BMRB Entry 52978

Name: Backbone 1H, 13C and 15N chemical shift assignment for human E3 ubiquitin-protein ligase SH3RF1 intrinsically disordered region (260-445)
Published: 2025-11-05

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52978

NMR-STAR file interactive viewer.
NMR-STAR v3 text 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:

Backbone 1H, 13C and 15N chemical shift assignment for human E3 ubiquitin-protein ligase SH3RF1 intrinsically disordered region (260-445)

Deposition date:

2025-03-24

Original release date:

2025-11-05

Authors:

Lenette, Kjaer; Luiza, Bessa; Delaforge, Elise; Jensen, Malene

Citation:

Citation: Lenette, Kjaer; Delaforge, Elise; Jensen, Malene. "Hierarchical folding-upon-binding of an intrinsically disordered protein" Nat. Commun. ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 189 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: pEsprit

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GRRAKQLIEWDKPPVPGVDA GECSSAAAQSSTAPKHSDTK KNTKKRHSFTSLTMANKSSQ ASQNRHSMEISPPVLISSSN PTAAARISELSGLSCSAPSQ VHISTTGLIVTPPPSSPVTT GPSFTFPSDVPYQAALGTLN PPLPPPPLLAATVLASTPPG ATAAAAAAGMGPRPMAGSTD QIAHLRPQT

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	421
15N chemical shifts	151
1H chemical shifts	151

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	POSH 260-445	1

Entities:

Entity 1, POSH 260-445 189 residues - Formula weight is not available

1

GLY

ARG

ALA

LYS

GLN

LEU

ILE

GLU

TRP

2

ASP

LYS

PRO

VAL

PRO

GLY

VAL

ASP

ALA

3

GLY

GLU

CYS

SER

ALA

GLN

SER

4

SER

THR

ALA

PRO

LYS

HIS

SER

ASP

THR

LYS

5

LYS

ASN

THR

LYS

ARG

HIS

SER

PHE

THR

6

SER

LEU

THR

MET

ALA

ASN

LYS

SER

GLN

7

ALA

SER

GLN

ASN

ARG

HIS

SER

MET

GLU

ILE

8

SER

PRO

VAL

LEU

ILE

SER

ASN

9

PRO

THR

ALA

ARG

ILE

SER

GLU

LEU

10

SER

GLY

LEU

SER

CYS

SER

ALA

PRO

SER

GLN

11

VAL

HIS

ILE

SER

THR

GLY

LEU

ILE

VAL

12

THR

PRO

SER

PRO

VAL

THR

13

GLY

PRO

SER

PHE

THR

PHE

PRO

SER

ASP

VAL

14

PRO

TYR

GLN

ALA

LEU

GLY

THR

LEU

ASN

15

PRO

LEU

PRO

LEU

ALA

16

ALA

THR

VAL

LEU

ALA

SER

THR

PRO

GLY

17

ALA

THR

ALA

GLY

MET

18

GLY

PRO

ARG

PRO

MET

ALA

GLY

SER

THR

ASP

19

GLN

ILE

ALA

HIS

LEU

ARG

PRO

GLN

THR

Samples:

sample_1: POSH 260-445, [U-13C; U-15N], 500 uM; sodium phosphate 50 mM; sodium chloride 150 mM; magnesium chloride 5 mM; DTT 10 mM

sample_conditions_1: ionic strength: 0.215 M; pH: 6; pressure: 1 atm; temperature: 298.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe - processing

MARS - chemical shift assignment

SPARKY - peak picking

NMR spectrometers:

Bruker AVANCE III 600 MHz