BMRBj - BMREntryMaster

	Total	¹H
All	96.9 % (124 of 128)	96.9 % (124 of 128)
Backbone	100.0 % (43 of 43)	100.0 % (43 of 43)
Sidechain	95.3 % (81 of 85)	95.3 % (81 of 85)
Aromatic	85.0 % (17 of 20)	85.0 % (17 of 20)
Methyl	100.0 % (8 of 8)	100.0 % (8 of 8)

1. entity

VIKHNRFLSE YQSNFLGGGY

Show sample condition

Sample

Solvent system trifluoroethanol/water, Pressure 1 atm, Temperature 295 K, pH 3.9, Details trifluoroethanol/water (30/70)

#	Name	Isotope labeling	Concentration
1	entity	natural abundance	8 mM
2	trifluoroethanol	natural abundance	30 %
3	water	natural abundance	70 %

Protein Blocks Logo

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

Release date

2014-10-06

Citation

3D structure determination of STARP peptides implicated in P. falciparum invasion of hepatic cells
Bermudez, A., Alba, M.P., Vanegas, M., Patarroyo, M.E.
Vaccine (2010), 28, 4989-4996, PubMed 20580741 , DOI 10.1016/j.vaccine.2010.05.025 , Abstract

Related entities 1. STARP peptide 20546, : 1 : 1 : 1 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_25191_2mty.nef
Input source #2: Coordindates	2mty.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
VIKHNRFLSEYQSNFLGGGY
||||||||||||||||||||
VIKHNRFLSEYQSNFLGGGY

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	20	0	0	100.0

Content subtype: combined_25191_2mty.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	126		100.0 (chain: A, length: 20)
1	Distance restraints	Discover_distance_constraints_5	OK	265 (1)	noe	100.0 (chain: A, length: 20)
2	Distance restraints	Discover_distance_constraints_4	Warning	2 (1)	hbond	20.0 (chain: A, length: 20)
1	Dihedral angle restraints	Discover_dihedral_6	OK	18 (18)	.	95.0 (chain: A, length: 20)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 20, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 126
- 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	HIS	HE2	8.26
6	ARG	HH11	7.18
6	ARG	HH12	7.18

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	128	122	95.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	43	42	97.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	85	80	94.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	8	7	87.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	20	17	85.0

Distance restraints

Saveframe: Discover_distance_constraints_5
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 20, Sequence coverage: 100.0%
- Total number of restraints: 263
- Weight of restraints: 1.0 (263)
- Potential type of restraints: square-well-parabolic (263)
- Range of distance target values: 2.3, 4.25 (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: 20, Sequence coverage: 20.0%
  - 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: 20, Sequence coverage: 95.0%
- Total number of restraints: 18
- Total number of restraints per polymer type: 18
- Weight of restraints: 1.0 (18)
- Potential type of restraints: square-well-parabolic (18)
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords Peptide of STARP from P. falciparum, Sporozoite

Search

Query history

Resources

Search for primary databases

Search for subsidiary databases

Display

Hits per page

Statistics

Query Changes will take effect after "OK" button is selected.

Maximum hits

Default conjunction operator

Omni-box

Search filter

Sequence search (BLAST)

E-value

Query sequence coverage

Miscellaneous

The number of previewed publications

Completeness of assigned chemical shift

Sequence chart about top aligned regions

Sequence chart about interacting regions

Hit context with highlight

Link destinations for BMRB, PDB and EMDB

Found 1 Document (0.551 seconds)

BMRB: 25191

Sample

Related entities 1. STARP peptide 20546, : 1 : 1 : 1 entities Detail

Experiments performed 3 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 5 contents Detail