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- PDB-1qlo: Structure of the active domain of the herpes simplex virus protei... -

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Entry
Database: PDB / ID: 1qlo
TitleStructure of the active domain of the herpes simplex virus protein ICP47 in water/sodium dodecyl sulfate solution determined by nuclear magnetic resonance spectroscopy
ComponentsHERPES SIMPLEX VIRUS PROTEIN ICP47
KeywordsMEMBRANE PROTEINS / HERPES SIMPLEX VIRUS / PROTEIN ICP47
Function / homologyHerpesvirus ICP47 / Herpesvirus US12 family / symbiont-mediated suppression of host adaptive immune response / symbiont-mediated suppression of host antigen processing and presentation / host cell cytoplasm / host cell nucleus / ICP47 protein
Function and homology information
Biological speciesHERPES SIMPLEX VIRUS
MethodSOLUTION NMR / simulated annealing
AuthorsPfaender, R. / Neumann, L. / Zweckstetter, M. / Seger, C. / Holak, T.A. / Tampe, R.
CitationJournal: Biochemistry / Year: 1999
Title: The Structure of the Active Domain of the Herpes Simplex Virus Protein Icp47 in Water/Sodium Dodecyl Sulfate Solution Determined by Nuclear Magnetic Resonance Spectroscopy.
Authors: Pfaender, R. / Neumann, L. / Zweckstetter, M. / Seger, C. / Holak, T.A. / Tampe, R.
History
DepositionSep 9, 1999Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 14, 1999Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jan 15, 2020Group: Data collection / Other / Category: pdbx_database_status / pdbx_nmr_software
Item: _pdbx_database_status.status_code_cs / _pdbx_database_status.status_code_mr / _pdbx_nmr_software.name
Revision 1.4May 15, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: HERPES SIMPLEX VIRUS PROTEIN ICP47


Theoretical massNumber of molelcules
Total (without water)4,0221
Polymers4,0221
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)19 / 40LEAST RESTRAINT VIOLATION ENERGY
Representative

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Components

#1: Protein/peptide HERPES SIMPLEX VIRUS PROTEIN ICP47 / / IMMEDIATE-EARLY PROTEIN IE12 / IMMEDIATE-EARLY-5 / VMW12


Mass: 4021.565 Da / Num. of mol.: 1 / Fragment: ACTIVE DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HERPES SIMPLEX VIRUS / Strain: TYPE 1 - STRAIN 17 / Production host: SPODOPTERA FRUGIPERDA (fall armyworm) / References: UniProt: P03170

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NOESY
121TOCSY
131COSY
NMR detailsText: SEE ARTICLE

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Sample preparation

Sample conditionspH: 7.4 / Temperature: 307 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AMXBrukerAMX5001
Bruker DRXBrukerDRX6002
Bruker DMXBrukerDMX7503

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Processing

NMR software
NameVersionDeveloperClassification
X-PLOR3.1BRUNGERrefinement
X-PLOR3.1structure solution
RefinementMethod: simulated annealing / Software ordinal: 1
NMR ensembleConformer selection criteria: LEAST RESTRAINT VIOLATION ENERGY
Conformers calculated total number: 40 / Conformers submitted total number: 19

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