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 5329

Title: Backbone and Side Chain 1H, 13C, and 15N chemical shift assignments for conserved eukaryotic protein ZK652.3 from C. elegans   PubMed: 12211038

Deposition date: 2002-03-20 Original release date: 2003-01-06

Authors: Cort, John; Chiang, Yiwen; Deyou, Zheng; Montelione, Gaetano; Kennedy, Michael

Citation: Cort, John; Chiang, Yiwen; Zheng, Deyou; Montelione, Gaetano; Kennedy, Michael. "NMR Structure of Conserved Eukaryotic Protein ZK652.3 from C. elegans: A Ubiquitin-like fold"  Proteins 48, 733-736 (2002).

Assembly members:
ZK652.3, polymer, 94 residues, 9800 Da.

Natural source:   Common Name: C. elegans   Taxonomy ID: 6239   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Caenorhabditis elegans

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15b

Entity Sequences (FASTA):
ZK652.3: MSGGTAATTAGSKVTFKITL TSDPKLPFKVLSVPESTPFT AVLKFAAEEFKVPAATSAII TNDGVGVNPAQPAGNIFLKH GSELRLIPRDRVGH

Data sets:
Data typeCount
13C chemical shifts365
1H chemical shifts527
15N chemical shifts85

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ZK652.31

Entities:

Entity 1, ZK652.3 94 residues - 9800 Da.

1   METSERGLYGLYTHRALAALATHRTHRALA
2   GLYSERLYSVALTHRPHELYSILETHRLEU
3   THRSERASPPROLYSLEUPROPHELYSVAL
4   LEUSERVALPROGLUSERTHRPROPHETHR
5   ALAVALLEULYSPHEALAALAGLUGLUPHE
6   LYSVALPROALAALATHRSERALAILEILE
7   THRASNASPGLYVALGLYVALASNPROALA
8   GLNPROALAGLYASNILEPHELEULYSHIS
9   GLYSERGLULEUARGLEUILEPROARGASP
10   ARGVALGLYHIS

Samples:

sample_1: ZK652.3, [U-99% 15N], 0.9 mM; ammonium acetate 10 mm; sodium chloride 50 mm

sample_2: ZK652.3, [U-99% 13C; U-99% 15N], 0.9 mM; ammonium acetate 10 mm; sodium chloride 50 mm

sample_3: ZK652.3, [U-10% 13C; U-99% 15N], 0.9 mM; ammonium acetate 10 mm; sodium chloride 50 mm

conditions_1: pH: 5.5; temperature: 298 K; ionic strength: 0.06 M

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCnot availablenot availableconditions_1
3D 1H-15N NOESY-HSQCnot availablenot availableconditions_1
3D HNHAnot availablenot availableconditions_1
2D 1H-13C HSQC (aliph)not availablenot availableconditions_1
HNCACBnot availablenot availableconditions_1
HNCOnot availablenot availableconditions_1
CBCA(CO)NHnot availablenot availableconditions_1
CBCACOCAHAnot availablenot availableconditions_1
HCCH-TOCSYnot availablenot availableconditions_1
HCC-TOCSY-NNHnot availablenot availableconditions_1
CCC-TOCSY-NNHnot availablenot availableconditions_1
3D CN-NOESY-HSQCnot availablenot availableconditions_1
4D CC-NOESYnot availablenot availableconditions_1
2D 1H-13C HSQC (alpha)not availablenot availableconditions_1
2D 1H-13C HSQC (alpha Sens. Enhanced)not availablenot availableconditions_1
2D 1H-13C HSQC (arom)not availablenot availableconditions_1

Software:

FELIX v98 - processing, assignment

NMR spectrometers:

  • VARIAN UNITY 600 MHz
  • VARIAN INOVA 600 MHz
  • VARIAN INOVA 750 MHz
  • VARIAN INOVA 800 MHz

Related Database Links:

PDB
EMBL CCD62548
GB AAG50218
REF NP_498705
SP P34661
AlphaFold P34661

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