BMRB Entry 52544

Name: Backbone resonance assignemnts of HUWE1 HECT domain N-lobe truncation D4141-4216
Published: 2024-07-16

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52544

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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:

Backbone resonance assignemnts of HUWE1 HECT domain N-lobe truncation D4141-4216

Deposition date:

2024-07-10

Original release date:

2024-07-16

Authors:

Zhang, Haoran; Li, Yan

Citation:

Citation: Zhang, Haoran; Li, Yan. "Backbone resonance assignemnts of HUWE1 HECT domain N-lobe truncation D4141-4216" .

Assembly members:

Assembly members:
entity_1, polymer, 195 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-28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPGSDFDVKRKYFRQELERL DEGLRKEDMAVHVRRDHVFE DSYRELHRKSPEEMKNRLYI VFEGEEGQDAGGLLREWYMI ISREMFNPMYALFRTSPGDR VTYTINPSSHCNPNHLSYFK FVGRIVAKAVYDNRLLECYF TRSFYKHILGKSGGGGSGAI RKQLAAFLEGFYEIIPKRLI SIFTEQELELLISGL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	538
15N chemical shifts	179
1H chemical shifts	179

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HUWE1 HECT domain N-lobe truncation D4141-4216	1

Entities:

Entity 1, HUWE1 HECT domain N-lobe truncation D4141-4216 195 residues - Formula weight is not available

Original residues 4141-4216 in the full-length HUWE1 HECT domain N-lobe (sequence 'VRYTDMESEDYHFYQGLVYLLENDVSTLGYDLTFSTEVQEFGVCEVRDLKPNGANILVTEENKKEYVHLVCQMRMT') was replaced with a 'GGGGS' linker in this truncated version of HUWE1 HECT domain N-lobe.

1

GLY

PRO

GLY

SER

ASP

PHE

ASP

VAL

LYS

ARG

2

LYS

TYR

PHE

ARG

GLN

GLU

LEU

GLU

ARG

LEU

3

ASP

GLU

GLY

LEU

ARG

LYS

GLU

ASP

MET

ALA

4

VAL

HIS

VAL

ARG

ASP

HIS

VAL

PHE

GLU

5

ASP

SER

TYR

ARG

GLU

LEU

HIS

ARG

LYS

SER

6

PRO

GLU

MET

LYS

ASN

ARG

LEU

TYR

ILE

7

VAL

PHE

GLU

GLY

GLU

GLY

GLN

ASP

ALA

8

GLY

LEU

ARG

GLU

TRP

TYR

MET

ILE

9

ILE

SER

ARG

GLU

MET

PHE

ASN

PRO

MET

TYR

10

ALA

LEU

PHE

ARG

THR

SER

PRO

GLY

ASP

ARG

11

VAL

THR

TYR

THR

ILE

ASN

PRO

SER

HIS

12

CYS

ASN

PRO

ASN

HIS

LEU

SER

TYR

PHE

LYS

13

PHE

VAL

GLY

ARG

ILE

VAL

ALA

LYS

ALA

VAL

14

TYR

ASP

ASN

ARG

LEU

GLU

CYS

TYR

PHE

15

THR

ARG

SER

PHE

TYR

LYS

HIS

ILE

LEU

GLY

16

LYS

SER

GLY

SER

GLY

ALA

ILE

17

ARG

LYS

GLN

LEU

ALA

PHE

LEU

GLU

GLY

18

PHE

TYR

GLU

ILE

PRO

LYS

ARG

LEU

ILE

19

SER

ILE

PHE

THR

GLU

GLN

GLU

LEU

GLU

LEU

20

LEU

ILE

SER

GLY

LEU

Samples:

sample_1: HUWE1 HECT domain N-lobe truncation D4141-4216, [U-99% 13C; U-99% 15N], 600 uM; D2O, [U-100% 2H], 5 % v/v; sodium chloride 200 mM; TRIS 20 mM; TCEP 2 mM

sample_conditions_1: ionic strength: 222.6 mM; pH: 8.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
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 HNCACO	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection

NMRPipe - processing

POKY - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker AVANCE NEO 800 MHz