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- PDB-2msa: Structural and immunological analysis of circumsporozoite protein... -

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Basic information

Entry
Database: PDB / ID: 2msa
TitleStructural and immunological analysis of circumsporozoite protein peptides: a further step in the identification of potential components of a minimal subunit-based, chemically synthesised antimalarial vaccine.
ComponentsCircumsporozoite protein peptide
KeywordsCELL INVASION / Clasic turn type II
Function / homology
Function and homology information


side of membrane / cell surface / plasma membrane / cytoplasm
Similarity search - Function
: / Plasmodium circumsporozoite protein / Thrombospondin type 1 domain / Thrombospondin type-1 (TSP1) repeat superfamily / Thrombospondin type-1 (TSP1) repeat profile. / Thrombospondin type 1 repeats / Thrombospondin type-1 (TSP1) repeat
Similarity search - Domain/homology
Circumsporozoite protein
Similarity search - Component
Biological speciesPlasmodium falciparum (malaria parasite P. falciparum)
MethodSOLUTION NMR / distance geometry, simulated annealing
Model detailslowest energy, model37
AuthorsAdriana, B. / Magnolia, V. / Manuel, P.E.
CitationJournal: Vaccine / Year: 2008
Title: Structural and immunological analysis of circumsporozoite protein peptides: a further step in the identification of potential components of a minimal subunit-based, chemically synthesised antimalarial vaccine.
Authors: Bermudez, A. / Vanegas, M. / Patarroyo, M.E.
History
DepositionJul 28, 2014Deposition site: BMRB / Processing site: RCSB
Revision 1.0Sep 3, 2014Provider: repository / Type: Initial release
Revision 1.1Jun 14, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / struct_conn
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 / _struct_conn.pdbx_leaving_atom_flag

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Circumsporozoite protein peptide


Theoretical massNumber of molelcules
Total (without water)1,4881
Polymers1,4881
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)1 / 50structures with the least restraint violations
RepresentativeModel #1

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Components

#1: Protein/peptide Circumsporozoite protein peptide


Mass: 1487.574 Da / Num. of mol.: 1 / Source method: obtained synthetically
Source: (synth.) Plasmodium falciparum (malaria parasite P. falciparum)
References: UniProt: P08307*PLUS

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
Details: Peptide synthetic modified derived of N-terminal and central region of Circumsporozoite protein (CSP)from Plasmodium falciparum. The person responsible for the deposition is a chemist with ...Details: Peptide synthetic modified derived of N-terminal and central region of Circumsporozoite protein (CSP)from Plasmodium falciparum. The person responsible for the deposition is a chemist with wide experience in NMR in solution of peptides synthetics.
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D DQF-COSY
1212D 1H-1H TOCSY
1312D 1H-1H NOESY

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Sample preparation

DetailsContents: 8 mM protein, trifluoroethanol/water / Solvent system: trifluoroethanol/water
SampleConc.: 8 mM / Component: entity-1
Sample conditionspH: 3.7 / Pressure: ambient / Temperature: 295 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.geometry optimization
Insight IIAccelrys Software Inc.refinement
RefinementMethod: distance geometry, simulated annealing / Software ordinal: 1
NMR ensembleConformer selection criteria: structures with the least restraint violations
Conformers calculated total number: 50 / Conformers submitted total number: 1

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