BMRB Entry 30786

Name: Solution NMR structure of human Brd3 ET domain with MLV IN C-terminal Tail Peptide (TP) complex
Published: 2021-03-02

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PDB ID: 7jq8
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30786
MolProbity Validation Chart

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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 NMR structure of human Brd3 ET domain with MLV IN C-terminal Tail Peptide (TP) complex

Deposition date:

2020-08-10

Original release date:

2021-03-02

Authors:

Aiyer, S.; Swapna, G.; Roth, M.; Montelione, G.

Citation:

Citation: Aiyer, S.; Swapna, G.; Ma, L.; Liu, G.; Hao, J.; Chalmers, G.; Jacobs, B.; Montelione, G.; Roth, M.. "A common binding motif in the ET domain of BRD3 forms polymorphic structural interfaces with host and viral proteins" Structure 29, 886-898 (2021).
PubMed: 33592170

Assembly members:

Assembly members:
entity_1, polymer, 96 residues, 11264.543 Da.
entity_2, polymer, 23 residues, 2812.281 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 BL21(DE3) Vector: pET15_NESG

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: HHHHHHSHMGKQASASYDSE EEEEGLPMSYDEKRQLSLDI NRLPGEKLGRVVHIIQSREP SLRDSNPDEIEIDFETLKPT TLRELERYVKSCLQKK
entity_2: SRLTWRVQRSQNPLKIRLTR EAP

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	358
15N chemical shifts	109
1H chemical shifts	751

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1
2	unit_2	2

Entities:

Entity 1, unit_1 96 residues - 11264.543 Da.

1

HIS

SER

HIS

MET

GLY

2

LYS

GLN

ALA

SER

ALA

SER

TYR

ASP

SER

GLU

3

GLU

GLY

LEU

PRO

MET

SER

TYR

4

ASP

GLU

LYS

ARG

GLN

LEU

SER

LEU

ASP

ILE

5

ASN

ARG

LEU

PRO

GLY

GLU

LYS

LEU

GLY

ARG

6

VAL

HIS

ILE

GLN

SER

ARG

GLU

PRO

7

SER

LEU

ARG

ASP

SER

ASN

PRO

ASP

GLU

ILE

8

GLU

ILE

ASP

PHE

GLU

THR

LEU

LYS

PRO

THR

9

THR

LEU

ARG

GLU

LEU

GLU

ARG

TYR

VAL

LYS

10

SER

CYS

LEU

GLN

LYS

Entity 2, unit_2 23 residues - 2812.281 Da.

1

SER

ARG

LEU

THR

TRP

ARG

VAL

GLN

ARG

SER

2

GLN

ASN

PRO

LEU

LYS

ILE

ARG

LEU

THR

ARG

3

GLU

ALA

PRO

Samples:

sample_1: MLV IN TP, [U-100% 13C; U-100% 15N], 0.5 ± 0.02 mM; sodium chloride 100 ± 0.02 mM; sodium phosphate 20 ± 0.02 mM; 2-mercaptoethanol 2 ± 0.02 mM

sample_2: sodium chloride 100 ± 0.02 mM; sodium phosphate 20 ± 0.02 mM; 2-mercaptoethanol 2 ± 0.02 mM; Brd3 ET, [U-100% 13C; U-100% 15N], 0.5 ± 0.02 mM

sample_3: sodium chloride 100 ± 0.02 mM; sodium phosphate 20 ± 0.02 mM; 2-mercaptoethanol 2 ± 0.02 mM; Brd3 ET 0.5 ± 0.02 mM

sample_4: sodium chloride 100 ± 0.02 mM; sodium phosphate 20 ± 0.02 mM; 2-mercaptoethanol 2 ± 0.02 mM; Brd3 ET 0.5 ± 0.02 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

sample_conditions_3: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

sample_conditions_4: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
1D_1H	sample_1	isotropic	sample_conditions_1
2D HNOE	sample_1	isotropic	sample_conditions_1
2D NH-HSQC	sample_1	isotropic	sample_conditions_1
2D CH-HSQC	sample_1	isotropic	sample_conditions_1
2D TROSY	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CN-simNOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
1D_1H	sample_2	isotropic	sample_conditions_2
2D-homoNOESY-13C15Nfilter	sample_2	isotropic	sample_conditions_2
3D 12C-14N_filtered NOESY	sample_2	isotropic	sample_conditions_2
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_2
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_2
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_2
3D HNCACB	sample_2	isotropic	sample_conditions_2
3D HNCA	sample_2	isotropic	sample_conditions_2
3D HNCO	sample_2	isotropic	sample_conditions_2
2D_CT_CHHSQC	sample_2	isotropic	sample_conditions_2
2D_CHHSQC	sample_2	isotropic	sample_conditions_2
2D_NH_HSQC	sample_2	isotropic	sample_conditions_2
2D HNOE	sample_2	isotropic	sample_conditions_2
3D Aromatic -NOESY	sample_3	isotropic	sample_conditions_3
3D CN_simNOESY	sample_3	isotropic	sample_conditions_3
1D_1H	sample_4	isotropic	sample_conditions_4
2D NHHSQC	sample_4	isotropic	sample_conditions_4
3D HNCACB	sample_4	isotropic	sample_conditions_4
3D HNCA	sample_4	isotropic	sample_conditions_4
2D CHHSQC	sample_4	isotropic	sample_conditions_4
2D NH-TROSY	sample_4	isotropic	sample_conditions_4
3D HBHA(CO)NH	sample_4	isotropic	sample_conditions_4
3D HCCH-TOCSY	sample_4	isotropic	sample_conditions_4
3D CN_simNOESY	sample_4	isotropic	sample_conditions_4
3D 12C_14N_NOESY	sample_4	isotropic	sample_conditions_4

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