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- PDB-2b0f: NMR Structure of the Human Rhinovirus 3C Protease (serotype 14) w... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2b0f | ||||||||||||
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Title | NMR Structure of the Human Rhinovirus 3C Protease (serotype 14) with covalently bound Ace-LEALFQ-ethylpropionate inhibitor | ||||||||||||
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![]() | HYDROLASE/HYDROLASE INHIBITOR / BETA BARREL / HYDROLASE-HYDROLASE INHIBITOR COMPLEX | ||||||||||||
Function / homology | ![]() lysis of host organelle involved in viral entry into host cell / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / endocytosis involved in viral entry into host cell / nucleoside-triphosphate phosphatase ...lysis of host organelle involved in viral entry into host cell / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / endocytosis involved in viral entry into host cell / nucleoside-triphosphate phosphatase / protein complex oligomerization / monoatomic ion channel activity / symbiont-mediated suppression of host gene expression / DNA replication / RNA helicase activity / induction by virus of host autophagy / RNA-directed RNA polymerase / viral RNA genome replication / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity / virus-mediated perturbation of host defense response / DNA-templated transcription / host cell nucleus / virion attachment to host cell / structural molecule activity / ATP hydrolysis activity / proteolysis / RNA binding / ATP binding / membrane / metal ion binding Similarity search - Function | ||||||||||||
Biological species | ![]() synthetic construct (others) | ||||||||||||
Method | SOLUTION NMR / simulated annealing, molecular dynamics torsion angle dynamics RECOORD water refinement | ||||||||||||
![]() | Bjorndahl, T.C. / Andrew, L.C. / Wishart, D.S. | ||||||||||||
![]() | ![]() Title: NMR solution structures of the apo and peptide-inhibited human rhinovirus 3C protease (Serotype 14): structural and dynamic comparison Authors: Bjorndahl, T.C. / Andrew, L.C. / Semenchenko, V. / Wishart, D.S. | ||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.1 MB | Display | ![]() |
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PDB format | ![]() | 962.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 369 KB | Display | ![]() |
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Full document | ![]() | 597.1 KB | Display | |
Data in XML | ![]() | 79.8 KB | Display | |
Data in CIF | ![]() | 100.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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 | Mass: 20021.877 Da / Num. of mol.: 1 / Fragment: Human Rhinovirus serotype 14 3C Protease Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 801.970 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: Peptidyl inhibitor synthesized via solid and solution phase pedtide synthesis Source: (synth.) synthetic construct (others) |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: H-bond donors determined from 15N HSQC exchanged into D2O. 3J HNHA couplings determined from HNHA. 13C-seperated NOESY collected in 99.96% D2O without wet water suppression to achieve cross ...Text: H-bond donors determined from 15N HSQC exchanged into D2O. 3J HNHA couplings determined from HNHA. 13C-seperated NOESY collected in 99.96% D2O without wet water suppression to achieve cross strand beta-sheet HA-HA NOEs. |
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Sample preparation
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Sample conditions |
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-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 500 MHz |
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Processing
NMR software |
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Refinement | Method: simulated annealing, molecular dynamics torsion angle dynamics RECOORD water refinement Software ordinal: 1 | ||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||
NMR ensemble | Conformer selection criteria: back calculated data agree with experimental NOESY spectrum,structures with acceptable covalent geometry,structures with favorable non-bond energy,structures with the ...Conformer selection criteria: back calculated data agree with experimental NOESY spectrum,structures with acceptable covalent geometry,structures with favorable non-bond energy,structures with the least restraint violations,structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |