BMRB Entry 27597

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for p53TAD in complex with S100A4
Published: 2022-02-02

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27597

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, 13C, and 15N Chemical Shift Assignments for p53TAD in complex with S100A4

Deposition date:

2018-09-04

Original release date:

2022-02-02

Authors:

F. Dudas, Erika; Bodor, Andrea; Sebak, Fanni

Citation:

Citation: Dudas, Erika; Palfy, Gyula; Menyhard, Dora; Sebak, Fanni; Ecsedi, Peter; Nyitray, Laszlo; Bodor, Andrea. "Tumor-Suppressor p53TAD1-60 Forms a Fuzzy Complex with Metastasis-Associated S100A4: Structural Insights and Dynamics by an NMR/MD Approach" Chembiochem 21, 3087-3095 (2020).
PubMed: 32511842

Assembly members:

Assembly members:
p53_TAD, polymer, 62 residues, Formula weight is not available
S100A4, polymer, 104 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: not known

Entity Sequences (FASTA):

Entity Sequences (FASTA):
p53_TAD: GSMEEPQSDPSVEPPLSQET FSDLWKLLPENNVLSPLPSQ AMDDLMLSPNNIEQWFTEDP GP
S100A4: GSHMACPLEKALDVMVSTFH KYSGKEGDKFKLNKSELKEL LTRELPSFLGKRTDEAAFQK LMSNLDSNRDNEVDFQEYCV FLSCIAMMCNEFFEGFPDKQ PRKK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	110
15N chemical shifts	46
1H chemical shifts	236

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	p53TAD	1
2	S100A4, chain 1	2
3	S100A4, chain 2	2

Entities:

Entity 1, p53TAD 62 residues - Formula weight is not available

Residues -1-0 represent a non-native affinity tag

1

GLY

SER

MET

GLU

PRO

GLN

SER

ASP

PRO

2

SER

VAL

GLU

PRO

LEU

SER

GLN

GLU

THR

3

PHE

SER

ASP

LEU

TRP

LYS

LEU

PRO

GLU

4

ASN

VAL

LEU

SER

PRO

LEU

PRO

SER

GLN

5

ALA

MET

ASP

LEU

MET

LEU

SER

PRO

ASN

6

ASN

ILE

GLU

GLN

TRP

PHE

THR

GLU

ASP

PRO

7

GLY

PRO

Entity 2, S100A4, chain 1 104 residues - Formula weight is not available

1

GLY

SER

HIS

MET

ALA

CYS

PRO

LEU

GLU

LYS

2

ALA

LEU

ASP

VAL

MET

VAL

SER

THR

PHE

HIS

3

LYS

TYR

SER

GLY

LYS

GLU

GLY

ASP

LYS

PHE

4

LYS

LEU

ASN

LYS

SER

GLU

LEU

LYS

GLU

LEU

5

LEU

THR

ARG

GLU

LEU

PRO

SER

PHE

LEU

GLY

6

LYS

ARG

THR

ASP

GLU

ALA

PHE

GLN

LYS

7

LEU

MET

SER

ASN

LEU

ASP

SER

ASN

ARG

ASP

8

ASN

GLU

VAL

ASP

PHE

GLN

GLU

TYR

CYS

VAL

9

PHE

LEU

SER

CYS

ILE

ALA

MET

CYS

ASN

10

GLU

PHE

GLU

GLY

PHE

PRO

ASP

LYS

GLN

11

PRO

ARG

LYS

Samples:

sample_1: p53 TAD, [U-100% 13C; U-100% 15N], 0.8 mM; S100A4 1.84 mM; MES 20 mM; sodium chloride 20 mM; TCEP 10 mM; calcium chloride 10 mM; sodium azide 3 mM; D2O, [U-2H], 50 uL; DSS 5 uL; H2O 635 uL

sample_conditions_1: ionic strength: 30 mM; pH: 5.78; pressure: 1 atm; temperature: 313 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 HNCACB	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - processing

SPARKY, Goddard - chemical shift assignment

CARA, Keller and Wuthrich - chemical shift assignment

CcpNMR, CCPN - chemical shift assignment

NMR spectrometers:

Bruker Avance 700 MHz

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