BMRB Entry 26628

Name: assignment of HuR RRM1-2
Published: 2015-09-23

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26628

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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:

assignment of HuR RRM1-2

Deposition date:

2015-08-08

Original release date:

2015-09-23

Authors:

Wang, Zhonghua

Citation:

Citation: Wang, Zhonghua; Bhattacharya, Akash; Ivanov, Dmitri. "Identification of small-molecule inhibitors of the HuR/RNA interaction using a fluorescence polarization screening assay followed by NMR validation." PLoS One 10, e0138780-e0138780 (2015).
PubMed: 26390015

Assembly members:

Assembly members:
HuR, polymer, 193 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: Pet14b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HuR: MHHHHHHMSNGYEDHMAEDC RGDIGRTNLIVNYLPQNMTQ DELRSLFSSIGEVESAKLIR DKVAGHSLGYGFVNYVTAKD AERAINTLNGLRLQSKTIKV SYARPSSEVIKDANLYISGL PRTMTQKDVEDMFSRFGRII NSRVLVDQTTGLSRGVAFIR FDKRSEAEEAITSFNGHKPP GSSEPITVKFAAN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	153
1H chemical shifts	153

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RRM1-2	1

Entities:

Entity 1, RRM1-2 193 residues - Formula weight is not available

1

MET

HIS

MET

SER

ASN

2

GLY

TYR

GLU

ASP

HIS

MET

ALA

GLU

ASP

CYS

3

ARG

GLY

ASP

ILE

GLY

ARG

THR

ASN

LEU

ILE

4

VAL

ASN

TYR

LEU

PRO

GLN

ASN

MET

THR

GLN

5

ASP

GLU

LEU

ARG

SER

LEU

PHE

SER

ILE

6

GLY

GLU

VAL

GLU

SER

ALA

LYS

LEU

ILE

ARG

7

ASP

LYS

VAL

ALA

GLY

HIS

SER

LEU

GLY

TYR

8

GLY

PHE

VAL

ASN

TYR

VAL

THR

ALA

LYS

ASP

9

ALA

GLU

ARG

ALA

ILE

ASN

THR

LEU

ASN

GLY

10

LEU

ARG

LEU

GLN

SER

LYS

THR

ILE

LYS

VAL

11

SER

TYR

ALA

ARG

PRO

SER

GLU

VAL

ILE

12

LYS

ASP

ALA

ASN

LEU

TYR

ILE

SER

GLY

LEU

13

PRO

ARG

THR

MET

THR

GLN

LYS

ASP

VAL

GLU

14

ASP

MET

PHE

SER

ARG

PHE

GLY

ARG

ILE

15

ASN

SER

ARG

VAL

LEU

VAL

ASP

GLN

THR

16

GLY

LEU

SER

ARG

GLY

VAL

ALA

PHE

ILE

ARG

17

PHE

ASP

LYS

ARG

SER

GLU

ALA

GLU

ALA

18

ILE

THR

SER

PHE

ASN

GLY

HIS

LYS

PRO

19

GLY

SER

GLU

PRO

ILE

THR

VAL

LYS

PHE

20

ALA

ASN

Samples:

sample_1: HuR, U-100% 13C; U-100% 15N, 0.15 mM; H2O 90%; D2O 10%; Nacl 150 mM; NaPi 50 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 298 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

Software:

nmrView, Johnson, One Moon Scientific - chemical shift assignment

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

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 600 MHz

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