BMRB Entry 15757

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15757

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Title:
1H, 13C and 15N assignment for eosinophil cationic protein
Deposition date:
2008-05-06
Original release date:
2009-05-14
Authors:
Rico, Manuel; Bruix, Marta; Laurents, Douglas; Santoro, Jorge; Jimenez, M. Angeles; Boix, Ester; Moussaoui, Mohammed; Nogues, M. Victoria
Citation:

Citation: Laurents, Douglas; Bruix, Marta; Jimenez, M Angeles; Santoro, Jorge; Boix, Ester; Moussaoui, Mohammed; Nogues, Maria Victoria; Rico, Manuel. "The (1)H, (13)C, (15)N resonance assignment, solution structure, and residue level stability of eosinophil cationic protein/RNase 3 determined by NMR spectroscopy."  Biopolymers 91, 1018-1028 (2009).
PubMed: 19189375

Assembly members:

Assembly members:
ECP, polymer, 134 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET11c

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ECP: MRPPQFTRAQWFAIQHISLN PPRCTIAMRAINNYRWRCKN QNTFLRTTFANVVNVCGNQS IRCPHNRTLNNCHRSRFRVP LLHCDLINPGAQNISNCRYA DRPGRRFYVVACDNRDPRDS PRYPVVPVHLDTTI

Data sets:
Data typeCount
13C chemical shifts527
15N chemical shifts161
1H chemical shifts961

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ECP monomer1

Entities:

Entity 1, ECP monomer 134 residues - Formula weight is not available

1   METARGPROPROGLNPHETHRARGALAGLN
2   TRPPHEALAILEGLNHISILESERLEUASN
3   PROPROARGCYSTHRILEALAMETARGALA
4   ILEASNASNTYRARGTRPARGCYSLYSASN
5   GLNASNTHRPHELEUARGTHRTHRPHEALA
6   ASNVALVALASNVALCYSGLYASNGLNSER
7   ILEARGCYSPROHISASNARGTHRLEUASN
8   ASNCYSHISARGSERARGPHEARGVALPRO
9   LEULEUHISCYSASPLEUILEASNPROGLY
10   ALAGLNASNILESERASNCYSARGTYRALA
11   ASPARGPROGLYARGARGPHETYRVALVAL
12   ALACYSASPASNARGASPPROARGASPSER
13   PROARGTYRPROVALVALPROVALHISLEU
14   ASPTHRTHRILE

Samples:

sample_1: ECP, [U-95% 15N], 1 ± 0.2 mM; potassium phosphate 50 ± 1 mM; DSS traces mM; potassium chloride <1 mM

sample_2: ECP, [U-95% 15N], 1 ± 0.2 mM; DSS traces mM; potassium phosphate 50 ± 1 mM; sodium chloride <10 mM

sample_3: ECP, [U-95% 13C; U-95% 15N], 1 ± 0.2 mM; DSS traces mM; potassium phosphate 50 ± 1 mM; sodium chloride <10 mM

sample_conditions_1: ionic strength: <0.1 M; pH: 4.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H COSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D HCCC-TOCSYsample_3isotropicsample_conditions_1

Software:

XEASY, Bartels et al. - chemical shift assignment, peak picking, processing

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

BMRB 18596
PDB
EMBL CAA33251 CAA34545 CAA39462
GB AAA50283 AAC50143 AAC50150 AAG09050 AAG09051
REF NP_002926 XP_004054906 XP_004054907
SP P12724 P47778 P47780
TPE CDG31917 CDG31938
AlphaFold P12724 P47778 P47780

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