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BMRB: 25834

2N84

Solution structure of the FHA domain of TbPar42

Authors

Rehic, E., Bayer, P.

Assembly

FHA domain of TbPar42

Entity

1. FHA domain of TbPar42 (polymer, Thiol state: all free), 179 monomers, 19264.20 Da Detail

GPMVTSTGLL SRVAAVEKAA EIAKPPPPKV VELTEAAKQL PQHIIGVTDP TKLNAQVSYF QCPPWAALPS VACHLQCTRD GLPLPALGLH RFPFYLFGRS KVCDYVLEHP SISSVHAVLV FHGGQRCFVL MDLGSTNGVK LNGNRIEKRR PLPAPVGSSI QFGFSSRVYK VQLGPPSSS

Formula weight

19264.2 Da

Source organism

Trypanosoma brucei

Exptl. method

solution NMR

Refine. method

torsion angle dynamics, simulated annealing, molecular dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 97.8 %, Completeness: 91.8 %, Completeness (bb): 94.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	91.8 % (1888 of 2057)	91.8 % (981 of 1069)	90.2 % (735 of 815)	99.4 % (172 of 173)
Backbone	94.3 % (977 of 1036)	94.9 % (335 of 353)	92.4 % (483 of 523)	99.4 % (159 of 160)
Sidechain	90.3 % (1071 of 1186)	90.2 % (646 of 716)	90.2 % (412 of 457)	100.0 % (13 of 13)
Aromatic	79.7 % (118 of 148)	86.5 % (64 of 74)	72.6 % (53 of 73)	100.0 % (1 of 1)
Methyl	100.0 % (214 of 214)	100.0 % (107 of 107)	100.0 % (107 of 107)

1. entity

GPMVTSTGLL SRVAAVEKAA EIAKPPPPKV VELTEAAKQL PQHIIGVTDP TKLNAQVSYF QCPPWAALPS VACHLQCTRD GLPLPALGLH RFPFYLFGRS KVCDYVLEHP SISSVHAVLV FHGGQRCFVL MDLGSTNGVK LNGNRIEKRR PLPAPVGSSI QFGFSSRVYK VQLGPPSSS

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Temperature 300.15 K, pH 6.23

#	Name	Isotope labeling	Concentration
1	15N13C FHA domain in 50mM KPiBuffer+2mM DTT	[U-13C; U-15N]	0.6 mM
2	KPiBuffer	natural abundance	50 mM
3	DTT	natural abundance	2 mM
4	D2O	natural abundance	10 %
5	H2O	natural abundance	90 %

Sample #2

Solvent system 90% H2O/10% D2O, Temperature 300.15 K, pH 6.23

#	Name	Isotope labeling	Concentration
6	15N FHA domain in 50mM KpiBuffer+2mM DTT	[U-15N]	1mM mM
7	KPiBuffer	natural abundance	50 mM
8	DTT	natural abundance	2 mM
9	D2O	natural abundance	10 %
10	H2O	natural abundance	90 %

Sample #3

Solvent system 100% D2O, Temperature 300.15 K, pH 6.23

#	Name	Isotope labeling	Concentration
11	13C FHA domain in 50mM KpiBuffer+2mM DTT	[U-13C]	0.6 mM
12	KPiBuffer	natural abundance	50 mM
13	DTT	natural abundance	2 mM
14	D2O	natural abundance	100 %

Sample #4

Solvent system 50 mMKPi Buffer + 2mM DTT, Temperature 300.15 K, pH 6.23

#	Name	Isotope labeling	Concentration
15	FHA domain in 50mM KPiBuffer+2mM DTT	natural abundance	1 mM
16	KPiBuffer	natural abundance	50 mM
17	DTT	natural abundance	2 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: -0.12 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: -0.12 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: 0.05 ppm, Outliers: 3 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: 0.39 ppm, Outliers: 5 Detail

