BMRB Entry 17812

Name: NMR STRUCTURE OF UHRF1 PHD DOMAINS IN A COMPLEX WITH HISTONE H3 PEPTIDE
Published: 2011-09-01

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PDB ID: 2lgk
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17812
MolProbity Validation Chart

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

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Title:

NMR STRUCTURE OF UHRF1 PHD DOMAINS IN A COMPLEX WITH HISTONE H3 PEPTIDE

Deposition date:

2011-07-28

Original release date:

2011-09-01

Authors:

Wang, Chengkun; Shen, Jie; Yang, Zhongzheng; Chen, Ping; Zhao, Bin; Hu, Wei; Lan, Wenxian; Tong, Xiaotian; Wu, Houming; Li, Guohong; Cao, Chunyang

Citation:

Citation: Wang, Chengkun; Shen, Jie; Yang, Zhongzheng; Chen, Ping; Zhao, Bin; Hu, Wei; Lan, Wenxian; Tong, Xiaotian; Wu, Houming; Li, Guohong; Cao, Chunyang. "Structural basis for site-specific reading of unmodified R2 of histone H3 tail by UHRF1 PHD finger." Cell Res. 21, 1379-1382 (2011).
PubMed: 21808299

Assembly members:

Assembly members:
entity_1, polymer, 69 residues, 7849.913 Da.
entity_2, polymer, 12 residues, 1350.580 Da.
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 Vector: pETduet

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SGPSCKHCKDDVNRLCRVCA CHLCGGRQDPDKQLMCDECD MAFHIYCLDPPLSSVPSEDE WYCPECRND
entity_2: ARTKQTARXSTG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	240
15N chemical shifts	64
1H chemical shifts	496

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
5	ZINC ION_3	3

Entities:

Entity 1, entity_1 69 residues - 7849.913 Da.

1

SER

GLY

PRO

SER

CYS

LYS

HIS

CYS

LYS

ASP

2

ASP

VAL

ASN

ARG

LEU

CYS

ARG

VAL

CYS

ALA

3

CYS

HIS

LEU

CYS

GLY

ARG

GLN

ASP

PRO

4

ASP

LYS

GLN

LEU

MET

CYS

ASP

GLU

CYS

ASP

5

MET

ALA

PHE

HIS

ILE

TYR

CYS

LEU

ASP

PRO

6

PRO

LEU

SER

VAL

PRO

SER

GLU

ASP

GLU

7

TRP

TYR

CYS

PRO

GLU

CYS

ARG

ASN

ASP

Entity 2, entity_2 12 residues - 1350.580 Da.

1

ALA

ARG

THR

LYS

GLN

THR

ALA

ARG

M3L

SER

2

THR

GLY

Entity 3, ZINC ION_1 - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 1.5 mM; entity_2 1.8 mM; H2O 90%; D2O 10%; KH2PO4 2 mM; Na2HPO4 10 mM; KCl 2.7 mM; NaCl 137 mM; DTT 3 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 atm; temperature: 293.13 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	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 HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	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 edited 15N/13C NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1

Software:

X-PLOR NIH v2.19, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

TALOS, Cornilescu, Delaglio and Bax - data analysis

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

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Varian INOVA 600 MHz

BMRB	17808 17813
PDB	2LGG 2LGK 2LGL 3ASK 3ASL 3SHB 3SOU 3SOW 3SOX 3T6R 3ZVY 3ZVZ 4GY5
DBJ	BAF36719 BAF36720 BAF82078 BAG37156
GB	AAF28469 AAI13876 AAK55744 AAV40831 ABQ59043
REF	NP_001041666 NP_001276979 NP_001276980 NP_001276981 NP_037414
SP	Q96T88
AlphaFold	Q96T88