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- PDB-2npl: NMR Structure of CARD d2 Domain -

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Basic information

Entry
Database: PDB / ID: 2npl
TitleNMR Structure of CARD d2 Domain
ComponentsCoxsackievirus and Adenovirus Receptor
KeywordsCELL ADHESION / Coxsakievirus and Adenovirus Receptor
Function / homology
Function and homology information


AV node cell-bundle of His cell adhesion involved in cell communication / cell adhesive protein binding involved in AV node cell-bundle of His cell communication / homotypic cell-cell adhesion / AV node cell to bundle of His cell communication / epithelial structure maintenance / regulation of AV node cell action potential / gamma-delta T cell activation / apicolateral plasma membrane / germ cell migration / transepithelial transport ...AV node cell-bundle of His cell adhesion involved in cell communication / cell adhesive protein binding involved in AV node cell-bundle of His cell communication / homotypic cell-cell adhesion / AV node cell to bundle of His cell communication / epithelial structure maintenance / regulation of AV node cell action potential / gamma-delta T cell activation / apicolateral plasma membrane / germ cell migration / transepithelial transport / cardiac muscle fiber development / negative regulation of cardiac muscle cell proliferation / cell-cell junction organization / connexin binding / heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules / intercalated disc / bicellular tight junction / actin cytoskeleton reorganization / acrosomal vesicle / mitochondrion organization / filopodium / cell adhesion molecule binding / PDZ domain binding / neutrophil chemotaxis / adherens junction / neuromuscular junction / beta-catenin binding / virus receptor activity / cell body / cell junction / cell-cell junction / growth cone / integrin binding / defense response to virus / regulation of immune response / heart development / leukocyte migration / basolateral plasma membrane / neuron projection / membrane raft / signaling receptor binding / integral component of plasma membrane / protein-containing complex / extracellular space / extracellular region / nucleoplasm / identical protein binding / plasma membrane / cytoplasm
Immunoglobulin-like domain / Immunoglobulin subtype / Immunoglobulin subtype 2 / Immunoglobulin V-set domain / Immunoglobulin domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold / Immunoglobulin / Immunoglobulins / Immunoglobulin-like ...Immunoglobulin-like domain / Immunoglobulin subtype / Immunoglobulin subtype 2 / Immunoglobulin V-set domain / Immunoglobulin domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold / Immunoglobulin / Immunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta
Coxsackievirus and adenovirus receptor
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / SA
Model type detailsminimized average
AuthorsJiang, S. / Caffrey, M.
CitationJournal: Protein Sci. / Year: 2007
Title: Solution structure of the coxsackievirus and adenovirus receptor domain 2
Authors: Jiang, S. / Caffrey, M.
Validation Report
SummaryFull reportAbout validation report
History
DepositionOct 27, 2006Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 13, 2007Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: 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
X: Coxsackievirus and Adenovirus Receptor


Theoretical massNumber of molelcules
Total (without water)10,5401
Polymers10,5401
Non-polymers00
Water0
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)1 / 30lowest energy
RepresentativeModel #1minimized average structure

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Components

#1: Protein Coxsackievirus and Adenovirus Receptor / Coxsackievirus B- adenovirus receptor / hCAR / CVB3-binding protein / HCVADR


Mass: 10539.775 Da / Num. of mol.: 1 / Fragment: Domain CAR 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CXADR, CAR / Production host: Escherichia coli (E. coli) / References: UniProt: P78310

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 15N-separated NOESY
1212D NOESY
131HNHA
1413D 13C-separated NOESY

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DRXBrukerDRX6001
Bruker AvanceBrukerAvance8002

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Processing

NMR software
NameVersionDeveloperClassification
CNS1.1Brunger, et alstructure solution
CNS1.1Brunger, et alrefinement
RefinementMethod: SA / Software ordinal: 1
Details: Structure is based on the average structure of the 30 lowest energy structures with 488 distance restraints, 234 dihedral restraints and 47 hodrogen bond restraints.
NMR representativeSelection criteria: minimized average structure
NMR ensembleConformer selection criteria: lowest energy / Conformers calculated total number: 30 / Conformers submitted total number: 1

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