BMRB Entry 52801

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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/BMR52801
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry

Title:
Assignment of SRSF6 RRM1
Deposition date:
2025-01-09
Original release date:
2026-05-06
Authors:
von Ehr, Julian; Schlundt, Andreas
Citation:

Citation: von Ehr, Julian; Schlundt, Andreas. "1H, 13C, 15N backbone chemical shift assignments and relaxation analysis of the single and tandem RRMs of the human serine-arginine rich splicing factor 6 (SRSF6)"  J. Magn. Reson. ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 76 residues, 8690 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: JvE001

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMAMPRVYIGRLSYNVREK DIQRFFSGYGRLLEVDLKNG YGFVEFEDSRDADDAVYELN GKELCGERVIVEHARG

Data typeCount
13C chemical shifts328
15N chemical shifts77
1H chemical shifts506

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RRM11

Entities:

Entity 1, RRM1 76 residues - 8690 Da.

First four residues (GAMA) are from TEV-protease cleavage site and are non-native residues. Therefore numbering starts with -3.

1   GLYALAMETALAMETPROARGVALTYRILE
2   GLYARGLEUSERTYRASNVALARGGLULYS
3   ASPILEGLNARGPHEPHESERGLYTYRGLY
4   ARGLEULEUGLUVALASPLEULYSASNGLY
5   TYRGLYPHEVALGLUPHEGLUASPSERARG
6   ASPALAASPASPALAVALTYRGLULEUASN
7   GLYLYSGLULEUCYSGLYGLUARGVALILE
8   VALGLUHISALAARGGLY

Samples:

sample_1: SRSF6 RRM1, [U-99% 13C; U-99% 15N], 290 uM; sodium phosphate 25 mM; sodium chloride 150 mM; DTT 2 mM

sample_2: SRSF6 RRM1, [U-99% 13C; U-99% 15N], 258 uM; sodium phosphate 25 mM; sodium chloride 150 mM; DTT 2 mM

sample_3: SRSF6 RRM1, [U-99% 13C; U-99% 15N], 250 uM; sodium phosphate 25 mM; sodium chloride 150 mM; DTT 2 mM

sample_4: SRSF6 RRM1, [U-99% 15N], 320 uM; sodium phosphate 25 mM; sodium chloride 150 mM; DTT 2 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCACONHsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_4isotropicsample_conditions_1

Software:

TOPSPIN v3.6 - 4.4 - collection, processing

ANALYSIS v2.5.1 - chemical shift assignment, data analysis, peak picking

CYANA v3.98.15 - structure solution

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE NEO 600 MHz
  • Bruker AVANCE NEO 900 MHz
  • Bruker AVANCE III 950 MHz

Related Database Links:

UNP Q13247

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