BMRBj - BMREntryMaster

	Total	¹H
All	89.8 % (114 of 127)	89.8 % (114 of 127)
Backbone	100.0 % (40 of 40)	100.0 % (40 of 40)
Sidechain	85.1 % (74 of 87)	85.1 % (74 of 87)
Aromatic	50.0 % (8 of 16)	50.0 % (8 of 16)
Methyl	100.0 % (8 of 8)	100.0 % (8 of 8)

1. entity

MIKSAFLPTG AFKADRYKSH X

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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	8 mM
2	water	natural abundance	70 %
3	trifluoroethanol	natural abundance	30 %

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

Release date

2015-09-30

Citation

Protection against experimental P falciparum malaria is associated with short AMA-1 peptide analogue alpha-helical structures
Cubillos, M., Salazar, L., Torres, L., Patarroyo, M.
Biochimie (2002), 84, 1181-1188, PubMed 12628294 , Abstract

Related entities 1. malaria short AMA-1 peptide analogue, : 1 : 25 : 8 entities Detail

Experiments performed 3 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_25190_2mtx.nef
Input source #2: Coordindates	2mtx.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	True (see coodinates for details)
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)

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:20:HIS:C	1:21:NH2:N	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
A	21	NH2	AMINO GROUP	Coordinates

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

--------10--------20-
MIKSAFLPTGAFKADRYKSHX
|||||||||||||||||||||
MIKSAFLPTGAFKADRYKSHX

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_25190_2mtx.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	1		No information
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	118		95.2 (chain: A, length: 21)
1	Distance restraints	Discover_distance_constraints_5	OK	120 (1)	noe	95.2 (chain: A, length: 21)
2	Distance restraints	Discover_distance_constraints_4	Warning	2 (1)	hbond	19.0 (chain: A, length: 21)
1	Dihedral angle restraints	Discover_dihedral_6	OK	19 (19)	.	95.2 (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: 95.2%
- Total number of assignments
  - ¹H chemical shifts: 118
- 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)
16	ARG	HH11	6.98
16	ARG	HH12	6.98
16	ARG	HH21	6.98
16	ARG	HH22	6.98

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	129	113	87.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	40	39	97.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	89	74	83.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	9	8	88.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	16	8	50.0

Covalent bonds

Saveframe: assembly
- Status: OK

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: 95.2%
- Total number of restraints: 120
- Weight of restraints: 1.0 (120)
- Potential type of restraints: square-well-parabolic (120)
- Range of distance target values: 2.3, 4.75 (Å)
- Histogram of distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map
- Saveframe: Discover_distance_constraints_4
  - Status: Warning
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 21, Sequence coverage: 19.0%
  - Total number of restraints: 2
  - Weight of restraints: 1.0 (2)
  - Potential type of restraints: square-well-parabolic (2)
  - 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: 95.2%
- Total number of restraints: 19
- Total number of restraints per polymer type: 19
- Weight of restraints: 1.0 (19)
- Potential type of restraints: square-well-parabolic (19)
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords Peptide of domain II of AMA-1 from P. falciparum

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BMRB: 25190

Sample

Related entities 1. malaria short AMA-1 peptide analogue, : 1 : 25 : 8 entities Detail

Experiments performed 3 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 5 contents Detail