+Open data
-Basic information
Entry | Database: PDB / ID: 2wlw | ||||||
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Title | Structure of the N-terminal capsid domain of HIV-2 | ||||||
Components | PEPTIDYL-PROLYL CIS-TRANS ISOMERASEProlyl isomerase | ||||||
Keywords | ISOMERASE / ROTAMASE / RHESUS MACAQUE TRIM-CYP | ||||||
Function / homology | Function and homology information negative regulation of protein K48-linked ubiquitination / regulation of apoptotic signaling pathway / cell adhesion molecule production / heparan sulfate binding / regulation of viral genome replication / leukocyte chemotaxis / negative regulation of stress-activated MAPK cascade / endothelial cell activation / cyclosporin A binding / protein peptidyl-prolyl isomerization ...negative regulation of protein K48-linked ubiquitination / regulation of apoptotic signaling pathway / cell adhesion molecule production / heparan sulfate binding / regulation of viral genome replication / leukocyte chemotaxis / negative regulation of stress-activated MAPK cascade / endothelial cell activation / cyclosporin A binding / protein peptidyl-prolyl isomerization / negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / positive regulation of protein dephosphorylation / activation of protein kinase B activity / neutrophil chemotaxis / negative regulation of protein phosphorylation / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / negative regulation of protein kinase activity / platelet aggregation / platelet activation / integrin binding / protein folding / cellular response to oxidative stress / positive regulation of NF-kappaB transcription factor activity / positive regulation of MAPK cascade / positive regulation of protein phosphorylation / apoptotic process / extracellular region / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | MACACA MULATTA (Rhesus monkey) | ||||||
Method | X-RAY DIFFRACTION / OTHER / Resolution: 1.5 Å | ||||||
Authors | Price, A.J. / Marzetta, F. / Lammers, M. / Ylinen, L.M.J. / Schaller, T. / Wilson, S.J. / Towers, G.J. / James, L.C. | ||||||
Citation | Journal: Nat.Struct.Mol.Biol. / Year: 2009 Title: Active Site Remodelling Switches HIV Specificity of Antiretroviral Trimcyp Authors: Price, A.J. / Marzetta, F. / Lammers, M. / Ylinen, L.M.J. / Schaller, T. / Wilson, S.J. / Towers, G.J. / James, L.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2wlw.cif.gz | 84.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2wlw.ent.gz | 64.9 KB | Display | PDB format |
PDBx/mmJSON format | 2wlw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wl/2wlw ftp://data.pdbj.org/pub/pdb/validation_reports/wl/2wlw | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 18016.473 Da / Num. of mol.: 1 / Fragment: CYPA DOMAIN, RESIDUES 46-210 Source method: isolated from a genetically manipulated source Source: (gene. exp.) MACACA MULATTA (Rhesus monkey) / Production host: ESCHERICHIA COLI (E. coli) References: UniProt: B1P761, UniProt: P62940*PLUS, peptidylprolyl isomerase |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 1.61 Å3/Da / Density % sol: 23.18 % / Description: NONE |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Wavelength: 1.5418 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.5→41 Å / Num. obs: 23059 / % possible obs: 96.5 % / Observed criterion σ(I): 2 / Redundancy: 3.6 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 11.2 |
-Processing
Software | Name: REFMAC / Version: 5.5.0088 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Method to determine structure: OTHER Starting model: NONE Resolution: 1.5→88.57 Å / Cor.coef. Fo:Fc: 0.973 / Cor.coef. Fo:Fc free: 0.965 / SU B: 1.322 / SU ML: 0.026 / Cross valid method: THROUGHOUT / σ(F): 2 / ESU R: 0.039 / ESU R Free: 0.04 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL PLUS MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 16.659 Å2
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Refinement step | Cycle: LAST / Resolution: 1.5→88.57 Å
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