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Open data
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Basic information
Entry | Database: PDB / ID: 2lr5 | ||||||
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Title | 1H chemical shift assignments for micasin | ||||||
![]() | micasin | ||||||
![]() | ANTIMICROBIAL PROTEIN | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Model details | lowest energy, model 1 | ||||||
![]() | Harvey, P.J. / Craik, D.J. / Zhu, S. | ||||||
![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 211 KB | Display | ![]() |
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PDB format | ![]() | 177.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 507.9 KB | Display | ![]() |
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Full document | ![]() | 670.8 KB | Display | |
Data in XML | ![]() | 22.3 KB | Display | |
Data in CIF | ![]() | 29.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | |
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Links
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Assembly
Deposited unit | ![]()
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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.) ![]() |
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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 |