BMRB Entry 26012

Name: Structural Model for the N-terminal Domain of Human Cdc37
Published: 2016-05-09

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PDB ID: 2nca
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26012
MolProbity Validation Chart

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	501
15N chemical shifts	117
1H chemical shifts	781

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 380 residues - 15212.184 Da.

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

1	GLY	HIS	MET	VAL	ASP	TYR	SER	VAL	TRP	ASP
2	HIS	ILE	GLU	VAL	SER	ASP	ASP	GLU	ASP	GLU
3	THR	HIS	PRO	ASN	ILE	ASP	THR	ALA	SER	LEU
4	PHE	ARG	TRP	ARG	HIS	GLN	ALA	ARG	VAL	GLU
5	ARG	MET	GLU	GLN	PHE	GLN	LYS	GLU	LYS	GLU
6	GLU	LEU	ASP	ARG	GLY	CYS	ARG	GLU	CYS	LYS
7	ARG	LYS	VAL	ALA	GLU	CYS	GLN	ARG	LYS	LEU
8	LYS	GLU	LEU	GLU	VAL	ALA	GLU	GLY	GLY	LYS
9	ALA	GLU	LEU	GLU	ARG	LEU	GLN	ALA	GLU	ALA
10	GLN	GLN	LEU	ARG	LYS	GLU	GLU	ARG	SER	TRP
11	GLU	GLN	LYS	LEU	GLU	GLU	MET	ARG	LYS	LYS
12	GLU	LYS	SER	MET	PRO	TRP	ASN	VAL	ASP	THR
13	LEU	SER	LYS	ASP	GLY	PHE	SER	LYS	SER	MET
14	VAL	ASN	THR	LYS	PRO	GLU	LYS	THR	GLU	GLU
15	ASP	SER	GLU	GLU	VAL	ARG	GLU	GLN	LYS	HIS
16	LYS	THR	PHE	VAL	GLU	LYS	TYR	GLU	LYS	GLN
17	ILE	LYS	HIS	PHE	GLY	MET	LEU	ARG	ARG	TRP
18	ASP	ASP	SER	GLN	LYS	TYR	LEU	SER	ASP	ASN
19	VAL	HIS	LEU	VAL	CYS	GLU	GLU	THR	ALA	ASN
20	TYR	LEU	VAL	ILE	TRP	CYS	ILE	ASP	LEU	GLU
21	VAL	GLU	GLU	LYS	CYS	ALA	LEU	MET	GLU	GLN
22	VAL	ALA	HIS	GLN	THR	ILE	VAL	MET	GLN	PHE
23	ILE	LEU	GLU	LEU	ALA	LYS	SER	LEU	LYS	VAL
24	ASP	PRO	ARG	ALA	CYS	PHE	ARG	GLN	PHE	PHE
25	THR	LYS	ILE	LYS	THR	ALA	ASP	ARG	GLN	TYR
26	MET	GLU	GLY	PHE	ASN	ASP	GLU	LEU	GLU	ALA
27	PHE	LYS	GLU	ARG	VAL	ARG	GLY	ARG	ALA	LYS
28	LEU	ARG	ILE	GLU	LYS	ALA	MET	LYS	GLU	TYR
29	GLU	GLU	GLU	GLU	ARG	LYS	LYS	ARG	LEU	GLY
30	PRO	GLY	GLY	LEU	ASP	PRO	VAL	GLU	VAL	TYR
31	GLU	SER	LEU	PRO	GLU	GLU	LEU	GLN	LYS	CYS
32	PHE	ASP	VAL	LYS	ASP	VAL	GLN	MET	LEU	GLN
33	ASP	ALA	ILE	SER	LYS	MET	ASP	PRO	THR	ASP
34	ALA	LYS	TYR	HIS	MET	GLN	ARG	CYS	ILE	ASP
35	SER	GLY	LEU	TRP	VAL	PRO	ASN	SER	LYS	ALA
36	SER	GLU	ALA	LYS	GLU	GLY	GLU	GLU	ALA	GLY
37	PRO	GLY	ASP	PRO	LEU	LEU	GLU	ALA	VAL	PRO
38	LYS	THR	GLY	ASP	GLU	LYS	ASP	VAL	SER	VAL

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	15N_labeled	isotropic	sample_conditions_1
2D 1H-13C HMQC	methyl_labeled	isotropic	sample_conditions_1
3D HNCA	13C_15N_labeled	isotropic	sample_conditions_1
3D HN(CO)CA	13C_15N_labeled	isotropic	sample_conditions_1
3D HNCACB	13C_15N_labeled	isotropic	sample_conditions_1
3D CBCA(CO)NH	13C_15N_labeled	isotropic	sample_conditions_1
3D HNCO	13C_15N_labeled	isotropic	sample_conditions_1
3D HCACO	13C_15N_labeled	isotropic	sample_conditions_1
3D H(CCO)NH	13C_15N_labeled	isotropic	sample_conditions_1
3D HCCH-TOCSY	13C_15N_labeled	isotropic	sample_conditions_1
3D C(CO)NH	13C_15N_labeled	isotropic	sample_conditions_1
3D 1H-15N NOESY	15N_labeled	isotropic	sample_conditions_1
3D 1H-13C NOESY	13C_15N_labeled	isotropic	sample_conditions_1
HMQC-NOESY-HMQC	methyl_labeled	isotropic	sample_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

Biological Magnetic Resonance Data Bank