BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	89.4 % (338 of 378)	98.5 % (192 of 195)	76.2 % (112 of 147)	94.4 % (34 of 36)
Backbone	96.9 % (157 of 162)	96.3 % (52 of 54)	98.8 % (80 of 81)	92.6 % (25 of 27)
Sidechain	85.6 % (208 of 243)	99.3 % (140 of 141)	63.4 % (59 of 93)	100.0 % (9 of 9)
Aromatic	55.1 % (43 of 78)	97.4 % (38 of 39)	0.0 % (0 of 34)	100.0 % (5 of 5)
Methyl	100.0 % (32 of 32)	100.0 % (16 of 16)	100.0 % (16 of 16)

1. MPER-Du151

EKDLLALDSW KNLWNWFNIT NWLWYIK

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 273 K, pH 6.6 (±0.1), Details 15N/13C-labeled MPER-Du151

#	Name	Isotope labeling	Concentration
1	MPER-Du151	[U-100% 13C; U-100% 15N]	1 mM
2	DPC	[U-100% 2H]	100 mM
3	H2O	natural abundance	90 %
4	D20	natural abundance	10 %

Sample #2

Solvent system 100% D2O, Pressure 1 atm, Temperature 273 K, pH 6.6 (±0.1), Details unlabeled MPER-Du151

#	Name	Isotope labeling	Concentration
9	MPER-Du151	natural abundance	1 mM
10	DPC	[U-100% 2H]	100 mM
11	D2O	natural abundance	100 %

Protein Blocks Logo

Calculated from 10 models in PDB: 2ME3, Strand ID: A Detail

Release date

2013-10-07

Citation

Disruption of helix-capping residues 671 and 674 reveals a role in HIV-1 entry for a specialized hinge segment of the membrane proximal external region of gp41
Sun, Z.J., Cheng, Y., Kim, M., Song, L., Choi, J., Kudahl, U.J., Brusic, V., Chowdhury, B., Yu, L., Seaman, M.S., Bellot, G., Shih, W.M., Wagner, G., Reinherz, E.L.
J. Mol. Biol. (2014), 426, 1095-1108, PubMed 24075869 , DOI 10.1016/j.jmb.2013.09.030 , Abstract

Entries sharing articles BMRB: 3 entries Detail

  BMRB: 19512 released on 2013-10-07
    Title HIV-1 gp41 clade B double alanine mutant Membrane Proximal External Region peptide in DPC micelle
  BMRB: 19513 released on 2013-10-07
    Title HIV-1 gp41 clade C Membrane Proximal External Region peptide in DPC micelle
  BMRB: 19515 released on 2013-10-07
    Title HIV-1 gp41 clade C Membrane Proximal External Region peptide in DPC micelle

Related entities 1. MPER-Du151, : 1 : 1 : 95 entities Detail

Experiments performed 7 experiments Detail

1 3D backbone

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 273 K, pH 6.6 (±0.1), Details 15N/13C-labeled MPER-Du151

#	Name	Isotope labeling	Concentration
1	MPER-Du151	[U-100% 13C; U-100% 15N]	1 mM
2	DPC	[U-100% 2H]	100 mM
3	H2O	natural abundance	90 %
4	D20	natural abundance	10 %

2 3D C(CO)NH,H(CCO)NH,HCCH-TOCSY

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 273 K, pH 6.6 (±0.1), Details 15N/13C-labeled MPER-Du151

#	Name	Isotope labeling	Concentration
1	MPER-Du151	[U-100% 13C; U-100% 15N]	1 mM
2	DPC	[U-100% 2H]	100 mM
3	H2O	natural abundance	90 %
4	D20	natural abundance	10 %

3 3D 1H-13C NOESY

Instrument

Bruker Avance - 750 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 273 K, pH 6.6 (±0.1), Details 15N/13C-labeled MPER-Du151

#	Name	Isotope labeling	Concentration
1	MPER-Du151	[U-100% 13C; U-100% 15N]	1 mM
2	DPC	[U-100% 2H]	100 mM
3	H2O	natural abundance	90 %
4	D20	natural abundance	10 %

4 3D 1H-15N NOESY

Instrument

Bruker Avance - 750 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 273 K, pH 6.6 (±0.1), Details 15N-labeled MPER-Du151

#	Name	Isotope labeling	Concentration
5	MPER-Du151	[U-100% 15N]	1 mM
6	DPC	[U-100% 2H]	100 mM
7	H2O	natural abundance	90 %
8	D20	natural abundance	10 %

5 3D HNHA

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 273 K, pH 6.6 (±0.1), Details 15N-labeled MPER-Du151

#	Name	Isotope labeling	Concentration
5	MPER-Du151	[U-100% 15N]	1 mM
6	DPC	[U-100% 2H]	100 mM
7	H2O	natural abundance	90 %
8	D20	natural abundance	10 %

6 2D 1H-1H NOESY,TOCSY

Instrument

Bruker Avance - 900 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 273 K, pH 6.6 (±0.1), Details unlabeled MPER-Du151

#	Name	Isotope labeling	Concentration
9	MPER-Du151	natural abundance	1 mM
10	DPC	[U-100% 2H]	100 mM
11	D2O	natural abundance	100 %

7 Q-J RDC

Instrument

Bruker Avance - 600 MHz

Sample

State anisotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 273 K, pH 6.6 (±0.1), Details 15N/13C-labeled MPER-Du151 for RDC

#	Name	Isotope labeling	Concentration
12	MPER-Du151	[U-100% 13C; U-100% 15N]	1 mM
13	DPC	[U-100% 2H]	100 mM
14	DNA nanotube	natural abundance	20 mg/mL
15	H2O	natural abundance	90 %
16	D20	natural abundance	10 %

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_19514_2me3.nef
Input source #2: Coordindates	2me3.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

---660-----670-------680---
EKDLLALDSWKNLWNWFNITNWLWYIK
|||||||||||||||||||||||||||
EKDLLALDSWKNLWNWFNITNWLWYIK
--------10--------20-------

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_19514_2me3.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	338		100.0 (chain: A, length: 27)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	481 (1)	noe	96.3 (chain: A, length: 27)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	47 (47)	.	96.3 (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: 192
  - ¹³C chemical shifts: 112
  - ¹⁵N chemical shifts: 34
- 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	195	192	98.5
¹³C chemical shifts	147	112	76.2
¹⁵N chemical shifts	36	34	94.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	54	52	96.3
¹³C chemical shifts	54	53	98.1
¹⁵N chemical shifts	27	25	92.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	141	140	99.3
¹³C chemical shifts	93	59	63.4
¹⁵N chemical shifts	9	9	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	16	16	100.0
¹³C chemical shifts	16	16	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	39	38	97.4
¹³C chemical shifts	34	0	0.0
¹⁵N chemical shifts	5	5	100.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 27, Sequence coverage: 96.3%
- Total number of restraints: 481
- Weight of restraints: 1.0 (481)
- Potential type of restraints: square-well-parabolic (481)
- Range of distance target values: 0.1, 4.8 (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: CNS/XPLOR_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 27, Sequence coverage: 96.3%
- 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 helix-hinge-helix, MPER, viral fusion

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Found 1 Document (0.417 seconds)

BMRB: 19514

Sample #1

Sample #2

Entries sharing articles BMRB: 3 entries Detail

Related entities 1. MPER-Du151, : 1 : 1 : 95 entities Detail

Experiments performed 7 experiments Detail

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NMR combined restraints 4 contents Detail