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- PDB-1ave: CRYSTAL STRUCTURE OF HEN EGG-WHITE APO-AVIDIN IN RELATION TO ITS ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ave | ||||||
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Title | CRYSTAL STRUCTURE OF HEN EGG-WHITE APO-AVIDIN IN RELATION TO ITS THERMAL STABILITY PROPERTIES | ||||||
![]() | AVIDIN![]() | ||||||
![]() | BIOTIN-BINDING PROTEIN | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Pugliese, L. / Coda, A. / Malcovati, M. / Bolognesi, M. | ||||||
![]() | ![]() Title: Crystal structure of apo-avidin from hen egg-white. Authors: Pugliese, L. / Malcovati, M. / Coda, A. / Bolognesi, M. #1: ![]() 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: ![]() 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 |
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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. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 57.7 KB | Display | ![]() |
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PDB format | ![]() | 46 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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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*. | |
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Components
#1: Protein | ![]() Mass: 14350.081 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #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 | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.39 Å3/Da / Density % sol: 48.44 % | |||||||||||||||||||||||||
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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
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-Data collection
Radiation | Scattering type: x-ray |
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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 |
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Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
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Refinement | Rfactor obs: 0.166 / Highest resolution: 2.8 Å | ||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.8 Å
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Refine LS restraints |
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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
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