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- PDB-1qae: THE ACTIVE SITE OF SERRATIA ENDONUCLEASE CONTAINS A CONSERVED MAG... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1qae | ||||||
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Title | THE ACTIVE SITE OF SERRATIA ENDONUCLEASE CONTAINS A CONSERVED MAGNESIUM-WATER CLUSTER | ||||||
![]() | PROTEIN (EXTRACELLULAR ENDONUCLEASE) | ||||||
![]() | ENDONUCLEASE / NUCLEASE / DNASE / RNASE / SUGAR-NONSPECIFIC NUCLEASE / MAGNESIUM | ||||||
Function / homology | ![]() Serratia marcescens nuclease / single-stranded DNA endodeoxyribonuclease activity / RNA endonuclease activity / nucleic acid binding / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Miller, M.D. / Krause, K.L. | ||||||
![]() | ![]() Title: The active site of Serratia endonuclease contains a conserved magnesium-water cluster. Authors: Miller, M.D. / Cai, J. / Krause, K.L. #1: ![]() Title: Identification of the Serratia Endonuclease Dimer: Structural Basis and Implications for Catalysis Authors: Miller, M.D. / Krause, K.L. #2: ![]() Title: 2.1 Angstroms Structure of Serratia Endonuclease Suggests a Mechanism for Binding to Double-Stranded DNA Authors: Miller, M.D. / Tanner, J. / Alpaugh, M. / Benedik, M.J. / Krause, K.L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 108.2 KB | Display | ![]() |
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PDB format | ![]() | 83.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 371.5 KB | Display | ![]() |
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Full document | ![]() | 374.9 KB | Display | |
Data in XML | ![]() | 10.5 KB | Display | |
Data in CIF | ![]() | 16.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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Noncrystallographic symmetry (NCS) | NCS domain:
NCS oper: (Code: given Matrix: (-0.999819, -0.018722, -0.003478), Vector: Details | MTRIX THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE VARIOUS DOMAINS IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND. APPLIED TO TRANSFORMED TO MTRIX RESIDUES RESIDUES RMSD M1 A 5 .. A 245 B 5 .. B 245 0.131 | |
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Components
#1: Protein | Mass: 26738.896 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Plasmid details: PLASMID WHICH ENCODES THE GENE AND CARRIES AN OPERATOR CONSTITUTIVE MUTATION Plasmid: PUC19NUC4OC / Gene (production host): NUCA / Production host: ![]() #2: Chemical | #3: Water | ChemComp-HOH / | Sequence details | REFERENCE DATABASE: GENBANK ENTRY_NAME: SMANUCES | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.57 Å3/Da / Density % sol: 52 % | ||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 8.2 Details: CRYSTALLIZATION METHOD: VAPOR DIFFUSION SITTING DROP CRYSTALLIZATION TEMPERATURE: 277 K CRYSTALLIZATION PH: 4.6 CRYSTALS WERE GROWN FROM PEG 3350, AMMONIUM SULFATE, SODIUM ACETATE, AND ...Details: CRYSTALLIZATION METHOD: VAPOR DIFFUSION SITTING DROP CRYSTALLIZATION TEMPERATURE: 277 K CRYSTALLIZATION PH: 4.6 CRYSTALS WERE GROWN FROM PEG 3350, AMMONIUM SULFATE, SODIUM ACETATE, AND STORED IN A STABILIZATION SOLUTION CONTAINING 20% PEG 3000, 400mM GLYCINE, 40mM TRIS, PH8.2 (293 K), 20% PEG 3000, 10% PEG 400. THIS SOLUTION WAS EXCHANGED THREE TIMES TO MINIMIZE CARRY OVER FROM THE STORAGE SOLUTION. AFTER 3 DAYS IN THE MAGNESIUM STABILIZATION SOLUTION, THE CRYSTAL OF DIMENSION 0.4 X 0.4 X 0.3 MM**2 WAS MOUNTED IN A SILICONIZED SPECIAL GLASS CAPILLARY. , VAPOR DIFFUSION, SITTING DROP | ||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / pH: 4.6 / Method: other | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 288 K |
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Diffraction source | Source: ![]() |
Detector | Type: ENRAF-NONIUS FAST / Detector: DIFFRACTOMETER / Date: Feb 2, 1998 |
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: 2.05→45 Å / Num. obs: 30574 / % possible obs: 84.3 % / Observed criterion σ(I): 0 / Redundancy: 3.1 % / Biso Wilson estimate: 6.6 Å2 / Rmerge(I) obs: 0.025 / Net I/σ(I): 40.87 |
Reflection shell | Resolution: 2.05→2.1 Å / Redundancy: 1.6 % / Rmerge(I) obs: 0.045 / Mean I/σ(I) obs: 18.9 / % possible all: 20.4 |
Reflection | *PLUS Num. measured all: 93785 |
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Processing
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Refinement | Starting model: 1.4 ANGSTROM STRUCTURE OF THE SERRATIAL ENDONUCLEASE (CAI, MILLER AND KRAUSE) WITH WATER AND ALTERNATE SIDE CHAIN CONFORMERS REMOVED AND THE SIDE CHAINS FOR THE ACTIVE SITE RESIDUES ...Starting model: 1.4 ANGSTROM STRUCTURE OF THE SERRATIAL ENDONUCLEASE (CAI, MILLER AND KRAUSE) WITH WATER AND ALTERNATE SIDE CHAIN CONFORMERS REMOVED AND THE SIDE CHAINS FOR THE ACTIVE SITE RESIDUES ARG 57, HIS 89, ASN 199 AND GLU 127 OMITTED Resolution: 2.05→50 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 10000000 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 2 Details: BULK SOLVENT MODEL USED, NCS B-FACTORS RESTRAINTS WERE APPLIED TO PROTEIN ATOMS AND PAIRS OF WATER MOLECULES WHICH DEVIATED LESS THAN 1.0 ANGSTROMS FROM NCS. THE PROTEIN ATOMS ARE IN GROUP 1 ...Details: BULK SOLVENT MODEL USED, NCS B-FACTORS RESTRAINTS WERE APPLIED TO PROTEIN ATOMS AND PAIRS OF WATER MOLECULES WHICH DEVIATED LESS THAN 1.0 ANGSTROMS FROM NCS. THE PROTEIN ATOMS ARE IN GROUP 1 AND THE WATER IS IN GROUP 2. WATER HOH 1 SITS ON THE NON-CRYSTALLOGRAPHIC 2-FOLD AXIS AND IT IS ITS OWN NCS MATE. THE WATER PAIRS IN GROUP 2 BEGIN WITH (HOH 2,HOH 3) AND END WITH (HOH 188, HOH 189). WATERS HOH 190 TO HOH 241 DO NOT HAVE NCS MATES WITHIN 1.0 ANGSTROMS. CRYST1 THERE IS STRONG PSEUDO-CENTERING ARISING FROM THE NON-CRYSTALLOGRAPHIC SYMMETRY. SHIFTING ONE MONOMER BY ONLY 1.4 ANGSTROMS WITH A 1 DEGREE ROTATION WOULD CHANGE THE SPACE GROUP TO I 2 2 2.
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Displacement parameters | Biso mean: 14.8 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.05→50 Å
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Refine LS restraints |
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Refine LS restraints NCS |
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LS refinement shell | Resolution: 2.05→2.18 Å / Rfactor Rfree error: 0.019 / Total num. of bins used: 6
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Xplor file |
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Software | *PLUS Name: X-PLOR(ONLINE) / Version: 3.851 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.167 / Rfactor Rfree: 0.21 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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