BMRB Entry 30901

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PDB ID: 7mn1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30901
MolProbity Validation Chart

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Title:
Rules for designing protein fold switches and their implications for the folding code
Deposition date:
2021-04-30
Original release date:
2022-05-09
Authors:
He, Y.; Chen, Y.; Ruan, B.; Choi, J.; Chen, Y.; Motabar, D.; Solomon, T.; Simmerman, R.; Kauffman, T.; Gallagher, T.; Bryan, P.; Orban, J.
Citation:

Citation: Ruan, Biao; He, Yanan; Chen, Yingwei; Choi, Eun Jung; Chen, Yihong; Motabar, Dana; Solomon, Tsega; Simmerman, Richard; Kauffman, Thomas; Gallagher, D. Travis; Orban, John; Bryan, Philip N.. "Design and characterization of a protein fold switching network"  Nat. Commun. 14, 431-431 (2023).
PubMed: 36702827

Assembly members:

Assembly members:
entity_1, polymer, 95 residues, 10600.333 Da.

Natural source:

Natural source:   Common Name: Thermus thermophilus   Taxonomy ID: 274   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Thermus thermophilus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SKTFEVNIVLNPNLDQKQLA QAKELAIKALKQYGIGVEKI KLIGNAKTVEAVEKLKQGIL LVYQIEAPADRVNDLARELR ILDAVRRVEVTYAAD

Data sets:
Data typeCount
13C chemical shifts279
15N chemical shifts82
1H chemical shifts289

Additional metadata:

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Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 95 residues - 10600.333 Da.

1   SERLYSTHRPHEGLUVALASNILEVALLEU
2   ASNPROASNLEUASPGLNLYSGLNLEUALA
3   GLNALALYSGLULEUALAILELYSALALEU
4   LYSGLNTYRGLYILEGLYVALGLULYSILE
5   LYSLEUILEGLYASNALALYSTHRVALGLU
6   ALAVALGLULYSLEULYSGLNGLYILELEU
7   LEUVALTYRGLNILEGLUALAPROALAASP
8   ARGVALASNASPLEUALAARGGLULEUARG
9   ILELEUASPALAVALARGARGVALGLUVAL
10   THRTYRALAALAASP

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