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 26012

Title: Structural Model for the N-terminal Domain of Human Cdc37   PubMed: 27105117

Deposition date: 2016-03-23 Original release date: 2016-05-09

Authors: Zhang, Ziming; Keramisanou, Dimitra; Gelis, Ioannis

Citation: Keramisanou, Dimitra; Aboalroub, Adam; Zhang, Ziming; Liu, Wenjun; Marshall, Devon; Diviney, Andrea; Larsen, Randy; Landgraf, Ralf; Gelis, Ioannis. "Molecular Mechanism of Protein Kinase Recognition and Sorting by the Hsp90 Kinome-Specific Cochaperone Cdc37."  Mol. Cell 62, 260-271 (2016).

Assembly members:
N-Cdc37, polymer, 380 residues, 15212.184 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):
N-Cdc37: GHMVDYSVWDHIEVSDDEDE THPNIDTASLFRWRHQARVE RMEQFQKEKEELDRGCRECK RKVAECQRKLKELEVAEGGK AELERLQAEAQQLRKEERSW EQKLEEMRKKEKSMPWNVDT LSKDGFSKSMVNTKPEKTEE DSEEVREQKHKTFVEKYEKQ IKHFGMLRRWDDSQKYLSDN VHLVCEETANYLVIWCIDLE VEEKCALMEQVAHQTIVMQF ILELAKSLKVDPRACFRQFF TKIKTADRQYMEGFNDELEA FKERVRGRAKLRIEKAMKEY EEEERKKRLGPGGLDPVEVY ESLPEELQKCFDVKDVQMLQ DAISKMDPTDAKYHMQRCID SGLWVPNSKASEAKEGEEAG PGDPLLEAVPKTGDEKDVSV

Data sets:
Data typeCount
13C chemical shifts501
15N chemical shifts117
1H chemical shifts781

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 380 residues - 15212.184 Da.

Residues 1-2 represent a non-native residues after Tag removal

1   GLYHISMETVALASPTYRSERVALTRPASP
2   HISILEGLUVALSERASPASPGLUASPGLU
3   THRHISPROASNILEASPTHRALASERLEU
4   PHEARGTRPARGHISGLNALAARGVALGLU
5   ARGMETGLUGLNPHEGLNLYSGLULYSGLU
6   GLULEUASPARGGLYCYSARGGLUCYSLYS
7   ARGLYSVALALAGLUCYSGLNARGLYSLEU
8   LYSGLULEUGLUVALALAGLUGLYGLYLYS
9   ALAGLULEUGLUARGLEUGLNALAGLUALA
10   GLNGLNLEUARGLYSGLUGLUARGSERTRP
11   GLUGLNLYSLEUGLUGLUMETARGLYSLYS
12   GLULYSSERMETPROTRPASNVALASPTHR
13   LEUSERLYSASPGLYPHESERLYSSERMET
14   VALASNTHRLYSPROGLULYSTHRGLUGLU
15   ASPSERGLUGLUVALARGGLUGLNLYSHIS
16   LYSTHRPHEVALGLULYSTYRGLULYSGLN
17   ILELYSHISPHEGLYMETLEUARGARGTRP
18   ASPASPSERGLNLYSTYRLEUSERASPASN
19   VALHISLEUVALCYSGLUGLUTHRALAASN
20   TYRLEUVALILETRPCYSILEASPLEUGLU
21   VALGLUGLULYSCYSALALEUMETGLUGLN
22   VALALAHISGLNTHRILEVALMETGLNPHE
23   ILELEUGLULEUALALYSSERLEULYSVAL
24   ASPPROARGALACYSPHEARGGLNPHEPHE
25   THRLYSILELYSTHRALAASPARGGLNTYR
26   METGLUGLYPHEASNASPGLULEUGLUALA
27   PHELYSGLUARGVALARGGLYARGALALYS
28   LEUARGILEGLULYSALAMETLYSGLUTYR
29   GLUGLUGLUGLUARGLYSLYSARGLEUGLY
30   PROGLYGLYLEUASPPROVALGLUVALTYR
31   GLUSERLEUPROGLUGLULEUGLNLYSCYS
32   PHEASPVALLYSASPVALGLNMETLEUGLN
33   ASPALAILESERLYSMETASPPROTHRASP
34   ALALYSTYRHISMETGLNARGCYSILEASP
35   SERGLYLEUTRPVALPROASNSERLYSALA
36   SERGLUALALYSGLUGLYGLUGLUALAGLY
37   PROGLYASPPROLEULEUGLUALAVALPRO
38   LYSTHRGLYASPGLULYSASPVALSERVAL

Samples:

15N_labeled: N-Cdc37, [U-100% 15N], 0.5 mM; NaCl 100 mM; H2O 90%; D2O, [U-2H], 10%

methyl_labeled: N-Cdc37, U-2H; VILMA methyl 1H/13C, 0.5 mM; NaCl 100 mM; D2O, [U-2H], 100%

13C_15N_labeled: N-Cdc37, [U-100% 13C; U-100% 15N], 0.5 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 7.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15N_labeledisotropicsample_conditions_1
2D 1H-13C HMQCmethyl_labeledisotropicsample_conditions_1
3D HNCA13C_15N_labeledisotropicsample_conditions_1
3D HN(CO)CA13C_15N_labeledisotropicsample_conditions_1
3D HNCACB13C_15N_labeledisotropicsample_conditions_1
3D CBCA(CO)NH13C_15N_labeledisotropicsample_conditions_1
3D HNCO13C_15N_labeledisotropicsample_conditions_1
3D HCACO13C_15N_labeledisotropicsample_conditions_1
3D H(CCO)NH13C_15N_labeledisotropicsample_conditions_1
3D HCCH-TOCSY13C_15N_labeledisotropicsample_conditions_1
3D C(CO)NH13C_15N_labeledisotropicsample_conditions_1
3D 1H-15N NOESY15N_labeledisotropicsample_conditions_1
3D 1H-13C NOESY13C_15N_labeledisotropicsample_conditions_1
HMQC-NOESY-HMQCmethyl_labeledisotropicsample_conditions_1

Software:

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

SPARKY, Goddard - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian Uniform NMR System 600 MHz
  • Varian Uniform NMR System 800 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