BMRB Entry 18094

Name: Solution structure of the AF4-AF9 complex
Published: 2013-01-07

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PDB ID: 2lm0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18094
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of the AF4-AF9 complex

Deposition date:

2011-11-18

Original release date:

2013-01-07

Authors:

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

Citation:

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).
PubMed: 23260655

Assembly members:

Assembly members:
AF4-Af9 fusion, polymer, 125 residues, 9252.518 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: pET 32a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
AF4-Af9 fusion: TRLPLPLRDTKLLSPLRDTP PPQSLMVKITLDLLSRIPQP PGKPMGSDKQIKNGECDKAY LDELVELHRRLMTLRERHIL QQIVNLIEETGHFHITNTTF DFDLCSLDKTTVRKLQSYLE TSGTS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	446
15N chemical shifts	108
1H chemical shifts	731

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	AF4-Af9 fusion	1

Entities:

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

1

THR

ARG

LEU

PRO

LEU

PRO

LEU

ARG

ASP

THR

2

LYS

LEU

SER

PRO

LEU

ARG

ASP

THR

PRO

3

PRO

GLN

SER

LEU

MET

VAL

LYS

ILE

THR

4

LEU

ASP

LEU

SER

ARG

ILE

PRO

GLN

PRO

5

PRO

GLY

LYS

PRO

MET

GLY

SER

ASP

LYS

GLN

6

ILE

LYS

ASN

GLY

GLU

CYS

ASP

LYS

ALA

TYR

7

LEU

ASP

GLU

LEU

VAL

GLU

LEU

HIS

ARG

8

LEU

MET

THR

LEU

ARG

GLU

ARG

HIS

ILE

LEU

9

GLN

ILE

VAL

ASN

LEU

ILE

GLU

THR

10

GLY

HIS

PHE

HIS

ILE

THR

ASN

THR

PHE

11

ASP

PHE

ASP

LEU

CYS

SER

LEU

ASP

LYS

THR

12

THR

VAL

ARG

LYS

LEU

GLN

SER

TYR

LEU

GLU

13

THR

SER

GLY

THR

SER

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	Sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	Sample_2	isotropic	sample_conditions_1
3D HNCO IPAP	sample_3	anisotropic	sample_conditions_1
3D HNCO IPAP	sample_4	anisotropic	sample_conditions_1
3D HNCO IPAP	sample_4	anisotropic	sample_conditions_1
3D HNCO IPAP	sample_4	anisotropic	sample_conditions_1

BMRB	19516
PDB	2LM0 2MV7
REF	XP_007898203 XP_010901183 XP_011595974

BMRB Entry 18094

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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