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- PDB-1go5: Structure of the C-terminal FG-binding domain of human Tap -

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Basic information

Entry
Database: PDB / ID: 1go5
TitleStructure of the C-terminal FG-binding domain of human Tap
ComponentsTIP ASSOCIATING PROTEIN
KeywordsNUCLEAR TRANSPORT / MRNA EXPORT / UBA / NUCLEOPORINS
Function / homology
Function and homology information


nuclear RNA export factor complex / nuclear inclusion body / Transport of the SLBP independent Mature mRNA / Transport of the SLBP Dependant Mature mRNA / Transport of Mature mRNA Derived from an Intronless Transcript / Transport of Mature mRNA derived from an Intron-Containing Transcript / poly(A)+ mRNA export from nucleus / mRNA export from nucleus / nuclear pore / cytoplasmic stress granule ...nuclear RNA export factor complex / nuclear inclusion body / Transport of the SLBP independent Mature mRNA / Transport of the SLBP Dependant Mature mRNA / Transport of Mature mRNA Derived from an Intronless Transcript / Transport of Mature mRNA derived from an Intron-Containing Transcript / poly(A)+ mRNA export from nucleus / mRNA export from nucleus / nuclear pore / cytoplasmic stress granule / protein transport / nuclear speck / mRNA binding / RNA binding / nucleoplasm / nucleus / cytoplasm / cytosol
Similarity search - Function
Nuclear RNA export factor Tap, RNA-binding domain / Tap, RNA-binding / TAP C-terminal (TAP-C) domain / TAP C-terminal domain / TAP C-terminal (TAP-C) domain profile. / C-terminal domain of vertebrate Tap protein / Nuclear RNA export factor / Nuclear transport factor 2, eukaryote / Nuclear transport factor 2 domain profile. / Nuclear transport factor 2 domain ...Nuclear RNA export factor Tap, RNA-binding domain / Tap, RNA-binding / TAP C-terminal (TAP-C) domain / TAP C-terminal domain / TAP C-terminal (TAP-C) domain profile. / C-terminal domain of vertebrate Tap protein / Nuclear RNA export factor / Nuclear transport factor 2, eukaryote / Nuclear transport factor 2 domain profile. / Nuclear transport factor 2 domain / Nuclear transport factor 2 (NTF2) domain / Ubiquitin-associated (UBA) domain / UBA-like superfamily / NTF2-like domain superfamily / Leucine-rich repeat profile. / Helicase, Ruva Protein; domain 3 / Leucine-rich repeat / Leucine-rich repeat domain superfamily / RNA-binding domain superfamily / Nucleotide-binding alpha-beta plait domain superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Nuclear RNA export factor 1
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodSOLUTION NMR / simulated annealing
AuthorsGrant, R.P. / Hurt, E. / Neuhaus, D. / Stewart, M.
CitationJournal: Nat.Struct.Biol. / Year: 2002
Title: Structure of the C-Terminal Fg-Nucleoporin Binding Domain of Tap/Nxf1
Authors: Grant, R.P. / Hurt, E. / Neuhaus, D. / Stewart, M.
History
DepositionOct 18, 2001Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 5, 2002Provider: 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 / pdbx_nmr_spectrometer
Item: _pdbx_database_status.status_code_cs / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model
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: TIP ASSOCIATING PROTEIN


Theoretical massNumber of molelcules
Total (without water)7,7191
Polymers7,7191
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)26 / 50RESTRAINT VIOLATIONS AND RMSD PROFILE
RepresentativeModel #1

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Components

#1: Protein TIP ASSOCIATING PROTEIN / TAP / NUCLEAR RNA EXPORT FACTOR 1


Mass: 7718.598 Da / Num. of mol.: 1 / Fragment: RESIDUES 551-619
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PMW172 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / References: UniProt: Q9UBU9

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NOESY
121DQF-COSY
131TOCSY
141DQ-CORR
NMR detailsText: THE STRUCTURE WAS DETERMINED USING HOMONUCLEAR NMR SPECTROSCOPY ON SAMPLES AT NATURAL ISOTOPIC ABUNDANCE

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Sample preparation

Sample conditionsIonic strength: 0.07 / pH: 6.0 / Temperature: 300 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DRXBrukerDRX5001
Bruker DMXBrukerDMX6002
Bruker AVANCEBrukerAVANCE8003

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Processing

NMR software
NameVersionDeveloperClassification
X-PLOR3.1BRUNGERrefinement
X-PLORstructure solution
RefinementMethod: simulated annealing / Software ordinal: 1 / Details: CAN BE FOUND IN THE JRNL CITATION ABOVE
NMR ensembleConformer selection criteria: RESTRAINT VIOLATIONS AND RMSD PROFILE
Conformers calculated total number: 50 / Conformers submitted total number: 26

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