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- PDB-5v2b: Peptide 38148 modified from fragment 41-60 of Plasmodium falcipar... -

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Basic information

Entry
Database: PDB / ID: 5v2b
TitlePeptide 38148 modified from fragment 41-60 of Plasmodium falciparum Thrombospondin-Related Sporozoite Protein (TRSP)
ComponentsThrombospondin-related sporozoite protein
KeywordsCELL INVASION / Modified peptide / Chemically synthesized / Pf-TRSP protein / Alpha-helix residues 8-18
Function / homologyCCN, TSP1 domain / CCN3 Nov like TSP1 domain / Thrombospondin type-1 (TSP1) repeat superfamily / Thrombospondin type-1 (TSP1) repeat profile. / Thrombospondin type 1 repeats / Thrombospondin type-1 (TSP1) repeat / signal transduction / plasma membrane / Thrombospondin-related sporozoite protein
Function and homology information
Biological speciesPlasmodium falciparum (malaria parasite P. falciparum)
MethodSOLUTION NMR / DGSA-distance geometry simulated annealing
AuthorsBermudez, A. / Patarroyo, M.E.
CitationJournal: To Be Published
Title: Peptide 38148 modified from fragment 41-60 of Plasmodium falciparum Thrombospondin-Related Sporozoite Protein (TRSP)
Authors: Bermudez, A. / Patarroyo, M.E.
History
DepositionMar 3, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 8, 2018Provider: repository / Type: Initial release
Revision 1.1Jun 14, 2023Group: Data collection / Database references / Other
Category: database_2 / pdbx_database_status / pdbx_nmr_software
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data / _pdbx_nmr_software.name
Revision 1.2May 15, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 / Item: _database_2.pdbx_DOI

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Thrombospondin-related sporozoite protein


Theoretical massNumber of molelcules
Total (without water)2,4321
Polymers2,4321
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area0 Å2
ΔGint0 kcal/mol
Surface area2380 Å2
MethodPISA
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)9 / 50structures with the least restraint violations
RepresentativeModel #1lowest energy

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Components

#1: Protein/peptide Thrombospondin-related sporozoite protein


Mass: 2431.622 Da / Num. of mol.: 1 / Fragment: UNP residues 41-60 / Mutation: V43T, R53K, L54H / Source method: obtained synthetically
Source: (synth.) Plasmodium falciparum (malaria parasite P. falciparum)
References: UniProt: Q8I2A0

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDSample stateSpectrometer-IDType
111anisotropic12D DQF-COSY; 2D 1H-1H TOCSY; 2D 1H-1H NOESY
221anisotropic12D 1H-1H TOCSY
331anisotropic12D 1H-1H TOCSY
441anisotropic12D 1H-1H TOCSY

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Sample preparation

DetailsType: solution / Contents: 16.6 mg/mL 38148, trifluoroethanol/water
Details: Peptide 38148 modified from fragment 41-60 of Plasmodium falciparum Thrombospondin-Related Sporozoite Protein (TRSP)
Label: 38148 / Solvent system: trifluoroethanol/water
SampleConc.: 16.6 mg/mL / Component: 38148 / Isotopic labeling: natural abundance
Sample conditions

Ionic strength: NULL Not defined / pH: 3.7 / PH err: 0.1 / Pressure: AMBIENT / Temperature err: 0.1

Conditions-IDDetailsLabelTemperature (K)
1TEMPERATURE AMBIENT38148 (295)295 K
2TEMPERATURE 285 K38148 (285)285 K
3TEMPERATURE 305 K38148 (305)305 K
4TEMPERATURE 315 K38148 (315)315 K

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NMR measurement

NMR spectrometerType: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz

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Processing

NMR software
NameDeveloperClassification
Insight IIAccelrys Software Inc.refinement
Insight IIAccelrys Software Inc.geometry optimization
RefinementMethod: DGSA-distance geometry simulated annealing / Software ordinal: 1 / Details: 220 NOEs
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the least restraint violations
Conformers calculated total number: 50 / Conformers submitted total number: 9

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