BMRB Entry 50539

Name: Mechanistic basis for ubiquitin modulation of a protein energy landscape
Published: 2021-03-17

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50539

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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:

Mechanistic basis for ubiquitin modulation of a protein energy landscape

Deposition date:

2020-10-28

Original release date:

2021-03-17

Authors:

Carroll, Emma; Latorraca, Naomi; Lindner, Johanna; Maguire, Brendan; Pelton, Jeff; Marqusee, Susan

Citation:

Citation: Carroll, Emma; Latorraca, Naomi; Lindner, Johanna; Maguire, Brendan; Pelton, Jeff; Marqusee, Susan. "Mechanistic basis for ubiquitin modulation of a protein energy landscape" Proc. Natl. Acad. Sci. U.S.A. 118, e2025126118-e2025126118 (2021).
PubMed: 33723075

Assembly members:

Assembly members:
entity_1, polymer, 92 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Bacillus amyloliquefaciens Taxonomy ID: 1390 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus amyloliquefaciens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pEC062

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPGRRAVINGEQIRSISDLH QTLRRELALPEYYGENLDAL WDALTGWVEYPLVLEWRQFE QSKQLTENGAESVLQVFREA RAEGCDITIILS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	123
15N chemical shifts	69
1H chemical shifts	69

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BarstarK60_AC1	1

Entities:

Entity 1, BarstarK60_AC1 92 residues - Formula weight is not available

Six mutations compared to wildtype Barstar - K1R K2R K21R K22R C40A K78R. Cloning artifact leaves GPG scar on N-terminus.

1

GLY

PRO

GLY

ARG

ALA

VAL

ILE

ASN

GLY

2

GLU

GLN

ILE

ARG

SER

ILE

SER

ASP

LEU

HIS

3

GLN

THR

LEU

ARG

GLU

LEU

ALA

LEU

PRO

4

GLU

TYR

GLY

GLU

ASN

LEU

ASP

ALA

LEU

5

TRP

ASP

ALA

LEU

THR

GLY

TRP

VAL

GLU

TYR

6

PRO

LEU

VAL

LEU

GLU

TRP

ARG

GLN

PHE

GLU

7

GLN

SER

LYS

GLN

LEU

THR

GLU

ASN

GLY

ALA

8

GLU

SER

VAL

LEU

GLN

VAL

PHE

ARG

GLU

ALA

9

ARG

ALA

GLU

GLY

CYS

ASP

ILE

THR

ILE

10

LEU

SER

Samples:

sample_1: BarstarK60, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 50 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 0.129 M; pH: 6.5; pressure: 1 bar; temperature: 298 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 HNCACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.2 - collection

CARA v1.9.1 - chemical shift assignment, data analysis

NMRPipe v8.7 - processing

NMR spectrometers:

Bruker-Biospin Inc. AV2 900 MHz