BMRB Entry 27813

Name: Amide chemical shifts of human IMP3 RRM1-2 (1-156)
Published: 2019-03-07

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27813

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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:

Amide chemical shifts of human IMP3 RRM1-2 (1-156)

Deposition date:

2019-03-02

Original release date:

2019-03-07

Authors:

Schlundt, Andreas; Sattler, Michael; Aziz, Masood; Wagner, Jacqueline

Citation:

Citation: Schneider, Tim; Hung, Lee-Hsueh; Aziz, Masood; Wilmen, Anna; Thaum, Stephanie; Wagner, Jacqueline; Janowski, Robert; Mueller, Simon; Schreiner, Silke; Friedhoff, Peter; Huettelmaier, Stefan; Niessing, Dierk; Sattler, Michael; Schlundt, Andreas; Bindereif, Albrecht. "Combinatorial recognition of clustered RNA elements by the multidomain RNA-binding protein IMP3." Nat. Commun. 10, 2266-2266 (2019).
PubMed: 31118463

Assembly members:

Assembly members:
IMP3_(IGF2BP3)_RRM1-2, polymer, 158 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: pETTrx1a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
IMP3_(IGF2BP3)_RRM1-2: GAMAKLYIGNLSENAAPSDL ESIFKDAKIPVSGPFLVKTG YAFVDCPDESWALKAIEALS GKIELHGKPIEVEHSVPKRQ RIRKLQIRNIPPHLQWEVLD SLLVQYGVVESCEQVNTDSE TAVVNVTYSSKDQARQALDK LNGFQLENFTLKVAYIPD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	145
1H chemical shifts	145

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	IMP3 RRM1-2	1

Entities:

Entity 1, IMP3 RRM1-2 158 residues - Formula weight is not available

M=1

1

GLY

ALA

MET

ALA

LYS

LEU

TYR

ILE

GLY

ASN

2

LEU

SER

GLU

ASN

ALA

PRO

SER

ASP

LEU

3

GLU

SER

ILE

PHE

LYS

ASP

ALA

LYS

ILE

PRO

4

VAL

SER

GLY

PRO

PHE

LEU

VAL

LYS

THR

GLY

5

TYR

ALA

PHE

VAL

ASP

CYS

PRO

ASP

GLU

SER

6

TRP

ALA

LEU

LYS

ALA

ILE

GLU

ALA

LEU

SER

7

GLY

LYS

ILE

GLU

LEU

HIS

GLY

LYS

PRO

ILE

8

GLU

VAL

GLU

HIS

SER

VAL

PRO

LYS

ARG

GLN

9

ARG

ILE

ARG

LYS

LEU

GLN

ILE

ARG

ASN

ILE

10

PRO

HIS

LEU

GLN

TRP

GLU

VAL

LEU

ASP

11

SER

LEU

VAL

GLN

TYR

GLY

VAL

GLU

12

SER

CYS

GLU

GLN

VAL

ASN

THR

ASP

SER

GLU

13

THR

ALA

VAL

ASN

VAL

THR

TYR

SER

14

LYS

ASP

GLN

ALA

ARG

GLN

ALA

LEU

ASP

LYS

15

LEU

ASN

GLY

PHE

GLN

LEU

GLU

ASN

PHE

THR

16

LEU

LYS

VAL

ALA

TYR

ILE

PRO

ASP

Samples:

sample_1: IMP3 (IGF2BP3) RRM1-2, [U-99% 13C; U-99% 15N], 0.5 mM; sodium chloride 150 mM; BisTris 20 mM; sodium azide 0.02%; TCEP 2 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker - collection, processing

CCPNMR_Analysis, CCPN - chemical shift assignment, data analysis

NMR spectrometers:

Bruker Avance 800 MHz
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