BMRB Entry 27322

Title:
C-terminal domain of Cdc37 cochaperone. Y298E phosphomimetic mutant.
Deposition date:
2017-12-03
Original release date:
2018-01-16
Authors:
Bachman, Ashleigh; Keramisanou, Dimitra; Kumar M. V., Vaasantha; Gelis, Ioannis
Citation:

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).
PubMed: 29343704

Assembly members:

Assembly members:
Cdc37_C-terminal_domain, polymer, 93 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: PDB.His.MBP

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts226
15N chemical shifts76
1H chemical shifts76

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Cdc371

Entities:

Entity 1, Cdc37 93 residues - Formula weight is not available

1   GLYMETGLYPROGLYGLYLEUASPPROVAL
2   GLUVALGLUGLUSERLEUPROGLUGLULEU
3   GLNLYSCYSPHEASPVALLYSASPVALGLN
4   METLEUGLNASPALAILESERLYSMETASP
5   PROTHRASPALALYSTYRHISMETGLNARG
6   CYSILEASPSERGLYLEUTRPVALPROASN
7   SERLYSALASERGLUALALYSGLUGLYGLU
8   GLUALAGLYPROGLYASPPROLEULEUGLU
9   ALAVALPROLYSTHRGLYASPGLULYSASP
10   VALSERVAL

Samples:

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

methyl-labeled: Cdc37 C-terminal domain, methyl-labeled, 0.5 mM

15N: 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:

NameSampleSample stateSample conditions
3D HNCA15N-13Cisotropicsample_conditions_1
3D HN(CO)CA15N-13Cisotropicsample_conditions_1
3D HNCACB15N-13Cisotropicsample_conditions_1
3D CBCA(CO)NH15N-13Cisotropicsample_conditions_1
3D 1H-15N NOESY15Nisotropicsample_conditions_1
2D 1H-15N HSQC15Nisotropicsample_conditions_1
2D 1H-13C HMQCmethyl-labeledisotropicsample_conditions_1
CH3-CH3 HMQC-NOESY-HMQCmethyl-labeledisotropicsample_conditions_1

Software:

SPARKY, T. D. Goddard and D. G. Kneller - data analysis

NMR spectrometers:

  • Agilent direct drive 800 MHz

Related Database Links:

UNP Q16543
AlphaFold Q53YA2

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