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Yorodumi- PDB-3jql: Crystal Structure of the Complex Formed Between Phospholipase A2 ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3jql | ||||||
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Title | Crystal Structure of the Complex Formed Between Phospholipase A2 and a Hexapeptide Fragment of Amyloid Beta Peptide, Lys-Leu-Val-Phe-Phe-Ala at 1.2 A Resolution | ||||||
Components |
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Keywords | HYDROLASE / PHOSPHOLIPASE A2 / HEXAPEPTIDE / AMYLOID BETA / Disulfide bond / Lipid degradation / Metal-binding / Secreted | ||||||
Function / homology | Function and homology information phospholipase A2 / phospholipase A2 activity / arachidonic acid secretion / phospholipid metabolic process / lipid catabolic process / calcium ion binding / extracellular region Similarity search - Function | ||||||
Biological species | Naja sagittifera (cobra) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.2 Å | ||||||
Authors | Mirza, Z. / Vikram, G. / Singh, N. / Sinha, M. / Sharma, S. / Srinivasan, A. / Kaur, P. / Singh, T.P. | ||||||
Citation | Journal: To be Published Title: Crystal Structure of the Complex Formed Between Phospholipase A2 and a Hexapeptide Fragment of Amyloid Beta Peptide, Lys-Leu-Val-Phe-Phe-Ala at 1.2 A Resolution Authors: Mirza, Z. / Vikram, G. / Singh, N. / Sinha, M. / Sharma, S. / Srinivasan, A. / Kaur, P. / Singh, T.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3jql.cif.gz | 66.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3jql.ent.gz | 48 KB | Display | PDB format |
PDBx/mmJSON format | 3jql.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jq/3jql ftp://data.pdbj.org/pub/pdb/validation_reports/jq/3jql | HTTPS FTP |
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-Related structure data
Related structure data | 1mf4S S: Starting model for refinement |
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Similar 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: 13128.515 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Naja sagittifera (cobra) / References: UniProt: P60045 |
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#2: Protein/peptide | Mass: 724.909 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: Peptide synthesis |
#3: Chemical | ChemComp-CA / |
#4: Water | ChemComp-HOH / |
Sequence details | IN CHAIN A, RESIDUE NUMBER 16 IS SIMPLY SKIPPED. THE AUTHORS BELIEVE THAT THE SEQRES IS CORRECT AND ...IN CHAIN A, RESIDUE NUMBER 16 IS SIMPLY SKIPPED. THE AUTHORS BELIEVE THAT THE SEQRES IS CORRECT AND THESE MUTATIONS ARE PRESENT IN THE DEPOSITED SEQUENCE. |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.04 Å3/Da / Density % sol: 39.83 % |
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Crystal grow | Temperature: 290 K / Method: vapor diffusion, hanging drop / pH: 6 Details: calcium chloride, sodium phosphate, PH6.0, VAPOR DIFFUSION, HANGING DROP, temperature 290K |
-Data collection
Diffraction | Mean temperature: 300 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU300 / Wavelength: 1.5418 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Mar 30, 2009 / Details: MIRROR |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.2→42 Å / Num. all: 34924 / Num. obs: 34924 / % possible obs: 95.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Rsym value: 0.036 / Net I/σ(I): 7.9 |
Reflection shell | Resolution: 1.2→1.22 Å / Mean I/σ(I) obs: 2.5 / Rsym value: 0.122 / % possible all: 94.6 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1MF4 Resolution: 1.2→42 Å / Cor.coef. Fo:Fc: 0.962 / Cor.coef. Fo:Fc free: 0.961 / SU B: 1.294 / SU ML: 0.027 / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R: 0.052 / ESU R Free: 0.047 / 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 / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 23.326 Å2
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Refinement step | Cycle: LAST / Resolution: 1.2→42 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.199→1.23 Å / Total num. of bins used: 20
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