BMRB Entry 30705

Name: Solution structure of the PHD of mouse UHRF1 (NP95)
Published: 2020-06-11

Click here to enlarge.

PDB ID: 6vfo
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30705
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Solution structure of the PHD of mouse UHRF1 (NP95)

Deposition date:

2020-01-06

Original release date:

2020-06-11

Authors:

Lemak, A.; Houliston, S.; Duan, S.; Arrowsmith, C.

Citation:

Citation: Tauber, Maria; Kreuz, Sarah; Lemak, Alexander; Mandal, Papita; Yerkesh, Zhadyra; Veluchamy, Alaguraj; Al-Gashgari, Bothayna; Aljahani, Abrar; Cortes-Medina, Lorena; Azhibek, Dulat; Fan, Lixin; Ong, Michelle; Duan, Shili; Houliston, Scott; Arrowsmith, Cheryl; Fischle, Wolfgang. "Alternative splicing and allosteric regulation modulate the chromatin binding of UHRF1" Nucleic Acids Res. 48, 7728-7747 (2020).
PubMed: 32609811

Assembly members:

Assembly members:
entity_1, polymer, 78 residues, 8693.900 Da.
entity_ZN, non-polymer, 65.409 Da.

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SGPSCRFCKDDENKPCRKCA CHVCGGREAPEKQLLCDECD MAFHLYCLKPPLTSVPPEPE WYCPSCRTDSSEVVQAGE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	303
15N chemical shifts	71
1H chemical shifts	486

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1
2	ZN ion, 1	2
3	ZN ion, 2	2
4	ZN ion, 3	2

Entities:

Entity 1, unit_1 78 residues - 8693.900 Da.

1

SER

GLY

PRO

SER

CYS

ARG

PHE

CYS

LYS

ASP

2

ASP

GLU

ASN

LYS

PRO

CYS

ARG

LYS

CYS

ALA

3

CYS

HIS

VAL

CYS

GLY

ARG

GLU

ALA

PRO

4

GLU

LYS

GLN

LEU

CYS

ASP

GLU

CYS

ASP

5

MET

ALA

PHE

HIS

LEU

TYR

CYS

LEU

LYS

PRO

6

PRO

LEU

THR

SER

VAL

PRO

GLU

PRO

GLU

7

TRP

TYR

CYS

PRO

SER

CYS

ARG

THR

ASP

SER

8

SER

GLU

VAL

GLN

ALA

GLY

GLU

Entity 2, ZN ion, 1 - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: PHD, [U-99% 13C; U-99% 15N], 200 uM; DTT 5 mM; beta-mercaptoethanol 2 mM; TCEP 5 mM; sodium chloride 150 mM; sodium phosphate 50 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 atm; temperature: 290 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

ABACUS, Lemak and Arrowsmith - chemical shift assignment

Sparky, Goddard - peak picking

NMR spectrometers:

Bruker AVANCE II 800 MHz
Bruker AVANCE III 600 MHz

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