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- PDB-2if1: HUMAN TRANSLATION INITIATION FACTOR EIF1, NMR, 29 STRUCTURES -

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Basic information

Entry
Database: PDB / ID: 2if1
TitleHUMAN TRANSLATION INITIATION FACTOR EIF1, NMR, 29 STRUCTURES
ComponentsEIF1
KeywordsTRANSLATION INITIATION FACTOR
Function / homology
Function and homology information


positive regulation of mRNA cis splicing, via spliceosome / multi-eIF complex / eukaryotic 43S preinitiation complex / translation factor activity, RNA binding / eukaryotic 48S preinitiation complex / regulation of translational initiation / ribosomal small subunit binding / translational initiation / translation initiation factor activity / RNA binding ...positive regulation of mRNA cis splicing, via spliceosome / multi-eIF complex / eukaryotic 43S preinitiation complex / translation factor activity, RNA binding / eukaryotic 48S preinitiation complex / regulation of translational initiation / ribosomal small subunit binding / translational initiation / translation initiation factor activity / RNA binding / nucleus / cytoplasm
Similarity search - Function
SUI1-like domain / Translation Initiation Factor Eif1 / Eukaryotic translation initiation factor SUI1 / SUI1 domain superfamily / Translation initiation factor SUI1 / Translation initiation factor SUI1 family profile. / SUI1 domain / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Eukaryotic translation initiation factor 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing
AuthorsFletcher, C.M. / Hellen, C.U.T. / Pestova, T.V. / Wagner, G.
CitationJournal: EMBO J. / Year: 1999
Title: Structure and interactions of the translation initiation factor eIF1.
Authors: Fletcher, C.M. / Pestova, T.V. / Hellen, C.U. / Wagner, G.
History
DepositionAug 4, 1998Processing site: BNL
Revision 1.0May 18, 1999Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 9, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site
Revision 1.4May 29, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: EIF1


Theoretical massNumber of molelcules
Total (without water)14,3271
Polymers14,3271
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)29 / 30LOW RESTRAINT VIOLATIONS
RepresentativeModel #1

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Components

#1: Protein EIF1 / SUI1


Mass: 14327.205 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: N-TERMINAL POLY-HISTIDINE TAG / Source: (gene. exp.) Homo sapiens (human) / Cell line: BL21 / Plasmid: PQE31(HIS6-EIF1) / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P41567

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Sample conditionsIonic strength: 400 mM / pH: 6.0 / Pressure: 1 atm / Temperature: 300 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian UNITYPLUSVarianUNITYPLUS4001
Varian INOVAVarianINOVA7502

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Processing

Software
NameVersionClassification
X-PLOR3.851model building
X-PLOR3.851refinement
X-PLOR3.851phasing
NMR software
NameVersionDeveloperClassification
X-PLOR3.851BRUNGERrefinement
X-PLOR3.851structure solution
RefinementMethod: simulated annealing / Software ordinal: 1
NMR ensembleConformer selection criteria: LOW RESTRAINT VIOLATIONS / Conformers calculated total number: 30 / Conformers submitted total number: 29

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