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Open data
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Basic information
Entry | Database: PDB / ID: 1swf | ||||||
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Title | CIRCULAR PERMUTED STREPTAVIDIN E51/A46 | ||||||
![]() | 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 | ![]() | 103.3 KB | Display | ![]() |
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PDB format | ![]() | 79.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 441.4 KB | Display | ![]() |
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Full document | ![]() | 447.3 KB | Display | |
Data in XML | ![]() | 21 KB | Display | |
Data in CIF | ![]() | 29.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1swgC ![]() 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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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: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2 Å3/Da / Density % sol: 40.79 % | |||||||||||||||
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Crystal grow | pH: 4.5 / Details: PROTEIN 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: 295 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS II / Detector: IMAGE PLATE / Date: Jun 24, 1996 / Details: MSC MIRRORS |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→50 Å / Num. obs: 28795 / % possible obs: 94 % / Rmerge(I) obs: 0.069 / Net I/σ(I): 5 |
Reflection shell | Resolution: 2→2.1 Å / Rmerge(I) obs: 0.38 / Mean I/σ(I) obs: 2 / % possible all: 82 |
Reflection | *PLUS Num. measured all: 93577 |
Reflection shell | *PLUS % possible obs: 82.1 % |
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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: 2→10 Å / Num. parameters: 15175 / Num. restraintsaints: 15088 / 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: 2→10 Å
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Refine LS restraints |
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Software | *PLUS Name: SHELXL-96 / Classification: refinement | |||||||||||||||||||||||||||||||||
Refinement | *PLUS σ(I): 2 / Rfactor Rwork: 0.19 | |||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 29 Å2 |