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- PDB-1i6z: BAG DOMAIN OF BAG1 COCHAPERONE -

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Basic information

Entry
Database: PDB / ID: 1i6z
TitleBAG DOMAIN OF BAG1 COCHAPERONE
ComponentsBAG-FAMILY MOLECULAR CHAPERONE REGULATOR-1
KeywordsCHAPERONE / triple helix bundle
Function / homology
Function and homology information


Regulation of HSF1-mediated heat shock response / adenyl-nucleotide exchange factor activity / positive regulation of smooth muscle cell apoptotic process / positive regulation of Schwann cell differentiation / protein localization to mitochondrion / negative regulation of motor neuron apoptotic process / negative regulation of protein phosphorylation / neuron differentiation / protein-folding chaperone binding / protein stabilization ...Regulation of HSF1-mediated heat shock response / adenyl-nucleotide exchange factor activity / positive regulation of smooth muscle cell apoptotic process / positive regulation of Schwann cell differentiation / protein localization to mitochondrion / negative regulation of motor neuron apoptotic process / negative regulation of protein phosphorylation / neuron differentiation / protein-folding chaperone binding / protein stabilization / apoptotic process / negative regulation of apoptotic process / perinuclear region of cytoplasm / membrane / nucleus / cytoplasm / cytosol
Similarity search - Function
BAG domain / BAG domain superfamily / Molecular chaperone regulator BAG / BAG domain / BAG domain / BAG domain profile. / BAG domains, present in regulator of Hsp70 proteins / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Ubiquitin family / Ubiquitin homologues ...BAG domain / BAG domain superfamily / Molecular chaperone regulator BAG / BAG domain / BAG domain / BAG domain profile. / BAG domains, present in regulator of Hsp70 proteins / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Ubiquitin-like domain superfamily / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
BAG family molecular chaperone regulator 1
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodSOLUTION NMR / torsion angle dynamics
AuthorsBriknarova, K. / Takayama, S. / Brive, L. / Havert, M.L. / Knee, D.A. / Velasco, J. / Homma, S. / Cabezas, E. / Stuart, J. / Hoyt, D.W. ...Briknarova, K. / Takayama, S. / Brive, L. / Havert, M.L. / Knee, D.A. / Velasco, J. / Homma, S. / Cabezas, E. / Stuart, J. / Hoyt, D.W. / Satterthwait, A.C. / Llinas, M. / Reed, J.C. / Ely, K.R.
CitationJournal: Nat.Struct.Biol. / Year: 2001
Title: Structural analysis of BAG1 cochaperone and its interactions with Hsc70 heat shock protein.
Authors: Briknarova, K. / Takayama, S. / Brive, L. / Havert, M.L. / Knee, D.A. / Velasco, J. / Homma, S. / Cabezas, E. / Stuart, J. / Hoyt, D.W. / Satterthwait, A.C. / Llinas, M. / Reed, J.C. / Ely, K.R.
History
DepositionMar 6, 2001Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 6, 2001Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_nmr_spectrometer / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model / _struct_ref_seq_dif.details
Revision 1.4May 22, 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: BAG-FAMILY MOLECULAR CHAPERONE REGULATOR-1


Theoretical massNumber of molelcules
Total (without water)15,5151
Polymers15,5151
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)25 / 25all calculated structures submitted
RepresentativeModel #1lowest energy

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Components

#1: Protein BAG-FAMILY MOLECULAR CHAPERONE REGULATOR-1 / BCL-2 BINDING ATHANOGENE-1 / BAG-1


Mass: 15514.893 Da / Num. of mol.: 1 / Fragment: BAG DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: BAG1 / Plasmid: PGEX-3X / Production host: Escherichia coli (E. coli) / References: UniProt: Q60739

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 15N-separated NOESY
1234D 13C-separated NOESY
1344D 15N-separated NOESY
1423D 13C/15N-separated NOESY
152CBCA(CO)NH
162HN(CA)CB
172C(CO)NH
182H(CCO)NH
192(H)CCH-TOCSY
1102HNCO

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Sample preparation

Details
Solution-IDContentsSolvent system
12mM BAG1 U-15N; 10mM potassium phosphate buffer, pH 7.2; 25mM KCl; 1mM EDTA; 1mM DTT; 0.02% NaN3; 90%H2O, 10%D2O90% H2O/10% D2O
22mM BAG1 U-15N,13C; 10mM potassium phosphate buffer, pH 7.2; 25mM KCl; 1mM EDTA; 1mM DTT; 0.02% NaN3; 90%H2O, 10%D2O90% H2O/10% D2O
32mM BAG1 U-15N,13C; 10mM potassium phosphate buffer, pH 7.2; 25mM KCl; 1mM EDTA; 1mM DTT; 0.02% NaN3; 100%D2O100% D2O
42mM BAG1 U-15N,2H; 10mM potassium phosphate buffer, pH 7.2; 25mM KCl; 1mM EDTA; 1mM DTT; 0.02% NaN3; 90%H2O, 10%D2O90% H2O/10% D2O
Sample conditionsIonic strength: 10mM potassium phosphate, 25mM KCl / pH: 7.2 / Pressure: ambient / Temperature: 310 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AVANCEBrukerAVANCE5001
Varian UNITYVarianUNITY5002
Varian INOVAVarianINOVA6003
Varian UNITYPLUSVarianUNITYPLUS7504

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Processing

NMR software
NameVersionDeveloperClassification
VNMRVariancollection
Felix98Molecular Simulations, Inc.processing
Felix98Molecular Simulations, Inc.data analysis
CNS1Brungerstructure solution
CNS1Brungerrefinement
RefinementMethod: torsion angle dynamics / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: all calculated structures submitted
Conformers calculated total number: 25 / Conformers submitted total number: 25

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