BMRB Entry 19248

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19248
MolProbity Validation Chart

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Title:
Structure of SRSF1 RRM2 in complex with the RNA 5'-UGAAGGAC-3'
Deposition date:
2013-05-17
Original release date:
2013-07-08
Authors:
Clery, Antoine; Sinha, Rahul; Anczukow, Olga; Corrionero, Anna; Moursy, Ahmed; Daubner, Gerrit; Valcarcel, Juan; Krainer, Adrian; Allain, Frederic
Citation:

Citation: Clery, Antoine; Sinha, Rahul; Anczukow, Olga; Corrionero, Anna; Moursy, Ahmed; Daubner, Gerrit; Valcarcel, Juan; Krainer, Adrian; Allain, Frederic H-T. "Isolated pseudo-RNA-recognition motifs of SR proteins can regulate splicing using a noncanonical mode of RNA recognition."  Proc. Natl. Acad. Sci. U.S.A. 110, E2802-E2811 (2013).
PubMed: 23836656

Assembly members:

Assembly members:
RNA_5'-UGAAGGAC-3, polymer, 8 residues, 2589.643 Da.
SRSF1_RRM2, polymer, 91 residues, 10338.676 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RNA_5'-UGAAGGAC-3: UGAAGGAC
SRSF1_RRM2: MAPRGRYGPPSRRSENRVVV SGLPPSGSWQDLKDHMREAG DVCYADVYRDGTGVVEFVRK EDMTYAVRKLDNTKFRSHEG ETAYIRVKVDG

Data sets:
Data typeCount
13C chemical shifts271
15N chemical shifts89
1H chemical shifts638

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1RNA_5'-UGAAGGAC-31
2SRSF1_RRM22

Entities:

Entity 1, RNA_5'-UGAAGGAC-3 8 residues - 2589.643 Da.

1   UGAAGGAC

Entity 2, SRSF1_RRM2 91 residues - 10338.676 Da.

1   METALAPROARGGLYARGTYRGLYPROPRO
2   SERARGARGSERGLUASNARGVALVALVAL
3   SERGLYLEUPROPROSERGLYSERTRPGLN
4   ASPLEULYSASPHISMETARGGLUALAGLY
5   ASPVALCYSTYRALAASPVALTYRARGASP
6   GLYTHRGLYVALVALGLUPHEVALARGLYS
7   GLUASPMETTHRTYRALAVALARGLYSLEU
8   ASPASNTHRLYSPHEARGSERHISGLUGLY
9   GLUTHRALATYRILEARGVALLYSVALASP
10   GLY

Samples:

sample_1: SRSF1_RRM2, [U-100% 15N], 0.8 mM; H2O 90%; D2O 10%

sample_2: SRSF1_RRM2, [U-100% 13C; U-100% 15N], 0.8 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 120 mM; pH: 5.5; pressure: 1 atm; temperature: 273 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 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 700 MHz

Related Database Links:

BMRB 19203
PDB
DBJ BAB93456 BAC37367 BAE29641 BAE88160 BAF82622
EMBL CAH92288
GB AAA03476 AAA35564 AAA35565 AAH10264 AAH42354
REF NP_001006919 NP_001033096 NP_001069862 NP_001071635 NP_001103022
SP Q07955 Q0VCY7 Q3YLA6 Q5R7H2 Q6DII2
TPG DAA19172
AlphaFold Q07955 Q0VCY7 Q3YLA6 Q5R7H2 Q6DII2

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