BMRBj - BMREntryMaster

	Total	¹H	¹³C
All	83.5 % (274 of 328)	96.2 % (179 of 186)	66.9 % (95 of 142)
Backbone	79.3 % (107 of 135)	96.5 % (55 of 57)	66.7 % (52 of 78)
Sidechain	88.0 % (191 of 217)	96.1 % (124 of 129)	76.1 % (67 of 88)
Aromatic	45.0 % (9 of 20)	90.0 % (9 of 10)	0.0 % (0 of 10)
Methyl	94.0 % (47 of 50)	100.0 % (25 of 25)	88.0 % (22 of 25)

1. TMDp

KKKLFIMIVG GLVGLRIVFA VLSIKKK

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Sample

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

#	Name	Isotope labeling	Concentration
1	TMDp	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: 2MG1, 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 trans-membrane region of HIV-1 gp41, : 1 : 2 : 48 entities Detail

Interaction partners 1. peptide derived from the trans-membrane region of HIV-1 gp41, : 8 interactors Detail

More details for 8 interactors identified by 5 citations

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_19581_2mg1.nef
Input source #2: Coordindates	2mg1.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-------
KKKLFIMIVGGLVGLRIVFAVLSIKKK
|||||||||||||||||||||||||||
KKKLFIMIVGGLVGLRIVFAVLSIKKK

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	27	0	0	100.0

Content subtype: combined_19581_2mg1.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	273		100.0 (chain: A, length: 27)
1	Distance restraints	DYANA/DIANA_distance_constraints_3	OK	501 (1)	noe	100.0 (chain: A, length: 27)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_2	OK	50 (50)	.	100.0 (chain: A, length: 27)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 27, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 179
  - ¹³C chemical shifts: 94
- 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	186	179	96.2
¹³C chemical shifts	142	94	66.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	57	55	96.5
¹³C chemical shifts	54	27	50.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	129	124	96.1
¹³C chemical shifts	88	67	76.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	26	26	100.0
¹³C chemical shifts	26	23	88.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	10	9	90.0
¹³C chemical shifts	10	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: 27, Sequence coverage: 100.0%
- Total number of restraints: 501
- Weight of restraints: 1.0 (501)
- Potential type of restraints: upper-bound-parabolic (501)
- Range of distance target values: 2.35, 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: 27, Sequence coverage: 100.0%
- Total number of restraints: 50
- Total number of restraints per polymer type: 50
- Weight of restraints: 1.0 (50)
- Potential type of restraints: square-well-parabolic (50)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords HIV-1 gp41 protein, neutralizing epitope, peptide, transmembrane domain

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Found 1 Document (0.669 seconds)

BMRB: 19581

Sample

Related entities 1. peptide derived from the trans-membrane region of HIV-1 gp41, : 1 : 2 : 48 entities Detail

Interaction partners 1. peptide derived from the trans-membrane region of HIV-1 gp41, : 8 interactors Detail

Experiments performed 4 experiments Detail

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Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 4 contents Detail