BMRB Entry 50899

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50899

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

Title:
1HN, 13C, and 15N backbone resonance assignments of the dimerization and earmuff domains of SET/TAF-1B/I2PP2A (residues 23-225)
Deposition date:
2021-04-16
Original release date:
2021-06-25
Authors:
Roth, Braden; DePalma, Ryan; Varney, Kristen; Weber, David; Ogretmen, Besim
Citation:

Citation: Roth, Braden; DePalma, Ryan; Cook, Mary; Varney, Kristen; Weber, David; Ogretmen, Besim. "1H, 13C, and 15N backbone resonance assignments of the SET/TAF-1\u03b2/I2PP2A oncoprotein (residues 23-225)"  Biomol. NMR Assignments ., .-. (2021).
PubMed: 34156643

Assembly members:

Assembly members:
entity_1, polymer, 204 residues, 24014.3033 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: pET28a_TEV_NdCdSET-WT

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GTSEKEQQEAIEHIDEVQNE IDRLNEQASEEILKVEQKYN KLRQPFFQKRSELIAKIPNF WVTTFVNHPQVSALLGEEDE EALHYLTRVEVTEFEDIKSG YRIDFYFDENPYFENKVLSK EFHLNESGDPSSKSTEIKWK SGKDLTKRSSQTQNKASRKR QHEEPESFFTWFTDHSDAGA DELGEVIKDDIWPNPLQYYL VPDM

Data typeCount
13C chemical shifts549
15N chemical shifts168
1H chemical shifts168

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SET/TAF-1B/I2PP2A (residues 23-225)1

Entities:

Entity 1, SET/TAF-1B/I2PP2A (residues 23-225) 204 residues - 24014.3033 Da.

contains a non-native glycine residue at position 22

1   GLYTHRSERGLULYSGLUGLNGLNGLUALA
2   ILEGLUHISILEASPGLUVALGLNASNGLU
3   ILEASPARGLEUASNGLUGLNALASERGLU
4   GLUILELEULYSVALGLUGLNLYSTYRASN
5   LYSLEUARGGLNPROPHEPHEGLNLYSARG
6   SERGLULEUILEALALYSILEPROASNPHE
7   TRPVALTHRTHRPHEVALASNHISPROGLN
8   VALSERALALEULEUGLYGLUGLUASPGLU
9   GLUALALEUHISTYRLEUTHRARGVALGLU
10   VALTHRGLUPHEGLUASPILELYSSERGLY
11   TYRARGILEASPPHETYRPHEASPGLUASN
12   PROTYRPHEGLUASNLYSVALLEUSERLYS
13   GLUPHEHISLEUASNGLUSERGLYASPPRO
14   SERSERLYSSERTHRGLUILELYSTRPLYS
15   SERGLYLYSASPLEUTHRLYSARGSERSER
16   GLNTHRGLNASNLYSALASERARGLYSARG
17   GLNHISGLUGLUPROGLUSERPHEPHETHR
18   TRPPHETHRASPHISSERASPALAGLYALA
19   ASPGLULEUGLYGLUVALILELYSASPASP
20   ILETRPPROASNPROLEUGLNTYRTYRLEU
21   VALPROASPMET

Samples:

sample_1: Molecule 1, [U-13C; U-15N; U-2H], 1.5 mM; Tris 20 mM; EDTA 50 mM; NaN3 3 mM

sample_conditions_1: ionic strength: 0.020 M; pH: 8.000; pressure: 1.000 atm; temperature: 310.000 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
2 (HNcaCO)sample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
5 (H[N[co[{CA|ca[C]}]]])sample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
7 (H[N[co[{CA|ca[C]}]]])sample_1isotropicsample_conditions_1
2D 1H-15N HSQC/HMQCsample_1isotropicsample_conditions_1

Software:

CcpNmr Analysis v2.5 - Backbone resonance assignment

TOPSPIN v3.6.1 - Data collection

NMRPipe vmac11_64 - data processing

NMR spectrometers:

  • Bruker AvanceIII 950 MHz

Related Database Links:

UniProt Q01105
AlphaFold Q6FHZ5

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