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 6702

Title: Resonance assignments of 30 kDa complexes of TFIID subunit TAF1 with TATA-binding protein   PubMed: 16222567

Deposition date: 2005-06-22 Original release date: 2006-11-06

Authors: Mal, Tapas; Liu, Dingjiang; Masutomi, Yutaka; Zheng, Le; Nakatani, Yoshihiro; Kokubo, Tetsuro; Ikura, Mitsuhiko

Citation: Mal, Tapas; Liu, Dingjiang; Masutomi, Yutaka; Zheng, Le; Nakatani, Yoshihiro; Kokubo, Tetsuro; Ikura, Mitsuhiko. "Resonance Assignments of 30 kDa Complexes of TFIID Subunit TAF1 with TATA-binding Protein"  J. Biomol. NMR 33, 76-76 (2005).

Assembly members:
yTAF1, polymer, 64 residues, Formula weight is not available
yTBPc, polymer, 192 residues, Formula weight is not available

Natural source:   Common Name: Saccharomyces Cerevisiae   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
yTAF1: TNLANEDEAYEAIFGGEFGS LEIGSYIGGDEGANSKDYTE HLPDAVDFEDEDELADDDDD LPEE
yTBPc: AAPESEKDTSATSGIVPTLQ NIVATVTLGCRLDLKTVALH ARNAEYNPKRFAAVIMRIRE PKTTALIFASGKMVVTGAKS EDDSKLASRKYARIIQKIGF AAKFTDFKIQNIVGSCDVKF PIRLEGLAFSHGTFSSYEPE LFPGLIYRMVKPKIVLLIFV SGKIVLTGAKQREEIYQAFE AIYPVLSEFRKM

Data sets:
Data typeCount
13C chemical shifts462
15N chemical shifts232
1H chemical shifts232

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1yTAF1c1
2yTBPc2

Entities:

Entity 1, yTAF1c 64 residues - Formula weight is not available

1   THRASNLEUALAASNGLUASPGLUALATYR
2   GLUALAILEPHEGLYGLYGLUPHEGLYSER
3   LEUGLUILEGLYSERTYRILEGLYGLYASP
4   GLUGLYALAASNSERLYSASPTYRTHRGLU
5   HISLEUPROASPALAVALASPPHEGLUASP
6   GLUASPGLULEUALAASPASPASPASPASP
7   LEUPROGLUGLU

Entity 2, yTBPc 192 residues - Formula weight is not available

1   ALAALAPROGLUSERGLULYSASPTHRSER
2   ALATHRSERGLYILEVALPROTHRLEUGLN
3   ASNILEVALALATHRVALTHRLEUGLYCYS
4   ARGLEUASPLEULYSTHRVALALALEUHIS
5   ALAARGASNALAGLUTYRASNPROLYSARG
6   PHEALAALAVALILEMETARGILEARGGLU
7   PROLYSTHRTHRALALEUILEPHEALASER
8   GLYLYSMETVALVALTHRGLYALALYSSER
9   GLUASPASPSERLYSLEUALASERARGLYS
10   TYRALAARGILEILEGLNLYSILEGLYPHE
11   ALAALALYSPHETHRASPPHELYSILEGLN
12   ASNILEVALGLYSERCYSASPVALLYSPHE
13   PROILEARGLEUGLUGLYLEUALAPHESER
14   HISGLYTHRPHESERSERTYRGLUPROGLU
15   LEUPHEPROGLYLEUILETYRARGMETVAL
16   LYSPROLYSILEVALLEULEUILEPHEVAL
17   SERGLYLYSILEVALLEUTHRGLYALALYS
18   GLNARGGLUGLUILETYRGLNALAPHEGLU
19   ALAILETYRPROVALLEUSERGLUPHEARG
20   LYSMET

Samples:

sample_1: yTAF1 mM; yTBPc mM; Tris buffer 20 mM

20_mM_Tris_buffer: pH: 7.5; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
HSQCnot availablenot availablenot available
HNCACAnot availablenot availablenot available
CBCACONNHnot availablenot availablenot available
HCCTOCSYNNHnot availablenot availablenot available

Software:

No software information available

NMR spectrometers:

    Related Database Links:

    BMRB 6700
    PDB
    DBJ GAA22978
    EMBL CAA34751 CAG60477 CAY79336 CCD25155 CCE61293
    GB AAA34458 AAA35146 AAA35147 AAB64675 AEP68354
    PRF 1515352A
    REF NP_011075 XP_001646300 XP_003670398 XP_003683727 XP_003955666
    SP P13393
    TPG DAA07809
    AlphaFold P13393

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