+Open data
-Basic information
Entry | Database: PDB / ID: 2wqg | ||||||
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Title | SAP domain from Tho1: L31W (fluorophore) mutant | ||||||
Components | PROTEIN THO1 | ||||||
Keywords | UNKNOWN FUNCTION | ||||||
Function / homology | Function and homology information poly(A)+ mRNA export from nucleus / protein-RNA complex assembly / transcription elongation by RNA polymerase II / double-stranded DNA binding / chromatin binding / RNA binding / nucleus Similarity search - Function | ||||||
Biological species | SACCHAROMYCES CEREVISIAE (brewer's yeast) | ||||||
Method | SOLUTION NMR / MANUAL ASSIGNMENT THEN SIMULATED ANNEALING | ||||||
Authors | Dodson, C.A. / Ferguson, N. / Rutherford, T.J. / Johnson, C.M. / Fersht, A.R. | ||||||
Citation | Journal: Protein Eng.Des.Sel. / Year: 2010 Title: Engineering a Two-Helix Bundle Protein for Folding Studies. Authors: Dodson, C.A. / Ferguson, N. / Rutherford, T.J. / Johnson, C.M. / Fersht, A.R. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR PROVIDED. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2wqg.cif.gz | 383.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2wqg.ent.gz | 331.7 KB | Display | PDB format |
PDBx/mmJSON format | 2wqg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wq/2wqg ftp://data.pdbj.org/pub/pdb/validation_reports/wq/2wqg | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar 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: 5655.264 Da / Num. of mol.: 1 / Fragment: SAP DOMAIN, RESIDUES 2-50 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast) Plasmid: PRSETA DERIVATIVE / Production host: ESCHERICHIA COLI BL21(DE3) (bacteria) / Variant (production host): C41 / References: UniProt: P40040 | ||
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Compound details | ENGINEEREDSequence details | SEQUENCE NUMBERING FOR CONSTRUCT AS GIVEN, NOT FOR FULL- LENGTH PROTEIN. L31W MUTANT STRUCTURE SOLVED HERE. | |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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NMR details | Text: STRUCTURE DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELLED SAMPLE. STEREO-SPECIFIC ASSIGNMENT OF LEU AND VAL FROM 10PC-13C LABELLED SAMPLE. |
-Sample preparation
Details | Contents: 95% WATER / 5% D20 |
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Sample conditions | Ionic strength: 500 mM / pH: 6.0 / Pressure: 1.0 atm / Temperature: 283.0 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: Avance / Field strength: 800 MHz |
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-Processing
NMR software |
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Refinement | Method: MANUAL ASSIGNMENT THEN SIMULATED ANNEALING / Software ordinal: 1 | ||||||||||||
NMR ensemble | Conformer selection criteria: STRUCTURES REACHING ACCEPTANCE CRITERIA OF MINIMUM RESTRAINT VIOLATION Conformers calculated total number: 25 / Conformers submitted total number: 25 |