BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 27432

Title: Solution structure of the cross-linked dimer of the SLy1 SAM domain S320C mutant   PubMed: 30631134

Deposition date: 2018-03-21 Original release date: 2019-01-25

Authors: Kukuk, Laura; Dingley, Andrew; Koenig, Bernd

Citation: Kukuk, Laura; Dingley, Andrew; Granzin, Joachim; Nagel-Steger, Luitgard; Thiagarajan-Rosenkranz, Pallavi; Ciupka, Daniel; Hanel, Karen; Batra-Safferling, Renu; Pacheco, Victor; Stoldt, Matthias; Pfeffer, Klaus; Beer-Hammer, Sandra; Willbold, Dieter; Koenig, Bernd. "Structure of the SLy1 SAM homodimer reveals a new interface for SAM domain self-association."  Sci. Rep. 9, 54-54 (2019).

Assembly members:
Sly1_SAM, polymer, 69 residues, 7940.9134 Da.

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

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

Entity Sequences (FASTA):
Sly1_SAM: GPKTLHELLERIGLEEHTST LLLNGYQTLEDFKELRETHL NELNIMDPQHRAKLLTAAEL LLDYDTGCE

Data sets:
Data typeCount
13C chemical shifts316
15N chemical shifts72
1H chemical shifts504

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SAM A1
2SAM B1

Entities:

Entity 1, SAM A 69 residues - 7940.9134 Da.

1   GLYPROLYSTHRLEUHISGLULEULEUGLU
2   ARGILEGLYLEUGLUGLUHISTHRSERTHR
3   LEULEULEUASNGLYTYRGLNTHRLEUGLU
4   ASPPHELYSGLULEUARGGLUTHRHISLEU
5   ASNGLULEUASNILEMETASPPROGLNHIS
6   ARGALALYSLEULEUTHRALAALAGLULEU
7   LEULEUASPTYRASPTHRGLYCYSGLU

Samples:

sample_1: Sly1 SAM, [U-13C; U-15N], 1.4 mM; potassium phosphate 50 mM; sodium chloride 20 mM; EDTA 0.2 mM; sodium azide 0.03%

sample_2: Sly1 SAM, [U-13C; U-15N], 0.8 mM; potassium phosphate 50 mM; sodium chloride 20 mM; EDTA 0.2 mM; sodium azide 0.03%; Sly1 SAM 0.8 mM

SAMsh_Standard: ionic strength: 0.098 M; pH: 6.4; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicSAMsh_Standard
2D 1H-13C HSQC aliphaticsample_1isotropicSAMsh_Standard
3D CBCA(CO)NHsample_1isotropicSAMsh_Standard
3D C(CO)NHsample_1isotropicSAMsh_Standard
3D HNCOsample_1isotropicSAMsh_Standard
3D HNCAsample_1isotropicSAMsh_Standard
3D HNCACBsample_1isotropicSAMsh_Standard
3D H(CCO)NHsample_1isotropicSAMsh_Standard
3D HCCH-TOCSYsample_1isotropicSAMsh_Standard
3D 1H-15N TOCSYsample_1isotropicSAMsh_Standard
3D 1H-13C NOESY aromaticsample_1isotropicSAMsh_Standard
3D 1H-15N NOESYsample_1isotropicSAMsh_Standard
3D 1H-13C NOESY aliphaticsample_1isotropicSAMsh_Standard
3D 1H-13C NOESY aliphaticsample_2isotropicSAMsh_Standard
3D 1H-15N NOESYsample_2isotropicSAMsh_Standard

Software:

ARIA v2.3.2, Linge, O'Donoghue and Nilges - chemical shift assignment

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

CcpNmr_Analysis v2.4, CCPN, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift assignment, data analysis, peak picking, processing

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - visualization of spectra

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz

Related Database Links:

UNP Q8K352

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts