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- PDB-7hsc: HIGH RESOLUTION SOLUTION STRUCTURE OF THE HEAT SHOCK COGNATE-70 K... -

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Basic information

Entry
Database: PDB / ID: 7hsc
TitleHIGH RESOLUTION SOLUTION STRUCTURE OF THE HEAT SHOCK COGNATE-70 KD SUBSTRATE BINDING DOMAIN OBTAINED BY MULTIDIMENSIONAL NMR TECHNIQUES
ComponentsPROTEIN (HEAT SHOCK COGNATE 70 KD PROTEIN 1)
KeywordsMOLECULAR CHAPERONE / HSP70 / PEPTIDE BINDING / PROTEIN FOLDING
Function / homology
Function and homology information


Attenuation phase / PKR-mediated signaling / positive regulation of protein refolding / prostaglandin binding / positive regulation of lysosomal membrane permeability / lysosomal matrix / Protein methylation / A1 adenosine receptor binding / HSF1-dependent transactivation / mRNA Splicing - Major Pathway ...Attenuation phase / PKR-mediated signaling / positive regulation of protein refolding / prostaglandin binding / positive regulation of lysosomal membrane permeability / lysosomal matrix / Protein methylation / A1 adenosine receptor binding / HSF1-dependent transactivation / mRNA Splicing - Major Pathway / AUF1 (hnRNP D0) binds and destabilizes mRNA / response to nickel cation / protein transmembrane import into intracellular organelle / negative regulation of supramolecular fiber organization / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / response to odorant / Lysosome Vesicle Biogenesis / positive regulation by host of viral genome replication / synaptic vesicle uncoating / protein-containing complex disassembly / GABA synthesis, release, reuptake and degradation / Golgi Associated Vesicle Biogenesis / messenger ribonucleoprotein complex / chaperone-mediated autophagy translocation complex disassembly / slow axonal transport / clathrin-uncoating ATPase activity / Regulation of HSF1-mediated heat shock response / protein targeting to lysosome involved in chaperone-mediated autophagy / late endosomal microautophagy / modulation by host of viral process / C3HC4-type RING finger domain binding / photoreceptor ribbon synapse / negative regulation of NLRP3 inflammasome complex assembly / clathrin coat disassembly / ATP-dependent protein disaggregase activity / maintenance of postsynaptic specialization structure / regulation of protein complex stability / Clathrin-mediated endocytosis / neuron spine / glycinergic synapse / Prp19 complex / postsynaptic specialization membrane / presynaptic cytosol / positive regulation of mRNA splicing, via spliceosome / protein folding chaperone complex / axo-dendritic transport / intermediate filament / regulation of postsynapse organization / negative regulation of cardiac muscle cell apoptotic process / postsynaptic cytosol / Neutrophil degranulation / chaperone-mediated autophagy / phosphatidylserine binding / response to starvation / non-chaperonin molecular chaperone ATPase / positive regulation of proteolysis / chaperone cofactor-dependent protein refolding / estrous cycle / asymmetric synapse / autophagosome / positive regulation of phagocytosis / chaperone-mediated protein folding / skeletal muscle tissue development / ATP metabolic process / protein folding chaperone / forebrain development / cellular response to cadmium ion / heat shock protein binding / photoreceptor inner segment / cerebellum development / lysosomal lumen / RNA splicing / dendritic shaft / response to progesterone / response to activity / kidney development / G protein-coupled receptor binding / ADP binding / peptide binding / ATP-dependent protein folding chaperone / spliceosomal complex / G1/S transition of mitotic cell cycle / regulation of protein stability / terminal bouton / cellular response to hydrogen peroxide / mRNA processing / positive regulation of T cell mediated cytotoxicity / protein import into nucleus / melanosome / unfolded protein binding / synaptic vesicle / protein-macromolecule adaptor activity / protein folding / late endosome / presynapse / response to estradiol / cellular response to heat / protein-folding chaperone binding / perikaryon / protein refolding
Similarity search - Function
Substrate Binding Domain Of DNAk; Chain A, domain 1 / Substrate Binding Domain Of DNAk; Chain A, domain 1 / Heat shock hsp70 proteins family signature 2. / Heat shock hsp70 proteins family signature 1. / Heat shock hsp70 proteins family signature 3. / Heat shock protein 70, conserved site / Heat shock protein 70kD, peptide-binding domain superfamily / Heat shock protein 70 family / Hsp70 protein / Heat shock protein 70kD, C-terminal domain superfamily ...Substrate Binding Domain Of DNAk; Chain A, domain 1 / Substrate Binding Domain Of DNAk; Chain A, domain 1 / Heat shock hsp70 proteins family signature 2. / Heat shock hsp70 proteins family signature 1. / Heat shock hsp70 proteins family signature 3. / Heat shock protein 70, conserved site / Heat shock protein 70kD, peptide-binding domain superfamily / Heat shock protein 70 family / Hsp70 protein / Heat shock protein 70kD, C-terminal domain superfamily / ATPase, nucleotide binding domain / Sandwich / Mainly Beta
Similarity search - Domain/homology
Heat shock cognate 71 kDa protein
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodSOLUTION NMR / DISTANCE GEOMETRY, SIMULATE ANNEALING
AuthorsMorshauser, R.C. / Hu, W. / Wang, H. / Pang, Y. / Flynn, G.C. / Zuiderweg, E.R.P.
CitationJournal: J.Mol.Biol. / Year: 1999
Title: High-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70.
Authors: Morshauser, R.C. / Hu, W. / Wang, H. / Pang, Y. / Flynn, G.C. / Zuiderweg, E.R.
History
DepositionMay 3, 1999Deposition site: BNL / Processing site: RCSB
Revision 1.0May 10, 1999Provider: repository / Type: Initial release
Revision 1.1Apr 26, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 16, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name
Revision 1.4Dec 27, 2023Group: 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: PROTEIN (HEAT SHOCK COGNATE 70 KD PROTEIN 1)


