BMRB Entry 50602

Name: Backbone assignment for human Mad1-CTD (597-718)
Published: 2021-04-01

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50602

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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 assignment for human Mad1-CTD (597-718)

Deposition date:

2020-11-30

Original release date:

2021-04-01

Authors:

Fischer, Elyse; Yu, Conny; Bellini, Dom; McLaughlin, Stephen; Orr, Christian; Wagner, Armin; Freund, Stefan; Barford, David

Citation:

Citation: Fischer, Elyse; Yu, Conny; Bellini, Dom; McLaughlin, Stephen; Orr, Christian; Wagner, Armin; Freund, Stefan; Barford, David. "Molecular mechanism of Mad1 kinetochore targeting by phosphorylated Bub1" EMBO Reports 19, e52242-e52242 (2021).
PubMed: 34013668

Assembly members:

Assembly members:
entity_1, polymer, 122 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: pRSFDuet-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SSKEVAELKKQVESAELKNQ RLKEVFQTKIQEFRKACYTL TGYQIDITTENQYRLTSLYA EHPGDCLIFKATSPSGSKMQ LLETEFSHTVGELIEVHLRR QDSIPAFLSSLTLELFSRQT VA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	339
15N chemical shifts	112
1H chemical shifts	112

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Mad1-CTD	1

Entities:

Entity 1, Mad1-CTD 122 residues - Formula weight is not available

1

SER

LYS

GLU

VAL

ALA

GLU

LEU

LYS

2

GLN

VAL

GLU

SER

ALA

GLU

LEU

LYS

ASN

GLN

3

ARG

LEU

LYS

GLU

VAL

PHE

GLN

THR

LYS

ILE

4

GLN

GLU

PHE

ARG

LYS

ALA

CYS

TYR

THR

LEU

5

THR

GLY

TYR

GLN

ILE

ASP

ILE

THR

GLU

6

ASN

GLN

TYR

ARG

LEU

THR

SER

LEU

TYR

ALA

7

GLU

HIS

PRO

GLY

ASP

CYS

LEU

ILE

PHE

LYS

8

ALA

THR

SER

PRO

SER

GLY

SER

LYS

MET

GLN

9

LEU

GLU

THR

GLU

PHE

SER

HIS

THR

VAL

10

GLY

GLU

LEU

ILE

GLU

VAL

HIS

LEU

ARG

11

GLN

ASP

SER

ILE

PRO

ALA

PHE

LEU

SER

12

LEU

THR

LEU

GLU

LEU

PHE

SER

ARG

GLN

THR

13

VAL

ALA

Samples:

sample_1: Mad1-CTD, [U-13C; U-15N; U-2H], 100 uM; HEPES 50 mM; sodium chloride 100 mM; TCEP 2 mM; sodium azide 0.02%

sample_conditions_1: pH: 7.0; 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 HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	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 HN(COCA)NNH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.6.1 - collection, processing

NMRFAM-SPARKY v1.47 - chemical shift assignment, data analysis, peak picking

MddNMR - processing

MARS - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 800 MHz
Bruker AVANCE III 600 MHz

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