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 18151

Title: 1H, 13C, and 15N chemical shift assignments for CdnL from Myxoccoccus xanthus   PubMed: 22392343

Authors: Jimenez, M. Angeles; Padmanabhan, S.; Mirassou, Yasmina

Citation: Mirassou, Yasmina; Elias-Arnanz, Montserrat; Padmanabhan, S.; Jimenez, M. Angeles. "(1)H, (13)C and (15)N assignments of CdnL, an essential protein in Myxococcus xanthus."  Biomol. NMR Assignments 7, 51-55 (2013).

Assembly members:
CdnL, polymer, 167 residues, 18982.7 Da.

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

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

Entity Sequences (FASTA):
CdnL: GSHMQTSFKTGDKAVYPGQG VGEVMGIEHTEVAGQRQSFY VLRILENGMRIMIPINKVGS VGLREIISEEDVKQVYSILK EKDISVDSTTWNRRYREYME KIKTGSVFEIAEVLRDLYLL KGDKDLSFGERKMLDTARSL LIKELSLAKDCSEDEIESDL KKIFNLA

Data sets:
Data typeCount
13C chemical shifts539
15N chemical shifts166
1H chemical shifts1082

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CdnL1

Entities:

Entity 1, CdnL 167 residues - 18982.7 Da.

GSH is the N-terminal cloning tag

1   GLYSERHISMETGLNTHRSERPHELYSTHR
2   GLYASPLYSALAVALTYRPROGLYGLNGLY
3   VALGLYGLUVALMETGLYILEGLUHISTHR
4   GLUVALALAGLYGLNARGGLNSERPHETYR
5   VALLEUARGILELEUGLUASNGLYMETARG
6   ILEMETILEPROILEASNLYSVALGLYSER
7   VALGLYLEUARGGLUILEILESERGLUGLU
8   ASPVALLYSGLNVALTYRSERILELEULYS
9   GLULYSASPILESERVALASPSERTHRTHR
10   TRPASNARGARGTYRARGGLUTYRMETGLU
11   LYSILELYSTHRGLYSERVALPHEGLUILE
12   ALAGLUVALLEUARGASPLEUTYRLEULEU
13   LYSGLYASPLYSASPLEUSERPHEGLYGLU
14   ARGLYSMETLEUASPTHRALAARGSERLEU
15   LEUILELYSGLULEUSERLEUALALYSASP
16   CYSSERGLUASPGLUILEGLUSERASPLEU
17   LYSLYSILEPHEASNLEUALA

Samples:

sample_1: CdnL 1 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; beta-mercaptoethanol 2 mM; DSS 0.5 mM

sample_2: CdnL 1 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; beta-mercaptoethanol 2 mM; DSS 0.5 mM

sample_3: CdnL, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; beta-mercaptoethanol 2 mM; DSS 0.5 mM

sample_4: CdnL, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; beta-mercaptoethanol 2 mM; DSS 0.5 mM

sample_5: CdnL 0.25 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; beta-mercaptoethanol 2 mM; DSS 0.1 mM

sample_6: CdnL 0.25 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; beta-mercaptoethanol 2 mM; DSS 0.1 mM

sample_7: CdnL, [U-100% 13C; U-100% 15N], 0.25 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; beta-mercaptoethanol 2 mM; DSS 0.5 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H COSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H COSYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_4isotropicsample_conditions_1
3D HCCH-TOCSYsample_4isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_4isotropicsample_conditions_1
2D 1H-1H COSYsample_5isotropicsample_conditions_1
2D 1H-1H TOCSYsample_5isotropicsample_conditions_1
2D 1H-1H NOESYsample_5isotropicsample_conditions_1
2D 1H-1H COSYsample_6isotropicsample_conditions_1
2D 1H-1H TOCSYsample_6isotropicsample_conditions_1
2D 1H-1H NOESYsample_6isotropicsample_conditions_1
2D 1H-15N HSQCsample_7isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_7isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

BMRB 15977
PDB
GB ABF89955 ADO71151 AEI66063 AFE08291 AGC44335
REF WP_002617724 WP_002625147 WP_002639129 WP_011552697 WP_013939202