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- PDB-2k5x: Chemical shift structure of COLICIN E9 DNASE domain with its cogn... -
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Basic information
Entry | Database: PDB / ID: 2k5x | ||||||
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Title | Chemical shift structure of COLICIN E9 DNASE domain with its cognate immunity protein IM9 | ||||||
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![]() | IMMUNE SYSTEM/HYDROLASE / COLICIN E9 / IMMUNITY PROTEIN IM9 / Bacteriocin immunity / Plasmid / Antibiotic / Antimicrobial / Bacteriocin / Endonuclease / Hydrolase / Metal-binding / Nuclease / Zinc / IMMUNE SYSTEM-HYDROLASE COMPLEX | ||||||
Function / homology | ![]() extrachromosomal circular DNA / bacteriocin immunity / toxic substance binding / endonuclease activity / killing of cells of another organism / Hydrolases; Acting on ester bonds / defense response to bacterium / protein domain specific binding / protein-containing complex / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Montalvao, R.W. / Cavalli, A. / Vendruscolo, M. | ||||||
![]() | ![]() Title: Structure Determination of Protein-Protein Complexes Using NMR Chemical Shifts: Case of an Endonuclease Colicin-Immunity Protein Complex Authors: Montalvao, R.W. / Cavalli, A. / Salvatella, X. / Blundell, T.L. / Vendruscolo, M. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 56.3 KB | Display | ![]() |
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PDB format | ![]() | 40.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 246.3 KB | Display | ![]() |
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Full document | ![]() | 246.1 KB | Display | |
Data in XML | ![]() | 7 KB | Display | |
Data in CIF | ![]() | 9.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data | |
Other databases |
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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 | Mass: 9592.500 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein | Mass: 15120.021 Da / Num. of mol.: 1 / Fragment: UNP residues 450-582 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P09883, Hydrolases; Acting on ester bonds |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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Sample preparation
Sample conditions | pH: 6.2 / Temperature: 298 K |
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-NMR measurement
NMR spectrometer | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 500 MHz |
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Processing
NMR software | Name: CHESHIRE / Developer: Andrea Cavalli / Classification: geometry optimization |
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Refinement | Method: simulated annealing / Software ordinal: 1 / Details: CHESHIRE |
NMR representative | Selection criteria: lowest energy |
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 500 / Conformers submitted total number: 1 |