BMRB Entry 27669

Name: Amide chemical shifts of full-length human HuR
Published: 2018-11-14

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27669

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Amide chemical shifts of full-length human HuR

Deposition date:

2018-10-30

Original release date:

2018-11-14

Authors:

Sattler, Michael; Schlundt, Andreas; Pabis, Marta; Popowicz, Grzegorz

Citation:

Citation: Pabis, Marta; Popowicz, Grzegorz; Stehle, Ralf; Fernandez-Ramos, David; Asami, Sam; Warner, Lisa; Garcia-Maurino, Sofia; Schlundt, Andreas; Martinez-Chantar, Maria; Diaz-Moreno, Irene; Sattler, Michael. "HuR biological function involves RRM3-mediated dimerization and RNA binding by all three RRMs." Nucleic Acids Res. 47, 1011-1029 (2019).
PubMed: 30418581

Assembly members:

Assembly members:
HuR_FL, polymer, 329 residues, 36317.13 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: pETM44

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HuR_FL: GPMASNGYEDHMAEDCRGDI GRTNLIVNYLPQNMTQDELR SLFSSIGEVESAKLIRDKVA GHSLGYGFVNYVTAKDAERA INTLNGLRLQSKTIKVSYAR PSSEVIKDANLYISGLPRTM TQKDVEDMFSRFGRIINSRV LVDQTTGLSRGVAFIRFDKR SEAEEAITSFNGHKPPGSSE PITVKFAANPNQNKNVALLS QLYHSPARRFGGPVHHQAQR FRFSPMGVDHMSGLSGVNVP GNASSGWCIFIYNLGQDADE GILWQMFGPFGAVTNVKVIR DFNTNKCKGFGFVTMTNYEE AAMAIASLNGYRLGDKILQV SFKTNKSHK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	212
1H chemical shifts	212

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HuR FL	1

Entities:

Entity 1, HuR FL 329 residues - 36317.13 Da.

GPMA is from cloning

1

GLY

PRO

MET

ALA

SER

ASN

GLY

TYR

GLU

ASP

2

HIS

MET

ALA

GLU

ASP

CYS

ARG

GLY

ASP

ILE

3

GLY

ARG

THR

ASN

LEU

ILE

VAL

ASN

TYR

LEU

4

PRO

GLN

ASN

MET

THR

GLN

ASP

GLU

LEU

ARG

5

SER

LEU

PHE

SER

ILE

GLY

GLU

VAL

GLU

6

SER

ALA

LYS

LEU

ILE

ARG

ASP

LYS

VAL

ALA

7

GLY

HIS

SER

LEU

GLY

TYR

GLY

PHE

VAL

ASN

8

TYR

VAL

THR

ALA

LYS

ASP

ALA

GLU

ARG

ALA

9

ILE

ASN

THR

LEU

ASN

GLY

LEU

ARG

LEU

GLN

10

SER

LYS

THR

ILE

LYS

VAL

SER

TYR

ALA

ARG

11

PRO

SER

GLU

VAL

ILE

LYS

ASP

ALA

ASN

12

LEU

TYR

ILE

SER

GLY

LEU

PRO

ARG

THR

MET

13

THR

GLN

LYS

ASP

VAL

GLU

ASP

MET

PHE

SER

14

ARG

PHE

GLY

ARG

ILE

ASN

SER

ARG

VAL

15

LEU

VAL

ASP

GLN

THR

GLY

LEU

SER

ARG

16

GLY

VAL

ALA

PHE

ILE

ARG

PHE

ASP

LYS

ARG

17

SER

GLU

ALA

GLU

ALA

ILE

THR

SER

PHE

18

ASN

GLY

HIS

LYS

PRO

GLY

SER

GLU

19

PRO

ILE

THR

VAL

LYS

PHE

ALA

ASN

PRO

20

ASN

GLN

ASN

LYS

ASN

VAL

ALA

LEU

SER

21

GLN

LEU

TYR

HIS

SER

PRO

ALA

ARG

PHE

22

GLY

PRO

VAL

HIS

GLN

ALA

GLN

ARG

23

PHE

ARG

PHE

SER

PRO

MET

GLY

VAL

ASP

HIS

24

MET

SER

GLY

LEU

SER

GLY

VAL

ASN

VAL

PRO

25

GLY

ASN

ALA

SER

GLY

TRP

CYS

ILE

PHE

26

ILE

TYR

ASN

LEU

GLY

GLN

ASP

ALA

ASP

GLU

27

GLY

ILE

LEU

TRP

GLN

MET

PHE

GLY

PRO

PHE

28

GLY

ALA

VAL

THR

ASN

VAL

LYS

VAL

ILE

ARG

29

ASP

PHE

ASN

THR

ASN

LYS

CYS

LYS

GLY

PHE

30

GLY

PHE

VAL

THR

MET

THR

ASN

TYR

GLU

31

ALA

MET

ALA

ILE

ALA

SER

LEU

ASN

GLY

32

TYR

ARG

LEU

GLY

ASP

LYS

ILE

LEU

GLN

VAL

33

SER

PHE

LYS

THR

ASN

LYS

SER

HIS

LYS

Samples:

sample_1: HuR FL, [U-15N; U-2H], 20 uM; sodium phosphate 20 mM; sodium chloride 200 mM; DTT, [U-2H], 5 mM; EDTA 1 mM

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CCPNMR_Analysis v2.4, CCPN - chemical shift assignment

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

NMR spectrometers:

Bruker Avance 800 MHz

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