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- PDB-1bm4: MOMLV CAPSID PROTEIN MAJOR HOMOLOGY REGION PEPTIDE ANALOG -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 1bm4
TitleMOMLV CAPSID PROTEIN MAJOR HOMOLOGY REGION PEPTIDE ANALOG
ComponentsPROTEIN (MOLONEY MURINE LEUKEMIA VIRUS CAPSID)
KeywordsVIRAL PROTEIN / MOLONEY MURINE LEUKEMIA VIRUS CAPSID PROTEIN / MOMLV / MU-MLV / CAPSID / MHR / MAJOR HOMOLOGY REGION
Function / homology
Function and homology information


host cell uropod / host cell late endosome membrane / viral budding via host ESCRT complex / host multivesicular body / viral nucleocapsid / structural constituent of virion / host cell plasma membrane / RNA binding / zinc ion binding / membrane
Similarity search - Function
Gamma-retroviral matrix protein / Gag polyprotein, inner coat protein p12 / Core shell protein Gag P30 / Matrix protein (MA), p15 / Gag polyprotein, inner coat protein p12 / Gag P30 core shell protein / Gamma-retroviral matrix domain superfamily / Retroviral matrix protein / Retrovirus capsid, N-terminal / zinc finger ...Gamma-retroviral matrix protein / Gag polyprotein, inner coat protein p12 / Core shell protein Gag P30 / Matrix protein (MA), p15 / Gag polyprotein, inner coat protein p12 / Gag P30 core shell protein / Gamma-retroviral matrix domain superfamily / Retroviral matrix protein / Retrovirus capsid, N-terminal / zinc finger / Zinc knuckle / Zinc finger, CCHC-type superfamily / Zinc finger, CCHC-type / Zinc finger CCHC-type profile.
Similarity search - Domain/homology
Gag polyprotein / Gag polyprotein
Similarity search - Component
MethodSOLUTION NMR / distance geometry
AuthorsClish, C.B. / Peyton, D.H. / Barklis, E.
CitationJournal: Eur.J.Biochem. / Year: 1998
Title: Solution structures of human immunodeficiency virus type 1 (HIV-1) and moloney murine leukemia virus (MoMLV) capsid protein major-homology-region peptide analogs by NMR spectroscopy.
Authors: Clish, C.B. / Peyton, D.H. / Barklis, E.
History
DepositionJul 28, 1998Deposition site: BNL / Processing site: RCSB
Revision 1.0Aug 5, 1998Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 14, 2018Group: Database references / Derived calculations
Category: pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _struct_ref_seq_dif.details
Revision 1.4Apr 10, 2024Group: Data collection / Database references
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_nmr_software / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: PROTEIN (MOLONEY MURINE LEUKEMIA VIRUS CAPSID)


Theoretical massNumber of molelcules
Total (without water)3,6801
Polymers3,6801
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)9 / 50LEAST RESTRAINT VIOLATION
Representative

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Components

#1: Protein/peptide PROTEIN (MOLONEY MURINE LEUKEMIA VIRUS CAPSID) / MOMLV CA MHR PEPTIDE ANALOG


Mass: 3680.196 Da / Num. of mol.: 1 / Fragment: MAJOR HOMOLOGY REGION PEPTIDE, N-TERMINAL CYS / Mutation: A1C / Source method: obtained synthetically
Details: THE PROTEIN WAS CHEMICALLY SYNTHESIZED FROM MOLONEY MURINE LEUKEMIA VIRUS (MOMLV).
Keywords: N-TERMINAL CYC / References: UniProt: Q9WJP4, UniProt: P03332*PLUS

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NOESY
121COSY
131TOCSY
NMR detailsText: THE STRUCTURE WAS DETERMINED WITH 2D-1H-NMR AND A SYNTHETIC PEPTIDE (5-7 MILLIMOLAR)

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Sample preparation

Sample conditionspH: 3.1 / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker AMX400 / Manufacturer: Bruker / Model: AMX400 / Field strength: 400 MHz

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Processing

NMR software
NameVersionDeveloperClassification
DiscoverBIOSYMrefinement
BIOSYM FELIXFELIXstructure solution
FELIX ASSIGNASSIGNstructure solution
DGIIstructure solution
Discoverstructure solution
RefinementMethod: distance geometry / Software ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE
NMR ensembleConformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 50 / Conformers submitted total number: 9

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