BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 30902

Title: Rules for designing protein fold switches and their implications for the folding code   PubMed: 36702827

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: 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).

Assembly members:
entity_1, polymer, 93 residues, 10461.855 Da.

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

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

Entity Sequences (FASTA):
entity_1: GIYTVKIVLNPKTNKGELTT EAVDAATALKNFGAKAQDVG VDGAWTYSDPTKTFPVGYRL IFKVEMPEDRVNDLARQLRQ RDNVSRVEVTRYK

Data sets:
Data typeCount
13C chemical shifts231
15N chemical shifts74
1H chemical shifts147

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 93 residues - 10461.855 Da.

1   GLYILETYRTHRVALLYSILEVALLEUASN
2   PROLYSTHRASNLYSGLYGLULEUTHRTHR
3   GLUALAVALASPALAALATHRALALEULYS
4   ASNPHEGLYALALYSALAGLNASPVALGLY
5   VALASPGLYALATRPTHRTYRSERASPPRO
6   THRLYSTHRPHEPROVALGLYTYRARGLEU
7   ILEPHELYSVALGLUMETPROGLUASPARG
8   VALASNASPLEUALAARGGLNLEUARGGLN
9   ARGASPASNVALSERARGVALGLUVALTHR
10   ARGTYRLYS

Samples:

sample_1: Sb2, [U-13C; U-15N], 0.3 mM; potassium phosphate 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 15NNOESYsample_1isotropicsample_conditions_1
3D 13CNOESYsample_1isotropicsample_conditions_1

Software:

CS-ROSETTA, Shen, Vernon, Baker and Bax - refinement, structure calculation

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

TopSpin, Bruker Biospin - collection

NMRFAM-SPARKY, NMRFAM - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AVANCE DMX 600 MHz

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