BMRB Entry 27358

Name: DNA binding protein inhibitor ID2 in 8M urea pH2.3
Published: 2018-04-18

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27358

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:

DNA binding protein inhibitor ID2 in 8M urea pH2.3

Deposition date:

2018-01-15

Original release date:

2018-04-18

Authors:

Roschger, Cornelia; Schubert, Mario; Cabrele, Chiara

Citation:

Citation: Roschger, Cornelia; Schubert, Mario; Regl, Christof; Andosch, Ancuela; Marquez Macheda, Augusto; Berger, Thomas; Huber, Christian; Lutz-Meindl, Ursula; Cabrele, Chiara. "The Recombinant Inhibitor of DNA Binding Id2 Forms Multimeric Structures via the Helix-Loop-Helix Domain and the Nuclear Export Signal" Int. J. Mol. Sci. 19, E1105-E1105 (2018).
PubMed: 29642431

Assembly members:

Assembly members:
Id2, polymer, 134 residues, Formula weight is not available

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: pET22b+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Id2: MKAFSPVRSVRKNSLSDHSL GISRSKTPVDDPMSLLYNMN DCYSKLKELVPSIPQNKKVS KMEILQHVIDYILDLQIALD SHPTIVSLHHQRPGQNQASR TPLTTLNTDISILSLQASEF PSELMSNDSKALCG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	382
15N chemical shifts	124
1H chemical shifts	129

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Id2	1

Entities:

Entity 1, Id2 134 residues - Formula weight is not available

1

MET

LYS

ALA

PHE

SER

PRO

VAL

ARG

SER

VAL

2

ARG

LYS

ASN

SER

LEU

SER

ASP

HIS

SER

LEU

3

GLY

ILE

SER

ARG

SER

LYS

THR

PRO

VAL

ASP

4

ASP

PRO

MET

SER

LEU

TYR

ASN

MET

ASN

5

ASP

CYS

TYR

SER

LYS

LEU

LYS

GLU

LEU

VAL

6

PRO

SER

ILE

PRO

GLN

ASN

LYS

VAL

SER

7

LYS

MET

GLU

ILE

LEU

GLN

HIS

VAL

ILE

ASP

8

TYR

ILE

LEU

ASP

LEU

GLN

ILE

ALA

LEU

ASP

9

SER

HIS

PRO

THR

ILE

VAL

SER

LEU

HIS

10

GLN

ARG

PRO

GLY

GLN

ASN

GLN

ALA

SER

ARG

11

THR

PRO

LEU

THR

LEU

ASN

THR

ASP

ILE

12

SER

ILE

LEU

SER

LEU

GLN

ALA

SER

GLU

PHE

13

PRO

SER

GLU

LEU

MET

SER

ASN

ASP

SER

LYS

14

ALA

LEU

CYS

GLY

Samples:

sample_1: Id2, [U-99% 13C; U-99% 15N], 0.74 mM; urea 8 M; chloride 180 mM

sample_conditions_1: ionic strength: 180 mM; pH: 2.3; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	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 HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D (H)NCANH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - processing

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz

SP	Q02363
AlphaFold	Q02363