BMRB Entry 11364

Title:
Solution structure of the first SURP domain of human splicing factor SF3a120
Deposition date:
2010-09-07
Original release date:
2011-09-07
Authors:
Kuwasako, K.; He, F.; Inoue, M.; Tanaka, A.; Sugano, S.; Guntert, P.; Muto, Y.; Yokoyama, S.
Citation:

Citation: Kuwasako, K.; He, F.; Inoue, M.; Tanaka, A.; Sugano, S.; Guntert, P.; Muto, Y.; Yokoyama, S.. "Solution structures of the SURP domains and the subunit-assembly mechanism within the splicing factor SF3a complex in 17S U2 snRNP"  Structure ., .-..

Assembly members:

Assembly members:
SURP domain, polymer, 64 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: cell free synthesis   Host organism: Escherichia coli   Vector: pET15b-SF3a120 SURP1

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts291
15N chemical shifts66
1H chemical shifts449

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SURP domain1

Entities:

Entity 1, SURP domain 64 residues - Formula weight is not available

1   GLYGLUVALARGASNILEVALASPLYSTHR
2   ALASERPHEVALALAARGASNGLYPROGLU
3   PHEGLUALAARGILEARGGLNASNGLUILE
4   ASNASNPROLYSPHEASNPHELEUASNPRO
5   ASNASPPROTYRHISALATYRTYRARGHIS
6   LYSVALSERGLUPHELYSGLUGLYLYSALA
7   GLNGLUPROSER

Samples:

sample_1: SURP domain, [U-13C; U-15N], 2.0 mM; soldium phosphate 20 mM; d-DTT 1 mM; H2O 90%; D2O 10%

condition_1: ionic strength: 20 mM; pH: 7.0; pressure: 1 atm; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYsample_1isotropiccondition_1
3D 13C-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.9321, Kobayashi, N. - data analysis

CYANA v2.1, Guntert, P. - refinement, structure solution

OPALP v1.4, Koradi, R. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 700 MHz
  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
REF XP_005961296 XP_007461252 XP_012967930

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