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 18094

Title: Solution structure of the AF4-AF9 complex   PubMed: 23260655

Authors: Leach, Benjamin; Lumba, Bhavna; Chang, Ming-Jin; Cierpicki, Tomasz; Johnson, Stephanie; Hemenway, Charles; Bushweller, John

Citation: Leach, Benjamin; Kuntimaddi, Aravinda; Schmidt, Charles; Cierpicki, Tomasz; Johnson, Stephanie; Bushweller, John. "Leukemia Fusion Target AF9 Is an Intrinsically Disordered Transcriptional Regulator that Recruits Multiple Partners via Coupled Folding and Binding."  Structure 21, 176-183 (2013).

Assembly members:
AF4-Af9 fusion, polymer, 125 residues, 9252.518 Da.

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):
AF4-Af9 fusion: TRLPLPLRDTKLLSPLRDTP PPQSLMVKITLDLLSRIPQP PGKPMGSDKQIKNGECDKAY LDELVELHRRLMTLRERHIL QQIVNLIEETGHFHITNTTF DFDLCSLDKTTVRKLQSYLE TSGTS

Data sets:
Data typeCount
13C chemical shifts446
15N chemical shifts108
1H chemical shifts731

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1AF4-Af9 fusion1

Entities:

Entity 1, AF4-Af9 fusion 125 residues - 9252.518 Da.

1   THRARGLEUPROLEUPROLEUARGASPTHR
2   LYSLEULEUSERPROLEUARGASPTHRPRO
3   PROPROGLNSERLEUMETVALLYSILETHR
4   LEUASPLEULEUSERARGILEPROGLNPRO
5   PROGLYLYSPROMETGLYSERASPLYSGLN
6   ILELYSASNGLYGLUCYSASPLYSALATYR
7   LEUASPGLULEUVALGLULEUHISARGARG
8   LEUMETTHRLEUARGGLUARGHISILELEU
9   GLNGLNILEVALASNLEUILEGLUGLUTHR
10   GLYHISPHEHISILETHRASNTHRTHRPHE
11   ASPPHEASPLEUCYSSERLEUASPLYSTHR
12   THRVALARGLYSLEUGLNSERTYRLEUGLU
13   THRSERGLYTHRSER

Samples:

sample_1: Bis-Tris 9.3 mM; MES 15.8 mM; sodium chloride 100 mM; DTT 1 mM; D2O, D-99%, 5%; AF4-AF9_fus, [U-100% 13C; U-100% 15N], 400 uM; H2O 95%

Sample_2: MES 15.8 mM; Bis-Tris 9.3 mM; sodium chloride 100 mM; DTT 1 mM; D2O, D-99%, 5%; AF4-AF9_fus, [U-100% 13C; U-100% 15N], 2 mM; H2O 95%

sample_3: Bis-Tris 9.3 mM; MES 15.8 mM; sodium chloride 100 mM; DTT 1 mM; D2O, D-99%, 5%; AF4-AF9_fus, [U-100% 13C; U-100% 15N], 400 uM; (3-acrylamidopropyl)-trimethylammonium chloride 3.5%; acrylic acid 3.5%; H2O 95%

sample_4: Bis-Tris 9.3 mM; MES 15.8 mM; sodium chloride 100 mM; DTT 1 mM; D2O, D-99%, 5%; AF4-AF9_fus, [U-100% 13C; U-100% 15N], 400 uM; (3-acrylamidopropyl)-trimethylammonium chloride 3.5%; acrylamide 3.5%; H2O 95%

sample_conditions_1: ionic strength: 100 mM; pH: 6.0; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYSample_2isotropicsample_conditions_1
2D 1H-15N HSQCSample_2isotropicsample_conditions_1
3D HNCO IPAPsample_3anisotropicsample_conditions_1
3D HNCO IPAPsample_4anisotropicsample_conditions_1
3D HNCO IPAPsample_4anisotropicsample_conditions_1
3D HNCO IPAPsample_4anisotropicsample_conditions_1

Software:

X-PLOR NIH v2.27, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

TOPSPIN, Bruker Biospin - collection

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

SPARKY, Goddard - peak picking

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker US2 800 MHz

Related Database Links:

BMRB 19516
PDB
REF XP_007898203 XP_010901183 XP_011595974