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Open data
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Basic information
Entry | Database: PDB / ID: 1vsk | ||||||
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Title | ASV INTEGRASE CORE DOMAIN D64N MUTATION IN CITRATE BUFFER PH 6.0 | ||||||
![]() | INTEGRASE | ||||||
![]() | HYDROLASE / ENDONUCLEASE / TRANSFERASE | ||||||
Function / homology | ![]() Hydrolases; Acting on peptide bonds (peptidases); Aspartic endopeptidases / ribonuclease H / virion component / DNA integration / viral genome integration into host DNA / RNA-directed DNA polymerase / establishment of integrated proviral latency / RNA stem-loop binding / RNA-directed DNA polymerase activity / RNA-DNA hybrid ribonuclease activity ...Hydrolases; Acting on peptide bonds (peptidases); Aspartic endopeptidases / ribonuclease H / virion component / DNA integration / viral genome integration into host DNA / RNA-directed DNA polymerase / establishment of integrated proviral latency / RNA stem-loop binding / RNA-directed DNA polymerase activity / RNA-DNA hybrid ribonuclease activity / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / viral nucleocapsid / DNA recombination / DNA-directed DNA polymerase / Hydrolases; Acting on ester bonds / aspartic-type endopeptidase activity / DNA-directed DNA polymerase activity / symbiont entry into host cell / proteolysis / DNA binding / zinc ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Lubkowski, J. / Yang, F. / Alexandratos, J. / Wlodawer, A. | ||||||
![]() | ![]() Title: Structural basis for inactivating mutations and pH-dependent activity of avian sarcoma virus integrase. Authors: Lubkowski, J. / Yang, F. / Alexandratos, J. / Merkel, G. / Katz, R.A. / Gravuer, K. / Skalka, A.M. / Wlodawer, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 42.8 KB | Display | ![]() |
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PDB format | ![]() | 29.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 422 KB | Display | ![]() |
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Full document | ![]() | 425.6 KB | Display | |
Data in XML | ![]() | 9 KB | Display | |
Data in CIF | ![]() | 12 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1vslC ![]() 1vsmC ![]() 1asvS 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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Unit cell |
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Details | THE BIOLOGICAL UNIT IS NOT YET KNOWN. THE MINIMUM MULTIMER IS BELIEVED TO CONTAIN AT LEAST THIS DIMER, SHOWN IN BOTH HIV-1 AND ASV INTEGRASE CORE DOMAIN STRUCTURES. |
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Components
#1: Protein | Mass: 15998.403 Da / Num. of mol.: 1 / Fragment: CATALYTIC CORE DOMAIN / Mutation: D64N Source method: isolated from a genetically manipulated source Details: P03354 FRAGMENT OF POLYPROTEIN POL-RSVP / Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P03354, UniProt: O92956*PLUS, RNA-directed DNA polymerase |
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#2: Water | ChemComp-HOH / |
Sequence details | THE APPARENT DISCREPANCY BETWEEN THE SEQUENCE PRESENTED HERE AND THE "POL_RSVP" SEQUENCE IS A ...THE APPARENT DISCREPANC |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.52 Å3/Da / Density % sol: 38 % | |||||||||||||||||||||||||
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Crystal grow | pH: 5.6 Details: 20% PEG 4000, 10% ISOPROPANOL, 0.1M NA CITRATE PH 5.6 | |||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.5 / Method: vapor diffusion, hanging drop / Details: Bujacz, G., (1995) J. Mol. Biol., 253, 333. | |||||||||||||||||||||||||
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: MAC Science DIP-2000 / Detector: IMAGE PLATE / Date: Oct 31, 1997 / Details: MIRRORS |
Radiation | Monochromator: DOUBLE CRYSTAL SI(111) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.15→20 Å / Num. obs: 10132 / % possible obs: 97 % / Observed criterion σ(I): -3 / Redundancy: 8.4 % / Rsym value: 0.077 / Net I/σ(I): 20.7 |
Reflection shell | Resolution: 2.15→2.21 Å / Mean I/σ(I) obs: 3.6 / Rsym value: 0.415 / % possible all: 96.5 |
Reflection | *PLUS Num. measured all: 85055 / Rmerge(I) obs: 0.077 |
Reflection shell | *PLUS % possible obs: 96.5 % / Rmerge(I) obs: 0.415 |
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Processing
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Refinement | Starting model: PDB ENTRY 1ASV Resolution: 2.2→8 Å / Data cutoff high absF: 100000 / Data cutoff low absF: 0.1 / Cross valid method: FREE R / σ(F): 2 Details: ATOMIC OCCUPANCIES OF DISORDERED ATOMS ARE SET TO ZERO IN COORDINATES
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Displacement parameters | Biso mean: 34.8 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati d res low obs: 0 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→8 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.2→2.3 Å / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor obs: 0.221 |