Protein Blocks Logo

Calculated from 10 models in PDB: 2N84, Strand ID: A Detail

Release date

2016-10-05

Citation

Solution structure of the FHA domain of TbPar42
Rehic, E., Bayer, P.
Not known

Related entities 1. FHA domain of TbPar42, : 10 entities Detail

Experiments performed 20 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Temperature 300.15 K, pH 6.23

#	Name	Isotope labeling	Concentration
6	15N FHA domain in 50mM KpiBuffer+2mM DTT	[U-15N]	1mM mM
7	KPiBuffer	natural abundance	50 mM
8	DTT	natural abundance	2 mM
9	D2O	natural abundance	10 %
10	H2O	natural abundance	90 %

2 2D 1H-13C HSQC aliphatic

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 100% D2O, Temperature 300.15 K, pH 6.23

#	Name	Isotope labeling	Concentration
11	13C FHA domain in 50mM KpiBuffer+2mM DTT	[U-13C]	0.6 mM
12	KPiBuffer	natural abundance	50 mM
13	DTT	natural abundance	2 mM
14	D2O	natural abundance	100 %

3 2D 1H-1H COSY

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 50 mMKPi Buffer + 2mM DTT, Temperature 300.15 K, pH 6.23

#	Name	Isotope labeling	Concentration
15	FHA domain in 50mM KPiBuffer+2mM DTT	natural abundance	1 mM
16	KPiBuffer	natural abundance	50 mM
17	DTT	natural abundance	2 mM

4 2D 1H-1H TOCSY

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 50 mMKPi Buffer + 2mM DTT, Temperature 300.15 K, pH 6.23

#	Name	Isotope labeling	Concentration
15	FHA domain in 50mM KPiBuffer+2mM DTT	natural abundance	1 mM
16	KPiBuffer	natural abundance	50 mM
17	DTT	natural abundance	2 mM

5 2D 1H-1H NOESY

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 50 mMKPi Buffer + 2mM DTT, Temperature 300.15 K, pH 6.23

#	Name	Isotope labeling	Concentration
15	FHA domain in 50mM KPiBuffer+2mM DTT	natural abundance	1 mM
16	KPiBuffer	natural abundance	50 mM
17	DTT	natural abundance	2 mM

6 3D CBCA(CO)NH

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Temperature 300.15 K, pH 6.23

#	Name	Isotope labeling	Concentration
1	15N13C FHA domain in 50mM KPiBuffer+2mM DTT	[U-13C; U-15N]	0.6 mM
2	KPiBuffer	natural abundance	50 mM
3	DTT	natural abundance	2 mM
4	D2O	natural abundance	10 %
5	H2O	natural abundance	90 %

7 3D HNCACB

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Temperature 300.15 K, pH 6.23

#	Name	Isotope labeling	Concentration
1	15N13C FHA domain in 50mM KPiBuffer+2mM DTT	[U-13C; U-15N]	0.6 mM
2	KPiBuffer	natural abundance	50 mM
3	DTT	natural abundance	2 mM
4	D2O	natural abundance	10 %
5	H2O	natural abundance	90 %

8 3D HBHA(CO)NH

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Temperature 300.15 K, pH 6.23

#	Name	Isotope labeling	Concentration
1	15N13C FHA domain in 50mM KPiBuffer+2mM DTT	[U-13C; U-15N]	0.6 mM
2	KPiBuffer	natural abundance	50 mM
3	DTT	natural abundance	2 mM
4	D2O	natural abundance	10 %
5	H2O	natural abundance	90 %

9 3D HNHA

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Temperature 300.15 K, pH 6.23

#	Name	Isotope labeling	Concentration
1	15N13C FHA domain in 50mM KPiBuffer+2mM DTT	[U-13C; U-15N]	0.6 mM
2	KPiBuffer	natural abundance	50 mM
3	DTT	natural abundance	2 mM
4	D2O	natural abundance	10 %
5	H2O	natural abundance	90 %

10 3D HN(CO)CA

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Temperature 300.15 K, pH 6.23

