BMRB Entry 6283

Title:
1H and 15N Chemical Shift Assignments for CLP
Deposition date:
2004-08-05
Original release date:
2004-12-15
Authors:
Liepinsh, Edvards; Rakonjac, Marija; Boissonneault, Vincent; Provost, Patrick; Samuelsson, Bengt; Radmark, Olof; Otting, Gottfried
Citation:

Citation: Liepinsh, Edvards; Rakonjac, Marija; Boissonneault, Vincent; Provost, Patrick; Samuelsson, Bengt; Radmark, Olof; Otting, Gottfried. "Letter to the Editor: NMR Structure of Human Coactosin-Like Protein"  J. Biomol. NMR 30, 353-356 (2004).

Assembly members:

Assembly members:
coactosin like protein, polymer, 145 residues, 16269 Da.

Natural source:

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

Experimental source:   Production method: recombinant technology

Experimental source:

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

Experimental source:   Production method: recombinant technology

Data sets:
Data typeCount
1H chemical shifts996
15N chemical shifts154

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1coactosin like protein1

Entities:

Entity 1, coactosin like protein 145 residues - 16269 Da.

1   GLYILEARGMETALATHRLYSILEASPLYS
2   GLUALACYSARGALAALATYRASNLEUVAL
3   ARGASPASPGLYSERALAVALILETRPVAL
4   THRPHELYSTYRASPGLYSERTHRILEVAL
5   PROGLYGLUGLNGLYALAGLUTYRGLNHIS
6   PHEILEGLNGLNCYSTHRASPASPVALARG
7   LEUPHEALAPHEVALARGPHETHRTHRGLY
8   ASPALAMETSERLYSARGSERLYSPHEALA
9   LEUILETHRTRPILEGLYGLUASNVALSER
10   GLYLEUGLNARGALALYSTHRGLYTHRASP
11   LYSTHRLEUVALLYSGLUVALVALGLNASN
12   PHEALALYSGLUPHEVALILESERASPARG
13   LYSGLULEUGLUGLUASPPHEILELYSSER
14   GLULEULYSLYSALAGLYGLYALAASNTYR
15   ASPALAGLNTHRGLU

Samples:

sample: coactosin like protein, [U-90% 15N], 0.15 mM; Tris buffer 8 mM; DTT 1 mM; NaCl 50 mM; D2O 5%

sample_conditions: temperature: 298 K; pH: 7

Experiments:

NameSampleSample stateSample conditions
1H15N_HSQCsamplenot availablesample_conditions
3D_NOESY-HSQCsamplenot availablesample_conditions
3D_TOCSY-HSQCsamplenot availablesample_conditions
2D_NOESYsamplenot availablesample_conditions
2D_TOCSYsamplenot availablesample_conditions
2D_DQF_COSYsamplenot availablesample_conditions

Software:

XWINNMR v2.8 - peak assignments

PROSA v2.8 - spectrum processing

DYANA v2.5 - structure calculation

OPAL v2.2 - structure refinement

NMR spectrometers:

  • Bruker DMX 600 MHz
  • Varian UNITY 800 MHz

Related Database Links:

BMRB 6071
PDB
DBJ BAG38040 BAJ20994
GB AAA88022 AAH10039 AAH10884 AAH16702 AAH42970
REF NP_001040058 NP_001248084 NP_066972 XP_001499912 XP_002761262
SP Q14019 Q2HJ57
TPG DAA20312
AlphaFold Q14019

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