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Open data
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Basic information
Entry | Database: PDB / ID: 2y32 | ||||||
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Title | Crystal structure of bradavidin | ||||||
![]() | BLR5658 PROTEIN | ||||||
![]() | BIOTIN-BINDING PROTEIN | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Leppiniemi, J. / Gronroos, T. / Johnson, M.S. / Kulomaa, M.S. / Hytonen, V.P. / Airenne, T.T. | ||||||
![]() | ![]() Title: Structure of Bradavidin - C-Terminal Residues Act as Intrinsic Ligands. Authors: Leppiniemi, J. / Gronroos, T. / Maatta, J.A.E. / Johnson, M.S. / Kulomaa, M.S. / Hytonen, V.P. / Airenne, T.T. | ||||||
History |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "CA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "DA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN -5-STRANDED BARREL THIS IS REPRESENTED BY A -4-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 | ![]() | 236.8 KB | Display | ![]() |
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PDB format | ![]() | 195.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 14391.656 Da / Num. of mol.: 4 / Fragment: RESIDUES 26-163 Source method: isolated from a genetically manipulated source Details: AUTHORS REPORT RESIDUES 1-25 ARE A SIGNAL PEPTIDE THAT IS ABSENT IN CRYSTALLIZED FORM Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() #2: Water | ChemComp-HOH / | ![]() Sequence details | RESIDUES 1-25 CORRESPOND | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.1 Å3/Da / Density % sol: 41 % / Description: HOMOLOGY MODELS WERE CREATED USING MODELLER. |
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Crystal grow![]() | Method: vapor diffusion, sitting drop Details: 0.7 MICROLITER OF WELL SOLUTION CONTAINING 25% PEG 4000, 0.17 M AMMONIUM ACETATE, AND 0.08 M SODIUM ACETATE, PH 4.6 WERE MIXED WITH 0.8 MICROLITER OF PROTEIN SOLUTION CONTAINING 0.4 MG PER ...Details: 0.7 MICROLITER OF WELL SOLUTION CONTAINING 25% PEG 4000, 0.17 M AMMONIUM ACETATE, AND 0.08 M SODIUM ACETATE, PH 4.6 WERE MIXED WITH 0.8 MICROLITER OF PROTEIN SOLUTION CONTAINING 0.4 MG PER ML OF PROTEIN, 50 MM SODIUM ACETATE, PH 4. THE PROTEIN SOLUTION WAS DILUTED WITH SATURATED SOLUTION OF 4-HYDROXYAZOBENZENE-2-CARBOXYLIC ACID IN 1 TO 10 VOLUME RATIO BEFORE CRYSTALLIZATION, WHICH WAS AT RT USING THE VAPOUR DIFFUSION METHOD AND SITTING DROPS. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH SX-165 / Detector: CCD / Date: Jun 7, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.78→25 Å / Num. obs: 46670 / % possible obs: 100 % / Observed criterion σ(I): -3 / Redundancy: 9.6 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 18 |
Reflection shell | Resolution: 1.78→1.88 Å / Redundancy: 9.6 % / Rmerge(I) obs: 0.42 / Mean I/σ(I) obs: 5.9 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: AN ENSEMBLE OF THREE HOMOLOGY MODELS OF BRADAVIDIN BASED ON PDB ENTRIES 1AVD, 1MK5, AND 2UYW. Resolution: 1.78→28.64 Å / Cor.coef. Fo:Fc: 0.966 / Cor.coef. Fo:Fc free: 0.951 / SU B: 3.123 / SU ML: 0.046 / Cross valid method: THROUGHOUT / ESU R: 0.114 / ESU R Free: 0.109 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 18.011 Å2
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Refinement step | Cycle: LAST / Resolution: 1.78→28.64 Å
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