+Open data
-Basic information
Entry | Database: PDB / ID: 1htz | ||||||
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Title | CRYSTAL STRUCTURE OF TEM52 BETA-LACTAMASE | ||||||
Components | BETA-LACTAMASE MUTANT TEM52 | ||||||
Keywords | HYDROLASE / Mutant form of beta-lactamase | ||||||
Function / homology | Function and homology information beta-lactam antibiotic catabolic process / beta-lactamase activity / beta-lactamase / response to antibiotic Similarity search - Function | ||||||
Biological species | Klebsiella pneumoniae (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å | ||||||
Authors | Stevens, R.C. / Orencia, M.C. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 2001 Title: Predicting the emergence of antibiotic resistance by directed evolution and structural analysis. Authors: Orencia, M.C. / Yoon, J.S. / Ness, J.E. / Stemmer, W.P. / Stevens, R.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1htz.cif.gz | 306.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1htz.ent.gz | 252.4 KB | Display | PDB format |
PDBx/mmJSON format | 1htz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1htz_validation.pdf.gz | 396.2 KB | Display | wwPDB validaton report |
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Full document | 1htz_full_validation.pdf.gz | 432.2 KB | Display | |
Data in XML | 1htz_validation.xml.gz | 34.2 KB | Display | |
Data in CIF | 1htz_validation.cif.gz | 54 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ht/1htz ftp://data.pdbj.org/pub/pdb/validation_reports/ht/1htz | HTTPS FTP |
-Related structure data
Related structure data | 1temS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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-Components
#1: Protein | Mass: 28941.998 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Klebsiella pneumoniae (bacteria) / Plasmid: PET30A / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: Q9R435, beta-lactamase #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 3 |
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-Sample preparation
Crystal | Density Matthews: 2.81 Å3/Da / Density % sol: 56.27 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 16% PEG8K, 125 mM MgOAc, 25mM Na citrate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 20K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 5.0.3 / Wavelength: 1 |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Jan 15, 1999 / Details: mirrors |
Radiation | Monochromator: ALS 5.0.2 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→20 Å / Num. all: 73211 / Num. obs: 69960 / % possible obs: 91 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 10 % / Biso Wilson estimate: 43.5 Å2 / Rmerge(I) obs: 0.115 / Net I/σ(I): 22.4 |
Reflection shell | Resolution: 2.4→2.5 Å / Redundancy: 6 % / Rmerge(I) obs: 0.432 / Mean I/σ(I) obs: 7.1 / % possible all: 80 |
Reflection | *PLUS Num. measured all: 736906 |
Reflection shell | *PLUS % possible obs: 80 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1TEM Resolution: 2.4→20 Å / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 2 / σ(I): 2 / Stereochemistry target values: Engh & Huber Details: 5 of 6 molecules refined using NCS, 6th molecule different due to packing. Pseudo-6 fold symmetry, attempts to process data as hexagonal or rhombohedral were unsuccessful
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Displacement parameters | Biso mean: 51 Å2 | |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→20 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Version: 0.9 / Classification: refinement | |||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: c_bond_d / Dev ideal: 0.006 |