BMRB Entry 27603

Name: Partial backbone assignments of Cse4 protein in 5M urea
Published: 2019-01-09

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27603

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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:

Partial backbone assignments of Cse4 protein in 5M urea

Deposition date:

2018-09-11

Original release date:

2019-01-09

Authors:

Kumar, Ashutosh; Malik, Nikita

Citation:

Citation: Malik, Nikita; Dantu, Sarath Chandra; Shukla, Shivangi; Kombrabail, Mamta; Ghosh, Santanu Kumar; Krishnamoorthy, Guruswamy; Kumar, Ashutosh. "Conformational flexibility of histone variant CENP-A" J. Biol. Chem. 293, 20273-20284 (2018).
PubMed: 30381395

Assembly members:

Assembly members:
Cse4, polymer, 229 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: pKS387

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Cse4: MSSKQQWVSSAIQSDSSGRS LSNVNRLAGDQQSINDRALS LLQRTRATKNLFPRREERRR YESSKSDLDIETDYEDQAGN LEIETENEEEAEMETEVPAP VRTHSYALDRYVRQKRREKQ RKQSLKRVEKKYTPSELALY EIRKYQRSTDLLISKIPFAR LVKEVTDEFTTKDQDLRWQS MAIMALQEASEAYLVGLLEH TNLLALHAKRITIMKKDMQL ARRIRGQFI

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	4
15N chemical shifts	65
1H chemical shifts	65

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Cse4	1

Entities:

Entity 1, Cse4 229 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

LYS

14

LYS

TYR

THR

PRO

SER

GLU

LEU

ALA

LEU

TYR

15

GLU

ILE

ARG

LYS

TYR

GLN

ARG

SER

THR

ASP

16

LEU

ILE

SER

LYS

ILE

PRO

PHE

ALA

ARG

17

LEU

VAL

LYS

GLU

VAL

THR

ASP

GLU

PHE

THR

18

THR

LYS

ASP

GLN

ASP

LEU

ARG

TRP

GLN

SER

19

MET

ALA

ILE

MET

ALA

LEU

GLN

GLU

ALA

SER

20

GLU

ALA

TYR

LEU

VAL

GLY

LEU

GLU

HIS

21

THR

ASN

LEU

ALA

LEU

HIS

ALA

LYS

ARG

22

ILE

THR

ILE

MET

LYS

ASP

MET

GLN

LEU

23

ALA

ARG

ILE

ARG

GLY

GLN

PHE

ILE

Samples:

sample_1: Cse4, [U-99% 13C; U-99% 15N], 700 uM; urea 5 M

sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

Bruker Avance 750 MHz

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