BMRB Entry 51203

Name: Backbone resonance assignment of budding yeast Centromeric H3 variant Cse4 N-terminus
Published: 2024-03-08

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51203

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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 resonance assignment of budding yeast Centromeric H3 variant Cse4 N-terminus

Deposition date:

2021-12-01

Original release date:

2024-03-08

Authors:

Shukla, Shivangi; Bhattacharya, Anusri; Kumar, Ashutosh

Citation:

Citation: Shukla, Shivangi; Bhattacharya, Anusri; Kumar, Ashutosh. "Disorder in CENP-ACse4 tail-chaperone interaction facilitates binding with Ame1/Okp1 at the kinetochore STRUCTURE-D-23-00019R7" Structure ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 129 residues, Formula weight is not available

Natural source:

Natural source: Common Name: baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX6p1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MSSKQQWVSSAIQSDSSGRS LSNVNRLAGDQQSINDRALS LLQRTRATKNLFPRREERRR YESSKSDLDIETDYEDQAGN LEIETENEEEAEMETEVPAP VRTHSYALDRYVRQKRREKQ RKQSLKRVE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	204
15N chemical shifts	86
1H chemical shifts	86

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Cse4 N-terminus	1

Entities:

Entity 1, Cse4 N-terminus 129 residues - Formula weight is not available

1

MET

SER

LYS

GLN

TRP

VAL

SER

2

ALA

ILE

GLN

SER

ASP

SER

GLY

ARG

SER

3

LEU

SER

ASN

VAL

ASN

ARG

LEU

ALA

GLY

ASP

4

GLN

SER

ILE

ASN

ASP

ARG

ALA

LEU

SER

5

LEU

GLN

ARG

THR

ARG

ALA

THR

LYS

ASN

6

LEU

PHE

PRO

ARG

GLU

ARG

7

TYR

GLU

SER

LYS

SER

ASP

LEU

ASP

ILE

8

GLU

THR

ASP

TYR

GLU

ASP

GLN

ALA

GLY

ASN

9

LEU

GLU

ILE

GLU

THR

GLU

ASN

GLU

10

ALA

GLU

MET

GLU

THR

GLU

VAL

PRO

ALA

PRO

11

VAL

ARG

THR

HIS

SER

TYR

ALA

LEU

ASP

ARG

12

TYR

VAL

ARG

GLN

LYS

ARG

GLU

LYS

GLN

13

ARG

LYS

GLN

SER

LEU

LYS

ARG

VAL

GLU

Samples:

sample_1: sodium phosphate 20 mM; sodium chloride 150 mM; EDTA 1 mM; Cse4 N-terminus, [U-100% 13C; U-100% 15N], 0.8 mM

sample_conditions_1: pH: 7.4; 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 HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNN	sample_1	isotropic	sample_conditions_1

Software:

NMRFAM-SPARKY v1.470 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 750 MHz

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