BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15882

Title: 1H, 15N, 13C backbone assignment of the SPF45 UHM domain   PubMed: 17589525

Deposition date: 2008-07-22 Original release date: 2008-10-01

Authors: Corsini, Lorenzo; Sattler, Michael

Citation: Corsini, Lorenzo; Bonnal, Sophie; Basquin, Jerome; Hothorn, Michael; Scheffzek, Klaus; Valcarcel, Juan; Sattler, Michael. "U2AF-homology motif interactions are required for alternative splicing regulation by SPF45."  Nat. Struct. Biol. 14, 620-629 (2007).

Assembly members:
SPF45, polymer, 104 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
SPF45: GAMKCPTKVVLLRNMVGAGE VDEDLEVETKEECEKYGKVG KCVIFEIPGAPDDEAVRIFL EFERVESAIKAVVDLNGRYF GGRVVKACFYNLDKFRVLDL AEQV

Data sets:
Data typeCount
13C chemical shifts196
1H chemical shifts96
15N chemical shifts96

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SPF451

Entities:

Entity 1, SPF45 104 residues - Formula weight is not available

1   GLYALAMETLYSCYSPROTHRLYSVALVAL
2   LEULEUARGASNMETVALGLYALAGLYGLU
3   VALASPGLUASPLEUGLUVALGLUTHRLYS
4   GLUGLUCYSGLULYSTYRGLYLYSVALGLY
5   LYSCYSVALILEPHEGLUILEPROGLYALA
6   PROASPASPGLUALAVALARGILEPHELEU
7   GLUPHEGLUARGVALGLUSERALAILELYS
8   ALAVALVALASPLEUASNGLYARGTYRPHE
9   GLYGLYARGVALVALLYSALACYSPHETYR
10   ASNLEUASPLYSPHEARGVALLEUASPLEU
11   ALAGLUGLNVAL

Samples:

sample_1: SPF45, [U-100% 13C; U-100% 15N], 0.5 ± 0.1 mM

sample_conditions_1: temperature: 300 K; pH: 7.00; pressure: 1 atm; ionic strength: 0.2 M

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1

Software:

NMRView v5.0.2, Johnson, One Moon Scientific - chemical shift assignment

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

NMR spectrometers:

  • Bruker DRX 500 MHz

Related Database Links:

PDB
DBJ BAE91606 BAG37457 BAI47074 BAK63294
GB AAC64085 AAH07871 AAH09064 AAH34896 AAH39322
REF NP_001013076 NP_001094553 NP_001139019 NP_001244661 NP_001267436
SP Q8JZX4 Q96I25
TPG DAA16000 DAA23631

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts