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- PDB-2mvz: Solution Structure for Cyclophilin A from Geobacillus Kaustophilus -
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Open data
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Basic information
Entry | Database: PDB / ID: 2mvz | ||||||
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Title | Solution Structure for Cyclophilin A from Geobacillus Kaustophilus | ||||||
![]() | Peptidyl-prolyl cis-trans isomerase | ||||||
![]() | ISOMERASE / Cyclophilin / Thermophile / PPIase | ||||||
Function / homology | ![]() peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / protein folding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Holliday, M.J. / Isern, N.G. / Geoffrey, A.S. / Zhang, F. / Eisenmesser, E.Z. | ||||||
![]() | ![]() Title: Structure and Dynamics of GeoCyp: A Thermophilic Cyclophilin with a Novel Substrate Binding Mechanism That Functions Efficiently at Low Temperatures. Authors: Holliday, M.J. / Camilloni, C. / Armstrong, G.S. / Isern, N.G. / Zhang, F. / Vendruscolo, M. / Eisenmesser, E.Z. #1: Journal: Biomol.Nmr Assign. / Year: 2014 Title: 1H, 13C, and 15N backbone and side chain resonance assignments of thermophilic Geobacillus kaustophilus cyclophilin-A. Authors: Holliday, M.J. / Zhang, F. / Isern, N.G. / Armstrong, G.S. / Eisenmesser, E.Z. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 839.7 KB | Display | ![]() |
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PDB format | ![]() | 705.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 391.4 KB | Display | ![]() |
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Full document | ![]() | 442.5 KB | Display | |
Data in XML | ![]() | 38.2 KB | Display | |
Data in CIF | ![]() | 66.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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NMR ensembles |
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Components
#1: Protein | Mass: 16136.172 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 | Contents: 1.0 mM [U-100% 13C; U-100% 15N] GeoCyp, 1.0 mM DTT, 50 mM sodium phosphate, 93% H2O/7% D2O Solvent system: 93% H2O/7% D2O | ||||||||||||||||
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Sample |
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Sample conditions | pH: 6.5 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||
NMR constraints | NOE constraints total: 1687 / NOE intraresidue total count: 387 / NOE long range total count: 487 / NOE medium range total count: 265 / NOE sequential total count: 548 | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 / Maximum upper distance constraint violation: 146 Å |