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BMRB: 25548

2N16

structure of a peptide

Authors

Heddi, B., Cheong, V.V.V., Martadinata, H., Phan, A.A.T.

Assembly

DHX36

Entity

1. DHX36 (polymer, Thiol state: not present), 20 monomers, 2354.752 Da Detail

SMHPGHLKGR EIGMWYAKKQ

Formula weight

2354.752 Da

Source organism

Exptl. method

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 95.0 %, Completeness: 76.0 %, Completeness (bb): 88.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	76.0 % (190 of 250)	71.6 % (96 of 134)	81.1 % (77 of 95)	81.0 % (17 of 21)
Backbone	88.1 % (104 of 118)	83.3 % (35 of 42)	91.2 % (52 of 57)	89.5 % (17 of 19)
Sidechain	68.5 % (102 of 149)	66.3 % (61 of 92)	74.5 % (41 of 55)	0.0 % (0 of 2)
Aromatic	35.7 % (10 of 28)	50.0 % (7 of 14)	23.1 % (3 of 13)	0.0 % (0 of 1)
Methyl	80.0 % (8 of 10)	60.0 % (3 of 5)	100.0 % (5 of 5)

1. entity

SMHPGHLKGR EIGMWYAKKQ

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 288 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 13C; U-100% 15N]	protein	0.1 ~ 1.0 mM
2	potassium chloride	natural abundance	salt	10.0 ~ 70.0 mM
3	potassium phosphate	natural abundance	buffer	10.0 ~ 20.0 mM
4	H2O	natural abundance	solvent	90 %
5	D2O	[U-2H]	solvent	10 %

Protein Blocks Logo

Calculated from 10 models in PDB: 2N16, Strand ID: A Detail

Release date

2015-07-26

Citation

Insights into G-quadruplex specific recognition by the DEAH-box helicase RHAU: Solution structure of a peptide-quadruplex complex
Heddi, B., Cheong, V.V.V., Martadinata, H., Phan, A.A.T.
Proc. Natl. Acad. Sci. U. S. A. (2015), 112, 9608-9613, PubMed 26195789 , DOI 10.1073/pnas.1422605112 , Abstract

Related entities 1. DHX36, : 4 entities Detail

Experiments performed 11 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 288 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 13C; U-100% 15N]	protein	0.1 ~ 1.0 mM
2	potassium chloride	natural abundance	salt	10.0 ~ 70.0 mM
3	potassium phosphate	natural abundance	buffer	10.0 ~ 20.0 mM
4	H2O	natural abundance	solvent	90 %
5	D2O	[U-2H]	solvent	10 %

2 3D CBCA(CO)NH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 288 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 13C; U-100% 15N]	protein	0.1 ~ 1.0 mM
2	potassium chloride	natural abundance	salt	10.0 ~ 70.0 mM
3	potassium phosphate	natural abundance	buffer	10.0 ~ 20.0 mM
4	H2O	natural abundance	solvent	90 %
5	D2O	[U-2H]	solvent	10 %

3 3D HNCO

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 288 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 13C; U-100% 15N]	protein	0.1 ~ 1.0 mM
2	potassium chloride	natural abundance	salt	10.0 ~ 70.0 mM
3	potassium phosphate	natural abundance	buffer	10.0 ~ 20.0 mM
4	H2O	natural abundance	solvent	90 %
5	D2O	[U-2H]	solvent	10 %

4 3D HNCACB

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 288 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 13C; U-100% 15N]	protein	0.1 ~ 1.0 mM
2	potassium chloride	natural abundance	salt	10.0 ~ 70.0 mM
3	potassium phosphate	natural abundance	buffer	10.0 ~ 20.0 mM
4	H2O	natural abundance	solvent	90 %
5	D2O	[U-2H]	solvent	10 %

