BMRB Entry 19735

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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/BMR19735
MolProbity Validation Chart

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Title:
Structure, dynamics and RNA binding of the multi-domain splicing factor TIA-1
Deposition date:
2014-01-13
Original release date:
2014-01-13
Authors:
Sattler, Michael; Wang, Iren
Citation:

Citation: Wang, Iren; Hennig, Janosch; Jagtap, Pravin Kumar Ankush; Sonntag, Miriam; Valcarcel, Juan; Sattler, Michael. "Structure, dynamics and RNA binding of the multi-domain splicing factor TIA-1."  Nucleic Acids Res. ., .-. (2014).
PubMed: 24682828

Assembly members:

Assembly members:
TIA-1_RRM2,3, polymer, 185 residues, 20568.250 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: pETtrx-1a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TIA-1_RRM2,3: AMANHFHVFVGDLSPEITTE DIKAAFAPFGRISDARVVKD MATGKSKGYGFVSFFNKWDA ENAIQQMGGQWLGGRQIRTN WATRKPPAPKSTYESNTKQL SYDEVVNQSSPSNCTVYCGG VTSGLTEQLMRQTFSPFGQI MEIRVFPDKGYSFVRFNSHE SAAHAIVSVNGTTIEGHVVK CYWGK

Data sets:
Data typeCount
1H chemical shifts1253
13C chemical shifts767
15N chemical shifts198

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1TIA-1 RRM2,3 monomer1

Entities:

Entity 1, TIA-1 RRM2,3 monomer 185 residues - 20568.250 Da.

Residues 89-92 (1-4) represent a tag from used construct after TEV cleavage, and residues 93-274 (5-186) are derived from the protein sequence of TIA-1.

1   ALAMETALAASNHISPHEHISVALPHEVAL
2   GLYASPLEUSERPROGLUILETHRTHRGLU
3   ASPILELYSALAALAPHEALAPROPHEGLY
4   ARGILESERASPALAARGVALVALLYSASP
5   METALATHRGLYLYSSERLYSGLYTYRGLY
6   PHEVALSERPHEPHEASNLYSTRPASPALA
7   GLUASNALAILEGLNGLNMETGLYGLYGLN
8   TRPLEUGLYGLYARGGLNILEARGTHRASN
9   TRPALATHRARGLYSPROPROALAPROLYS
10   SERTHRTYRGLUSERASNTHRLYSGLNLEU
11   SERTYRASPGLUVALVALASNGLNSERSER
12   PROSERASNCYSTHRVALTYRCYSGLYGLY
13   VALTHRSERGLYLEUTHRGLUGLNLEUMET
14   ARGGLNTHRPHESERPROPHEGLYGLNILE
15   METGLUILEARGVALPHEPROASPLYSGLY
16   TYRSERPHEVALARGPHEASNSERHISGLU
17   SERALAALAHISALAILEVALSERVALASN
18   GLYTHRTHRILEGLUGLYHISVALVALLYS
19   CYSTYRTRPGLYLYS

Samples:

sample_1: TIA-1 RRM2,3, [U-99% 13C; U-99% 15N], 0.1-0.7 mM; sodium phosphate 10 mM; sodium chloride 50 mM; DTT 10 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_2: TIA-1 RRM2,3, [U-99% 15N], 0.1-0.55 mM; sodium phosphate 10 mM; sodium chloride 50 mM; DTT 10 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_3: TIA-1 RRM2,3, [U-10% 13C], 0.1-0.5 mM; sodium phosphate 10 mM; sodium chloride 50 mM; DTT 10 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 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-13C HSQCsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

TOPSPIN, Bruker Biospin - collection, data analysis, processing

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

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

TALOS, Cornilescu, Delaglio and Bax - chemical shift calculation, data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 750 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz

Related Database Links:

uniprot P31483-2
PDB
REF XP_005264588 XP_009182643 XP_011239587 XP_012381224
AlphaFold Q96B58

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