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Yorodumi- PDB-1amu: PHENYLALANINE ACTIVATING DOMAIN OF GRAMICIDIN SYNTHETASE 1 IN A C... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1amu | ||||||
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Title | PHENYLALANINE ACTIVATING DOMAIN OF GRAMICIDIN SYNTHETASE 1 IN A COMPLEX WITH AMP AND PHENYLALANINE | ||||||
Components | GRAMICIDIN SYNTHETASE 1 | ||||||
Keywords | PEPTIDE SYNTHETASE / GRSA / ADENYLATE FORMING | ||||||
Function / homology | Function and homology information phenylalanine racemase (ATP-hydrolysing) / phenylalanine racemase (ATP-hydrolyzing) activity / ligase activity / antibiotic biosynthetic process / ATP binding Similarity search - Function | ||||||
Biological species | Brevibacillus brevis (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MIR / Resolution: 1.9 Å | ||||||
Authors | Conti, E. / Stachelhaus, T. / Marahiel, M.A. / Brick, P. | ||||||
Citation | Journal: EMBO J. / Year: 1997 Title: Structural basis for the activation of phenylalanine in the non-ribosomal biosynthesis of gramicidin S. Authors: Conti, E. / Stachelhaus, T. / Marahiel, M.A. / Brick, P. #1: Journal: J.Biol.Chem. / Year: 1995 Title: Modular Structure of Peptide Synthetases Revealed by Dissection of the Multifunctional Enzyme Grsa Authors: Stachelhaus, T. / Marahiel, M.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1amu.cif.gz | 225.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1amu.ent.gz | 176.7 KB | Display | PDB format |
PDBx/mmJSON format | 1amu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/am/1amu ftp://data.pdbj.org/pub/pdb/validation_reports/am/1amu | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 64131.793 Da / Num. of mol.: 2 Fragment: ADENYLATE FORMING DOMAIN, RESIDUES 1 - 556 PLUS A 7 RESIDUE C-TERMINAL TAG - SHHHHHH Source method: isolated from a genetically manipulated source Source: (gene. exp.) Brevibacillus brevis (bacteria) / Gene: GRSA / Plasmid: PQE60 / Production host: Escherichia coli (E. coli) / Strain (production host): M15(PREP4) References: UniProt: P14687, UniProt: P0C061*PLUS, phenylalanine racemase (ATP-hydrolysing) |
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-Non-polymers , 5 types, 577 molecules
#2: Chemical | #3: Chemical | #4: Chemical | #5: Chemical | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 50 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 291 K / Method: vapor diffusion / pH: 6.5 Details: CRYSTALS WERE GROWN USING THE VAPOR DIFFUSION TECHNIQUE. THE PROTEIN AT 15 MG/ML IN 10 MM TRIS-HCL PH7.8, 50 MM NACL, 15% GLYCEROL, 2 MM ATP, 2 MM L-PHE AND 4 MM MGCL2 WAS EQUILIBRATED WITH ...Details: CRYSTALS WERE GROWN USING THE VAPOR DIFFUSION TECHNIQUE. THE PROTEIN AT 15 MG/ML IN 10 MM TRIS-HCL PH7.8, 50 MM NACL, 15% GLYCEROL, 2 MM ATP, 2 MM L-PHE AND 4 MM MGCL2 WAS EQUILIBRATED WITH AN EQUAL VOLUME OF RESERVOIR SOLUTION CONTAINING 28-32%(W/V) METHOXY POLYETHYLENE GLYCOL 5000, 200 MM AMMONIUM SULFATE, AND 100 MM ADA PH6.5 AT 18C., vapor diffusion, temperature 291K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 18 ℃ / pH: 7.8 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: EMBL/DESY, HAMBURG / Beamline: BW7B / Wavelength: 0.88 |
Detector | Type: MAR scanner 300 mm plate / Detector: IMAGE PLATE / Date: Sep 9, 1996 |
Radiation | Monochromator: Y / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.88 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→20 Å / Num. obs: 91144 / % possible obs: 96.4 % / Redundancy: 2.5 % / Rmerge(I) obs: 0.051 / Net I/σ(I): 7.3 |
Reflection shell | Resolution: 1.9→2 Å / Redundancy: 1.9 % / Rmerge(I) obs: 0.232 / Mean I/σ(I) obs: 2.7 / % possible all: 88.3 |
Reflection | *PLUS Num. measured all: 230285 |
Reflection shell | *PLUS % possible obs: 88.3 % |
-Processing
Software |
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Refinement | Method to determine structure: MIR / Resolution: 1.9→20 Å / Rfactor Rfree error: 0.004 / Data cutoff high absF: 0 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 33 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→20 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: UNRESTRAINED | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 1.9→1.99 Å / Rfactor Rfree error: 0.016 / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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