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 18472

Title: Apo form gt CsoR   PubMed: 23001947

Deposition date: 2012-05-18 Original release date: 2019-08-30

Authors: Coyne, Harold; Giedroc, David; Kester, Benjamin

Citation: Coyne, Harold; Giedroc, David. "Backbone resonance assignments of the homotetrameric (48 kD) copper sensor CsoR from Geobacillus thermodenitrificans in the apo- and Cu(I)-bound states: insights into copper-mediated allostery"  Biomol. NMR Assign. 7, 279-283 (2013).

Assembly members:
Apo_form_gt_CsoR, polymer, 105 residues, 12056 Da.

Natural source:   Common Name: Geobacillus thermodenitrifcans   Taxonomy ID: 33940   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Geobacillus thermodenitrifcans

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET 15b

Entity Sequences (FASTA):
Apo_form_gt_CsoR: MAHPSQEEHVLHGTMIPRTK EEIENIMKRLKRIEGQVRGV QKMVEDNRYCIDILVQISAI QAALRQVGMQLLERHANHCV AKAIREGSGEQSLRELMDVI KQFAK

Data sets:
Data typeCount
13C chemical shifts298
15N chemical shifts98
1H chemical shifts98

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Apo form gt CsoR, 11
2Apo form gt CsoR, 21
3Apo form gt CsoR, 31
4Apo form gt CsoR, 41

Entities:

Entity 1, Apo form gt CsoR, 1 105 residues - 12056 Da.

1   METALAHISPROSERGLNGLUGLUHISVAL
2   LEUHISGLYTHRMETILEPROARGTHRLYS
3   GLUGLUILEGLUASNILEMETLYSARGLEU
4   LYSARGILEGLUGLYGLNVALARGGLYVAL
5   GLNLYSMETVALGLUASPASNARGTYRCYS
6   ILEASPILELEUVALGLNILESERALAILE
7   GLNALAALALEUARGGLNVALGLYMETGLN
8   LEULEUGLUARGHISALAASNHISCYSVAL
9   ALALYSALAILEARGGLUGLYSERGLYGLU
10   GLNSERLEUARGGLULEUMETASPVALILE
11   LYSGLNPHEALALYS

Samples:

sample_1: Apo form gt CsoR, [U-100% 13C; U-100% 15N; U-70% 2H], 0.4 – 0.8 mM; NaCl 115 mM; TCEP 5 mM; EDTA 3 mM; ARG 20 mM; GLU 20 mM

sample_conditions_1: ionic strength: 0.115 M; pH: 6.0; pressure: 1 atm; temperature: 322 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 800 MHz

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