BMRB Entry 27206

Name: Centrosomin aa1090-1148
Published: 2018-01-31

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27206

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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:

Centrosomin aa1090-1148

Deposition date:

2017-08-07

Original release date:

2018-01-31

Authors:

Agard, David; Kelly, Mark; Rusan, Nassar; Bo, Huang; Keszthelyi, Bettina; Fagerstrom, Carey; Citron, Yemima

Citation:

Citation: Citron, Y Rose; Fagerstrom, Carey; Keszthelyi, Bettina; Huang, Bo; Rusan, Nasser; Kelly, Mark; Agard, David. "The centrosomin CM2 domain is a multi-functional binding domain with distinct cell cycle roles" PLoS ONE 13, e0190530-e0190530 (2018).
PubMed: 29315319

Assembly members:

Assembly members:
CM2, polymer, 63 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET51a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CM2: GPGSENAELRRKLIRTKRAF EDTYEKLRMANKAKAQVEKD IKNQILKTHNVLRNVRSNME NEL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	179
15N chemical shifts	61
1H chemical shifts	107

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Cm2	1

Entities:

Entity 1, Cm2 63 residues - Formula weight is not available

Residues 1-4 are non-native residues leftover from the protease cleavage site. Chemical shifts from residues 1 and 2 are not identified.

1

GLY

PRO

GLY

SER

GLU

ASN

ALA

GLU

LEU

ARG

2

ARG

LYS

LEU

ILE

ARG

THR

LYS

ARG

ALA

PHE

3

GLU

ASP

THR

TYR

GLU

LYS

LEU

ARG

MET

ALA

4

ASN

LYS

ALA

LYS

ALA

GLN

VAL

GLU

LYS

ASP

5

ILE

LYS

ASN

GLN

ILE

LEU

LYS

THR

HIS

ASN

6

VAL

LEU

ARG

ASN

VAL

ARG

SER

ASN

MET

GLU

7

ASN

GLU

LEU

Samples:

sample_1: sodium chloride 150 mM; Trizma 10 mM; sodium azide .02%; ammonium sulfate, [U-100% 15N], 1.25 g/L; glucose, [U-100% 13C], 2 g/L; Centrosomin, [U-100% 13C;U-100% 15N], 715 uM

sample_conditions_1: ionic strength: 0.15 M; pH: 7.2; pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
3D CBCANH	sample_1	isotropic	sample_conditions_1
3D hNcaNH	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CCPNMR, CCPN - chemical shift assignment, peak picking

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 500 MHz
Bruker Avance 800 MHz

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