BMRB Entry 11365

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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/BMR11365
MolProbity Validation Chart

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Title:
Solution structure of the second SURP domain of human splicing factor SF3a120 in complex with a fragment of human splicing factor SF3a60
Deposition date:
2010-09-07
Original release date:
2011-09-07
Authors:
He, F.; Kuwasako, K.; Inoue, M.; 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:
Splicing factor 3A subunit 3, residues_70-107, polymer, 38 residues, Formula weight is not available
Splicing factor 3 subunit 1, SURP domain, polymer, 85 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: PGEX6P-1-SF3A60 (71-107)-HIS(6)-SF3A120 SURP2 (134-217)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Splicing factor 3A subunit 3, residues_70-107: GELNAISGPNEFAEFYNRLK QIKEFHRKHPNEICVPMS
Splicing factor 3 subunit 1, SURP domain: GAQVIQETIVPKEPPPEFEF IADPPSISAFDLDVVKLTAQ FVARNGRQFLTQLMQKEQRN YQFDFLRPQHSLFNYFTKLV EQYTK

Data sets:
Data typeCount
13C chemical shifts580
15N chemical shifts123
1H chemical shifts907

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Splicing factor 3A subunit 3, residues_70-1071
2Splicing factor 3 subunit 1, SURP domain2

Entities:

Entity 1, Splicing factor 3A subunit 3, residues_70-107 38 residues - Formula weight is not available

1   GLYGLULEUASNALAILESERGLYPROASN
2   GLUPHEALAGLUPHETYRASNARGLEULYS
3   GLNILELYSGLUPHEHISARGLYSHISPRO
4   ASNGLUILECYSVALPROMETSER

Entity 2, Splicing factor 3 subunit 1, SURP domain 85 residues - Formula weight is not available

1   GLYALAGLNVALILEGLNGLUTHRILEVAL
2   PROLYSGLUPROPROPROGLUPHEGLUPHE
3   ILEALAASPPROPROSERILESERALAPHE
4   ASPLEUASPVALVALLYSLEUTHRALAGLN
5   PHEVALALAARGASNGLYARGGLNPHELEU
6   THRGLNLEUMETGLNLYSGLUGLNARGASN
7   TYRGLNPHEASPPHELEUARGPROGLNHIS
8   SERLEUPHEASNTYRPHETHRLYSLEUVAL
9   GLUGLNTYRTHRLYS

Samples:

sample_1: Splicing factor 3A subunit 3, residues_70-107, [U-13C; U-15N], 2.0 mM; Splicing factor 3 subunit 1, SURP domain, [U-13C; U-15N], 2.0 mM; sodium phosphate 20 mM; d-DTT 1 mM; H2O 90%; D2O 10%

condition_1: ionic strength: 20 mM; pH: 6.0; pressure: 1 atm; temperature: 308 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
DBJ BAB29971 BAC27111 BAD96274 BAE01061 BAE29808 BAG64353
EMBL CAA57388 CAH65397 CDQ78487 CDQ81146 CAF94386
GB AAA19625 AAH02395 AAH09141 AAH11523 AAH92058 EOA97698
REF NP_001004289 NP_001020869 NP_001029720 NP_001233382 NP_001270624 XP_001498301 XP_003258118 XP_003433446 XP_003478368 XP_003483501
SP Q12874 Q9D554
TPG DAA31011
AlphaFold Q12874 Q9D554

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