+Open data
-Basic information
Entry | Database: PDB / ID: 2lr5 | ||||||
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Title | 1H chemical shift assignments for micasin | ||||||
Components | micasin | ||||||
Keywords | ANTIMICROBIAL PROTEIN | ||||||
Biological species | Arthroderma otae (fungus) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Harvey, P.J. / Craik, D.J. / Zhu, S. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2012 Title: Dermatophytic defensin with antiinfective potential Authors: Zhu, S. / Gao, B. / Harvey, P.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 | 2lr5.cif.gz | 211 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2lr5.ent.gz | 177.4 KB | Display | PDB format |
PDBx/mmJSON format | 2lr5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2lr5_validation.pdf.gz | 507.9 KB | Display | wwPDB validaton report |
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Full document | 2lr5_full_validation.pdf.gz | 670.8 KB | Display | |
Data in XML | 2lr5_validation.xml.gz | 22.3 KB | Display | |
Data in CIF | 2lr5_validation.cif.gz | 29.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lr/2lr5 ftp://data.pdbj.org/pub/pdb/validation_reports/lr/2lr5 | 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: 4067.702 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Arthroderma otae (fungus) |
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Sequence details | THE SEQUENCE OF THIS PROTEIN WAS NOT AVAILABLE AT THE UNIPROT KNOWLEDGEBASE DATABASE (UNIPROTKB) AT ...THE SEQUENCE OF THIS PROTEIN WAS NOT AVAILABLE AT THE UNIPROT KNOWLEDGEB |
-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: 3 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 261 / NOE intraresidue total count: 79 / NOE long range total count: 29 / NOE medium range total count: 49 / NOE sequential total count: 93 / Protein chi angle constraints total count: 7 / Protein phi angle constraints total count: 28 / Protein psi angle constraints total count: 19 | ||||||||||||||||||||||||||||
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 |