BMRB Entry 36491

Title:
Solution structure of RRM2 of Human SART3
Deposition date:
2022-05-29
Original release date:
2026-03-30
Authors:
Kim, I.; Bang, K.; Park, C.; Kim, N.; Suh, J.
Citation:

Citation: Kim, Iktae; Bang, Kyeong-Mi; An, So Young; Park, Changkon; Shin, Ji-Yeon; Kim, Youngim; Song, Hyun Kyu; Suh, Jeong-Yong; Kim, Nak-Kyoon. "Structural investigation of human U6 snRNA recognition by spliceosomal recycling factor SART3 RNA recognition motifs"  FEBS J. 293, 1323-1340 (2026).
PubMed: 41046346

Assembly members:

Assembly members:
Squamous cell carcinoma antigen recognized by T-cells 3, polymer, 84 residues, 9351.867 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):
Squamous cell carcinoma antigen recognized by T-cells 3: GSHMLEKHKLFISGLPFSCT KEELEEICKAHGTVKDLRLV TNRAGKPKGLAYVEYENESQ ASQAVMKMDGMTIKENIIKV AISN

Data sets:
Data typeCount
13C chemical shifts345
15N chemical shifts84
1H chemical shifts559

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 84 residues - 9351.867 Da.

1   GLYSERHISMETLEUGLULYSHISLYSLEU
2   PHEILESERGLYLEUPROPHESERCYSTHR
3   LYSGLUGLULEUGLUGLUILECYSLYSALA
4   HISGLYTHRVALLYSASPLEUARGLEUVAL
5   THRASNARGALAGLYLYSPROLYSGLYLEU
6   ALATYRVALGLUTYRGLUASNGLUSERGLN
7   ALASERGLNALAVALMETLYSMETASPGLY
8   METTHRILELYSGLUASNILEILELYSVAL
9   ALAILESERASN

Samples:

sample_1: Human SART3 RRM2, [U-100% 13C; U-100% 15N], 0.8 mM; DTT 1 mM; sodium phosphate 20 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 20 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMRFAM-SPARKY, NMRFAM-SPARKY - chemical shift assignment

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

TopSpin, Bruker Biospin - collection

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Bruker ascend 800 MHz

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