BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 25740

Title: C-terminal domain of Cdc37 cochaperone   PubMed: 26400850

Deposition date: 2015-08-02 Original release date: 2015-10-05

Authors: Keramisanou, Dimitra; Dudhat, Amit; Pare, Michael

Citation: Zhang, Ziming; Keramisanou, Dimitra; Dudhat, Amit; Pare, Michael; Gelis, Ioannis. "The C-terminal domain of human Cdc37 studied by solution NMR"  J. Biomol. NMR 63, 315-321 (2015).

Assembly members:
Cdc37, polymer, 94 residues, 10197.445 Da.

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: GHMGPGGLDPVEVYESLPEE LQKCFDVKDVQMLQDAISKM DPTDAKYHMQRCIDSGLWVP NSKASEAKEGEEAGPGDPLL EAVPKTGDEKDVSV

Data sets:
Data typeCount
13C chemical shifts351
15N chemical shifts86
1H chemical shifts583

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Cdc371

Entities:

Entity 1, Cdc37 94 residues - 10197.445 Da.

Residues 285-287 represent a non-native fragment after removal of purification tag

1   GLYHISMETGLYPROGLYGLYLEUASPPRO
2   VALGLUVALTYRGLUSERLEUPROGLUGLU
3   LEUGLNLYSCYSPHEASPVALLYSASPVAL
4   GLNMETLEUGLNASPALAILESERLYSMET
5   ASPPROTHRASPALALYSTYRHISMETGLN
6   ARGCYSILEASPSERGLYLEUTRPVALPRO
7   ASNSERLYSALASERGLUALALYSGLUGLY
8   GLUGLUALAGLYPROGLYASPPROLEULEU
9   GLUALAVALPROLYSTHRGLYASPGLULYS
10   ASPVALSERVAL

Samples:

sample_1: Cdc37, [U-100% 13C; U-100% 15N], 0.3 – 0.5 mM; sodium chloride 100 mM; HEPES 50 mM; D2O, [U-100% 2H], 7%; H2O 93%; DTT 2 mM

sample_2: Cdc37, [U-100% 15N], 0.3 – 0.5 mM; sodium chloride 100 mM; HEPES 50 mM; D2O, [U-2H], 7%; H2O 93%; DTT 2 mM

sample_3: Cdc37, [U-10% 13C; U-100% 15N], 0.3 – 0.5 mM; sodium chloride 100 mM; HEPES 5 mM; D2O, [U-2H], 7%; H2O 93%; DTT 2 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2anisotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure solution

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

SPARKY, Goddard - data analysis

NMR spectrometers:

  • Varian VNMRS 800 MHz
  • Varian VNMRS 600 MHz

Related Database Links:

UNP Q16543

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