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- PDB-1hr1: Structure of an indolicidin peptide derivative with P-->A substitution -
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Open data
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Basic information
Entry | Database: PDB / ID: 1hr1 | ||||||
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Title | Structure of an indolicidin peptide derivative with P-->A substitution | ||||||
![]() | INDOLICIDIN | ||||||
![]() | ANTIBIOTIC / ANTIMICROBIAL PROTEIN / alpha-helix / cationic antimicrobial peptide | ||||||
Function / homology | ![]() Antimicrobial peptides / Neutrophil degranulation / defense response to fungus / lipopolysaccharide binding / antimicrobial humoral immune response mediated by antimicrobial peptide / defense response to Gram-negative bacterium / killing of cells of another organism / defense response to Gram-positive bacterium / innate immune response / extracellular space Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / distance geometry, simulated annealing | ||||||
![]() | Friedrich, C.L. / Rozek, A. / Patrzykat, A. / Hancock, R.E.W. | ||||||
![]() | ![]() Title: Structure and mechanism of action of an indolicidin peptide derivative with improved activity against Gram-positive bacteria Authors: Friedrich, C.L. / Rozek, A. / Patrzykat, A. / Hancock, R.E.W. #1: ![]() Title: Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles. Authors: Rozek, A. / Friedrich, C.L. / Hancock, R.E.W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 72.7 KB | Display | ![]() |
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PDB format | ![]() | 56 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 339.5 KB | Display | ![]() |
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Full document | ![]() | 423.6 KB | Display | |
Data in XML | ![]() | 6.8 KB | Display | |
Data in CIF | ![]() | 10 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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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: 1830.188 Da / Num. of mol.: 1 / Mutation: P3A,P7A,P10A / Source method: obtained synthetically Details: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE OCCURS NATURALLY IN BOS TAURUS. THE SEQUENCE IS NATURALLY AMIDATED AT C-TERMINUS. Source: (synth.) ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: 2D NOESY |
NMR details | Text: This structure was determined using standard 2D homonuclear techniques. |
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Sample preparation
Details | Contents: 2mM CP10A; 200mM dodecylphosphocholine / Solvent system: 10 mM phosphate buffer; 90%H2O,10%D2O |
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Sample conditions | Ionic strength: 200mM DPC / pH: 4.0 / Pressure: ambient / Temperature: 310 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AMX / Manufacturer: Bruker / Model: AMX / Field strength: 600 MHz |
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Processing
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Refinement | Method: distance geometry, simulated annealing / Software ordinal: 1 Details: The structures are based on 167 (non-redundant) NOE-derived distance restraints, 77 intraresidue and 90 inter-residue restraints. Structures were generated using DGII (MSI) and then refined using XPLOR. | ||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations,structures with the lowest energy Conformers calculated total number: 20 / Conformers submitted total number: 15 |