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Open data
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Basic information
Entry | Database: PDB / ID: 1swg | ||||||
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Title | CIRCULAR PERMUTED STREPTAVIDIN E51/A46 IN COMPLEX WITH BIOTIN | ||||||
![]() | CIRCULARLY PERMUTED CORE-STREPTAVIDIN E51/A46 | ||||||
![]() | BIOTIN-BINDING PROTEIN / BIOTIN BINDING PROTEIN / CIRCULAR PERMUTATION / BIOTIN | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Freitag, S. / Chu, V. / Le Trong, I. / Stayton, P.S. / Stenkamp, R.E. | ||||||
![]() | ![]() Title: Thermodynamic and structural consequences of flexible loop deletion by circular permutation in the streptavidin-biotin system. Authors: Chu, V. / Freitag, S. / Le Trong, I. / Stenkamp, R.E. / Stayton, P.S. #1: ![]() Title: Thermodynamic Consequences of the Deletion of a Flexible Loop by Circular Permutation in the Streptavidin-Biotin System Authors: Chu, V. / Freitag, S. / Le Trong, I. / Stenkamp, R.E. / Stayton, P.S. #2: ![]() Title: Structural Studies of the Streptavidin Binding Loop Authors: Freitag, S. / Le Trong, I. / Klumb, L. / Stayton, P.S. / Stenkamp, R.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 106.1 KB | Display | ![]() |
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PDB format | ![]() | 82 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 461.7 KB | Display | ![]() |
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Full document | ![]() | 468 KB | Display | |
Data in XML | ![]() | 23.4 KB | Display | |
Data in CIF | ![]() | 32.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1swfC ![]() 1swaS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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3 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 13329.403 Da / Num. of mol.: 4 Mutation: DELETION OF SURFACE LOOP RESIDUES 45 - 50 FROM THE SEQUENCE. THE OLD N- AND C-TERMINI (S139, A13, RESPECTIVELY) ARE CONNECTED INTRODUCING THE FOUR ADDITIONAL RESIDUES GGGS Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | ChemComp-BTN / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 48.87 % | ||||||||||||||||||||
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Crystal grow | pH: 4.5 Details: PROTEIN (12MG/ML, 10MM BIOTIN) WAS CRYSTALLIZED FROM 52% MPD (PH 4.5) | ||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jun 1, 1997 / Details: RH-COATED SILICON MIRROR |
Radiation | Monochromator: SI(111) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 1.75→30 Å / Num. obs: 51393 / % possible obs: 98 % / Observed criterion σ(I): -3 / Redundancy: 4 % / Rmerge(I) obs: 0.031 / Net I/σ(I): 19.9 |
Reflection shell | Resolution: 1.75→1.81 Å / Redundancy: 3 % / Rmerge(I) obs: 0.261 / Mean I/σ(I) obs: 2 / % possible all: 87 |
Reflection | *PLUS % possible obs: 98.2 % / Num. measured all: 417564 / Rmerge(I) obs: 0.03 |
Reflection shell | *PLUS % possible obs: 96.2 % / Rmerge(I) obs: 0.17 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1SWA (EXCLUDING RESIDUES 46 - 51 IN ALL SUBUNITS) Resolution: 1.8→10 Å / Num. parameters: 15527 / Num. restraintsaints: 17457 / Stereochemistry target values: ENGH AND HUBER
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Solvent computation | Solvent model: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201 | |||||||||||||||||||||||||||||||||
Refine analyze | Num. disordered residues: 0 / Occupancy sum hydrogen: 3354 / Occupancy sum non hydrogen: 3790 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→10 Å
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Refine LS restraints |
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Software | *PLUS Name: SHELXL-97 / Classification: refinement | |||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rfree: 0.231 / Rfactor Rwork: 0.181 | |||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 27 Å2 |