BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 50552

Title: structure of SRSF1 RRM1 bound to RNA (AACAAA)   PubMed: 33462199

Deposition date: 2020-11-09 Original release date: 2020-12-10

Authors: Clery, Antoine

Citation: Clery, Antoine; Krepl, Miroslav; Nguyen, Cristina; Moursy, Ahmed; Jorjani, Hadi; Katsantoni, Maria; Okoniewski, Michal; Mittal, Nitish; Zavolan, Mihaela; Sponer, Jiri; Allain, Frederic. "Structure of SRSF1 RRM1 bound to RNA reveals an unexpected bimodal mode of interaction and explains its involvement in SMN1 exon7 splicing"  Nat. Commun. 12, 428-428 (2021).

Assembly members:
entity_1, polymer, 6 residues, Formula weight is not available
entity_2, polymer, 84 residues, Formula weight is not available

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

Experimental source:   Production method: obtained from a vendor

Entity Sequences (FASTA):
entity_1: AACAAA
entity_2: VIRGPAGNNDCRIYVGNLPP DIRTKDIEDVFSKYGAIRDI DLKNRRGGPPFAFVEFEDPR DAEDAVSGRDGYDYDGYRLR VEFP

Data sets:
Data typeCount
13C chemical shifts213
15N chemical shifts74
1H chemical shifts550

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1subunit11
2subunit22

Entities:

Entity 1, subunit1 6 residues - Formula weight is not available

1   AACAAA

Entity 2, subunit2 84 residues - Formula weight is not available

1   VALILEARGGLYPROALAGLYASNASNASP
2   CYSARGILETYRVALGLYASNLEUPROPRO
3   ASPILEARGTHRLYSASPILEGLUASPVAL
4   PHESERLYSTYRGLYALAILEARGASPILE
5   ASPLEULYSASNARGARGGLYGLYPROPRO
6   PHEALAPHEVALGLUPHEGLUASPPROARG
7   ASPALAGLUASPALAVALSERGLYARGASP
8   GLYTYRASPTYRASPGLYTYRARGLEUARG
9   VALGLUPHEPRO

Samples:

sample_1: RNA 0.5 mM; SRSF1 bound to RNA, [U-100% 15N], 0.5 mM

sample_2: RNA 0.5 mM; SRSF1 bound to RNA, [U-100% 13C; U-100% 15N], 0.5 mM

sample_conditions_1: ionic strength: 120 mM; pH: 7; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

AMBER v12 - refinement

CYANA - structure solution

TOPSPIN - collection

SPARKY - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 700 MHz
  • Bruker AVANCE III 900 MHz

Related Database Links:

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