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 18627

Title: 1H, 13C, and 15N Chemical Shift Assignments for Calcium free, Myristoylated Visinin-like protein 3   PubMed: 23250791

Deposition date: 2012-07-31 Original release date: 2013-02-14

Authors: Li, Congmin; Ames, James

Citation: Li, Congmin; Ames, James. "H, 13C, and 15N chemical shift assignments of neuronal calcium sensor protein, hippocalcin."  Biomol. NMR Assignments 8, 63-66 (2014).

Assembly members:
VILIP-3 monomer, polymer, 193 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: pET3d

Entity Sequences (FASTA):
VILIP-3 monomer: MGKQNSKLRPEVLQDLRENT EFTDHELQEWYKGFLKDCPT GHLTVDEFKKIYANFFPYGD ASKFAEHVFRTFDTNGDGTI DFREFIIALSVTSRGKLEQK LKWAFSMYDLDGNGYISRSE MLEIVQAIYKMVSSVMKMPE DESTPEKRTDKIFRQMDTNN DGKLSLEEFIRGAKSDPSIV RLLQCDPSSASQF

Data sets:
Data typeCount
13C chemical shifts599
15N chemical shifts174
1H chemical shifts1103

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1VILIP-3 monomer1

Entities:

Entity 1, VILIP-3 monomer 193 residues - Formula weight is not available

1   METGLYLYSGLNASNSERLYSLEUARGPRO
2   GLUVALLEUGLNASPLEUARGGLUASNTHR
3   GLUPHETHRASPHISGLULEUGLNGLUTRP
4   TYRLYSGLYPHELEULYSASPCYSPROTHR
5   GLYHISLEUTHRVALASPGLUPHELYSLYS
6   ILETYRALAASNPHEPHEPROTYRGLYASP
7   ALASERLYSPHEALAGLUHISVALPHEARG
8   THRPHEASPTHRASNGLYASPGLYTHRILE
9   ASPPHEARGGLUPHEILEILEALALEUSER
10   VALTHRSERARGGLYLYSLEUGLUGLNLYS
11   LEULYSTRPALAPHESERMETTYRASPLEU
12   ASPGLYASNGLYTYRILESERARGSERGLU
13   METLEUGLUILEVALGLNALAILETYRLYS
14   METVALSERSERVALMETLYSMETPROGLU
15   ASPGLUSERTHRPROGLULYSARGTHRASP
16   LYSILEPHEARGGLNMETASPTHRASNASN
17   ASPGLYLYSLEUSERLEUGLUGLUPHEILE
18   ARGGLYALALYSSERASPPROSERILEVAL
19   ARGLEULEUGLNCYSASPPROSERSERALA
20   SERGLNPHE

Samples:

sample_1: Myristoylated VILIP-3, [U-100% 15N], 0.5 – 1 mM; H2O 90%; D2O 10%

sample_2: Myristoylated VILIP-3, [U-100% 13C; U-100% 15N], 0.5-1 mM; H2O 90%; D2O 10%

sample_3: Myristoylated VILIP-3, [U-100% 13C; U-100% 15N], 0.5-1 mM; D2O 100%

sample_4: Myristoylated VILIP-3 0.5-1 mM; D2O 100%

sample_conditions_1: ionic strength: 0 M; pH: 7.4; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker Avance 800 MHz

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