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- PDB-32mp: Solution structure of a chimeric peptide derived from trpzip2 and... -

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Basic information

Entry
Database: PDB / ID: 32mp
TitleSolution structure of a chimeric peptide derived from trpzip2 and the disulfide loop of the PilA protein from P. aeruginosa
ComponentsFimbrial protein
KeywordsIMMUNE SYSTEM / STRUCTURE FROM CYANA 3.98.15
Function / homology
Function and homology information


type IV pilus / type IV pilus-dependent motility / cell adhesion / membrane
Similarity search - Function
Fimbrial protein pilin / Pilin (bacterial filament) / Prokaryotic N-terminal methylation site. / Prokaryotic N-terminal methylation motif / Prokaryotic N-terminal methylation site / Pilin-like
Similarity search - Domain/homology
Biological speciesPseudomonas aeruginosa (bacteria)
MethodSOLUTION NMR / torsion angle dynamics
AuthorsSette, M.
Funding support Italy, 1items
OrganizationGrant numberCountry
Other privateFFC 13/2023 Italy
CitationJournal: Front Immunol / Year: 2026
Title: Structured peptides as vaccine antigens against infections
Authors: Trappetti, C. / van Ingen, H. / Falconi, M. / Romeo, A. / Sancamillo, G. / Caprini, M. / Oggioni, M.R. / Sette, M.
History
DepositionJul 16, 2026Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 19, 2026Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Fimbrial protein


Theoretical massNumber of molelcules
Total (without water)3,1641
Polymers3,1641
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: NMR Distance Restraints, Distance and dihedral NMR restraints
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 100target function
RepresentativeModel #1target function

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Components

#1: Protein/peptide Fimbrial protein / Pilin


Mass: 3164.460 Da / Num. of mol.: 1 / Source method: obtained synthetically
Details: Chimeric peptide between disulfide loop of PilA protein and trpzip2 peptide
Source: (synth.) Pseudomonas aeruginosa (bacteria) / References: UniProt: P02973
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDSample stateSpectrometer-IDType
111isotropic12D TOCSY
121isotropic12D NOESY
131isotropic12D 13C HSQC

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Sample preparation

DetailsType: solution / Contents: 0.69 mM No labelling trpzip2PAK, 90% H2O/10% D2O / Details: 25 mM potassium phosphate buffer at pH 6.1 / Label: 1H sample / Solvent system: 90% H2O/10% D2O
SampleConc.: 0.69 mM / Component: trpzip2PAK / Isotopic labeling: No labelling
Sample conditionsIonic strength: 28.68 mM / Label: Conditions / pH: 6.1 / Pressure: 1 atm / Temperature: 308 K

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NMR measurement

NMR spectrometerType: Bruker AVANCE NEO / Manufacturer: Bruker / Model: AVANCE NEO / Field strength: 900 MHz

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Processing

NMR software
NameDeveloperClassification
NMRPipeDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Baxprocessing
NMRFAM-SPARKYGoddard-Markleychemical shift assignment
NMRFAM-SPARKYGoddard-Markleypeak picking
CYANAGuntertstructure calculation
CYANAGuntertrefinement
RefinementMethod: torsion angle dynamics / Software ordinal: 4
NMR representativeSelection criteria: target function
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20

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