BMRB Entry 30177

Name: Solution NMR structure of PHF20 PHD domain in complex with a histone H3K4me2 peptide
Published: 2016-10-07

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PDB ID: 5tbn
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR30177
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 PHF20 PHD domain in complex with a histone H3K4me2 peptide

Deposition date:

2016-09-12

Original release date:

2016-10-07

Authors:

Cui, G.; Botuyan, M.; Mer, G.

Citation:

Citation: Klein, Brianna; Wang, Xiaoyan; Cui, Gaofeng; Yuan, Chao; Botuyan, Maria Victoria; Lin, Kevin; Lu, Yue; Wang, Xiaolu; Zhao, Yue; Bruns, Christiane; Mer, Georges; Shi, Xiaobing; Kutateladze, Tatiana. "PHF20 Readers Link Methylation of Histone H3K4 and p53 with H4K16 Acetylation" Cell Rep 17, 1158-1170 (2016).
PubMed: 27760318

Assembly members:

Assembly members:
entity_1, polymer, 57 residues, 6834.700 Da.
entity_2, polymer, 12 residues, 1276.490 Da.
entity_ZN, non-polymer, 65.409 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GHMDRYDFEVVRCICEVQEE NDFMIQCEECQCWQHGVCMG LLEENVPEKYTCYVCQD
entity_2: ARTXQTARKSTX

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	289
15N chemical shifts	62
1H chemical shifts	454

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
3	ZINC ION, 1	3
4	ZINC ION, 2	3

Entities:

Entity 1, entity_1 57 residues - 6834.700 Da.

1

GLY

HIS

MET

ASP

ARG

TYR

ASP

PHE

GLU

VAL

2

VAL

ARG

CYS

ILE

CYS

GLU

VAL

GLN

GLU

3

ASN

ASP

PHE

MET

ILE

GLN

CYS

GLU

CYS

4

GLN

CYS

TRP

GLN

HIS

GLY

VAL

CYS

MET

GLY

5

LEU

GLU

ASN

VAL

PRO

GLU

LYS

TYR

6

THR

CYS

TYR

VAL

CYS

GLN

ASP

Entity 2, entity_2 12 residues - 1276.490 Da.

1

ALA

ARG

THR

MLY

GLN

THR

ALA

ARG

LYS

SER

2

THR

NH2

Entity 3, ZINC ION, 1 - Zn - 65.409 Da.

1

ZN

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D NH(CA)CO	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1
3D 13C,15N-filtered, 13C/15N-edited NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_3	isotropic	sample_conditions_1
2D 1H-1H COSY	sample_3	isotropic	sample_conditions_1

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CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks

BMRB Entry 30177

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: