+
Open data
-
Basic information
Entry | Database: PDB / ID: 1os8 | ||||||
---|---|---|---|---|---|---|---|
Title | RECOMBINANT STREPTOMYCES GRISEUS TRYPSIN | ||||||
![]() | trypsin | ||||||
![]() | HYDROLASE / TRYPSIN / SERINE PROTEASE | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Page, M.J. / Wong, S.L. / Hewitt, J. / Strynadka, N.C. / MacGillivray, R.T. | ||||||
![]() | ![]() Title: Engineering the Primary Substrate Specificity of Streptomyces griseus Trypsin. Authors: Page, M.J. / Wong, S.L. / Hewitt, J. / Strynadka, N.C. / MacGillivray, R.T. #1: ![]() Title: Refined Crystal Structure of Streptomyces Griseus Trypsin at 1.7 Angstroms Resolution Authors: Read, R.J. / James, M.N.G. #2: ![]() Title: Critical Comparison of Comparative Model Building of Streptomyces Griseus Trypsin Authors: Read, R.J. / Brayer, G.D. / Jurasek, L. / James, M.N.G. | ||||||
History |
| ||||||
Remark 999 | SEQUENCE AMINO ACID NUMBERING IS BASED ON CHYMOTRYPSINOGEN AND IS THE SAME AS THAT USED IN THE ...SEQUENCE AMINO ACID NUMBERING IS BASED ON CHYMOTRYPSINOGEN AND IS THE SAME AS THAT USED IN THE NATIVE STRUCTURE (PDB ID 1SGT). |
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 59.8 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 42.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 425.4 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 425.8 KB | Display | |
Data in XML | ![]() | 12.1 KB | Display | |
Data in CIF | ![]() | 17.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1ossC ![]() 1sgtS S: Starting model for refinement C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 23122.787 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
---|---|
#2: Chemical | ChemComp-SO4 / |
#3: Chemical | ChemComp-CA / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.02 Å3/Da / Density % sol: 38.73 % | ||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 1.55 M AMMONIUM SULPHATE, 10 MM CALCIUM ACETATE, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: microdialysis / Details: Read, R.J., (1988) J.Mol.Biol., 200, 523. | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Nov 20, 2002 |
Radiation | Monochromator: OSMIC MIRRORS / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.55→25 Å / Num. all: 73616 / Num. obs: 26599 / % possible obs: 86.2 % / Observed criterion σ(I): 2 / Biso Wilson estimate: 14.7 Å2 / Rmerge(I) obs: 0.041 / Net I/σ(I): 20.4 |
Reflection shell | Resolution: 1.55→1.61 Å / Rmerge(I) obs: 0.182 / Mean I/σ(I) obs: 5.1 / % possible all: 74.1 |
Reflection | *PLUS Highest resolution: 1.5 Å / Num. obs: 25923 / % possible obs: 84.1 % / Redundancy: 2.8 % |
Reflection shell | *PLUS Lowest resolution: 1.65 Å / % possible obs: 74.1 % |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: RIGID BODY REFINEMENT Starting model: 1SGT Resolution: 1.55→13.92 Å / Rfactor Rfree error: 0.006 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
| ||||||||||||||||||||||||||||||||||||
Solvent computation | Solvent model: FLAT MODEL / Bsol: 51.8134 Å2 / ksol: 0.415275 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 12.9 Å2
| ||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error free: 0.2 Å / Luzzati sigma a free: 0.16 Å | ||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.55→13.92 Å
| ||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 1.55→1.65 Å / Rfactor Rfree error: 0.019 / Total num. of bins used: 6
| ||||||||||||||||||||||||||||||||||||
Xplor file |
| ||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: XTALVIEW / Classification: refinement | ||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.5 Å | ||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
|