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- PDB-2gum: Crystal structure of the extracellular domain of glycoprotein B f... -

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Basic information

Entry
Database: PDB / ID: 2gum
TitleCrystal structure of the extracellular domain of glycoprotein B from Herpes Simplex Virus type I
ComponentsGlycoprotein B
KeywordsVIRAL PROTEIN / ENVELOPE GLYCOPROTEIN / MEMBRANE FUSION
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 / identical protein binding / membrane
Similarity search - Function
Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #1890 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #3280 / SH3 type barrels. - #1230 / PH-domain like - #100 / Herpesvirus Glycoprotein B ectodomain / Herpesvirus Glycoprotein B / Herpesvirus Glycoprotein B, PH-like domain 1 / Herpesvirus Glycoprotein B, PH-like domain 2 / Herpesvirus Glycoprotein B / Herpesvirus Glycoprotein B PH-like domain ...Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #1890 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #3280 / SH3 type barrels. - #1230 / PH-domain like - #100 / Herpesvirus Glycoprotein B ectodomain / Herpesvirus Glycoprotein B / Herpesvirus Glycoprotein B, PH-like domain 1 / Herpesvirus Glycoprotein B, PH-like domain 2 / Herpesvirus Glycoprotein B / Herpesvirus Glycoprotein B PH-like domain / Herpesvirus Glycoprotein B, PH-like domain 2 superfamily / PH-domain like / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Helix non-globular / Special / SH3 type barrels. / Roll / Up-down Bundle / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
Envelope glycoprotein B
Similarity search - Component
Biological speciesHuman herpesvirus 1 (Herpes simplex virus type 1)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.1 Å
AuthorsHeldwein, E.E.
CitationJournal: Science / Year: 2006
Title: Crystal structure of glycoprotein B from herpes simplex virus 1.
Authors: Heldwein, E.E. / Lou, H. / Bender, F.C. / Cohen, G.H. / Eisenberg, R.J. / Harrison, S.C.
History
DepositionMay 1, 2006Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 25, 2006Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Source and taxonomy / Version format compliance
Revision 1.3Oct 18, 2017Group: Refinement description / Category: software

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Glycoprotein B
B: Glycoprotein B
C: Glycoprotein B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)215,0977
Polymers215,0053
Non-polymers924
Water4,017223
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area37460 Å2
ΔGint-220 kcal/mol
Surface area74730 Å2
MethodPISA
Unit cell
Length a, b, c (Å)84.959, 100.039, 100.133
Angle α, β, γ (deg.)67.04, 77.99, 70.31
Int Tables number1
Space group name H-MP1
DetailsThe asymmetric unit contain a single biological unit, a trimer

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Components

#1: Protein Glycoprotein B


Mass: 71668.188 Da / Num. of mol.: 3 / Fragment: residues 103-730
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human herpesvirus 1 (Herpes simplex virus type 1)
Genus: Simplexvirus / Strain: KOS / Gene: GB, UL27 / Plasmid: pVT-Bac / Production host: Spodoptera frugiperda (fall armyworm) / Strain (production host): SF9 / References: UniProt: P06437
#2: Chemical
ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Na
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 223 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 3.42 Å3/Da / Density % sol: 64 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7
Details: 8% PEG 6000, 0.1 M Na Hepes, 15% 2-methyl-2,4-pentanediol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.97944 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Jun 16, 2005
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97944 Å / Relative weight: 1
ReflectionResolution: 2.1→41.2 Å / Num. all: 145731 / Num. obs: 145731 / % possible obs: 0.878 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.7 % / Rmerge(I) obs: 0.066 / Net I/σ(I): 18.1
Reflection shellResolution: 2.1→2.18 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.331 / Mean I/σ(I) obs: 3.7 / Num. unique all: 145627 / % possible all: 0.588

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Processing

Software
NameVersionClassification
ADSCdata collection
DENZOdata reduction
SnBphasing
CNS1.1refinement
SCALEPACKdata scaling
RefinementMethod to determine structure: SAD / Resolution: 2.1→41.2 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.2747 7446 -thin-resolution shells
Rwork0.2479 ---
all0.2479 166194 --
obs0.2479 145731 87.7 %-
Refinement stepCycle: LAST / Resolution: 2.1→41.2 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13996 0 4 223 14223

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