BMRB Entry 34466

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34466
MolProbity Validation Chart

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Title:
Solution structure of U2AF2 RRM1,2
Deposition date:
2019-12-17
Original release date:
2020-04-28
Authors:
Kang, H.; Sattler, M.
Citation:

Citation: Kang, H.; Sanchez-Rico, C.; Ebersberger, S.; Sutandy, F.; Busch, A.; Welte, T.; Stehle, R.; Hipp, C.; Schulz, L.; Buchbender, A.; Zarnack, K.; Konig, J.; Sattler, M.. "An autoinhibitory intramolecular interaction proof-reads RNA recognition by the essential splicing factor U2AF2."  Proc. Natl. Acad. Sci. U.S.A. 117, 7140-7149 (2020).
PubMed: 32188783

Assembly members:

Assembly members:
entity_1, polymer, 205 residues, 22342.486 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: AMVGSQMTRQARRLYVGNIP FGITEEAMMDFFNAQMRLGG LTQAPGNPVLAVQINQDKNF AFLEFRSVDETTQAMAFDGI IFQGQSLKIRRPHDYQPLPG MSENPSVYVPGVVSTVVPDS AHKLFIGGLPNYLNDDQVKE LLTSFGPLKAFNLVKDSATG LSKGYAFCEYVDINVTDQAI AGLNGMQLGDKKLLVQRASV GAKNA

Data sets:
Data typeCount
13C chemical shifts655
15N chemical shifts215
1H chemical shifts1370

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 205 residues - 22342.486 Da.

1   ALAMETVALGLYSERGLNMETTHRARGGLN
2   ALAARGARGLEUTYRVALGLYASNILEPRO
3   PHEGLYILETHRGLUGLUALAMETMETASP
4   PHEPHEASNALAGLNMETARGLEUGLYGLY
5   LEUTHRGLNALAPROGLYASNPROVALLEU
6   ALAVALGLNILEASNGLNASPLYSASNPHE
7   ALAPHELEUGLUPHEARGSERVALASPGLU
8   THRTHRGLNALAMETALAPHEASPGLYILE
9   ILEPHEGLNGLYGLNSERLEULYSILEARG
10   ARGPROHISASPTYRGLNPROLEUPROGLY
11   METSERGLUASNPROSERVALTYRVALPRO
12   GLYVALVALSERTHRVALVALPROASPSER
13   ALAHISLYSLEUPHEILEGLYGLYLEUPRO
14   ASNTYRLEUASNASPASPGLNVALLYSGLU
15   LEULEUTHRSERPHEGLYPROLEULYSALA
16   PHEASNLEUVALLYSASPSERALATHRGLY
17   LEUSERLYSGLYTYRALAPHECYSGLUTYR
18   VALASPILEASNVALTHRASPGLNALAILE
19   ALAGLYLEUASNGLYMETGLNLEUGLYASP
20   LYSLYSLEULEUVALGLNARGALASERVAL
21   GLYALALYSASNALA

Samples:

sample_1: U2AF2, [U-13C; U-15N], 0.5 mM; sodium phosphoate 20 mM; sodium chloride 50 mM; DTT 2 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

ARIA, Linge, O'Donoghue and Nilges - refinement

Sparky, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III 800 MHz

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