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- PDB-1p0r: Solution Structure of UBL5 a human Ubiquitin-Like Protein -

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Basic information

Entry
Database: PDB / ID: 1p0r
TitleSolution Structure of UBL5 a human Ubiquitin-Like Protein
Componentsubiquitin-like 5
KeywordsPROTEIN BINDING / Ubiquitin-like fold
Function / homology
Function and homology information


positive regulation of protein targeting to mitochondrion / Cajal body / mRNA Splicing - Major Pathway / protein modification process / protein tag activity / mRNA splicing, via spliceosome / nucleoplasm / nucleus / cytoplasm
Similarity search - Function
Ubiquitin-like modifier Hub1/Ubl5 / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / Ubiquitin-like (UB roll) / Ubiquitin family / Ubiquitin-like domain / Ubiquitin-like domain superfamily / Roll / Alpha Beta
Similarity search - Domain/homology
Ubiquitin-like protein 5
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing
Model type detailsminimized average
AuthorsMcNally, T. / Huang, Q. / Janis, R.S. / Liu, Z. / Olejniczak, E.T. / Reilly, R.M.
CitationJournal: Protein Sci. / Year: 2003
Title: Structural analysis of UBL5, a novel ubiquitin-like modifier
Authors: McNally, T. / Huang, Q. / Janis, R.S. / Liu, Z. / Olejniczak, E.T. / Reilly, R.M.
History
DepositionApr 10, 2003Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 28, 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: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly ...database_2 / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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: ubiquitin-like 5


Theoretical massNumber of molelcules
Total (without water)10,7321
Polymers10,7321
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)1 / -
RepresentativeModel #1minimized average structure

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Components

#1: Protein ubiquitin-like 5


Mass: 10732.312 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: pet15b / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): bl21(DE3) / References: UniProt: Q9BZL1

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 15N-separated NOESY
1223D 13C-separated NOESY

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Sample preparation

Details
Solution-IDContentsSolvent system
1.5mM UBL5 U-15N,13C 50mM sodium phosphate (pH 5.7), 2mM Dtt90% H2O/10% D2O
21.0mM UBL5 U-15N,13C 50mM sodium phosphate (pH 5.7), 2mM Dtt100% D2O
Sample conditionsIonic strength: 50mM sodium phosphate / pH: 5.7 / Pressure: ambient / Temperature: 298 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 softwareName: CNX / Version: 2000 / Developer: Brunger, A.T. / Classification: refinement
RefinementMethod: simulated annealing / Software ordinal: 1
Details: Based on 952 NMR-derived distance and torsion angle restraints.
NMR representativeSelection criteria: minimized average structure
NMR ensembleConformers submitted total number: 1

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