BMRB Entry 50133

Name: Backbone 1H and 15N chemical shift assignments of chimeric SC Sup35NM, 5MT-B
Published: 2020-03-30

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50133

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

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Title: Backbone 1H and 15N chemical shift assignments of chimeric SC Sup35NM, 5MT-B PubMed: 32284601

Deposition date: 2019-12-15 Original release date: 2020-03-30

Authors: Shida, Toshinobu; Kamatari, Yuji; Yamaguchi, Yoshiki; Kuwata, Kazuo; Tanaka, Motomasa

Citation: Shida, Toshinobu; Kamatari, Yuji; Yoda, Takao; Yamaguchi, Yoshiki; Feig, Michael; Ohhashi, Yumiko; Sugita, Yuji; Kuwata, Kazuo; Tanaka, Motomasa. "Short Disordered Protein Segment Regulates Cross-Species Transmission of a Yeast Prion" Nat. Chem. Biol. 16, 756-765 (2020).

Assembly members:
entity_1, polymer, 260 residues, Formula weight is not available

Natural source: Common Name: baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET29b

Entity Sequences (FASTA):
entity_1: MSDSNQGNNQQNYQQYNQYG QYQQYNNRYQGYQAYNAQAQ PAGGYYQNYQGYSGYQQGGY QQYNPDAGYQQQYNPQGGYQ QYNPQGGYQQQFNPQGGRGN YKNFNYNNNLQGYQAGFQPQ SQGMSLNDFQKQQKQAAPKP KKTLKLVSSSGIKLANATKK VGTKPAESDKKEEEKSAETK EPTKEPTKVEEPVKKEEKPV QTEEKTEEKSELPKVEDLKI SESTHNTNNANVTSADALIK EQEEEVDDEVVNDHHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	244
1H chemical shifts	244

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	5MT-B	1

Entities:

Entity 1, 5MT-B 260 residues - Formula weight is not available

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

Samples:

sample_1: 5MT-B, [U-99% 15N], 60 uM; MES 50 mM; H2O 90%; D2O, [U-99% 2H], 10%

sample_conditions_1: ionic strength: 50 mM; pH: 4.0; pressure: 1 atm; temperature: 310.15 K

Experiments:

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

Software:

SPARKY v3.114, Goddard - data analysis

NMR spectrometers:

Bruker Avance 600 MHz

Biological Magnetic Resonance Data Bank