BMRB Entry 52275

Name: Backbone resonances of full-length O-Mad2 R133A
Published: 2025-05-15

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52275

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Backbone resonances of full-length O-Mad2 R133A

Deposition date:

2024-01-23

Original release date:

2025-05-15

Authors:

Yu, Conny; Fischer, Elyse; Greener, Joe; Freund, Stefan; Barford, David

Citation:

Citation: Yu, Conny; Fischer, Elyse; Greener, Joe; Yang, Jing; Zhang, Ziguo; Freund, Stefan; Barford, David. "Molecular mechanism of Mad2 conformational conversion promoted by the Mad2-interaction motif of Cdc20" Protein Sci. 34, e70099-e70099 (2025).
PubMed: 40143766

Assembly members:

Assembly members:
entity_1, polymer, 205 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MALQLSREQGITLRGSAEIV AEFFSFGINSILYQRGIYPS ETFTRVQKYGLTLLVTTDLE LIKYLNNVVEQLKDWLYKCS VQKLVVVISNIESGEVLERW QFDIECDKTAKDDSAPREKS QKAIQDEIRSVIAQITATVT FLPLLEVSCSFDLLIYTDKD LVVPEKWEESGPQFITNSEE VRLRSFTTTIHKVNSMVAYK IPVND

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	546
15N chemical shifts	190
1H chemical shifts	185

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	O-Mad2	1

Entities:

Entity 1, O-Mad2 205 residues - Formula weight is not available

1

MET

ALA

LEU

GLN

LEU

SER

ARG

GLU

GLN

GLY

2

ILE

THR

LEU

ARG

GLY

SER

ALA

GLU

ILE

VAL

3

ALA

GLU

PHE

SER

PHE

GLY

ILE

ASN

SER

4

ILE

LEU

TYR

GLN

ARG

GLY

ILE

TYR

PRO

SER

5

GLU

THR

PHE

THR

ARG

VAL

GLN

LYS

TYR

GLY

6

LEU

THR

LEU

VAL

THR

ASP

LEU

GLU

7

LEU

ILE

LYS

TYR

LEU

ASN

VAL

GLU

8

GLN

LEU

LYS

ASP

TRP

LEU

TYR

LYS

CYS

SER

9

VAL

GLN

LYS

LEU

VAL

ILE

SER

ASN

10

ILE

GLU

SER

GLY

GLU

VAL

LEU

GLU

ARG

TRP

11

GLN

PHE

ASP

ILE

GLU

CYS

ASP

LYS

THR

ALA

12

LYS

ASP

SER

ALA

PRO

ARG

GLU

LYS

SER

13

GLN

LYS

ALA

ILE

GLN

ASP

GLU

ILE

ARG

SER

14

VAL

ILE

ALA

GLN

ILE

THR

ALA

THR

VAL

THR

15

PHE

LEU

PRO

LEU

GLU

VAL

SER

CYS

SER

16

PHE

ASP

LEU

ILE

TYR

THR

ASP

LYS

ASP

17

LEU

VAL

PRO

GLU

LYS

TRP

GLU

SER

18

GLY

PRO

GLN

PHE

ILE

THR

ASN

SER

GLU

19

VAL

ARG

LEU

ARG

SER

PHE

THR

ILE

20

HIS

LYS

VAL

ASN

SER

MET

VAL

ALA

TYR

LYS

21

ILE

PRO

VAL

ASN

ASP

Samples:

sample_1: O-Mad2 FL R133A, [U-100% 15N], 100 uM; HEPES 20 mM; sodium chloride 100 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 298 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 HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	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, data analysis

NMRFAM-SPARKY - data analysis

POKY - data analysis

MARS - chemical shift assignment

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