BMRB Entry 18802

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18802
MolProbity Validation Chart

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Title:
Structure, phosphorylation and U2AF65 binding of the Nterminal domain of splicing factor 1 during 3 splice site recognition
Deposition date:
2012-10-22
Original release date:
2013-01-28
Authors:
Madl, Tobias; Sattler, Michael; Zhang, Yun; Bagdiul, Ivona; Kern, Thomas; Kang, Hyun-Seo; Zou, Peijian; Maeusbacher, Nina; Sieber, Stephan; Kraemer, Angela
Citation:

Citation: Zhang, Yun; Madl, Tobias; Bagdiul, Ivona; Kern, Thomas; Kang, Hyun-Seo; Zou, Peijian; Maeusbacher, Nina; Sieber, Stephan; Kraemer, Angela; Sattler, Michael. "Structure, phosphorylation and U2AF65 binding of the N-terminal domain of splicing factor 1 during 3'-splice site recognition"  Nucleic Acids Res. 41, 1343-1354 (2013).
PubMed: 23175611

Assembly members:

Assembly members:
entity, polymer, 121 residues, 13821.896 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   Vector: petM11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GAMEQKTVIPGMPTVIPPGL TREQERAYIVQLQIEDLTRK LRTGDLGIPPNPEDRSPSPE PIYNSEGKRLNTREFRTRKK LEEERHNLITEMVALNPDFK PPADYKPPATRVSDKVMIPQ D

Data sets:
Data typeCount
13C chemical shifts544
15N chemical shifts116
1H chemical shifts860

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SF1N1

Entities:

Entity 1, SF1N 121 residues - 13821.896 Da.

1   GLYALAMETGLUGLNLYSTHRVALILEPRO
2   GLYMETPROTHRVALILEPROPROGLYLEU
3   THRARGGLUGLNGLUARGALATYRILEVAL
4   GLNLEUGLNILEGLUASPLEUTHRARGLYS
5   LEUARGTHRGLYASPLEUGLYILEPROPRO
6   ASNPROGLUASPARGSERPROSERPROGLU
7   PROILETYRASNSERGLUGLYLYSARGLEU
8   ASNTHRARGGLUPHEARGTHRARGLYSLYS
9   LEUGLUGLUGLUARGHISASNLEUILETHR
10   GLUMETVALALALEUASNPROASPPHELYS
11   PROPROALAASPTYRLYSPROPROALATHR
12   ARGVALSERASPLYSVALMETILEPROGLN
13   ASP

Samples:

sample_1: SF1N, [U-15N], 100 – 600 uM; SF1N, [U-13C; U-15N], 100 – 600 uM; SF1N, [U-13C; U-15N; U-2H], 100 – 600 uM; sodium phosphate 20 mM; NaCl 50 mM; DTT 1 mM; sodium azide 0.1%; EDTA 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 70 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

ARIA v2.1, Linge, O'Donoghue and Nilges - structure solution

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 750 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 500 MHz

Related Database Links:

BMRB 18808
PDB
DBJ BAA05116 BAA05117 BAE01434 BAE26935 BAE27661
EMBL CAA03883 CAA59797 CAA70018 CAA70019 CAA73359
GB AAB03514 AAB04033 AAH08080 AAH08724 AAH09091
PIR S52735
REF NP_001011340 NP_001075083 NP_001104261 NP_001104263 NP_001162562
SP Q15637 Q64213
TPG DAA13585
AlphaFold Q15637 Q64213

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