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- PDB-1o0x: Crystal structure of Methionine aminopeptidase (TM1478) from Ther... -
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Basic information
Entry | Database: PDB / ID: 1o0x | ||||||
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Title | Crystal structure of Methionine aminopeptidase (TM1478) from Thermotoga maritima at 1.90 A resolution | ||||||
![]() | Methionine aminopeptidase | ||||||
![]() | HYDROLASE / TM1478 / Methionine aminopeptidase / STRUCTURAL GENOMICS / JCSG / PSI / Protein Structure Initiative / Joint Center for Structural Genomics | ||||||
Function / homology | ![]() : / methionyl aminopeptidase / metalloaminopeptidase activity / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Joint Center for Structural Genomics (JCSG) | ||||||
![]() | ![]() Title: Crystal structure of a methionine aminopeptidase (TM1478) from Thermotoga maritima at 1.9 A resolution. Authors: Spraggon, G. / Schwarzenbacher, R. / Kreusch, A. / McMullan, D. / Brinen, L.S. / Canaves, J.M. / Dai, X. / Deacon, A.M. / Elsliger, M.A. / Eshagi, S. / Floyd, R. / Godzik, A. / Grittini, C. ...Authors: Spraggon, G. / Schwarzenbacher, R. / Kreusch, A. / McMullan, D. / Brinen, L.S. / Canaves, J.M. / Dai, X. / Deacon, A.M. / Elsliger, M.A. / Eshagi, S. / Floyd, R. / Godzik, A. / Grittini, C. / Grzechnik, S.K. / Jaroszewski, L. / Karlak, C. / Klock, H.E. / Koesema, E. / Kovarik, J.S. / Kuhn, P. / McPhillips, T.M. / Miller, M.D. / Morse, A. / Moy, K. / Ouyang, J. / Page, R. / Quijano, K. / Rezezadeh, F. / Robb, A. / Sims, E. / Stevens, R.C. / van den Bedem, H. / Velasquez, J. / Vincent, J. / von Delft, F. / Wang, X. / West, B. / Wolf, G. / Xu, Q. / Hodgson, K.O. / Wooley, J. / Lesley, S.A. / Wilson, I.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 | ![]() | 67 KB | Display | ![]() |
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PDB format | ![]() | 47.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 426.3 KB | Display | ![]() |
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Full document | ![]() | 432 KB | Display | |
Data in XML | ![]() | 13.6 KB | Display | |
Data in CIF | ![]() | 19.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1matS S: Starting model for refinement |
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Similar structure data | |
Other databases |
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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: 28991.502 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.47 Å3/Da / Density % sol: 50.14 % | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / pH: 5.6 Details: 19% iso-propanol, 19% P4K, 0.095 M Na-citrate pH 5.6, 5% glycerol, VAPOR DIFFUSION,SITTING DROP,NANODROP, temperature 293K, pH 5.60 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.9 / Method: vapor diffusion | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: ADSC QUANTUM 4 / Detector: CCD / Date: May 29, 2001 |
Radiation | Monochromator: ASYMMETRICALLY CUT SI CRYSTAL, CYLINDRICALLY BENT Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→50 Å / Num. obs: 21470 / % possible obs: 90.6 % / Biso Wilson estimate: 53 Å2 / Rsym value: 0.07 / Net I/σ(I): 16.53 |
Reflection shell | Resolution: 1.9→1.97 Å / Mean I/σ(I) obs: 2.95 / % possible all: 90 |
Reflection | *PLUS Highest resolution: 1.9 Å / Lowest resolution: 50 Å / Num. measured all: 102128 / Rmerge(I) obs: 0.07 |
Reflection shell | *PLUS % possible obs: 90 % / Rmerge(I) obs: 0.614 / Mean I/σ(I) obs: 3 |
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Processing
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT WITH PROGRAM AMORE Starting model: 1MAT Resolution: 1.9→47.53 Å / Isotropic thermal model: ANISOTROPIC / Cross valid method: FREE R / σ(F): 0 Stereochemistry target values: STANDARD CNS DICTIONARY/ENGH AND HUBER Details: ASN 77 IS IN DISALLOWED REGION OF RAMACHANDRAN. THIS IS NOT PART OF THE ACTIVE SITE BUT IS A CONSERVED FEATURE OF ALL METHIONINE AMINO PEPTIDASES. A DIMETAL BINDING SITE LOCATED AT THE ...Details: ASN 77 IS IN DISALLOWED REGION OF RAMACHANDRAN. THIS IS NOT PART OF THE ACTIVE SITE BUT IS A CONSERVED FEATURE OF ALL METHIONINE AMINO PEPTIDASES. A DIMETAL BINDING SITE LOCATED AT THE ACTIVE SITE OF THE MOLECULE DOES NOT HAVE ANY METALS BOUND. HIS 174 HAS A CLEARLY DEFINED DOUBLE CONFORMATION.
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Solvent computation | Solvent model: BULK SOLVENT CORRECTION / Bsol: 0.4 Å2 / ksol: 76.77 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 44.2 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.9→47.53 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.9→1.93 Å / Total num. of bins used: 21
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Software | *PLUS Version: 1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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