BMRB Entry 52264

Name: Chemical shift data from MCL1 bound to PUMA
Published: 2024-11-14

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52264

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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:

Chemical shift data from MCL1 bound to PUMA

Deposition date:

2024-01-06

Original release date:

2024-11-14

Authors:

Newcombe, Estella; Due, Amanda; Sottini, Andrea; Fernandes, Catarina; Delaforge, Elise; Schuler, Benjamin; Skriver, Karen; Olsen, Johan; Kragelund, Birthe

Citation:

Citation: Newcombe, Estella; Due, Amanda; Sottini, Andrea; Fernandes, Catarina; Delaforge, Elise; Schuler, Benjamin; Skriver, Karen; Olsen, Johan; Kragelund, Birthe. "The importance of stereochemistry in the disorder-order continuum of protein-protein interactions" .

Assembly members:

Assembly members:
entity_1, polymer, 159 residues, Formula weight is not available
entity_2, polymer, 27 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX 4T-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSEDDLYRQSLEIISRYLRE QATGSKDSKPLGEAGAAGRR ALETLRRVGDGAQRNHETAF QGMLRKLDIKNEGDVKSFSR VMVHVFKDGVTNWGRIVTLI SFGAFVAKHLKSVNQESFIE PLAETITDVLVRTKRDWLVK QRGWDGFVEFFHVQDLEGG
entity_2: EEEWAREIGAQLRRAADDLN AQYERRM

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	267
15N chemical shifts	141
1H chemical shifts	141

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MCL1	1
2	PUMA	2

Entities:

Entity 1, MCL1 159 residues - Formula weight is not available

MCL1 residues 152 - 308, with sites 150G,151S residual from TEV protease cleavage.

1

GLY

SER

GLU

ASP

LEU

TYR

ARG

GLN

SER

2

LEU

GLU

ILE

SER

ARG

TYR

LEU

ARG

GLU

3

GLN

ALA

THR

GLY

SER

LYS

ASP

SER

LYS

PRO

4

LEU

GLY

GLU

ALA

GLY

ALA

GLY

ARG

5

ALA

LEU

GLU

THR

LEU

ARG

VAL

GLY

ASP

6

GLY

ALA

GLN

ARG

ASN

HIS

GLU

THR

ALA

PHE

7

GLN

GLY

MET

LEU

ARG

LYS

LEU

ASP

ILE

LYS

8

ASN

GLU

GLY

ASP

VAL

LYS

SER

PHE

SER

ARG

9

VAL

MET

VAL

HIS

VAL

PHE

LYS

ASP

GLY

VAL

10

THR

ASN

TRP

GLY

ARG

ILE

VAL

THR

LEU

ILE

11

SER

PHE

GLY

ALA

PHE

VAL

ALA

LYS

HIS

LEU

12

LYS

SER

VAL

ASN

GLN

GLU

SER

PHE

ILE

GLU

13

PRO

LEU

ALA

GLU

THR

ILE

THR

ASP

VAL

LEU

14

VAL

ARG

THR

LYS

ARG

ASP

TRP

LEU

VAL

LYS

15

GLN

ARG

GLY

TRP

ASP

GLY

PHE

VAL

GLU

PHE

16

PHE

HIS

VAL

GLN

ASP

LEU

GLU

GLY

Entity 2, PUMA 27 residues - Formula weight is not available

PUMA peptide residues 130-156

1

GLU

TRP

ALA

ARG

GLU

ILE

GLY

ALA

2

GLN

LEU

ARG

ALA

ASP

LEU

ASN

3

ALA

GLN

TYR

GLU

ARG

MET

Samples:

sample_1: MCL1, [U-100% 13C; U-100% 15N], 250 uM; PUMA 500 uM; D2O 10%; DSS 0.25 mM; sodium phosphate 50 mM; sodium azide 0.02%

sample_conditions_1: pH: 7.00; temperature: 298 K

Experiments:

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

Software:

TOPSPIN - collection

CcpNMR - chemical shift assignment

qMDD - processing

NMRPipe - processing

NMR spectrometers:

Bruker AVANCE III 800 MHz

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