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Found 1 Document (1.266 seconds)

BMRB: 16792

2KVU

Solution NMR Structure of SAP domain of MKL/myocardin-like protein 1 from H.sapiens, Northeast Structural Genomics Consortium Target Target HR4547E

Authors

Liu, G., Janjua, J., Xiao, R., Acton, T.B., Rost, B., Montelione, G.T.

Assembly

SAP domain of MKL/myocardin-like protein 1

Entity

1. SAP domain of MKL/myocardin-like protein 1 (polymer, Thiol state: not present), 75 monomers, 8145.271 Da Detail

MGHHHHHHSH MSTPLTGKPG ALPANLDDMK VAELKQELKL RSLPVSGTKT ELIERLRAYQ DQISPVPGAP KAPAA

Formula weight

8145.271 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

molecular dynamics, distance geometry, simulated annealing, torsion angle dynamics

Data set

assigned_chemical_shifts, spectral_peak_list

Chem. Shift Complete

Sequence coverage: 85.3 %, Completeness: 77.1 %, Completeness (bb): 69.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	77.1 % (657 of 852)	84.3 % (377 of 447)	66.2 % (221 of 334)	83.1 % (59 of 71)
Backbone	69.8 % (303 of 434)	82.3 % (121 of 147)	57.7 % (127 of 220)	82.1 % (55 of 67)
Sidechain	84.8 % (414 of 488)	85.3 % (256 of 300)	83.7 % (154 of 184)	100.0 % (4 of 4)
Aromatic	16.7 % (6 of 36)	22.2 % (4 of 18)	11.1 % (2 of 18)
Methyl	100.0 % (80 of 80)	100.0 % (40 of 40)	100.0 % (40 of 40)

1. SAP domain of MKL/myocardin-like protein 1

MGHHHHHHSH MSTPLTGKPG ALPANLDDMK VAELKQELKL RSLPVSGTKT ELIERLRAYQ DQISPVPGAP KAPAA

Show sample condition

Sample #1

Solvent system 95% H2O/5% D2O, Temperature 298 K, pH 6.5, Details 1.1 mM [U-100% 13C; U-100% 15N] HR4547E, 95% H2O/5% D2O,NMR buffer pH 6.5

#	Name	Isotope labeling	Concentration
1	HR4547E	[U-100% 13C; U-100% 15N]	1.1 mM
2	H2O	natural abundance	95 %
3	D2O	natural abundance	5 %

Sample #2

Solvent system 95% H2O/5% D2O, Temperature 298 K, pH 6.5, Details 0.8 mM [U-5% 13C; U-100% 15N] HR4547E, 95% H2O/5% D2O

#	Name	Isotope labeling	Concentration
4	HR4547E	[U-10% 13C; U-100% 15N]	0.82 mM
5	H2O	natural abundance	95 %
6	D2O	natural abundance	5 %

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: 0.23 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: 0.23 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: 0.11 ppm, Outliers: 4 Detail

Protein Blocks Logo

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

Release date

2010-04-25

Related entities 1. SAP domain of MKL/myocardin-like protein 1, : 1 : 1 : 2 : 5 entities Detail

Interaction partners 1. SAP domain of MKL/myocardin-like protein 1, : 11 interactors Detail

More details for 11 interactors identified by 5 citations

Experiments performed 7 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Temperature 298 K, pH 6.5, Details 1.1 mM [U-100% 13C; U-100% 15N] HR4547E, 95% H2O/5% D2O,NMR buffer pH 6.5

#	Name	Isotope labeling	Concentration
1	HR4547E	[U-100% 13C; U-100% 15N]	1.1 mM
2	H2O	natural abundance	95 %
3	D2O	natural abundance	5 %

2 2D 1H-13C HSQC

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Temperature 298 K, pH 6.5, Details 0.8 mM [U-5% 13C; U-100% 15N] HR4547E, 95% H2O/5% D2O

#	Name	Isotope labeling	Concentration
4	HR4547E	[U-10% 13C; U-100% 15N]	0.82 mM
5	H2O	natural abundance	95 %
6	D2O	natural abundance	5 %

3 3D HNCO

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Temperature 298 K, pH 6.5, Details 1.1 mM [U-100% 13C; U-100% 15N] HR4547E, 95% H2O/5% D2O,NMR buffer pH 6.5

#	Name	Isotope labeling	Concentration
1	HR4547E	[U-100% 13C; U-100% 15N]	1.1 mM
2	H2O	natural abundance	95 %
3	D2O	natural abundance	5 %

