BMRB Entry 27937

Name: NMR backbone assignment of full-length human 4E-BP1 I15A F114A mutant
Published: 2021-04-21

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27937

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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:

NMR backbone assignment of full-length human 4E-BP1 I15A F114A mutant

Deposition date:

2019-06-06

Original release date:

2021-04-21

Authors:

Boehm, Raphael; Hiller, Sebastian

Citation:

Citation: Boehm, Raphael; Imseng, Stefan; Jakob, Roman; Hall, Michael; Maier, Timm; Hiller, Sebastian. "The dynamic mechanism of 4E-BP1 recognition and phosphorylation by mTORC1" Mol. Cell 81, 2403-2416 (2021).
PubMed: 33852892

Assembly members:

Assembly members:
4E-BP1, polymer, 119 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: pET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
4E-BP1: GMSGGSSCSQTPSRAAPATR RVVLGDGVQLPPGDYSTTPG GTLFSTTPGGTRIIYDRKFL MECRNSPVTKTPPRDLPTIP GVTSPSSDEPPMEASQSHLR NSPEDKRAGGEESQAEMDI

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	193
15N chemical shifts	89
1H chemical shifts	89

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	4E-BP1	1

Entities:

Entity 1, 4E-BP1 119 residues - Formula weight is not available

Residue 1 is non-native

1

GLY

MET

SER

GLY

SER

CYS

SER

GLN

2

THR

PRO

SER

ARG

ALA

PRO

ALA

THR

ARG

3

ARG

VAL

LEU

GLY

ASP

GLY

VAL

GLN

LEU

4

PRO

GLY

ASP

TYR

SER

THR

PRO

GLY

5

GLY

THR

LEU

PHE

SER

THR

PRO

GLY

6

THR

ARG

ILE

TYR

ASP

ARG

LYS

PHE

LEU

7

MET

GLU

CYS

ARG

ASN

SER

PRO

VAL

THR

LYS

8

THR

PRO

ARG

ASP

LEU

PRO

THR

ILE

PRO

9

GLY

VAL

THR

SER

PRO

SER

ASP

GLU

PRO

10

PRO

MET

GLU

ALA

SER

GLN

SER

HIS

LEU

ARG

11

ASN

SER

PRO

GLU

ASP

LYS

ARG

ALA

GLY

12

GLU

SER

GLN

ALA

GLU

MET

ASP

ILE

Samples:

sample_1: 4E-BP1, [U-99% 13C; U-99% 15N], 250 uM; sodium phosphate 30 mM; sodium chloride 160 mM; EDTA 1 mM; DTT 10 mM

sample_conditions_1: ionic strength: 0.19 M; pH: 6; pressure: 1 atm; temperature: 293.15 K

Experiments:

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

Software:

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

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

NMR spectrometers:

Bruker Avance 700 MHz

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