 15N]		1.2 mM
2	NACL	natural abundance		200 mM

11 3D HCCH-TOCSY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1.0 atm, Temperature 298 K, pH 4.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 15N]		1.2 mM
2	NACL	natural abundance		200 mM

12 3D 1H-13C-15N simutaneous NOESY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1.0 atm, Temperature 298 K, pH 4.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 15N]		1.2 mM
2	NACL	natural abundance		200 mM

NMR combined restraints 6 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_16349_2kk1.nef
Input source #2: Coordindates	2kk1.cif
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

None

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100
MGHHHHHHSHMANGAAGTKVALRKTKQAAEKISADKISKEALLECADLLSSALTEPVPNSQLVDTGHQLLDYCSGYVDCIPQTRNKFAFREAVSKLELSL
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MGHHHHHHSHMANGAAGTKVALRKTKQAAEKISADKISKEALLECADLLSSALTEPVPNSQLVDTGHQLLDYCSGYVDCIPQTRNKFAFREAVSKLELSL

-------110-------120-------130-----
QELQVSSAAAGVPGTNPVLNNLLSCVQEISDVVQR
|||||||||||||||||||||||||||||||||||
QELQVSSAAAGVPGTNPVLNNLLSCVQEISDVVQR

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	135	0	0	100.0

Content subtype: combined_16349_2kk1.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1442		99.3 (chain: A, length: 135)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	4740 (1)	noe	97.8 (chain: A, length: 135)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	84 (1)	hbond	48.9 (chain: A, length: 135)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_4	OK	172 (172)	.	72.6 (chain: A, length: 135)
2	Dihedral angle restraints	DYANA/DIANA_dihedral_7	OK	172 (172)	.	72.6 (chain: A, length: 135)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 135, Sequence coverage: 99.3%
- Total number of assignments
  - ¹H chemical shifts: 750
  - ¹³C chemical shifts: 547
  - ¹⁵N chemical shifts: 145
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- Peptide bond of PRO
- Tautomeric state of HIS
- Rotameric state of ILE , LEU, and VAL
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: A

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
73	CYS	HG	2.94

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	772	749	97.0
¹³C chemical shifts	582	547	94.0
¹⁵N chemical shifts	148	145	98.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	272	268	98.5
¹³C chemical shifts	270	261	96.7
¹⁵N chemical shifts	130	127	97.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	500	481	96.2
¹³C chemical shifts	312	286	91.7
¹⁵N chemical shifts	18	18	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	85	84	98.8
¹³C chemical shifts	85	84	98.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	34	20	58.8
¹³C chemical shifts	34	11	32.4

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 135, Sequence coverage: 97.8%
- Total number of restraints: 4737
- Weight of restraints: 1.0 (4737)
- Potential type of restraints: square-well-parabolic (4737)
- Range of distance target values: 2.34, 4.81 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_3
  - Status: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 135, Sequence coverage: 48.9%
  - Total number of restraints: 84
  - Weight of restraints: 1.0 (84)
  - Potential type of restraints: square-well-parabolic (84)
  - Range of distance target values: 2.05, 2.62 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
  - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_4
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 135, Sequence coverage: 72.6%
- Total number of restraints: 172
- Total number of restraints per polymer type: 172
- Weight of restraints: 1.0 (172)
- Potential type of restraints: square-well-parabolic (172)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A
- Saveframe: DYANA/DIANA_dihedral_7
  - Status: OK
  - Experiment type: .
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 135, Sequence coverage: 72.6%
  - Total number of restraints: 172
  - Total number of restraints per polymer type: 172
  - Weight of restraints: 1.0 (172)
  - Potential type of restraints: square-well-parabolic (172)
  - Plot of Phi-Psi angle restraints
  - Dihedral angle restraints per residue
    - Chain_ID: A

Keywords F-actin binding domain, nesg, NMR, Tyrosin-protein kinase ABL2, NESG, Tyrosin protein kinase abl2

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Found 1 Document (1.643 seconds)

BMRB: 16349

Sample #1

Sample #2

Sample #3

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Tyrosine-protein kinase ABL2, : 1 : 16 entities Detail

Interaction partners 1. Tyrosine-protein kinase ABL2, : 31 interactors Detail

Experiments performed 12 experiments Detail

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NMR combined restraints 6 contents Detail