[English] 日本語
![](img/lk-miru.gif)
- PDB-6nyx: Human parainfluenza virus type 3 fusion protein N-terminal heptad... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 6nyx | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Human parainfluenza virus type 3 fusion protein N-terminal heptad repeat domain+VI | |||||||||
![]() | (Fusion glycoprotein F0) x 2 | |||||||||
![]() | ANTIVIRAL PROTEIN / Fusion protein / fusion inhibitor / six-helix bundle | |||||||||
Function / homology | ![]() symbiont entry into host cell / fusion of virus membrane with host plasma membrane / viral envelope / host cell plasma membrane / virion membrane / membrane / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Outlaw, V.K. / Kreitler, D.F. / Gellman, S.H. | |||||||||
Funding support | ![]()
| |||||||||
![]() | ![]() Title: Dual Inhibition of Human Parainfluenza Type 3 and Respiratory Syncytial Virus Infectivity with a Single Agent. Authors: Outlaw, V.K. / Bottom-Tanzer, S. / Kreitler, D.F. / Gellman, S.H. / Porotto, M. / Moscona, A. | |||||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 310 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 237.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 575.9 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 582.6 KB | Display | |
Data in XML | ![]() | 29.7 KB | Display | |
Data in CIF | ![]() | 44.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6nroC ![]() 6ntxC ![]() 1ztmS S: Starting model for refinement C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||||||
2 | ![]()
| ||||||||||||
3 | ![]()
| ||||||||||||
4 | ![]()
| ||||||||||||
5 | ![]()
| ||||||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 5656.473 Da / Num. of mol.: 9 / Fragment: UNP residues 139-189 / Source method: obtained synthetically Details: This compound is derived from residues 139-189 of the HPIV3 fusion glycoprotein. It is acetylated at the N-terminus and amidated at the C-terminus. Source: (synth.) ![]() #2: Protein/peptide | Mass: 4196.825 Da / Num. of mol.: 9 / Fragment: UNP residues 449-484 / Mutation: E459V, A463I / Source method: obtained synthetically Details: VI is a synthetic peptide derived from residues 449-484 of the HPIV3 fusion glycoprotein C-terminal heptad repeat domain with substitutions E459V and A463I. It is acetylated at the N- ...Details: VI is a synthetic peptide derived from residues 449-484 of the HPIV3 fusion glycoprotein C-terminal heptad repeat domain with substitutions E459V and A463I. It is acetylated at the N-terminus and amidated at the C-terminus. Source: (synth.) ![]() #3: Chemical | ChemComp-PG4 / | #4: Chemical | ChemComp-PEG / | #5: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2 Å3/Da / Density % sol: 38.48 % |
---|---|
Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 30 mM NaF, 30 mM NaBr, 30 mM NaI, 20% (v/v) PEG 500 MME, 10% (w/v) PEG 20000 in 100 mM imidazole/MES monohydrate buffer (pH 6.5) |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Feb 13, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97856 Å / Relative weight: 1 |
Reflection | Resolution: 1.85→38.12 Å / Num. obs: 56066 / % possible obs: 99.82 % / Redundancy: 5.7 % / Biso Wilson estimate: 31.14 Å2 / CC1/2: 0.999 / Rpim(I) all: 0.03216 / Rrim(I) all: 0.07694 / Rsym value: 0.06986 / Net I/σ(I): 12.85 |
Reflection shell | Resolution: 1.85→1.916 Å / Redundancy: 5.4 % / Mean I/σ(I) obs: 1.35 / Num. unique obs: 5640 / CC1/2: 0.66 / Rpim(I) all: 0.5373 / Rrim(I) all: 1.254 / Rsym value: 1.132 / % possible all: 99.96 |
-
Processing
Software |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: 1ZTM Resolution: 1.85→38.12 Å / SU ML: 0.2386 / Cross valid method: FREE R-VALUE / σ(F): 1.97 / Phase error: 24.7929
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 45.67 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.85→38.12 Å
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell |
|