[English] 日本語
![](img/lk-miru.gif)
- PDB-1npq: structure of a rhodamine-labeled N-domain Troponin C mutant (Ca2+... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1npq | ||||||
---|---|---|---|---|---|---|---|
Title | structure of a rhodamine-labeled N-domain Troponin C mutant (Ca2+ saturated) in complex with skeletal Troponin I 115-131 | ||||||
![]() |
| ||||||
![]() | STRUCTURAL PROTEIN / Troponin C- Troponin I complex / bifunctional rhodamine labeled Toponin C | ||||||
Function / homology | ![]() troponin T binding / troponin complex / Striated Muscle Contraction / skeletal muscle contraction / cardiac muscle contraction / actin binding / calcium ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / simulated annealing using torsion angle dynamics, cartesian dynamics with the program CNS 1.1 | ||||||
Model type details | minimized average | ||||||
![]() | Mercier, P. / Ferguson, R.E. / Irving, M. / Corrie, J.E.T. / Trentham, D.R. / Sykes, B.D. | ||||||
![]() | ![]() Title: NMR Structure of a Bifunctional Rhodamine Labeled N-Domain of Troponin C Complexed with the Regulatory "Switch" Peptide from Troponin I: Implications for in Situ Fluorescence Studies in Muscle Fibers Authors: Mercier, P. / Ferguson, R.E. / Irving, M. / Corrie, J.E.T. / Trentham, D.R. / Sykes, B.D. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 664.7 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 555.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein | Mass: 9932.144 Da / Num. of mol.: 1 / Fragment: TnC, residues 1-90 / Mutation: E56C, E63C Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
---|---|
#2: Protein/peptide | Mass: 1890.303 Da / Num. of mol.: 1 / Fragment: switch peptide, residues 115-131 / Source method: obtained synthetically Details: This sequence occurs naturally in Oryctolagus cuniculus (rabit) References: UniProt: P02643 |
#3: Chemical |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
| ||||||||||||||||||||||||
NMR details | Text: The structure was determined using triple-resonance spectroscopy. The chemical shifts for TnI115-131 were obtained from a 2D_15N/13C_filtered-DIPSI experiment. Intramolecular NOEs for TnI115- ...Text: The structure was determined using triple-resonance spectroscopy. The chemical shifts for TnI115-131 were obtained from a 2D_15N/13C_filtered-DIPSI experiment. Intramolecular NOEs for TnI115-131 were obtained from a 2D_15N/13C_filtered-NOESY experiment. |
-
Sample preparation
Details | Contents: 320 mM KCl, 10 mM imidazole, 1.3% NaN3, pH 6.5, ~1mM sNTnC.2Ca2+.TnI115-131.BR56-63 Solvent system: 90% H2O/10% D2O |
---|---|
Sample conditions | Ionic strength: 320 mM KCl / pH: 6.5 / Pressure: ambiant / Temperature: 303 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
|
---|
-
Processing
NMR software |
| ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: simulated annealing using torsion angle dynamics, cartesian dynamics with the program CNS 1.1 Software ordinal: 1 Details: calcium restraints were introduced only during the 2nd cooling stage using cartesian dynamics. See table 3 of the reference paper for a detailed description of the distance and dihedral restraints. | ||||||||||||||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 21 |