BMRB Entry 25803

Name: UBL domain of the yeast DNA damage-inducible protein homolog 1
Published: 2016-07-13

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PDB ID: 2n7e
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25803
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:

UBL domain of the yeast DNA damage-inducible protein homolog 1

Deposition date:

2015-09-09

Original release date:

2016-07-13

Authors:

Siva, Monika; Grantz Saskova, Klara; Veverka, Vaclav

Citation:

Citation: Klima, Martin; Toth, Daniel; Hexnerova, Rozalie; Baumlova, Adriana; Chalupska, Dominika; Tykvart, Jan; Rezabkova, Lenka; Sengupta, Nivedita; Man, Petr; Dubankova, Anna; Humpolickova, Jana; Nencka, Radim; Veverka, Vaclav; Balla, Tamas; Boura, Evzen. "Structural insights and in vitro reconstitution of membrane targeting and activation of human PI4KB by the ACBD3 protein" Sci. Rep. 6, 23641-23641 (2016).
PubMed: 27009356

Assembly members:

Assembly members:
entity, polymer, 86 residues, 9692.008 Da.

Natural source:

Natural source: Common Name: baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: n/a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: HIEGRHMDLTISNELTGEIY GPIEVSEDMALTDLIALLQA DCGFDKTKHDLYYNMDILDS NRTQSLKELGLKTDDLLLIR GKISNS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	360
15N chemical shifts	89
1H chemical shifts	614

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 86 residues - 9692.008 Da.

1

HIS

ILE

GLU

GLY

ARG

HIS

MET

ASP

LEU

THR

2

ILE

SER

ASN

GLU

LEU

THR

GLY

GLU

ILE

TYR

3

GLY

PRO

ILE

GLU

VAL

SER

GLU

ASP

MET

ALA

4

LEU

THR

ASP

LEU

ILE

ALA

LEU

GLN

ALA

5

ASP

CYS

GLY

PHE

ASP

LYS

THR

LYS

HIS

ASP

6

LEU

TYR

ASN

MET

ASP

ILE

LEU

ASP

SER

7

ASN

ARG

THR

GLN

SER

LEU

LYS

GLU

LEU

GLY

8

LEU

LYS

THR

ASP

LEU

ILE

ARG

9

GLY

LYS

ILE

SER

ASN

SER

Samples:

sample_1: sodium phosphate 25 mM; sodium chloride 100 mM; entity, [U-13C; U-15N], 0.4 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	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 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

YASARA, YASARA - refinement

NMR spectrometers:

Bruker Avance 600 MHz

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