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- PDB-1qtt: SOLUTION STRUCTURE OF THE ONCOPROTEIN P13MTCP1 -

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Basic information

Entry
Database: PDB / ID: 1qtt
TitleSOLUTION STRUCTURE OF THE ONCOPROTEIN P13MTCP1
ComponentsPRODUCT OF THE MTCP1 ONCOGENE
KeywordsGENE REGULATION / BETA BARREL
Function / homology
Function and homology information


protein serine/threonine kinase activator activity / intracellular signal transduction / protein kinase binding
Similarity search - Function
Proto-oncogene - Oncogene Product P14tcl1 / TCL1/MTCP1 / TCL1/MTCP1 / TCL1/MTCP1 superfamily / TCL1/MTCP1 family / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / torsion angle dynamics
AuthorsGuignard, L. / Padilla, A. / Mispelter, J. / Yang, Y.-S. / Stern, M.-H. / Lhoste, J.-M. / Roumestand, C.
Citation
Journal: J.Biomol.NMR / Year: 2000
Title: Backbone dynamics and solution structure refinement of the 15N-labeled human oncogenic protein p13MTCP1: comparison with X-ray data.
Authors: Guignard, L. / Padilla, A. / Mispelter, J. / Yang, Y.S. / Stern, M.H. / Lhoste, J.M. / Roumestand, C.
#1: Journal: J.Biomol.NMR / Year: 1998
Title: Solution structure of the recombinant human oncoprotein p13MTCP1
Authors: Yang, Y.-S. / Guignard, L. / Padilla, A. / Hoh, F. / Strub, M.-P.
History
DepositionJun 29, 1999Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 19, 2001Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jan 24, 2018Group: Database references / Derived calculations / Structure summary
Category: audit_author / citation_author ...audit_author / citation_author / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _audit_author.name / _citation_author.name
Revision 1.4May 1, 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: PRODUCT OF THE MTCP1 ONCOGENE


Theoretical massNumber of molelcules
Total (without water)13,6801
Polymers13,6801
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 200target function
RepresentativeModel #1fewest violations

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Components

#1: Protein PRODUCT OF THE MTCP1 ONCOGENE


Mass: 13680.420 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Cell: T-CELLS / Cell line (production host): BL21 / Production host: Escherichia coli (E. coli) / References: UniProt: P56278

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 15N-SEPARATED NOESY
1212D NOESY
131DQF-COSY

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Sample preparation

DetailsContents: 2MM P13MTCP1 U-15N; 20MM PHOSPHATE BUFFER NA;90% H2O, 10% D2O
Sample conditionspH: 6.5 / Pressure: AMBIENT / Temperature: 303 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AMXBrukerAMX6001
Bruker DMXBrukerDMX8002
Bruker AMXBrukerAMX4003

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Processing

NMR software
NameVersionDeveloperClassification
DYANA1.5GUNTERTstructure solution
DYANA1.5GUNTERTrefinement
RefinementMethod: torsion angle dynamics / Software ordinal: 1
Details: THE STRUCTURES ARE BASED ON A TOTAL OF 1773 NOE RESTRAINTS, 80 DIHEDRAL ANGLE RESTRAINTS
NMR representativeSelection criteria: fewest violations
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 200 / Conformers submitted total number: 20

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