#	Name	Isotope labeling	Concentration
1	15N13C FHA domain in 50mM KPiBuffer+2mM DTT	[U-13C; U-15N]	0.6 mM
2	KPiBuffer	natural abundance	50 mM
3	DTT	natural abundance	2 mM
4	D2O	natural abundance	10 %
5	H2O	natural abundance	90 %

11 3D HCACO

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Temperature 300.15 K, pH 6.23

#	Name	Isotope labeling	Concentration
1	15N13C FHA domain in 50mM KPiBuffer+2mM DTT	[U-13C; U-15N]	0.6 mM
2	KPiBuffer	natural abundance	50 mM
3	DTT	natural abundance	2 mM
4	D2O	natural abundance	10 %
5	H2O	natural abundance	90 %

12 3D HNCO

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Temperature 300.15 K, pH 6.23

#	Name	Isotope labeling	Concentration
1	15N13C FHA domain in 50mM KPiBuffer+2mM DTT	[U-13C; U-15N]	0.6 mM
2	KPiBuffer	natural abundance	50 mM
3	DTT	natural abundance	2 mM
4	D2O	natural abundance	10 %
5	H2O	natural abundance	90 %

13 2D 1H-13C HSQC aromatic

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Temperature 300.15 K, pH 6.23

#	Name	Isotope labeling	Concentration
1	15N13C FHA domain in 50mM KPiBuffer+2mM DTT	[U-13C; U-15N]	0.6 mM
2	KPiBuffer	natural abundance	50 mM
3	DTT	natural abundance	2 mM
4	D2O	natural abundance	10 %
5	H2O	natural abundance	90 %

14 3D C(CO)NH

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Temperature 300.15 K, pH 6.23

#	Name	Isotope labeling	Concentration
1	15N13C FHA domain in 50mM KPiBuffer+2mM DTT	[U-13C; U-15N]	0.6 mM
2	KPiBuffer	natural abundance	50 mM
3	DTT	natural abundance	2 mM
4	D2O	natural abundance	10 %
5	H2O	natural abundance	90 %

15 3D H(CCO)NH

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Temperature 300.15 K, pH 6.23

#	Name	Isotope labeling	Concentration
1	15N13C FHA domain in 50mM KPiBuffer+2mM DTT	[U-13C; U-15N]	0.6 mM
2	KPiBuffer	natural abundance	50 mM
3	DTT	natural abundance	2 mM
4	D2O	natural abundance	10 %
5	H2O	natural abundance	90 %

16 3D HCCH-COSY

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 100% D2O, Temperature 300.15 K, pH 6.23

#	Name	Isotope labeling	Concentration
11	13C FHA domain in 50mM KpiBuffer+2mM DTT	[U-13C]	0.6 mM
12	KPiBuffer	natural abundance	50 mM
13	DTT	natural abundance	2 mM
14	D2O	natural abundance	100 %

17 3D HCCH-TOCSY

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 100% D2O, Temperature 300.15 K, pH 6.23

#	Name	Isotope labeling	Concentration
11	13C FHA domain in 50mM KpiBuffer+2mM DTT	[U-13C]	0.6 mM
12	KPiBuffer	natural abundance	50 mM
13	DTT	natural abundance	2 mM
14	D2O	natural abundance	100 %

18 3D 1H-13C NOESY aromatic

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 100% D2O, Temperature 300.15 K, pH 6.23

#	Name	Isotope labeling	Concentration
11	13C FHA domain in 50mM KpiBuffer+2mM DTT	[U-13C]	0.6 mM
12	KPiBuffer	natural abundance	50 mM
13	DTT	natural abundance	2 mM
14	D2O	natural abundance	100 %

19 3D 1H-15N TOCSY

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Temperature 300.15 K, pH 6.23

#	Name	Isotope labeling	Concentration
6	15N FHA domain in 50mM KpiBuffer+2mM DTT	[U-15N]	1mM mM
7	KPiBuffer	natural abundance	50 mM
8	DTT	natural abundance	2 mM
9	D2O	natural abundance	10 %
10	H2O	natural abundance	90 %

20 3D 1H-15N NOESY

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Temperature 300.15 K, pH 6.23

