BMRB Entry 27381

Name: Backbone assignment of human TRIM25 PRYSPRY domain
Published: 2018-05-22

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27381

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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:

Backbone assignment of human TRIM25 PRYSPRY domain

Deposition date:

2018-01-23

Original release date:

2018-05-22

Authors:

Haubrich, Kevin; Hennig, Janosch

Citation:

Citation: Koliopoulos, Marios; Lethier, Mathilde; van der Veen, Annemarthe; Haubrich, Kevin; Hennig, Janosch; Kowalinski, Eva; Stevens, Rebecca; Martin, Stephen; Reis e Sousa, Caetano; Cusack, Stephen; Rittinger, Katrin. "Molecular mechanism of influenza A NS1-mediated TRIM25 recognition and inhibition" Nat. Commun. 9, 1820-1820 (2018).
PubMed: 29739942

Assembly members:

Assembly members:
TRIM25_PRYSPRY, polymer, 194 residues, 22.2 Da.

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: pETm22

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TRIM25_PRYSPRY: GPKVLETFLAKSRPELLEYY IKVILDYNTAHNKVALSECY TVASVAEMPQNYRPHPQRFT YCSQVLGLHCYKKGIHYWEV ELQKNNFCGVGICYGSMNRQ GPESRLGRNSASWCVEWFNT KISAWHNNVEKTLPSTKATR VGVLLNCDHGFVIFFAVADK VHLMYKFRVDFTEALYPAFW VFSAGATLSICSPK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	335
15N chemical shifts	175
1H chemical shifts	175

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PRYSPRY	1

Entities:

Entity 1, PRYSPRY 194 residues - 22.2 Da.

GP artifact of precision protease cleavage. Native sequence corresonds to TRIM25 439-630

1

GLY

PRO

LYS

VAL

LEU

GLU

THR

PHE

LEU

ALA

2

LYS

SER

ARG

PRO

GLU

LEU

GLU

TYR

3

ILE

LYS

VAL

ILE

LEU

ASP

TYR

ASN

THR

ALA

4

HIS

ASN

LYS

VAL

ALA

LEU

SER

GLU

CYS

TYR

5

THR

VAL

ALA

SER

VAL

ALA

GLU

MET

PRO

GLN

6

ASN

TYR

ARG

PRO

HIS

PRO

GLN

ARG

PHE

THR

7

TYR

CYS

SER

GLN

VAL

LEU

GLY

LEU

HIS

CYS

8

TYR

LYS

GLY

ILE

HIS

TYR

TRP

GLU

VAL

9

GLU

LEU

GLN

LYS

ASN

PHE

CYS

GLY

VAL

10

GLY

ILE

CYS

TYR

GLY

SER

MET

ASN

ARG

GLN

11

GLY

PRO

GLU

SER

ARG

LEU

GLY

ARG

ASN

SER

12

ALA

SER

TRP

CYS

VAL

GLU

TRP

PHE

ASN

THR

13

LYS

ILE

SER

ALA

TRP

HIS

ASN

VAL

GLU

14

LYS

THR

LEU

PRO

SER

THR

LYS

ALA

THR

ARG

15

VAL

GLY

VAL

LEU

ASN

CYS

ASP

HIS

GLY

16

PHE

VAL

ILE

PHE

ALA

VAL

ALA

ASP

LYS

17

VAL

HIS

LEU

MET

TYR

LYS

PHE

ARG

VAL

ASP

18

PHE

THR

GLU

ALA

LEU

TYR

PRO

ALA

PHE

TRP

19

VAL

PHE

SER

ALA

GLY

ALA

THR

LEU

SER

ILE

20

CYS

SER

PRO

LYS

Samples:

sample_1: TRIM25 PRYSPRY, [U-99% 13C; U-99% 15N], 0.45 ± 0.05 mM; sodium phosphate 20 mM; sodium chloride 150 mM; TCEP 0.2 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 170 mM; pH: 6.5; pressure: 1 atm; temperature: 289 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

Software:

Cara v1.8.4, Keller and Wuthrich - chemical shift assignment, peak picking

NMRPipe v8.7, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN v2.1, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 800 MHz

UNP	Q14258
AlphaFold	Q14258