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BMRB: 18617

2LWA

Conformational ensemble for the G8A mutant of the influenza hemagglutinin fusion peptide

Authors

Lorieau, J.L., Louis, J.M., Schwieters, C.D., Bax, A.

Assembly

G8A mutant of the influenza hemagglutinin fusion peptide

Entity

1. G8A mutant of the influenza hemagglutinin fusion peptide (polymer, Thiol state: not present), 30 monomers, 3161.587 × 3 Da Detail

GLFGAIAAFI EGGWTGMIDG WYGSGKKKKD

Total weight

9484.761 Da

Max. entity weight

3161.587 Da

Source organism

Influenza A virus

Exptl. method

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 80.0 %, Completeness: 32.2 %, Completeness (bb): 57.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	32.2 % (110 of 342)	31.3 % (55 of 176)	24.6 % (33 of 134)	68.8 % (22 of 32)
Backbone	57.8 % (104 of 180)	77.9 % (53 of 68)	35.4 % (29 of 82)	73.3 % (22 of 30)
Sidechain	4.3 % (8 of 184)	1.9 % (2 of 108)	8.1 % (6 of 74)	0.0 % (0 of 2)
Aromatic	0.0 % (0 of 52)	0.0 % (0 of 26)	0.0 % (0 of 24)	0.0 % (0 of 2)
Methyl	8.3 % (2 of 24)	8.3 % (1 of 12)	8.3 % (1 of 12)

1. Hemagglutinin Fusion Peptide G8A mutant

GLFGAIAAFI EGGWTGMIDG WYGSGKKKKD

Show sample condition

Sample

Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 305.0 (±0.1) K, pH 7.3 (±0.1), Details pH 7.3

#	Name	Isotope labeling	Type	Concentration
1	Hemagglutinin Fusion Peptide G8A mutant	[U-100% 13C; U-100% 15N]		0.3 ~ 0.6 (±0.1) mM
2	TRIS	natural abundance		25 mM
3	DPC	[U-100% 2H]		130.0 ~ 160.0 mM
4	D2O	natural abundance		7 %
5	H2O	natural abundance		93 %

Protein Blocks Logo

Calculated from 20 models in PDB: 2LWA, Strand ID: A, B, C Detail

Heteronucl. T₁

42 T₁ values in 2 lists
Coherence Sz, Field strength (¹H) 600 MHz, 900 MHz, Pressure 1 atm, Temperature 305.0 (±0.1) K, pH 7.4 (±0.1) Detail

Heteronucl. T₂

42 T₂ values in 2 lists
Coherence I(+,-), Field strength (¹H) 600 MHz, 900 MHz, Pressure 1 atm, Temperature 305.0 (±0.1) K, pH 7.4 (±0.1) Detail

Heteronucl. NOE

21 NOE values in 1 lists
Value type relative intensities, Field strength (¹H) 500 MHz, Pressure 1 atm, Temperature 305.0 (±0.1) K, pH 7.4 (±0.1) Detail

Heteronucl. T₁/T₂

42 T₁/T₂ values in 2 lists
Field strength (¹H) 600 MHz, 900 MHz, Pressure 1 atm, Temperature 305.0 (±0.1) K, pH 7.4 (±0.1) Detail

Release date

2012-12-03

Citation

pH-triggered, activated-state conformations of the influenza hemagglutinin fusion peptide revealed by NMR
Lorieau, J.L., Louis, J.M., Schwieters, C.D., Bax, A.
Proc. Natl. Acad. Sci. U. S. A. (2012), 109, 19994-19999, PubMed 23169643 , DOI 10.1073/pnas.1213801109 , Abstract

Related entities 1. G8A mutant of the influenza hemagglutinin fusion peptide, : 1 : 1 : 2 entities Detail

Experiments performed 5 experiments Detail

1 2D 1H-13C HSQC

Instrument

Bruker Avance - 750 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 305.0 (±0.1) K, pH 7.3 (±0.1), Details pH 7.3

#	Name	Isotope labeling	Type	Concentration
1	Hemagglutinin Fusion Peptide G8A mutant	[U-100% 13C; U-100% 15N]		0.3 ~ 0.6 (±0.1) mM
2	TRIS	natural abundance		25 mM
3	DPC	[U-100% 2H]		130.0 ~ 160.0 mM
4	D2O	natural abundance		7 %
5	H2O	natural abundance		93 %

2 2D 1H-15N HSQC

Instrument

Bruker Avance - 900 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 305.0 (±0.1) K, pH 7.3 (±0.1), Details pH 7.3

