SV40 T ANTIGEN DNA-BINDING DOMAIN, NMR, 30 STRUCTURES
Components
SV40 T ANTIGEN
Keywords
DNA BINDING PROTEIN / REPLICATION / ORIGIN-BINDING DOMAIN / DNA-BINDING PROTEIN / EARLY PROTEIN / ACETYLATION / NUCLEAR PROTEIN
Function / homology
Function and homology information
symbiont-mediated suppression of host JAK-STAT cascade via inhibition of JAK1 activity / bidirectional double-stranded viral DNA replication / viral DNA genome replication / DNA 3'-5' helicase / DNA unwinding involved in DNA replication / symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint / DNA replication origin binding / helicase activity / double-stranded DNA binding / single-stranded DNA binding ...symbiont-mediated suppression of host JAK-STAT cascade via inhibition of JAK1 activity / bidirectional double-stranded viral DNA replication / viral DNA genome replication / DNA 3'-5' helicase / DNA unwinding involved in DNA replication / symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint / DNA replication origin binding / helicase activity / double-stranded DNA binding / single-stranded DNA binding / DNA replication / symbiont-mediated perturbation of host ubiquitin-like protein modification / symbiont-mediated suppression of host innate immune response / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / hydrolase activity / virus-mediated perturbation of host defense response / host cell nucleus / ATP binding / identical protein binding / metal ion binding Similarity search - Function
Replication Protein E1; Chain: A, - #20 / Large T antigen, polyomaviridae / Replication Protein E1; Chain: A, / Large T antigen, polyomavirus, C-terminal / Zinc finger, large T-antigen D1-type / Origin of replication binding protein / Polyomavirus large T antigen C-terminus / Large T-antigen (T-ag) origin-binding domain (OBD) profile. / Zinc finger large T-antigen (T-ag) D1-type profile. / T antigen, Ori-binding ...Replication Protein E1; Chain: A, - #20 / Large T antigen, polyomaviridae / Replication Protein E1; Chain: A, / Large T antigen, polyomavirus, C-terminal / Zinc finger, large T-antigen D1-type / Origin of replication binding protein / Polyomavirus large T antigen C-terminus / Large T-antigen (T-ag) origin-binding domain (OBD) profile. / Zinc finger large T-antigen (T-ag) D1-type profile. / T antigen, Ori-binding / Zinc finger, large T-antigen D1 domain superfamily / Helicase, superfamily 3, DNA virus / Superfamily 3 helicase of DNA viruses domain profile. / DnaJ molecular chaperone homology domain / dnaJ domain profile. / Chaperone J-domain superfamily / DnaJ domain / P-loop containing nucleoside triphosphate hydrolase / 3-Layer(aba) Sandwich / Alpha Beta Similarity search - Domain/homology
Mass: 15414.633 Da / Num. of mol.: 1 / Fragment: DNA BINDING DOMAIN, RESIDUES 131 - 260 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Simian virus 40 / Genus: Polyomavirus / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P03070, UniProt: Q98ZP7*PLUS
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Experimental details
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Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Type
1
1
1
NOESY
1
2
1
TOCSY
1
3
1
HNCA
1
4
1
HN(CO)CA
1
5
1
(H)CCH-TOCSY
NMR details
Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED SV40 T-ANTIGEN DNA BINDING DOMAIN.
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Sample preparation
Sample conditions
pH: 5.5 / Temperature: 303 K
Crystal grow
*PLUS
Method: other / Details: NMR
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NMR measurement
NMR spectrometer
Type: Bruker AMX500 / Manufacturer: Bruker / Model: AMX500 / Field strength: 500 MHz
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Processing
NMR software
Name
Developer
Classification
X-PLOR
BRUNGER
refinement
Felix
structuresolution
X-PLOR
structuresolution
Refinement
Method: simulated annealing / Software ordinal: 1 Details: THE STRUCTURES ARE BASED ON 2168 INTERPROTON DISTANCE RESTRAINTS DERIVED FROM NOE MEASUREMENTS, AND 123 BACKBONE TORSION ANGLE RESTRAINTS DERIVED FROM COUPLING CONSTRAINTS. A TOTAL OF 30 ...Details: THE STRUCTURES ARE BASED ON 2168 INTERPROTON DISTANCE RESTRAINTS DERIVED FROM NOE MEASUREMENTS, AND 123 BACKBONE TORSION ANGLE RESTRAINTS DERIVED FROM COUPLING CONSTRAINTS. A TOTAL OF 30 STRUCTURES WERE CALCULATED.
NMR ensemble
Conformers calculated total number: 30 / Conformers submitted total number: 30
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