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Yorodumi- PDB-1sip: ALTERNATIVE NATIVE FLAP CONFORMATION REVEALED BY 2.3 ANGSTROMS RE... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1sip | ||||||
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Title | ALTERNATIVE NATIVE FLAP CONFORMATION REVEALED BY 2.3 ANGSTROMS RESOLUTION STRUCTURE OF SIV PROTEINASE | ||||||
Components | UNLIGANDED SIV PROTEASE | ||||||
Keywords | HYDROLASE(ACID PROTEINASE) | ||||||
Function / homology | Function and homology information exoribonuclease H activity / DNA integration / viral genome integration into host DNA / establishment of integrated proviral latency / RNA stem-loop binding / RNA-directed DNA polymerase activity / RNA-DNA hybrid ribonuclease activity / DNA recombination / aspartic-type endopeptidase activity / symbiont entry into host cell ...exoribonuclease H activity / DNA integration / viral genome integration into host DNA / establishment of integrated proviral latency / RNA stem-loop binding / RNA-directed DNA polymerase activity / RNA-DNA hybrid ribonuclease activity / DNA recombination / aspartic-type endopeptidase activity / symbiont entry into host cell / proteolysis / DNA binding / zinc ion binding Similarity search - Function | ||||||
Biological species | Simian immunodeficiency virus | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.3 Å | ||||||
Authors | Wilderspin, A.F. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1994 Title: Alternative native flap conformation revealed by 2.3 A resolution structure of SIV proteinase. Authors: Wilderspin, A.F. / Sugrue, R.J. #1: Journal: Protein Expr.Purif. / Year: 1994 Title: Purification of Crystallizable Recombinant Sivmac251-32H Proteinase Authors: Sugrue, R.J. / Almond, N. / Kitchin, P. / Richardson, S.M.H. / Wilderspin, A.F. #2: Journal: J.Mol.Biol. / Year: 1993 Title: Crystallization and Preliminary X-Ray Investigation of Recombinant Simian Immunodeficiency Virus Proteinase Authors: Wilderspin, A.F. / Sugrue, R.J. | ||||||
History |
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Remark 700 | SHEET THE STRANDS IN THE *SHEET* RECORDS CORRESPOND TO THE NOTATION IN *JRNL* AS FOLLOWS. 1=B, 2=C, ...SHEET THE STRANDS IN THE *SHEET* RECORDS CORRESPOND TO THE NOTATION IN *JRNL* AS FOLLOWS. 1=B, 2=C, 3=D', 4=D, 5=C', 6=B', 7=A'. THE DIMER INTERFACE IS COMPOSED OF INTERDIGITATED N- AND C-TERMINAL STRANDS FROM BOTH SUBUNITS FORMING A FOUR-STRANDED ANTI-PARALLEL BETA-SHEET, S2. APPLICATION OF THE TWO-FOLD ROTATION TO RESIDUES 2 - 4 AND 95 - 99 GENERATES RESIDUES 2' - 4' AND 95' - 99', RESPECTIVELY. BECAUSE OF THE LIMITATIONS IMPOSED BY THE PROTEIN DATA BANK FORMAT, IT IS NOT POSSIBLE TO PRESENT THIS SHEET ON *SHEET* RECORDS. INSTEAD THIS SHEET IS SPECIFIED IN THIS REMARK. STRANDS 1 AND 3 ARE FROM THE MOLECULE IN THIS ENTRY, AND ARE TERMED STRAND A AND STRAND T IN *JRNL*; STRANDS 2 AND 4 ARE FROM THE SYMMETRY-RELATED MOLECULE. S2 4 GLN 2 SER 4 0 S2 4 MET 95' PHE 99' -1 S2 4 MET 95 PHE 99 -1 S2 4 GLN 2' SER 4' -1 |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1sip.cif.gz | 31.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1sip.ent.gz | 20.7 KB | Display | PDB format |
PDBx/mmJSON format | 1sip.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1sip_validation.pdf.gz | 367.3 KB | Display | wwPDB validaton report |
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Full document | 1sip_full_validation.pdf.gz | 377.4 KB | Display | |
Data in XML | 1sip_validation.xml.gz | 5.1 KB | Display | |
Data in CIF | 1sip_validation.cif.gz | 6.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/si/1sip ftp://data.pdbj.org/pub/pdb/validation_reports/si/1sip | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 10787.413 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Simian immunodeficiency virus / Genus: Lentivirus / Cell line: S2 / Organ: LEAVES References: UniProt: Q87706, UniProt: Q88016*PLUS, Hydrolases; Acting on peptide bonds (peptidases); Aspartic endopeptidases |
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#2: Water | ChemComp-HOH / |
Sequence details | THERE ARE THREE SEQUENCE VARIATIONS BETWEEN SIVMAC251-32H SHOWN IN SEQRES AND THE DATA BASE ENTRY ...THERE ARE THREE SEQUENCE VARIATIONS |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.23 Å3/Da / Density % sol: 44.87 % | ||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 21 ℃ / pH: 5.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.3 Å / Num. obs: 4457 / % possible obs: 97.7 % / Num. measured all: 25196 / Rmerge(I) obs: 0.075 |
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Reflection shell | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 2.46 Å / % possible obs: 89.8 % |
-Processing
Software |
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Refinement | Resolution: 2.3→8 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 2.3→8 Å
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Refine LS restraints |
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Refinement | *PLUS Num. reflection all: 4457 / Rfactor all: 0.17 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS |