+Open data
-Basic information
Entry | Database: PDB / ID: 1hu5 | ||||||
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Title | SOLUTION STRUCTURE OF OVISPIRIN-1 | ||||||
Components | OVISPIRIN-1 | ||||||
Keywords | UNKNOWN FUNCTION / solution structure | ||||||
Method | SOLUTION NMR / simulated annealing, torsion angle dynamics | ||||||
Authors | Sawai, M.V. / Waring, A.J. / Kearney, W.R. / McCray Jr., P.B. / Forsyth, W.R. / Lehrer, R.I. / Tack, B.F. | ||||||
Citation | Journal: 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 |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1hu5.cif.gz | 131.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1hu5.ent.gz | 93.3 KB | Display | PDB format |
PDBx/mmJSON format | 1hu5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hu/1hu5 ftp://data.pdbj.org/pub/pdb/validation_reports/hu/1hu5 | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 2270.896 Da / Num. of mol.: 1 / Source method: obtained synthetically |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 0.88 mM OVISPIRIN-1; 50 mM sodium phosphate buffer Solvent system: 50% H2O, 40% TFE-D3, 10% D2O |
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Sample conditions | Ionic strength: 0.05 / pH: 6.32 / Pressure: 1 atm / Temperature: 298 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 500 MHz |
-Processing
NMR software |
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Refinement | Method: simulated annealing, torsion angle dynamics / Software ordinal: 1 Details: The structures are based on 172 distance constraints and 25 dihedral angle constraints. | ||||||||||||
NMR representative | Selection criteria: lowest target function | ||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 50 / Conformers submitted total number: 20 |