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- PDB-7dmd: Solution structure of human Aha1 N-terminal domain -

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Basic information

Entry
Database: PDB / ID: 7dmd
TitleSolution structure of human Aha1 N-terminal domain
ComponentsActivator of 90 kDa heat shock protein ATPase homolog 1
KeywordsSTRUCTURAL PROTEIN / N-terminal domain of human Activator of Hsp90 ATPase homolog 1
Function / homology
Function and homology information


positive regulation of ATP-dependent activity / ATPase activator activity / Hsp90 protein binding / protein folding / protein-folding chaperone binding / cadherin binding / endoplasmic reticulum / extracellular exosome / cytosol
Similarity search - Function
Activator of Hsp90 ATPase, N-terminal / Activator of Hsp90 ATPase, Aha1 / Activator of Hsp90 ATPase, N-terminal / Activator of Hsp90 ATPase, N-terminal / Activator of Hsp90 ATPase homologue 1-like / Activator of Hsp90 ATPase homolog 1-like protein / START-like domain superfamily
Similarity search - Domain/homology
Activator of 90 kDa heat shock protein ATPase homolog 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing
AuthorsHu, H. / Zhou, C. / Zhang, N.
Funding support China, 1items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC) China
CitationJournal: Molecules / Year: 2021
Title: Aha1 Exhibits Distinctive Dynamics Behavior and Chaperone-Like Activity.
Authors: Hu, H. / Wang, Q. / Du, J. / Liu, Z. / Ding, Y. / Xue, H. / Zhou, C. / Feng, L. / Zhang, N.
History
DepositionDec 3, 2020Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Apr 21, 2021Provider: repository / Type: Initial release
Revision 1.1May 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: Activator of 90 kDa heat shock protein ATPase homolog 1


Theoretical massNumber of molelcules
Total (without water)15,1361
Polymers15,1361
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 100structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein Activator of 90 kDa heat shock protein ATPase homolog 1 / AHA1 / p38


Mass: 15135.936 Da / Num. of mol.: 1 / Fragment: N-terminal domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: AHSA1, C14orf3, HSPC322 / Production host: Escherichia coli (E. coli) / References: UniProt: O95433

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDSample stateSpectrometer-IDType
111isotropic12D 1H-15N HSQC
123isotropic12D 1H-13C HSQC
134anisotropic12D 1H-15N IPAP-HSQC
142isotropic13D HNCO
152isotropic13D HN(CA)CO
162isotropic13D HNCA
172isotropic13D CBCA(CO)NH
182isotropic13D HN(CA)CB
192isotropic13D HBHA(CO)NH
1102isotropic13D H(CCO)NH
1112isotropic13D C(CO)NH
1123isotropic13D (H)CCH-TOCSY
1131isotropic13D 1H-15N NOESY
1143isotropic13D 1H-13C NOESY

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Sample preparation

Details
TypeSolution-IDContentsLabelSolvent system
solution10.5 mM [U-15N] Aha1N, 90% H2O/10% D2O15N_Aha1N90% H2O/10% D2O
solution20.5 mM [U-15N;U-13C] Aha1N, 90% H2O/10% D2O15N;13C_Aha1N90% H2O/10% D2O
solution30.5 mM [U-13C] Aha1N, 100% D2O13C_Aha1N100% D2O
filamentous virus40.5 mM [U-15N] Aha1N, 37% virus/53% H2O/10% D2O15N_Aha1N37% virus/53% H2O/10% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
0.5 mMAha1N[U-15N]1
0.5 mMAha1N[U-15N;U-13C]2
0.5 mMAha1N[U-13C]3
0.5 mMAha1N[U-15N]4
Sample conditionsIonic strength: 150 mM / Label: conditions_1 / pH: 7.5 / Pressure: 1 atm / Temperature: 298 K

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NMR measurement

NMR spectrometerType: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz

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Processing

NMR software
NameDeveloperClassification
X-PLOR NIHSchwieters, Kuszewski, Tjandra and Clorerefinement
X-PLOR NIHSchwieters, Kuszewski, Tjandra and Clorestructure calculation
CARAKeller and Wuthrichchemical shift assignment
CARAKeller and Wuthrichpeak picking
RefinementMethod: simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 100 / Conformers submitted total number: 20

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