#	Name	Isotope labeling	Concentration
6	15N FHA domain in 50mM KpiBuffer+2mM DTT	[U-15N]	1mM mM
7	KPiBuffer	natural abundance	50 mM
8	DTT	natural abundance	2 mM
9	D2O	natural abundance	10 %
10	H2O	natural abundance	90 %

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_25834_2n84.nef
Input source #2: Coordindates	2n84.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

-0--------10--------20--------30--------40--------50--------60--------70--------80--------90-------1
GPMVTSTGLLSRVAAVEKAAEIAKPPPPKVVELTEAAKQLPQHIIGVTDPTKLNAQVSYFQCPPWAALPSVACHLQCTRDGLPLPALGLHRFPFYLFGRS
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
GPMVTSTGLLSRVAAVEKAAEIAKPPPPKVVELTEAAKQLPQHIIGVTDPTKLNAQVSYFQCPPWAALPSVACHLQCTRDGLPLPALGLHRFPFYLFGRS
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100

00-------110-------120-------130-------140-------150-------160-------170-------
KVCDYVLEHPSISSVHAVLVFHGGQRCFVLMDLGSTNGVKLNGNRIEKRRPLPAPVGSSIQFGFSSRVYKVQLGPPSSS
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
KVCDYVLEHPSISSVHAVLVFHGGQRCFVLMDLGSTNGVKLNGNRIEKRRPLPAPVGSSIQFGFSSRVYKVQLGPPSSS
-------110-------120-------130-------140-------150-------160-------170---------

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	179	0	0	100.0

Content subtype: combined_25834_2n84.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1864		96.1 (chain: A, length: 179)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	Warning	2587 (1)	noe	96.1 (chain: A, length: 179)
2	Distance restraints	DYANA/DIANA_distance_constraints_4	Warning	168 (1)	hbond	29.6 (chain: A, length: 179)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_3	OK	1455 (1455)	.	94.4 (chain: A, length: 179)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 179, Sequence coverage: 96.1%
- Total number of assignments
  - ¹H chemical shifts: 968
  - ¹³C chemical shifts: 724
  - ¹⁵N chemical shifts: 172
- 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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	1069	968	90.6
¹³C chemical shifts	815	724	88.8
¹⁵N chemical shifts	182	172	94.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	353	336	95.2
¹³C chemical shifts	358	318	88.8
¹⁵N chemical shifts	160	159	99.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	716	632	88.3
¹³C chemical shifts	457	406	88.8
¹⁵N chemical shifts	22	13	59.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	109	107	98.2
¹³C chemical shifts	109	107	98.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	74	64	86.5
¹³C chemical shifts	73	53	72.6
¹⁵N chemical shifts	1	1	100.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 179, Sequence coverage: 96.1%
- Total number of restraints: 2579
- Weight of restraints: 1.0 (2579)
- Potential type of restraints: upper-bound-parabolic (2579)
- Range of distance target values: 2.4, 5.5 (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: DYANA/DIANA_distance_constraints_4
  - Status: Warning
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 179, Sequence coverage: 29.6%
  - Total number of restraints: 168
  - Weight of restraints: 1.0 (168)
  - Potential type of restraints: upper-bound-parabolic (168)
  - Range of distance target values: 1.7, 3.5 (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

Dihedral angle restraints

Saveframe: DYANA/DIANA_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 179, Sequence coverage: 94.4%
- Total number of restraints: 1455
- Total number of restraints per polymer type: 1455
- Weight of restraints: 1.0 (1455)
- Potential type of restraints: square-well-parabolic (1455)
- Plot of Phi-Psi angle restraints
- Plot of Chi1-Chi2 angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords FHA domain, TbPar42, Trypanosoma brucei, parvulin, protein

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Found 1 Document (0.78 seconds)

BMRB: 25834

Sample #1

Sample #2

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Sample #4

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. FHA domain of TbPar42, : 10 entities Detail

Experiments performed 20 experiments Detail

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NMR combined restraints 5 contents Detail