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 51486

Title: Assignment of SAM1-SASH1 domain   PubMed: 36341956

Deposition date: 2022-06-09 Original release date: 2022-11-11

Authors: Clements, Christopher; Shellman, Yiqun; Vogeli, Beat; Henen, Morkos

Citation: Clements, Christopher; Vogeli, Beat; Shellman, Yiqun; Henen, Morkos. "SAM1 domain in SASH1 is showing two solution species among them one is monomeric disordered and the other is folded oligomeric."  J. Struct. Biol. 214, 107914-107914 (2022).

Assembly members:
entity_1, polymer, 82 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pMAL-c4x-1-H

Entity Sequences (FASTA):
entity_1: SKGRPPQPKSVEDLLDRINL KEHMPTFLFNGYEDLDTFKL LEEEDLDELNIRDPEHRAVL LTAVELLQEYDSNSDQHHHH HH

Data sets:
Data typeCount
13C chemical shifts192
15N chemical shifts57
1H chemical shifts57

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SAM1-SASH11

Entities:

Entity 1, SAM1-SASH1 82 residues - Formula weight is not available

1   SERLYSGLYARGPROPROGLNPROLYSSER
2   VALGLUASPLEULEUASPARGILEASNLEU
3   LYSGLUHISMETPROTHRPHELEUPHEASN
4   GLYTYRGLUASPLEUASPTHRPHELYSLEU
5   LEUGLUGLUGLUASPLEUASPGLULEUASN
6   ILEARGASPPROGLUHISARGALAVALLEU
7   LEUTHRALAVALGLULEULEUGLNGLUTYR
8   ASPSERASNSERASPGLNHISHISHISHIS
9   HISHIS

Samples:

sample_1: SAM1-SASH1, [U-100% 13C; U-100% 15N], 345.7 uM; NaCl 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1

Software:

CcpNMR - chemical shift assignment, data analysis, peak picking

VNMRj - collection

NMRPipe - data analysis, peak picking, processing

SPARKY - data analysis

NMR spectrometers:

  • Varian INOVA 900 MHz
  • Bruker AVANCE NEO 600 MHz

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