Theoretical massNumber of molelcules
Total (without water)17,5591
Polymers17,5591
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)1 / 50AVERAGE OF LOWEST TOTAL ENERGY
Representative

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Components

#1: Protein PROTEIN (HEAT SHOCK COGNATE 70 KD PROTEIN 1)


Mass: 17558.746 Da / Num. of mol.: 1 / Fragment: SUBSTRATE BINDING DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Strain: JM109(DE3) / Production host: Escherichia coli (E. coli) / Strain (production host): JM109(DE3) / References: UniProt: P63018

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111HNCA
121HN(CA)HA
131HN(CO)CA
141HA(CACO)NH
151CP H(C)CCH-TOCSY
161CP (H)CCH-TOCSY
171CP(H)C(CCACO)NH-TOCSY
18115N-RESOLVED NOESY-HSQC
19113CRESOLVED NOESY-HMQC
11014D 13C
111113C RESOLVED HMQC-NOESY3D 13C
112113N RESOLVED HMQC-NOESY-HSQC3D 13C
113113C RESOLVED HMQC-NOESY-HSQC
1141-HSQC
NMR detailsText: ENERGY MINIMIZED AVERAGE. ASSIGNMENTS OBTAINED WITH TRIPLE RESONANCE NMR SPECTROSCOPY; STEREO-SPECIFIC ASSIGNMENTS WITH 10% 13C LABELED GLUCOSE; STRUCTURE WITH 2 HIGH RESOLUTION 4-D AND 6 3D ...Text: ENERGY MINIMIZED AVERAGE. ASSIGNMENTS OBTAINED WITH TRIPLE RESONANCE NMR SPECTROSCOPY; STEREO-SPECIFIC ASSIGNMENTS WITH 10% 13C LABELED GLUCOSE; STRUCTURE WITH 2 HIGH RESOLUTION 4-D AND 6 3D HETERONUCLEAR-RESOLVED NOESY EXPERIMENTS. SCALAR COUPLINGS WITH HNHA; DYNAMICS WITH T1 AND T2 (NITROGEN)

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Sample preparation

DetailsContents: 1.5 MM 15N OR 15N,13C LABELED PROTEIN 5%D20/95%H2O AND 100%D2O
Sample conditionsIonic strength: 50 mM SODIUM PHOSPHATE / pH: 7.0 / 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 AMX 500BrukerAMX 5005001
Bruker AMX 600BrukerAMX 6006002
Bruker DMX 750BrukerDMX 7507503

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Processing

NMR software
NameVersionDeveloperClassification
DiscoverBIOSYMrefinement
Felixstructure solution
MSI INSIGHTINSIGHTstructure solution
MSI DISCOVERDISCOVERstructure solution
RefinementMethod: DISTANCE GEOMETRY, SIMULATE ANNEALING / Software ordinal: 1
Details: STRUCTURE WAS EXTENSIVELY MINIMIZED. THE PROTOCOL CAN BE FOUND IN THE JMB PAPER (IN PRESS, 1999)
NMR ensembleConformer selection criteria: AVERAGE OF LOWEST TOTAL ENERGY
Conformers calculated total number: 50 / Conformers submitted total number: 1

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