BMRB Entry 30206

Name: Solution structures of Brd2 second bromodomain in complex with stat3 peptide
Published: 2017-02-20

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PDB ID: 5u5s
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR30206
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution structures of Brd2 second bromodomain in complex with stat3 peptide PubMed: 28262505

Deposition date: 2016-12-07 Original release date: 2017-02-20

Authors: Zeng, L.; Zhou, M.

Citation: Cheung, K.; Zhang, F.; Jaganathan, A.; Sharma, R.; Zhang, Q.; Konuma, T.; Shen, T.; Lee, J.-Y., J.; Ren, C.; Chen, C.-H., C.; Lu, G.; Olson, M.; Zhang, W.; Kaplan, M.; Littman, D.; Walsh, M.; Xiong, H.; Zeng, L.; Zhou, M.. "Distinct Roles of Brd2 and Brd4 in Potentiating the Transcriptional Program for Th17 Cell Differentiation" Mol. Cell 65, 1068-1080 (2017).

Assembly members:
entity_1, polymer, 112 residues, 13157.136 Da.
entity_2, polymer, 12 residues, 1540.808 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):
entity_1: GKLSEQLKHCNGILKELLSK KHAAYAWPFYKPVDASALGL HDYHDIIKHPMDLSTVKRKM ENRDYRDAQEFAADVRLMFS NCYKYNPPDHDVVAMARKLQ DVFEFRYAKMPD
entity_2: HNLLRIXQFLQS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
13C chemical shifts	448
15N chemical shifts	100
1H chemical shifts	834

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	2

Entities:

Entity 1, entity_1 112 residues - 13157.136 Da.

1

GLY

LYS

LEU

SER

GLU

GLN

LEU

LYS

HIS

CYS

2

ASN

GLY

ILE

LEU

LYS

GLU

LEU

SER

LYS

3

LYS

HIS

ALA

TYR

ALA

TRP

PRO

PHE

TYR

4

LYS

PRO

VAL

ASP

ALA

SER

ALA

LEU

GLY

LEU

5

HIS

ASP

TYR

HIS

ASP

ILE

LYS

HIS

PRO

6

MET

ASP

LEU

SER

THR

VAL

LYS

ARG

LYS

MET

7

GLU

ASN

ARG

ASP

TYR

ARG

ASP

ALA

GLN

GLU

8

PHE

ALA

ASP

VAL

ARG

LEU

MET

PHE

SER

9

ASN

CYS

TYR

LYS

TYR

ASN

PRO

ASP

HIS

10

ASP

VAL

ALA

MET

ALA

ARG

LYS

LEU

GLN

11

ASP

VAL

PHE

GLU

PHE

ARG

TYR

ALA

LYS

MET

12

PRO

ASP

Entity 2, entity_2 12 residues - 1540.808 Da.

1

HIS

ASN

LEU

ARG

ILE

ALY

GLN

PHE

LEU

2

GLN

SER

Samples:

sample_1: DTT, [U-2H], 2 mM; EDTA 2 mM; sodium chloride 100 mM; sodium phosphate 10 mM; entity_1 mM; entity_2 mM

sample_2: DTT, [U-2H], 2 mM; EDTA 2 mM; sodium chloride 100 mM; sodium phosphate 10 mM; entity_1 mM; entity_2 mM

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HNCOCACB	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C filtered NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C filtered NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

ARIA v2.3, Linge, O'Donoghue and Nilges - refinement

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation

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

NMRView v5.04, Johnson, One Moon Scientific - chemical shift assignment, peak picking

ProcheckNMR, Laskowski and MacArthur - data analysis

TALOS, Cornilescu, Delaglio and Bax - refinement

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz
Bruker Avance 900 MHz

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