[English] 日本語
Yorodumi- PDB-1ave: CRYSTAL STRUCTURE OF HEN EGG-WHITE APO-AVIDIN IN RELATION TO ITS ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1ave | ||||||
---|---|---|---|---|---|---|---|
Title | CRYSTAL STRUCTURE OF HEN EGG-WHITE APO-AVIDIN IN RELATION TO ITS THERMAL STABILITY PROPERTIES | ||||||
Components | AVIDIN | ||||||
Keywords | BIOTIN-BINDING PROTEIN | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Gallus gallus (chicken) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.8 Å | ||||||
Authors | Pugliese, L. / Coda, A. / Malcovati, M. / Bolognesi, M. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1994 Title: Crystal structure of apo-avidin from hen egg-white. Authors: Pugliese, L. / Malcovati, M. / Coda, A. / Bolognesi, M. #1: Journal: J.Mol.Biol. / Year: 1993 Title: Three-Dimensional Structure of the Tetragonal Crystal Form of Egg-White Avidin in its Functional Complex with Biotin at 2.7 Angstroms Resolution Authors: Pugliese, L. / Coda, A. / Malcovati, M. / Bolognesi, M. #2: Journal: J.Mol.Biol. / Year: 1984 Title: Crystallization of Hen Egg-White Avidin in a Tetragonal Form Authors: Gatti, G. / Bolognesi, M. / Coda, A. / Chiolerio, F. / Filippini, E. / Malcovati, M. | ||||||
History |
| ||||||
Remark 700 | SHEET THE SHEET PRESENTED AS *CH1* ON SHEET RECORDS BELOW IS ACTUALLY AN EIGHT-STRANDED BETA-BARREL. ...SHEET THE SHEET PRESENTED AS *CH1* ON SHEET RECORDS BELOW IS ACTUALLY AN EIGHT-STRANDED BETA-BARREL. THIS IS REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1ave.cif.gz | 57.7 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1ave.ent.gz | 46 KB | Display | PDB format |
PDBx/mmJSON format | 1ave.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ave_validation.pdf.gz | 447.3 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1ave_full_validation.pdf.gz | 465.3 KB | Display | |
Data in XML | 1ave_validation.xml.gz | 14 KB | Display | |
Data in CIF | 1ave_validation.cif.gz | 17.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/av/1ave ftp://data.pdbj.org/pub/pdb/validation_reports/av/1ave | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.4074, 0.9132, -0.008), Vector: Details | THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL YIELD APPROXIMATE COORDINATES FOR CHAIN *B* WHEN APPLIED TO CHAIN *A*. | |
-Components
#1: Protein | Mass: 14350.081 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Gallus gallus (chicken) / References: UniProt: P02701 #2: Sugar | #3: Water | ChemComp-HOH / | Sequence details | POSITION 34 SHOWS RESIDUE MICROHETEROGENEITY (THR OR ILE), AS DETERMINED FROM AMINO ACID SEQUENCING. ...POSITION 34 SHOWS RESIDUE MICROHETER | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
---|
-Sample preparation
Crystal | Density Matthews: 2.39 Å3/Da / Density % sol: 48.44 % | |||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | *PLUS pH: 5.7 / Method: vapor diffusion, hanging dropDetails: referred to 'Pugliese, L.', (1993) J.Mol.Biol., 231, 698-710 | |||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Radiation | Scattering type: x-ray |
---|---|
Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 10 Å / Num. obs: 6390 / Num. measured all: 29082 / Rmerge(I) obs: 0.09 |
-Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Rfactor obs: 0.166 / Highest resolution: 2.8 Å | ||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.8 Å
| ||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||
Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 10 Å / Num. reflection obs: 6390 / Rfactor obs: 0.166 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
|