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- PDB-1hpw: STRUCTURE OF A PILIN MONOMER FROM PSEUDOMONAS AERUGINOSA: IMPLICA... -

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Basic information

Entry
Database: PDB / ID: 1hpw
TitleSTRUCTURE OF A PILIN MONOMER FROM PSEUDOMONAS AERUGINOSA: IMPLICATIONS FOR THE ASSEMBLY OF PILI.
ComponentsFIMBRIAL PROTEIN
KeywordsCONTRACTILE PROTEIN / fimbria / methylation
Function / homology
Function and homology information


glycosphingolipid binding / biological process involved in interaction with host / pilus / periplasmic space / cell adhesion / membrane
Similarity search - Function
Glycoprotein, Type 4 Pilin / Glycoprotein, Type 4 Pilin / Fimbrial protein pilin / Pilin (bacterial filament) / Prokaryotic N-terminal methylation site. / Prokaryotic N-terminal methylation motif / Prokaryotic N-terminal methylation site / Pilin-like / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Biological speciesPseudomonas aeruginosa (bacteria)
MethodSOLUTION NMR / distance geometry simulated annealing
AuthorsKeizer, D.W. / Slupsky, C.M. / Campbell, A.P. / Irvin, R.T. / Sykes, B.D.
CitationJournal: J.Biol.Chem. / Year: 2001
Title: Structure of a pilin monomer from Pseudomonas aeruginosa: implications for the assembly of pili.
Authors: Keizer, D.W. / Slupsky, C.M. / Kalisiak, M. / Campbell, A.P. / Crump, M.P. / Sastry, P.A. / Hazes, B. / Irvin, R.T. / Sykes, B.D.
History
DepositionDec 13, 2000Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 2, 2001Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name

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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)13,1171
Polymers13,1171
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / 50structures with the lowest energy
RepresentativeModel #9closest to the average

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Components

#1: Protein FIMBRIAL PROTEIN / PILIN


Mass: 13116.644 Da / Num. of mol.: 1 / Fragment: PILIN (RESIDUES 29-150)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pseudomonas aeruginosa (bacteria) / Strain: K122-4 / Plasmid: PRLD / Production host: Escherichia coli (E. coli) / Strain (production host): DH5ALPHA / References: UniProt: P17838

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D NOESY
1213D 15N-separated NOESY
131DQF-COSY
141HNHA

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Sample preparation

DetailsContents: 0.5 mM K122-4 pilin dissolved in either 90% H2O/10% D2O or 99% D2O containing 20 mM deuterated sodium acetate, 1 mM NaN3 and 1 mM DSS, pH 5.0.
Sample conditionspH: 5.1 / Temperature: 303 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian UNITYVarianUNITY6001
Varian INOVAVarianINOVA8002

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Processing

NMR software
NameVersionDeveloperClassification
VNMR6.2BVariancollection
NMRPipeDelaglioprocessing
NMRView4.2Johnsondata analysis
X-PLOR3.851Brungerrefinement
RefinementMethod: distance geometry simulated annealing / Software ordinal: 1
Details: The structures are based on a total of 1213 restraints, 1032 are NOE-derived distance constraints, 181 dihedral angle restraints, 30 distance restraints from hydrogen bonds.
NMR representativeSelection criteria: closest to the average
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 50 / Conformers submitted total number: 10

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