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Yorodumi- PDB-2n5q: Solution structure of cystein-rich peptide jS1 from Jasminum sambac -
+Open data
-Basic information
Entry | Database: PDB / ID: 2n5q | ||||||
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Title | Solution structure of cystein-rich peptide jS1 from Jasminum sambac | ||||||
Components | cysteine-rich peptide jS1 | ||||||
Keywords | UNKNOWN FUNCTION / cystein-rich peptide | ||||||
Function / homology | Jasmintide 1 Function and homology information | ||||||
Biological species | Jasminum sambac (Arabian jasmine) | ||||||
Method | SOLUTION NMR / DGSA-distance geometry simulated annealing | ||||||
Model details | lowest energy, model1 | ||||||
Authors | Shin, J. / Kumari, G. / Serra, A. / Nguyen, P.Q.T. / Yoon, H. / Tam, J.P. | ||||||
Citation | Journal: To be Published Title: Identification of a cysteine-rich peptide family with unusual disulfide connectivity from Jasminum sambac Authors: Shin, J. / Kumari, G. / Serra, A. / Nguyen, P.Q.T. / Yoon, H. / Sze, S. / Tam, J.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2n5q.cif.gz | 164.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2n5q.ent.gz | 136.5 KB | Display | PDB format |
PDBx/mmJSON format | 2n5q.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2n5q_validation.pdf.gz | 492.5 KB | Display | wwPDB validaton report |
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Full document | 2n5q_full_validation.pdf.gz | 602.9 KB | Display | |
Data in XML | 2n5q_validation.xml.gz | 16.1 KB | Display | |
Data in CIF | 2n5q_validation.cif.gz | 23.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/n5/2n5q ftp://data.pdbj.org/pub/pdb/validation_reports/n5/2n5q | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 3132.690 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Jasminum sambac (Arabian jasmine) / References: UniProt: A0A0S2KUN2*PLUS |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | pH: 7 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 700 MHz |
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-Processing
NMR software |
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Refinement | Method: DGSA-distance geometry simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 / Representative conformer: 1 |