BMRB Entry 30703

Name: Solution structure of the TTD and linker region of UHRF1
Published: 2020-06-11

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PDB ID: 6ved
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30703
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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 structure of the TTD and linker region of UHRF1

Deposition date:

2019-12-31

Original release date:

2020-06-11

Authors:

Lemak, A.; Houliston, S.; Duan, S.; Ong, M.; 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, 168 residues, 19475.812 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: GLYKVNEYVDARDTNMGAWF EAQVVRVTRKAPSRDEPCSS TSRPALEEDVIYHVKYDDYP ENGVVQMNSRDVRARARTII KWQDLEVGQVVMLNYNPDNP KERGFWYDAEISRKRETRTA RELYANVVLGDDSLNDCRII FVDEVFKIERPGEGSPMVDN PMRRKSGP

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	616
15N chemical shifts	149
1H chemical shifts	1027

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 168 residues - 19475.812 Da.

1

GLY

LEU

TYR

LYS

VAL

ASN

GLU

TYR

VAL

ASP

2

ALA

ARG

ASP

THR

ASN

MET

GLY

ALA

TRP

PHE

3

GLU

ALA

GLN

VAL

ARG

VAL

THR

ARG

LYS

4

ALA

PRO

SER

ARG

ASP

GLU

PRO

CYS

SER

5

THR

SER

ARG

PRO

ALA

LEU

GLU

ASP

VAL

6

ILE

TYR

HIS

VAL

LYS

TYR

ASP

TYR

PRO

7

GLU

ASN

GLY

VAL

GLN

MET

ASN

SER

ARG

8

ASP

VAL

ARG

ALA

ARG

ALA

ARG

THR

ILE

9

LYS

TRP

GLN

ASP

LEU

GLU

VAL

GLY

GLN

VAL

10

VAL

MET

LEU

ASN

TYR

ASN

PRO

ASP

ASN

PRO

11

LYS

GLU

ARG

GLY

PHE

TRP

TYR

ASP

ALA

GLU

12

ILE

SER

ARG

LYS

ARG

GLU

THR

ARG

THR

ALA

13

ARG

GLU

LEU

TYR

ALA

ASN

VAL

LEU

GLY

14

ASP

SER

LEU

ASN

ASP

CYS

ARG

ILE

15

PHE

VAL

ASP

GLU

VAL

PHE

LYS

ILE

GLU

ARG

16

PRO

GLY

GLU

GLY

SER

PRO

MET

VAL

ASP

ASN

17

PRO

MET

ARG

LYS

SER

GLY

PRO

Samples:

sample_1: TTD-linker, [U-99% 13C; U-99% 15N], 250 uM; sodium chloride 150 mM; sodium phosphate 25 mM; DTT 5 mM; beta-mercaptoethanol 2 mM; TCEP 2 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 atm; temperature: 303 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 HNCA	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	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 HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

ABACUS, Lemak and Arrowsmith - chemical shift assignment

Sparky, Goddard - peak picking

NMR spectrometers:

Bruker AVANCE III 600 MHz
Bruker AVANCE II 800 MHz

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