BMRB Entry 27324

Name: C-terminal domain of Cdc37 co-chaperone, unfolded in the presence of 8M Urea.
Published: 2018-01-16

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27324

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

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Title: C-terminal domain of Cdc37 co-chaperone, unfolded in the presence of 8M Urea. PubMed: 29343704

Deposition date: 2017-12-03 Original release date: 2018-01-16

Authors: Bachman, Ashleigh; Keramisanou, Dimitra; Kumar M. V., Vasantha; Gelis, Ioannis

Citation: Bachman, Ashleigh; Keramisanou, Dimitra; Xu, Wanping; Beebe, Kristin; Moses, Michael; Vasantha Kumar, M; Gray, Geoffrey; Noor, Radwan Ebna; van der Vaart, Arjan; Neckers, Len; Gelis, Ioannis. "Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation" Nat. Commun. 9, 265-265 (2018).

Assembly members:
Cdc37, polymer, 93 residues, Formula weight is not available

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
Cdc37: GMGPGGLDPVEVYESLPEEL QKCFDVKDVQMLQDAISKMD PTDAKYHMQRCIDSGLWVPN SKASEAKEGEEAGPGDPLLE AVPKTGDEKDVSV

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	163
15N chemical shifts	75
1H chemical shifts	75

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	C-terminal domain of Cdc37	1

Entities:

Entity 1, C-terminal domain of Cdc37 93 residues - Formula weight is not available

1

GLY

MET

GLY

PRO

GLY

LEU

ASP

PRO

VAL

2

GLU

VAL

TYR

GLU

SER

LEU

PRO

GLU

LEU

3

GLN

LYS

CYS

PHE

ASP

VAL

LYS

ASP

VAL

GLN

4

MET

LEU

GLN

ASP

ALA

ILE

SER

LYS

MET

ASP

5

PRO

THR

ASP

ALA

LYS

TYR

HIS

MET

GLN

ARG

6

CYS

ILE

ASP

SER

GLY

LEU

TRP

VAL

PRO

ASN

7

SER

LYS

ALA

SER

GLU

ALA

LYS

GLU

GLY

GLU

8

GLU

ALA

GLY

PRO

GLY

ASP

PRO

LEU

GLU

9

ALA

VAL

PRO

LYS

THR

GLY

ASP

GLU

LYS

ASP

10

VAL

SER

VAL

Samples:

sample_2: Cdc37, [U-100% 13C; U-100% 15N], 0.5 mM

sample_1: Cdc37, [U-100% 15N], 0.5 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7.5; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Agilent direct drive 800 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts