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Yorodumi- PDB-1i18: SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF RIBOFLAVIN SYNTHAS... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1i18 | ||||||
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Title | SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF RIBOFLAVIN SYNTHASE FROM E. COLI | ||||||
Components | RIBOFLAVIN SYNTHASE ALPHA CHAIN | ||||||
Keywords | TRANSFERASE / GREEK-KEY-BARREL | ||||||
Function / homology | Function and homology information riboflavin synthase / riboflavin synthase activity / riboflavin biosynthetic process / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Truffault, V. / Coles, M. / Diercks, T. / Abelmann, K. / Eberhardt, S. / Luettgen, H. / Bacher, A. / Kessler, H. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2001 Title: The solution structure of the N-terminal domain of riboflavin synthase. Authors: Truffault, V. / Coles, M. / Diercks, T. / Abelmann, K. / Eberhardt, S. / Luttgen, H. / Bacher, A. / Kessler, H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1i18.cif.gz | 1.2 MB | Display | PDBx/mmCIF format |
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PDB format | pdb1i18.ent.gz | 1 MB | Display | PDB format |
PDBx/mmJSON format | 1i18.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1i18_validation.pdf.gz | 524.6 KB | Display | wwPDB validaton report |
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Full document | 1i18_full_validation.pdf.gz | 846.7 KB | Display | |
Data in XML | 1i18_validation.xml.gz | 162.4 KB | Display | |
Data in CIF | 1i18_validation.cif.gz | 183.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/i1/1i18 ftp://data.pdbj.org/pub/pdb/validation_reports/i1/1i18 | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 10575.960 Da / Num. of mol.: 2 / Fragment: N-TERMINAL DOMAIN, RESIDUES 1-97 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli) References: UniProt: P29015, UniProt: P0AFU8*PLUS, riboflavin synthase #2: Chemical | |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample conditions |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: STRUCTURES BASED ON 2569 NOE RESTRAINTS (353*2 INTRARES., 365*2 SEQUENTIAL, 159*2 MEDIUM-RANGE, 372*2 LONG-RANGE, 71 INTERMOLECULAR) 56*2 DIHEDRAL RESTRAINTS, 42*2 H-BONDS | ||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 50 / Conformers submitted total number: 21 |