BMRB Entry 52108

Name: Backbone 1H and 15N chemical shift assignments of K29-linked diubiquitin
Published: 2023-09-05

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52108

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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 1H and 15N chemical shift assignments of K29-linked diubiquitin

Deposition date:

2023-08-31

Original release date:

2023-09-05

Authors:

Kurbah, Iladeiti; Castaneda, Carlos; Fushman, David

Citation:

Citation: Kurbah, Iladeiti; Castaneda, Carlos; Fushman, David. "TBD" Biomol. NMR Assignments ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 76 residues, 8564.84 Da.

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: pET3a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MQIFVKTLTGKTITLEVEPS DTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
- assigned_chemical_shifts_2

Data type	Count
15N chemical shifts	139
1H chemical shifts	139

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ubiquitin, Chain A	1
2	ubiquitin, Chain B	1

Entities:

Entity 1, ubiquitin, Chain A 76 residues - 8564.84 Da.

K29-linked diubiquitin

1

MET

GLN

ILE

PHE

VAL

LYS

THR

LEU

THR

GLY

2

LYS

THR

ILE

THR

LEU

GLU

VAL

GLU

PRO

SER

3

ASP

THR

ILE

GLU

ASN

VAL

LYS

ALA

LYS

ILE

4

GLN

ASP

LYS

GLU

GLY

ILE

PRO

ASP

GLN

5

GLN

ARG

LEU

ILE

PHE

ALA

GLY

LYS

GLN

LEU

6

GLU

ASP

GLY

ARG

THR

LEU

SER

ASP

TYR

ASN

7

ILE

GLN

LYS

GLU

SER

THR

LEU

HIS

LEU

VAL

8

LEU

ARG

LEU

ARG

GLY

Samples:

sample_1: ubiquitin, Chain A, [U-99% 15N], 150 uM; ubiquitin, Chain B 150 uM; sodium phosphate 20 mM

sample_2: ubiquitin, Chain A 150 uM; ubiquitin, Chain B, [U-99% 15N], 150 uM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6.8; pressure: 1 atm; temperature: 296 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1

Software:

NMRFAM-SPARKY v1.470 - chemical shift assignment, peak picking

TOPSPIN v4.1.4 - processing of raw NMR data

NMR spectrometers:

Bruker AVANCE III 600 MHz