1NEB

SH3 DOMAIN FROM HUMAN NEBULIN, NMR, MINIMIZED AVERAGE STRUCTURE

> Summary

Summary for 1NEB

DescriptorNEBULIN
Functional Keywordssh3 domain, nebulin, z-disk assembly, actin-binding
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm, myofibril, sarcomere P20929
Total number of polymer chains1
Total molecular weight6614.46
Authors
Politou, A.S.,Pastore, A. (deposition date: 1997-08-07, release date: 1997-12-24, modification date: 2009-02-24)
Primary citation
Politou, A.S.,Millevoi, S.,Gautel, M.,Kolmerer, B.,Pastore, A.
SH3 in muscles: solution structure of the SH3 domain from nebulin.
J.Mol.Biol., 276:189-202, 1998
PubMed: 9514727
DOI: 10.1006/jmbi.1997.1521
MImport into Mendeley
Experimental method
SOLUTION NMR
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Structure validation

ClashscoreRamachandran outliersSidechain outliers115.2%20.0%MetricValuePercentile RanksWorseBetterPercentile relative to all structuresPercentile relative to all NMR structures

More Asymmetric unit images

Molmil generated image of 1neb
no rotation
Molmil generated image of 1neb
rotated about x axis by 90°
Molmil generated image of 1neb
rotated about y axis by 90°

> Structural details

Entity

Chain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
ANEBULINpolymer606614.51
UniProt (P20929)
Pfam (PF14604)
Homo sapiens (human)@PDBj

Sequence viewer

Contents of the asymmetric unit

PolymersNumber of chains1
Total molecular weight6614.5
Non-Polymers*Number of molecules0
Total molecular weight0.0
All*Total molecular weight6614.5
*Water molecules are not included.

> Experimental details

Spectrometer

Experimental method:SOLUTION NMR
Spectrometer IDSpectrometer makerSpectrometer modelSpectrometer typeSpectrometer field strength
1BRUKERAMX500
2BRUKERAMX600

Experiment

experiment idconditions idsolution idExperiment type
111NOESY
211TOCSY
311DQF-COSY

NMR Sample

conditions idNMR sample pHNMR sample pressureNMR sample temperature
16.9300

Conformers

Conformers Calculated Total Number100
Conformers Submitted Total Number1

> Functional details

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Functional Information from GO Data

ChainGOidnamespacecontents
A0015629cellular_componentactin cytoskeleton
A0005829cellular_componentcytosol
A0070062cellular_componentextracellular exosome
A0030018cellular_componentZ disc
A0008307molecular_functionstructural constituent of muscle
A0030049biological_processmuscle filament sliding
A0007517biological_processmuscle organ development
A0030832biological_processregulation of actin filament length
A0007525biological_processsomatic muscle development
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Functional Information from PDB Data

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Functional Information from PDB atom coordinates for the "HETATM" binding sites

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Functional Information from PROSITE/UniProt

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Functional Information from SwissProt/UniProt

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Catalytic Information from CSA

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Catalytic Information from CATRES

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> Sequence Neighbor

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