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- PDB-1xnl: ASLV fusion peptide -

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Basic information

Entry
Database: PDB / ID: 1xnl
TitleASLV fusion peptide
Componentsmembrane protein gp37Biological membrane
KeywordsVIRAL PROTEIN / fusion protein / virus entry / membrane fusion
Function / homology
Function and homology information


symbiont entry into host cell / fusion of virus membrane with host plasma membrane / viral envelope / virion attachment to host cell / host cell plasma membrane / virion membrane / membrane
Similarity search - Function
Rous sarcoma virus, Gp95, envelope protein / Avian retrovirus envelope protein, gp85 / ENV polyprotein (coat polyprotein) / TLV/ENV coat polyprotein
Similarity search - Domain/homology
Envelope glycoprotein gp95
Similarity search - Component
MethodSOLUTION NMR / distance geometry, simulated annealing
AuthorsCheng, S.F. / Wu, C.W. / Kantchev, E.A. / Chang, D.K.
CitationJournal: Eur.J.Biochem. / Year: 2004
Title: Structure and membrane interaction of the internal fusion peptide of avian sarcoma leukosis virus
Authors: Cheng, S.F. / Wu, C.W. / Kantchev, E.A. / Chang, D.K.
History
DepositionOct 5, 2004Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 11, 2005Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly ...database_2 / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Remark 999SEQUENCE COORDINATES FOR SIDECHAIN ATOMS WERE NOT PROVIDED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: membrane protein gp37


Theoretical massNumber of molelcules
Total (without water)2,8641
Polymers2,8641
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)20 / 350structures with the least restraint violations
RepresentativeModel #1fewest violations

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Components

#1: Protein/peptide membrane protein gp37 / Biological membrane / ASLV/FP


Mass: 2864.350 Da / Num. of mol.: 1 / Source method: obtained synthetically
Details: The peptide was chemically synthesized. The sequence of the peptide is naturally found in avian sarcoma leukosis virus.
References: UniProt: P03397

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D NOESY (300 msec mixing time)
1212D TOCSY
NMR detailsText: This structure was determined using standard 2D homonuclear techniques.

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Sample preparation

DetailsContents: 1mM:100mM peptide:d25-SDS / Solvent system: 10% D2O
Sample conditionspH: 5.0 / Pressure: ambient / Temperature: 298 K

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometerType: Bruker AMX / Manufacturer: Bruker / Model: AMX / Field strength: 500 MHz

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Processing

NMR softwareName: DGII / Version: 2000.1 / Classification: refinement
RefinementMethod: distance geometry, simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: fewest violations
NMR ensembleConformer selection criteria: structures with the least restraint violations
Conformers calculated total number: 350 / Conformers submitted total number: 20

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