#	Name	Isotope labeling	Type	Concentration
1	Hemagglutinin Fusion Peptide G8A mutant	[U-100% 13C; U-100% 15N]		0.3 ~ 0.6 (±0.1) mM
2	TRIS	natural abundance		25 mM
3	DPC	[U-100% 2H]		130.0 ~ 160.0 mM
4	D2O	natural abundance		7 %
5	H2O	natural abundance		93 %

3 3D HNCA

Instrument

Bruker Avance - 500 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 305.0 (±0.1) K, pH 7.3 (±0.1), Details pH 7.3

#	Name	Isotope labeling	Type	Concentration
1	Hemagglutinin Fusion Peptide G8A mutant	[U-100% 13C; U-100% 15N]		0.3 ~ 0.6 (±0.1) mM
2	TRIS	natural abundance		25 mM
3	DPC	[U-100% 2H]		130.0 ~ 160.0 mM
4	D2O	natural abundance		7 %
5	H2O	natural abundance		93 %

4 3D 1H-15N NOESY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 305.0 (±0.1) K, pH 7.3 (±0.1), Details pH 7.3

#	Name	Isotope labeling	Type	Concentration
1	Hemagglutinin Fusion Peptide G8A mutant	[U-100% 13C; U-100% 15N]		0.3 ~ 0.6 (±0.1) mM
2	TRIS	natural abundance		25 mM
3	DPC	[U-100% 2H]		130.0 ~ 160.0 mM
4	D2O	natural abundance		7 %
5	H2O	natural abundance		93 %

5 2D 1H-1H NOESY

Instrument

Bruker Avance - 900 MHz

Sample

State isotropic, Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 305.0 (±0.1) K, pH 7.3 (±0.1), Details pH 7.3

#	Name	Isotope labeling	Type	Concentration
1	Hemagglutinin Fusion Peptide G8A mutant	[U-100% 13C; U-100% 15N]		0.3 ~ 0.6 (±0.1) mM
2	TRIS	natural abundance		25 mM
3	DPC	[U-100% 2H]		130.0 ~ 160.0 mM
4	D2O	natural abundance		7 %
5	H2O	natural abundance		93 %

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints, RDC restraints	combined_18617_2lwa.nef
Input source #2: Coordindates	2lwa.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
GLFGAIAAFIEGGWTGMIDGWYGSGKKKKD
||||||||||||||||||||||||||||||
GLFGAIAAFIEGGWTGMIDGWYGSGKKKKD

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

--------10--------20--------30
GLFGAIAAFIEGGWTGMIDGWYGSGKKKKD
||||||||||||||||||||||||||||||
GLFGAIAAFIEGGWTGMIDGWYGSGKKKKD

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

--------10--------20--------30
GLFGAIAAFIEGGWTGMIDGWYGSGKKKKD
||||||||||||||||||||||||||||||
GLFGAIAAFIEGGWTGMIDGWYGSGKKKKD

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	30	0	0	100.0
B	B	30	0	0	100.0
C	C	30	0	0	100.0

Content subtype: combined_18617_2lwa.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	OK	95		76.7 (chain: A, length: 30)
1	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	478 (1)	noe	73.3 (chain: A, length: 30)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_2	OK	40 (40)	.	76.7 (chain: A, length: 30)
1	RDC restraints	CNS/XPLOR_dipolar_coupling_4	OK	47 (42)	.	73.3 (chain: A, length: 30)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 30, Sequence coverage: 76.7%
- Total number of assignments
  - ¹H chemical shifts: 51
  - ¹³C chemical shifts: 23
  - ¹⁵N chemical shifts: 21
- Completeness of assignments
  - Entity_assemble_ID: A
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: A

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_3
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 30, Sequence coverage: 73.3%
- Total number of restraints: 477
- Weight of restraints: 1.0 (477)
- Potential type of restraints: square-well-parabolic (477)
- Range of distance target values: 1.9, 6.5 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
  - Chain_ID: B
    None
  - Chain_ID: C
    None
- 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: 30, Sequence coverage: 76.7%
- Total number of restraints: 40
- Total number of restraints per polymer type: 40
- Weight of restraints: 1.0 (40)
- Potential type of restraints: square-well-parabolic (40)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

RDC restraints

Saveframe: CNS/XPLOR_dipolar_coupling_4
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 30, Sequence coverage: 73.3%
- Total number of restraints: 47
- Potential type of restraints: undefined (47)
- Range of observed RDC values: 100.0, -100.0 (Hz)
- RDC restraints per residue
  - Chain_ID: A
    None

Keywords conformations, ensemble, fusion peptide, G8A mutant, hemagglutinin, membrane protein, Solution NMR