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- PDB-2myo: SOLUTION STRUCTURE OF MYOTROPHIN, NMR, MINIMIZED AVERAGE STRUCTURE -

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Basic information

Entry
Database: PDB / ID: 2myo
TitleSOLUTION STRUCTURE OF MYOTROPHIN, NMR, MINIMIZED AVERAGE STRUCTURE
ComponentsMYOTROPHIN
KeywordsANK-REPEAT / MYOTROPHIN / ACETYLATION
Function / homology
Function and homology information


positive regulation of macromolecule biosynthetic process / regulation of barbed-end actin filament capping / cerebellar granule cell differentiation / F-actin capping protein complex / catecholamine metabolic process / skeletal muscle tissue regeneration / regulation of cell size / positive regulation of cardiac muscle hypertrophy / striated muscle cell differentiation / positive regulation of protein metabolic process ...positive regulation of macromolecule biosynthetic process / regulation of barbed-end actin filament capping / cerebellar granule cell differentiation / F-actin capping protein complex / catecholamine metabolic process / skeletal muscle tissue regeneration / regulation of cell size / positive regulation of cardiac muscle hypertrophy / striated muscle cell differentiation / positive regulation of protein metabolic process / neuron differentiation / cellular response to mechanical stimulus / positive regulation of NF-kappaB transcription factor activity / positive regulation of cell growth / sequence-specific DNA binding / axon / perinuclear region of cytoplasm / nucleus / cytosol / cytoplasm
Similarity search - Function
: / Ankyrin repeat-containing domain / Ankyrin repeats (3 copies) / Ankyrin repeat profile. / Ankyrin repeat region circular profile. / ankyrin repeats / Ankyrin repeat / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / Ankyrin repeat-containing domain superfamily / Alpha Horseshoe / Mainly Alpha
Similarity search - Domain/homology
Biological speciesRattus norvegicus (Norway rat)
MethodSOLUTION NMR / simulated annealing
AuthorsYang, Y. / Nanduri, S. / Sen, S. / Qin, J.
Citation
Journal: Structure / Year: 1998
Title: The structural basis of ankyrin-like repeat function as revealed by the solution structure of myotrophin.
Authors: Yang, Y. / Nanduri, S. / Sen, S. / Qin, J.
#1: Journal: Protein Sci. / Year: 1997
Title: Nuclear Magnetic Resonance Assignment and Secondary Structure of an Ankyrin-Like Repeat-Bearing Protein: Myotrophin
Authors: Yang, Y. / Rao, N.S. / Walker, E. / Sen, S. / Qin, J.
History
DepositionAug 17, 1998Processing site: BNL
Revision 1.0Aug 17, 1999Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 16, 2022Group: Database references / Derived calculations ...Database references / Derived calculations / Experimental preparation / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_exptl_sample_conditions / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _pdbx_nmr_exptl_sample_conditions.pressure_units
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: MYOTROPHIN


Theoretical massNumber of molelcules
Total (without water)12,8791
Polymers12,8791
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)1 / 90RESTRAINT VIOLATION
Representative

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Components

#1: Protein MYOTROPHIN


Mass: 12878.768 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Rattus norvegicus (Norway rat) / Organ: HEART / References: UniProt: P62775

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D- AND 4D-NOESY
1213D-TOCSY
131HN(CA)CB
141HNHA
151C(CO)NH
161H(CCO)NH
171(H)CCH-TOCSY

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Sample preparation

DetailsContents: H2O
Sample conditionsIonic strength: 50 mM PHOSPHATE BUFFER / pH: 6.2 / Pressure: 1 atm / Temperature: 297 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Varian INOVA600 / Manufacturer: Varian / Model: INOVA600 / Field strength: 600 MHz

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Processing

Software
NameClassification
X-PLORmodel building
X-PLORrefinement
X-PLORphasing
NMR software
NameClassification
XPLORstructure solution
XPLORrefinement
RefinementMethod: simulated annealing / Software ordinal: 1
NMR ensembleConformer selection criteria: RESTRAINT VIOLATION / Conformers calculated total number: 90 / Conformers submitted total number: 1

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