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- PDB-1pao: A COMPARISON OF NMR SOLUTION STRUCTURES OF THE RECEPTOR BINDING D... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1pao | ||||||
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Title | A COMPARISON OF NMR SOLUTION STRUCTURES OF THE RECEPTOR BINDING DOMAINS OF PSEUDOMONAS AERUGINOSA PILI STRAINS PAO, KB7, AND PAK: IMPLICATIONS FOR RECEPTOR BINDING AND SYNTHETIC VACCINE DESIGN | ||||||
![]() | PAO PILIN, TRANS | ||||||
![]() | FIMBRIAL PROTEIN | ||||||
Function / homology | ![]() type IV pilus / type IV pilus-dependent motility / single-species biofilm formation on inanimate substrate / cell adhesion involved in single-species biofilm formation / pilus / regulation of calcium-mediated signaling / host cell endoplasmic reticulum membrane / cell surface / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Campbell, A.P. / Mcinnes, C. / Hodges, R.S. / Sykes, B.D. | ||||||
![]() | ![]() Title: Comparison of NMR solution structures of the receptor binding domains of Pseudomonas aeruginosa pili strains PAO, KB7, and PAK: implications for receptor binding and synthetic vaccine design. Authors: Campbell, A.P. / McInnes, C. / Hodges, R.S. / Sykes, B.D. #1: ![]() Title: Conformational Differences between Cis and Trans Proline Isomers of a Peptide Antigen Representing the Receptor Binding Domain of Pseudomonas Aeruginosa as Studied by 1H NMR Authors: Mcinnes, C. / Kay, C.M. / Hodges, R.S. / Sykes, B.D. #2: ![]() Title: NMR Solution Structure and Flexibility of a Peptide Antigen Representing the Receptor Binding Domain of Pseudomonas Aeruginosa Authors: Mcinnes, C. / Soennichsen, F.D. / Kay, C.M. / Hodges, R.S. / Sykes, B.D. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 141.7 KB | Display | ![]() |
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PDB format | ![]() | 110.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 323.8 KB | Display | ![]() |
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Full document | ![]() | 408.7 KB | Display | |
Data in XML | ![]() | 8.9 KB | Display | |
Data in CIF | ![]() | 15.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1kb7C ![]() 1kb8C ![]() 1nilC ![]() 1nimC ![]() 1panC C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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NMR ensembles |
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Components
#1: Protein/peptide | Mass: 1871.120 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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Sample preparation
Crystal grow | *PLUS Method: other |
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Processing
NMR software | Name: PEPFLEX II / Classification: refinement |
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NMR ensemble | Conformers submitted total number: 33 |