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- PDB-1p9c: NMR solution structure of the C-terminal ubiquitin-interacting mo... -

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Basic information

Entry
Database: PDB / ID: 1p9c
TitleNMR solution structure of the C-terminal ubiquitin-interacting motif of the proteasome subunit S5a
Components26S proteasome non-ATPase regulatory subunit 4
KeywordsLIGAND BINDING PROTEIN / ALPHA HELIX / HAIRPIN LOOP
Function / homology
Function and homology information


proteasome accessory complex / proteasome regulatory particle, base subcomplex / Proteasome assembly / polyubiquitin modification-dependent protein binding / proteasome complex / molecular adaptor activity / proteasome-mediated ubiquitin-dependent protein catabolic process / RNA binding / nucleoplasm / identical protein binding ...proteasome accessory complex / proteasome regulatory particle, base subcomplex / Proteasome assembly / polyubiquitin modification-dependent protein binding / proteasome complex / molecular adaptor activity / proteasome-mediated ubiquitin-dependent protein catabolic process / RNA binding / nucleoplasm / identical protein binding / nucleus / cytosol
Similarity search - Function
Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #120 / : / Ubiquitin interaction motif / Proteasome subunit Rpn10 / Ubiquitin-interacting motif. / von Willebrand factor type A domain / Ubiquitin interacting motif / Ubiquitin-interacting motif (UIM) domain profile. / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / von Willebrand factor (vWF) type A domain ...Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #120 / : / Ubiquitin interaction motif / Proteasome subunit Rpn10 / Ubiquitin-interacting motif. / von Willebrand factor type A domain / Ubiquitin interacting motif / Ubiquitin-interacting motif (UIM) domain profile. / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / von Willebrand factor (vWF) type A domain / VWFA domain profile. / von Willebrand factor, type A / von Willebrand factor A-like domain superfamily / Helix non-globular / Special
Similarity search - Domain/homology
26S proteasome non-ATPase regulatory subunit 4
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing
AuthorsMueller, T.D. / Feigon, J.
CitationJournal: Embo J. / Year: 2003
Title: Structural determinants for the binding of ubiquitin-like domains to the proteasome.
Authors: Mueller, T.D. / Feigon, J.
History
DepositionMay 10, 2003Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 7, 2003Provider: repository / Type: Initial release
Revision 1.1Apr 29, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: 26S proteasome non-ATPase regulatory subunit 4


Theoretical massNumber of molelcules
Total (without water)4,9161
Polymers4,9161
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / 100structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein/peptide 26S proteasome non-ATPase regulatory subunit 4 / 26S proteasome regulatory subunit S5A / Rpn10 / Multiubiquitin chain binding protein / ...26S proteasome regulatory subunit S5A / Rpn10 / Multiubiquitin chain binding protein / Antisecretory factor-1 / AF / ASF


Mass: 4916.343 Da / Num. of mol.: 1 / Fragment: C-terminal ubiquitin-interacting motif
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PSMD4 OR MCB1 / Production host: Escherichia coli (E. coli) / References: UniProt: P55036

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D NOESY
1223D 13C-separated NOESY
NMR detailsText: The structure was determined using standard triple-resonance NMR spectroscopy techniques

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Sample preparation

Details
Solution-IDContentsSolvent system
12mM S5a peptide, unlabeled50mM sodium phosphate; 100mM sodium chloride; 5% D2O
22mM S5a peptide U-15N,13C50mM sodium phosphate; 100mM sodium chloride; 5% D2O
Sample conditionsIonic strength: 150mM / pH: 6.5 / Pressure: ambient / Temperature: 300 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DRXBrukerDRX5001
Bruker DRXBrukerDRX6002

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Processing

NMR software
NameVersionDeveloperClassification
XwinNMR2.5Bruker Karlsruheprocessing
AURELIA2.8.9Neidigdata analysis
X-PLOR3.1Brungerstructure solution
X-PLOR3.1Brungerrefinement
RefinementMethod: simulated annealing / Software ordinal: 1
Details: The structures are based on a total of 474 distance restraints, 452 are NOE-derived distance restraints, 22 are from hydrogen bonds
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 100 / Conformers submitted total number: 10

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