1WYP

Solution structure of the CH domain of human Calponin 1

> Summary

Summary for 1WYP

DescriptorCalponin 1
Functional Keywordsch domain, f-actin binding, all-alpha, structural genomics, nppsfa, riken structural genomics/proteomics initiative, rsgi, structural protein
Biological sourceHomo sapiens (human)
Total number of polymer chains1
Total molecular weight14991.91
Authors
Tomizawa, T.,Kigawa, T.,Koshiba, S.,Inoue, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2005-02-15, release date: 2005-08-15, modification date: 2009-02-24)
Primary citation
Tomizawa, T.,Kigawa, T.,Koshiba, S.,Inoue, M.,Yokoyama, S.
Solution structure of the CH domain of human Calponin 1
To be Published,
Experimental method
SOLUTION NMR
NMR Information
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Structure validation

ClashscoreRamachandran outliersSidechain outliers142.8%4.3%MetricValuePercentile RanksWorseBetterPercentile relative to all structuresPercentile relative to all NMR structures

More Asymmetric unit images

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

> Structural details

Entity

Chain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
ACalponin 1polymer13614991.91
UniProt (P51911)
Pfam (PF00307)
Homo sapiens (human)@PDBjCalponin H1, smooth muscle, Basic calponin

Sequence viewer

Contents of the asymmetric unit

PolymersNumber of chains1
Total molecular weight14991.9
Non-Polymers*Number of molecules0
Total molecular weight0.0
All*Total molecular weight14991.9
*Water molecules are not included.

> Experimental details

Spectrometer

Experimental method:SOLUTION NMR

Spectrometer IDSpectrometer makerSpectrometer modelSpectrometer typeSpectrometer field strength
1BrukerAVANCE800

Experiment

experiment idconditions idsolution idExperiment type
1113D_15N-separated_NOESY
2113D_13C-separated_NOESY

NMR Sample

conditions idNMR sample pHNMR sample pressureNMR sample temperature
17ambient298

Conformers

Conformers Calculated Total Number100
Conformers Submitted Total Number20

> Functional details

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Functional Information from GO Data

ChainGOidnamespacecontents
A0005856cellular_componentcytoskeleton
A0005925cellular_componentfocal adhesion
A0031032biological_processactomyosin structure organization
A0006940biological_processregulation of smooth muscle contraction
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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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