BMRB Entry 18121

Title:
1H, 13C, and 15N chemical shift assignments for CdnLNt from Myxoccoccus xanthus   PubMed: 22392343
Deposition date:
2011-12-07
Original release date:
2012-03-09
Authors:
Jimenez, M. Angeles; Padmanabhan, S.
Citation:

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:

Assembly members:
CdnL_N-terminal_domain, polymer, 71 residues, 7776.9 Da.

Natural source:

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pTYB12

Experimental source:

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pTYB12

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CdnL_N-terminal_domain: AGHMQTSFKTGDKAVYPGQG VGEVMGIEHTEVAGQRQSFY VLRILENGMRIMIPINKVGS VGLREIISEED

Data sets:
Data typeCount
13C chemical shifts431
15N chemical shifts138
1H chemical shifts628

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CdnLNt1

Entities:

Entity 1, CdnLNt 71 residues - 7776.9 Da.

AGH is the N-terminal cloning tag

1   ALAGLYHISMETGLNTHRSERPHELYSTHR
2   GLYASPLYSALAVALTYRPROGLYGLNGLY
3   VALGLYGLUVALMETGLYILEGLUHISTHR
4   GLUVALALAGLYGLNARGGLNSERPHETYR
5   VALLEUARGILELEUGLUASNGLYMETARG
6   ILEMETILEPROILEASNLYSVALGLYSER
7   VALGLYLEUARGGLUILEILESERGLUGLU
8   ASP

Samples:

sample_1: CdnL N-terminal domain 1 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; DSS 0.5 mM

sample_2: CdnL N-terminal domain 1 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; DSS 0.5 mM

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

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

sample_5: CdnL N-terminal domain, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; DSS 0.25 mM

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

sample_conditions_2: ionic strength: 0.15 M; pH: 7.0; pressure: 1 atm; temperature: 288 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 HNCACBsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HBHA(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-15N HSQCsample_5isotropicsample_conditions_1
3D HNCAsample_5isotropicsample_conditions_1
3D CBCA(CO)NHsample_5isotropicsample_conditions_1
3D HBHA(CO)NHsample_5isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_2
3D HNCOsample_3isotropicsample_conditions_2
3D HNCAsample_3isotropicsample_conditions_2
3D HNCACBsample_3isotropicsample_conditions_2
3D CBCA(CO)NHsample_3isotropicsample_conditions_2
3D HBHA(CO)NHsample_3isotropicsample_conditions_2
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

BMRB 18151
PDB
GB ABF89955 ADO71151 AEI66063 AFE08291 AGC44335
REF WP_002617724 WP_002625147 WP_002639129 WP_011552697 WP_013939202

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