4 3D CBCA(CO)NH

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Temperature 298 K, pH 6.5, Details 1.1 mM [U-100% 13C; U-100% 15N] HR4547E, 95% H2O/5% D2O,NMR buffer pH 6.5

#	Name	Isotope labeling	Concentration
1	HR4547E	[U-100% 13C; U-100% 15N]	1.1 mM
2	H2O	natural abundance	95 %
3	D2O	natural abundance	5 %

5 3D HNCACB

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Temperature 298 K, pH 6.5, Details 1.1 mM [U-100% 13C; U-100% 15N] HR4547E, 95% H2O/5% D2O,NMR buffer pH 6.5

#	Name	Isotope labeling	Concentration
1	HR4547E	[U-100% 13C; U-100% 15N]	1.1 mM
2	H2O	natural abundance	95 %
3	D2O	natural abundance	5 %

6 3D 1H-13C arom NOESY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Temperature 298 K, pH 6.5, Details 1.1 mM [U-100% 13C; U-100% 15N] HR4547E, 95% H2O/5% D2O,NMR buffer pH 6.5

#	Name	Isotope labeling	Concentration
1	HR4547E	[U-100% 13C; U-100% 15N]	1.1 mM
2	H2O	natural abundance	95 %
3	D2O	natural abundance	5 %

7 3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Temperature 298 K, pH 6.5, Details 1.1 mM [U-100% 13C; U-100% 15N] HR4547E, 95% H2O/5% D2O,NMR buffer pH 6.5

#	Name	Isotope labeling	Concentration
1	HR4547E	[U-100% 13C; U-100% 15N]	1.1 mM
2	H2O	natural abundance	95 %
3	D2O	natural abundance	5 %

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_16792_2kvu.nef
Input source #2: Coordindates	2kvu.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-----
MGHHHHHHSHMSTPLTGKPGALPANLDDMKVAELKQELKLRSLPVSGTKTELIERLRAYQDQISPVPGAPKAPAA
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MGHHHHHHSHMSTPLTGKPGALPANLDDMKVAELKQELKLRSLPVSGTKTELIERLRAYQDQISPVPGAPKAPAA

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	75	0	0	100.0

Content subtype: combined_16792_2kvu.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	660		85.3 (chain: A, length: 75)
1	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	2002 (1)	noe	85.3 (chain: A, length: 75)
2	Distance restraints	CNS/XPLOR_distance_constraints_4	Warning	14 (1)	hbond	16.0 (chain: A, length: 75)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_2	OK	48 (48)	.	37.3 (chain: A, length: 75)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 75, Sequence coverage: 85.3%
- Total number of assignments
  - ¹H chemical shifts: 381
  - ¹³C chemical shifts: 218
  - ¹⁵N chemical shifts: 61
- Completeness of assignments
  - Entity_assemble_ID: A
- Peptide bond of PRO
- 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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	447	381	85.2
¹³C chemical shifts	334	218	65.3
¹⁵N chemical shifts	74	61	82.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	147	123	83.7
¹³C chemical shifts	150	64	42.7
¹⁵N chemical shifts	67	55	82.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	300	258	86.0
¹³C chemical shifts	184	154	83.7
¹⁵N chemical shifts	7	6	85.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	43	41	95.3
¹³C chemical shifts	43	41	95.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	18	4	22.2
¹³C chemical shifts	18	2	11.1

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_3
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 75, Sequence coverage: 85.3%
- Total number of restraints: 2002
- Weight of restraints: 1.0 (2002)
- Potential type of restraints: square-well-parabolic (2002)
- Range of distance target values: 2.25, 4.35 (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_4
  - Status: Warning
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 75, Sequence coverage: 16.0%
  - Total number of restraints: 14
  - Weight of restraints: 1.0 (14)
  - Potential type of restraints: square-well-parabolic (14)
  - 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_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 75, Sequence coverage: 37.3%
- Total number of restraints: 48
- Total number of restraints per polymer type: 48
- Weight of restraints: 1.0 (48)
- Potential type of restraints: square-well-parabolic (48)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue

Keywords Megakaryoblastic leukemia, Myocardin, SAP, leukemia, ranscription factor, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG), PSI-2, Protein NMR, Protein Structure Initiative, Structural Genomics, Target HR4547E

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Found 1 Document (1.266 seconds)

BMRB: 16792

Sample #1

Sample #2

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. SAP domain of MKL/myocardin-like protein 1, : 1 : 1 : 2 : 5 entities Detail

Interaction partners 1. SAP domain of MKL/myocardin-like protein 1, : 11 interactors Detail

Experiments performed 7 experiments Detail

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Sample

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NMR combined restraints 5 contents Detail