BMRB Entry 15977

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15977
MolProbity Validation Chart

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Title:
Backbone and side chain 1H, 13C and 15N chemical shifts for the C-terminal domain of CdnL from Myxococcus xanthus
Deposition date:
2008-10-06
Original release date:
2008-11-15
Authors:
Mirassou, Yasmina; Garcia-Moreno, Diana; Santiveri, Clara; Santoro, Jorge; Elias-Arnanz, Monserrat; Padmanabhan, S.; Jimenez, M. Angeles
Citation:

Citation: Mirassou, Yasmina; Garcia-Moreno, Diana; Santiveri, Clara; Santoro, Jorge; Elias-Arnanz, Montserrat; Padmanabhan, S.; Jimenez, M. Angeles. "1H, 13C and 15N backbone and side chain resonance assignments of the C-terminal domain of CdnL from Myxococcus xanthus"  Biomol. NMR Assignments 3, 9-12 (2009).
PubMed: 19636935

Assembly members:

Assembly members:
CdnLC, polymer, 113 residues, Formula weight is not available

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CdnLC: GSHMGSVGLREIISEEDVKQ VYSILKEKDISVDSTTWNRR YREYMEKIKTGSVFEIAEVL RDLYLLKGDKDLSFGERKML DTARSLLIKELSLAKDCSED EIESDLKKIFNLA

Data sets:
Data typeCount
13C chemical shifts499
15N chemical shifts119
1H chemical shifts834

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CdnLC1

Entities:

Entity 1, CdnLC 113 residues - Formula weight is not available

The three N-terminal GSH residues are a cloning tag

1   GLYSERHISMETGLYSERVALGLYLEUARG
2   GLUILEILESERGLUGLUASPVALLYSGLN
3   VALTYRSERILELEULYSGLULYSASPILE
4   SERVALASPSERTHRTHRTRPASNARGARG
5   TYRARGGLUTYRMETGLULYSILELYSTHR
6   GLYSERVALPHEGLUILEALAGLUVALLEU
7   ARGASPLEUTYRLEULEULYSGLYASPLYS
8   ASPLEUSERPHEGLYGLUARGLYSMETLEU
9   ASPTHRALAARGSERLEULEUILELYSGLU
10   LEUSERLEUALALYSASPCYSSERGLUASP
11   GLUILEGLUSERASPLEULYSLYSILEPHE
12   ASNLEUALA

Samples:

sample_1: CdnLC, [U-100% 13C; U-100% 15N], 1-2 mM; sodium chloride 150 mM; sodium phosphate 50 mM; beta-mercaptoethanol 2 mM; sodium azide 0.05%; DSS 0.2 mM

sample_2: CdnLC, [U-100% 13C; U-100% 15N], 2 mM; sodium chloride 150 mM; sodium phosphate 50 mM; beta-mercaptoethanol 2 mM; sodium azide 0.05%; DSS 0.2 mM

sample_3: CdnLC 1.5 mM; sodium chloride 150 mM; sodium phosphate 50 mM; beta-mercaptoethanol 2 mM; sodium azide 0.05%; DSS 0.2 mM

sample_4: CdnLC 1.5 mM; sodium chloride 150 mM; sodium phosphate 50 mM; beta-mercaptoethanol 2 mM; sodium azide 0.05%; DSS 0.2 mM

sample_conditions_1: ionic strength: 200 mM; pH: 7.0; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HA(CA)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-1H COSYsample_3isotropicsample_conditions_1
2D 1H-1H TOCSYsample_3isotropicsample_conditions_1
2D 1H-1H 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-13C HSQCsample_4isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment, peak picking

TALOS, Cornilescu, Delaglio and Bax - dihedral angle constraints

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 18151
PDB
GB ABF89955
REF WP_011552697

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