[English] 日本語
![](img/lk-miru.gif)
- PDB-1cx1: SECOND N-TERMINAL CELLULOSE-BINDING DOMAIN FROM CELLULOMONAS FIMI... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1cx1 | ||||||
---|---|---|---|---|---|---|---|
Title | SECOND N-TERMINAL CELLULOSE-BINDING DOMAIN FROM CELLULOMONAS FIMI BETA-1,4-GLUCANASE C, NMR, 22 STRUCTURES | ||||||
![]() | ENDOGLUCANASE C | ||||||
![]() | HYDROLASE / CELLULOSE-BINDING DOMAIN / CELLOOLIGOSACHARIDES / CELLULASE / PROTEIN- CARBOHYDRATE INTERACTION | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / ALL CALCULATIONS WERE PERFORMED USING X-PLOR V3.8 WITH SCRIPTS FROM THE X-PLOR 3.1 MANUAL A. A. BRUNGER (1992), NEW HAVEN: YALE UNIVERSITY PRESS ACCORDING TO THE METHOD DESCRIBED BY M. NILGES, G. M. CLORE, A. M. GRONENBORN | ||||||
Model type details | minimized average | ||||||
![]() | Brun, E. / Johnson, P.E. / Creagh, L.A. / Haynes, C.A. / Tomme, P. / Webster, P. / Kilburn, D.G. / McIntosh, L.P. | ||||||
![]() | ![]() Title: Structure and binding specificity of the second N-terminal cellulose-binding domain from Cellulomonas fimi endoglucanase C. Authors: Brun, E. / Johnson, P.E. / Creagh, A.L. / Tomme, P. / Webster, P. / Haynes, C.A. / McIntosh, L.P. #1: ![]() Title: The cellulose-binding domains from Cellulomonas fimi beta-1, 4-glucanase CenC bind nitroxide spin-labeled cellooligosaccharides in multiple orientations Authors: Brun, E. / Johnson, P.E. / MacKenzie, L. / Withers, S.G. / McIntosh, L.P. #2: ![]() Title: Structure of the N-terminal Cellulose-Binding Domain of Cellulomonas Fimi CenC Determined by Nucelar Magnetic Resonance Spectroscopy Authors: Johnson, P.E. / Joshi, M.D. / Tomme, P. / Kilburn, D.G. / McIntosh, L.P. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 1 MB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 900 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 353.1 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 653.2 KB | Display | |
Data in XML | ![]() | 107.1 KB | Display | |
Data in CIF | ![]() | 140.3 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: 15877.379 Da / Num. of mol.: 1 / Fragment: RESIDUES 176-328 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
| ||||||||||||||||||||||||
NMR details | Text: CBDN2 WAS STUDIED IN THE PRESENCE OF SATURATING CONCENTRATIONS OF CELLOPENTAOSE. HOWEVER, DUE TO SPECTRAL OVERLAP, THE OLIGOSACCHARIDE WAS NOT INCLUDED IN THE STRUCTURE CALCULATIONS |
-
Sample preparation
Details |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
Sample conditions | Ionic strength: 50mMNACL / pH: 6 / Pressure: 1 atm / Temperature: 35 K | ||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Varian UNITY / Manufacturer: Varian / Model: UNITY / Field strength: 500 MHz |
---|
-
Processing
NMR software |
| ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: ALL CALCULATIONS WERE PERFORMED USING X-PLOR V3.8 WITH SCRIPTS FROM THE X-PLOR 3.1 MANUAL A. A. BRUNGER (1992), NEW HAVEN: YALE UNIVERSITY PRESS ACCORDING TO THE METHOD DESCRIBED BY M. ...Method: ALL CALCULATIONS WERE PERFORMED USING X-PLOR V3.8 WITH SCRIPTS FROM THE X-PLOR 3.1 MANUAL A. A. BRUNGER (1992), NEW HAVEN: YALE UNIVERSITY PRESS ACCORDING TO THE METHOD DESCRIBED BY M. NILGES, G. M. CLORE, A. M. GRONENBORN Software ordinal: 1 Details: A TOTAL OF 1510 NOE DERIVED DISTANCE RESTRAINTS THAT COMPRISE 700 INTRARESIDUE, 332 SEQUENTIAL, 83 SHORT RANGE (1<|I-J|<=4), 394 LONG RANGE (|I-J|>4) WERE INCLUDED.. 1 DISULPHIDE BOND DISTANCE RESTRAINT, 86 HYDROGEN BOND RESTRAINTS, 53 PHI ANGLE RESTRAINTS, 70 PSI ANGLE RESTRAINTS, AND 48 CHI1 RESTRAINTS WERE ALSO INCLUDED. | ||||||||||||||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: STRUCTURES WITH ACCEPTABLE COVALENT GEOMETRY,STRUCTURES WITH THE LEAST RESTRAINT VIOLATIONS,STRUCTURES WITH THE LOWEST ENERGY Conformers calculated total number: 60 / Conformers submitted total number: 22 |