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- PDB-1hu5: SOLUTION STRUCTURE OF OVISPIRIN-1 -

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Basic information

Entry
Database: PDB / ID: 1hu5
TitleSOLUTION STRUCTURE OF OVISPIRIN-1
ComponentsOVISPIRIN-1
KeywordsUNKNOWN FUNCTION / solution structure
MethodSOLUTION NMR / simulated annealing, torsion angle dynamics
AuthorsSawai, M.V. / Waring, A.J. / Kearney, W.R. / McCray Jr., P.B. / Forsyth, W.R. / Lehrer, R.I. / Tack, B.F.
CitationJournal: Protein Eng. / Year: 2002
Title: Impact of single-residue mutations on the structure and function of ovispirin/novispirin antimicrobial peptides.
Authors: Sawai, M.V. / Waring, A.J. / Kearney, W.R. / McCray Jr., P.B. / Forsyth, W.R. / Lehrer, R.I. / Tack, B.F.
History
DepositionJan 4, 2001Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 5, 2002Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: OVISPIRIN-1


Theoretical massNumber of molelcules
Total (without water)2,2711
Polymers2,2711
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)20 / 50target function
RepresentativeModel #1lowest target function

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Components

#1: Protein/peptide OVISPIRIN-1


Mass: 2270.896 Da / Num. of mol.: 1 / Source method: obtained synthetically

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D NOESY
121DQF-COSY
131TOCSY

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Sample preparation

DetailsContents: 0.88 mM OVISPIRIN-1; 50 mM sodium phosphate buffer
Solvent system: 50% H2O, 40% TFE-D3, 10% D2O
Sample conditionsIonic strength: 0.05 / pH: 6.32 / Pressure: 1 atm / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometerType: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 500 MHz

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Processing

NMR software
NameVersionDeveloperClassification
DYANA1.5Guentertstructure solution
DYANA1.5Guentertrefinement
RefinementMethod: simulated annealing, torsion angle dynamics / Software ordinal: 1
Details: The structures are based on 172 distance constraints and 25 dihedral angle constraints.
NMR representativeSelection criteria: lowest target function
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 50 / Conformers submitted total number: 20

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