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Found 1 Document (0.51 seconds)

BMRB: 25204

2MUA

Shifting the Polarity of some Critical Residues in Malarial Peptides Binding to Host Cells is a Key Factor in Breaking Conserved Antigens

Authors

Cifuentes, G., Bermudez, A., Rodriguez, R., Patarroyo, M., Patarroyo, M.

Assembly

Malarial Peptide 6673

Entity

1. Malarial Peptide 6673 (polymer, Thiol state: not present), 21 monomers, 2454.863 Da Detail

YLGRSGGDII KKMQTLWDEI M

Formula weight

2454.863 Da

Exptl. method

solution NMR

Refine. method

distance geometry, simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 98.5 %, Completeness (bb): 100.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	98.5 % (133 of 135)	98.5 % (133 of 135)
Backbone	100.0 % (45 of 45)	100.0 % (45 of 45)
Sidechain	97.8 % (88 of 90)	97.8 % (88 of 90)
Aromatic	100.0 % (10 of 10)	100.0 % (10 of 10)
Methyl	100.0 % (11 of 11)	100.0 % (11 of 11)

1. entity

YLGRSGGDII KKMQTLWDEI M

Show sample condition

Sample

Solvent system trifluoroethanol/water, Pressure 1 atm, Temperature 295 K, pH 3.7, Details trifluoroethanol/water 30%/70%

#	Name	Isotope labeling	Concentration
1	entity	natural abundance	10.0 ~ 12.0 mM
2	H2O	natural abundance	70 %
3	trifluoroethanol	natural abundance	30 %

Protein Blocks Logo

Calculated from 1 models in PDB: 2MUA, Strand ID: A Detail

Release date

2015-09-13

Citation

Shifting the polarity of some critical residues in malarial peptides' binding to host cells is a key factor in breaking conserved antigens' code of silence
Cifuentes, G., Bermudez, A., Rodriguez, R., Patarroyo, M., Patarroyo, M.
Med. Chem. (2008), 4, 278-292, PubMed 18473921 , DOI: , Abstract

Related entities 1. Malarial Peptide 6673, : 3 : 3 entities Detail

Experiments performed 3 experiments Detail

NMR combined restraints 6 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_25204_2mua.nef
Input source #2: Coordindates	2mua.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-
YLGRSGGDIIKKMQTLWDEIM
|||||||||||||||||||||
YLGRSGGDIIKKMQTLWDEIM

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	21	0	0	100.0

Content subtype: combined_25204_2mua.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	137		100.0 (chain: A, length: 21)
1	Distance restraints	Discover_distance_constraints_5	OK	229 (1)	noe	100.0 (chain: A, length: 21)
2	Distance restraints	Discover_distance_constraints_4	OK	11 (1)	hbond	76.2 (chain: A, length: 21)
1	Dihedral angle restraints	Discover_dihedral_6	OK	20 (20)	.	100.0 (chain: A, length: 21)
2	Dihedral angle restraints	Discover_dihedral_7	Warning	4 (4)	.	19.0 (chain: A, length: 21)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 21, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 137
- 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

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
4	ARG	HH11	7.12
4	ARG	HH12	7.12
4	ARG	HH21	6.7
4	ARG	HH22	6.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	135	132	97.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	45	44	97.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	90	88	97.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	13	12	92.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	10	10	100.0

Distance restraints

Saveframe: Discover_distance_constraints_5
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 21, Sequence coverage: 100.0%
- Total number of restraints: 229
- Weight of restraints: 1.0 (229)
- Potential type of restraints: square-well-parabolic (229)
- Range of distance target values: 2.3, 5.75 (Å)
- Histogram of distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map
- Saveframe: Discover_distance_constraints_4
  - Status: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 21, Sequence coverage: 76.2%
  - Total number of restraints: 11
  - Weight of restraints: 1.0 (11)
  - Potential type of restraints: square-well-parabolic (11)
  - Range of distance target values: 2.15, 2.15 (Å)
  - Distance restraints per residue
    - Chain_ID: A
  - Distance restraints on contact map

Dihedral angle restraints

Saveframe: Discover_dihedral_6
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 21, Sequence coverage: 100.0%
- Total number of restraints: 20
- Total number of restraints per polymer type: 20
- Weight of restraints: 1.0 (20)
- Potential type of restraints: square-well-parabolic (20)
- Dihedral angle restraints per residue
  - Chain_ID: A
- Saveframe: Discover_dihedral_7
  - Status: Warning
  - Experiment type: .
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 21, Sequence coverage: 19.0%
  - Total number of restraints: 4
  - Total number of restraints per polymer type: 4
  - Weight of restraints: 1.0 (4)
  - Potential type of restraints: square-well-parabolic (4)
  - Dihedral angle restraints per residue

Keywords Peptide of Ring-Infected Erythrocyte Surface Antigen (RESA)-155 from Plasmodium falciparum

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Found 1 Document (0.51 seconds)

BMRB: 25204

Sample

Related entities 1. Malarial Peptide 6673, : 3 : 3 entities Detail

Experiments performed 3 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 6 contents Detail