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- PDB-6eai: CRYSTAL STRUCTURE OF HUMAN RESPIRATORY SYNCYTIAL VIRUS FUSION GLY... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6eai | |||||||||
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Title | CRYSTAL STRUCTURE OF HUMAN RESPIRATORY SYNCYTIAL VIRUS FUSION GLYCOPROTEIN INHIBITOR ESCAPE VARIANT S398L STABILIZED IN THE PREFUSION STATE | |||||||||
![]() | Fusion glycoprotein F0 | |||||||||
![]() | VIRAL PROTEIN / CLASS I VIRAL FUSION PROTEIN / FUSION / RESPIRATORY SYNCYTIAL VIRUS / PREFUSION / FUSION INHIBITOR | |||||||||
Function / homology | ![]() positive regulation of syncytium formation by virus / Translation of respiratory syncytial virus mRNAs / RSV-host interactions / host cell Golgi membrane / Maturation of hRSV A proteins / Assembly and release of respiratory syncytial virus (RSV) virions / Respiratory syncytial virus (RSV) attachment and entry / entry receptor-mediated virion attachment to host cell / symbiont entry into host cell / fusion of virus membrane with host plasma membrane ...positive regulation of syncytium formation by virus / Translation of respiratory syncytial virus mRNAs / RSV-host interactions / host cell Golgi membrane / Maturation of hRSV A proteins / Assembly and release of respiratory syncytial virus (RSV) virions / Respiratory syncytial virus (RSV) attachment and entry / entry receptor-mediated virion attachment to host cell / symbiont entry into host cell / fusion of virus membrane with host plasma membrane / viral envelope / host cell plasma membrane / virion membrane / identical protein binding / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Battles, M.B. / McLellan, J.S. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural Basis for Respiratory Syncytial Virus Fusion Inhibitor Resistance Authors: Battles, M.B. / McLellan, J.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 | ![]() | 272 KB | Display | ![]() |
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PDB format | ![]() | 215 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 536.6 KB | Display | ![]() |
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Full document | ![]() | 553.3 KB | Display | |
Data in XML | ![]() | 46.1 KB | Display | |
Data in CIF | ![]() | 61.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6eadC ![]() 6eaeC ![]() 6eafC ![]() 6eagC ![]() 6eahC ![]() 6eajC ![]() 6eakC ![]() 6ealC ![]() 6eamC ![]() 6eanC ![]() 5ea4S S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
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Components
-Protein / Sugars , 2 types, 6 molecules ABC![](data/chem/img/NAG.gif)
![](data/chem/img/NAG.gif)
#1: Protein | Mass: 63244.422 Da / Num. of mol.: 3 / Fragment: RSV F ectodomain / Mutation: S155C, S290C, S190F, V207L, S398L Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Sugar | |
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-Non-polymers , 4 types, 37 molecules ![](data/chem/img/SO4.gif)
![](data/chem/img/NHE.gif)
![](data/chem/img/TAR.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/NHE.gif)
![](data/chem/img/TAR.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-SO4 / #4: Chemical | ChemComp-NHE / #5: Chemical | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.22 Å3/Da / Density % sol: 61.77 % / Mosaicity: 0.41 ° |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 9.5 / Details: 1.52M K/Na tartrate, 0.2M LiSO4, 0.1M CHES pH 9.5 |
-Data collection
Diffraction | Mean temperature: 80 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jul 20, 2016 |
Radiation | Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9793 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→43.61 Å / Num. obs: 60906 / % possible obs: 99.3 % / Redundancy: 6.8 % / Biso Wilson estimate: 72.57 Å2 / CC1/2: 0.997 / Rmerge(I) obs: 0.103 / Rpim(I) all: 0.039 / Rrim(I) all: 0.111 / Net I/σ(I): 12.5 / Num. measured all: 415693 / Scaling rejects: 11 |
Reflection shell | Resolution: 2.8→2.87 Å / Redundancy: 6.2 % / Rmerge(I) obs: 1.246 / Num. unique obs: 4451 / CC1/2: 0.525 / Rpim(I) all: 0.485 / Rrim(I) all: 1.344 / % possible all: 99.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 5EA4 Resolution: 2.8→43.608 Å / SU ML: 0.38 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 24.3
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 213.98 Å2 / Biso mean: 80.8653 Å2 / Biso min: 29.71 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.8→43.608 Å
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Refine LS restraints NCS |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 22
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