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- PDB-2bzm: Solution structure of the primary host recognition region of comp... -

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Basic information

Entry
Database: PDB / ID: 2bzm
TitleSolution structure of the primary host recognition region of complement factor H
ComponentsCOMPLEMENT FACTOR H
KeywordsIMMUNE SYSTEM / FACTOR H / COMPLEMENT / HUS / HEPARIN / POLYANIONS / IMMUNE RESPONSE / INNATE IMMUNITY / COMPLEMENT ALTERNATE PATHWAY
Function / homology
Function and homology information


regulation of complement activation, alternative pathway / symbiont cell surface / regulation of complement-dependent cytotoxicity / complement component C3b binding / regulation of complement activation / heparan sulfate proteoglycan binding / serine-type endopeptidase complex / complement activation / complement activation, alternative pathway / Regulation of Complement cascade ...regulation of complement activation, alternative pathway / symbiont cell surface / regulation of complement-dependent cytotoxicity / complement component C3b binding / regulation of complement activation / heparan sulfate proteoglycan binding / serine-type endopeptidase complex / complement activation / complement activation, alternative pathway / Regulation of Complement cascade / heparin binding / blood microparticle / proteolysis / extracellular space / extracellular exosome / extracellular region / identical protein binding
Similarity search - Function
: / Complement Module, domain 1 / Complement Module; domain 1 / Sushi repeat (SCR repeat) / Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR) / Sushi/SCR/CCP domain / Sushi/CCP/SCR domain profile. / Sushi/SCR/CCP superfamily / Ribbon / Mainly Beta
Similarity search - Domain/homology
Biological speciesHOMO SAPIENS (human)
MethodSOLUTION NMR / RESTRAINED MOLECULAR DYNAMICS
AuthorsHerbert, A.P. / Uhrin, D. / Lyon, M. / Pangburn, M.K. / Barlow, P.N.
CitationJournal: J.Biol.Chem. / Year: 2006
Title: Disease-Associated Sequence Variations Congregate in a Polyanion Recognition Patch on Human Factor H Revealed in Three-Dimensional Structure.
Authors: Herbert, A.P. / Uhrin, D. / Lyon, M. / Pangburn, M.K. / Barlow, P.N.
History
DepositionAug 18, 2005Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 22, 2006Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: COMPLEMENT FACTOR H


Theoretical massNumber of molelcules
Total (without water)14,7741
Polymers14,7741
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)26 / -LOWEST OVERALL ENERGY
RepresentativeModel #1

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Components

#1: Protein COMPLEMENT FACTOR H / H FACTOR 1


Mass: 14773.793 Da / Num. of mol.: 1 / Fragment: CCPS 19-20, RESIDUES 1107-1231
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: PICHIA PASTORIS (fungus) / Strain (production host): KM71H / References: UniProt: P08603

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D-15N-HSQC-NOESY
1213D-13C- HSQC-NOESY
NMR detailsText: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED FACTOR H CCP MODULES 19-20

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Sample preparation

DetailsContents: 10% WATER/90% D2O
Sample conditionsIonic strength: 200 mM / pH: 4 / Pressure: 1.0 atm / Temperature: 310.0 K

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NMR measurement

NMR spectrometerType: Bruker AM / Manufacturer: Bruker / Model: AM / Field strength: 800 MHz

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Processing

NMR software
NameDeveloperClassification
CNSBRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE- KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ, RICE,SIMONSON,WARRENrefinement
ANSIGstructure solution
RefinementMethod: RESTRAINED MOLECULAR DYNAMICS / Software ordinal: 1
NMR ensembleConformer selection criteria: LOWEST OVERALL ENERGY / Conformers submitted total number: 26

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