BMRB Entry 15664

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15664

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Title:
1H, 13C, and 15N chemical shift assignments of the C-terminal domain of the protein YqiJ from Escherichia coli
Deposition date:
2008-02-19
Original release date:
2009-06-10
Authors:
Moller, Heiko; Drees, Christina; Hinderhofer, Markus; Boos, Winfried
Citation:

Citation: Hinderhofer, Markus; Walker, Christina; Friemel, Anke; Stuermer, Heiko; Reuter, Alexander. "Evolution of prokaryotic SPFH proteins."  BMC Evol. Biol. 9, 10-10 (2009).
PubMed: 19138386

Assembly members:

Assembly members:
YqiJ, polymer, 100 residues, 11089.6 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pHIHO1422

Entity Sequences (FASTA):

Entity Sequences (FASTA):
YqiJ: GSHMLEDPTGKIVAPWIPRD HSSAITEEEYIGSMALITGH QATSGNPCEGKLTDQFGQIH YLLLEPEEGKIFTKGDKVLI ICRLSATRYLAENNPWPQIL

Data sets:
Data typeCount
13C chemical shifts436
15N chemical shifts91
1H chemical shifts643

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1YqiJ1

Entities:

Entity 1, YqiJ 100 residues - 11089.6 Da.

1   GLYSERHISMETLEUGLUASPPROTHRGLY
2   LYSILEVALALAPROTRPILEPROARGASP
3   HISSERSERALAILETHRGLUGLUGLUTYR
4   ILEGLYSERMETALALEUILETHRGLYHIS
5   GLNALATHRSERGLYASNPROCYSGLUGLY
6   LYSLEUTHRASPGLNPHEGLYGLNILEHIS
7   TYRLEULEULEUGLUPROGLUGLUGLYLYS
8   ILEPHETHRLYSGLYASPLYSVALLEUILE
9   ILECYSARGLEUSERALATHRARGTYRLEU
10   ALAGLUASNASNPROTRPPROGLNILELEU

Samples:

sample_1: YqiJ, [U-13C; U-15N], 1 mM; TRIS 50 mM; sodium chloride 300 mM; sodium azide 4 mM; TCEP 5 mM; H2O 95%; D2O 5%

sample_2: YqiJ, [U-13C; U-15N], 1 mM; TRIS 50 mM; sodium chloride 300 mM; sodium azide 4 mM; TCEP 5 mM; D2O 100%

sample_3: YqiJ, [U-15N], 1.2 mM; TRIS 50 mM; sodium chloride 300 mM; sodium azide 4 mM; TCEP 5 mM; H2O 95%; D2O 5%

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_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(CGCDCE)HEsample_2isotropicsample_conditions_1
(HB)CB(CGCD)HDsample_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 v2.0, Bruker Biospin - processing

NMR spectrometers:

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

Related Database Links:

DBJ BAB37355 BAE77102 BAG78853 BAI27332 BAI32447
EMBL CAQ33387 CAR00011 CAR14688 CAR19662 CAU99595
GB AAC76086 AAG58184 AAZ89770 ABG71122 ABV07459
REF NP_311959 NP_417522 WP_000016376 WP_000599922 WP_000599923
SP P76657
AlphaFold P76657

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