BMRB Entry 51662

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51662

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Title:
1H, 13C and 15N NMR chemical shift assignments of LytM N-terminal domain (residues 26-184)
Deposition date:
2022-10-14
Original release date:
2023-12-01
Authors:
Pitkanen, Ilona; Tossavainen, Helena; Permi, Perttu
Citation:

Citation: Pitkanen, Ilona; Tossavainen, Helena; Permi, Perttu. "1H, 13C, and 15N NMR chemical shift assignment of LytM N-terminal domain (residues 26-184)"  Biomol. NMR Assign. 17, 257-263 (2023).
PubMed: 37742292

Assembly members:

Assembly members:
entity_1, polymer, 160 residues, 17406 Da.

Natural source:

Natural source:   Common Name: Staphylococcus aureus   Taxonomy ID: 1280   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Staphylococcus aureus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAETTNTQQAHTQMSTQSQD VSYGTYYTIDSNGDYHHTPD GNWNQAMFDNKEYSYTFVDA QGHTHYFYNCYPKNANANGS GQTYVNPATAGDNNDYTASQ SQQHINQYGYQSNVGPDASY YSHSNNNQAYNSHDGNGKVN YPNGTSNQNGGSASKATASG

Data sets:
Data typeCount
13C chemical shifts546
15N chemical shifts166
1H chemical shifts629

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1N-terminal domain of LytM (26-184)1

Entities:

Entity 1, N-terminal domain of LytM (26-184) 160 residues - 17406 Da.

1   GLYALAGLUTHRTHRASNTHRGLNGLNALA
2   HISTHRGLNMETSERTHRGLNSERGLNASP
3   VALSERTYRGLYTHRTYRTYRTHRILEASP
4   SERASNGLYASPTYRHISHISTHRPROASP
5   GLYASNTRPASNGLNALAMETPHEASPASN
6   LYSGLUTYRSERTYRTHRPHEVALASPALA
7   GLNGLYHISTHRHISTYRPHETYRASNCYS
8   TYRPROLYSASNALAASNALAASNGLYSER
9   GLYGLNTHRTYRVALASNPROALATHRALA
10   GLYASPASNASNASPTYRTHRALASERGLN
11   SERGLNGLNHISILEASNGLNTYRGLYTYR
12   GLNSERASNVALGLYPROASPALASERTYR
13   TYRSERHISSERASNASNASNGLNALATYR
14   ASNSERHISASPGLYASNGLYLYSVALASN
15   TYRPROASNGLYTHRSERASNGLNASNGLY
16   GLYSERALASERLYSALATHRALASERGLY

Samples:

sample_1: LytM (26-107), [U-13C; U-15N], 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM

sample_2: LytM (26-184), [U-13C; U-15N], 0.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM

sample_conditions_1: ionic strength: 70 mM; pH: 6.5; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D i(HCA)CO(CA)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D H(CC)(CO)NHsample_1isotropicsample_conditions_1
3D (H)CC(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HC(C)H-COSYsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D i(HCA)CO(CA)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(CO)CACBsample_2isotropicsample_conditions_1
3D HA(CA)CONsample_2isotropicsample_conditions_1
3D HA(CA)CONi/i+1sample_2isotropicsample_conditions_1
4D HACANCOsample_2isotropicsample_conditions_1
4D HACACONsample_2isotropicsample_conditions_1

Software:

ANALYSIS v2.4.2 - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

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