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- PDB-2n7h: Hybrid structure of the Type 1 Pilus of Uropathogenic E.coli -

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Basic information

Entry
Database: PDB / ID: 2n7h
TitleHybrid structure of the Type 1 Pilus of Uropathogenic E.coli
ComponentsFimA
KeywordsSTRUCTURAL PROTEIN
Function / homology
Function and homology information


cell adhesion involved in single-species biofilm formation / pilus / cell adhesion / identical protein binding
Similarity search - Function
Fimbrial-type adhesion domain / Fimbrial protein / Fimbrial-type adhesion domain superfamily / Adhesion domain superfamily
Similarity search - Domain/homology
Type-1 fimbrial protein, A chain / FimA
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodSOLID-STATE NMR / torsion angle dynamics
Model detailslowest energy, model1
AuthorsHabenstein, B. / Loquet, A. / Giller, K. / Vasa, S. / Becker, S. / Habeck, M. / Lange, A.
CitationJournal: Angew.Chem.Int.Ed.Engl. / Year: 2015
Title: Hybrid Structure of the Type 1 Pilus of Uropathogenic Escherichia coli.
Authors: Habenstein, B. / Loquet, A. / Hwang, S. / Giller, K. / Vasa, S.K. / Becker, S. / Habeck, M. / Lange, A.
History
DepositionSep 11, 2015Deposition site: BMRB / Processing site: RCSB
Revision 1.0Sep 23, 2015Provider: repository / Type: Initial release
SupersessionOct 7, 2015ID: 2MX3
Revision 1.1Oct 7, 2015Group: Advisory
Revision 1.2Oct 14, 2015Group: Database references

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: FimA
B: FimA
C: FimA
D: FimA
E: FimA
F: FimA


Theoretical massNumber of molelcules
Total (without water)95,7996
Polymers95,7996
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 / 1100target function
RepresentativeModel #1lowest energy

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Components

#1: Protein
FimA / Fimbrial protein / Type-1 fimbrial protein subunit A / Type-1 fimbrial protein / A chain


Mass: 15966.440 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: fimA, JW4277, PGD_03541, pilA / Production host: Escherichia coli (E. coli) / References: UniProt: Q547G4, UniProt: P04128*PLUS

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Experimental details

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Experiment

ExperimentMethod: SOLID-STATE NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NCACB 2D
121N(CO)CACB 3D
131NCACB 3D
141NCOCA 3D
151CANCO 3D
161NCACO 3D
171NCACO 2D
181N(CO)CACB 2D
191NCOCA 2D
1101NCO 2D
1111NCA 2D
1121CC PDSD
1132CC PDSD
1142CC PDSD

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Sample preparation

Details
Solution-IDContentsSolvent system
180-90 uM [U-100% 13C; U-100% 15N] FimA, 10 mM sodium phosphate pH 7.010 mM sodium phosphate
280-90 uM 2-glycerol 13C; U-100% 15N FimA, 10 mM sodium phosphate pH 7.010 mM sodium phosphate
Sample
Conc. (mg/ml)UnitsComponentIsotopic labelingConc. range (mg/ml)Solution-ID
uMFimA-1[U-100% 13C; U-100% 15N]80-901
10 mMsodium phosphate-21
uMFimA-32-glycerol 13C; U-100% 15N80-902
10 mMsodium phosphate-42
Sample conditionspH: 7 / Pressure: 1 atm / Temperature: 280 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AvanceBrukerAvance8501
Bruker AvanceBrukerAvance6002

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Processing

NMR software
NameDeveloperClassification
CcpNMR_AnalysisCCPNchemical shift assignment
ISDRieping, Nilges, Habeckrefinement
RefinementMethod: torsion angle dynamics / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 1100 / Conformers submitted total number: 10

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