BMRB

Biological Magnetic Resonance Data Bank


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BMRB Entry 25400

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25400
MolProbity Validation Chart

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Title: Solution structure of firefly light organ fatty acid binding protein (lcFABP)   PubMed: 26373428

Deposition date: 2014-12-18 Original release date: 2016-01-19

Authors: Tseng, Kai-Li; Lyu, Ping-Chiang

Citation: Tseng, Kai-Li; Lee, Yi-Zong; Chen, Yun-Ru; Lyu, Ping-Chiang. "(1)H, (15)N and (13)C resonance assignments of light organ-associated fatty acid-binding protein of Taiwanese fireflies"  Biomol. NMR Assign. 10, 71-74 (2016).

Assembly members:
lcFABP, polymer, 130 residues, Formula weight is not available

Natural source:   Common Name: beetles   Taxonomy ID: 1071519   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Luciola cerata

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET23a

Entity Sequences (FASTA):
lcFABP: MVQLAGTYKLEKNENFEEYL AALGVPQDSIKKANSPGVVY EIIVNGNKFTFKSSSGMNST LIVNEEVEEVLGTVNMNIKS FTKLEGSKLVVNSELPDGRK GTRTYEFCDKGFVLTMCAGD MVAKRYFIRT

Data sets:
Data typeCount
13C chemical shifts512
15N chemical shifts136
1H chemical shifts853

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1lcFABP1

Entities:

Entity 1, lcFABP 130 residues - Formula weight is not available

1   METVALGLNLEUALAGLYTHRTYRLYSLEU
2   GLULYSASNGLUASNPHEGLUGLUTYRLEU
3   ALAALALEUGLYVALPROGLNASPSERILE
4   LYSLYSALAASNSERPROGLYVALVALTYR
5   GLUILEILEVALASNGLYASNLYSPHETHR
6   PHELYSSERSERSERGLYMETASNSERTHR
7   LEUILEVALASNGLUGLUVALGLUGLUVAL
8   LEUGLYTHRVALASNMETASNILELYSSER
9   PHETHRLYSLEUGLUGLYSERLYSLEUVAL
10   VALASNSERGLULEUPROASPGLYARGLYS
11   GLYTHRARGTHRTYRGLUPHECYSASPLYS
12   GLYPHEVALLEUTHRMETCYSALAGLYASP
13   METVALALALYSARGTYRPHEILEARGTHR

Samples:

sample_1: lcFABP, [U-98% 13C; U-98% 15N], 0.9 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 0.02%; L-Arg 50 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 0.12 M; pH: 5.9; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CC(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

VNMRJ, Varian - collection

TOPSPIN v3.2, Bruker Biospin - collection, processing

SPARKY v3.114, Goddard - chemical shift assignment, peak picking

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

Molmol, Koradi, Billeter and Wuthrich - data analysis, graphic display

NMR spectrometers:

  • Varian VNMRS 700 MHz
  • Bruker Avance 600 MHz

Related Database Links:

NCBI JN222802

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