+Open data
-Basic information
Entry | Database: PDB / ID: 1n1u | ||||||
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Title | NMR structure of [Ala1,15]kalata B1 | ||||||
Components | kalata B1 | ||||||
Keywords | ANTIBIOTIC / cystine knot / triple stranded beta sheet / cyclic peptide | ||||||
Function / homology | Cyclotide, moebius, conserved site / Cyclotides Moebius subfamily signature. / Cyclotides profile. / Cyclotide / Cyclotide superfamily / Cyclotide family / killing of cells of another organism / defense response to bacterium / Kalata-B1 Function and homology information | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Daly, N.L. / Clark, R.J. / Craik, D.J. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2003 Title: Disulfide Folding Pathways of Cystine Knot Proteins. TYING THE KNOT WITHIN THE CIRCULAR BACKBONE OF THE CYCLOTIDES Authors: Daly, N.L. / Clark, R.J. / Craik, D.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1n1u.cif.gz | 129.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1n1u.ent.gz | 103.1 KB | Display | PDB format |
PDBx/mmJSON format | 1n1u.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/n1/1n1u ftp://data.pdbj.org/pub/pdb/validation_reports/n1/1n1u | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 2853.215 Da / Num. of mol.: 1 / Mutation: A1C, A15C / Source method: obtained synthetically Details: This sequence has Cys1 and Cys15, of the naturally occurring kalata B1 peptide, replaced with Ala residues. References: UniProt: P56254 |
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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: 1mM [Ala1,15]kalata B1 / Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 0 / pH: 3.8 / Pressure: ambient / Temperature: 290 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: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 750 MHz |
-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 Details: The structures are based on a total of 321 NOE derived distance restraints, 19 angle restraints and 20 distance restraints from hydrogen bonds. | ||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 20 |