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- PDB-1h9e: LEM-LIKE DOMAIN OF HUMAN INNER NUCLEAR MEMBRANE PROTEIN LAP2 -

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Basic information

Entry
Database: PDB / ID: 1h9e
TitleLEM-LIKE DOMAIN OF HUMAN INNER NUCLEAR MEMBRANE PROTEIN LAP2
ComponentsLAMINA-ASSOCIATED POLYPEPTIDE 2
KeywordsMEMBRANE PROTEIN / INNER NUCLEAR MEMBRANE PROTEIN / LAMINA-ASSOCIATED POLYPEPTIDE / EMERIN / LEM DOMAIN
Function / homology
Function and homology information


Depolymerization of the Nuclear Lamina / Nuclear Envelope Breakdown / lamin binding / Initiation of Nuclear Envelope (NE) Reformation / nuclear inner membrane / nuclear envelope / nuclear membrane / membrane => GO:0016020 / cadherin binding / chromatin ...Depolymerization of the Nuclear Lamina / Nuclear Envelope Breakdown / lamin binding / Initiation of Nuclear Envelope (NE) Reformation / nuclear inner membrane / nuclear envelope / nuclear membrane / membrane => GO:0016020 / cadherin binding / chromatin / DNA binding / membrane / nucleus / cytoplasm
Similarity search - Function
Transcription Termination Factor Rho, Rna-binding Domain; Chain A, Domain 1 - #40 / LEM-like domain / Lamina-associated polypeptide 2 alpha, C-terminal / Thymopoietin protein / Lamina-associated polypeptide 2 alpha / LEM-like domain profile. / Thymopoietin / LEM domain / LEM domain / LEM domain profile. ...Transcription Termination Factor Rho, Rna-binding Domain; Chain A, Domain 1 - #40 / LEM-like domain / Lamina-associated polypeptide 2 alpha, C-terminal / Thymopoietin protein / Lamina-associated polypeptide 2 alpha / LEM-like domain profile. / Thymopoietin / LEM domain / LEM domain / LEM domain profile. / in nuclear membrane-associated proteins / LEM/LEM-like domain superfamily / Transcription Termination Factor Rho, Rna-binding Domain; Chain A, Domain 1 / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Lamina-associated polypeptide 2, isoform alpha / Lamina-associated polypeptide 2, isoforms beta/gamma
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodSOLUTION NMR / simulated annealing
AuthorsLaguri, C. / Gilquin, B. / Wolff, N. / Romi-Lebrun, R. / Courchay, K. / Callebaut, I. / Worman, H.J. / Zinn-Justin, S.
CitationJournal: Structure / Year: 2001
Title: Structural Characterization of the Lem Motif Common to Three Human Inner Nuclear Membrane Proteins
Authors: Laguri, C. / Gilquin, B. / Wolff, N. / Romi-Lebrun, R. / Courchay, K. / Callebaut, I. / Worman, H.J. / Zinn-Justin, S.
History
DepositionMar 8, 2001Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 17, 2001Provider: repository / Type: Initial release
Revision 1.1May 7, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jun 14, 2017Group: Structure summary / Category: pdbx_nmr_representative / Item: _pdbx_nmr_representative.conformer_id
Remark 650 HELIX DETERMINATION METHOD: RAMACHANDRAN

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: LAMINA-ASSOCIATED POLYPEPTIDE 2


Theoretical massNumber of molelcules
Total (without water)6,2801
Polymers6,2801
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)10 / 200LOWER ENERGY
RepresentativeModel #2

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Components

#1: Protein LAMINA-ASSOCIATED POLYPEPTIDE 2 / THYMOPOIETIN / TP BETA/GAMMA / THYMOPOIETIN-RELATED PEPTIDE ISOFORMS BETA/GAMMA / TPRP ISOFORMS BETA/GAMMA


Mass: 6280.145 Da / Num. of mol.: 1 / Fragment: LEM-LIKE DOMAIN, RESIDUES 2-57 / Source method: obtained synthetically / Source: (synth.) HOMO SAPIENS (human) / References: UniProt: P42167, UniProt: P42166*PLUS
Compound detailsPLAYS IMPORTANT ROLES IN T-CELL DEVELOPMENT AND FUNCTION.

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111COSY
121TOCSY
131NOESY
141ROESY

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Sample preparation

Sample conditionsIonic strength: 20 mM / pH: 6.3 / Pressure: 1 atm / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DRXBrukerDRX5001
Bruker DRXBrukerDRX6002

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Processing

NMR software
NameVersionDeveloperClassification
X-PLOR3.1BRUNGERrefinement
X-PLOR3.1structure solution
RefinementMethod: simulated annealing / Software ordinal: 1
NMR ensembleConformer selection criteria: LOWER ENERGY / Conformers calculated total number: 200 / Conformers submitted total number: 10

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