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- PDB-7dme: Solution structure of human Aha1 -

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Basic information

Entry
Database: PDB / ID: 7dme
TitleSolution structure of human Aha1
ComponentsActivator of 90 kDa heat shock protein ATPase homolog 1
KeywordsSTRUCTURAL PROTEIN / 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 / DGSA-distance geometry 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 2.0Sep 22, 2021Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Experimental preparation / Refinement description
Category: atom_site / database_2 ...atom_site / database_2 / pdbx_nmr_exptl / pdbx_nmr_exptl_sample / pdbx_nmr_refine / pdbx_nmr_sample_details / pdbx_validate_close_contact / pdbx_validate_planes / pdbx_validate_torsion
Item: _atom_site.Cartn_x / _atom_site.Cartn_y ..._atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_exptl.solution_id / _pdbx_nmr_exptl_sample.isotopic_labeling / _pdbx_nmr_exptl_sample.solution_id / _pdbx_nmr_refine.method / _pdbx_nmr_sample_details.contents / _pdbx_nmr_sample_details.label / _pdbx_nmr_sample_details.solution_id / _pdbx_nmr_sample_details.solvent_system / _pdbx_nmr_sample_details.type / _pdbx_validate_close_contact.PDB_model_num / _pdbx_validate_close_contact.auth_atom_id_1 / _pdbx_validate_close_contact.auth_atom_id_2 / _pdbx_validate_close_contact.auth_comp_id_1 / _pdbx_validate_close_contact.auth_comp_id_2 / _pdbx_validate_close_contact.auth_seq_id_1 / _pdbx_validate_close_contact.auth_seq_id_2 / _pdbx_validate_close_contact.dist / _pdbx_validate_planes.rmsd
Description: Model orientation/position / Provider: author / Type: Coordinate replacement
Revision 2.1May 15, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 / Item: _database_2.pdbx_DOI

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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)34,6501
Polymers34,6501
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: 34650.168 Da / Num. of mol.: 1
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
116isotropic12D 1H-15N HSQC
125anisotropic12D 1H-15N IPAP-HSQC
137isotropic13D HNCO
147isotropic13D HN(CA)CO
157isotropic13D HNCA
167isotropic13D CBCA(CO)NH
177isotropic13D HN(CA)CB
187isotropic13D HBHA(CO)NH
197isotropic13D H(CCO)NH
1106isotropic13D 1H-15N NOESY

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Sample preparation

Details
TypeSolution-IDContentsLabelSolvent system
filamentous virus50.5 mM [U-15N70%2H] Aha1, 28% virus/62% H2O/10% D2O15N2H_Aha128% virus/62% H2O/10% D2O
solution60.5 mM [U-15N50%2H] Aha1, 90% H2O/10% D2O15N2H_Aha190% H2O/10% D2O
solution70.5 mM [U-15N13C50%2H] Aha1, 90% H2O/10% D2O15N13C2H_Aha190% H2O/10% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
0.5 mMAha1[U-15N70%2H]5
0.5 mMAha1[U-15N50%2H]6
0.5 mMAha1[U-15N13C50%2H]7
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: DGSA-distance geometry 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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