[English] 日本語
![](img/lk-miru.gif)
- PDB-1m9l: Relaxation-based Refined Structure Of Chlamydomonas Outer Arm Dyn... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1m9l | ||||||
---|---|---|---|---|---|---|---|
Title | Relaxation-based Refined Structure Of Chlamydomonas Outer Arm Dynein Light Chain 1 | ||||||
![]() | Outer Arm Dynein Light Chain 1 | ||||||
![]() | CONTRACTILE PROTEIN / Leucine-rich repeat / Relaxation / Structural refinement / Backbone dynamics / Structure from MOLMOL | ||||||
Function / homology | ![]() outer dynein arm / outer dynein arm assembly / dynein heavy chain binding / motile cilium / alpha-tubulin binding / microtubule Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / simulated annealing, molecular dynamics | ||||||
![]() | Wu, H.W. / Maciejewski, M.W. / Marintchev, A. / Benashski, S.E. / Mullen, G.P. / King, S.M. | ||||||
![]() | ![]() Title: Relaxation-based structure refinement and backbone molecular dynamics of the Dynein motor domain-associated light chain Authors: Wu, H. / Blackledge, M. / Maciejewski, M.W. / Mullen, G.P. / King, S.M. #1: ![]() Title: Solution Structure of A Dynein Motor Domain Associated Light Chain Authors: Wu, H.W. / Maciejewski, M.W. / Marintchev, A. / Benashski, S.E. / Mullen, G.P. / King, S.M. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 919.5 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 765.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 353.8 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 435.2 KB | Display | |
Data in XML | ![]() | 57.1 KB | Display | |
Data in CIF | ![]() | 75.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein | Mass: 22317.715 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
| ||||||||||||||||
NMR details | Text: using relaxation R2/R1 ratios as long range constraints to refine structure. |
-
Sample preparation
Details | Contents: ~2.0 mM Light Chain 1 protein, U-15N, 2.5 mM Tris.Cl pH 6.7, 100 mM NaCl; 90% H2O, 10% D2O. Solvent system: 90% H2O/10% D2O |
---|---|
Sample conditions | pH: 6.7 / Pressure: ambient / Temperature: 298 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
|
-
Processing
NMR software |
| ||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: simulated annealing, molecular dynamics / Software ordinal: 1 | ||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||
NMR ensemble | Conformer selection criteria: all calculated structures submitted Conformers calculated total number: 15 / Conformers submitted total number: 15 |