5 2D 1H-13C HSQC aliphatic

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 288 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 13C; U-100% 15N]	protein	0.1 ~ 1.0 mM
2	potassium chloride	natural abundance	salt	10.0 ~ 70.0 mM
3	potassium phosphate	natural abundance	buffer	10.0 ~ 20.0 mM
4	H2O	natural abundance	solvent	90 %
5	D2O	[U-2H]	solvent	10 %

6 3D C(CO)NH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 288 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 13C; U-100% 15N]	protein	0.1 ~ 1.0 mM
2	potassium chloride	natural abundance	salt	10.0 ~ 70.0 mM
3	potassium phosphate	natural abundance	buffer	10.0 ~ 20.0 mM
4	H2O	natural abundance	solvent	90 %
5	D2O	[U-2H]	solvent	10 %

7 3D HCCH-TOCSY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 288 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 13C; U-100% 15N]	protein	0.1 ~ 1.0 mM
2	potassium chloride	natural abundance	salt	10.0 ~ 70.0 mM
3	potassium phosphate	natural abundance	buffer	10.0 ~ 20.0 mM
4	H2O	natural abundance	solvent	90 %
5	D2O	[U-2H]	solvent	10 %

8 3D HNHA

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 288 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 13C; U-100% 15N]	protein	0.1 ~ 1.0 mM
2	potassium chloride	natural abundance	salt	10.0 ~ 70.0 mM
3	potassium phosphate	natural abundance	buffer	10.0 ~ 20.0 mM
4	H2O	natural abundance	solvent	90 %
5	D2O	[U-2H]	solvent	10 %

9 3D 1H-15N NOESY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 288 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 13C; U-100% 15N]	protein	0.1 ~ 1.0 mM
2	potassium chloride	natural abundance	salt	10.0 ~ 70.0 mM
3	potassium phosphate	natural abundance	buffer	10.0 ~ 20.0 mM
4	H2O	natural abundance	solvent	90 %
5	D2O	[U-2H]	solvent	10 %

10 3D 1H-13C NOESY aliphatic

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 288 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 13C; U-100% 15N]	protein	0.1 ~ 1.0 mM
2	potassium chloride	natural abundance	salt	10.0 ~ 70.0 mM
3	potassium phosphate	natural abundance	buffer	10.0 ~ 20.0 mM
4	H2O	natural abundance	solvent	90 %
5	D2O	[U-2H]	solvent	10 %

11 3D H(CCO)NH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 288 K, pH 6.5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-100% 13C; U-100% 15N]	protein	0.1 ~ 1.0 mM
2	potassium chloride	natural abundance	salt	10.0 ~ 70.0 mM
3	potassium phosphate	natural abundance	buffer	10.0 ~ 20.0 mM
4	H2O	natural abundance	solvent	90 %
5	D2O	[U-2H]	solvent	10 %

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_25548_2n16.nef
Input source #2: Coordindates	2n16.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
SMHPGHLKGREIGMWYAKKQ
||||||||||||||||||||
SMHPGHLKGREIGMWYAKKQ

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	20	0	0	100.0

Content subtype: combined_25548_2n16.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	OK	201		95.0 (chain: A, length: 20)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	OK	186 (1)	noe	85.0 (chain: A, length: 20)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_3	OK	180 (180)	.	95.0 (chain: A, length: 20)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 20, Sequence coverage: 95.0%
- Total number of assignments
  - ¹H chemical shifts: 107
  - ¹³C chemical shifts: 77
  - ¹⁵N chemical shifts: 17
- 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

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 20, Sequence coverage: 85.0%
- Total number of restraints: 186
- Weight of restraints: 1.0 (186)
- Potential type of restraints: upper-bound-parabolic (186)
- Range of distance target values: 2.56, 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

Dihedral angle restraints

Saveframe: DYANA/DIANA_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 20, Sequence coverage: 95.0%
- Total number of restraints: 180
- Total number of restraints per polymer type: 180
- Weight of restraints: 1.0 (180)
- Potential type of restraints: square-well-parabolic (180)
- Plot of Phi-Psi angle restraints
- Plot of Chi1-Chi2 angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords peptide