2NDE

Solution Structure of Mutant of BMAP-28(1-18)

> Summary

Summary for 2NDE

Related2NDC
DescriptorCathelicidin-5 (1 entity in total)
Functional Keywordsamp, antimicrobial protein
Biological sourceBos taurus (bovine)
Cellular locationSecreted P54229
Total number of polymer chains1
Total molecular weight1999.49
Authors
Agadi, N.,Kumar, A. (deposition date: 2016-05-12, release date: 2017-09-13)
Primary citation
Agadi, N.,Kumar, A.
Structure, Function And Membrane Interaction Studies of Two Synthetic Peptides Using Solution And Solid State NMR
To be Published,
Experimental method
SOLUTION NMR
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Structure validation

ClashscoreRamachandran outliersSidechain outliers62.3%3.0%MetricValuePercentile RanksWorseBetterPercentile relative to all structuresPercentile relative to all NMR structures

More Asymmetric unit images

Molmil generated image of 2nde
no rotation
Molmil generated image of 2nde
rotated about x axis by 90°
Molmil generated image of 2nde
rotated about y axis by 90°

> Structural details

Entity

Chain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
ACathelicidin-5polymer181999.51
UniProt (P54229)
Bos taurusAntibacterial peptide BMAP-28, Myeloid antibacterial peptide 28

Sequence viewer

Contents of the asymmetric unit

PolymersNumber of chains1
Total molecular weight1999.5
Non-Polymers*Number of molecules0
Total molecular weight0.0
All*Total molecular weight1999.5
*Water molecules are not included.

> Experimental details

Spectrometer

Experimental method:SOLUTION NMR

Spectrometer IDSpectrometer makerSpectrometer modelSpectrometer typeSpectrometer field strength
1BrukerASCENDBruker ASCEND750
2BrukerAvanceBruker Avance700

Experiment

experiment idconditions idsolution idExperiment type
1112D 1H-1H TOCSY
2112D 1H-15N HSQC
3112D 1H-13C HSQC
4112D 1H-1H NOESY

NMR Sample

conditions idNMR sample pHNMR sample pressureNMR sample temperature
16.6ambient298

Conformers

Conformers Calculated Total Number200
Conformers Submitted Total Number10

> Functional details

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Functional Information from GO Data

ChainGOidnamespacecontents
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Functional Information from PDB Data

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

site_idNumber of ResiduesDetails
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Functional Information from PROSITE/UniProt

site_idNumber of ResiduesDetails
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Functional Information from SwissProt/UniProt

site_idNumber of ResiduesDetails
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Catalytic Information from CSA

site_idNumber of ResiduesDetails

> Sequence Neighbor

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