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Yorodumi- PDB-1nsj: CRYSTAL STRUCTURE OF PHOSPHORIBOSYL ANTHRANILATE ISOMERASE FROM T... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1nsj | ||||||
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Title | CRYSTAL STRUCTURE OF PHOSPHORIBOSYL ANTHRANILATE ISOMERASE FROM THERMOTOGA MARITIMA | ||||||
Components | PHOSPHORIBOSYL ANTHRANILATE ISOMERASE | ||||||
Keywords | ISOMERASE / PHOSPHORIBOSYL ANTHRANILATE ISOMERASE / THERMOSTABILITY | ||||||
Function / homology | Function and homology information phosphoribosylanthranilate isomerase / phosphoribosylanthranilate isomerase activity / tryptophan biosynthetic process Similarity search - Function | ||||||
Biological species | Thermotoga maritima (bacteria) | ||||||
Method | X-RAY DIFFRACTION / MIR / Resolution: 2 Å | ||||||
Authors | Hennig, M. / Jansonius, J.N.J. | ||||||
Citation | Journal: Biochemistry / Year: 1997 Title: Crystal structure at 2.0 A resolution of phosphoribosyl anthranilate isomerase from the hyperthermophile Thermotoga maritima: possible determinants of protein stability. Authors: Hennig, M. / Sterner, R. / Kirschner, K. / Jansonius, J.N. #1: Journal: Protein Sci. / Year: 1996 Title: Phosphoribosyl Anthranilate Isomerase from Thermotoga Maritima is an Extremely Stable and Active Homodimer Authors: Sterner, R. / Kleemann, G.R. / Szadkowski, H. / Lustig, A. / Hennig, M. / Kirschner, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1nsj.cif.gz | 54.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1nsj.ent.gz | 40 KB | Display | PDB format |
PDBx/mmJSON format | 1nsj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ns/1nsj ftp://data.pdbj.org/pub/pdb/validation_reports/ns/1nsj | 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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Unit cell |
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-Components
#1: Protein | Mass: 23070.549 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermotoga maritima (bacteria) / Gene: TRPF / Plasmid: PQE-60 / Gene (production host): TRPF / Production host: Escherichia coli (E. coli) References: UniProt: Q56320, phosphoribosylanthranilate isomerase |
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#2: Chemical | ChemComp-PO4 / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 3 |
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-Sample preparation
Crystal | Density Matthews: 2.71 Å3/Da / Density % sol: 45 % / Description: HEAVY ATOM DERIVATIVE PHASING | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 Details: PROTEIN 19.4 MG/ML IN 0.05 M POTASSIUM PHOSPHATE PH 7.5, 1MM EDTA, 0.4 MM DTT MIXED WITH RESERVOIR 1:1 CONTAINING 1.5-2.1 M AMMONIUM SULFATE, 10 MM COCL2, 0.1 M MES PH 6.5, PH range: 6.5-7.5 | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, hanging dropDetails: drop solution was mixed with an equal volume of reservoir solution | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 277 K |
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Diffraction source | Source: ROTATING ANODE / Type: ELLIOTT GX-18 / Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jan 9, 1995 |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→20 Å / Num. obs: 17903 / % possible obs: 98.8 % / Observed criterion σ(I): 0 / Redundancy: 6.6 % / Rmerge(I) obs: 0.064 / Net I/σ(I): 8.6 |
Reflection shell | Resolution: 2→2.11 Å / Redundancy: 4.5 % / Rmerge(I) obs: 0.311 / Mean I/σ(I) obs: 2.4 / % possible all: 96.2 |
Reflection | *PLUS Num. measured all: 118018 |
Reflection shell | *PLUS % possible obs: 96.2 % |
-Processing
Software |
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Refinement | Method to determine structure: MIR / Resolution: 2→15 Å / σ(F): 0 Details: RESIDUES 129 - 136 ARE IN THE MODEL WITH OCCUPANCIES = 0, BECAUSE THERE IS NO ELECTRON DENSITY FOR THESE RESIDUES; THEY WERE BUILT STEREOCHEMICALLY ONLY.
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Displacement parameters | Biso mean: 32.1 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→15 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.03 Å / Total num. of bins used: 20
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 10 Å / % reflection Rfree: 5 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |