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- PDB-4blm: BETA-LACTAMASE OF BACILLUS LICHENIFORMIS 749(SLASH)C. REFINEMENT ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4blm | ||||||
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Title | BETA-LACTAMASE OF BACILLUS LICHENIFORMIS 749(SLASH)C. REFINEMENT AT 2 ANGSTROMS RESOLUTION AND ANALYSIS OF HYDRATION | ||||||
![]() | BETA-LACTAMASE | ||||||
![]() | HYDROLASE(ACTING IN CYCLIC AMIDES) | ||||||
Function / homology | ![]() beta-lactam antibiotic catabolic process / beta-lactamase activity / beta-lactamase / response to antibiotic / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Knox, J.R. / Moews, P.C. | ||||||
![]() | ![]() Title: Beta-lactamase of Bacillus licheniformis 749/C. Refinement at 2 A resolution and analysis of hydration. Authors: Knox, J.R. / Moews, P.C. #1: ![]() Title: Beta-Lactamase of Bacillus Licheniformis 749(Slash)C at 2 Angstroms Resolution Authors: Moews, P.C. / Knox, J.R. / Dideberg, O. / Charlier, P. / Frere, J.-M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 121.9 KB | Display | ![]() |
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PDB format | ![]() | 94.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 441.6 KB | Display | ![]() |
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Full document | ![]() | 464.2 KB | Display | |
Data in XML | ![]() | 29.1 KB | Display | |
Data in CIF | ![]() | 41.6 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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1 | ![]()
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2 | ![]()
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Unit cell |
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Atom site foot note | 1: RESIDUES PRO A 167 AND PRO B 167 ARE CIS PROLINES. | ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.8708, 0.00104, 0.49164), Vector: |
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Components
#1: Protein | Mass: 29542.436 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | Sequence details | RESIDUE NUMBERING IS BASED ON R.P.AMBLER ET AL. (BIOCHEM. J., V. 276, P. 269, 1991). THEREFORE, ...RESIDUE NUMBERING IS BASED ON R.P.AMBLER ET AL. (BIOCHEM. J., V. 276, P. 269, 1991). THEREFORE, THERE ARE NO RESIDUES NUMBERED 58, 84, 85, 239, AND 253. | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.16 Å3/Da / Density % sol: 43.15 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 20 ℃ / pH: 6.8 / Method: vapor diffusion, hanging drop / Details: Kelly, J. A., (1985) J. Biol. Chem., 260, 6449. | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Num. all: 30090 / % possible obs: 94 % |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 2→10 Å / σ(F): 3 /
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Refinement step | Cycle: LAST / Resolution: 2→10 Å
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Refine LS restraints |
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Software | *PLUS Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.161 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |