BMRB Entry 34317

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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/BMR34317
MolProbity Validation Chart

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Title:
Structure of human SRSF1 RRM1 bound to AACAAA RNA
Deposition date:
2018-09-21
Original release date:
2020-11-12
Authors:
Allain, F.; Clery, A.
Citation:

Citation: Clery, Antoine; Krepl, Miroslav; Nguyen, Cristina; Moursy, Ahmed; Jorjani, Hadi; Katsantoni, Maria; Okoniewski, Michal; Mittal, Nitish; Zavolan, Mihaela; Sponer, Jiri; Allain, Frederic H-T. "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).
PubMed: 33462199

Assembly members:

Assembly members:
entity_1, polymer, 161 residues, 17956.693 Da.
entity_2, polymer, 6 residues, 1906.253 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: MQYKLILNGKTLKGETTTEA VDAATAEKVFKQYANDNGVD GEWTYDDATKTFTVTEGSHH HHHHMSGGGVIRGPAGNNDC RIYVGNLPPDIRTKDIEDVF SKYGAIRDIDLKNRRGGPPF AFVEFEDPRDAEDAVSGRDG YDYDGYRLRVEFPRSGRGTG R
entity_2: AACAAA

Data sets:
Data typeCount
13C chemical shifts213
15N chemical shifts74
1H chemical shifts557

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 161 residues - 17956.693 Da.

1   METGLNTYRLYSLEUILELEUASNGLYLYS
2   THRLEULYSGLYGLUTHRTHRTHRGLUALA
3   VALASPALAALATHRALAGLULYSVALPHE
4   LYSGLNTYRALAASNASPASNGLYVALASP
5   GLYGLUTRPTHRTYRASPASPALATHRLYS
6   THRPHETHRVALTHRGLUGLYSERHISHIS
7   HISHISHISHISMETSERGLYGLYGLYVAL
8   ILEARGGLYPROALAGLYASNASNASPCYS
9   ARGILETYRVALGLYASNLEUPROPROASP
10   ILEARGTHRLYSASPILEGLUASPVALPHE
11   SERLYSTYRGLYALAILEARGASPILEASP
12   LEULYSASNARGARGGLYGLYPROPROPHE
13   ALAPHEVALGLUPHEGLUASPPROARGASP
14   ALAGLUASPALAVALSERGLYARGASPGLY
15   TYRASPTYRASPGLYTYRARGLEUARGVAL
16   GLUPHEPROARGSERGLYARGGLYTHRGLY
17   ARG

Entity 2, entity_2 6 residues - 1906.253 Da.

1   AACAAA

Samples:

sample_1: SRSF1 RRM1, [U-99% 15N], 0.5 mM; RNA (5'-R(*AP*AP*CP*AP*AP*A)-3') 0.5 mM

sample_2: SRSF1 RRM1, [U-99% 15N], 0.5 mM; RNA (5'-R(*AP*AP*CP*AP*AP*A)-3') 0.5 mM

sample_3: SRSF1 RRM1, [U-99% 13C; U-99% 15N], 0.5 mM; RNA (5'-R(*AP*AP*CP*AP*AP*A)-3') 0.5 mM

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

Experiments:

NameSampleSample stateSample conditions
2D NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_3isotropicsample_conditions_1

Software:

Amber, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

Sparky, Goddard - chemical shift assignment

CANDID, Herrmann, Guntert and Wuthrich - peak picking

NMR spectrometers:

  • Bruker 500 AVIII 500 MHz
  • Bruker 600 AVIII 600 MHz
  • Bruker 700 AVIII 700 MHz
  • Bruker 900 AVIII 900 MHz

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