+Open data
-Basic information
Entry | Database: PDB / ID: 2kvx | ||||||
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Title | Solution structure of kalata B12 | ||||||
Components | Kalata-B12 | ||||||
Keywords | PLANT PROTEIN / kalata | ||||||
Function / homology | Cyclotide / Cyclotide superfamily / Cyclotide family / defense response / Kalata-B12 Function and homology information | ||||||
Biological species | Oldenlandia affinis (plant) | ||||||
Method | SOLUTION NMR / molecular dynamics | ||||||
Authors | Wang, C.K. | ||||||
Citation | Journal: Biochemistry / Year: 2011 Title: The role of conserved Glu residue on cyclotide stability and activity: a structural and functional study of kalata B12, a naturally occurring Glu to Asp mutant. Authors: Wang, C.K. / Clark, R.J. / Harvey, P.J. / Rosengren, K.J. / Cemazar, M. / 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 | 2kvx.cif.gz | 128.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2kvx.ent.gz | 103.7 KB | Display | PDB format |
PDBx/mmJSON format | 2kvx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2kvx_validation.pdf.gz | 327 KB | Display | wwPDB validaton report |
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Full document | 2kvx_full_validation.pdf.gz | 414.9 KB | Display | |
Data in XML | 2kvx_validation.xml.gz | 10.3 KB | Display | |
Data in CIF | 2kvx_validation.cif.gz | 16.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kv/2kvx ftp://data.pdbj.org/pub/pdb/validation_reports/kv/2kvx | HTTPS FTP |
-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: 2905.289 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: The peptide was chemically synthesized. / Source: (synth.) Oldenlandia affinis (plant) / References: UniProt: P85130 |
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Sequence details | THIS PEPTIDE IS CYCLIC |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 0.3 mM protein, 90% H2O/10% D2O / Solvent system: 90% H2O/10% D2O |
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Sample | Conc.: 0.3 mM / Component: entity-1 |
Sample conditions | Ionic strength: 0 / pH: 5 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker ARX / Manufacturer: Bruker / Model: ARX / Field strength: 900 MHz |
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-Processing
NMR software |
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Refinement | Method: molecular dynamics / Software ordinal: 1 | ||||||
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 / Representative conformer: 1 |