BMRB Entry 27216

Name: Chemical shift assignments of prothymosin alpha in complex with Histone H1
Published: 2018-02-12

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27216

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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 prothymosin alpha in complex with Histone H1

Deposition date:

2017-08-14

Original release date:

2018-02-12

Authors:

Bugge, Katrine; Kragelund, Birthe; Fernandes, Catarina; 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
Histone_H1, polymer, 197 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
Histone_H1: TENSTSAPAAKPKRAKASKK STDHPKYSDMIVAAIQAEKN RAGSSRQSIQKYIKSHYKVG ENADSQIKLSIKRLVTTGVL KQTKGVGASGSFRLAKSDEP KKSVAFKKTKKEIKKVATPK KASKPKKAASKAPTKKPKAT PVKKAKKKLAATPKKAKKPK TVKAKPVKASKPKKAKPVKP KAKSSAKRAGKKKGGPR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	172
15N chemical shifts	102
1H chemical shifts	99

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Prothymosin alpha	1
2	Histone H1	2

Entities:

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

GP is leftover from cleavage from a tag, and residue numbering does not include these first two residues.

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

Entity 2, Histone H1 197 residues - Formula weight is not available

1

THR

GLU

ASN

SER

THR

SER

ALA

PRO

ALA

2

LYS

PRO

LYS

ARG

ALA

LYS

ALA

SER

LYS

3

SER

THR

ASP

HIS

PRO

LYS

TYR

SER

ASP

MET

4

ILE

VAL

ALA

ILE

GLN

ALA

GLU

LYS

ASN

5

ARG

ALA

GLY

SER

ARG

GLN

SER

ILE

GLN

6

LYS

TYR

ILE

LYS

SER

HIS

TYR

LYS

VAL

GLY

7

GLU

ASN

ALA

ASP

SER

GLN

ILE

LYS

LEU

SER

8

ILE

LYS

ARG

LEU

VAL

THR

GLY

VAL

LEU

9

LYS

GLN

THR

LYS

GLY

VAL

GLY

ALA

SER

GLY

10

SER

PHE

ARG

LEU

ALA

LYS

SER

ASP

GLU

PRO

11

LYS

SER

VAL

ALA

PHE

LYS

THR

LYS

12

LYS

GLU

ILE

LYS

VAL

ALA

THR

PRO

LYS

13

LYS

ALA

SER

LYS

PRO

LYS

ALA

SER

14

LYS

ALA

PRO

THR

LYS

PRO

LYS

ALA

THR

15

PRO

VAL

LYS

ALA

LYS

LEU

ALA

16

ALA

THR

PRO

LYS

ALA

LYS

PRO

LYS

17

THR

VAL

LYS

ALA

LYS

PRO

VAL

LYS

ALA

SER

18

LYS

PRO

LYS

ALA

LYS

PRO

VAL

LYS

PRO

19

LYS

ALA

LYS

SER

ALA

LYS

ARG

ALA

GLY

20

LYS

GLY

PRO

ARG

Samples:

sample_1: Prothymosin alpha, [U-100% 13C; U-100% 15N], 100 uM; Histone H1 80 uM; DSS 0.7 mM; D2O, [U-100% 2H], 10%; EDTA 0.1 mM; TBS buffer 165 mM; Tris-HCl 10 mM; KCl 155 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

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