+Open data
-Basic information
Entry | Database: PDB / ID: 1ni7 | ||||||
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Title | NORTHEAST STRUCTURAL GENOMIC CONSORTIUM TARGET ER75 | ||||||
Components | Hypothetical protein ygdKHypothesis | ||||||
Keywords | STRUCTURAL GENOMICS / Unknown function / ER75 / RD-NMR / PSI / Protein Structure Initiative / Northeast Structural Genomics Consortium / NESG | ||||||
Function / homology | Function and homology information cyclic threonylcarbamoyladenosine biosynthetic process / sulfur carrier activity Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / distance geometry simulated annealing torsion angle dynamics | ||||||
Authors | Liu, G. / Chiang, Y. / Acton, T. / Montelione, G.T. / Szyperski, T. / Northeast Structural Genomics Consortium (NESG) | ||||||
Citation | Journal: Protein Sci. / Year: 2005 Title: High-quality homology models derived from NMR and X-ray structures of E. coli proteins YgdK and Suf E suggest that all members of the YgdK/Suf E protein family are enhancers of cysteine desulfurases. Authors: Liu, G. / Li, Z. / Chiang, Y. / Acton, T. / Montelione, G.T. / Murray, D. / Szyperski, T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ni7.cif.gz | 884.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ni7.ent.gz | 765.3 KB | Display | PDB format |
PDBx/mmJSON format | 1ni7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ni/1ni7 ftp://data.pdbj.org/pub/pdb/validation_reports/ni/1ni7 | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 17027.365 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: YGDK / Plasmid: pET21-ER75-21 / Production host: Escherichia coli (E. coli) / References: UniProt: Q46926, UniProt: P0AGF2*PLUS |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined with the help of Reduced-dimensional NMR techniques (RD-NMR) |
-Sample preparation
Details |
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Sample conditions | pH: 6.5 / Pressure: ambient / Temperature: 298 K | |||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: distance geometry simulated annealing torsion angle dynamics Software ordinal: 1 Details: This structure was determined with the help of Reduced-dimensional NMR techniques (RD-NMR).The residue ranges of well defined regions of the structure are :16-27,31-45,51-58,63-72,74-120,134- ...Details: This structure was determined with the help of Reduced-dimensional NMR techniques (RD-NMR).The residue ranges of well defined regions of the structure are :16-27,31-45,51-58,63-72,74-120,134-148; The backbone mean rmsd for well-defined regions is 0.48+-0.07A, and all heavy atom mean rmsd for well-defined regions is 0.87+-0.07A. | ||||||||||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 |