+Open data
-Basic information
Entry | Database: PDB / ID: 1ew3 | ||||||
---|---|---|---|---|---|---|---|
Title | CRYSTAL STRUCTURE OF THE MAJOR HORSE ALLERGEN EQU C 1 | ||||||
Components | ALLERGEN EQU C 1 | ||||||
Keywords | ALLERGEN / lipocalin / beta barrel | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Equus caballus (horse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.3 Å | ||||||
Authors | Lascombe, M.B. / Gregoire, C. / Poncet, P. / Tavares, G.A. / Rosinski-Chupin, I. / Rabillon, J. / Goubran-Botros, H. / Mazie, J.C. / David, B. / Alzari, P.M. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2000 Title: Crystal structure of the allergen Equ c 1. A dimeric lipocalin with restricted IgE-reactive epitopes. Authors: Lascombe, M.B. / Gregoire, C. / Poncet, P. / Tavares, G.A. / Rosinski-Chupin, I. / Rabillon, J. / Goubran-Botros, H. / Mazie, J.C. / David, B. / Alzari, P.M. #1: Journal: Acta Crystallogr.,Sect.D / Year: 1999 Title: Crystallization and Preliminary Crystallographic Analysis of the Major Horse Allergen Equ c 1 Authors: Gregoire, C. / Tavares, G.A. / Lorenzo, H.K. / Dandeu, J.P. / David, B. / Alzari, P.M. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1ew3.cif.gz | 42.9 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1ew3.ent.gz | 33.3 KB | Display | PDB format |
PDBx/mmJSON format | 1ew3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ew/1ew3 ftp://data.pdbj.org/pub/pdb/validation_reports/ew/1ew3 | HTTPS FTP |
---|
-Related structure data
Similar structure data |
---|
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
Details | The biological assembly is probably a dimer constructed from the given coordinates and a symmetry partner generated by the crystallographic two-fold axis |
-Components
#1: Protein | Mass: 18747.090 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Equus caballus (horse) / Organ: SUBLINGUAL SALIVARY GLAND / Plasmid: PET28 / Production host: Escherichia coli (E. coli) / References: UniProt: Q95182 |
---|---|
#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.75 Å3/Da / Density % sol: 55.33 % | ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: ammonium sulphate, Tris-HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 291.0K | ||||||||||||||||||||
Crystal grow | *PLUS | ||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, Hamburg / Beamline: X31 / Wavelength: 1.2 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Dec 7, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.2 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→20 Å / Num. all: 43339 / Num. obs: 9166 / % possible obs: 94.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 1 / Redundancy: 4.7 % / Biso Wilson estimate: 48 Å2 / Rmerge(I) obs: 0.082 / Net I/σ(I): 13.2 |
Reflection shell | Resolution: 2.3→2.4 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.431 / % possible all: 97.7 |
Reflection shell | *PLUS % possible obs: 97.7 % |
-Processing
Software |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 2.3→15 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
| ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→15 Å
| ||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||
Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||
LS refinement shell | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 2.4 Å / Rfactor Rfree: 0.331 / Rfactor Rwork: 0.21 / Num. reflection obs: 1119 |