BMRBj - BMREntryMaster

	Total	¹H	¹³C
All	81.4 % (297 of 365)	97.6 % (203 of 208)	59.9 % (94 of 157)
Backbone	77.1 % (108 of 140)	94.8 % (55 of 58)	64.6 % (53 of 82)
Sidechain	85.3 % (214 of 251)	98.7 % (148 of 150)	65.3 % (66 of 101)
Aromatic	52.5 % (32 of 61)	100.0 % (32 of 32)	0.0 % (0 of 29)
Methyl	100.0 % (38 of 38)	100.0 % (19 of 19)	100.0 % (19 of 19)

1. CpreTM

KKKNWFDITN WLWYIKLFIM IVGGLVKK

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Sample

Solvent system hexafluoroisopropanol/water, Pressure 1 atm, Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Concentration
1	CpreTM	natural abundance	0.5 mM
2	H2O	natural abundance	67.5 %
3	D2O	[U-100% 2H]	7.5 %
4	hexafluoroisopropanol	natural abundance	25 %
5	HEPES	natural abundance	2 mM
6	DSS	natural abundance	0.1 mM

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Calculated from 20 models in PDB: 2MG2, Strand ID: A Detail

Release date

2015-03-22

Citation

The Atomic Structure of the HIV-1 gp41 Transmembrane Domain and its Connection to the Inmmunogenic Membrane-proximal External Region
Serrano, S., Apellaniz, B., Huarte, N., Jimenez, M., Nieva, J.L.
Not known

Related entities 1. peptide derived from the membrane proximal external region of HIV-1 gp41, : 1 : 1 : 88 entities Detail

Experiments performed 4 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_19582_2mg2.nef
Input source #2: Coordindates	2mg2.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--------
KKKNWFDITNWLWYIKLFIMIVGGLVKK
||||||||||||||||||||||||||||
KKKNWFDITNWLWYIKLFIMIVGGLVKK

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	28	0	0	100.0

Content subtype: combined_19582_2mg2.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	290		100.0 (chain: A, length: 28)
1	Distance restraints	DYANA/DIANA_distance_constraints_3	OK	502 (1)	noe	100.0 (chain: A, length: 28)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_2	OK	47 (47)	.	100.0 (chain: A, length: 28)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 28, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 203
  - ¹³C chemical shifts: 87
- Completeness of assignments
  - Entity_assemble_ID: A
- 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	208	203	97.6
¹³C chemical shifts	157	87	55.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	58	55	94.8
¹³C chemical shifts	56	24	42.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	150	148	98.7
¹³C chemical shifts	101	63	62.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	20	20	100.0
¹³C chemical shifts	20	20	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	32	32	100.0
¹³C chemical shifts	29	0	0.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_3
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 28, Sequence coverage: 100.0%
- Total number of restraints: 502
- Weight of restraints: 1.0 (502)
- Potential type of restraints: upper-bound-parabolic (502)
- Range of distance target values: 2.59, 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_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 28, Sequence coverage: 100.0%
- Total number of restraints: 47
- Total number of restraints per polymer type: 47
- Weight of restraints: 1.0 (47)
- Potential type of restraints: square-well-parabolic (47)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords HIV-1 gp41 protein, MPER, neutralizing epitope, peptide, peptide vaccine

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BMRB: 19582

Sample

Related entities 1. peptide derived from the membrane proximal external region of HIV-1 gp41, : 1 : 1 : 88 entities Detail

Experiments performed 4 experiments Detail

Instrument

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Sample

NMR combined restraints 4 contents Detail