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 6498

Title: Backbone and side-chain 1H, 13C, and 15N Chemical Shift Assignments for SIP (1-77)   PubMed: 15996101

Deposition date: 2005-02-08 Original release date: 2005-08-16

Authors: Bhattacharya, Shibani; Lee, Young-Tae; Michowski, Wojciech; Filipek, Anna; Kuznicki, Jacek; Chazin, Walter

Citation: Bhattacharya, Shibani; Lee, Young-Tae; Michowski, Wojciech; Filipek, Anna; Kuznicki, Jacek; Chazin, Walter. "The Modular Structure of SIP Facilitates Its Role in Stabilizing Multiprotein Assemblies(,)."  Biochemistry 44, 9462-9471 (2005).

Assembly members:
single chain biopolymer, polymer, 77 residues, Formula weight is not available

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   Vector: pET28

Entity Sequences (FASTA):
single chain biopolymer: MASVLEELQKDLEEVKVLLE KSTRKRLRDTLTSEKSKIET ELKNKMQQKSQKKPELDNEK PAAVVAPLTTGYTVKIS

Data sets:
  • assigned_chemical_shifts
Data typeCount
1H chemical shifts561
13C chemical shifts335
15N chemical shifts77

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SIP N-Domain, SIP (1-77)1

Entities:

Entity 1, SIP N-Domain, SIP (1-77) 77 residues - Formula weight is not available

1   METALASERVALLEUGLUGLULEUGLNLYS
2   ASPLEUGLUGLUVALLYSVALLEULEUGLU
3   LYSSERTHRARGLYSARGLEUARGASPTHR
4   LEUTHRSERGLULYSSERLYSILEGLUTHR
5   GLULEULYSASNLYSMETGLNGLNLYSSER
6   GLNLYSLYSPROGLULEUASPASNGLULYS
7   PROALAALAVALVALALAPROLEUTHRTHR
8   GLYTYRTHRVALLYSILESER

Samples:

Sample_1: single chain biopolymer, [U-100% 13C; U-100% 15N], 1.0 mM; NaPi 20.0 mM; NaCl 50 mM; H2O 90%

Sample_2: single chain biopolymer, [U-100% 13C], 1 mM; NaPi 20 mM; NaCl 50 mM; D2O 100%

Sample_3: single chain biopolymer, [U-10% 13C], 1 mM; NaPi 20 mM; NaCl 50 mM; D2O 100%

Exp_cond_1: pH: 7.0; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
1H-15N HSQCnot availablenot availablenot available
1H-13C CT-HSQCnot availablenot availablenot available
3D-HNCOnot availablenot availablenot available
3D-HNCACBnot availablenot availablenot available
3D-CBCA(CO)NHnot availablenot availablenot available
3D-HC(CCO)NHnot availablenot availablenot available
3D-(H)CC(CO)NHnot availablenot availablenot available
3D-HCCH-TOCSYnot availablenot availablenot available

Software:

FELIX v2000 - processing, analysis

NMR spectrometers:

  • Bruker AVANCE 600 MHz

Related Database Links:

PDB
GB AAC16757 AAH25948 EDL39341
REF NP_033916
SP Q9CXW3
AlphaFold Q9CXW3

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