[English] 日本語
![](img/lk-miru.gif)
- PDB-2m3x: Solution structure of Ph1500: a homohexameric protein centered on... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 2m3x | ||||||
---|---|---|---|---|---|---|---|
Title | Solution structure of Ph1500: a homohexameric protein centered on a 12-bladed beta-propeller | ||||||
![]() | PH1500 | ||||||
![]() | UNKNOWN FUNCTION / beta-propeller / 12-bladed / homohexamer / beta-clam | ||||||
Function / homology | ![]() Thrombin, subunit H - #360 / : / Domain of unknown function (DUF6849) / Vcp-like ATPase; Chain A, domain 2 - #10 / Vcp-like ATPase; Chain A, domain 2 / CDC48, domain 2 / Cell division protein 48 (CDC48), domain 2 / Cell division protein 48 (CDC48) domain 2 / CDC48 domain 2-like superfamily / Thrombin, subunit H ...Thrombin, subunit H - #360 / : / Domain of unknown function (DUF6849) / Vcp-like ATPase; Chain A, domain 2 - #10 / Vcp-like ATPase; Chain A, domain 2 / CDC48, domain 2 / Cell division protein 48 (CDC48), domain 2 / Cell division protein 48 (CDC48) domain 2 / CDC48 domain 2-like superfamily / Thrombin, subunit H / Roll / Beta Barrel / Mainly Beta / Alpha Beta Similarity search - Domain/homology | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | minimized average structure, model1 | ||||||
Model type details | minimized average | ||||||
![]() | Varnay, I. / Truffault, V. / Kessler, H. / Coles, M. | ||||||
![]() | ![]() Title: Solution structure of Ph1500: a homohexameric protein centered on a 12-bladed beta-propeller Authors: Ammelburg, M. / Schiff, J. / Hartmann, M.D. / Varnay, I. / Djuranovic, S. / Truffault, V. / Martin, J. / Coles, M. / Lupas, A.N. #2: Journal: J.Am.Chem.Soc. / Year: 2010 Title: Optimized measurement temperature gives access to the solution structure of a 49 kDa homohexameric -propeller Authors: Varnay, I. / Truffault, V. / Djuranovic, S.D. / Ursinus, A. / Coles, M. / Kessler, H. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 5.5 MB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 4.7 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 451.6 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 1006.8 KB | Display | |
Data in XML | ![]() | 297.1 KB | Display | |
Data in CIF | ![]() | 433.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
---|---|
Similar structure data | |
Other databases |
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein | Mass: 16728.738 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3 Gene: PH1500 / Production host: ![]() ![]() |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-
Sample preparation
Details |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Sample |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Sample conditions |
|
-NMR measurement
NMR spectrometer |
|
---|
-
Processing
NMR software |
| ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: simulated annealing / Software ordinal: 1 Details: Refinement is asymmetric. Each monomer has independent restraints and no symmetry operation is applied | ||||||||||||||||||||||||
NMR constraints | Protein chi angle constraints total count: 100 / Protein other angle constraints total count: 47 / Protein phi angle constraints total count: 131 / Protein psi angle constraints total count: 136 | ||||||||||||||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 50 / Conformers submitted total number: 20 / Maximum lower distance constraint violation: 0.04 Å / Maximum torsion angle constraint violation: 0.4 ° / Maximum upper distance constraint violation: 0.14 Å | ||||||||||||||||||||||||
NMR ensemble rms | Distance rms dev: 0.0047 Å |