BMRB Entry 50031

Name: CDC25B-R482A
Published: 2019-10-29

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50031

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

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Title: CDC25B-R482A PubMed: 31738549

Deposition date: 2019-10-04 Original release date: 2019-10-29

Authors: Reis, Andre

Citation: Reis, Andre; Sayegh, Raphael; Marana, Sandro; Arantes, Guilherme. "Combining free energy simulations and NMR chemical-shift perturbation to identify transient cation-pi contacts in proteins" J. Chem. Inf. Model. 60, 890-897 (2020).

Assembly members:
entity_1, polymer, 200 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 Vector: pET-28a

Entity Sequences (FASTA):
entity_1: GSMEFQSDHRELIGDYSKAF LLQTVDGKHQDLKYISPETM VALLTGKFSNIVDKFVIVDC RYPYEYEGGHIKTAVNLPLE RDAESFLLKSPIAPCSLDKR VILIFHCEFSSERGPAMCRF IRERDRAVNDYPSLYYPEMY ILKGGYKEFFPQHPNFCEPQ DYRPMNHEAFKDELKTFRLK TRSWAGERSRRELCSRLQDQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	146
1H chemical shifts	146

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CDC25B-R482A	1

Entities:

Entity 1, CDC25B-R482A 200 residues - Formula weight is not available

1	GLY	SER	MET	GLU	PHE	GLN	SER	ASP	HIS	ARG
2	GLU	LEU	ILE	GLY	ASP	TYR	SER	LYS	ALA	PHE
3	LEU	LEU	GLN	THR	VAL	ASP	GLY	LYS	HIS	GLN
4	ASP	LEU	LYS	TYR	ILE	SER	PRO	GLU	THR	MET
5	VAL	ALA	LEU	LEU	THR	GLY	LYS	PHE	SER	ASN
6	ILE	VAL	ASP	LYS	PHE	VAL	ILE	VAL	ASP	CYS
7	ARG	TYR	PRO	TYR	GLU	TYR	GLU	GLY	GLY	HIS
8	ILE	LYS	THR	ALA	VAL	ASN	LEU	PRO	LEU	GLU
9	ARG	ASP	ALA	GLU	SER	PHE	LEU	LEU	LYS	SER
10	PRO	ILE	ALA	PRO	CYS	SER	LEU	ASP	LYS	ARG
11	VAL	ILE	LEU	ILE	PHE	HIS	CYS	GLU	PHE	SER
12	SER	GLU	ARG	GLY	PRO	ALA	MET	CYS	ARG	PHE
13	ILE	ARG	GLU	ARG	ASP	ARG	ALA	VAL	ASN	ASP
14	TYR	PRO	SER	LEU	TYR	TYR	PRO	GLU	MET	TYR
15	ILE	LEU	LYS	GLY	GLY	TYR	LYS	GLU	PHE	PHE
16	PRO	GLN	HIS	PRO	ASN	PHE	CYS	GLU	PRO	GLN
17	ASP	TYR	ARG	PRO	MET	ASN	HIS	GLU	ALA	PHE
18	LYS	ASP	GLU	LEU	LYS	THR	PHE	ARG	LEU	LYS
19	THR	ARG	SER	TRP	ALA	GLY	GLU	ARG	SER	ARG
20	ARG	GLU	LEU	CYS	SER	ARG	LEU	GLN	ASP	GLN

Samples:

sample_1: entity_1, [U-100% 15N], 0.2 mM; NaH2PO4 20 mM; NaCl 50 mM; BMER 5 mM; dithiotreitol 2 mM

sample_conditions_1: ionic strength: 0.075 M; pH: 6.7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

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

NMR spectrometers:

Bruker AIII 800 MHz

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

1	GLY	SER	MET	GLU	PHE	GLN	SER	ASP	HIS	ARG
2	GLU	LEU	ILE	GLY	ASP	TYR	SER	LYS	ALA	PHE
3	LEU	LEU	GLN	THR	VAL	ASP	GLY	LYS	HIS	GLN
4	ASP	LEU	LYS	TYR	ILE	SER	PRO	GLU	THR	MET
5	VAL	ALA	LEU	LEU	THR	GLY	LYS	PHE	SER	ASN
6	ILE	VAL	ASP	LYS	PHE	VAL	ILE	VAL	ASP	CYS
7	ARG	TYR	PRO	TYR	GLU	TYR	GLU	GLY	GLY	HIS
8	ILE	LYS	THR	ALA	VAL	ASN	LEU	PRO	LEU	GLU
9	ARG	ASP	ALA	GLU	SER	PHE	LEU	LEU	LYS	SER
10	PRO	ILE	ALA	PRO	CYS	SER	LEU	ASP	LYS	ARG
11	VAL	ILE	LEU	ILE	PHE	HIS	CYS	GLU	PHE	SER
12	SER	GLU	ARG	GLY	PRO	ALA	MET	CYS	ARG	PHE
13	ILE	ARG	GLU	ARG	ASP	ARG	ALA	VAL	ASN	ASP
14	TYR	PRO	SER	LEU	TYR	TYR	PRO	GLU	MET	TYR
15	ILE	LEU	LYS	GLY	GLY	TYR	LYS	GLU	PHE	PHE
16	PRO	GLN	HIS	PRO	ASN	PHE	CYS	GLU	PRO	GLN
17	ASP	TYR	ARG	PRO	MET	ASN	HIS	GLU	ALA	PHE
18	LYS	ASP	GLU	LEU	LYS	THR	PHE	ARG	LEU	LYS
19	THR	ARG	SER	TRP	ALA	GLY	GLU	ARG	SER	ARG
20	ARG	GLU	LEU	CYS	SER	ARG	LEU	GLN	ASP	GLN

