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Yorodumi- PDB-3nwa: Glycoprotein B from Herpes simplex virus type 1, W174R mutant, low-pH -
+Open data
-Basic information
Entry | Database: PDB / ID: 3nwa | ||||||
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Title | Glycoprotein B from Herpes simplex virus type 1, W174R mutant, low-pH | ||||||
Components | Envelope glycoprotein B | ||||||
Keywords | VIRAL PROTEIN / Coiled-Coil / ENVELOPE GLYCOPROTEIN / MEMBRANE FUSION / Glycoprotein B / Herpesvirus 1 / HSV-1 / Membrane | ||||||
Function / homology | Function and homology information host cell Golgi membrane / host cell endosome membrane / symbiont entry into host cell / viral envelope / virion attachment to host cell / host cell plasma membrane / virion membrane / membrane / identical protein binding Similarity search - Function | ||||||
Biological species | Human herpesvirus 1 (Herpes simplex virus type 1) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2629 Å | ||||||
Authors | Stampfer, S.D. / Lou, H. / Cohen, G.H. / Eisenberg, R.J. / Heldwein, E.E. | ||||||
Citation | Journal: J.Virol. / Year: 2010 Title: Structural basis of local, pH-dependent conformational changes in glycoprotein B from herpes simplex virus type 1. Authors: Stampfer, S.D. / Lou, H. / Cohen, G.H. / Eisenberg, R.J. / Heldwein, E.E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3nwa.cif.gz | 537.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3nwa.ent.gz | 436.2 KB | Display | PDB format |
PDBx/mmJSON format | 3nwa.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nw/3nwa ftp://data.pdbj.org/pub/pdb/validation_reports/nw/3nwa | HTTPS FTP |
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-Related structure data
Related structure data | 3nw8C 3nwdC 3nwfC 2gumS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 78844.281 Da / Num. of mol.: 4 / Fragment: Ectodomain (UNP residues 30 to 730) / Mutation: W174R Source method: isolated from a genetically manipulated source Details: W174R mutation Source: (gene. exp.) Human herpesvirus 1 (Herpes simplex virus type 1) Strain: KOS / Gene: gB, UL27 / Plasmid: pVT-Bac / Production host: Spodoptera frugiperda (fall armyworm) / Strain (production host): SF9 / References: UniProt: P06437 #2: Sugar | ChemComp-NAG / #3: Chemical | ChemComp-MRY / #4: Water | ChemComp-HOH / | Sequence details | AUTHORS STATE THAT HSV-1 STRAIN KOS SEQUENCE IN THE UNP DATABASE CONTAINS THREE MUTATIONS RELATIVE ...AUTHORS STATE THAT HSV-1 STRAIN KOS SEQUENCE IN THE UNP DATABASE CONTAINS THREE MUTATIONS RELATIVE TO SEQUENCES OF OTHER STRAINS OF HSV-1 AND HSV-2. THEIR SEQUENCE WAS DERIVED FROM THE SEQUENCE OF HSV-1 KOS GB FROM PLASMID PKBXX (S. PERSON) AND DOES NOT CONTAIN THESE MUTATIONS. | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 4.03 Å3/Da / Density % sol: 69.5 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.5 Details: 7% PEG 4000, 0.5M NaCl, 0.1M sodium citrate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X25 / Wavelength: 0.9795 Å |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Nov 12, 2008 |
Radiation | Monochromator: SAGITALLY FOCUSED Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 2.2629→48.3517 Å / Num. all: 229990 / Num. obs: 227148 / % possible obs: 98.7643 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.3 % / Rmerge(I) obs: 0.12 / Net I/σ(I): 7.57 |
Reflection shell | Resolution: 2.26→2.3 Å / Redundancy: 1.7 % / Mean I/σ(I) obs: 1.06 / % possible all: 72 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 2GUM Resolution: 2.2629→47.3159 Å / Cross valid method: THROUGHOUT / σ(F): 0.05 / Stereochemistry target values: TWIN_LSQ_F
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 42.934 Å2 / ksol: 0.368 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.2629→47.3159 Å
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Refine LS restraints |
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LS refinement shell |
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