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 6500

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for SIP (74-178)   PubMed: 15996101

Deposition date: 2005-02-14 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:
SIP (74-178), polymer, 105 residues, Formula weight is not available

Natural source:   Common Name: house 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):
SIP (74-178): VKISNYGWDQSDKFVKIYIT LTGVHQVPTENVQVHFTERS FDLLVKNLNGKNYSMIVNNL LKPISVESSSKKVKTDTVII LCRKKAENTRWDYLTQVEKE CKEKE

Data sets:
  • assigned_chemical_shifts
Data typeCount
13C chemical shifts279
15N chemical shifts93
1H chemical shifts93

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SIP CS-Domain1

Entities:

Entity 1, SIP CS-Domain 105 residues - Formula weight is not available

1   VALLYSILESERASNTYRGLYTRPASPGLN
2   SERASPLYSPHEVALLYSILETYRILETHR
3   LEUTHRGLYVALHISGLNVALPROTHRGLU
4   ASNVALGLNVALHISPHETHRGLUARGSER
5   PHEASPLEULEUVALLYSASNLEUASNGLY
6   LYSASNTYRSERMETILEVALASNASNLEU
7   LEULYSPROILESERVALGLUSERSERSER
8   LYSLYSVALLYSTHRASPTHRVALILEILE
9   LEUCYSARGLYSLYSALAGLUASNTHRARG
10   TRPASPTYRLEUTHRGLNVALGLULYSGLU
11   CYSLYSGLULYSGLU

Samples:

Sample_1: SIP (74-178), [U-100% 13C; U-100% 15N], 1.0 mM; NaPi 20 mM; NaCl 50 mM; DTT 5 mM; H2O 90%; D2O 10%

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

Software:

FELIX v2000 - analysis, processing

NMR spectrometers:

  • Bruker AVANCE 600 MHz

Related Database Links:

GB AAC16757 AAH25948 AAH79007 EDL39341 EDM09438
REF NP_001004208 NP_033916 XP_002928087 XP_003130369 XP_003497720
SP Q6AYK6 Q9CXW3
AlphaFold Q6AYK6 Q9CXW3

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