BMRB Entry 15475

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15475

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Title:
1H, 13C, and 15N chemical shift assignments of the C-terminal domain of the protein YuaF from Bacillus subtilis
Deposition date:
2007-09-18
Original release date:
2008-08-18
Authors:
Moller, Heiko; Walker, Christina; Hinderhofer, Markus; Witte, David; Boos, Winfried
Citation:

Citation: Walker, Christina; Hinderhofer, Markus; Witte, David; Boos, Winfried; Moeller, Heiko. "Solution Structure of the Soluble Domain of the NfeD Protein YuaF from Bacillus subtilis"  J. Biomol. NMR 42, 69-76 (2008).
PubMed: 18696230

Assembly members:

Assembly members:
YuaF, polymer, 84 residues, 8843.8 Da.

Natural source:

Natural source:   Common Name: Bacillus subtilis   Taxonomy ID: 1423   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus subtilis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pHIHO1421

Entity Sequences (FASTA):

Entity Sequences (FASTA):
YuaF: GSHMLESSAEESLAYREDDL RGRLGKVITAVPVDGFGEVV IEGIGGTISKSAVSFDNQQI SYGTTVLVVDINNGVLSVTP HEPI

Data sets:
Data typeCount
13C chemical shifts362
15N chemical shifts84
1H chemical shifts544

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1YuaF1

Entities:

Entity 1, YuaF 84 residues - 8843.8 Da.

1   GLYSERHISMETLEUGLUSERSERALAGLU
2   GLUSERLEUALATYRARGGLUASPASPLEU
3   ARGGLYARGLEUGLYLYSVALILETHRALA
4   VALPROVALASPGLYPHEGLYGLUVALVAL
5   ILEGLUGLYILEGLYGLYTHRILESERLYS
6   SERALAVALSERPHEASPASNGLNGLNILE
7   SERTYRGLYTHRTHRVALLEUVALVALASP
8   ILEASNASNGLYVALLEUSERVALTHRPRO
9   HISGLUPROILE

Samples:

sample_1: YuaF, [U-13C; U-15N], 0.9 mM; TRIS 50 mM; sodium chloride 300 mM; sodium azide 4 mM; H2O 95%; D2O 5%

sample_2: YuaF, [U-13C; U-15N], 0.9 mM; TRIS 50 mM; sodium chloride 300 mM; sodium azide 4 mM; D2O 100%

sample_3: YuaF, [U-15N], 1 mM; TRIS 50 mM; sodium chloride 300 mM; sodium azide 4 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 300 mM; pH: 7.5; pressure: 1 atm; temperature: 280 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
(HB)CB(CGCD)HDsample_2isotropicsample_conditions_1
(HB)CB(CGCDCE)HEsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1

Software:

xwinnmr v3.6, Bruker Biospin - collection

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment

TOPSPIN v1.3.b.20, Bruker Biospin - processing

NMR spectrometers:

  • Bruker Avance DRX 600 MHz
  • Bruker Avance III 800 MHz

Related Database Links:

PDB
DBJ BAI86617 BAM55168 BAM59181 GAK80134
EMBL CAB15080 CCU60134 CEI58332 CEJ78754 CUB18741
GB ADV93901 AEP92103 AFQ58945 AGA22830 AGE64696
REF NP_390980 WP_003243808 WP_009968051 WP_014477773 WP_014480657
SP O32077
AlphaFold O32077

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