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 15770

Title: 1H, 13C and 15N chemical shifts for the Myxococcus xanthus CarS1 antirepressor protein   PubMed: 19636942

Deposition date: 2008-05-13 Original release date: 2009-01-15

Authors: Jimenez, M. Angeles; Gonzalez, Carlos; Padmanabhan, S.; Leon, Esther; Navarro-Aviles, Gloria; Elias-Arnanz, Montserrat

Citation: Leon, Esther; Gonzalez, Carlos; Elias-Arnanz, Montserrat; Padmanabhan, S.; Jimenez, M. Angeles. "1H, 13C and 15N backbone and side chain resonance assignments of a Myxococcus xanthus anti-repressor with no known sequence homologues"  Biomol. NMR Assignments 3, 37-40 (2009).

Assembly members:
CarS1, polymer, 106 residues, Formula weight is not available

Natural source:   Common Name: Myxococcus xanthus   Taxonomy ID: 34   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Myxococcus xanthus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15b

Entity Sequences (FASTA):
CarS1: MGSSHHHHHHSSGLVPRGSH MIQDPSLIICHDVDGAPVRI GAKVKVVPHSEDGTISQRFL GQTGIVVGLVFDDPATQYPD DPLIQVLVEGLGEDLFFPEE LELAPE

Data sets:
Data typeCount
13C chemical shifts371
15N chemical shifts78
1H chemical shifts1208

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CarS11

Entities:

Entity 1, CarS1 106 residues - Formula weight is not available

Residues 1-20 corresponds to a non-native His-tag

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METILEGLNASPPROSERLEUILEILECYS
4   HISASPVALASPGLYALAPROVALARGILE
5   GLYALALYSVALLYSVALVALPROHISSER
6   GLUASPGLYTHRILESERGLNARGPHELEU
7   GLYGLNTHRGLYILEVALVALGLYLEUVAL
8   PHEASPASPPROALATHRGLNTYRPROASP
9   ASPPROLEUILEGLNVALLEUVALGLUGLY
10   LEUGLYGLUASPLEUPHEPHEPROGLUGLU
11   LEUGLULEUALAPROGLU

Samples:

sample_1: CarS1, [U-100% 13C; U-100% 15N], 1 ± 0.2 mM; H2O 90%; D2O, [U-99% 2H], 10%; sodium phosphate 50 mM; DTT 1 mM; sodium azide 0.1 mM; DSS 0.2 mM

sample_2: CarS1, [U-100% 13C; U-100% 15N], 1 ± 0.2 mM; D2O, [U-99% 2H], 100%; sodium phosphate 50 mM; DTT 1 mM; sodium azide 0.1 mM; DSS 0.2 mM

sample_3: CarS1, [U-100% 15N], 1 ± 0.2 mM; H2O 90%; D2O, [U-99% 2H], 10%; sodium phosphate 50 mM; DTT 1 mM; sodium azide 0.1 mM; DSS 0.2 mM

sample_4: CarS1 1 ± 0.2 mM; H2O 90%; D2O, [U-99% 2H], 10%; sodium phosphate 50 mM; DTT 1 mM; sodium azide 0.1 mM; DSS 0.2 mM

sample_5: CarS1 1 ± 0.2 mM; D2O, [U-99% 2H], 100%; sodium phosphate 50 mM; DTT 1 mM; sodium azide 0.1 mM; DSS 0.2 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298.4 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D HA(CA)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D HNHAsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
2D 1H-1H COSYsample_4isotropicsample_conditions_1
2D 1H-1H TOCSYsample_4isotropicsample_conditions_1
2D 1H-1H NOESYsample_4isotropicsample_conditions_1
2D 1H-1H COSYsample_5isotropicsample_conditions_1
2D 1H-1H TOCSYsample_5isotropicsample_conditions_1
2D 1H-1H NOESYsample_5isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

TOPSPIN, Bruker - processing

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
EMBL CAA50383
GB ABF92626
REF WP_011554097
SP Q06911
AlphaFold Q06911

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