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Yorodumi- PDB-1nr3: SOLUTION STRUCTURE OF THE PROTEIN MTH0916: THE NORTHEAST STRUCTUR... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1nr3 | |||||||||
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Title | SOLUTION STRUCTURE OF THE PROTEIN MTH0916: THE NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET TT212 | |||||||||
Components | DNA-binding protein tfx | |||||||||
Keywords | TRANSCRIPTION / NORTHEAST STRUCTURAL GENOMICS CONSORTIUM / REDUCED-DIMENSIONALITY NMR / PSI / Protein Structure Initiative / NESG | |||||||||
Function / homology | Function and homology information DNA-templated transcription initiation / DNA-binding transcription factor activity / DNA binding Similarity search - Function | |||||||||
Biological species | Methanothermobacter thermautotrophicus (archaea) | |||||||||
Method | SOLUTION NMR / TORSION ANGLE DYNAMICS, SIMULATED ANNEALING | |||||||||
Authors | Shen, Y. / Liu, G. / Bhaskaran, R. / Yee, A. / Arrowsmith, C. / Szyperski, T. / Northeast Structural Genomics Consortium (NESG) | |||||||||
Citation | Journal: To be Published Title: SOLUTION STRUCTURE OF THE PROTEIN MTH0916: THE NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET TT212 Authors: SHEN, Y. / LIU, G. / BHASKARAN, R. / YEE, A. / ARROWSMITH, C. / SZYPERSKI, T. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1nr3.cif.gz | 724.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1nr3.ent.gz | 600.7 KB | Display | PDB format |
PDBx/mmJSON format | 1nr3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1nr3_validation.pdf.gz | 479.9 KB | Display | wwPDB validaton report |
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Full document | 1nr3_full_validation.pdf.gz | 722.2 KB | Display | |
Data in XML | 1nr3_validation.xml.gz | 85.7 KB | Display | |
Data in CIF | 1nr3_validation.cif.gz | 96.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nr/1nr3 ftp://data.pdbj.org/pub/pdb/validation_reports/nr/1nr3 | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 14190.438 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Methanothermobacter thermautotrophicus (archaea) Production host: Escherichia coli (E. coli) / References: UniProt: O27001 |
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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 using RD techniques. |
-Sample preparation
Details | Contents: 1mM TT212 U-15N, 13C, 450mM NaCl, 10mM DTT, 20mM ZnCl2, 0.01% AZIDE Solvent system: 95% H2O/5% D2O |
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Sample conditions | pH: 6.5 / Pressure: ambient / Temperature: 298 K |
-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: TORSION ANGLE DYNAMICS, SIMULATED ANNEALING / Software ordinal: 1 Details: THE CALCULATION WAS PERFORMED BY TORSION ANGLE DYNAMICS USING DYANA. CYANA WAS USED TO HELP IN THE IDENTIFICATION OF AMBIGUOUS NOE ASSIGNMENTS. | ||||||||||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 |