BMRB Entry 27215

Name: Chemical shift assignments of free prothymosin alpha
Published: 2018-02-12

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27215

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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:

Chemical shift assignments of free prothymosin alpha

Deposition date:

2017-08-14

Original release date:

2018-02-12

Authors:

Bugge, Katrine; Fernandes, Catarina; Kragelund, Birthe; Borgia, Alessandro; Borgia, Madeleine; Heidarsson, Petur; Schuler, Benjamin

Citation:

Citation: Borgia, Alessandro; Borgia, Madeleine; Bugge, Katrine; Kissling, Vera; Heidarsson, Petur; Fernandes, Catarina; Sottini, Andrea; Soranno, Andrea; Buholzer, Karin; Nettels, Daniel; Kragelund, Birthe; Best, Robert; Schuler, Benjamin. "Extreme disorder in an ultrahigh-affinity protein complex." Nature 555, 61-66 (2018).
PubMed: 29466338

Assembly members:

Assembly members:
Prothymosin_alpha, polymer, 112 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: pET47b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Prothymosin_alpha: GPMSDAAVDTSSEITTKDLK EKKEVVEEAENGRDAPANGN ANEENGEQEADNEVDEEEEE GGEEEEEEEEGDGEEEDGDE DEEAESATGKRAAEDDEDDD VDTKKQKTDEDD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	279
15N chemical shifts	105
1H chemical shifts	169

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	free prothymosin alpha	1

Entities:

Entity 1, free prothymosin alpha 112 residues - Formula weight is not available

The N-terminal "GP" is a tag cleavage leftover which is not counted in the residue numbering (1Met).

1

GLY

PRO

MET

SER

ASP

ALA

VAL

ASP

THR

2

SER

GLU

ILE

THR

LYS

ASP

LEU

LYS

3

GLU

LYS

GLU

VAL

GLU

ALA

GLU

4

ASN

GLY

ARG

ASP

ALA

PRO

ALA

ASN

GLY

ASN

5

ALA

ASN

GLU

ASN

GLY

GLU

GLN

GLU

ALA

6

ASP

ASN

GLU

VAL

ASP

GLU

7

GLY

GLU

8

GLY

ASP

GLY

GLU

ASP

GLY

ASP

GLU

9

ASP

GLU

ALA

GLU

SER

ALA

THR

GLY

LYS

10

ARG

ALA

GLU

ASP

GLU

ASP

11

VAL

ASP

THR

LYS

GLN

LYS

THR

ASP

GLU

12

ASP

Samples:

sample_1: Prothymosin alpha, [U-100% 13C; U-100% 15N], 100 uM; Tris-HCl 10 mM; KCL 155 mM; EDTA 0.1 mM

sample_conditions_1: ionic strength: 165 mM; pH: 7.4; pressure: 1 atm; temperature: 283 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 HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)NNH	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

Ccpnmr_Analysis, CCPN - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 750 MHz
Varian INOVA 800 MHz

UNP	P06454
AlphaFold	Q15592