[English] 日本語
![](img/lk-miru.gif)
- PDB-1dgw: Structure of the rhombohedral crystal of canavalin from jack bean -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1dgw | ||||||
---|---|---|---|---|---|---|---|
Title | Structure of the rhombohedral crystal of canavalin from jack bean | ||||||
![]() | (CANAVALIN) x 3 | ||||||
![]() | PLANT PROTEIN / DUPLICATED SWISS-ROLL BETA BARRELS / LOOPS WITH ALPHA HELICES / MEROHEDRAL/ HEMIHEDRAL TWINNING | ||||||
Function / homology | ![]() nutrient reservoir activity / protein-containing complex / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Ko, T.-P. / McPherson, A. | ||||||
![]() | ![]() Title: X-ray diffraction and atomic force microscopy analysis of twinned crystals: rhombohedral canavalin. Authors: Ko, T.P. / Kuznetsov, Y.G. / Malkin, A.J. / Day, J. / McPherson, A. #1: ![]() Title: Determination of three crystal structures of canavalin by molecular replacement Authors: Ko, T.-P. / Ng, J.D. / Day, J. / Greenwood, A. / McPherson, A. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 87.4 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 66.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 20640.342 Da / Num. of mol.: 1 / Fragment: RESIDUES 46-223 / Source method: isolated from a natural source Details: LEGUME STORAGE PROTEIN; LIMITED DIGESTION BY TRYPSIN Source: (natural) ![]() ![]() |
---|---|
#2: Protein | Mass: 9073.182 Da / Num. of mol.: 1 / Fragment: RESIDUES 246-324 / Source method: isolated from a natural source Details: LEGUME STORAGE PROTEIN; LIMITED DIGESTION BY TRYPSIN Source: (natural) ![]() ![]() |
#3: Protein | Mass: 10269.446 Da / Num. of mol.: 1 / Fragment: RESIDUES 331-423 / Source method: isolated from a natural source Details: LEGUME STORAGE PROTEIN; LIMITED DIGESTION BY TRYPSIN Source: (natural) ![]() ![]() |
#4: Chemical | ChemComp-PO4 / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 3.43 Å3/Da / Density % sol: 64.11 % |
---|---|
Crystal grow | Temperature: 293 K / Method: liquid diffusion / pH: 6.8 Details: DULBECCO'S PHOSPHATE BUFFERED SALINE, AMMONIUM HYDROXIDE (TRACE), MICROGRAVITY, pH 6.8, LIQUID DIFFUSION, temperature 293K |
Crystal grow | *PLUS Details: Koszelak, S., (1995) Biophys. J., 69, 13. |
-Data collection
Diffraction | Mean temperature: 298 K |
---|---|
Diffraction source | Source: ![]() |
Detector | Type: SDMS / Detector: AREA DETECTOR / Date: Aug 23, 1994 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.69→300 Å / Num. all: 56649 / Num. obs: 56649 / % possible obs: 95 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6.1 % / Biso Wilson estimate: 27.2 Å2 / Rmerge(I) obs: 0.088 / Net I/σ(I): 18.7 |
Reflection shell | Resolution: 1.69→1.78 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.304 / % possible all: 81.1 |
Reflection | *PLUS Lowest resolution: 300 Å / Num. measured all: 343806 / Rmerge(I) obs: 0.0885 |
Reflection shell | *PLUS % possible obs: 81.1 % / Num. unique obs: 6947 / Num. measured obs: 16233 / Mean I/σ(I) obs: 1.05 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 1.7→300 Å / σ(F): 2 / σ(I): 0 / Stereochemistry target values: ENGH & HUBER / Details: THE REFINEMENT USED A TWIN FRACTION OF 0.426.
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.7→300 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: CNS / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.7 Å / Lowest resolution: 500 Å / Num. reflection obs: 49983 / σ(F): 2 / % reflection Rfree: 8 % / Rfactor Rfree: 0.245 / Rfactor Rwork: 0.176 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | *PLUS Highest resolution: 1.7 Å / Lowest resolution: 1.78 Å / Rfactor Rfree: 0.386 / Rfactor Rwork: 0.375 / Num. reflection obs: 4062 |