BMRB Entry 34517

Name: Structure of eIF4G1 (37-49) - PUB1 RRM3 chimera in solution
Published: 2021-05-21

Click here to enlarge.

PDB ID: 6z29
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34517
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Structure of eIF4G1 (37-49) - PUB1 RRM3 chimera in solution

Deposition date:

2020-05-15

Original release date:

2021-05-21

Authors:

Chaves-Arquero, B.; Martinez-Lumbreras, S.; Perez-Canadillas, J.

Citation:

Citation: Chaves-Arquero, B.; Martinez-Lumbreras, S.; Sibille, N.; Camero, S.; Bernardo, P.; Jimenez, M.; Zorrilla, S.; Perez-Canadillas, J.. "eIF4G1 N-terminal intrinsically disordered domain is a multi-docking station for RNA, Pab1, Pub1, and self-assembly" Front. Mol. Biosci. 9, 986121-986121 (2022).
PubMed: 36213119

Assembly members:

Assembly members:
entity_1, polymer, 116 residues, 13031.693 Da.

Natural source:

Natural source: Common Name: budding yeasts Taxonomy ID: 559292 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSGYTNYNNGSNYTQKKQTI GLPPQVNPQAVDHIIRSAPP RVTTAYIGNIPHFATEADLI PLFQNFGFILDFKHYPEKGC CFIKYDTHEQAAVCIVALAN FPFQGRNLRTGWGKER

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	351
15N chemical shifts	127
1H chemical shifts	754

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 116 residues - 13031.693 Da.

1

GLY

SER

GLY

TYR

THR

ASN

TYR

ASN

GLY

2

SER

ASN

TYR

THR

GLN

LYS

GLN

THR

ILE

3

GLY

LEU

PRO

GLN

VAL

ASN

PRO

GLN

ALA

4

VAL

ASP

HIS

ILE

ARG

SER

ALA

PRO

5

ARG

VAL

THR

ALA

TYR

ILE

GLY

ASN

ILE

6

PRO

HIS

PHE

ALA

THR

GLU

ALA

ASP

LEU

ILE

7

PRO

LEU

PHE

GLN

ASN

PHE

GLY

PHE

ILE

LEU

8

ASP

PHE

LYS

HIS

TYR

PRO

GLU

LYS

GLY

CYS

9

CYS

PHE

ILE

LYS

TYR

ASP

THR

HIS

GLU

GLN

10

ALA

VAL

CYS

ILE

VAL

ALA

LEU

ALA

ASN

11

PHE

PRO

PHE

GLN

GLY

ARG

ASN

LEU

ARG

THR

12

GLY

TRP

GLY

LYS

GLU

ARG

Samples:

sample_1: eIF4G1(37-49)/PUB1(RRM3) Chimera 250 uM; potassium phosphate 25 mM; sodium chloride 25 mM; DTT 0.1 mM

sample_2: eIF4G1(37-49)/PUB1(RRM3) Chimera 250 uM; potassium phosphate 25 mM; sodium chloride 25 mM; DTT 0.1 mM

sample_3: eIF4G1(37-49)/PUB1(RRM3) Chimera, [U-13C; U-15N], 148 uM; potassium phosphate 25 mM; sodium chloride 25 mM; DTT 0.1 mM

sample_conditions_1: ionic strength: 0.050 M; pH: 5.0; pressure: 1 atm; temperature: 301.2 K

sample_conditions_2: ionic strength: 0.050 M; pH: 5.0; pressure: 1 atm; temperature: 301.2 K

sample_conditions_3: ionic strength: 0.050 M; pH: 5.0; pressure: 1 atm; temperature: 301.2 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_3
2D 1H-13C HSQC aliphatic	sample_3	isotropic	sample_conditions_3
3D HNCO	sample_3	isotropic	sample_conditions_3
3D HNCA	sample_3	isotropic	sample_conditions_3
3D CBCA(CO)NH	sample_3	isotropic	sample_conditions_3
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_2
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_2

Software:

TopSpin, Bruker Biospin - collection, processing

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

CcpNmr Analysis, CCPN - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

Amber, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

Bruker AVANCE II 800 MHz

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