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Open data
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Basic information
Entry | Database: PDB / ID: 6s1w | ||||||
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Title | Crystal structure of dimeric M-PMV protease D26N mutant | ||||||
![]() | Gag-Pro-Pol polyprotein | ||||||
![]() | HYDROLASE / Mason-Pfizer Monkey Virus / M-PMV / retrovirus / retropepsin / aspartic protease / dimerization / flap structure / apo | ||||||
Function / homology | ![]() dUTP diphosphatase / dUTP diphosphatase activity / Hydrolases; Acting on peptide bonds (peptidases); Aspartic endopeptidases / ribonuclease H / 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 ...dUTP diphosphatase / dUTP diphosphatase activity / Hydrolases; Acting on peptide bonds (peptidases); Aspartic endopeptidases / ribonuclease H / 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 / structural constituent of virion / 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 | ![]() ![]() ![]() | ||||||
![]() | Wosicki, S. / Gilski, M. / Jaskolski, M. / Zabranska, H. / Pichova, I. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Comparison of a retroviral protease in monomeric and dimeric states. Authors: Wosicki, S. / Gilski, M. / Zabranska, H. / Pichova, I. / Jaskolski, M. #1: ![]() Title: Crystal structure of a monomeric retroviral protease solved by protein folding game players. Authors: Khatib, F. / DiMaio, F. / Cooper, S. / Kazmierczyk, M. / Gilski, M. / Krzywda, S. / Zabranska, H. / Pichova, I. / Thompson, J. / Popovic, Z. / Jaskolski, M. / Baker, D. #2: Journal: Acta Crystallogr.,Sect.D / Year: 2011 Title: High-resolution structure of a retroviral protease folded as a monomer. Authors: Gilski, M. / Kazmierczyk, M. / Krzywda, S. / Zabranska, H. / Cooper, S. / Popovic, Z. / Khatib, F. / DiMaio, F. / Thompson, J. / Baker, D. / Pichova, I. / Jaskolski, M. #3: Journal: Nature / Year: 1989 Title: Crystal structure of a retroviral protease proves relationship to aspartic protease family. Authors: Miller, M. / Jaskolski, M. / Rao, J.K. / Leis, J. / Wlodawer, A. #4: ![]() Title: Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease. Authors: Wlodawer, A. / Miller, M. / Jaskolski, M. / Sathyanarayana, B.K. / Baldwin, E. / Weber, I.T. / Selk, L.M. / Clawson, L. / Schneider, J. / Kent, S.B. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 102.3 KB | Display | ![]() |
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PDB format | ![]() | 78.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 428.4 KB | Display | ![]() |
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Full document | ![]() | 429.6 KB | Display | |
Data in XML | ![]() | 11 KB | Display | |
Data in CIF | ![]() | 14.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6s1uSC ![]() 6s1vC S: Starting model for refinement C: citing same article ( |
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Similar structure data | |
Experimental dataset #1 | Data reference: ![]() |
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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 domain:
NCS domain segments: Component-ID: _ / Ens-ID: 1 / Beg auth comp-ID: TRP / Beg label comp-ID: TRP / End auth comp-ID: PRO / End label comp-ID: PRO / Refine code: _ / Auth seq-ID: 1 - 108 / Label seq-ID: 1 - 108
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Components
#1: Protein | Mass: 12963.964 Da / Num. of mol.: 2 / Mutation: D26N; ENGINEERED MUTATION Source method: isolated from a genetically manipulated source Details: Gaps in the sequence indicate residues that were not modeled because of poor electron density. Source: (gene. exp.) ![]() Production host: ![]() ![]() References: UniProt: P07572, dUTP diphosphatase, Hydrolases; Acting on peptide bonds (peptidases); Aspartic endopeptidases, RNA-directed DNA polymerase, DNA-directed DNA polymerase, ribonuclease H, ...References: UniProt: P07572, dUTP diphosphatase, Hydrolases; Acting on peptide bonds (peptidases); Aspartic endopeptidases, RNA-directed DNA polymerase, DNA-directed DNA polymerase, ribonuclease H, Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases, Hydrolases; Acting on ester bonds #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.37 Å3/Da / Density % sol: 48.17 % / Description: plate |
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Crystal grow | Temperature: 292 K / Method: vapor diffusion, hanging drop / pH: 5.6 Details: Protein solution: 4.1 mg/mL protein, 5 mM TCEP, 10 mM Tris buffer pH 7.4; Reservoir solution: 0.1 M sodium citrate buffer, 15% propan-2-ol, 5 mM TCEP; |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Mar 28, 2013 |
Radiation | Monochromator: Double Crystal Monochromator, Si-111 crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.91841 Å / Relative weight: 1 |
Reflection | Resolution: 1.98→48.91 Å / Num. obs: 17123 / % possible obs: 98.9 % / Redundancy: 3.62 % / Biso Wilson estimate: 25 Å2 / CC1/2: 0.997 / Rmerge(I) obs: 0.119 / Rrim(I) all: 0.139 / Net I/σ(I): 8.24 |
Reflection shell | Resolution: 1.98→2.1 Å / Redundancy: 3.4 % / Rmerge(I) obs: 0.627 / Mean I/σ(I) obs: 2.03 / Num. unique obs: 2594 / CC1/2: 0.521 / Rrim(I) all: 0.737 / % possible all: 94.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 6S1U, chain A Resolution: 1.98→48.8 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.911 / SU B: 13.585 / SU ML: 0.169 / Cross valid method: FREE R-VALUE / ESU R: 0.183 / ESU R Free: 0.178 / Details: HYDROGEN ATOMS WERE ADDED AT RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 34.024 Å2
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Refinement step | Cycle: LAST / Resolution: 1.98→48.8 Å
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Refine LS restraints |
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