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- PDB-2ivw: The solution structure of a domain from the Neisseria meningitidi... -

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Basic information

Entry
Database: PDB / ID: 2ivw
TitleThe solution structure of a domain from the Neisseria meningitidis PilP pilot protein.
ComponentsPILP PILOT PROTEIN
KeywordsLIPOPROTEIN / PILUS BIOGENESIS / NEISSERIA MENINGITIDIS / SECRETIN / PILOT PROTEIN
Function / homologySH3 type barrels. - #830 / Type IV pilus inner membrane component PilP / Pilus assembly protein, PilP / SH3 type barrels. / Prokaryotic membrane lipoprotein lipid attachment site profile. / Roll / Mainly Beta / PilP protein
Function and homology information
Biological speciesNEISSERIA MENINGITIDIS (bacteria)
MethodSOLUTION NMR / CYANA2.1
AuthorsGolovanov, A.P. / Balasingham, S. / Tzitzilonis, C. / Goult, B.T. / Lian, L.-Y. / Homberset, H. / Tonjum, T. / Derrick, J.P.
CitationJournal: J. Mol. Biol. / Year: 2006
Title: The solution structure of a domain from the Neisseria meningitidis lipoprotein PilP reveals a new beta-sandwich fold.
Authors: Golovanov, A.P. / Balasingham, S. / Tzitzilonis, C. / Goult, B.T. / Lian, L.Y. / Homberset, H. / Tonjum, T. / Derrick, J.P.
History
DepositionJun 20, 2006Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 13, 2007Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3May 9, 2018Group: Data collection / Database references
Category: citation / citation_author / pdbx_nmr_spectrometer
Item: _citation.journal_abbrev / _citation.page_last ..._citation.journal_abbrev / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.title / _citation_author.name / _pdbx_nmr_spectrometer.model
Revision 1.4May 15, 2024Group: Data collection / Database references / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / 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_mr / _pdbx_nmr_software.name

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: PILP PILOT PROTEIN


Theoretical massNumber of molelcules
Total (without water)12,4751
Polymers12,4751
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)20 / 100LOWEST TARGET FUNCTION
RepresentativeModel #1

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Components

#1: Protein PILP PILOT PROTEIN


Mass: 12474.708 Da / Num. of mol.: 1 / Fragment: FOLDED DOMAIN, RESIDUES 69-181
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) NEISSERIA MENINGITIDIS (bacteria) / Strain: Z2491 / Plasmid: PET101/D-TOPO / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q7DD77

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
11115N-EDITED NOESY-HSQC
12113C- EDITED NOESY-HSQC
131HOMONUCLEAR 2D NOESY
NMR detailsText: THE STRUCTURE WAS DETERMINED USING 3D AND HOMONUCLEAR 2D NMR SPECTROSCOPY ON (13C,15N), (15N)- LABELED AND UNLABELLED PILP.

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Sample preparation

DetailsContents: 95% WATER/5% D2O, 20MM PHOSPHATE BUFFER, 1MM EDTA
Sample conditionsIonic strength: 20 mM / pH: 6.1 / Pressure: 1.0 atm / Temperature: 303.0 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
CYANAP.GUNTERT ET AL.refinement
CYANAstructure solution
RefinementMethod: CYANA2.1 / Software ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. THE STRUCTURE OF PILP FRAGMENT 69-181 IS PRESENTED. THE LONGER PROTEIN CONSTRUCT (RESIDUES 20-181) HAS BEEN STUDIED BY NMR WHICH ...Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. THE STRUCTURE OF PILP FRAGMENT 69-181 IS PRESENTED. THE LONGER PROTEIN CONSTRUCT (RESIDUES 20-181) HAS BEEN STUDIED BY NMR WHICH REVEALED THAT N-TERMINAL PART OF POLYPEPTIDE CHAIN IS FLEXIBLE AND UNFOLDED.
NMR ensembleConformer selection criteria: LOWEST TARGET FUNCTION / Conformers calculated total number: 100 / Conformers submitted total number: 20

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