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- PDB-1gpp: Crystal structure of the S.cerevisiae Homing Endonuclease PI-SceI... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1gpp | ||||||
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Title | Crystal structure of the S.cerevisiae Homing Endonuclease PI-SceI Domain I | ||||||
![]() | ENDONUCLEASE PI-SCEI | ||||||
![]() | ENDONUCLEASE / HOMING / PROTEIN SPLICING | ||||||
Function / homology | ![]() Insulin receptor recycling / Transferrin endocytosis and recycling / ROS and RNS production in phagocytes / Amino acids regulate mTORC1 / Golgi lumen acidification / endosomal lumen acidification / vacuolar proton-transporting V-type ATPase, V1 domain / proton-transporting V-type ATPase complex / protein metabolic process / intein-mediated protein splicing ...Insulin receptor recycling / Transferrin endocytosis and recycling / ROS and RNS production in phagocytes / Amino acids regulate mTORC1 / Golgi lumen acidification / endosomal lumen acidification / vacuolar proton-transporting V-type ATPase, V1 domain / proton-transporting V-type ATPase complex / protein metabolic process / intein-mediated protein splicing / intron homing / fungal-type vacuole membrane / vacuolar proton-transporting V-type ATPase complex / vacuolar acidification / H+-transporting two-sector ATPase / proton transmembrane transport / phagocytic vesicle / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / endonuclease activity / Hydrolases; Acting on ester bonds / Golgi membrane / mRNA binding / DNA binding / ATP binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Werner, E. / Wende, W. / Pingoud, A. / Heinemann, U. | ||||||
![]() | ![]() Title: High Resolution Crystal Structure of Domain I of the Saccharomyces Cerevisiae Homing Endonuclease Pi-Scei Authors: Werner, E. / Wende, W. / Pingoud, A. / Heinemann, U. | ||||||
History |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 7-STRANDED BARREL THIS IS REPRESENTED BY A 8-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 114.8 KB | Display | ![]() |
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PDB format | ![]() | 88.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 428.4 KB | Display | ![]() |
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Full document | ![]() | 431.1 KB | Display | |
Data in XML | ![]() | 14.1 KB | Display | |
Data in CIF | ![]() | 21.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1vdeS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 27034.643 Da / Num. of mol.: 1 Fragment: PROTEIN SPLICING DOMAIN, RESIDUES 284-466,693-736, SEE REMARK 999 Mutation: YES Source method: isolated from a genetically manipulated source Details: GLY183 LINKS ILE182 AND ALA410, WHERE IN THE FULL LENGTH PROTEIN IS DOMAIN II Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() References: UniProt: P17255, H+-transporting two-sector ATPase |
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#2: Water | ChemComp-HOH / |
Compound details | MUTATIONS: ARG327SER, VAL350MET, ILE415VAL, LEU466GLY |
Sequence details | THE PROTEIN PI-SCEI IS AN INTEIN OF THE PRIMARY TRANSLATION PRODUCT OF THE ATP SYNTHASE (SWS ENTRY ...THE PROTEIN PI-SCEI IS AN INTEIN OF THE PRIMARY TRANSLATIO |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.7 Å3/Da / Density % sol: 54 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 4.8 Details: 30 % PEG4000, 0.1 M SODIUM CITRATE PH 5.6, 0.2 M NH4-ACETATE | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 5.6 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: May 15, 2001 / Details: MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8453 Å / Relative weight: 1 |
Reflection | Resolution: 1.35→20 Å / Num. obs: 51602 / % possible obs: 94.1 % / Redundancy: 2.5 % / Rmerge(I) obs: 0.029 / Net I/σ(I): 34.5 |
Reflection shell | Resolution: 1.35→1.37 Å / Redundancy: 1.5 % / Rmerge(I) obs: 0.164 / Mean I/σ(I) obs: 2.5 / % possible all: 64.1 |
Reflection | *PLUS Lowest resolution: 20 Å / Num. measured all: 359618 |
Reflection shell | *PLUS % possible obs: 64.1 % / Num. unique obs: 1141 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1VDE Resolution: 1.35→20 Å / Cor.coef. Fo:Fc: 0.976 / Cor.coef. Fo:Fc free: 0.963 / SU B: 2.249 / SU ML: 0.048 / Cross valid method: THROUGHOUT / ESU R: 0.056 / ESU R Free: 0.055 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. FIRST 8 RESIDUES OF THE HIS-TAG AND RESIDUES 55 - 66 ARE NOT VISIBLE IN ELECTRON DENSITY.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 19.93 Å2
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Refinement step | Cycle: LAST / Resolution: 1.35→20 Å
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Refine LS restraints |
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