BMRB Entry 27582

Name: Backbone 1H,15N Chemical Shift Assignments human Pdx1 (146-233)
Published: 2018-11-28

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27582

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:

Backbone 1H,15N Chemical Shift Assignments human Pdx1 (146-233)

Deposition date:

2018-08-21

Original release date:

2018-11-28

Authors:

Ostertag, Michael; Messias, Ana; Popowicz, Grzegorz; Sattler, Michael

Citation:

Citation: Ostertag, Michael; Messias, Ana; Sattler, Michael; Popowicz, Grzegorz. "The Structure of the SPOP-Pdx1 Interface Reveals Insights into the Phosphorylation-Dependent Binding Regulation" Structure 27, 327-334 (2019).
PubMed: 30449689

Assembly members:

Assembly members:
Pdx1, polymer, 92 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: pETM-11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Pdx1: GAMGNKRTRTAYTRAQLLEL EKEFLFNKYISRPRRVELAV MLNLTERHIKIWFQNRRMKW KKEEDKKRGGGTAVGGGGVA EPEQDCAVTSGE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	72
1H chemical shifts	72

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Pdx1 DBD-SBS	1

Entities:

Entity 1, Pdx1 DBD-SBS 92 residues - Formula weight is not available

Pdx1 starts at Asn146, previous residues are cloning artifacts

1

GLY

ALA

MET

GLY

ASN

LYS

ARG

THR

ARG

THR

2

ALA

TYR

THR

ARG

ALA

GLN

LEU

GLU

LEU

3

GLU

LYS

GLU

PHE

LEU

PHE

ASN

LYS

TYR

ILE

4

SER

ARG

PRO

ARG

VAL

GLU

LEU

ALA

VAL

5

MET

LEU

ASN

LEU

THR

GLU

ARG

HIS

ILE

LYS

6

ILE

TRP

PHE

GLN

ASN

ARG

MET

LYS

TRP

7

LYS

GLU

ASP

LYS

ARG

GLY

8

GLY

THR

ALA

VAL

GLY

VAL

ALA

9

GLU

PRO

GLU

GLN

ASP

CYS

ALA

VAL

THR

SER

10

GLY

GLU

Samples:

sample_1: Pdx1, [U-15N], 300 uM; NaCl 137 mM; KCl 2.7 mM; Na2HPO4 10 mM; KH2PO4 1.8 mM; beta-ME 5 mM

sample_conditions_1: ionic strength: 137 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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