BMRBj - BMREntryMaster

Found 1 Document (1.196 seconds)

BMRB: 4298

A Synthetic Cyclic Peptide Corresponding to the Complete V3 Loop of the RF HIV-1 Strain in Water Solution

Authors

Vranken, W.F., Budesinsky, M., Martins, J.C., Fant, F., Boulez, K., Gras-Masse, H., Borremans, F.AM.

Assembly

V3 loop peptide of RF HIV-1 gp120 envelope protein

Entity

1. V3 loop peptide of RF HIV-1 gp120 envelope protein (polymer), 35 monomers, 3840.400 Da Detail

CTRPNNNTRK SITKGPGRVI YATGQIIGDI RKAHC

Formula weight

3840.4 Da

Entity Connection

disulfide 1 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS1:SG	1:CYS35:SG

Source organism

Human immunodeficiency virus

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 100.0 %, Completeness (bb): 100.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	100.0 % (210 of 210)	100.0 % (210 of 210)
Backbone	100.0 % (72 of 72)	100.0 % (72 of 72)
Sidechain	100.0 % (138 of 138)	100.0 % (138 of 138)
Aromatic	100.0 % (6 of 6)	100.0 % (6 of 6)
Methyl	100.0 % (18 of 18)	100.0 % (18 of 18)

1. V3 loop

CTRPNNNTRK SITKGPGRVI YATGQIIGDI RKAHC

Show sample condition

Sample

Temperature 275 (±0.2) K, pH 2.5 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	V3 loop			4.0 mM

Release date

1999-03-09

Citation 1

Conformational features of a synthetic cyclic peptide corresponding to the complete V3 loop of the RF HIV-1 strain in water and water/trifluoroethanol solutions
Vranken, W.F., Budesinsky, M., Martins, J.C., Fant, F., Boulez, K., Gras-Masse, H., Borremans, F.AM.
Eur. J. Biochem. (1996), 236, 100-108, PubMed 8617252 , DOI 10.1111/j.1432-1033.1996.00100.x , Abstract

Show more 1 citaion

Citation 2

1H, 13C and 15N chemical shift referencing in biomolecular NMR
Wishart, D.S., Bigam, C.G., Yao, J., Abildgaard, F., Dyson, H.J., Oldfield, E., Markley, J.L., Sykes, B.D.
J. Biomol. NMR (1995), 6, 135-140, PubMed 8589602 , DOI 10.1007/bf00211777 , Abstract

Hide non-primary 1 citaion

Related entities 1. V3 loop peptide of RF HIV-1 gp120 envelope protein, : 1 : 151 entities Detail

Experiments performed 4 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4298_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	True (see coordinates for details)
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:1:CYS:SG	1:35:CYS:SG	unknown	unknown	n/a

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Content subtype: bmr4298_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_one	Warning	255		100.0 (chain: 1, length: 35)
1	Chemical shift references	chemical_shift_reference_one	OK	1		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_one
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 35, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 255
- Completeness of assignments
  - Entity_assemble_ID: 1
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
10	LYS	HZ1	7.65
10	LYS	HZ2	7.65
10	LYS	HZ3	7.65
14	LYS	HZ1	7.62
14	LYS	HZ2	7.62
14	LYS	HZ3	7.62
32	LYS	HZ1	7.65
32	LYS	HZ2	7.65
32	LYS	HZ3	7.65

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	210	210	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	72	72	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	138	138	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	18	18	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	6	6	100.0

Keywords amphipathic helix, CD, human immunodeficiency virus type 1, NMR, RF V3 loop

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Found 1 Document (1.196 seconds)

BMRB: 4298

Sample

Related entities 1. V3 loop peptide of RF HIV-1 gp120 envelope protein, : 1 : 151 entities Detail

Experiments performed 4 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Chemical shift validation 3 contents Detail