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Open data
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Basic information
Entry | Database: PDB / ID: 1gl9 | ||||||
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Title | Archaeoglobus fulgidus reverse gyrase complexed with ADPNP | ||||||
![]() | REVERSE GYRASE | ||||||
![]() | TOPOISOMERASE / DNA SUPERCOILING / ARCHAEA / HELICASE | ||||||
Function / homology | ![]() Isomerases; Isomerases altering macromolecular conformation; Enzymes altering nucleic acid conformation / reverse gyrase activity / DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity / DNA unwinding involved in DNA replication / DNA topological change / ATP hydrolysis activity / DNA binding / zinc ion binding / ATP binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Rodriguez, A.C. / Stock, D. | ||||||
![]() | ![]() Title: Crystal Structure of Reverse Gyrase: Insights Into the Positive Supercoiling of DNA. Authors: Rodriguez, A.C. / Stock, D. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 419.6 KB | Display | ![]() |
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PDB format | ![]() | 335.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1 MB | Display | ![]() |
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Full document | ![]() | 1.2 MB | Display | |
Data in XML | ![]() | 90.6 KB | Display | |
Data in CIF | ![]() | 119.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1gkuSC 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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1 | ![]()
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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.98909, -0.06165, -0.13379), Vector: |
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Components
#1: Protein | Mass: 121535.023 Da / Num. of mol.: 2 / Mutation: YES Source method: isolated from a genetically manipulated source Details: ADENYLYLIMIDODIPHOSPHATE (ADPNP) / Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | #3: Chemical | Compound details | CHAIN B ENGINEERED MUTATION PRO719LEU, LEU1046MET. RESIDUES N-TERMINAL TO B31 IN MOLECULE B, AND TO ...CHAIN B ENGINEERED | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.44 Å3/Da / Density % sol: 58.7 % | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6 Details: 15% PEG 1000, 15% ETHYLENE GLYCOL 100 MM CACODYLATE (PH 6),2MM ADPNP | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 18 ℃ / pH: 8 / Method: vapor diffusion, sitting 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: ADSC / Date: Feb 15, 2001 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9686 Å / Relative weight: 1 |
Reflection | Resolution: 3.2→34 Å / Num. obs: 38400 / % possible obs: 96.7 % / Redundancy: 3.3 % / Biso Wilson estimate: 81 Å2 / Rsym value: 0.102 / Net I/σ(I): 5.2 |
Reflection shell | Resolution: 3.2→3.35 Å / Redundancy: 2.9 % / Mean I/σ(I) obs: 2.3 / Rsym value: 0.321 / % possible all: 96.7 |
Reflection | *PLUS Lowest resolution: 34 Å / Num. obs: 38401 / Rmerge(I) obs: 0.102 |
Reflection shell | *PLUS % possible obs: 96.7 % / Rmerge(I) obs: 0.321 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1GKU Resolution: 3.2→34 Å / Data cutoff high absF: 10000 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: MLF Details: RESIDUES N-TERMINAL TO B31 IN MOLECULE B, AND TO RESIDUE C32 IN MOLECULE C HAVE BEEN MODELLED AS POLYALANINE. THEIR IDENTITY AND NUMBERING IN THE PROTEIN SEQUENCE IS ARBITRARY.
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Solvent computation | Bsol: 59.5563 Å2 / ksol: 0.285991 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 75.6 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 3.2→34 Å
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Refine LS restraints |
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Refine LS restraints NCS | Weight Biso : 10 / Weight position: 15 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 3.2→3.31 Å / Total num. of bins used: 10
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Xplor file |
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Software | *PLUS Name: CNS / Version: 1.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 34 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |