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Open data
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Basic information
Entry | Database: PDB / ID: 6fd7 | ||||||
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Title | NMR structure of the first TPR domain of the human RPAP3 protein | ||||||
![]() | RNA polymerase II-associated protein 3 | ||||||
![]() | CHAPERONE / TPR HSP chaperone | ||||||
Function / homology | ![]() R2TP complex / RPAP3/R2TP/prefoldin-like complex / protein folding chaperone complex / protein stabilization / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / molecular dynamics | ||||||
![]() | Quinternet, M. / Chagot, M.E. / Manival, X. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Deep Structural Analysis of RPAP3 and PIH1D1, Two Components of the HSP90 Co-chaperone R2TP Complex. Authors: Henri, J. / Chagot, M.E. / Bourguet, M. / Abel, Y. / Terral, G. / Maurizy, C. / Aigueperse, C. / Georgescauld, F. / Vandermoere, F. / Saint-Fort, R. / Behm-Ansmant, I. / Charpentier, B. / ...Authors: Henri, J. / Chagot, M.E. / Bourguet, M. / Abel, Y. / Terral, G. / Maurizy, C. / Aigueperse, C. / Georgescauld, F. / Vandermoere, F. / Saint-Fort, R. / Behm-Ansmant, I. / Charpentier, B. / Pradet-Balade, B. / Verheggen, C. / Bertrand, E. / Meyer, P. / Cianferani, S. / Manival, X. / Quinternet, M. #1: Journal: Biomol NMR Assign / Year: 2015 Title: (1)H, (15)N and (13)C resonance assignments of the two TPR domains from the human RPAP3 protein. Authors: Chagot, M.E. / Jacquemin, C. / Branlant, C. / Charpentier, B. / Manival, X. / Quinternet, M. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 774.2 KB | Display | ![]() |
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PDB format | ![]() | 659.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 6fdpC ![]() 6fdtC ![]() 6gxzC C: citing same article ( |
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Similar structure data | |
Other databases |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 14490.407 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Type: solution Contents: 1 mM [U-13C; U-15N] RPAP3-TPR1, 10 mM sodium phosphate, 150 mM sodium chloride, 0.5 mM TCEP, 95% H2O/5% D2O Label: sample_1 / Solvent system: 95% H2O/5% D2O | ||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 150 mM / Label: cond_1 / pH: 6.4 / Pressure: 1 atm / Temperature: 303 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE III / Manufacturer: Bruker / Model: AVANCE III / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: molecular dynamics / Software ordinal: 5 | ||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest restraint energies Conformers calculated total number: 200 / Conformers submitted total number: 20 |