BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 34452

Title: Reconstructing the Origins of the HemD-like fold   PubMed: 31724394

Deposition date: 2019-11-19 Original release date: 2019-11-22

Authors: Coles, M.; Toledo-Patino, S.; Chaubey, M.; Hocker, B.

Citation: Toledo-Patino, S.; Chaubey, M.; Coles, M.; Hoecker, B.. "Reconstructing the Remote Origins of a Fold Singleton from a Flavodoxin-Like Ancestor"  Biochemistry ., .-. (2019).

Assembly members:
entity_1, polymer, 125 residues, 13651.649 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

Entity Sequences (FASTA):
entity_1: MDPKVLIMRGEGGREFLAER LRGQGVQVDYLPLDYPAGEL LARVRAERLNGLVVSSGQGL QNLYQLAAADWPEIGRLPLF VPSPRVAEMARELGAQRVID CRGASAPALLAALTSAALEH HHHHH

Data sets:
Data typeCount
13C chemical shifts477
15N chemical shifts109
1H chemical shifts817

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 125 residues - 13651.649 Da.

1   METASPPROLYSVALLEUILEMETARGGLY
2   GLUGLYGLYARGGLUPHELEUALAGLUARG
3   LEUARGGLYGLNGLYVALGLNVALASPTYR
4   LEUPROLEUASPTYRPROALAGLYGLULEU
5   LEUALAARGVALARGALAGLUARGLEUASN
6   GLYLEUVALVALSERSERGLYGLNGLYLEU
7   GLNASNLEUTYRGLNLEUALAALAALAASP
8   TRPPROGLUILEGLYARGLEUPROLEUPHE
9   VALPROSERPROARGVALALAGLUMETALA
10   ARGGLULEUGLYALAGLNARGVALILEASP
11   CYSARGGLYALASERALAPROALALEULEU
12   ALAALALEUTHRSERALAALALEUGLUHIS
13   HISHISHISHISHIS

Samples:

sample_1: cU3Sd, [U-13C; U-15N], 29 mM

sample_conditions_1: ionic strength: 1 Not defined; pH: 8; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - collection

Sparky, Goddard - chemical shift assignment

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III 800 MHz

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