+Open data
-Basic information
Entry | Database: PDB / ID: 6n05 | |||||||||
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Title | Structure of anti-crispr protein, AcrIIC2 | |||||||||
Components | AcrIIC2 | |||||||||
Keywords | VIRAL PROTEIN / Prophage protein. Anti-CRISPR | |||||||||
Function / homology | Phage associated protein Function and homology information | |||||||||
Biological species | Neisseria meningitidis (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.5 Å | |||||||||
Authors | Shah, M. / Thavalingham, A. / Maxwell, K.L. / Moraes, T.F. | |||||||||
Funding support | Canada, 2items
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Citation | Journal: Nat Commun / Year: 2019 Title: Inhibition of CRISPR-Cas9 ribonucleoprotein complex assembly by anti-CRISPR AcrIIC2. Authors: Thavalingam, A. / Cheng, Z. / Garcia, B. / Huang, X. / Shah, M. / Sun, W. / Wang, M. / Harrington, L. / Hwang, S. / Hidalgo-Reyes, Y. / Sontheimer, E.J. / Doudna, J. / Davidson, A.R. / ...Authors: Thavalingam, A. / Cheng, Z. / Garcia, B. / Huang, X. / Shah, M. / Sun, W. / Wang, M. / Harrington, L. / Hwang, S. / Hidalgo-Reyes, Y. / Sontheimer, E.J. / Doudna, J. / Davidson, A.R. / Moraes, T.F. / Wang, Y. / Maxwell, K.L. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6n05.cif.gz | 101.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6n05.ent.gz | 81.9 KB | Display | PDB format |
PDBx/mmJSON format | 6n05.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6n05_validation.pdf.gz | 439.3 KB | Display | wwPDB validaton report |
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Full document | 6n05_full_validation.pdf.gz | 444.2 KB | Display | |
Data in XML | 6n05_validation.xml.gz | 10.5 KB | Display | |
Data in CIF | 6n05_validation.cif.gz | 13.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/n0/6n05 ftp://data.pdbj.org/pub/pdb/validation_reports/n0/6n05 | HTTPS FTP |
-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: 18245.176 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Neisseria meningitidis (bacteria) / Gene: COH52_04850 / Plasmid: pHAT4 / Production host: Escherichia coli BL21 (bacteria) / References: UniProt: A0A425B3G2 #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.39 Å3/Da / Density % sol: 48.58 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.5 / Details: 0.1M sodium citrate, 5% propanol and 20% PEG 4000 |
-Data collection
Diffraction | Mean temperature: 105 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: CLSI / Beamline: 08B1-1 / Wavelength: 0.9789 Å |
Detector | Type: RAYONIX MX300HE / Detector: CCD / Date: Jul 19, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9789 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→49.232 Å / Num. obs: 12871 / % possible obs: 99.95 % / Redundancy: 14.1 % / CC1/2: 0.5 / Net I/σ(I): 23.8 |
Reflection shell | Resolution: 2.5→2.589 Å / Mean I/σ(I) obs: 1.45 / Num. unique obs: 1250 / CC1/2: 0.684 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: SAD / Resolution: 2.5→49.232 Å / SU ML: 0.39 / Cross valid method: FREE R-VALUE / σ(F): 1.92 / Phase error: 29.54
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 251 Å2 / Biso min: 39.81 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.5→49.232 Å
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 8
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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