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- PDB-4ihd: Crystal Structure of Uncleaved ThnT T282C, derivatized at the act... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4ihd | ||||||
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Title | Crystal Structure of Uncleaved ThnT T282C, derivatized at the active site with EtHg | ||||||
![]() | ThnT protein | ||||||
![]() | HYDROLASE / DOM-fold / Clan PE / Family P1 / Autoproteolysis / Pantetheine Hydrolase / Thienamycin Biosynthesis / Ethylmercury derivatization of C282 | ||||||
Function / homology | ![]() aminopeptidase activity / transferase activity / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Buller, A.R. / Schildbach, J.F. / Townsend, C.A. | ||||||
![]() | ![]() Title: Exploring the Role of Conformational Heterogeneity in cis-Autoproteolytic Activation of ThnT. Authors: Buller, A.R. / Freeman, M.F. / Schildbach, J.F. / Townsend, C.A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 275.7 KB | Display | ![]() |
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PDB format | ![]() | 221.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 448.8 KB | Display | ![]() |
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Full document | ![]() | 454.7 KB | Display | |
Data in XML | ![]() | 32.4 KB | Display | |
Data in CIF | ![]() | 49.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4iheC ![]() 3s3uS S: Starting model for refinement C: citing same article ( |
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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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3 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 41374.117 Da / Num. of mol.: 2 / Mutation: T282C Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.16 Å3/Da / Density % sol: 43.12 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 12%PEG3350, 0.5M NaAcetate, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: RAYONIX MX-325 / Detector: CCD / Date: May 30, 2009 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0036 Å / Relative weight: 1 |
Reflection | Resolution: 1.65→50 Å / Num. all: 81725 / Num. obs: 76644 / % possible obs: 94.1 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 6.8 % / Rmerge(I) obs: 0.048 / Net I/σ(I): 34.2 |
Reflection shell | Resolution: 1.65→1.7 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.348 / Mean I/σ(I) obs: 2.2 / Num. unique all: 2138 / % possible all: 54.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 3S3U Resolution: 1.65→35.7 Å / Cor.coef. Fo:Fc: 0.973 / Cor.coef. Fo:Fc free: 0.964 / SU B: 3.298 / SU ML: 0.056 / Cross valid method: THROUGHOUT / ESU R: 0.089 / ESU R Free: 0.087 / 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: 29.617 Å2
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Refinement step | Cycle: LAST / Resolution: 1.65→35.7 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.65→1.693 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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