1	GLY	SER	MET	GLU	PHE	GLN	SER	ASP	HIS	ARG
2	GLU	LEU	ILE	GLY	ASP	TYR	SER	LYS	ALA	PHE
3	LEU	LEU	GLN	THR	VAL	ASP	GLY	LYS	HIS	GLN
4	ASP	LEU	LYS	TYR	ILE	SER	PRO	GLU	THR	MET
5	VAL	ALA	LEU	LEU	THR	GLY	LYS	PHE	SER	ASN
6	ILE	VAL	ASP	LYS	PHE	VAL	ILE	VAL	ASP	CYS
7	ARG	TYR	PRO	TYR	GLU	TYR	GLU	GLY	GLY	HIS
8	ILE	LYS	THR	ALA	VAL	ASN	LEU	PRO	LEU	GLU
9	ARG	ASP	ALA	GLU	SER	PHE	LEU	LEU	LYS	SER
10	PRO	ILE	ALA	PRO	CYS	SER	LEU	ASP	LYS	ARG
11	VAL	ILE	LEU	ILE	PHE	HIS	CYS	GLU	PHE	SER
12	SER	GLU	ARG	GLY	PRO	ALA	MET	CYS	ARG	PHE
13	ILE	ARG	GLU	ARG	ASP	ARG	ALA	VAL	ASN	ASP
14	TYR	PRO	SER	LEU	TYR	TYR	PRO	GLU	MET	TYR
15	ILE	LEU	LYS	GLY	GLY	TYR	LYS	GLU	PHE	PHE
16	PRO	GLN	HIS	PRO	ASN	PHE	CYS	GLU	PRO	GLN
17	ASP	TYR	ARG	PRO	MET	ASN	HIS	GLU	ALA	PHE
18	LYS	ASP	GLU	LEU	LYS	THR	PHE	ARG	LEU	LYS
19	THR	ARG	SER	TRP	ALA	GLY	GLU	ARG	SER	ARG
20	ARG	GLU	LEU	CYS	SER	ARG	LEU	GLN	ASP	GLN

1	GLY	SER	MET	GLU	PHE	GLN	SER	ASP	HIS	ARG
2	GLU	LEU	ILE	GLY	ASP	TYR	SER	LYS	ALA	PHE
3	LEU	LEU	GLN	THR	VAL	ASP	GLY	LYS	HIS	GLN
4	ASP	LEU	LYS	TYR	ILE	SER	PRO	GLU	THR	MET
5	VAL	ALA	LEU	LEU	THR	GLY	LYS	PHE	SER	ASN
6	ILE	VAL	ASP	LYS	PHE	VAL	ILE	VAL	ASP	CYS
7	ARG	TYR	PRO	TYR	GLU	TYR	GLU	GLY	GLY	HIS
8	ILE	LYS	THR	ALA	VAL	ASN	LEU	PRO	LEU	GLU
9	ARG	ASP	ALA	GLU	SER	PHE	LEU	LEU	LYS	SER
10	PRO	ILE	ALA	PRO	CYS	SER	LEU	ASP	LYS	ARG
11	VAL	ILE	LEU	ILE	PHE	HIS	CYS	GLU	PHE	SER
12	SER	GLU	ARG	GLY	PRO	ALA	MET	CYS	ARG	PHE
13	ILE	ARG	GLU	ARG	ASP	ARG	ALA	VAL	ASN	ASP
14	TYR	PRO	SER	LEU	TYR	TYR	PRO	GLU	MET	TYR
15	ILE	LEU	LYS	GLY	GLY	TYR	LYS	GLU	PHE	PHE
16	PRO	GLN	HIS	PRO	ASN	PHE	CYS	GLU	PRO	GLN
17	ASP	TYR	ARG	PRO	MET	ASN	HIS	GLU	ALA	PHE
18	LYS	ASP	GLU	LEU	LYS	THR	PHE	ARG	LEU	LYS
19	THR	ARG	SER	TRP	ALA	GLY	GLU	ARG	SER	ARG
20	ARG	GLU	LEU	CYS	SER	ARG	LEU	GLN	ASP	GLN