BMRB Entry 17622

Title:
Solution structure of the closed conformation of human U2AF65 tandem RRM1 and RRM2 domains
Deposition date:
2011-05-04
Original release date:
2011-08-03
Authors:
Mackereth, C.; Madl, T.; Simon, B.; Zanier, K.; Gasch, A.; Sattler, Michael
Citation:

Citation: Mackereth, C.; Madl, T.; Bonnal, S.; Simon, B.; Zanier, K.; Gasch, A.; Rybin, V.; Valcarcel, J.; Sattler, Michael. "Multi-domain conformational selection underlies pre-mRNA splicing regulation by U2AF"  Nature ., .-..

Assembly members:

Assembly members:
HUMAN_U2AF65, polymer, 198 residues, 21491.534 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETM-11

Experimental source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETM-11

Data sets:
Data typeCount
13C chemical shifts497
15N chemical shifts187
1H chemical shifts939

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1HUMAN U2AF651

Entities:

Entity 1, HUMAN U2AF65 198 residues - 21491.534 Da.

1   GLYALAMETALAARGARGLEUTYRVALGLY
2   ASNILEPROPHEGLYILETHRGLUGLUALA
3   METMETASPPHEPHEASNALAGLNMETARG
4   LEUGLYGLYLEUTHRGLNALAPROGLYASN
5   PROVALLEUALAVALGLNILEASNGLNASP
6   LYSASNPHEALAPHELEUGLUPHEARGSER
7   VALASPGLUTHRTHRGLNALAMETALAPHE
8   ASPGLYILEILEPHEGLNGLYGLNSERLEU
9   LYSILEARGARGPROHISASPTYRGLNPRO
10   LEUPROGLYMETSERGLUASNPROSERVAL
11   TYRVALPROGLYVALVALSERTHRVALVAL
12   PROASPSERALAHISLYSLEUPHEILEGLY
13   GLYLEUPROASNTYRLEUASNASPASPGLN
14   VALLYSGLULEULEUTHRSERPHEGLYPRO
15   LEULYSALAPHEASNLEUVALLYSASPSER
16   ALATHRGLYLEUSERLYSGLYTYRALAPHE
17   CYSGLUTYRVALASPILEASNVALTHRASP
18   GLNALAILEALAGLYLEUASNGLYMETGLN
19   LEUGLYASPLYSLYSLEULEUVALGLNARG
20   ALASERVALGLYALALYSASNALA

Samples:

sample_1: HUMAN_U2AF65, [U-13C; U-15N], 0.2 mM; H2O 90%; D2O 10%; sodium phosphate 20 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 70.000 mM; pH: 6.500; pressure: 1.000 atm; temperature: 295.000 K

Experiments:

NameSampleSample stateSample conditions
1Hsample_1solutionsample_conditions_1
15N HSQC (PRE)sample_1solutionsample_conditions_1

Software:

AutoDep v4.3, PDBe - collection

CNS vany, BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- - chemical shift assignment

SPARKY vany, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

UNP U2AF2_HUMAN
BMRB 17623
PDB
DBJ BAC37309 BAG70075 BAG70201 BAI45669
EMBL CAA45409 CAA45874 CAA45875 CAF97922
GB AAH07487 AAH08740 AAH30574 AAH43071 AAH44032
PRF 1805352A
REF NP_001001217 NP_001012496 NP_001025127 NP_001068804 NP_001080595
SP P26368 P26369
TPG DAA19368
AlphaFold P26369

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks