BMRB Entry 27827

Name: Human IMP3 KH1-2 delta 1 amide chemical shifts
Published: 2019-03-07

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27827

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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:

Human IMP3 KH1-2 delta 1 amide chemical shifts

Deposition date:

2019-03-06

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)_KH1-2_delta1, polymer, 168 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)_KH1-2_delta1: GAMAKPCDLPLRLLVPTQFV GAIIGDDGATIRNITKQTQS KIDVHRKENAGAAEKSITIL STPEGTSAACKSILEIMHKE AQDIKFTEEIPLKILAHNNF VGRLIGKEGRNLKKIEQDTD TKITISPLQELTLYNPERTI TVKGNVETCAKAEEEIMKKI RESYENDI

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 KH1-2 delta1	1

Entities:

Entity 1, IMP3 KH1-2 delta1 168 residues - Formula weight is not available

GAMA is artefact from cloning

1

GLY

ALA

MET

ALA

LYS

PRO

CYS

ASP

LEU

PRO

2

LEU

ARG

LEU

VAL

PRO

THR

GLN

PHE

VAL

3

GLY

ALA

ILE

GLY

ASP

GLY

ALA

THR

4

ILE

ARG

ASN

ILE

THR

LYS

GLN

THR

GLN

SER

5

LYS

ILE

ASP

VAL

HIS

ARG

LYS

GLU

ASN

ALA

6

GLY

ALA

GLU

LYS

SER

ILE

THR

ILE

LEU

7

SER

THR

PRO

GLU

GLY

THR

SER

ALA

CYS

8

LYS

SER

ILE

LEU

GLU

ILE

MET

HIS

LYS

GLU

9

ALA

GLN

ASP

ILE

LYS

PHE

THR

GLU

ILE

10

PRO

LEU

LYS

ILE

LEU

ALA

HIS

ASN

PHE

11

VAL

GLY

ARG

LEU

ILE

GLY

LYS

GLU

GLY

ARG

12

ASN

LEU

LYS

ILE

GLU

GLN

ASP

THR

ASP

13

THR

LYS

ILE

THR

ILE

SER

PRO

LEU

GLN

GLU

14

LEU

THR

LEU

TYR

ASN

PRO

GLU

ARG

THR

ILE

15

THR

VAL

LYS

GLY

ASN

VAL

GLU

THR

CYS

ALA

16

LYS

ALA

GLU

ILE

MET

LYS

ILE

17

ARG

GLU

SER

TYR

GLU

ASN

ASP

ILE

Samples:

sample_1: IMP3 (IGF2BP3) KH1-2 delta1, [U-15N], 0.125 mM; BisTris 20 mM; sodium chloride 150 mM; TCEP 2 mM; sodium azide 0.02%

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

Software:

TOPSPIN, Bruker - collection, processing

CCPNMR_Analysis, CCPN - chemical shift assignment, data analysis

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz
Bruker Avance 900 MHz
Bruker Avance 950 MHz

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